data_9DLW
# 
_entry.id   9DLW 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9DLW         pdb_00009dlw 10.2210/pdb9dlw/pdb 
WWPDB D_1000288336 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-06 
2 'Structure model' 1 1 2024-12-04 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_CSD'          
4  2 'Structure model' '_citation.journal_id_ISSN'         
5  2 'Structure model' '_citation.journal_volume'          
6  2 'Structure model' '_citation.page_first'              
7  2 'Structure model' '_citation.page_last'               
8  2 'Structure model' '_citation.pdbx_database_id_DOI'    
9  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 2 'Structure model' '_citation.title'                   
11 2 'Structure model' '_citation.year'                    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DLW 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-11 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 9B9H unspecified 
PDB . 9B9T unspecified 
PDB . 9B9W unspecified 
PDB . 9BA2 unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              mvedadi@oicr.on.ca 
_pdbx_contact_author.name_first         Masoud 
_pdbx_contact_author.name_last          Vedadi 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0574-0169 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Mabanglo, M.F.' 1 0000-0003-4671-4159 
'Mamai, A.'      2 0009-0001-3125-1991 
'Wilson, B.J.'   3 0009-0003-1132-8095 
'Hoffer, L.'     4 0000-0003-1906-7128 
'Al-awar, R.'    5 0000-0002-4185-055X 
'Vedadi, M.'     6 0000-0002-0574-0169 
# 
_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            15 
_citation.language                  ? 
_citation.page_first                10165 
_citation.page_last                 10165 
_citation.title                     
'Crystal structures of DCAF1-PROTAC-WDR5 ternary complexes provide insight into DCAF1 substrate specificity.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-024-54500-x 
_citation.pdbx_database_id_PubMed   39580491 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Mabanglo, M.F.'       1  ?                   
primary 'Wilson, B.'           2  ?                   
primary 'Noureldin, M.'        3  ?                   
primary 'Kimani, S.W.'         4  0000-0002-6960-3833 
primary 'Mamai, A.'            5  ?                   
primary 'Krausser, C.'         6  ?                   
primary 'Gonzalez-Alvarez, H.' 7  ?                   
primary 'Srivastava, S.'       8  ?                   
primary 'Mohammed, M.'         9  ?                   
primary 'Hoffer, L.'           10 0000-0003-1906-7128 
primary 'Chan, M.'             11 ?                   
primary 'Avrumutsoae, J.'      12 ?                   
primary 'Li, A.S.M.'           13 ?                   
primary 'Hajian, T.'           14 ?                   
primary 'Tucker, S.'           15 ?                   
primary 'Green, S.'            16 0000-0002-2960-9683 
primary 'Szewczyk, M.'         17 ?                   
primary 'Barsyte-Lovejoy, D.'  18 0000-0002-6560-9621 
primary 'Santhakumar, V.'      19 0000-0002-7001-557X 
primary 'Ackloo, S.'           20 0000-0002-9696-1839 
primary 'Loppnau, P.'          21 ?                   
primary 'Li, Y.'               22 0000-0002-9512-5265 
primary 'Seitova, A.'          23 ?                   
primary 'Kiyota, T.'           24 0000-0001-6313-3482 
primary 'Wang, J.G.'           25 ?                   
primary 'Prive, G.G.'          26 ?                   
primary 'Kuntz, D.A.'          27 0000-0003-3584-4804 
primary 'Patel, B.'            28 ?                   
primary 'Rathod, V.'           29 ?                   
primary 'Vala, A.'             30 ?                   
primary 'Rout, B.'             31 ?                   
primary 'Aman, A.'             32 0000-0002-0275-205X 
primary 'Poda, G.'             33 ?                   
primary 'Uehling, D.'          34 ?                   
primary 'Ramnauth, J.'         35 ?                   
primary 'Halabelian, L.'       36 0000-0003-4361-3619 
primary 'Marcellus, R.'        37 ?                   
primary 'Al-Awar, R.'          38 ?                   
primary 'Vedadi, M.'           39 0000-0002-0574-0169 
# 
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 'DDB1- and CUL4-associated factor 1' 38298.820 1   2.7.11.1 ? 'residues 1080-1390' ? 
2 polymer     man 'WD repeat-containing protein 5' 36433.207 1   ?        ? ?                    ? 
3 non-polymer syn 
;N-{(1P)-5'-({(32E)-33-[(3P)-4-{[(1S)-3-amino-1-(3-chloro-4-fluorophenyl)-3-oxopropyl]carbamoyl}-3-(4-chloro-2-fluorophenyl)-1H-pyrrol-2-yl]-31-oxo-3,6,9,12,15,18,21,24,27-nonaoxa-30-azatritriacont-32-en-1-yl}carbamoyl)-2'-fluoro-4-[(3R,5S)-3,4,5-trimethylpiperazin-1-yl][1,1'-biphenyl]-3-yl}-6-oxo-4-(trifluoromethyl)-1,6-dihydropyridine-3-carboxamide
;
1475.356  1   ?        ? ?                    ? 
4 water       nat water 18.015    419 ?        ? ?                    ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'HIV-1 Vpr-binding protein,VprBP,Serine/threonine-protein kinase VPRBP,Vpr-interacting protein' 
2 'BMP2-induced 3-kb gene protein'                                                                
# 
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 
;MGSSHHHHHHSSGRENLYFQGSSRASAFRPISVFREANEDESGFTCCAFSARERFLMLGTCTGQLKLYNVFSGQEEASYN
CHNSAITHLEPSRDGSLLLTSATWSQPLSALWGMKSVFDMKHSFTEDHYVEFSKHSQDRVIGTKGDIAHIYDIQTGNKLL
TLFNPDLANNYKRNCATFNPTDDLVLNDGVLWDVRSAQAIHKFDKFNMNISGVFHPNGLEVIINTEIWDLRTFHLLHTVP
ALDQCRVVFNHTGTVMYGAMLQADDEDDLMEERMKSPFGSSFRTFNATDYKPIATIDVKRNIFDLCTDTKDCYLAVIENQ
GSMDALNMDTVCRLYEVG
;
;MGSSHHHHHHSSGRENLYFQGSSRASAFRPISVFREANEDESGFTCCAFSARERFLMLGTCTGQLKLYNVFSGQEEASYN
CHNSAITHLEPSRDGSLLLTSATWSQPLSALWGMKSVFDMKHSFTEDHYVEFSKHSQDRVIGTKGDIAHIYDIQTGNKLL
TLFNPDLANNYKRNCATFNPTDDLVLNDGVLWDVRSAQAIHKFDKFNMNISGVFHPNGLEVIINTEIWDLRTFHLLHTVP
ALDQCRVVFNHTGTVMYGAMLQADDEDDLMEERMKSPFGSSFRTFNATDYKPIATIDVKRNIFDLCTDTKDCYLAVIENQ
GSMDALNMDTVCRLYEVG
;
B ? 
2 'polypeptide(L)' no no 
;MHHHHHHSSGRENLYFQGTQSKPTPVKPNYALKFTLAGHTKAVSSVKFSPNGEWLASSSADKLIKIWGAYDGKFEKTISG
HKLGISDVAWSSDSNLLVSASDDKTLKIWDVSSGKCLKTLKGHSNYVFCCNFNPQSNLIVSGSFDESVRIWDVKTGKCLK
TLPAHSDPVSAVHFNRDGSLIVSSSYDGLCRIWDTASGQCLKTLIDDDNPPVSFVKFSPNGKYILAATLDNTLKLWDYSK
GKCLKTYTGHKNEKYCIFANFSVTGGKWIVSGSEDNLVYIWNLQTKEIVQKLQGHTDVVISTACHPTENIIASAALENDK
TIKLWKSDC
;
;MHHHHHHSSGRENLYFQGTQSKPTPVKPNYALKFTLAGHTKAVSSVKFSPNGEWLASSSADKLIKIWGAYDGKFEKTISG
HKLGISDVAWSSDSNLLVSASDDKTLKIWDVSSGKCLKTLKGHSNYVFCCNFNPQSNLIVSGSFDESVRIWDVKTGKCLK
TLPAHSDPVSAVHFNRDGSLIVSSSYDGLCRIWDTASGQCLKTLIDDDNPPVSFVKFSPNGKYILAATLDNTLKLWDYSK
GKCLKTYTGHKNEKYCIFANFSVTGGKWIVSGSEDNLVYIWNLQTKEIVQKLQGHTDVVISTACHPTENIIASAALENDK
TIKLWKSDC
;
A ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 
;N-{(1P)-5'-({(32E)-33-[(3P)-4-{[(1S)-3-amino-1-(3-chloro-4-fluorophenyl)-3-oxopropyl]carbamoyl}-3-(4-chloro-2-fluorophenyl)-1H-pyrrol-2-yl]-31-oxo-3,6,9,12,15,18,21,24,27-nonaoxa-30-azatritriacont-32-en-1-yl}carbamoyl)-2'-fluoro-4-[(3R,5S)-3,4,5-trimethylpiperazin-1-yl][1,1'-biphenyl]-3-yl}-6-oxo-4-(trifluoromethyl)-1,6-dihydropyridine-3-carboxamide
;
A1BAF 
4 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  SER n 
1 13  GLY n 
1 14  ARG n 
1 15  GLU n 
1 16  ASN n 
1 17  LEU n 
1 18  TYR n 
1 19  PHE n 
1 20  GLN n 
1 21  GLY n 
1 22  SER n 
1 23  SER n 
1 24  ARG n 
1 25  ALA n 
1 26  SER n 
1 27  ALA n 
1 28  PHE n 
1 29  ARG n 
1 30  PRO n 
1 31  ILE n 
1 32  SER n 
1 33  VAL n 
1 34  PHE n 
1 35  ARG n 
1 36  GLU n 
1 37  ALA n 
1 38  ASN n 
1 39  GLU n 
1 40  ASP n 
1 41  GLU n 
1 42  SER n 
1 43  GLY n 
1 44  PHE n 
1 45  THR n 
1 46  CYS n 
1 47  CYS n 
1 48  ALA n 
1 49  PHE n 
1 50  SER n 
1 51  ALA n 
1 52  ARG n 
1 53  GLU n 
1 54  ARG n 
1 55  PHE n 
1 56  LEU n 
1 57  MET n 
1 58  LEU n 
1 59  GLY n 
1 60  THR n 
1 61  CYS n 
1 62  THR n 
1 63  GLY n 
1 64  GLN n 
1 65  LEU n 
1 66  LYS n 
1 67  LEU n 
1 68  TYR n 
1 69  ASN n 
1 70  VAL n 
1 71  PHE n 
1 72  SER n 
1 73  GLY n 
1 74  GLN n 
1 75  GLU n 
1 76  GLU n 
1 77  ALA n 
1 78  SER n 
1 79  TYR n 
1 80  ASN n 
1 81  CYS n 
1 82  HIS n 
1 83  ASN n 
1 84  SER n 
1 85  ALA n 
1 86  ILE n 
1 87  THR n 
1 88  HIS n 
1 89  LEU n 
1 90  GLU n 
1 91  PRO n 
1 92  SER n 
1 93  ARG n 
1 94  ASP n 
1 95  GLY n 
1 96  SER n 
1 97  LEU n 
1 98  LEU n 
1 99  LEU n 
1 100 THR n 
1 101 SER n 
1 102 ALA n 
1 103 THR n 
1 104 TRP n 
1 105 SER n 
1 106 GLN n 
1 107 PRO n 
1 108 LEU n 
1 109 SER n 
1 110 ALA n 
1 111 LEU n 
1 112 TRP n 
1 113 GLY n 
1 114 MET n 
1 115 LYS n 
1 116 SER n 
1 117 VAL n 
1 118 PHE n 
1 119 ASP n 
1 120 MET n 
1 121 LYS n 
1 122 HIS n 
1 123 SER n 
1 124 PHE n 
1 125 THR n 
1 126 GLU n 
1 127 ASP n 
1 128 HIS n 
1 129 TYR n 
1 130 VAL n 
1 131 GLU n 
1 132 PHE n 
1 133 SER n 
1 134 LYS n 
1 135 HIS n 
1 136 SER n 
1 137 GLN n 
1 138 ASP n 
1 139 ARG n 
1 140 VAL n 
1 141 ILE n 
1 142 GLY n 
1 143 THR n 
1 144 LYS n 
1 145 GLY n 
1 146 ASP n 
1 147 ILE n 
1 148 ALA n 
1 149 HIS n 
1 150 ILE n 
1 151 TYR n 
1 152 ASP n 
1 153 ILE n 
1 154 GLN n 
1 155 THR n 
1 156 GLY n 
1 157 ASN n 
1 158 LYS n 
1 159 LEU n 
1 160 LEU n 
1 161 THR n 
1 162 LEU n 
1 163 PHE n 
1 164 ASN n 
1 165 PRO n 
1 166 ASP n 
1 167 LEU n 
1 168 ALA n 
1 169 ASN n 
1 170 ASN n 
1 171 TYR n 
1 172 LYS n 
1 173 ARG n 
1 174 ASN n 
1 175 CYS n 
1 176 ALA n 
1 177 THR n 
1 178 PHE n 
1 179 ASN n 
1 180 PRO n 
1 181 THR n 
1 182 ASP n 
1 183 ASP n 
1 184 LEU n 
1 185 VAL n 
1 186 LEU n 
1 187 ASN n 
1 188 ASP n 
1 189 GLY n 
1 190 VAL n 
1 191 LEU n 
1 192 TRP n 
1 193 ASP n 
1 194 VAL n 
1 195 ARG n 
1 196 SER n 
1 197 ALA n 
1 198 GLN n 
1 199 ALA n 
1 200 ILE n 
1 201 HIS n 
1 202 LYS n 
1 203 PHE n 
1 204 ASP n 
1 205 LYS n 
1 206 PHE n 
1 207 ASN n 
1 208 MET n 
1 209 ASN n 
1 210 ILE n 
1 211 SER n 
1 212 GLY n 
1 213 VAL n 
1 214 PHE n 
1 215 HIS n 
1 216 PRO n 
1 217 ASN n 
1 218 GLY n 
1 219 LEU n 
1 220 GLU n 
1 221 VAL n 
1 222 ILE n 
1 223 ILE n 
1 224 ASN n 
1 225 THR n 
1 226 GLU n 
1 227 ILE n 
1 228 TRP n 
1 229 ASP n 
1 230 LEU n 
1 231 ARG n 
1 232 THR n 
1 233 PHE n 
1 234 HIS n 
1 235 LEU n 
1 236 LEU n 
1 237 HIS n 
1 238 THR n 
1 239 VAL n 
1 240 PRO n 
1 241 ALA n 
1 242 LEU n 
1 243 ASP n 
1 244 GLN n 
1 245 CYS n 
1 246 ARG n 
1 247 VAL n 
1 248 VAL n 
1 249 PHE n 
1 250 ASN n 
1 251 HIS n 
1 252 THR n 
1 253 GLY n 
1 254 THR n 
1 255 VAL n 
1 256 MET n 
1 257 TYR n 
1 258 GLY n 
1 259 ALA n 
1 260 MET n 
1 261 LEU n 
1 262 GLN n 
1 263 ALA n 
1 264 ASP n 
1 265 ASP n 
1 266 GLU n 
1 267 ASP n 
1 268 ASP n 
1 269 LEU n 
1 270 MET n 
1 271 GLU n 
1 272 GLU n 
1 273 ARG n 
1 274 MET n 
1 275 LYS n 
1 276 SER n 
1 277 PRO n 
1 278 PHE n 
1 279 GLY n 
1 280 SER n 
1 281 SER n 
1 282 PHE n 
1 283 ARG n 
1 284 THR n 
1 285 PHE n 
1 286 ASN n 
1 287 ALA n 
1 288 THR n 
1 289 ASP n 
1 290 TYR n 
1 291 LYS n 
1 292 PRO n 
1 293 ILE n 
1 294 ALA n 
1 295 THR n 
1 296 ILE n 
1 297 ASP n 
1 298 VAL n 
1 299 LYS n 
1 300 ARG n 
1 301 ASN n 
1 302 ILE n 
1 303 PHE n 
1 304 ASP n 
1 305 LEU n 
1 306 CYS n 
1 307 THR n 
1 308 ASP n 
1 309 THR n 
1 310 LYS n 
1 311 ASP n 
1 312 CYS n 
1 313 TYR n 
1 314 LEU n 
1 315 ALA n 
1 316 VAL n 
1 317 ILE n 
1 318 GLU n 
1 319 ASN n 
1 320 GLN n 
1 321 GLY n 
1 322 SER n 
1 323 MET n 
1 324 ASP n 
1 325 ALA n 
1 326 LEU n 
1 327 ASN n 
1 328 MET n 
1 329 ASP n 
1 330 THR n 
1 331 VAL n 
1 332 CYS n 
1 333 ARG n 
1 334 LEU n 
1 335 TYR n 
1 336 GLU n 
1 337 VAL n 
1 338 GLY n 
2 1   MET n 
2 2   HIS n 
2 3   HIS n 
2 4   HIS n 
2 5   HIS n 
2 6   HIS n 
2 7   HIS n 
2 8   SER n 
2 9   SER n 
2 10  GLY n 
2 11  ARG n 
2 12  GLU n 
2 13  ASN n 
2 14  LEU n 
2 15  TYR n 
2 16  PHE n 
2 17  GLN n 
2 18  GLY n 
2 19  THR n 
2 20  GLN n 
2 21  SER n 
2 22  LYS n 
2 23  PRO n 
2 24  THR n 
2 25  PRO n 
2 26  VAL n 
2 27  LYS n 
2 28  PRO n 
2 29  ASN n 
2 30  TYR n 
2 31  ALA n 
2 32  LEU n 
2 33  LYS n 
2 34  PHE n 
2 35  THR n 
2 36  LEU n 
2 37  ALA n 
2 38  GLY n 
2 39  HIS n 
2 40  THR n 
2 41  LYS n 
2 42  ALA n 
2 43  VAL n 
2 44  SER n 
2 45  SER n 
2 46  VAL n 
2 47  LYS n 
2 48  PHE n 
2 49  SER n 
2 50  PRO n 
2 51  ASN n 
2 52  GLY n 
2 53  GLU n 
2 54  TRP n 
2 55  LEU n 
2 56  ALA n 
2 57  SER n 
2 58  SER n 
2 59  SER n 
2 60  ALA n 
2 61  ASP n 
2 62  LYS n 
2 63  LEU n 
2 64  ILE n 
2 65  LYS n 
2 66  ILE n 
2 67  TRP n 
2 68  GLY n 
2 69  ALA n 
2 70  TYR n 
2 71  ASP n 
2 72  GLY n 
2 73  LYS n 
2 74  PHE n 
2 75  GLU n 
2 76  LYS n 
2 77  THR n 
2 78  ILE n 
2 79  SER n 
2 80  GLY n 
2 81  HIS n 
2 82  LYS n 
2 83  LEU n 
2 84  GLY n 
2 85  ILE n 
2 86  SER n 
2 87  ASP n 
2 88  VAL n 
2 89  ALA n 
2 90  TRP n 
2 91  SER n 
2 92  SER n 
2 93  ASP n 
2 94  SER n 
2 95  ASN n 
2 96  LEU n 
2 97  LEU n 
2 98  VAL n 
2 99  SER n 
2 100 ALA n 
2 101 SER n 
2 102 ASP n 
2 103 ASP n 
2 104 LYS n 
2 105 THR n 
2 106 LEU n 
2 107 LYS n 
2 108 ILE n 
2 109 TRP n 
2 110 ASP n 
2 111 VAL n 
2 112 SER n 
2 113 SER n 
2 114 GLY n 
2 115 LYS n 
2 116 CYS n 
2 117 LEU n 
2 118 LYS n 
2 119 THR n 
2 120 LEU n 
2 121 LYS n 
2 122 GLY n 
2 123 HIS n 
2 124 SER n 
2 125 ASN n 
2 126 TYR n 
2 127 VAL n 
2 128 PHE n 
2 129 CYS n 
2 130 CYS n 
2 131 ASN n 
2 132 PHE n 
2 133 ASN n 
2 134 PRO n 
2 135 GLN n 
2 136 SER n 
2 137 ASN n 
2 138 LEU n 
2 139 ILE n 
2 140 VAL n 
2 141 SER n 
2 142 GLY n 
2 143 SER n 
2 144 PHE n 
2 145 ASP n 
2 146 GLU n 
2 147 SER n 
2 148 VAL n 
2 149 ARG n 
2 150 ILE n 
2 151 TRP n 
2 152 ASP n 
2 153 VAL n 
2 154 LYS n 
2 155 THR n 
2 156 GLY n 
2 157 LYS n 
2 158 CYS n 
2 159 LEU n 
2 160 LYS n 
2 161 THR n 
2 162 LEU n 
2 163 PRO n 
2 164 ALA n 
2 165 HIS n 
2 166 SER n 
2 167 ASP n 
2 168 PRO n 
2 169 VAL n 
2 170 SER n 
2 171 ALA n 
2 172 VAL n 
2 173 HIS n 
2 174 PHE n 
2 175 ASN n 
2 176 ARG n 
2 177 ASP n 
2 178 GLY n 
2 179 SER n 
2 180 LEU n 
2 181 ILE n 
2 182 VAL n 
2 183 SER n 
2 184 SER n 
2 185 SER n 
2 186 TYR n 
2 187 ASP n 
2 188 GLY n 
2 189 LEU n 
2 190 CYS n 
2 191 ARG n 
2 192 ILE n 
2 193 TRP n 
2 194 ASP n 
2 195 THR n 
2 196 ALA n 
2 197 SER n 
2 198 GLY n 
2 199 GLN n 
2 200 CYS n 
2 201 LEU n 
2 202 LYS n 
2 203 THR n 
2 204 LEU n 
2 205 ILE n 
2 206 ASP n 
2 207 ASP n 
2 208 ASP n 
2 209 ASN n 
2 210 PRO n 
2 211 PRO n 
2 212 VAL n 
2 213 SER n 
2 214 PHE n 
2 215 VAL n 
2 216 LYS n 
2 217 PHE n 
2 218 SER n 
2 219 PRO n 
2 220 ASN n 
2 221 GLY n 
2 222 LYS n 
2 223 TYR n 
2 224 ILE n 
2 225 LEU n 
2 226 ALA n 
2 227 ALA n 
2 228 THR n 
2 229 LEU n 
2 230 ASP n 
2 231 ASN n 
2 232 THR n 
2 233 LEU n 
2 234 LYS n 
2 235 LEU n 
2 236 TRP n 
2 237 ASP n 
2 238 TYR n 
2 239 SER n 
2 240 LYS n 
2 241 GLY n 
2 242 LYS n 
2 243 CYS n 
2 244 LEU n 
2 245 LYS n 
2 246 THR n 
2 247 TYR n 
2 248 THR n 
2 249 GLY n 
2 250 HIS n 
2 251 LYS n 
2 252 ASN n 
2 253 GLU n 
2 254 LYS n 
2 255 TYR n 
2 256 CYS n 
2 257 ILE n 
2 258 PHE n 
2 259 ALA n 
2 260 ASN n 
2 261 PHE n 
2 262 SER n 
2 263 VAL n 
2 264 THR n 
2 265 GLY n 
2 266 GLY n 
2 267 LYS n 
2 268 TRP n 
2 269 ILE n 
2 270 VAL n 
2 271 SER n 
2 272 GLY n 
2 273 SER n 
2 274 GLU n 
2 275 ASP n 
2 276 ASN n 
2 277 LEU n 
2 278 VAL n 
2 279 TYR n 
2 280 ILE n 
2 281 TRP n 
2 282 ASN n 
2 283 LEU n 
2 284 GLN n 
2 285 THR n 
2 286 LYS n 
2 287 GLU n 
2 288 ILE n 
2 289 VAL n 
2 290 GLN n 
2 291 LYS n 
2 292 LEU n 
2 293 GLN n 
2 294 GLY n 
2 295 HIS n 
2 296 THR n 
2 297 ASP n 
2 298 VAL n 
2 299 VAL n 
2 300 ILE n 
2 301 SER n 
2 302 THR n 
2 303 ALA n 
2 304 CYS n 
2 305 HIS n 
2 306 PRO n 
2 307 THR n 
2 308 GLU n 
2 309 ASN n 
2 310 ILE n 
2 311 ILE n 
2 312 ALA n 
2 313 SER n 
2 314 ALA n 
2 315 ALA n 
2 316 LEU n 
2 317 GLU n 
2 318 ASN n 
2 319 ASP n 
2 320 LYS n 
2 321 THR n 
2 322 ILE n 
2 323 LYS n 
2 324 LEU n 
2 325 TRP n 
2 326 LYS n 
2 327 SER n 
2 328 ASP n 
2 329 CYS 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' 1 338 human ? 'DCAF1, KIAA0800, RIP, VPRBP' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 329 human ? 'WDR5, BIG3'                  ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
A1BAF non-polymer         . 
;N-{(1P)-5'-({(32E)-33-[(3P)-4-{[(1S)-3-amino-1-(3-chloro-4-fluorophenyl)-3-oxopropyl]carbamoyl}-3-(4-chloro-2-fluorophenyl)-1H-pyrrol-2-yl]-31-oxo-3,6,9,12,15,18,21,24,27-nonaoxa-30-azatritriacont-32-en-1-yl}carbamoyl)-2'-fluoro-4-[(3R,5S)-3,4,5-trimethylpiperazin-1-yl][1,1'-biphenyl]-3-yl}-6-oxo-4-(trifluoromethyl)-1,6-dihydropyridine-3-carboxamide
;
OICR-41114 'C70 H83 Cl2 F6 N9 O15' 1475.356 
ALA   'L-peptide linking' y ALANINE ?          'C3 H7 N O2'            89.093   
ARG   'L-peptide linking' y ARGININE ?          'C6 H15 N4 O2 1'        175.209  
ASN   'L-peptide linking' y ASPARAGINE ?          'C4 H8 N2 O3'           132.118  
ASP   'L-peptide linking' y 'ASPARTIC ACID' ?          'C4 H7 N O4'            133.103  
CYS   'L-peptide linking' y CYSTEINE ?          'C3 H7 N O2 S'          121.158  
GLN   'L-peptide linking' y GLUTAMINE ?          'C5 H10 N2 O3'          146.144  
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ?          'C5 H9 N O4'            147.129  
GLY   'peptide linking'   y GLYCINE ?          'C2 H5 N O2'            75.067   
HIS   'L-peptide linking' y HISTIDINE ?          'C6 H10 N3 O2 1'        156.162  
HOH   non-polymer         . WATER ?          'H2 O'                  18.015   
ILE   'L-peptide linking' y ISOLEUCINE ?          'C6 H13 N O2'           131.173  
LEU   'L-peptide linking' y LEUCINE ?          'C6 H13 N O2'           131.173  
LYS   'L-peptide linking' y LYSINE ?          'C6 H15 N2 O2 1'        147.195  
MET   'L-peptide linking' y METHIONINE ?          'C5 H11 N O2 S'         149.211  
PHE   'L-peptide linking' y PHENYLALANINE ?          'C9 H11 N O2'           165.189  
PRO   'L-peptide linking' y PROLINE ?          'C5 H9 N O2'            115.130  
SER   'L-peptide linking' y SERINE ?          'C3 H7 N O3'            105.093  
THR   'L-peptide linking' y THREONINE ?          'C4 H9 N O3'            119.119  
TRP   'L-peptide linking' y TRYPTOPHAN ?          'C11 H12 N2 O2'         204.225  
TYR   'L-peptide linking' y TYROSINE ?          'C9 H11 N O3'           181.189  
VAL   'L-peptide linking' y VALINE ?          'C5 H11 N O2'           117.146  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1053 ?    ?   ?   B . n 
A 1 2   GLY 2   1054 ?    ?   ?   B . n 
A 1 3   SER 3   1055 ?    ?   ?   B . n 
A 1 4   SER 4   1056 ?    ?   ?   B . n 
A 1 5   HIS 5   1057 ?    ?   ?   B . n 
A 1 6   HIS 6   1058 ?    ?   ?   B . n 
A 1 7   HIS 7   1059 ?    ?   ?   B . n 
A 1 8   HIS 8   1060 ?    ?   ?   B . n 
A 1 9   HIS 9   1061 ?    ?   ?   B . n 
A 1 10  HIS 10  1062 ?    ?   ?   B . n 
A 1 11  SER 11  1063 ?    ?   ?   B . n 
A 1 12  SER 12  1064 ?    ?   ?   B . n 
A 1 13  GLY 13  1065 ?    ?   ?   B . n 
A 1 14  ARG 14  1066 ?    ?   ?   B . n 
A 1 15  GLU 15  1067 ?    ?   ?   B . n 
A 1 16  ASN 16  1068 ?    ?   ?   B . n 
A 1 17  LEU 17  1069 ?    ?   ?   B . n 
A 1 18  TYR 18  1070 ?    ?   ?   B . n 
A 1 19  PHE 19  1071 ?    ?   ?   B . n 
A 1 20  GLN 20  1072 ?    ?   ?   B . n 
A 1 21  GLY 21  1073 ?    ?   ?   B . n 
A 1 22  SER 22  1074 ?    ?   ?   B . n 
A 1 23  SER 23  1075 ?    ?   ?   B . n 
A 1 24  ARG 24  1076 ?    ?   ?   B . n 
A 1 25  ALA 25  1077 ?    ?   ?   B . n 
A 1 26  SER 26  1078 ?    ?   ?   B . n 
A 1 27  ALA 27  1079 ?    ?   ?   B . n 
A 1 28  PHE 28  1080 1080 PHE PHE B . n 
A 1 29  ARG 29  1081 1081 ARG ARG B . n 
A 1 30  PRO 30  1082 1082 PRO PRO B . n 
A 1 31  ILE 31  1083 1083 ILE ILE B . n 
A 1 32  SER 32  1084 1084 SER SER B . n 
A 1 33  VAL 33  1085 1085 VAL VAL B . n 
A 1 34  PHE 34  1086 1086 PHE PHE B . n 
A 1 35  ARG 35  1087 1087 ARG ARG B . n 
A 1 36  GLU 36  1088 1088 GLU GLU B . n 
A 1 37  ALA 37  1089 1089 ALA ALA B . n 
A 1 38  ASN 38  1090 1090 ASN ASN B . n 
A 1 39  GLU 39  1091 1091 GLU GLU B . n 
A 1 40  ASP 40  1092 1092 ASP ASP B . n 
A 1 41  GLU 41  1093 1093 GLU GLU B . n 
A 1 42  SER 42  1094 1094 SER SER B . n 
A 1 43  GLY 43  1095 1095 GLY GLY B . n 
A 1 44  PHE 44  1096 1096 PHE PHE B . n 
A 1 45  THR 45  1097 1097 THR THR B . n 
A 1 46  CYS 46  1098 1098 CYS CYS B . n 
A 1 47  CYS 47  1099 1099 CYS CYS B . n 
A 1 48  ALA 48  1100 1100 ALA ALA B . n 
A 1 49  PHE 49  1101 1101 PHE PHE B . n 
A 1 50  SER 50  1102 1102 SER SER B . n 
A 1 51  ALA 51  1103 1103 ALA ALA B . n 
A 1 52  ARG 52  1104 1104 ARG ARG B . n 
A 1 53  GLU 53  1105 1105 GLU GLU B . n 
A 1 54  ARG 54  1106 1106 ARG ARG B . n 
A 1 55  PHE 55  1107 1107 PHE PHE B . n 
A 1 56  LEU 56  1108 1108 LEU LEU B . n 
A 1 57  MET 57  1109 1109 MET MET B . n 
A 1 58  LEU 58  1110 1110 LEU LEU B . n 
A 1 59  GLY 59  1111 1111 GLY GLY B . n 
A 1 60  THR 60  1112 1112 THR THR B . n 
A 1 61  CYS 61  1113 1113 CYS CYS B . n 
A 1 62  THR 62  1114 1114 THR THR B . n 
A 1 63  GLY 63  1115 1115 GLY GLY B . n 
A 1 64  GLN 64  1116 1116 GLN GLN B . n 
A 1 65  LEU 65  1117 1117 LEU LEU B . n 
A 1 66  LYS 66  1118 1118 LYS LYS B . n 
A 1 67  LEU 67  1119 1119 LEU LEU B . n 
A 1 68  TYR 68  1120 1120 TYR TYR B . n 
A 1 69  ASN 69  1121 1121 ASN ASN B . n 
A 1 70  VAL 70  1122 1122 VAL VAL B . n 
A 1 71  PHE 71  1123 1123 PHE PHE B . n 
A 1 72  SER 72  1124 1124 SER SER B . n 
A 1 73  GLY 73  1125 1125 GLY GLY B . n 
A 1 74  GLN 74  1126 1126 GLN GLN B . n 
A 1 75  GLU 75  1127 1127 GLU GLU B . n 
A 1 76  GLU 76  1128 1128 GLU GLU B . n 
A 1 77  ALA 77  1129 1129 ALA ALA B . n 
A 1 78  SER 78  1130 1130 SER SER B . n 
A 1 79  TYR 79  1131 1131 TYR TYR B . n 
A 1 80  ASN 80  1132 1132 ASN ASN B . n 
A 1 81  CYS 81  1133 1133 CYS CYS B . n 
A 1 82  HIS 82  1134 1134 HIS HIS B . n 
A 1 83  ASN 83  1135 1135 ASN ASN B . n 
A 1 84  SER 84  1136 1136 SER SER B . n 
A 1 85  ALA 85  1137 1137 ALA ALA B . n 
A 1 86  ILE 86  1138 1138 ILE ILE B . n 
A 1 87  THR 87  1139 1139 THR THR B . n 
A 1 88  HIS 88  1140 1140 HIS HIS B . n 
A 1 89  LEU 89  1141 1141 LEU LEU B . n 
A 1 90  GLU 90  1142 1142 GLU GLU B . n 
A 1 91  PRO 91  1143 1143 PRO PRO B . n 
A 1 92  SER 92  1144 1144 SER SER B . n 
A 1 93  ARG 93  1145 1145 ARG ARG B . n 
A 1 94  ASP 94  1146 1146 ASP ASP B . n 
A 1 95  GLY 95  1147 1147 GLY GLY B . n 
A 1 96  SER 96  1148 1148 SER SER B . n 
A 1 97  LEU 97  1149 1149 LEU LEU B . n 
A 1 98  LEU 98  1150 1150 LEU LEU B . n 
A 1 99  LEU 99  1151 1151 LEU LEU B . n 
A 1 100 THR 100 1152 1152 THR THR B . n 
A 1 101 SER 101 1153 1153 SER SER B . n 
A 1 102 ALA 102 1154 1154 ALA ALA B . n 
A 1 103 THR 103 1155 1155 THR THR B . n 
A 1 104 TRP 104 1156 1156 TRP TRP B . n 
A 1 105 SER 105 1157 1157 SER SER B . n 
A 1 106 GLN 106 1158 1158 GLN GLN B . n 
A 1 107 PRO 107 1159 1159 PRO PRO B . n 
A 1 108 LEU 108 1160 1160 LEU LEU B . n 
A 1 109 SER 109 1161 1161 SER SER B . n 
A 1 110 ALA 110 1162 1162 ALA ALA B . n 
A 1 111 LEU 111 1163 1163 LEU LEU B . n 
A 1 112 TRP 112 1164 1164 TRP TRP B . n 
A 1 113 GLY 113 1165 1165 GLY GLY B . n 
A 1 114 MET 114 1166 1166 MET MET B . n 
A 1 115 LYS 115 1167 1167 LYS LYS B . n 
A 1 116 SER 116 1168 1168 SER SER B . n 
A 1 117 VAL 117 1169 1169 VAL VAL B . n 
A 1 118 PHE 118 1170 1170 PHE PHE B . n 
A 1 119 ASP 119 1171 1171 ASP ASP B . n 
A 1 120 MET 120 1172 1172 MET MET B . n 
A 1 121 LYS 121 1173 1173 LYS LYS B . n 
A 1 122 HIS 122 1174 1174 HIS HIS B . n 
A 1 123 SER 123 1175 1175 SER SER B . n 
A 1 124 PHE 124 1176 1176 PHE PHE B . n 
A 1 125 THR 125 1177 1177 THR THR B . n 
A 1 126 GLU 126 1178 1178 GLU GLU B . n 
A 1 127 ASP 127 1179 1179 ASP ASP B . n 
A 1 128 HIS 128 1180 1180 HIS HIS B . n 
A 1 129 TYR 129 1181 1181 TYR TYR B . n 
A 1 130 VAL 130 1182 1182 VAL VAL B . n 
A 1 131 GLU 131 1183 1183 GLU GLU B . n 
A 1 132 PHE 132 1184 1184 PHE PHE B . n 
A 1 133 SER 133 1185 1185 SER SER B . n 
A 1 134 LYS 134 1186 1186 LYS LYS B . n 
A 1 135 HIS 135 1187 1187 HIS HIS B . n 
A 1 136 SER 136 1188 1188 SER SER B . n 
A 1 137 GLN 137 1189 1189 GLN GLN B . n 
A 1 138 ASP 138 1190 1190 ASP ASP B . n 
A 1 139 ARG 139 1191 1191 ARG ARG B . n 
A 1 140 VAL 140 1192 1192 VAL VAL B . n 
A 1 141 ILE 141 1193 1193 ILE ILE B . n 
A 1 142 GLY 142 1194 1194 GLY GLY B . n 
A 1 143 THR 143 1195 1195 THR THR B . n 
A 1 144 LYS 144 1196 1196 LYS LYS B . n 
A 1 145 GLY 145 1197 1197 GLY GLY B . n 
A 1 146 ASP 146 1198 1198 ASP ASP B . n 
A 1 147 ILE 147 1199 1199 ILE ILE B . n 
A 1 148 ALA 148 1200 1200 ALA ALA B . n 
A 1 149 HIS 149 1201 1201 HIS HIS B . n 
A 1 150 ILE 150 1202 1202 ILE ILE B . n 
A 1 151 TYR 151 1203 1203 TYR TYR B . n 
A 1 152 ASP 152 1204 1204 ASP ASP B . n 
A 1 153 ILE 153 1205 1205 ILE ILE B . n 
A 1 154 GLN 154 1206 1206 GLN GLN B . n 
A 1 155 THR 155 1207 1207 THR THR B . n 
A 1 156 GLY 156 1208 1208 GLY GLY B . n 
A 1 157 ASN 157 1209 1209 ASN ASN B . n 
A 1 158 LYS 158 1210 1210 LYS LYS B . n 
A 1 159 LEU 159 1211 1211 LEU LEU B . n 
A 1 160 LEU 160 1212 1212 LEU LEU B . n 
A 1 161 THR 161 1213 1213 THR THR B . n 
A 1 162 LEU 162 1214 1214 LEU LEU B . n 
A 1 163 PHE 163 1215 1215 PHE PHE B . n 
A 1 164 ASN 164 1216 1216 ASN ASN B . n 
A 1 165 PRO 165 1217 1217 PRO PRO B . n 
A 1 166 ASP 166 1218 1218 ASP ASP B . n 
A 1 167 LEU 167 1219 1219 LEU LEU B . n 
A 1 168 ALA 168 1220 1220 ALA ALA B . n 
A 1 169 ASN 169 1221 1221 ASN ASN B . n 
A 1 170 ASN 170 1222 1222 ASN ASN B . n 
A 1 171 TYR 171 1223 1223 TYR TYR B . n 
A 1 172 LYS 172 1224 1224 LYS LYS B . n 
A 1 173 ARG 173 1225 1225 ARG ARG B . n 
A 1 174 ASN 174 1226 1226 ASN ASN B . n 
A 1 175 CYS 175 1227 1227 CYS CYS B . n 
A 1 176 ALA 176 1228 1228 ALA ALA B . n 
A 1 177 THR 177 1229 1229 THR THR B . n 
A 1 178 PHE 178 1230 1230 PHE PHE B . n 
A 1 179 ASN 179 1231 1231 ASN ASN B . n 
A 1 180 PRO 180 1232 1232 PRO PRO B . n 
A 1 181 THR 181 1233 1233 THR THR B . n 
A 1 182 ASP 182 1234 1234 ASP ASP B . n 
A 1 183 ASP 183 1235 1235 ASP ASP B . n 
A 1 184 LEU 184 1236 1236 LEU LEU B . n 
A 1 185 VAL 185 1237 1237 VAL VAL B . n 
A 1 186 LEU 186 1238 1238 LEU LEU B . n 
A 1 187 ASN 187 1239 1239 ASN ASN B . n 
A 1 188 ASP 188 1240 1240 ASP ASP B . n 
A 1 189 GLY 189 1241 1241 GLY GLY B . n 
A 1 190 VAL 190 1242 1242 VAL VAL B . n 
A 1 191 LEU 191 1243 1243 LEU LEU B . n 
A 1 192 TRP 192 1244 1244 TRP TRP B . n 
A 1 193 ASP 193 1245 1245 ASP ASP B . n 
A 1 194 VAL 194 1246 1246 VAL VAL B . n 
A 1 195 ARG 195 1247 1247 ARG ARG B . n 
A 1 196 SER 196 1248 1248 SER SER B . n 
A 1 197 ALA 197 1249 1249 ALA ALA B . n 
A 1 198 GLN 198 1250 1250 GLN GLN B . n 
A 1 199 ALA 199 1251 1251 ALA ALA B . n 
A 1 200 ILE 200 1252 1252 ILE ILE B . n 
A 1 201 HIS 201 1253 1253 HIS HIS B . n 
A 1 202 LYS 202 1254 1254 LYS LYS B . n 
A 1 203 PHE 203 1255 1255 PHE PHE B . n 
A 1 204 ASP 204 1256 1256 ASP ASP B . n 
A 1 205 LYS 205 1257 1257 LYS LYS B . n 
A 1 206 PHE 206 1258 1258 PHE PHE B . n 
A 1 207 ASN 207 1259 1259 ASN ASN B . n 
A 1 208 MET 208 1260 1260 MET MET B . n 
A 1 209 ASN 209 1261 1261 ASN ASN B . n 
A 1 210 ILE 210 1262 1262 ILE ILE B . n 
A 1 211 SER 211 1263 1263 SER SER B . n 
A 1 212 GLY 212 1264 1264 GLY GLY B . n 
A 1 213 VAL 213 1265 1265 VAL VAL B . n 
A 1 214 PHE 214 1266 1266 PHE PHE B . n 
A 1 215 HIS 215 1267 1267 HIS HIS B . n 
A 1 216 PRO 216 1268 1268 PRO PRO B . n 
A 1 217 ASN 217 1269 1269 ASN ASN B . n 
A 1 218 GLY 218 1270 1270 GLY GLY B . n 
A 1 219 LEU 219 1271 1271 LEU LEU B . n 
A 1 220 GLU 220 1272 1272 GLU GLU B . n 
A 1 221 VAL 221 1273 1273 VAL VAL B . n 
A 1 222 ILE 222 1274 1274 ILE ILE B . n 
A 1 223 ILE 223 1275 1275 ILE ILE B . n 
A 1 224 ASN 224 1276 1276 ASN ASN B . n 
A 1 225 THR 225 1277 1277 THR THR B . n 
A 1 226 GLU 226 1278 1278 GLU GLU B . n 
A 1 227 ILE 227 1279 1279 ILE ILE B . n 
A 1 228 TRP 228 1280 1280 TRP TRP B . n 
A 1 229 ASP 229 1281 1281 ASP ASP B . n 
A 1 230 LEU 230 1282 1282 LEU LEU B . n 
A 1 231 ARG 231 1283 1283 ARG ARG B . n 
A 1 232 THR 232 1284 1284 THR THR B . n 
A 1 233 PHE 233 1285 1285 PHE PHE B . n 
A 1 234 HIS 234 1286 1286 HIS HIS B . n 
A 1 235 LEU 235 1287 1287 LEU LEU B . n 
A 1 236 LEU 236 1288 1288 LEU LEU B . n 
A 1 237 HIS 237 1289 1289 HIS HIS B . n 
A 1 238 THR 238 1290 1290 THR THR B . n 
A 1 239 VAL 239 1291 1291 VAL VAL B . n 
A 1 240 PRO 240 1292 1292 PRO PRO B . n 
A 1 241 ALA 241 1293 1293 ALA ALA B . n 
A 1 242 LEU 242 1294 1294 LEU LEU B . n 
A 1 243 ASP 243 1295 1295 ASP ASP B . n 
A 1 244 GLN 244 1296 1296 GLN GLN B . n 
A 1 245 CYS 245 1297 1297 CYS CYS B . n 
A 1 246 ARG 246 1298 1298 ARG ARG B . n 
A 1 247 VAL 247 1299 1299 VAL VAL B . n 
A 1 248 VAL 248 1300 1300 VAL VAL B . n 
A 1 249 PHE 249 1301 1301 PHE PHE B . n 
A 1 250 ASN 250 1302 1302 ASN ASN B . n 
A 1 251 HIS 251 1303 1303 HIS HIS B . n 
A 1 252 THR 252 1304 1304 THR THR B . n 
A 1 253 GLY 253 1305 1305 GLY GLY B . n 
A 1 254 THR 254 1306 1306 THR THR B . n 
A 1 255 VAL 255 1307 1307 VAL VAL B . n 
A 1 256 MET 256 1308 1308 MET MET B . n 
A 1 257 TYR 257 1309 1309 TYR TYR B . n 
A 1 258 GLY 258 1310 1310 GLY GLY B . n 
A 1 259 ALA 259 1311 1311 ALA ALA B . n 
A 1 260 MET 260 1312 1312 MET MET B . n 
A 1 261 LEU 261 1313 1313 LEU LEU B . n 
A 1 262 GLN 262 1314 1314 GLN GLN B . n 
A 1 263 ALA 263 1315 1315 ALA ALA B . n 
A 1 264 ASP 264 1316 1316 ASP ASP B . n 
A 1 265 ASP 265 1317 1317 ASP ASP B . n 
A 1 266 GLU 266 1318 1318 GLU GLU B . n 
A 1 267 ASP 267 1319 1319 ASP ASP B . n 
A 1 268 ASP 268 1320 1320 ASP ASP B . n 
A 1 269 LEU 269 1321 1321 LEU LEU B . n 
A 1 270 MET 270 1322 1322 MET MET B . n 
A 1 271 GLU 271 1323 1323 GLU GLU B . n 
A 1 272 GLU 272 1324 1324 GLU GLU B . n 
A 1 273 ARG 273 1325 1325 ARG ARG B . n 
A 1 274 MET 274 1326 1326 MET MET B . n 
A 1 275 LYS 275 1327 1327 LYS LYS B . n 
A 1 276 SER 276 1328 1328 SER SER B . n 
A 1 277 PRO 277 1329 1329 PRO PRO B . n 
A 1 278 PHE 278 1330 1330 PHE PHE B . n 
A 1 279 GLY 279 1331 1331 GLY GLY B . n 
A 1 280 SER 280 1332 1332 SER SER B . n 
A 1 281 SER 281 1333 1333 SER SER B . n 
A 1 282 PHE 282 1334 1334 PHE PHE B . n 
A 1 283 ARG 283 1335 1335 ARG ARG B . n 
A 1 284 THR 284 1336 1336 THR THR B . n 
A 1 285 PHE 285 1337 1337 PHE PHE B . n 
A 1 286 ASN 286 1338 1338 ASN ASN B . n 
A 1 287 ALA 287 1339 1339 ALA ALA B . n 
A 1 288 THR 288 1340 1340 THR THR B . n 
A 1 289 ASP 289 1341 1341 ASP ASP B . n 
A 1 290 TYR 290 1342 1342 TYR TYR B . n 
A 1 291 LYS 291 1343 1343 LYS LYS B . n 
A 1 292 PRO 292 1344 1344 PRO PRO B . n 
A 1 293 ILE 293 1345 1345 ILE ILE B . n 
A 1 294 ALA 294 1346 1346 ALA ALA B . n 
A 1 295 THR 295 1347 1347 THR THR B . n 
A 1 296 ILE 296 1348 1348 ILE ILE B . n 
A 1 297 ASP 297 1349 1349 ASP ASP B . n 
A 1 298 VAL 298 1350 1350 VAL VAL B . n 
A 1 299 LYS 299 1351 1351 LYS LYS B . n 
A 1 300 ARG 300 1352 1352 ARG ARG B . n 
A 1 301 ASN 301 1353 1353 ASN ASN B . n 
A 1 302 ILE 302 1354 1354 ILE ILE B . n 
A 1 303 PHE 303 1355 1355 PHE PHE B . n 
A 1 304 ASP 304 1356 1356 ASP ASP B . n 
A 1 305 LEU 305 1357 1357 LEU LEU B . n 
A 1 306 CYS 306 1358 1358 CYS CYS B . n 
A 1 307 THR 307 1359 1359 THR THR B . n 
A 1 308 ASP 308 1360 1360 ASP ASP B . n 
A 1 309 THR 309 1361 1361 THR THR B . n 
A 1 310 LYS 310 1362 1362 LYS LYS B . n 
A 1 311 ASP 311 1363 1363 ASP ASP B . n 
A 1 312 CYS 312 1364 1364 CYS CYS B . n 
A 1 313 TYR 313 1365 1365 TYR TYR B . n 
A 1 314 LEU 314 1366 1366 LEU LEU B . n 
A 1 315 ALA 315 1367 1367 ALA ALA B . n 
A 1 316 VAL 316 1368 1368 VAL VAL B . n 
A 1 317 ILE 317 1369 1369 ILE ILE B . n 
A 1 318 GLU 318 1370 1370 GLU GLU B . n 
A 1 319 ASN 319 1371 1371 ASN ASN B . n 
A 1 320 GLN 320 1372 1372 GLN GLN B . n 
A 1 321 GLY 321 1373 1373 GLY GLY B . n 
A 1 322 SER 322 1374 1374 SER SER B . n 
A 1 323 MET 323 1375 1375 MET MET B . n 
A 1 324 ASP 324 1376 1376 ASP ASP B . n 
A 1 325 ALA 325 1377 1377 ALA ALA B . n 
A 1 326 LEU 326 1378 1378 LEU LEU B . n 
A 1 327 ASN 327 1379 1379 ASN ASN B . n 
A 1 328 MET 328 1380 1380 MET MET B . n 
A 1 329 ASP 329 1381 1381 ASP ASP B . n 
A 1 330 THR 330 1382 1382 THR THR B . n 
A 1 331 VAL 331 1383 1383 VAL VAL B . n 
A 1 332 CYS 332 1384 1384 CYS CYS B . n 
A 1 333 ARG 333 1385 1385 ARG ARG B . n 
A 1 334 LEU 334 1386 1386 LEU LEU B . n 
A 1 335 TYR 335 1387 1387 TYR TYR B . n 
A 1 336 GLU 336 1388 1388 GLU GLU B . n 
A 1 337 VAL 337 1389 1389 VAL VAL B . n 
A 1 338 GLY 338 1390 1390 GLY GLY B . n 
B 2 1   MET 1   6    ?    ?   ?   A . n 
B 2 2   HIS 2   7    ?    ?   ?   A . n 
B 2 3   HIS 3   8    ?    ?   ?   A . n 
B 2 4   HIS 4   9    ?    ?   ?   A . n 
B 2 5   HIS 5   10   ?    ?   ?   A . n 
B 2 6   HIS 6   11   ?    ?   ?   A . n 
B 2 7   HIS 7   12   ?    ?   ?   A . n 
B 2 8   SER 8   13   ?    ?   ?   A . n 
B 2 9   SER 9   14   ?    ?   ?   A . n 
B 2 10  GLY 10  15   ?    ?   ?   A . n 
B 2 11  ARG 11  16   ?    ?   ?   A . n 
B 2 12  GLU 12  17   ?    ?   ?   A . n 
B 2 13  ASN 13  18   ?    ?   ?   A . n 
B 2 14  LEU 14  19   ?    ?   ?   A . n 
B 2 15  TYR 15  20   ?    ?   ?   A . n 
B 2 16  PHE 16  21   ?    ?   ?   A . n 
B 2 17  GLN 17  22   ?    ?   ?   A . n 
B 2 18  GLY 18  23   ?    ?   ?   A . n 
B 2 19  THR 19  24   ?    ?   ?   A . n 
B 2 20  GLN 20  25   ?    ?   ?   A . n 
B 2 21  SER 21  26   ?    ?   ?   A . n 
B 2 22  LYS 22  27   ?    ?   ?   A . n 
B 2 23  PRO 23  28   ?    ?   ?   A . n 
B 2 24  THR 24  29   ?    ?   ?   A . n 
B 2 25  PRO 25  30   ?    ?   ?   A . n 
B 2 26  VAL 26  31   31   VAL VAL A . n 
B 2 27  LYS 27  32   32   LYS LYS A . n 
B 2 28  PRO 28  33   33   PRO PRO A . n 
B 2 29  ASN 29  34   34   ASN ASN A . n 
B 2 30  TYR 30  35   35   TYR TYR A . n 
B 2 31  ALA 31  36   36   ALA ALA A . n 
B 2 32  LEU 32  37   37   LEU LEU A . n 
B 2 33  LYS 33  38   38   LYS LYS A . n 
B 2 34  PHE 34  39   39   PHE PHE A . n 
B 2 35  THR 35  40   40   THR THR A . n 
B 2 36  LEU 36  41   41   LEU LEU A . n 
B 2 37  ALA 37  42   42   ALA ALA A . n 
B 2 38  GLY 38  43   43   GLY GLY A . n 
B 2 39  HIS 39  44   44   HIS HIS A . n 
B 2 40  THR 40  45   45   THR THR A . n 
B 2 41  LYS 41  46   46   LYS LYS A . n 
B 2 42  ALA 42  47   47   ALA ALA A . n 
B 2 43  VAL 43  48   48   VAL VAL A . n 
B 2 44  SER 44  49   49   SER SER A . n 
B 2 45  SER 45  50   50   SER SER A . n 
B 2 46  VAL 46  51   51   VAL VAL A . n 
B 2 47  LYS 47  52   52   LYS LYS A . n 
B 2 48  PHE 48  53   53   PHE PHE A . n 
B 2 49  SER 49  54   54   SER SER A . n 
B 2 50  PRO 50  55   55   PRO PRO A . n 
B 2 51  ASN 51  56   56   ASN ASN A . n 
B 2 52  GLY 52  57   57   GLY GLY A . n 
B 2 53  GLU 53  58   58   GLU GLU A . n 
B 2 54  TRP 54  59   59   TRP TRP A . n 
B 2 55  LEU 55  60   60   LEU LEU A . n 
B 2 56  ALA 56  61   61   ALA ALA A . n 
B 2 57  SER 57  62   62   SER SER A . n 
B 2 58  SER 58  63   63   SER SER A . n 
B 2 59  SER 59  64   64   SER SER A . n 
B 2 60  ALA 60  65   65   ALA ALA A . n 
B 2 61  ASP 61  66   66   ASP ASP A . n 
B 2 62  LYS 62  67   67   LYS LYS A . n 
B 2 63  LEU 63  68   68   LEU LEU A . n 
B 2 64  ILE 64  69   69   ILE ILE A . n 
B 2 65  LYS 65  70   70   LYS LYS A . n 
B 2 66  ILE 66  71   71   ILE ILE A . n 
B 2 67  TRP 67  72   72   TRP TRP A . n 
B 2 68  GLY 68  73   73   GLY GLY A . n 
B 2 69  ALA 69  74   74   ALA ALA A . n 
B 2 70  TYR 70  75   75   TYR TYR A . n 
B 2 71  ASP 71  76   76   ASP ASP A . n 
B 2 72  GLY 72  77   77   GLY GLY A . n 
B 2 73  LYS 73  78   78   LYS LYS A . n 
B 2 74  PHE 74  79   79   PHE PHE A . n 
B 2 75  GLU 75  80   80   GLU GLU A . n 
B 2 76  LYS 76  81   81   LYS LYS A . n 
B 2 77  THR 77  82   82   THR THR A . n 
B 2 78  ILE 78  83   83   ILE ILE A . n 
B 2 79  SER 79  84   84   SER SER A . n 
B 2 80  GLY 80  85   85   GLY GLY A . n 
B 2 81  HIS 81  86   86   HIS HIS A . n 
B 2 82  LYS 82  87   87   LYS LYS A . n 
B 2 83  LEU 83  88   88   LEU LEU A . n 
B 2 84  GLY 84  89   89   GLY GLY A . n 
B 2 85  ILE 85  90   90   ILE ILE A . n 
B 2 86  SER 86  91   91   SER SER A . n 
B 2 87  ASP 87  92   92   ASP ASP A . n 
B 2 88  VAL 88  93   93   VAL VAL A . n 
B 2 89  ALA 89  94   94   ALA ALA A . n 
B 2 90  TRP 90  95   95   TRP TRP A . n 
B 2 91  SER 91  96   96   SER SER A . n 
B 2 92  SER 92  97   97   SER SER A . n 
B 2 93  ASP 93  98   98   ASP ASP A . n 
B 2 94  SER 94  99   99   SER SER A . n 
B 2 95  ASN 95  100  100  ASN ASN A . n 
B 2 96  LEU 96  101  101  LEU LEU A . n 
B 2 97  LEU 97  102  102  LEU LEU A . n 
B 2 98  VAL 98  103  103  VAL VAL A . n 
B 2 99  SER 99  104  104  SER SER A . n 
B 2 100 ALA 100 105  105  ALA ALA A . n 
B 2 101 SER 101 106  106  SER SER A . n 
B 2 102 ASP 102 107  107  ASP ASP A . n 
B 2 103 ASP 103 108  108  ASP ASP A . n 
B 2 104 LYS 104 109  109  LYS LYS A . n 
B 2 105 THR 105 110  110  THR THR A . n 
B 2 106 LEU 106 111  111  LEU LEU A . n 
B 2 107 LYS 107 112  112  LYS LYS A . n 
B 2 108 ILE 108 113  113  ILE ILE A . n 
B 2 109 TRP 109 114  114  TRP TRP A . n 
B 2 110 ASP 110 115  115  ASP ASP A . n 
B 2 111 VAL 111 116  116  VAL VAL A . n 
B 2 112 SER 112 117  117  SER SER A . n 
B 2 113 SER 113 118  118  SER SER A . n 
B 2 114 GLY 114 119  119  GLY GLY A . n 
B 2 115 LYS 115 120  120  LYS LYS A . n 
B 2 116 CYS 116 121  121  CYS CYS A . n 
B 2 117 LEU 117 122  122  LEU LEU A . n 
B 2 118 LYS 118 123  123  LYS LYS A . n 
B 2 119 THR 119 124  124  THR THR A . n 
B 2 120 LEU 120 125  125  LEU LEU A . n 
B 2 121 LYS 121 126  126  LYS LYS A . n 
B 2 122 GLY 122 127  127  GLY GLY A . n 
B 2 123 HIS 123 128  128  HIS HIS A . n 
B 2 124 SER 124 129  129  SER SER A . n 
B 2 125 ASN 125 130  130  ASN ASN A . n 
B 2 126 TYR 126 131  131  TYR TYR A . n 
B 2 127 VAL 127 132  132  VAL VAL A . n 
B 2 128 PHE 128 133  133  PHE PHE A . n 
B 2 129 CYS 129 134  134  CYS CYS A . n 
B 2 130 CYS 130 135  135  CYS CYS A . n 
B 2 131 ASN 131 136  136  ASN ASN A . n 
B 2 132 PHE 132 137  137  PHE PHE A . n 
B 2 133 ASN 133 138  138  ASN ASN A . n 
B 2 134 PRO 134 139  139  PRO PRO A . n 
B 2 135 GLN 135 140  140  GLN GLN A . n 
B 2 136 SER 136 141  141  SER SER A . n 
B 2 137 ASN 137 142  142  ASN ASN A . n 
B 2 138 LEU 138 143  143  LEU LEU A . n 
B 2 139 ILE 139 144  144  ILE ILE A . n 
B 2 140 VAL 140 145  145  VAL VAL A . n 
B 2 141 SER 141 146  146  SER SER A . n 
B 2 142 GLY 142 147  147  GLY GLY A . n 
B 2 143 SER 143 148  148  SER SER A . n 
B 2 144 PHE 144 149  149  PHE PHE A . n 
B 2 145 ASP 145 150  150  ASP ASP A . n 
B 2 146 GLU 146 151  151  GLU GLU A . n 
B 2 147 SER 147 152  152  SER SER A . n 
B 2 148 VAL 148 153  153  VAL VAL A . n 
B 2 149 ARG 149 154  154  ARG ARG A . n 
B 2 150 ILE 150 155  155  ILE ILE A . n 
B 2 151 TRP 151 156  156  TRP TRP A . n 
B 2 152 ASP 152 157  157  ASP ASP A . n 
B 2 153 VAL 153 158  158  VAL VAL A . n 
B 2 154 LYS 154 159  159  LYS LYS A . n 
B 2 155 THR 155 160  160  THR THR A . n 
B 2 156 GLY 156 161  161  GLY GLY A . n 
B 2 157 LYS 157 162  162  LYS LYS A . n 
B 2 158 CYS 158 163  163  CYS CYS A . n 
B 2 159 LEU 159 164  164  LEU LEU A . n 
B 2 160 LYS 160 165  165  LYS LYS A . n 
B 2 161 THR 161 166  166  THR THR A . n 
B 2 162 LEU 162 167  167  LEU LEU A . n 
B 2 163 PRO 163 168  168  PRO PRO A . n 
B 2 164 ALA 164 169  169  ALA ALA A . n 
B 2 165 HIS 165 170  170  HIS HIS A . n 
B 2 166 SER 166 171  171  SER SER A . n 
B 2 167 ASP 167 172  172  ASP ASP A . n 
B 2 168 PRO 168 173  173  PRO PRO A . n 
B 2 169 VAL 169 174  174  VAL VAL A . n 
B 2 170 SER 170 175  175  SER SER A . n 
B 2 171 ALA 171 176  176  ALA ALA A . n 
B 2 172 VAL 172 177  177  VAL VAL A . n 
B 2 173 HIS 173 178  178  HIS HIS A . n 
B 2 174 PHE 174 179  179  PHE PHE A . n 
B 2 175 ASN 175 180  180  ASN ASN A . n 
B 2 176 ARG 176 181  181  ARG ARG A . n 
B 2 177 ASP 177 182  182  ASP ASP A . n 
B 2 178 GLY 178 183  183  GLY GLY A . n 
B 2 179 SER 179 184  184  SER SER A . n 
B 2 180 LEU 180 185  185  LEU LEU A . n 
B 2 181 ILE 181 186  186  ILE ILE A . n 
B 2 182 VAL 182 187  187  VAL VAL A . n 
B 2 183 SER 183 188  188  SER SER A . n 
B 2 184 SER 184 189  189  SER SER A . n 
B 2 185 SER 185 190  190  SER SER A . n 
B 2 186 TYR 186 191  191  TYR TYR A . n 
B 2 187 ASP 187 192  192  ASP ASP A . n 
B 2 188 GLY 188 193  193  GLY GLY A . n 
B 2 189 LEU 189 194  194  LEU LEU A . n 
B 2 190 CYS 190 195  195  CYS CYS A . n 
B 2 191 ARG 191 196  196  ARG ARG A . n 
B 2 192 ILE 192 197  197  ILE ILE A . n 
B 2 193 TRP 193 198  198  TRP TRP A . n 
B 2 194 ASP 194 199  199  ASP ASP A . n 
B 2 195 THR 195 200  200  THR THR A . n 
B 2 196 ALA 196 201  201  ALA ALA A . n 
B 2 197 SER 197 202  202  SER SER A . n 
B 2 198 GLY 198 203  203  GLY GLY A . n 
B 2 199 GLN 199 204  204  GLN GLN A . n 
B 2 200 CYS 200 205  205  CYS CYS A . n 
B 2 201 LEU 201 206  206  LEU LEU A . n 
B 2 202 LYS 202 207  207  LYS LYS A . n 
B 2 203 THR 203 208  208  THR THR A . n 
B 2 204 LEU 204 209  209  LEU LEU A . n 
B 2 205 ILE 205 210  210  ILE ILE A . n 
B 2 206 ASP 206 211  211  ASP ASP A . n 
B 2 207 ASP 207 212  212  ASP ASP A . n 
B 2 208 ASP 208 213  213  ASP ASP A . n 
B 2 209 ASN 209 214  214  ASN ASN A . n 
B 2 210 PRO 210 215  215  PRO PRO A . n 
B 2 211 PRO 211 216  216  PRO PRO A . n 
B 2 212 VAL 212 217  217  VAL VAL A . n 
B 2 213 SER 213 218  218  SER SER A . n 
B 2 214 PHE 214 219  219  PHE PHE A . n 
B 2 215 VAL 215 220  220  VAL VAL A . n 
B 2 216 LYS 216 221  221  LYS LYS A . n 
B 2 217 PHE 217 222  222  PHE PHE A . n 
B 2 218 SER 218 223  223  SER SER A . n 
B 2 219 PRO 219 224  224  PRO PRO A . n 
B 2 220 ASN 220 225  225  ASN ASN A . n 
B 2 221 GLY 221 226  226  GLY GLY A . n 
B 2 222 LYS 222 227  227  LYS LYS A . n 
B 2 223 TYR 223 228  228  TYR TYR A . n 
B 2 224 ILE 224 229  229  ILE ILE A . n 
B 2 225 LEU 225 230  230  LEU LEU A . n 
B 2 226 ALA 226 231  231  ALA ALA A . n 
B 2 227 ALA 227 232  232  ALA ALA A . n 
B 2 228 THR 228 233  233  THR THR A . n 
B 2 229 LEU 229 234  234  LEU LEU A . n 
B 2 230 ASP 230 235  235  ASP ASP A . n 
B 2 231 ASN 231 236  236  ASN ASN A . n 
B 2 232 THR 232 237  237  THR THR A . n 
B 2 233 LEU 233 238  238  LEU LEU A . n 
B 2 234 LYS 234 239  239  LYS LYS A . n 
B 2 235 LEU 235 240  240  LEU LEU A . n 
B 2 236 TRP 236 241  241  TRP TRP A . n 
B 2 237 ASP 237 242  242  ASP ASP A . n 
B 2 238 TYR 238 243  243  TYR TYR A . n 
B 2 239 SER 239 244  244  SER SER A . n 
B 2 240 LYS 240 245  245  LYS LYS A . n 
B 2 241 GLY 241 246  246  GLY GLY A . n 
B 2 242 LYS 242 247  247  LYS LYS A . n 
B 2 243 CYS 243 248  248  CYS CYS A . n 
B 2 244 LEU 244 249  249  LEU LEU A . n 
B 2 245 LYS 245 250  250  LYS LYS A . n 
B 2 246 THR 246 251  251  THR THR A . n 
B 2 247 TYR 247 252  252  TYR TYR A . n 
B 2 248 THR 248 253  253  THR THR A . n 
B 2 249 GLY 249 254  254  GLY GLY A . n 
B 2 250 HIS 250 255  255  HIS HIS A . n 
B 2 251 LYS 251 256  256  LYS LYS A . n 
B 2 252 ASN 252 257  257  ASN ASN A . n 
B 2 253 GLU 253 258  258  GLU GLU A . n 
B 2 254 LYS 254 259  259  LYS LYS A . n 
B 2 255 TYR 255 260  260  TYR TYR A . n 
B 2 256 CYS 256 261  261  CYS CYS A . n 
B 2 257 ILE 257 262  262  ILE ILE A . n 
B 2 258 PHE 258 263  263  PHE PHE A . n 
B 2 259 ALA 259 264  264  ALA ALA A . n 
B 2 260 ASN 260 265  265  ASN ASN A . n 
B 2 261 PHE 261 266  266  PHE PHE A . n 
B 2 262 SER 262 267  267  SER SER A . n 
B 2 263 VAL 263 268  268  VAL VAL A . n 
B 2 264 THR 264 269  269  THR THR A . n 
B 2 265 GLY 265 270  270  GLY GLY A . n 
B 2 266 GLY 266 271  271  GLY GLY A . n 
B 2 267 LYS 267 272  272  LYS LYS A . n 
B 2 268 TRP 268 273  273  TRP TRP A . n 
B 2 269 ILE 269 274  274  ILE ILE A . n 
B 2 270 VAL 270 275  275  VAL VAL A . n 
B 2 271 SER 271 276  276  SER SER A . n 
B 2 272 GLY 272 277  277  GLY GLY A . n 
B 2 273 SER 273 278  278  SER SER A . n 
B 2 274 GLU 274 279  279  GLU GLU A . n 
B 2 275 ASP 275 280  280  ASP ASP A . n 
B 2 276 ASN 276 281  281  ASN ASN A . n 
B 2 277 LEU 277 282  282  LEU LEU A . n 
B 2 278 VAL 278 283  283  VAL VAL A . n 
B 2 279 TYR 279 284  284  TYR TYR A . n 
B 2 280 ILE 280 285  285  ILE ILE A . n 
B 2 281 TRP 281 286  286  TRP TRP A . n 
B 2 282 ASN 282 287  287  ASN ASN A . n 
B 2 283 LEU 283 288  288  LEU LEU A . n 
B 2 284 GLN 284 289  289  GLN GLN A . n 
B 2 285 THR 285 290  290  THR THR A . n 
B 2 286 LYS 286 291  291  LYS LYS A . n 
B 2 287 GLU 287 292  292  GLU GLU A . n 
B 2 288 ILE 288 293  293  ILE ILE A . n 
B 2 289 VAL 289 294  294  VAL VAL A . n 
B 2 290 GLN 290 295  295  GLN GLN A . n 
B 2 291 LYS 291 296  296  LYS LYS A . n 
B 2 292 LEU 292 297  297  LEU LEU A . n 
B 2 293 GLN 293 298  298  GLN GLN A . n 
B 2 294 GLY 294 299  299  GLY GLY A . n 
B 2 295 HIS 295 300  300  HIS HIS A . n 
B 2 296 THR 296 301  301  THR THR A . n 
B 2 297 ASP 297 302  302  ASP ASP A . n 
B 2 298 VAL 298 303  303  VAL VAL A . n 
B 2 299 VAL 299 304  304  VAL VAL A . n 
B 2 300 ILE 300 305  305  ILE ILE A . n 
B 2 301 SER 301 306  306  SER SER A . n 
B 2 302 THR 302 307  307  THR THR A . n 
B 2 303 ALA 303 308  308  ALA ALA A . n 
B 2 304 CYS 304 309  309  CYS CYS A . n 
B 2 305 HIS 305 310  310  HIS HIS A . n 
B 2 306 PRO 306 311  311  PRO PRO A . n 
B 2 307 THR 307 312  312  THR THR A . n 
B 2 308 GLU 308 313  313  GLU GLU A . n 
B 2 309 ASN 309 314  314  ASN ASN A . n 
B 2 310 ILE 310 315  315  ILE ILE A . n 
B 2 311 ILE 311 316  316  ILE ILE A . n 
B 2 312 ALA 312 317  317  ALA ALA A . n 
B 2 313 SER 313 318  318  SER SER A . n 
B 2 314 ALA 314 319  319  ALA ALA A . n 
B 2 315 ALA 315 320  320  ALA ALA A . n 
B 2 316 LEU 316 321  321  LEU LEU A . n 
B 2 317 GLU 317 322  322  GLU GLU A . n 
B 2 318 ASN 318 323  323  ASN ASN A . n 
B 2 319 ASP 319 324  324  ASP ASP A . n 
B 2 320 LYS 320 325  325  LYS LYS A . n 
B 2 321 THR 321 326  326  THR THR A . n 
B 2 322 ILE 322 327  327  ILE ILE A . n 
B 2 323 LYS 323 328  328  LYS LYS A . n 
B 2 324 LEU 324 329  329  LEU LEU A . n 
B 2 325 TRP 325 330  330  TRP TRP A . n 
B 2 326 LYS 326 331  331  LYS LYS A . n 
B 2 327 SER 327 332  332  SER SER A . n 
B 2 328 ASP 328 333  333  ASP ASP A . n 
B 2 329 CYS 329 334  334  CYS CYS A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BAF 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BAF 
_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 A1BAF 1   1401 1401 A1BAF 411 B . 
D 4 HOH   1   1501 332  HOH   HOH B . 
D 4 HOH   2   1502 2    HOH   HOH B . 
D 4 HOH   3   1503 321  HOH   HOH B . 
D 4 HOH   4   1504 367  HOH   HOH B . 
D 4 HOH   5   1505 251  HOH   HOH B . 
D 4 HOH   6   1506 96   HOH   HOH B . 
D 4 HOH   7   1507 173  HOH   HOH B . 
D 4 HOH   8   1508 90   HOH   HOH B . 
D 4 HOH   9   1509 174  HOH   HOH B . 
D 4 HOH   10  1510 388  HOH   HOH B . 
D 4 HOH   11  1511 240  HOH   HOH B . 
D 4 HOH   12  1512 259  HOH   HOH B . 
D 4 HOH   13  1513 1    HOH   HOH B . 
D 4 HOH   14  1514 417  HOH   HOH B . 
D 4 HOH   15  1515 349  HOH   HOH B . 
D 4 HOH   16  1516 25   HOH   HOH B . 
D 4 HOH   17  1517 9    HOH   HOH B . 
D 4 HOH   18  1518 389  HOH   HOH B . 
D 4 HOH   19  1519 63   HOH   HOH B . 
D 4 HOH   20  1520 8    HOH   HOH B . 
D 4 HOH   21  1521 318  HOH   HOH B . 
D 4 HOH   22  1522 121  HOH   HOH B . 
D 4 HOH   23  1523 256  HOH   HOH B . 
D 4 HOH   24  1524 62   HOH   HOH B . 
D 4 HOH   25  1525 257  HOH   HOH B . 
D 4 HOH   26  1526 183  HOH   HOH B . 
D 4 HOH   27  1527 133  HOH   HOH B . 
D 4 HOH   28  1528 287  HOH   HOH B . 
D 4 HOH   29  1529 227  HOH   HOH B . 
D 4 HOH   30  1530 220  HOH   HOH B . 
D 4 HOH   31  1531 89   HOH   HOH B . 
D 4 HOH   32  1532 165  HOH   HOH B . 
D 4 HOH   33  1533 212  HOH   HOH B . 
D 4 HOH   34  1534 4    HOH   HOH B . 
D 4 HOH   35  1535 206  HOH   HOH B . 
D 4 HOH   36  1536 47   HOH   HOH B . 
D 4 HOH   37  1537 48   HOH   HOH B . 
D 4 HOH   38  1538 102  HOH   HOH B . 
D 4 HOH   39  1539 135  HOH   HOH B . 
D 4 HOH   40  1540 68   HOH   HOH B . 
D 4 HOH   41  1541 95   HOH   HOH B . 
D 4 HOH   42  1542 224  HOH   HOH B . 
D 4 HOH   43  1543 83   HOH   HOH B . 
D 4 HOH   44  1544 88   HOH   HOH B . 
D 4 HOH   45  1545 340  HOH   HOH B . 
D 4 HOH   46  1546 310  HOH   HOH B . 
D 4 HOH   47  1547 41   HOH   HOH B . 
D 4 HOH   48  1548 263  HOH   HOH B . 
D 4 HOH   49  1549 167  HOH   HOH B . 
D 4 HOH   50  1550 81   HOH   HOH B . 
D 4 HOH   51  1551 120  HOH   HOH B . 
D 4 HOH   52  1552 320  HOH   HOH B . 
D 4 HOH   53  1553 329  HOH   HOH B . 
D 4 HOH   54  1554 362  HOH   HOH B . 
D 4 HOH   55  1555 228  HOH   HOH B . 
D 4 HOH   56  1556 155  HOH   HOH B . 
D 4 HOH   57  1557 168  HOH   HOH B . 
D 4 HOH   58  1558 200  HOH   HOH B . 
D 4 HOH   59  1559 335  HOH   HOH B . 
D 4 HOH   60  1560 28   HOH   HOH B . 
D 4 HOH   61  1561 30   HOH   HOH B . 
D 4 HOH   62  1562 11   HOH   HOH B . 
D 4 HOH   63  1563 179  HOH   HOH B . 
D 4 HOH   64  1564 31   HOH   HOH B . 
D 4 HOH   65  1565 58   HOH   HOH B . 
D 4 HOH   66  1566 50   HOH   HOH B . 
D 4 HOH   67  1567 187  HOH   HOH B . 
D 4 HOH   68  1568 69   HOH   HOH B . 
D 4 HOH   69  1569 333  HOH   HOH B . 
D 4 HOH   70  1570 198  HOH   HOH B . 
D 4 HOH   71  1571 350  HOH   HOH B . 
D 4 HOH   72  1572 73   HOH   HOH B . 
D 4 HOH   73  1573 59   HOH   HOH B . 
D 4 HOH   74  1574 131  HOH   HOH B . 
D 4 HOH   75  1575 29   HOH   HOH B . 
D 4 HOH   76  1576 146  HOH   HOH B . 
D 4 HOH   77  1577 36   HOH   HOH B . 
D 4 HOH   78  1578 363  HOH   HOH B . 
D 4 HOH   79  1579 343  HOH   HOH B . 
D 4 HOH   80  1580 51   HOH   HOH B . 
D 4 HOH   81  1581 239  HOH   HOH B . 
D 4 HOH   82  1582 308  HOH   HOH B . 
D 4 HOH   83  1583 262  HOH   HOH B . 
D 4 HOH   84  1584 93   HOH   HOH B . 
D 4 HOH   85  1585 351  HOH   HOH B . 
D 4 HOH   86  1586 298  HOH   HOH B . 
D 4 HOH   87  1587 288  HOH   HOH B . 
D 4 HOH   88  1588 307  HOH   HOH B . 
D 4 HOH   89  1589 237  HOH   HOH B . 
D 4 HOH   90  1590 23   HOH   HOH B . 
D 4 HOH   91  1591 184  HOH   HOH B . 
D 4 HOH   92  1592 195  HOH   HOH B . 
D 4 HOH   93  1593 414  HOH   HOH B . 
D 4 HOH   94  1594 122  HOH   HOH B . 
D 4 HOH   95  1595 86   HOH   HOH B . 
D 4 HOH   96  1596 61   HOH   HOH B . 
D 4 HOH   97  1597 326  HOH   HOH B . 
D 4 HOH   98  1598 208  HOH   HOH B . 
D 4 HOH   99  1599 398  HOH   HOH B . 
D 4 HOH   100 1600 180  HOH   HOH B . 
D 4 HOH   101 1601 252  HOH   HOH B . 
D 4 HOH   102 1602 192  HOH   HOH B . 
D 4 HOH   103 1603 141  HOH   HOH B . 
D 4 HOH   104 1604 205  HOH   HOH B . 
D 4 HOH   105 1605 282  HOH   HOH B . 
D 4 HOH   106 1606 411  HOH   HOH B . 
D 4 HOH   107 1607 243  HOH   HOH B . 
D 4 HOH   108 1608 101  HOH   HOH B . 
D 4 HOH   109 1609 365  HOH   HOH B . 
D 4 HOH   110 1610 108  HOH   HOH B . 
D 4 HOH   111 1611 128  HOH   HOH B . 
D 4 HOH   112 1612 137  HOH   HOH B . 
D 4 HOH   113 1613 342  HOH   HOH B . 
D 4 HOH   114 1614 207  HOH   HOH B . 
D 4 HOH   115 1615 82   HOH   HOH B . 
D 4 HOH   116 1616 247  HOH   HOH B . 
D 4 HOH   117 1617 358  HOH   HOH B . 
D 4 HOH   118 1618 197  HOH   HOH B . 
D 4 HOH   119 1619 216  HOH   HOH B . 
D 4 HOH   120 1620 204  HOH   HOH B . 
D 4 HOH   121 1621 236  HOH   HOH B . 
D 4 HOH   122 1622 377  HOH   HOH B . 
D 4 HOH   123 1623 42   HOH   HOH B . 
D 4 HOH   124 1624 383  HOH   HOH B . 
D 4 HOH   125 1625 309  HOH   HOH B . 
D 4 HOH   126 1626 70   HOH   HOH B . 
D 4 HOH   127 1627 87   HOH   HOH B . 
D 4 HOH   128 1628 78   HOH   HOH B . 
D 4 HOH   129 1629 129  HOH   HOH B . 
D 4 HOH   130 1630 374  HOH   HOH B . 
D 4 HOH   131 1631 324  HOH   HOH B . 
D 4 HOH   132 1632 255  HOH   HOH B . 
D 4 HOH   133 1633 105  HOH   HOH B . 
D 4 HOH   134 1634 110  HOH   HOH B . 
D 4 HOH   135 1635 400  HOH   HOH B . 
D 4 HOH   136 1636 7    HOH   HOH B . 
D 4 HOH   137 1637 305  HOH   HOH B . 
D 4 HOH   138 1638 397  HOH   HOH B . 
D 4 HOH   139 1639 314  HOH   HOH B . 
D 4 HOH   140 1640 292  HOH   HOH B . 
D 4 HOH   141 1641 289  HOH   HOH B . 
D 4 HOH   142 1642 274  HOH   HOH B . 
D 4 HOH   143 1643 393  HOH   HOH B . 
D 4 HOH   144 1644 98   HOH   HOH B . 
D 4 HOH   145 1645 382  HOH   HOH B . 
D 4 HOH   146 1646 238  HOH   HOH B . 
D 4 HOH   147 1647 378  HOH   HOH B . 
D 4 HOH   148 1648 258  HOH   HOH B . 
D 4 HOH   149 1649 338  HOH   HOH B . 
D 4 HOH   150 1650 66   HOH   HOH B . 
D 4 HOH   151 1651 295  HOH   HOH B . 
D 4 HOH   152 1652 402  HOH   HOH B . 
D 4 HOH   153 1653 406  HOH   HOH B . 
D 4 HOH   154 1654 202  HOH   HOH B . 
D 4 HOH   155 1655 233  HOH   HOH B . 
D 4 HOH   156 1656 172  HOH   HOH B . 
D 4 HOH   157 1657 229  HOH   HOH B . 
D 4 HOH   158 1658 391  HOH   HOH B . 
D 4 HOH   159 1659 395  HOH   HOH B . 
D 4 HOH   160 1660 296  HOH   HOH B . 
D 4 HOH   161 1661 344  HOH   HOH B . 
D 4 HOH   162 1662 248  HOH   HOH B . 
D 4 HOH   163 1663 353  HOH   HOH B . 
D 4 HOH   164 1664 348  HOH   HOH B . 
D 4 HOH   165 1665 386  HOH   HOH B . 
D 4 HOH   166 1666 244  HOH   HOH B . 
D 4 HOH   167 1667 399  HOH   HOH B . 
D 4 HOH   168 1668 280  HOH   HOH B . 
D 4 HOH   169 1669 413  HOH   HOH B . 
D 4 HOH   170 1670 154  HOH   HOH B . 
D 4 HOH   171 1671 193  HOH   HOH B . 
D 4 HOH   172 1672 341  HOH   HOH B . 
D 4 HOH   173 1673 375  HOH   HOH B . 
D 4 HOH   174 1674 225  HOH   HOH B . 
D 4 HOH   175 1675 392  HOH   HOH B . 
D 4 HOH   176 1676 345  HOH   HOH B . 
D 4 HOH   177 1677 161  HOH   HOH B . 
D 4 HOH   178 1678 371  HOH   HOH B . 
D 4 HOH   179 1679 222  HOH   HOH B . 
D 4 HOH   180 1680 140  HOH   HOH B . 
D 4 HOH   181 1681 107  HOH   HOH B . 
D 4 HOH   182 1682 219  HOH   HOH B . 
D 4 HOH   183 1683 337  HOH   HOH B . 
D 4 HOH   184 1684 347  HOH   HOH B . 
D 4 HOH   185 1685 323  HOH   HOH B . 
D 4 HOH   186 1686 315  HOH   HOH B . 
D 4 HOH   187 1687 322  HOH   HOH B . 
E 4 HOH   1   401  301  HOH   HOH A . 
E 4 HOH   2   402  79   HOH   HOH A . 
E 4 HOH   3   403  311  HOH   HOH A . 
E 4 HOH   4   404  32   HOH   HOH A . 
E 4 HOH   5   405  13   HOH   HOH A . 
E 4 HOH   6   406  232  HOH   HOH A . 
E 4 HOH   7   407  188  HOH   HOH A . 
E 4 HOH   8   408  124  HOH   HOH A . 
E 4 HOH   9   409  313  HOH   HOH A . 
E 4 HOH   10  410  359  HOH   HOH A . 
E 4 HOH   11  411  404  HOH   HOH A . 
E 4 HOH   12  412  158  HOH   HOH A . 
E 4 HOH   13  413  175  HOH   HOH A . 
E 4 HOH   14  414  104  HOH   HOH A . 
E 4 HOH   15  415  17   HOH   HOH A . 
E 4 HOH   16  416  126  HOH   HOH A . 
E 4 HOH   17  417  26   HOH   HOH A . 
E 4 HOH   18  418  369  HOH   HOH A . 
E 4 HOH   19  419  381  HOH   HOH A . 
E 4 HOH   20  420  65   HOH   HOH A . 
E 4 HOH   21  421  38   HOH   HOH A . 
E 4 HOH   22  422  3    HOH   HOH A . 
E 4 HOH   23  423  275  HOH   HOH A . 
E 4 HOH   24  424  71   HOH   HOH A . 
E 4 HOH   25  425  260  HOH   HOH A . 
E 4 HOH   26  426  111  HOH   HOH A . 
E 4 HOH   27  427  370  HOH   HOH A . 
E 4 HOH   28  428  20   HOH   HOH A . 
E 4 HOH   29  429  316  HOH   HOH A . 
E 4 HOH   30  430  12   HOH   HOH A . 
E 4 HOH   31  431  15   HOH   HOH A . 
E 4 HOH   32  432  159  HOH   HOH A . 
E 4 HOH   33  433  22   HOH   HOH A . 
E 4 HOH   34  434  164  HOH   HOH A . 
E 4 HOH   35  435  286  HOH   HOH A . 
E 4 HOH   36  436  60   HOH   HOH A . 
E 4 HOH   37  437  114  HOH   HOH A . 
E 4 HOH   38  438  19   HOH   HOH A . 
E 4 HOH   39  439  151  HOH   HOH A . 
E 4 HOH   40  440  143  HOH   HOH A . 
E 4 HOH   41  441  77   HOH   HOH A . 
E 4 HOH   42  442  112  HOH   HOH A . 
E 4 HOH   43  443  218  HOH   HOH A . 
E 4 HOH   44  444  125  HOH   HOH A . 
E 4 HOH   45  445  379  HOH   HOH A . 
E 4 HOH   46  446  75   HOH   HOH A . 
E 4 HOH   47  447  372  HOH   HOH A . 
E 4 HOH   48  448  16   HOH   HOH A . 
E 4 HOH   49  449  152  HOH   HOH A . 
E 4 HOH   50  450  39   HOH   HOH A . 
E 4 HOH   51  451  312  HOH   HOH A . 
E 4 HOH   52  452  52   HOH   HOH A . 
E 4 HOH   53  453  215  HOH   HOH A . 
E 4 HOH   54  454  148  HOH   HOH A . 
E 4 HOH   55  455  118  HOH   HOH A . 
E 4 HOH   56  456  45   HOH   HOH A . 
E 4 HOH   57  457  214  HOH   HOH A . 
E 4 HOH   58  458  5    HOH   HOH A . 
E 4 HOH   59  459  294  HOH   HOH A . 
E 4 HOH   60  460  171  HOH   HOH A . 
E 4 HOH   61  461  302  HOH   HOH A . 
E 4 HOH   62  462  113  HOH   HOH A . 
E 4 HOH   63  463  277  HOH   HOH A . 
E 4 HOH   64  464  235  HOH   HOH A . 
E 4 HOH   65  465  299  HOH   HOH A . 
E 4 HOH   66  466  150  HOH   HOH A . 
E 4 HOH   67  467  37   HOH   HOH A . 
E 4 HOH   68  468  319  HOH   HOH A . 
E 4 HOH   69  469  234  HOH   HOH A . 
E 4 HOH   70  470  103  HOH   HOH A . 
E 4 HOH   71  471  33   HOH   HOH A . 
E 4 HOH   72  472  145  HOH   HOH A . 
E 4 HOH   73  473  246  HOH   HOH A . 
E 4 HOH   74  474  276  HOH   HOH A . 
E 4 HOH   75  475  84   HOH   HOH A . 
E 4 HOH   76  476  91   HOH   HOH A . 
E 4 HOH   77  477  357  HOH   HOH A . 
E 4 HOH   78  478  18   HOH   HOH A . 
E 4 HOH   79  479  265  HOH   HOH A . 
E 4 HOH   80  480  394  HOH   HOH A . 
E 4 HOH   81  481  217  HOH   HOH A . 
E 4 HOH   82  482  94   HOH   HOH A . 
E 4 HOH   83  483  85   HOH   HOH A . 
E 4 HOH   84  484  210  HOH   HOH A . 
E 4 HOH   85  485  44   HOH   HOH A . 
E 4 HOH   86  486  21   HOH   HOH A . 
E 4 HOH   87  487  201  HOH   HOH A . 
E 4 HOH   88  488  74   HOH   HOH A . 
E 4 HOH   89  489  27   HOH   HOH A . 
E 4 HOH   90  490  373  HOH   HOH A . 
E 4 HOH   91  491  327  HOH   HOH A . 
E 4 HOH   92  492  43   HOH   HOH A . 
E 4 HOH   93  493  14   HOH   HOH A . 
E 4 HOH   94  494  156  HOH   HOH A . 
E 4 HOH   95  495  163  HOH   HOH A . 
E 4 HOH   96  496  46   HOH   HOH A . 
E 4 HOH   97  497  76   HOH   HOH A . 
E 4 HOH   98  498  317  HOH   HOH A . 
E 4 HOH   99  499  181  HOH   HOH A . 
E 4 HOH   100 500  97   HOH   HOH A . 
E 4 HOH   101 501  56   HOH   HOH A . 
E 4 HOH   102 502  134  HOH   HOH A . 
E 4 HOH   103 503  54   HOH   HOH A . 
E 4 HOH   104 504  24   HOH   HOH A . 
E 4 HOH   105 505  109  HOH   HOH A . 
E 4 HOH   106 506  290  HOH   HOH A . 
E 4 HOH   107 507  189  HOH   HOH A . 
E 4 HOH   108 508  160  HOH   HOH A . 
E 4 HOH   109 509  331  HOH   HOH A . 
E 4 HOH   110 510  170  HOH   HOH A . 
E 4 HOH   111 511  186  HOH   HOH A . 
E 4 HOH   112 512  67   HOH   HOH A . 
E 4 HOH   113 513  390  HOH   HOH A . 
E 4 HOH   114 514  190  HOH   HOH A . 
E 4 HOH   115 515  384  HOH   HOH A . 
E 4 HOH   116 516  100  HOH   HOH A . 
E 4 HOH   117 517  6    HOH   HOH A . 
E 4 HOH   118 518  55   HOH   HOH A . 
E 4 HOH   119 519  231  HOH   HOH A . 
E 4 HOH   120 520  261  HOH   HOH A . 
E 4 HOH   121 521  291  HOH   HOH A . 
E 4 HOH   122 522  182  HOH   HOH A . 
E 4 HOH   123 523  34   HOH   HOH A . 
E 4 HOH   124 524  203  HOH   HOH A . 
E 4 HOH   125 525  53   HOH   HOH A . 
E 4 HOH   126 526  249  HOH   HOH A . 
E 4 HOH   127 527  178  HOH   HOH A . 
E 4 HOH   128 528  40   HOH   HOH A . 
E 4 HOH   129 529  57   HOH   HOH A . 
E 4 HOH   130 530  270  HOH   HOH A . 
E 4 HOH   131 531  366  HOH   HOH A . 
E 4 HOH   132 532  144  HOH   HOH A . 
E 4 HOH   133 533  284  HOH   HOH A . 
E 4 HOH   134 534  119  HOH   HOH A . 
E 4 HOH   135 535  355  HOH   HOH A . 
E 4 HOH   136 536  272  HOH   HOH A . 
E 4 HOH   137 537  10   HOH   HOH A . 
E 4 HOH   138 538  354  HOH   HOH A . 
E 4 HOH   139 539  116  HOH   HOH A . 
E 4 HOH   140 540  136  HOH   HOH A . 
E 4 HOH   141 541  346  HOH   HOH A . 
E 4 HOH   142 542  92   HOH   HOH A . 
E 4 HOH   143 543  242  HOH   HOH A . 
E 4 HOH   144 544  176  HOH   HOH A . 
E 4 HOH   145 545  169  HOH   HOH A . 
E 4 HOH   146 546  266  HOH   HOH A . 
E 4 HOH   147 547  142  HOH   HOH A . 
E 4 HOH   148 548  49   HOH   HOH A . 
E 4 HOH   149 549  117  HOH   HOH A . 
E 4 HOH   150 550  132  HOH   HOH A . 
E 4 HOH   151 551  281  HOH   HOH A . 
E 4 HOH   152 552  405  HOH   HOH A . 
E 4 HOH   153 553  254  HOH   HOH A . 
E 4 HOH   154 554  162  HOH   HOH A . 
E 4 HOH   155 555  273  HOH   HOH A . 
E 4 HOH   156 556  267  HOH   HOH A . 
E 4 HOH   157 557  223  HOH   HOH A . 
E 4 HOH   158 558  123  HOH   HOH A . 
E 4 HOH   159 559  376  HOH   HOH A . 
E 4 HOH   160 560  221  HOH   HOH A . 
E 4 HOH   161 561  72   HOH   HOH A . 
E 4 HOH   162 562  387  HOH   HOH A . 
E 4 HOH   163 563  153  HOH   HOH A . 
E 4 HOH   164 564  147  HOH   HOH A . 
E 4 HOH   165 565  226  HOH   HOH A . 
E 4 HOH   166 566  64   HOH   HOH A . 
E 4 HOH   167 567  416  HOH   HOH A . 
E 4 HOH   168 568  303  HOH   HOH A . 
E 4 HOH   169 569  293  HOH   HOH A . 
E 4 HOH   170 570  364  HOH   HOH A . 
E 4 HOH   171 571  271  HOH   HOH A . 
E 4 HOH   172 572  35   HOH   HOH A . 
E 4 HOH   173 573  199  HOH   HOH A . 
E 4 HOH   174 574  336  HOH   HOH A . 
E 4 HOH   175 575  285  HOH   HOH A . 
E 4 HOH   176 576  304  HOH   HOH A . 
E 4 HOH   177 577  99   HOH   HOH A . 
E 4 HOH   178 578  157  HOH   HOH A . 
E 4 HOH   179 579  196  HOH   HOH A . 
E 4 HOH   180 580  409  HOH   HOH A . 
E 4 HOH   181 581  328  HOH   HOH A . 
E 4 HOH   182 582  194  HOH   HOH A . 
E 4 HOH   183 583  356  HOH   HOH A . 
E 4 HOH   184 584  230  HOH   HOH A . 
E 4 HOH   185 585  368  HOH   HOH A . 
E 4 HOH   186 586  420  HOH   HOH A . 
E 4 HOH   187 587  241  HOH   HOH A . 
E 4 HOH   188 588  339  HOH   HOH A . 
E 4 HOH   189 589  106  HOH   HOH A . 
E 4 HOH   190 590  209  HOH   HOH A . 
E 4 HOH   191 591  412  HOH   HOH A . 
E 4 HOH   192 592  213  HOH   HOH A . 
E 4 HOH   193 593  325  HOH   HOH A . 
E 4 HOH   194 594  306  HOH   HOH A . 
E 4 HOH   195 595  268  HOH   HOH A . 
E 4 HOH   196 596  330  HOH   HOH A . 
E 4 HOH   197 597  418  HOH   HOH A . 
E 4 HOH   198 598  149  HOH   HOH A . 
E 4 HOH   199 599  139  HOH   HOH A . 
E 4 HOH   200 600  191  HOH   HOH A . 
E 4 HOH   201 601  361  HOH   HOH A . 
E 4 HOH   202 602  245  HOH   HOH A . 
E 4 HOH   203 603  407  HOH   HOH A . 
E 4 HOH   204 604  115  HOH   HOH A . 
E 4 HOH   205 605  138  HOH   HOH A . 
E 4 HOH   206 606  396  HOH   HOH A . 
E 4 HOH   207 607  401  HOH   HOH A . 
E 4 HOH   208 608  283  HOH   HOH A . 
E 4 HOH   209 609  352  HOH   HOH A . 
E 4 HOH   210 610  408  HOH   HOH A . 
E 4 HOH   211 611  185  HOH   HOH A . 
E 4 HOH   212 612  177  HOH   HOH A . 
E 4 HOH   213 613  278  HOH   HOH A . 
E 4 HOH   214 614  419  HOH   HOH A . 
E 4 HOH   215 615  130  HOH   HOH A . 
E 4 HOH   216 616  360  HOH   HOH A . 
E 4 HOH   217 617  380  HOH   HOH A . 
E 4 HOH   218 618  297  HOH   HOH A . 
E 4 HOH   219 619  127  HOH   HOH A . 
E 4 HOH   220 620  269  HOH   HOH A . 
E 4 HOH   221 621  166  HOH   HOH A . 
E 4 HOH   222 622  264  HOH   HOH A . 
E 4 HOH   223 623  300  HOH   HOH A . 
E 4 HOH   224 624  410  HOH   HOH A . 
E 4 HOH   225 625  250  HOH   HOH A . 
E 4 HOH   226 626  211  HOH   HOH A . 
E 4 HOH   227 627  279  HOH   HOH A . 
E 4 HOH   228 628  403  HOH   HOH A . 
E 4 HOH   229 629  415  HOH   HOH A . 
E 4 HOH   230 630  253  HOH   HOH A . 
E 4 HOH   231 631  334  HOH   HOH A . 
E 4 HOH   232 632  385  HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? 1.21.1_5286 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? CrysalisPro ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DLW 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     80.225 
_cell.length_a_esd                 ? 
_cell.length_b                     83.882 
_cell.length_b_esd                 ? 
_cell.length_c                     131.483 
_cell.length_c_esd                 ? 
_cell.volume                       884799.673 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9DLW 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9DLW 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.96 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          58.44 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.9 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '1.8 M Sodium phosphate monobasic monohydrate, potassium phosphate dibasic / pH 6.9' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            294 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER R 1M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-06-21 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.54189 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'RIGAKU MICROMAX-002+' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.54189 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          17.30 
_reflns.entry_id                                       9DLW 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.07 
_reflns.d_resolution_low                               28.59 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     52605 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           95.80 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.69 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.989 
_reflns.pdbx_CC_star                                   0.997 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.07 
_reflns_shell.d_res_low                                     2.11 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2423 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.448 
_reflns_shell.pdbx_CC_star                                  0.997 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               20.66 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9DLW 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.07 
_refine.ls_d_res_low                             28.59 
_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                     52465 
_refine.ls_number_reflns_R_free                  2645 
_refine.ls_number_reflns_R_work                  49820 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.80 
_refine.ls_percent_reflns_R_free                 5.04 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2018 
_refine.ls_R_factor_R_free                       0.2422 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1997 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 24.6376 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.2731 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.07 
_refine_hist.d_res_low                        28.59 
_refine_hist.number_atoms_solvent             419 
_refine_hist.number_atoms_total               5354 
_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        4833 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         102 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0113  ? 5088 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.9556  ? 6907 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0563  ? 758  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0067  ? 874  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.3802 ? 1824 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.07 2.11  . . 129 2289 84.19 . . . . 0.2832 . . . . . . . . . . . 0.3722 
'X-RAY DIFFRACTION' 2.11 2.15  . . 131 2358 88.67 . . . . 0.2542 . . . . . . . . . . . 0.3145 
'X-RAY DIFFRACTION' 2.15 2.19  . . 140 2479 91.51 . . . . 0.2673 . . . . . . . . . . . 0.2900 
'X-RAY DIFFRACTION' 2.19 2.24  . . 131 2477 91.93 . . . . 0.3514 . . . . . . . . . . . 0.3837 
'X-RAY DIFFRACTION' 2.24 2.29  . . 129 2494 92.59 . . . . 0.3848 . . . . . . . . . . . 0.4153 
'X-RAY DIFFRACTION' 2.29 2.35  . . 146 2537 94.31 . . . . 0.2812 . . . . . . . . . . . 0.3615 
'X-RAY DIFFRACTION' 2.35 2.41  . . 146 2639 97.38 . . . . 0.2179 . . . . . . . . . . . 0.2605 
'X-RAY DIFFRACTION' 2.41 2.48  . . 132 2697 99.12 . . . . 0.2198 . . . . . . . . . . . 0.2814 
'X-RAY DIFFRACTION' 2.48 2.56  . . 125 2727 99.76 . . . . 0.2049 . . . . . . . . . . . 0.2458 
'X-RAY DIFFRACTION' 2.56 2.66  . . 157 2704 99.90 . . . . 0.1948 . . . . . . . . . . . 0.2847 
'X-RAY DIFFRACTION' 2.66 2.76  . . 134 2729 99.93 . . . . 0.1932 . . . . . . . . . . . 0.2280 
'X-RAY DIFFRACTION' 2.76 2.89  . . 142 2720 99.97 . . . . 0.1882 . . . . . . . . . . . 0.2426 
'X-RAY DIFFRACTION' 2.89 3.04  . . 130 2734 99.76 . . . . 0.1934 . . . . . . . . . . . 0.2446 
'X-RAY DIFFRACTION' 3.04 3.23  . . 138 2745 99.24 . . . . 0.1876 . . . . . . . . . . . 0.2431 
'X-RAY DIFFRACTION' 3.23 3.48  . . 137 2711 98.96 . . . . 0.1727 . . . . . . . . . . . 0.1946 
'X-RAY DIFFRACTION' 3.48 3.83  . . 168 2697 98.18 . . . . 0.1735 . . . . . . . . . . . 0.2109 
'X-RAY DIFFRACTION' 3.83 4.38  . . 130 2710 97.09 . . . . 0.1417 . . . . . . . . . . . 0.1545 
'X-RAY DIFFRACTION' 4.38 5.51  . . 167 2679 96.15 . . . . 0.1302 . . . . . . . . . . . 0.1722 
'X-RAY DIFFRACTION' 5.51 28.59 . . 133 2694 91.64 . . . . 0.1680 . . . . . . . . . . . 0.2032 
# 
_struct.entry_id                     9DLW 
_struct.title                        'Crystal structure of the ternary complex of DCAF1 and WDR5 with PROTAC, OICR-41114' 
_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        9DLW 
_struct_keywords.text            'E3 ligase, adaptor, PROTAC, WDR, ternary complex, PROTEIN BINDING' 
_struct_keywords.pdbx_keywords   'PROTEIN BINDING' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
# 
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 DCAF1_HUMAN Q9Y4B6 ? 1 
;FRPISVFREANEDESGFTCCAFSARERFLMLGTCTGQLKLYNVFSGQEEASYNCHNSAITHLEPSRDGSLLLTSATWSQP
LSALWGMKSVFDMKHSFTEDHYVEFSKHSQDRVIGTKGDIAHIYDIQTGNKLLTLFNPDLANNYKRNCATFNPTDDLVLN
DGVLWDVRSAQAIHKFDKFNMNISGVFHPNGLEVIINTEIWDLRTFHLLHTVPALDQCRVVFNHTGTVMYGAMLQADDED
DLMEERMKSPFGSSFRTFNATDYKPIATIDVKRNIFDLCTDTKDCYLAVIENQGSMDALNMDTVCRLYEVG
;
1080 
2 UNP WDR5_HUMAN  P61964 ? 2 
;TQSKPTPVKPNYALKFTLAGHTKAVSSVKFSPNGEWLASSSADKLIKIWGAYDGKFEKTISGHKLGISDVAWSSDSNLLV
SASDDKTLKIWDVSSGKCLKTLKGHSNYVFCCNFNPQSNLIVSGSFDESVRIWDVKTGKCLKTLPAHSDPVSAVHFNRDG
SLIVSSSYDGLCRIWDTASGQCLKTLIDDDNPPVSFVKFSPNGKYILAATLDNTLKLWDYSKGKCLKTYTGHKNEKYCIF
ANFSVTGGKWIVSGSEDNLVYIWNLQTKEIVQKLQGHTDVVISTACHPTENIIASAALENDKTIKLWKSDC
;
24   
# 
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 9DLW B 28 ? 338 ? Q9Y4B6 1080 ? 1390 ? 1080 1390 
2 2 9DLW A 19 ? 329 ? P61964 24   ? 334  ? 24   334  
# 
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 9DLW MET B 1  ? UNP Q9Y4B6 ? ? 'initiating methionine' 1053 1  
1 9DLW GLY B 2  ? UNP Q9Y4B6 ? ? 'expression tag'        1054 2  
1 9DLW SER B 3  ? UNP Q9Y4B6 ? ? 'expression tag'        1055 3  
1 9DLW SER B 4  ? UNP Q9Y4B6 ? ? 'expression tag'        1056 4  
1 9DLW HIS B 5  ? UNP Q9Y4B6 ? ? 'expression tag'        1057 5  
1 9DLW HIS B 6  ? UNP Q9Y4B6 ? ? 'expression tag'        1058 6  
1 9DLW HIS B 7  ? UNP Q9Y4B6 ? ? 'expression tag'        1059 7  
1 9DLW HIS B 8  ? UNP Q9Y4B6 ? ? 'expression tag'        1060 8  
1 9DLW HIS B 9  ? UNP Q9Y4B6 ? ? 'expression tag'        1061 9  
1 9DLW HIS B 10 ? UNP Q9Y4B6 ? ? 'expression tag'        1062 10 
1 9DLW SER B 11 ? UNP Q9Y4B6 ? ? 'expression tag'        1063 11 
1 9DLW SER B 12 ? UNP Q9Y4B6 ? ? 'expression tag'        1064 12 
1 9DLW GLY B 13 ? UNP Q9Y4B6 ? ? 'expression tag'        1065 13 
1 9DLW ARG B 14 ? UNP Q9Y4B6 ? ? 'expression tag'        1066 14 
1 9DLW GLU B 15 ? UNP Q9Y4B6 ? ? 'expression tag'        1067 15 
1 9DLW ASN B 16 ? UNP Q9Y4B6 ? ? 'expression tag'        1068 16 
1 9DLW LEU B 17 ? UNP Q9Y4B6 ? ? 'expression tag'        1069 17 
1 9DLW TYR B 18 ? UNP Q9Y4B6 ? ? 'expression tag'        1070 18 
1 9DLW PHE B 19 ? UNP Q9Y4B6 ? ? 'expression tag'        1071 19 
1 9DLW GLN B 20 ? UNP Q9Y4B6 ? ? 'expression tag'        1072 20 
1 9DLW GLY B 21 ? UNP Q9Y4B6 ? ? 'expression tag'        1073 21 
1 9DLW SER B 22 ? UNP Q9Y4B6 ? ? 'expression tag'        1074 22 
1 9DLW SER B 23 ? UNP Q9Y4B6 ? ? 'expression tag'        1075 23 
1 9DLW ARG B 24 ? UNP Q9Y4B6 ? ? 'expression tag'        1076 24 
1 9DLW ALA B 25 ? UNP Q9Y4B6 ? ? 'expression tag'        1077 25 
1 9DLW SER B 26 ? UNP Q9Y4B6 ? ? 'expression tag'        1078 26 
1 9DLW ALA B 27 ? UNP Q9Y4B6 ? ? 'expression tag'        1079 27 
2 9DLW MET A 1  ? UNP P61964 ? ? 'initiating methionine' 6    28 
2 9DLW HIS A 2  ? UNP P61964 ? ? 'expression tag'        7    29 
2 9DLW HIS A 3  ? UNP P61964 ? ? 'expression tag'        8    30 
2 9DLW HIS A 4  ? UNP P61964 ? ? 'expression tag'        9    31 
2 9DLW HIS A 5  ? UNP P61964 ? ? 'expression tag'        10   32 
2 9DLW HIS A 6  ? UNP P61964 ? ? 'expression tag'        11   33 
2 9DLW HIS A 7  ? UNP P61964 ? ? 'expression tag'        12   34 
2 9DLW SER A 8  ? UNP P61964 ? ? 'expression tag'        13   35 
2 9DLW SER A 9  ? UNP P61964 ? ? 'expression tag'        14   36 
2 9DLW GLY A 10 ? UNP P61964 ? ? 'expression tag'        15   37 
2 9DLW ARG A 11 ? UNP P61964 ? ? 'expression tag'        16   38 
2 9DLW GLU A 12 ? UNP P61964 ? ? 'expression tag'        17   39 
2 9DLW ASN A 13 ? UNP P61964 ? ? 'expression tag'        18   40 
2 9DLW LEU A 14 ? UNP P61964 ? ? 'expression tag'        19   41 
2 9DLW TYR A 15 ? UNP P61964 ? ? 'expression tag'        20   42 
2 9DLW PHE A 16 ? UNP P61964 ? ? 'expression tag'        21   43 
2 9DLW GLN A 17 ? UNP P61964 ? ? 'expression tag'        22   44 
2 9DLW GLY A 18 ? UNP P61964 ? ? 'expression tag'        23   45 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'surface plasmon resonance' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 PRO A 240 ? ASP A 243 ? PRO B 1292 ASP B 1295 5 ? 4 
HELX_P HELX_P2 AA2 ASP A 268 ? MET A 274 ? ASP B 1320 MET B 1326 1 ? 7 
HELX_P HELX_P3 AA3 MET A 323 ? MET A 328 ? MET B 1375 MET B 1380 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLN 
_struct_mon_prot_cis.label_seq_id           106 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           GLN 
_struct_mon_prot_cis.auth_seq_id            1158 
_struct_mon_prot_cis.auth_asym_id           B 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    107 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     1159 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    B 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       0.14 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 4 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 4 ? 
AA8 ? 4 ? 
AA9 ? 4 ? 
AB1 ? 4 ? 
AB2 ? 4 ? 
AB3 ? 4 ? 
AB4 ? 4 ? 
AB5 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ARG A 29  ? ARG A 35  ? ARG B 1081 ARG B 1087 
AA1 2 THR A 330 ? GLU A 336 ? THR B 1382 GLU B 1388 
AA1 3 TYR A 313 ? ASN A 319 ? TYR B 1365 ASN B 1371 
AA1 4 ILE A 302 ? THR A 307 ? ILE B 1354 THR B 1359 
AA2 1 PHE A 44  ? PHE A 49  ? PHE B 1096 PHE B 1101 
AA2 2 PHE A 55  ? THR A 60  ? PHE B 1107 THR B 1112 
AA2 3 GLN A 64  ? ASN A 69  ? GLN B 1116 ASN B 1121 
AA2 4 GLU A 75  ? ASN A 80  ? GLU B 1127 ASN B 1132 
AA3 1 HIS A 88  ? PRO A 91  ? HIS B 1140 PRO B 1143 
AA3 2 LEU A 97  ? SER A 101 ? LEU B 1149 SER B 1153 
AA3 3 SER A 109 ? GLY A 113 ? SER B 1161 GLY B 1165 
AA3 4 ASP A 119 ? PHE A 124 ? ASP B 1171 PHE B 1176 
AA4 1 TYR A 129 ? PHE A 132 ? TYR B 1181 PHE B 1184 
AA4 2 ARG A 139 ? LYS A 144 ? ARG B 1191 LYS B 1196 
AA4 3 ILE A 147 ? ASP A 152 ? ILE B 1199 ASP B 1204 
AA4 4 LYS A 158 ? LEU A 162 ? LYS B 1210 LEU B 1214 
AA5 1 THR A 177 ? PHE A 178 ? THR B 1229 PHE B 1230 
AA5 2 LEU A 184 ? ASN A 187 ? LEU B 1236 ASN B 1239 
AA5 3 VAL A 190 ? ASP A 193 ? VAL B 1242 ASP B 1245 
AA5 4 GLN A 198 ? LYS A 202 ? GLN B 1250 LYS B 1254 
AA6 1 VAL A 213 ? PHE A 214 ? VAL B 1265 PHE B 1266 
AA6 2 GLU A 220 ? ILE A 223 ? GLU B 1272 ILE B 1275 
AA6 3 GLU A 226 ? ASP A 229 ? GLU B 1278 ASP B 1281 
AA6 4 LEU A 235 ? THR A 238 ? LEU B 1287 THR B 1290 
AA7 1 CYS A 245 ? PHE A 249 ? CYS B 1297 PHE B 1301 
AA7 2 VAL A 255 ? LEU A 261 ? VAL B 1307 LEU B 1313 
AA7 3 PHE A 278 ? ASN A 286 ? PHE B 1330 ASN B 1338 
AA7 4 PRO A 292 ? ASP A 297 ? PRO B 1344 ASP B 1349 
AA8 1 ALA B 31  ? LEU B 36  ? ALA A 36   LEU A 41   
AA8 2 ILE B 322 ? LYS B 326 ? ILE A 327  LYS A 331  
AA8 3 ILE B 310 ? ALA B 315 ? ILE A 315  ALA A 320  
AA8 4 VAL B 299 ? CYS B 304 ? VAL A 304  CYS A 309  
AA9 1 VAL B 43  ? PHE B 48  ? VAL A 48   PHE A 53   
AA9 2 TRP B 54  ? SER B 59  ? TRP A 59   SER A 64   
AA9 3 LEU B 63  ? GLY B 68  ? LEU A 68   GLY A 73   
AA9 4 PHE B 74  ? SER B 79  ? PHE A 79   SER A 84   
AB1 1 ILE B 85  ? TRP B 90  ? ILE A 90   TRP A 95   
AB1 2 LEU B 96  ? SER B 101 ? LEU A 101  SER A 106  
AB1 3 THR B 105 ? ASP B 110 ? THR A 110  ASP A 115  
AB1 4 CYS B 116 ? LYS B 121 ? CYS A 121  LYS A 126  
AB2 1 VAL B 127 ? PHE B 132 ? VAL A 132  PHE A 137  
AB2 2 LEU B 138 ? SER B 143 ? LEU A 143  SER A 148  
AB2 3 VAL B 148 ? ASP B 152 ? VAL A 153  ASP A 157  
AB2 4 CYS B 158 ? LEU B 162 ? CYS A 163  LEU A 167  
AB3 1 VAL B 169 ? PHE B 174 ? VAL A 174  PHE A 179  
AB3 2 LEU B 180 ? SER B 185 ? LEU A 185  SER A 190  
AB3 3 CYS B 190 ? ASP B 194 ? CYS A 195  ASP A 199  
AB3 4 CYS B 200 ? LEU B 204 ? CYS A 205  LEU A 209  
AB4 1 VAL B 212 ? PHE B 217 ? VAL A 217  PHE A 222  
AB4 2 TYR B 223 ? THR B 228 ? TYR A 228  THR A 233  
AB4 3 THR B 232 ? ASP B 237 ? THR A 237  ASP A 242  
AB4 4 LYS B 242 ? TYR B 247 ? LYS A 247  TYR A 252  
AB5 1 ALA B 259 ? SER B 262 ? ALA A 264  SER A 267  
AB5 2 TRP B 268 ? SER B 271 ? TRP A 273  SER A 276  
AB5 3 VAL B 278 ? ASN B 282 ? VAL A 283  ASN A 287  
AB5 4 ILE B 288 ? LEU B 292 ? ILE A 293  LEU A 297  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ILE A 31  ? N ILE B 1083 O LEU A 334 ? O LEU B 1386 
AA1 2 3 O TYR A 335 ? O TYR B 1387 N LEU A 314 ? N LEU B 1366 
AA1 3 4 O ILE A 317 ? O ILE B 1369 N PHE A 303 ? N PHE B 1355 
AA2 1 2 N ALA A 48  ? N ALA B 1100 O MET A 57  ? O MET B 1109 
AA2 2 3 N LEU A 58  ? N LEU B 1110 O LYS A 66  ? O LYS B 1118 
AA2 3 4 N LEU A 67  ? N LEU B 1119 O GLU A 76  ? O GLU B 1128 
AA3 1 2 N GLU A 90  ? N GLU B 1142 O LEU A 99  ? O LEU B 1151 
AA3 2 3 N LEU A 98  ? N LEU B 1150 O TRP A 112 ? O TRP B 1164 
AA3 3 4 N LEU A 111 ? N LEU B 1163 O LYS A 121 ? O LYS B 1173 
AA4 1 2 N GLU A 131 ? N GLU B 1183 O ILE A 141 ? O ILE B 1193 
AA4 2 3 N VAL A 140 ? N VAL B 1192 O TYR A 151 ? O TYR B 1203 
AA4 3 4 N ILE A 150 ? N ILE B 1202 O LEU A 159 ? O LEU B 1211 
AA5 1 2 N THR A 177 ? N THR B 1229 O LEU A 186 ? O LEU B 1238 
AA5 2 3 N VAL A 185 ? N VAL B 1237 O TRP A 192 ? O TRP B 1244 
AA5 3 4 N ASP A 193 ? N ASP B 1245 O GLN A 198 ? O GLN B 1250 
AA6 1 2 N VAL A 213 ? N VAL B 1265 O ILE A 222 ? O ILE B 1274 
AA6 2 3 N ILE A 223 ? N ILE B 1275 O GLU A 226 ? O GLU B 1278 
AA6 3 4 N ILE A 227 ? N ILE B 1279 O LEU A 236 ? O LEU B 1288 
AA7 1 2 N VAL A 248 ? N VAL B 1300 O TYR A 257 ? O TYR B 1309 
AA7 2 3 N GLY A 258 ? N GLY B 1310 O ARG A 283 ? O ARG B 1335 
AA7 3 4 N THR A 284 ? N THR B 1336 O ILE A 293 ? O ILE B 1345 
AA8 1 2 N LEU B 36  ? N LEU A 41   O ILE B 322 ? O ILE A 327  
AA8 2 3 O TRP B 325 ? O TRP A 330  N ILE B 311 ? N ILE A 316  
AA8 3 4 O ALA B 312 ? O ALA A 317  N ALA B 303 ? N ALA A 308  
AA9 1 2 N LYS B 47  ? N LYS A 52   O ALA B 56  ? O ALA A 61   
AA9 2 3 N LEU B 55  ? N LEU A 60   O TRP B 67  ? O TRP A 72   
AA9 3 4 N ILE B 64  ? N ILE A 69   O ILE B 78  ? O ILE A 83   
AB1 1 2 N SER B 86  ? N SER A 91   O ALA B 100 ? O ALA A 105  
AB1 2 3 N LEU B 97  ? N LEU A 102  O TRP B 109 ? O TRP A 114  
AB1 3 4 N LEU B 106 ? N LEU A 111  O LEU B 120 ? O LEU A 125  
AB2 1 2 N ASN B 131 ? N ASN A 136  O VAL B 140 ? O VAL A 145  
AB2 2 3 N ILE B 139 ? N ILE A 144  O TRP B 151 ? O TRP A 156  
AB2 3 4 N VAL B 148 ? N VAL A 153  O LEU B 162 ? O LEU A 167  
AB3 1 2 N HIS B 173 ? N HIS A 178  O VAL B 182 ? O VAL A 187  
AB3 2 3 N ILE B 181 ? N ILE A 186  O TRP B 193 ? O TRP A 198  
AB3 3 4 N ILE B 192 ? N ILE A 197  O LEU B 201 ? O LEU A 206  
AB4 1 2 N LYS B 216 ? N LYS A 221  O LEU B 225 ? O LEU A 230  
AB4 2 3 N ILE B 224 ? N ILE A 229  O TRP B 236 ? O TRP A 241  
AB4 3 4 N LEU B 235 ? N LEU A 240  O LEU B 244 ? O LEU A 249  
AB5 1 2 N ASN B 260 ? N ASN A 265  O VAL B 270 ? O VAL A 275  
AB5 2 3 N SER B 271 ? N SER A 276  O TYR B 279 ? O TYR A 284  
AB5 3 4 N ILE B 280 ? N ILE A 285  O VAL B 289 ? O VAL A 294  
# 
_pdbx_entry_details.entry_id                   9DLW 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 OD2 A ASP   107  ? ? H37 B A1BAF 1401 ? ? 1.51 
2  1 H30 B A1BAF 1401 ? ? O   B HOH   1509 ? ? 1.52 
3  1 OE1 B GLN   1314 ? ? O   B HOH   1501 ? ? 1.94 
4  1 O   B HOH   1503 ? ? O   B HOH   1622 ? ? 1.95 
5  1 O   B HOH   1514 ? ? O   B HOH   1658 ? ? 2.05 
6  1 ND2 B ASN   1132 ? ? O   B HOH   1502 ? ? 2.09 
7  1 OE1 B GLU   1093 ? ? O   B HOH   1503 ? ? 2.11 
8  1 OD1 A ASP   213  ? ? O   A HOH   401  ? ? 2.15 
9  1 O   A HOH   590  ? ? O   A HOH   593  ? ? 2.17 
10 1 O   B HOH   1634 ? ? O   A HOH   543  ? ? 2.18 
11 1 OG  A SER   50   ? B OG  A SER   63   ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    B 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     1508 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     1625 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   3_544 
_pdbx_validate_symm_contact.dist              2.16 
# 
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 ASN B 1090 ? ? 83.48   -40.58  
2  1 ARG B 1106 ? ? 88.14   -19.49  
3  1 ALA B 1154 ? ? -110.32 -163.69 
4  1 THR B 1155 ? ? -101.44 -60.64  
5  1 SER B 1168 ? ? 54.40   -85.20  
6  1 HIS B 1187 ? ? -80.97  -78.17  
7  1 ASN B 1276 ? ? 60.01   -122.31 
8  1 ALA B 1315 ? ? -122.63 -93.34  
9  1 ASP B 1316 ? ? 38.50   87.16   
10 1 GLU B 1318 ? ? -68.49  1.84    
11 1 ILE B 1345 ? ? -107.11 -70.29  
12 1 ASP B 1376 ? ? 64.60   -142.37 
13 1 ASN B 1379 ? ? -103.74 74.09   
14 1 ASP B 1381 ? ? -154.72 89.25   
15 1 LYS A 109  ? ? 82.49   6.47    
16 1 ASN A 130  ? ? -160.59 -169.91 
17 1 ASP A 211  ? ? -104.69 -139.53 
18 1 LEU A 234  ? ? -75.56  37.52   
19 1 LYS A 259  ? ? -132.22 -42.84  
20 1 LEU A 321  ? ? -87.23  -158.26 
21 1 ASP A 324  ? ? -126.08 -63.76  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1  1 O ? B HOH 1686 ? 6.18  . 
2  1 O ? B HOH 1687 ? 8.61  . 
3  1 O ? A HOH 625  ? 5.98  . 
4  1 O ? A HOH 626  ? 6.70  . 
5  1 O ? A HOH 627  ? 6.92  . 
6  1 O ? A HOH 628  ? 7.85  . 
7  1 O ? A HOH 629  ? 7.85  . 
8  1 O ? A HOH 630  ? 8.31  . 
9  1 O ? A HOH 631  ? 9.04  . 
10 1 O ? A HOH 632  ? 11.84 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 B MET 1053 ? A MET 1  
2  1 Y 1 B GLY 1054 ? A GLY 2  
3  1 Y 1 B SER 1055 ? A SER 3  
4  1 Y 1 B SER 1056 ? A SER 4  
5  1 Y 1 B HIS 1057 ? A HIS 5  
6  1 Y 1 B HIS 1058 ? A HIS 6  
7  1 Y 1 B HIS 1059 ? A HIS 7  
8  1 Y 1 B HIS 1060 ? A HIS 8  
9  1 Y 1 B HIS 1061 ? A HIS 9  
10 1 Y 1 B HIS 1062 ? A HIS 10 
11 1 Y 1 B SER 1063 ? A SER 11 
12 1 Y 1 B SER 1064 ? A SER 12 
13 1 Y 1 B GLY 1065 ? A GLY 13 
14 1 Y 1 B ARG 1066 ? A ARG 14 
15 1 Y 1 B GLU 1067 ? A GLU 15 
16 1 Y 1 B ASN 1068 ? A ASN 16 
17 1 Y 1 B LEU 1069 ? A LEU 17 
18 1 Y 1 B TYR 1070 ? A TYR 18 
19 1 Y 1 B PHE 1071 ? A PHE 19 
20 1 Y 1 B GLN 1072 ? A GLN 20 
21 1 Y 1 B GLY 1073 ? A GLY 21 
22 1 Y 1 B SER 1074 ? A SER 22 
23 1 Y 1 B SER 1075 ? A SER 23 
24 1 Y 1 B ARG 1076 ? A ARG 24 
25 1 Y 1 B ALA 1077 ? A ALA 25 
26 1 Y 1 B SER 1078 ? A SER 26 
27 1 Y 1 B ALA 1079 ? A ALA 27 
28 1 Y 1 A MET 6    ? B MET 1  
29 1 Y 1 A HIS 7    ? B HIS 2  
30 1 Y 1 A HIS 8    ? B HIS 3  
31 1 Y 1 A HIS 9    ? B HIS 4  
32 1 Y 1 A HIS 10   ? B HIS 5  
33 1 Y 1 A HIS 11   ? B HIS 6  
34 1 Y 1 A HIS 12   ? B HIS 7  
35 1 Y 1 A SER 13   ? B SER 8  
36 1 Y 1 A SER 14   ? B SER 9  
37 1 Y 1 A GLY 15   ? B GLY 10 
38 1 Y 1 A ARG 16   ? B ARG 11 
39 1 Y 1 A GLU 17   ? B GLU 12 
40 1 Y 1 A ASN 18   ? B ASN 13 
41 1 Y 1 A LEU 19   ? B LEU 14 
42 1 Y 1 A TYR 20   ? B TYR 15 
43 1 Y 1 A PHE 21   ? B PHE 16 
44 1 Y 1 A GLN 22   ? B GLN 17 
45 1 Y 1 A GLY 23   ? B GLY 18 
46 1 Y 1 A THR 24   ? B THR 19 
47 1 Y 1 A GLN 25   ? B GLN 20 
48 1 Y 1 A SER 26   ? B SER 21 
49 1 Y 1 A LYS 27   ? B LYS 22 
50 1 Y 1 A PRO 28   ? B PRO 23 
51 1 Y 1 A THR 29   ? B THR 24 
52 1 Y 1 A PRO 30   ? B PRO 25 
# 
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 
A1BAF C10  C  N N 1   
A1BAF C11  C  Y N 2   
A1BAF C12  C  Y N 3   
A1BAF C13  C  Y N 4   
A1BAF C14  C  Y N 5   
A1BAF C15  C  Y N 6   
A1BAF C16  C  Y N 7   
A1BAF C17  C  Y N 8   
A1BAF C18  C  Y N 9   
A1BAF C19  C  Y N 10  
A1BAF C20  C  Y N 11  
A1BAF C21  C  N N 12  
A1BAF C22  C  N S 13  
A1BAF C23  C  N N 14  
A1BAF C24  C  Y N 15  
A1BAF C25  C  Y N 16  
A1BAF C26  C  Y N 17  
A1BAF C01  C  N N 18  
A1BAF C02  C  N S 19  
A1BAF C03  C  N N 20  
A1BAF C04  C  N N 21  
A1BAF C05  C  N R 22  
A1BAF C06  C  N N 23  
A1BAF C07  C  N N 24  
A1BAF C08  C  N N 25  
A1BAF C09  C  N N 26  
A1BAF C27  C  Y N 27  
A1BAF C28  C  Y N 28  
A1BAF C29  C  Y N 29  
A1BAF C30  C  N N 30  
A1BAF C31  C  Y N 31  
A1BAF C32  C  Y N 32  
A1BAF C33  C  Y N 33  
A1BAF C34  C  Y N 34  
A1BAF C35  C  Y N 35  
A1BAF C36  C  Y N 36  
A1BAF C37  C  Y N 37  
A1BAF C38  C  N N 38  
A1BAF C39  C  N N 39  
A1BAF C40  C  N N 40  
A1BAF C41  C  N N 41  
A1BAF C42  C  N N 42  
A1BAF C43  C  N N 43  
A1BAF C44  C  Y N 44  
A1BAF C45  C  Y N 45  
A1BAF C46  C  Y N 46  
A1BAF C47  C  Y N 47  
A1BAF C48  C  Y N 48  
A1BAF C49  C  N N 49  
A1BAF C50  C  N N 50  
A1BAF C51  C  N N 51  
A1BAF C52  C  N N 52  
A1BAF C53  C  N N 53  
A1BAF C54  C  N N 54  
A1BAF C55  C  N N 55  
A1BAF C56  C  N N 56  
A1BAF C57  C  N N 57  
A1BAF C58  C  N N 58  
A1BAF C59  C  N N 59  
A1BAF C60  C  N N 60  
A1BAF C61  C  N N 61  
A1BAF C62  C  N N 62  
A1BAF C63  C  N N 63  
A1BAF C64  C  N N 64  
A1BAF C65  C  N N 65  
A1BAF C66  C  N N 66  
A1BAF C67  C  N N 67  
A1BAF C68  C  N N 68  
A1BAF C69  C  N N 69  
A1BAF C70  C  N N 70  
A1BAF F01  F  N N 71  
A1BAF F02  F  N N 72  
A1BAF F03  F  N N 73  
A1BAF F04  F  N N 74  
A1BAF F05  F  N N 75  
A1BAF F06  F  N N 76  
A1BAF N01  N  N N 77  
A1BAF N02  N  N N 78  
A1BAF N03  N  Y N 79  
A1BAF N04  N  N N 80  
A1BAF N05  N  N N 81  
A1BAF N06  N  N N 82  
A1BAF N07  N  N N 83  
A1BAF N08  N  N N 84  
A1BAF N09  N  N N 85  
A1BAF O01  O  N N 86  
A1BAF O02  O  N N 87  
A1BAF O03  O  N N 88  
A1BAF O04  O  N N 89  
A1BAF O05  O  N N 90  
A1BAF O06  O  N N 91  
A1BAF O07  O  N N 92  
A1BAF O08  O  N N 93  
A1BAF O09  O  N N 94  
A1BAF O10  O  N N 95  
A1BAF O11  O  N N 96  
A1BAF O12  O  N N 97  
A1BAF O13  O  N N 98  
A1BAF O14  O  N N 99  
A1BAF O15  O  N N 100 
A1BAF CL01 CL N N 101 
A1BAF CL02 CL N N 102 
A1BAF H17  H  N N 103 
A1BAF H18  H  N N 104 
A1BAF H20  H  N N 105 
A1BAF H21  H  N N 106 
A1BAF H22  H  N N 107 
A1BAF H24  H  N N 108 
A1BAF H26  H  N N 109 
A1BAF H25  H  N N 110 
A1BAF H27  H  N N 111 
A1BAF H28  H  N N 112 
A1BAF H02  H  N N 113 
A1BAF H01  H  N N 114 
A1BAF H03  H  N N 115 
A1BAF H05  H  N N 116 
A1BAF H04  H  N N 117 
A1BAF H06  H  N N 118 
A1BAF H09  H  N N 119 
A1BAF H07  H  N N 120 
A1BAF H08  H  N N 121 
A1BAF H10  H  N N 122 
A1BAF H12  H  N N 123 
A1BAF H13  H  N N 124 
A1BAF H11  H  N N 125 
A1BAF H15  H  N N 126 
A1BAF H14  H  N N 127 
A1BAF H16  H  N N 128 
A1BAF H29  H  N N 129 
A1BAF H32  H  N N 130 
A1BAF H33  H  N N 131 
A1BAF H34  H  N N 132 
A1BAF H36  H  N N 133 
A1BAF H38  H  N N 134 
A1BAF H39  H  N N 135 
A1BAF H40  H  N N 136 
A1BAF H41  H  N N 137 
A1BAF H44  H  N N 138 
A1BAF H43  H  N N 139 
A1BAF H46  H  N N 140 
A1BAF H45  H  N N 141 
A1BAF H47  H  N N 142 
A1BAF H48  H  N N 143 
A1BAF H49  H  N N 144 
A1BAF H50  H  N N 145 
A1BAF H52  H  N N 146 
A1BAF H51  H  N N 147 
A1BAF H53  H  N N 148 
A1BAF H54  H  N N 149 
A1BAF H56  H  N N 150 
A1BAF H55  H  N N 151 
A1BAF H58  H  N N 152 
A1BAF H57  H  N N 153 
A1BAF H59  H  N N 154 
A1BAF H60  H  N N 155 
A1BAF H61  H  N N 156 
A1BAF H62  H  N N 157 
A1BAF H64  H  N N 158 
A1BAF H63  H  N N 159 
A1BAF H65  H  N N 160 
A1BAF H66  H  N N 161 
A1BAF H68  H  N N 162 
A1BAF H67  H  N N 163 
A1BAF H70  H  N N 164 
A1BAF H69  H  N N 165 
A1BAF H72  H  N N 166 
A1BAF H71  H  N N 167 
A1BAF H74  H  N N 168 
A1BAF H73  H  N N 169 
A1BAF H76  H  N N 170 
A1BAF H75  H  N N 171 
A1BAF H78  H  N N 172 
A1BAF H77  H  N N 173 
A1BAF H79  H  N N 174 
A1BAF H80  H  N N 175 
A1BAF H82  H  N N 176 
A1BAF H81  H  N N 177 
A1BAF H19  H  N N 178 
A1BAF H23  H  N N 179 
A1BAF H30  H  N N 180 
A1BAF H31  H  N N 181 
A1BAF H35  H  N N 182 
A1BAF H37  H  N N 183 
A1BAF H42  H  N N 184 
A1BAF H83  H  N N 185 
ALA   N    N  N N 186 
ALA   CA   C  N S 187 
ALA   C    C  N N 188 
ALA   O    O  N N 189 
ALA   CB   C  N N 190 
ALA   OXT  O  N N 191 
ALA   H    H  N N 192 
ALA   H2   H  N N 193 
ALA   HA   H  N N 194 
ALA   HB1  H  N N 195 
ALA   HB2  H  N N 196 
ALA   HB3  H  N N 197 
ALA   HXT  H  N N 198 
ARG   N    N  N N 199 
ARG   CA   C  N S 200 
ARG   C    C  N N 201 
ARG   O    O  N N 202 
ARG   CB   C  N N 203 
ARG   CG   C  N N 204 
ARG   CD   C  N N 205 
ARG   NE   N  N N 206 
ARG   CZ   C  N N 207 
ARG   NH1  N  N N 208 
ARG   NH2  N  N N 209 
ARG   OXT  O  N N 210 
ARG   H    H  N N 211 
ARG   H2   H  N N 212 
ARG   HA   H  N N 213 
ARG   HB2  H  N N 214 
ARG   HB3  H  N N 215 
ARG   HG2  H  N N 216 
ARG   HG3  H  N N 217 
ARG   HD2  H  N N 218 
ARG   HD3  H  N N 219 
ARG   HE   H  N N 220 
ARG   HH11 H  N N 221 
ARG   HH12 H  N N 222 
ARG   HH21 H  N N 223 
ARG   HH22 H  N N 224 
ARG   HXT  H  N N 225 
ASN   N    N  N N 226 
ASN   CA   C  N S 227 
ASN   C    C  N N 228 
ASN   O    O  N N 229 
ASN   CB   C  N N 230 
ASN   CG   C  N N 231 
ASN   OD1  O  N N 232 
ASN   ND2  N  N N 233 
ASN   OXT  O  N N 234 
ASN   H    H  N N 235 
ASN   H2   H  N N 236 
ASN   HA   H  N N 237 
ASN   HB2  H  N N 238 
ASN   HB3  H  N N 239 
ASN   HD21 H  N N 240 
ASN   HD22 H  N N 241 
ASN   HXT  H  N N 242 
ASP   N    N  N N 243 
ASP   CA   C  N S 244 
ASP   C    C  N N 245 
ASP   O    O  N N 246 
ASP   CB   C  N N 247 
ASP   CG   C  N N 248 
ASP   OD1  O  N N 249 
ASP   OD2  O  N N 250 
ASP   OXT  O  N N 251 
ASP   H    H  N N 252 
ASP   H2   H  N N 253 
ASP   HA   H  N N 254 
ASP   HB2  H  N N 255 
ASP   HB3  H  N N 256 
ASP   HD2  H  N N 257 
ASP   HXT  H  N N 258 
CYS   N    N  N N 259 
CYS   CA   C  N R 260 
CYS   C    C  N N 261 
CYS   O    O  N N 262 
CYS   CB   C  N N 263 
CYS   SG   S  N N 264 
CYS   OXT  O  N N 265 
CYS   H    H  N N 266 
CYS   H2   H  N N 267 
CYS   HA   H  N N 268 
CYS   HB2  H  N N 269 
CYS   HB3  H  N N 270 
CYS   HG   H  N N 271 
CYS   HXT  H  N N 272 
GLN   N    N  N N 273 
GLN   CA   C  N S 274 
GLN   C    C  N N 275 
GLN   O    O  N N 276 
GLN   CB   C  N N 277 
GLN   CG   C  N N 278 
GLN   CD   C  N N 279 
GLN   OE1  O  N N 280 
GLN   NE2  N  N N 281 
GLN   OXT  O  N N 282 
GLN   H    H  N N 283 
GLN   H2   H  N N 284 
GLN   HA   H  N N 285 
GLN   HB2  H  N N 286 
GLN   HB3  H  N N 287 
GLN   HG2  H  N N 288 
GLN   HG3  H  N N 289 
GLN   HE21 H  N N 290 
GLN   HE22 H  N N 291 
GLN   HXT  H  N N 292 
GLU   N    N  N N 293 
GLU   CA   C  N S 294 
GLU   C    C  N N 295 
GLU   O    O  N N 296 
GLU   CB   C  N N 297 
GLU   CG   C  N N 298 
GLU   CD   C  N N 299 
GLU   OE1  O  N N 300 
GLU   OE2  O  N N 301 
GLU   OXT  O  N N 302 
GLU   H    H  N N 303 
GLU   H2   H  N N 304 
GLU   HA   H  N N 305 
GLU   HB2  H  N N 306 
GLU   HB3  H  N N 307 
GLU   HG2  H  N N 308 
GLU   HG3  H  N N 309 
GLU   HE2  H  N N 310 
GLU   HXT  H  N N 311 
GLY   N    N  N N 312 
GLY   CA   C  N N 313 
GLY   C    C  N N 314 
GLY   O    O  N N 315 
GLY   OXT  O  N N 316 
GLY   H    H  N N 317 
GLY   H2   H  N N 318 
GLY   HA2  H  N N 319 
GLY   HA3  H  N N 320 
GLY   HXT  H  N N 321 
HIS   N    N  N N 322 
HIS   CA   C  N S 323 
HIS   C    C  N N 324 
HIS   O    O  N N 325 
HIS   CB   C  N N 326 
HIS   CG   C  Y N 327 
HIS   ND1  N  Y N 328 
HIS   CD2  C  Y N 329 
HIS   CE1  C  Y N 330 
HIS   NE2  N  Y N 331 
HIS   OXT  O  N N 332 
HIS   H    H  N N 333 
HIS   H2   H  N N 334 
HIS   HA   H  N N 335 
HIS   HB2  H  N N 336 
HIS   HB3  H  N N 337 
HIS   HD1  H  N N 338 
HIS   HD2  H  N N 339 
HIS   HE1  H  N N 340 
HIS   HE2  H  N N 341 
HIS   HXT  H  N N 342 
HOH   O    O  N N 343 
HOH   H1   H  N N 344 
HOH   H2   H  N N 345 
ILE   N    N  N N 346 
ILE   CA   C  N S 347 
ILE   C    C  N N 348 
ILE   O    O  N N 349 
ILE   CB   C  N S 350 
ILE   CG1  C  N N 351 
ILE   CG2  C  N N 352 
ILE   CD1  C  N N 353 
ILE   OXT  O  N N 354 
ILE   H    H  N N 355 
ILE   H2   H  N N 356 
ILE   HA   H  N N 357 
ILE   HB   H  N N 358 
ILE   HG12 H  N N 359 
ILE   HG13 H  N N 360 
ILE   HG21 H  N N 361 
ILE   HG22 H  N N 362 
ILE   HG23 H  N N 363 
ILE   HD11 H  N N 364 
ILE   HD12 H  N N 365 
ILE   HD13 H  N N 366 
ILE   HXT  H  N N 367 
LEU   N    N  N N 368 
LEU   CA   C  N S 369 
LEU   C    C  N N 370 
LEU   O    O  N N 371 
LEU   CB   C  N N 372 
LEU   CG   C  N N 373 
LEU   CD1  C  N N 374 
LEU   CD2  C  N N 375 
LEU   OXT  O  N N 376 
LEU   H    H  N N 377 
LEU   H2   H  N N 378 
LEU   HA   H  N N 379 
LEU   HB2  H  N N 380 
LEU   HB3  H  N N 381 
LEU   HG   H  N N 382 
LEU   HD11 H  N N 383 
LEU   HD12 H  N N 384 
LEU   HD13 H  N N 385 
LEU   HD21 H  N N 386 
LEU   HD22 H  N N 387 
LEU   HD23 H  N N 388 
LEU   HXT  H  N N 389 
LYS   N    N  N N 390 
LYS   CA   C  N S 391 
LYS   C    C  N N 392 
LYS   O    O  N N 393 
LYS   CB   C  N N 394 
LYS   CG   C  N N 395 
LYS   CD   C  N N 396 
LYS   CE   C  N N 397 
LYS   NZ   N  N N 398 
LYS   OXT  O  N N 399 
LYS   H    H  N N 400 
LYS   H2   H  N N 401 
LYS   HA   H  N N 402 
LYS   HB2  H  N N 403 
LYS   HB3  H  N N 404 
LYS   HG2  H  N N 405 
LYS   HG3  H  N N 406 
LYS   HD2  H  N N 407 
LYS   HD3  H  N N 408 
LYS   HE2  H  N N 409 
LYS   HE3  H  N N 410 
LYS   HZ1  H  N N 411 
LYS   HZ2  H  N N 412 
LYS   HZ3  H  N N 413 
LYS   HXT  H  N N 414 
MET   N    N  N N 415 
MET   CA   C  N S 416 
MET   C    C  N N 417 
MET   O    O  N N 418 
MET   CB   C  N N 419 
MET   CG   C  N N 420 
MET   SD   S  N N 421 
MET   CE   C  N N 422 
MET   OXT  O  N N 423 
MET   H    H  N N 424 
MET   H2   H  N N 425 
MET   HA   H  N N 426 
MET   HB2  H  N N 427 
MET   HB3  H  N N 428 
MET   HG2  H  N N 429 
MET   HG3  H  N N 430 
MET   HE1  H  N N 431 
MET   HE2  H  N N 432 
MET   HE3  H  N N 433 
MET   HXT  H  N N 434 
PHE   N    N  N N 435 
PHE   CA   C  N S 436 
PHE   C    C  N N 437 
PHE   O    O  N N 438 
PHE   CB   C  N N 439 
PHE   CG   C  Y N 440 
PHE   CD1  C  Y N 441 
PHE   CD2  C  Y N 442 
PHE   CE1  C  Y N 443 
PHE   CE2  C  Y N 444 
PHE   CZ   C  Y N 445 
PHE   OXT  O  N N 446 
PHE   H    H  N N 447 
PHE   H2   H  N N 448 
PHE   HA   H  N N 449 
PHE   HB2  H  N N 450 
PHE   HB3  H  N N 451 
PHE   HD1  H  N N 452 
PHE   HD2  H  N N 453 
PHE   HE1  H  N N 454 
PHE   HE2  H  N N 455 
PHE   HZ   H  N N 456 
PHE   HXT  H  N N 457 
PRO   N    N  N N 458 
PRO   CA   C  N S 459 
PRO   C    C  N N 460 
PRO   O    O  N N 461 
PRO   CB   C  N N 462 
PRO   CG   C  N N 463 
PRO   CD   C  N N 464 
PRO   OXT  O  N N 465 
PRO   H    H  N N 466 
PRO   HA   H  N N 467 
PRO   HB2  H  N N 468 
PRO   HB3  H  N N 469 
PRO   HG2  H  N N 470 
PRO   HG3  H  N N 471 
PRO   HD2  H  N N 472 
PRO   HD3  H  N N 473 
PRO   HXT  H  N N 474 
SER   N    N  N N 475 
SER   CA   C  N S 476 
SER   C    C  N N 477 
SER   O    O  N N 478 
SER   CB   C  N N 479 
SER   OG   O  N N 480 
SER   OXT  O  N N 481 
SER   H    H  N N 482 
SER   H2   H  N N 483 
SER   HA   H  N N 484 
SER   HB2  H  N N 485 
SER   HB3  H  N N 486 
SER   HG   H  N N 487 
SER   HXT  H  N N 488 
THR   N    N  N N 489 
THR   CA   C  N S 490 
THR   C    C  N N 491 
THR   O    O  N N 492 
THR   CB   C  N R 493 
THR   OG1  O  N N 494 
THR   CG2  C  N N 495 
THR   OXT  O  N N 496 
THR   H    H  N N 497 
THR   H2   H  N N 498 
THR   HA   H  N N 499 
THR   HB   H  N N 500 
THR   HG1  H  N N 501 
THR   HG21 H  N N 502 
THR   HG22 H  N N 503 
THR   HG23 H  N N 504 
THR   HXT  H  N N 505 
TRP   N    N  N N 506 
TRP   CA   C  N S 507 
TRP   C    C  N N 508 
TRP   O    O  N N 509 
TRP   CB   C  N N 510 
TRP   CG   C  Y N 511 
TRP   CD1  C  Y N 512 
TRP   CD2  C  Y N 513 
TRP   NE1  N  Y N 514 
TRP   CE2  C  Y N 515 
TRP   CE3  C  Y N 516 
TRP   CZ2  C  Y N 517 
TRP   CZ3  C  Y N 518 
TRP   CH2  C  Y N 519 
TRP   OXT  O  N N 520 
TRP   H    H  N N 521 
TRP   H2   H  N N 522 
TRP   HA   H  N N 523 
TRP   HB2  H  N N 524 
TRP   HB3  H  N N 525 
TRP   HD1  H  N N 526 
TRP   HE1  H  N N 527 
TRP   HE3  H  N N 528 
TRP   HZ2  H  N N 529 
TRP   HZ3  H  N N 530 
TRP   HH2  H  N N 531 
TRP   HXT  H  N N 532 
TYR   N    N  N N 533 
TYR   CA   C  N S 534 
TYR   C    C  N N 535 
TYR   O    O  N N 536 
TYR   CB   C  N N 537 
TYR   CG   C  Y N 538 
TYR   CD1  C  Y N 539 
TYR   CD2  C  Y N 540 
TYR   CE1  C  Y N 541 
TYR   CE2  C  Y N 542 
TYR   CZ   C  Y N 543 
TYR   OH   O  N N 544 
TYR   OXT  O  N N 545 
TYR   H    H  N N 546 
TYR   H2   H  N N 547 
TYR   HA   H  N N 548 
TYR   HB2  H  N N 549 
TYR   HB3  H  N N 550 
TYR   HD1  H  N N 551 
TYR   HD2  H  N N 552 
TYR   HE1  H  N N 553 
TYR   HE2  H  N N 554 
TYR   HH   H  N N 555 
TYR   HXT  H  N N 556 
VAL   N    N  N N 557 
VAL   CA   C  N S 558 
VAL   C    C  N N 559 
VAL   O    O  N N 560 
VAL   CB   C  N N 561 
VAL   CG1  C  N N 562 
VAL   CG2  C  N N 563 
VAL   OXT  O  N N 564 
VAL   H    H  N N 565 
VAL   H2   H  N N 566 
VAL   HA   H  N N 567 
VAL   HB   H  N N 568 
VAL   HG11 H  N N 569 
VAL   HG12 H  N N 570 
VAL   HG13 H  N N 571 
VAL   HG21 H  N N 572 
VAL   HG22 H  N N 573 
VAL   HG23 H  N N 574 
VAL   HXT  H  N N 575 
# 
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 
A1BAF N01 C01  sing N N 1   
A1BAF N01 C07  sing N N 2   
A1BAF N01 C33  sing N N 3   
A1BAF N02 C02  sing N N 4   
A1BAF N02 C04  sing N N 5   
A1BAF N02 C05  sing N N 6   
A1BAF N03 C11  sing Y N 7   
A1BAF N03 C14  sing Y N 8   
A1BAF N04 C21  sing N N 9   
A1BAF N04 C22  sing N N 10  
A1BAF N05 C30  sing N N 11  
A1BAF N06 C34  sing N N 12  
A1BAF N06 C38  sing N N 13  
A1BAF N07 C40  sing N N 14  
A1BAF N07 C41  sing N N 15  
A1BAF N08 C49  sing N N 16  
A1BAF N08 C50  sing N N 17  
A1BAF N09 C08  sing N N 18  
A1BAF N09 C69  sing N N 19  
A1BAF C01 C02  sing N N 20  
A1BAF C02 C03  sing N N 21  
A1BAF C05 C06  sing N N 22  
A1BAF C05 C07  sing N N 23  
A1BAF C08 C09  sing N N 24  
A1BAF C08 O01  doub N N 25  
A1BAF C09 C10  doub N E 26  
A1BAF C10 C11  sing N N 27  
A1BAF C11 C12  doub Y N 28  
A1BAF C12 C13  sing Y N 29  
A1BAF C12 C15  sing N N 30  
A1BAF C13 C14  doub Y N 31  
A1BAF C13 C21  sing N N 32  
A1BAF C15 C16  doub Y N 33  
A1BAF C15 C20  sing Y N 34  
A1BAF C16 C17  sing Y N 35  
A1BAF C16 F01  sing N N 36  
A1BAF C17 C18  doub Y N 37  
A1BAF C18 C19  sing Y N 38  
A1BAF C18 CL01 sing N N 39  
A1BAF C19 C20  doub Y N 40  
A1BAF C21 O02  doub N N 41  
A1BAF C22 C23  sing N N 42  
A1BAF C22 C24  sing N N 43  
A1BAF C23 C30  sing N N 44  
A1BAF C24 C25  doub Y N 45  
A1BAF C24 C29  sing Y N 46  
A1BAF C25 C26  sing Y N 47  
A1BAF C26 C27  doub Y N 48  
A1BAF C27 C28  sing Y N 49  
A1BAF C27 F02  sing N N 50  
A1BAF C28 C29  doub Y N 51  
A1BAF C28 CL02 sing N N 52  
A1BAF C30 O03  doub N N 53  
A1BAF C31 C32  doub Y N 54  
A1BAF C31 C36  sing Y N 55  
A1BAF C32 C33  sing Y N 56  
A1BAF C33 C34  doub Y N 57  
A1BAF C34 C35  sing Y N 58  
A1BAF C35 C36  doub Y N 59  
A1BAF C36 C37  sing N N 60  
A1BAF C37 C44  doub Y N 61  
A1BAF C37 C48  sing Y N 62  
A1BAF C38 C39  sing N N 63  
A1BAF C38 O04  doub N N 64  
A1BAF C39 C40  doub N N 65  
A1BAF C39 C43  sing N N 66  
A1BAF C41 C42  sing N N 67  
A1BAF C41 O05  doub N N 68  
A1BAF C42 C43  doub N N 69  
A1BAF C43 C70  sing N N 70  
A1BAF C44 C45  sing Y N 71  
A1BAF C45 C46  doub Y N 72  
A1BAF C45 C49  sing N N 73  
A1BAF C46 C47  sing Y N 74  
A1BAF C47 C48  doub Y N 75  
A1BAF C48 F03  sing N N 76  
A1BAF C49 O06  doub N N 77  
A1BAF C50 C51  sing N N 78  
A1BAF C51 O07  sing N N 79  
A1BAF C52 C53  sing N N 80  
A1BAF C52 O07  sing N N 81  
A1BAF C53 O08  sing N N 82  
A1BAF C54 C55  sing N N 83  
A1BAF C54 O08  sing N N 84  
A1BAF C55 O09  sing N N 85  
A1BAF C56 C57  sing N N 86  
A1BAF C56 O09  sing N N 87  
A1BAF C57 O10  sing N N 88  
A1BAF C58 C59  sing N N 89  
A1BAF C58 O10  sing N N 90  
A1BAF C59 O11  sing N N 91  
A1BAF C60 C61  sing N N 92  
A1BAF C60 O11  sing N N 93  
A1BAF C61 O12  sing N N 94  
A1BAF C62 C63  sing N N 95  
A1BAF C62 O12  sing N N 96  
A1BAF C63 O13  sing N N 97  
A1BAF C64 C65  sing N N 98  
A1BAF C64 O13  sing N N 99  
A1BAF C65 O14  sing N N 100 
A1BAF C66 C67  sing N N 101 
A1BAF C66 O14  sing N N 102 
A1BAF C67 O15  sing N N 103 
A1BAF C68 C69  sing N N 104 
A1BAF C68 O15  sing N N 105 
A1BAF C70 F04  sing N N 106 
A1BAF C70 F05  sing N N 107 
A1BAF C70 F06  sing N N 108 
A1BAF C10 H17  sing N N 109 
A1BAF C14 H18  sing N N 110 
A1BAF C17 H20  sing N N 111 
A1BAF C19 H21  sing N N 112 
A1BAF C20 H22  sing N N 113 
A1BAF C22 H24  sing N N 114 
A1BAF C23 H26  sing N N 115 
A1BAF C23 H25  sing N N 116 
A1BAF C25 H27  sing N N 117 
A1BAF C26 H28  sing N N 118 
A1BAF C01 H02  sing N N 119 
A1BAF C01 H01  sing N N 120 
A1BAF C02 H03  sing N N 121 
A1BAF C03 H05  sing N N 122 
A1BAF C03 H04  sing N N 123 
A1BAF C03 H06  sing N N 124 
A1BAF C04 H09  sing N N 125 
A1BAF C04 H07  sing N N 126 
A1BAF C04 H08  sing N N 127 
A1BAF C05 H10  sing N N 128 
A1BAF C06 H12  sing N N 129 
A1BAF C06 H13  sing N N 130 
A1BAF C06 H11  sing N N 131 
A1BAF C07 H15  sing N N 132 
A1BAF C07 H14  sing N N 133 
A1BAF C09 H16  sing N N 134 
A1BAF C29 H29  sing N N 135 
A1BAF C31 H32  sing N N 136 
A1BAF C32 H33  sing N N 137 
A1BAF C35 H34  sing N N 138 
A1BAF C40 H36  sing N N 139 
A1BAF C42 H38  sing N N 140 
A1BAF C44 H39  sing N N 141 
A1BAF C46 H40  sing N N 142 
A1BAF C47 H41  sing N N 143 
A1BAF C50 H44  sing N N 144 
A1BAF C50 H43  sing N N 145 
A1BAF C51 H46  sing N N 146 
A1BAF C51 H45  sing N N 147 
A1BAF C52 H47  sing N N 148 
A1BAF C52 H48  sing N N 149 
A1BAF C53 H49  sing N N 150 
A1BAF C53 H50  sing N N 151 
A1BAF C54 H52  sing N N 152 
A1BAF C54 H51  sing N N 153 
A1BAF C55 H53  sing N N 154 
A1BAF C55 H54  sing N N 155 
A1BAF C56 H56  sing N N 156 
A1BAF C56 H55  sing N N 157 
A1BAF C57 H58  sing N N 158 
A1BAF C57 H57  sing N N 159 
A1BAF C58 H59  sing N N 160 
A1BAF C58 H60  sing N N 161 
A1BAF C59 H61  sing N N 162 
A1BAF C59 H62  sing N N 163 
A1BAF C60 H64  sing N N 164 
A1BAF C60 H63  sing N N 165 
A1BAF C61 H65  sing N N 166 
A1BAF C61 H66  sing N N 167 
A1BAF C62 H68  sing N N 168 
A1BAF C62 H67  sing N N 169 
A1BAF C63 H70  sing N N 170 
A1BAF C63 H69  sing N N 171 
A1BAF C64 H72  sing N N 172 
A1BAF C64 H71  sing N N 173 
A1BAF C65 H74  sing N N 174 
A1BAF C65 H73  sing N N 175 
A1BAF C66 H76  sing N N 176 
A1BAF C66 H75  sing N N 177 
A1BAF C67 H78  sing N N 178 
A1BAF C67 H77  sing N N 179 
A1BAF C68 H79  sing N N 180 
A1BAF C68 H80  sing N N 181 
A1BAF C69 H82  sing N N 182 
A1BAF C69 H81  sing N N 183 
A1BAF N03 H19  sing N N 184 
A1BAF N04 H23  sing N N 185 
A1BAF N05 H30  sing N N 186 
A1BAF N05 H31  sing N N 187 
A1BAF N06 H35  sing N N 188 
A1BAF N07 H37  sing N N 189 
A1BAF N08 H42  sing N N 190 
A1BAF N09 H83  sing N N 191 
ALA   N   CA   sing N N 192 
ALA   N   H    sing N N 193 
ALA   N   H2   sing N N 194 
ALA   CA  C    sing N N 195 
ALA   CA  CB   sing N N 196 
ALA   CA  HA   sing N N 197 
ALA   C   O    doub N N 198 
ALA   C   OXT  sing N N 199 
ALA   CB  HB1  sing N N 200 
ALA   CB  HB2  sing N N 201 
ALA   CB  HB3  sing N N 202 
ALA   OXT HXT  sing N N 203 
ARG   N   CA   sing N N 204 
ARG   N   H    sing N N 205 
ARG   N   H2   sing N N 206 
ARG   CA  C    sing N N 207 
ARG   CA  CB   sing N N 208 
ARG   CA  HA   sing N N 209 
ARG   C   O    doub N N 210 
ARG   C   OXT  sing N N 211 
ARG   CB  CG   sing N N 212 
ARG   CB  HB2  sing N N 213 
ARG   CB  HB3  sing N N 214 
ARG   CG  CD   sing N N 215 
ARG   CG  HG2  sing N N 216 
ARG   CG  HG3  sing N N 217 
ARG   CD  NE   sing N N 218 
ARG   CD  HD2  sing N N 219 
ARG   CD  HD3  sing N N 220 
ARG   NE  CZ   sing N N 221 
ARG   NE  HE   sing N N 222 
ARG   CZ  NH1  sing N N 223 
ARG   CZ  NH2  doub N N 224 
ARG   NH1 HH11 sing N N 225 
ARG   NH1 HH12 sing N N 226 
ARG   NH2 HH21 sing N N 227 
ARG   NH2 HH22 sing N N 228 
ARG   OXT HXT  sing N N 229 
ASN   N   CA   sing N N 230 
ASN   N   H    sing N N 231 
ASN   N   H2   sing N N 232 
ASN   CA  C    sing N N 233 
ASN   CA  CB   sing N N 234 
ASN   CA  HA   sing N N 235 
ASN   C   O    doub N N 236 
ASN   C   OXT  sing N N 237 
ASN   CB  CG   sing N N 238 
ASN   CB  HB2  sing N N 239 
ASN   CB  HB3  sing N N 240 
ASN   CG  OD1  doub N N 241 
ASN   CG  ND2  sing N N 242 
ASN   ND2 HD21 sing N N 243 
ASN   ND2 HD22 sing N N 244 
ASN   OXT HXT  sing N N 245 
ASP   N   CA   sing N N 246 
ASP   N   H    sing N N 247 
ASP   N   H2   sing N N 248 
ASP   CA  C    sing N N 249 
ASP   CA  CB   sing N N 250 
ASP   CA  HA   sing N N 251 
ASP   C   O    doub N N 252 
ASP   C   OXT  sing N N 253 
ASP   CB  CG   sing N N 254 
ASP   CB  HB2  sing N N 255 
ASP   CB  HB3  sing N N 256 
ASP   CG  OD1  doub N N 257 
ASP   CG  OD2  sing N N 258 
ASP   OD2 HD2  sing N N 259 
ASP   OXT HXT  sing N N 260 
CYS   N   CA   sing N N 261 
CYS   N   H    sing N N 262 
CYS   N   H2   sing N N 263 
CYS   CA  C    sing N N 264 
CYS   CA  CB   sing N N 265 
CYS   CA  HA   sing N N 266 
CYS   C   O    doub N N 267 
CYS   C   OXT  sing N N 268 
CYS   CB  SG   sing N N 269 
CYS   CB  HB2  sing N N 270 
CYS   CB  HB3  sing N N 271 
CYS   SG  HG   sing N N 272 
CYS   OXT HXT  sing N N 273 
GLN   N   CA   sing N N 274 
GLN   N   H    sing N N 275 
GLN   N   H2   sing N N 276 
GLN   CA  C    sing N N 277 
GLN   CA  CB   sing N N 278 
GLN   CA  HA   sing N N 279 
GLN   C   O    doub N N 280 
GLN   C   OXT  sing N N 281 
GLN   CB  CG   sing N N 282 
GLN   CB  HB2  sing N N 283 
GLN   CB  HB3  sing N N 284 
GLN   CG  CD   sing N N 285 
GLN   CG  HG2  sing N N 286 
GLN   CG  HG3  sing N N 287 
GLN   CD  OE1  doub N N 288 
GLN   CD  NE2  sing N N 289 
GLN   NE2 HE21 sing N N 290 
GLN   NE2 HE22 sing N N 291 
GLN   OXT HXT  sing N N 292 
GLU   N   CA   sing N N 293 
GLU   N   H    sing N N 294 
GLU   N   H2   sing N N 295 
GLU   CA  C    sing N N 296 
GLU   CA  CB   sing N N 297 
GLU   CA  HA   sing N N 298 
GLU   C   O    doub N N 299 
GLU   C   OXT  sing N N 300 
GLU   CB  CG   sing N N 301 
GLU   CB  HB2  sing N N 302 
GLU   CB  HB3  sing N N 303 
GLU   CG  CD   sing N N 304 
GLU   CG  HG2  sing N N 305 
GLU   CG  HG3  sing N N 306 
GLU   CD  OE1  doub N N 307 
GLU   CD  OE2  sing N N 308 
GLU   OE2 HE2  sing N N 309 
GLU   OXT HXT  sing N N 310 
GLY   N   CA   sing N N 311 
GLY   N   H    sing N N 312 
GLY   N   H2   sing N N 313 
GLY   CA  C    sing N N 314 
GLY   CA  HA2  sing N N 315 
GLY   CA  HA3  sing N N 316 
GLY   C   O    doub N N 317 
GLY   C   OXT  sing N N 318 
GLY   OXT HXT  sing N N 319 
HIS   N   CA   sing N N 320 
HIS   N   H    sing N N 321 
HIS   N   H2   sing N N 322 
HIS   CA  C    sing N N 323 
HIS   CA  CB   sing N N 324 
HIS   CA  HA   sing N N 325 
HIS   C   O    doub N N 326 
HIS   C   OXT  sing N N 327 
HIS   CB  CG   sing N N 328 
HIS   CB  HB2  sing N N 329 
HIS   CB  HB3  sing N N 330 
HIS   CG  ND1  sing Y N 331 
HIS   CG  CD2  doub Y N 332 
HIS   ND1 CE1  doub Y N 333 
HIS   ND1 HD1  sing N N 334 
HIS   CD2 NE2  sing Y N 335 
HIS   CD2 HD2  sing N N 336 
HIS   CE1 NE2  sing Y N 337 
HIS   CE1 HE1  sing N N 338 
HIS   NE2 HE2  sing N N 339 
HIS   OXT HXT  sing N N 340 
HOH   O   H1   sing N N 341 
HOH   O   H2   sing N N 342 
ILE   N   CA   sing N N 343 
ILE   N   H    sing N N 344 
ILE   N   H2   sing N N 345 
ILE   CA  C    sing N N 346 
ILE   CA  CB   sing N N 347 
ILE   CA  HA   sing N N 348 
ILE   C   O    doub N N 349 
ILE   C   OXT  sing N N 350 
ILE   CB  CG1  sing N N 351 
ILE   CB  CG2  sing N N 352 
ILE   CB  HB   sing N N 353 
ILE   CG1 CD1  sing N N 354 
ILE   CG1 HG12 sing N N 355 
ILE   CG1 HG13 sing N N 356 
ILE   CG2 HG21 sing N N 357 
ILE   CG2 HG22 sing N N 358 
ILE   CG2 HG23 sing N N 359 
ILE   CD1 HD11 sing N N 360 
ILE   CD1 HD12 sing N N 361 
ILE   CD1 HD13 sing N N 362 
ILE   OXT HXT  sing N N 363 
LEU   N   CA   sing N N 364 
LEU   N   H    sing N N 365 
LEU   N   H2   sing N N 366 
LEU   CA  C    sing N N 367 
LEU   CA  CB   sing N N 368 
LEU   CA  HA   sing N N 369 
LEU   C   O    doub N N 370 
LEU   C   OXT  sing N N 371 
LEU   CB  CG   sing N N 372 
LEU   CB  HB2  sing N N 373 
LEU   CB  HB3  sing N N 374 
LEU   CG  CD1  sing N N 375 
LEU   CG  CD2  sing N N 376 
LEU   CG  HG   sing N N 377 
LEU   CD1 HD11 sing N N 378 
LEU   CD1 HD12 sing N N 379 
LEU   CD1 HD13 sing N N 380 
LEU   CD2 HD21 sing N N 381 
LEU   CD2 HD22 sing N N 382 
LEU   CD2 HD23 sing N N 383 
LEU   OXT HXT  sing N N 384 
LYS   N   CA   sing N N 385 
LYS   N   H    sing N N 386 
LYS   N   H2   sing N N 387 
LYS   CA  C    sing N N 388 
LYS   CA  CB   sing N N 389 
LYS   CA  HA   sing N N 390 
LYS   C   O    doub N N 391 
LYS   C   OXT  sing N N 392 
LYS   CB  CG   sing N N 393 
LYS   CB  HB2  sing N N 394 
LYS   CB  HB3  sing N N 395 
LYS   CG  CD   sing N N 396 
LYS   CG  HG2  sing N N 397 
LYS   CG  HG3  sing N N 398 
LYS   CD  CE   sing N N 399 
LYS   CD  HD2  sing N N 400 
LYS   CD  HD3  sing N N 401 
LYS   CE  NZ   sing N N 402 
LYS   CE  HE2  sing N N 403 
LYS   CE  HE3  sing N N 404 
LYS   NZ  HZ1  sing N N 405 
LYS   NZ  HZ2  sing N N 406 
LYS   NZ  HZ3  sing N N 407 
LYS   OXT HXT  sing N N 408 
MET   N   CA   sing N N 409 
MET   N   H    sing N N 410 
MET   N   H2   sing N N 411 
MET   CA  C    sing N N 412 
MET   CA  CB   sing N N 413 
MET   CA  HA   sing N N 414 
MET   C   O    doub N N 415 
MET   C   OXT  sing N N 416 
MET   CB  CG   sing N N 417 
MET   CB  HB2  sing N N 418 
MET   CB  HB3  sing N N 419 
MET   CG  SD   sing N N 420 
MET   CG  HG2  sing N N 421 
MET   CG  HG3  sing N N 422 
MET   SD  CE   sing N N 423 
MET   CE  HE1  sing N N 424 
MET   CE  HE2  sing N N 425 
MET   CE  HE3  sing N N 426 
MET   OXT HXT  sing N N 427 
PHE   N   CA   sing N N 428 
PHE   N   H    sing N N 429 
PHE   N   H2   sing N N 430 
PHE   CA  C    sing N N 431 
PHE   CA  CB   sing N N 432 
PHE   CA  HA   sing N N 433 
PHE   C   O    doub N N 434 
PHE   C   OXT  sing N N 435 
PHE   CB  CG   sing N N 436 
PHE   CB  HB2  sing N N 437 
PHE   CB  HB3  sing N N 438 
PHE   CG  CD1  doub Y N 439 
PHE   CG  CD2  sing Y N 440 
PHE   CD1 CE1  sing Y N 441 
PHE   CD1 HD1  sing N N 442 
PHE   CD2 CE2  doub Y N 443 
PHE   CD2 HD2  sing N N 444 
PHE   CE1 CZ   doub Y N 445 
PHE   CE1 HE1  sing N N 446 
PHE   CE2 CZ   sing Y N 447 
PHE   CE2 HE2  sing N N 448 
PHE   CZ  HZ   sing N N 449 
PHE   OXT HXT  sing N N 450 
PRO   N   CA   sing N N 451 
PRO   N   CD   sing N N 452 
PRO   N   H    sing N N 453 
PRO   CA  C    sing N N 454 
PRO   CA  CB   sing N N 455 
PRO   CA  HA   sing N N 456 
PRO   C   O    doub N N 457 
PRO   C   OXT  sing N N 458 
PRO   CB  CG   sing N N 459 
PRO   CB  HB2  sing N N 460 
PRO   CB  HB3  sing N N 461 
PRO   CG  CD   sing N N 462 
PRO   CG  HG2  sing N N 463 
PRO   CG  HG3  sing N N 464 
PRO   CD  HD2  sing N N 465 
PRO   CD  HD3  sing N N 466 
PRO   OXT HXT  sing N N 467 
SER   N   CA   sing N N 468 
SER   N   H    sing N N 469 
SER   N   H2   sing N N 470 
SER   CA  C    sing N N 471 
SER   CA  CB   sing N N 472 
SER   CA  HA   sing N N 473 
SER   C   O    doub N N 474 
SER   C   OXT  sing N N 475 
SER   CB  OG   sing N N 476 
SER   CB  HB2  sing N N 477 
SER   CB  HB3  sing N N 478 
SER   OG  HG   sing N N 479 
SER   OXT HXT  sing N N 480 
THR   N   CA   sing N N 481 
THR   N   H    sing N N 482 
THR   N   H2   sing N N 483 
THR   CA  C    sing N N 484 
THR   CA  CB   sing N N 485 
THR   CA  HA   sing N N 486 
THR   C   O    doub N N 487 
THR   C   OXT  sing N N 488 
THR   CB  OG1  sing N N 489 
THR   CB  CG2  sing N N 490 
THR   CB  HB   sing N N 491 
THR   OG1 HG1  sing N N 492 
THR   CG2 HG21 sing N N 493 
THR   CG2 HG22 sing N N 494 
THR   CG2 HG23 sing N N 495 
THR   OXT HXT  sing N N 496 
TRP   N   CA   sing N N 497 
TRP   N   H    sing N N 498 
TRP   N   H2   sing N N 499 
TRP   CA  C    sing N N 500 
TRP   CA  CB   sing N N 501 
TRP   CA  HA   sing N N 502 
TRP   C   O    doub N N 503 
TRP   C   OXT  sing N N 504 
TRP   CB  CG   sing N N 505 
TRP   CB  HB2  sing N N 506 
TRP   CB  HB3  sing N N 507 
TRP   CG  CD1  doub Y N 508 
TRP   CG  CD2  sing Y N 509 
TRP   CD1 NE1  sing Y N 510 
TRP   CD1 HD1  sing N N 511 
TRP   CD2 CE2  doub Y N 512 
TRP   CD2 CE3  sing Y N 513 
TRP   NE1 CE2  sing Y N 514 
TRP   NE1 HE1  sing N N 515 
TRP   CE2 CZ2  sing Y N 516 
TRP   CE3 CZ3  doub Y N 517 
TRP   CE3 HE3  sing N N 518 
TRP   CZ2 CH2  doub Y N 519 
TRP   CZ2 HZ2  sing N N 520 
TRP   CZ3 CH2  sing Y N 521 
TRP   CZ3 HZ3  sing N N 522 
TRP   CH2 HH2  sing N N 523 
TRP   OXT HXT  sing N N 524 
TYR   N   CA   sing N N 525 
TYR   N   H    sing N N 526 
TYR   N   H2   sing N N 527 
TYR   CA  C    sing N N 528 
TYR   CA  CB   sing N N 529 
TYR   CA  HA   sing N N 530 
TYR   C   O    doub N N 531 
TYR   C   OXT  sing N N 532 
TYR   CB  CG   sing N N 533 
TYR   CB  HB2  sing N N 534 
TYR   CB  HB3  sing N N 535 
TYR   CG  CD1  doub Y N 536 
TYR   CG  CD2  sing Y N 537 
TYR   CD1 CE1  sing Y N 538 
TYR   CD1 HD1  sing N N 539 
TYR   CD2 CE2  doub Y N 540 
TYR   CD2 HD2  sing N N 541 
TYR   CE1 CZ   doub Y N 542 
TYR   CE1 HE1  sing N N 543 
TYR   CE2 CZ   sing Y N 544 
TYR   CE2 HE2  sing N N 545 
TYR   CZ  OH   sing N N 546 
TYR   OH  HH   sing N N 547 
TYR   OXT HXT  sing N N 548 
VAL   N   CA   sing N N 549 
VAL   N   H    sing N N 550 
VAL   N   H2   sing N N 551 
VAL   CA  C    sing N N 552 
VAL   CA  CB   sing N N 553 
VAL   CA  HA   sing N N 554 
VAL   C   O    doub N N 555 
VAL   C   OXT  sing N N 556 
VAL   CB  CG1  sing N N 557 
VAL   CB  CG2  sing N N 558 
VAL   CB  HB   sing N N 559 
VAL   CG1 HG11 sing N N 560 
VAL   CG1 HG12 sing N N 561 
VAL   CG1 HG13 sing N N 562 
VAL   CG2 HG21 sing N N 563 
VAL   CG2 HG22 sing N N 564 
VAL   CG2 HG23 sing N N 565 
VAL   OXT HXT  sing N N 566 
# 
_pdbx_audit_support.funding_organization   'Ontario Institute for Cancer Research' 
_pdbx_audit_support.country                Canada 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_initial_refinement_model.id 
_pdbx_initial_refinement_model.entity_id_list 
_pdbx_initial_refinement_model.type 
_pdbx_initial_refinement_model.source_name 
_pdbx_initial_refinement_model.accession_code 
_pdbx_initial_refinement_model.details 
1 ? 'experimental model' PDB 8F8E ? 
2 ? 'experimental model' PDB 2GNQ ? 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9DLW 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.012465 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011922 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.007606 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL ? ? 9.50761 7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
F  ? ? 4.90428 4.07044 ? ? 12.99538 1.63651  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H  ? ? 0.51345 0.48472 ? ? 24.73122 6.32584  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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    . PHE   A 1 28  ? -4.54957  -21.79796 -42.88138 1.000 29.85377  ? 1080 PHE   B N    1 
ATOM   2    C  CA   . PHE   A 1 28  ? -3.80739  -22.49492 -41.83248 1.000 38.98909  ? 1080 PHE   B CA   1 
ATOM   3    C  C    . PHE   A 1 28  ? -4.49422  -23.79001 -41.40246 1.000 31.36806  ? 1080 PHE   B C    1 
ATOM   4    O  O    . PHE   A 1 28  ? -5.24512  -23.82412 -40.42238 1.000 33.06317  ? 1080 PHE   B O    1 
ATOM   5    C  CB   . PHE   A 1 28  ? -3.60236  -21.57595 -40.62747 1.000 32.35917  ? 1080 PHE   B CB   1 
ATOM   6    C  CG   . PHE   A 1 28  ? -2.83051  -20.33786 -40.95750 1.000 34.73958  ? 1080 PHE   B CG   1 
ATOM   7    C  CD1  . PHE   A 1 28  ? -1.45152  -20.37172 -41.04065 1.000 32.03239  ? 1080 PHE   B CD1  1 
ATOM   8    C  CD2  . PHE   A 1 28  ? -3.48366  -19.14791 -41.21739 1.000 34.91901  ? 1080 PHE   B CD2  1 
ATOM   9    C  CE1  . PHE   A 1 28  ? -0.73966  -19.23964 -41.36368 1.000 31.54886  ? 1080 PHE   B CE1  1 
ATOM   10   C  CE2  . PHE   A 1 28  ? -2.77780  -18.00883 -41.53743 1.000 33.46810  ? 1080 PHE   B CE2  1 
ATOM   11   C  CZ   . PHE   A 1 28  ? -1.40480  -18.05370 -41.61357 1.000 35.61469  ? 1080 PHE   B CZ   1 
ATOM   12   N  N    . ARG   A 1 29  ? -4.20219  -24.85095 -42.13853 1.000 31.43530  ? 1081 ARG   B N    1 
ATOM   13   C  CA   . ARG   A 1 29  ? -4.77603  -26.16502 -41.87052 1.000 30.81100  ? 1081 ARG   B CA   1 
ATOM   14   C  C    . ARG   A 1 29  ? -3.97485  -26.87298 -40.78162 1.000 26.17056  ? 1081 ARG   B C    1 
ATOM   15   O  O    . ARG   A 1 29  ? -2.75585  -27.01585 -40.91175 1.000 26.88494  ? 1081 ARG   B O    1 
ATOM   16   C  CB   . ARG   A 1 29  ? -4.78608  -26.99797 -43.14854 1.000 28.78276  ? 1081 ARG   B CB   1 
ATOM   17   C  CG   . ARG   A 1 29  ? -5.49094  -28.34605 -43.02752 1.000 39.75466  ? 1081 ARG   B CG   1 
ATOM   18   C  CD   . ARG   A 1 29  ? -5.69102  -28.98502 -44.40352 1.000 38.88936  ? 1081 ARG   B CD   1 
ATOM   19   N  NE   . ARG   A 1 29  ? -4.41505  -29.31387 -45.03167 1.000 44.31862  ? 1081 ARG   B NE   1 
ATOM   20   C  CZ   . ARG   A 1 29  ? -3.78392  -30.47581 -44.90377 1.000 57.80569  ? 1081 ARG   B CZ   1 
ATOM   21   N  NH1  . ARG   A 1 29  ? -4.30175  -31.47189 -44.19876 1.000 55.71962  ? 1081 ARG   B NH1  1 
ATOM   22   N  NH2  . ARG   A 1 29  ? -2.60297  -30.64367 -45.49690 1.000 42.54025  ? 1081 ARG   B NH2  1 
ATOM   23   N  N    . PRO   A 1 30  ? -4.61470  -27.31508 -39.69957 1.000 24.94620  ? 1082 PRO   B N    1 
ATOM   24   C  CA   . PRO   A 1 30  ? -3.89252  -28.08705 -38.67468 1.000 22.79330  ? 1082 PRO   B CA   1 
ATOM   25   C  C    . PRO   A 1 30  ? -3.29246  -29.35197 -39.26978 1.000 18.21318  ? 1082 PRO   B C    1 
ATOM   26   O  O    . PRO   A 1 30  ? -3.96246  -30.09601 -39.98974 1.000 24.80606  ? 1082 PRO   B O    1 
ATOM   27   C  CB   . PRO   A 1 30  ? -4.97538  -28.42019 -37.64058 1.000 27.04250  ? 1082 PRO   B CB   1 
ATOM   28   C  CG   . PRO   A 1 30  ? -6.10950  -27.49129 -37.92843 1.000 28.11893  ? 1082 PRO   B CG   1 
ATOM   29   C  CD   . PRO   A 1 30  ? -6.04268  -27.15323 -39.38842 1.000 23.90586  ? 1082 PRO   B CD   1 
ATOM   30   N  N    . ILE   A 1 31  ? -2.02140  -29.59285 -38.95692 1.000 17.89480  ? 1083 ILE   B N    1 
ATOM   31   C  CA   . ILE   A 1 31  ? -1.27134  -30.72576 -39.48404 1.000 12.37909  ? 1083 ILE   B CA   1 
ATOM   32   C  C    . ILE   A 1 31  ? -0.88813  -31.70876 -38.38412 1.000 22.54069  ? 1083 ILE   B C    1 
ATOM   33   O  O    . ILE   A 1 31  ? -0.92403  -32.92476 -38.58616 1.000 20.77322  ? 1083 ILE   B O    1 
ATOM   34   C  CB   . ILE   A 1 31  ? -0.01147  -30.22861 -40.23115 1.000 21.18873  ? 1083 ILE   B CB   1 
ATOM   35   C  CG1  . ILE   A 1 31  ? -0.39567  -29.54860 -41.54409 1.000 36.15006  ? 1083 ILE   B CG1  1 
ATOM   36   C  CG2  . ILE   A 1 31  ? 0.98162   -31.36850 -40.46129 1.000 20.48105  ? 1083 ILE   B CG2  1 
ATOM   37   C  CD1  . ILE   A 1 31  ? -1.38668  -30.33867 -42.36901 1.000 28.12855  ? 1083 ILE   B CD1  1 
ATOM   38   N  N    . SER   A 1 32  ? -0.49706  -31.19777 -37.22014 1.000 20.08897  ? 1084 SER   B N    1 
ATOM   39   C  CA   . SER   A 1 32  ? 0.01213   -32.03375 -36.14722 1.000 19.80201  ? 1084 SER   B CA   1 
ATOM   40   C  C    . SER   A 1 32  ? -0.18481  -31.30282 -34.82817 1.000 21.76184  ? 1084 SER   B C    1 
ATOM   41   O  O    . SER   A 1 32  ? -0.20692  -30.06583 -34.78213 1.000 16.96216  ? 1084 SER   B O    1 
ATOM   42   C  CB   . SER   A 1 32  ? 1.49214   -32.36360 -36.36138 1.000 15.39685  ? 1084 SER   B CB   1 
ATOM   43   O  OG   . SER   A 1 32  ? 1.95133   -33.28859 -35.40146 1.000 18.78565  ? 1084 SER   B OG   1 
ATOM   44   N  N    . VAL   A 1 33  ? -0.32562  -32.07887 -33.76119 1.000 17.87388  ? 1085 VAL   B N    1 
ATOM   45   C  CA   . VAL   A 1 33  ? -0.36554  -31.53693 -32.40916 1.000 14.06851  ? 1085 VAL   B CA   1 
ATOM   46   C  C    . VAL   A 1 33  ? 0.37865   -32.50389 -31.50327 1.000 18.20392  ? 1085 VAL   B C    1 
ATOM   47   O  O    . VAL   A 1 33  ? 0.36575   -33.71988 -31.71932 1.000 16.96780  ? 1085 VAL   B O    1 
ATOM   48   C  CB   . VAL   A 1 33  ? -1.81151  -31.32609 -31.91401 1.000 18.61044  ? 1085 VAL   B CB   1 
ATOM   49   C  CG1  . VAL   A 1 33  ? -2.49035  -32.67516 -31.70099 1.000 17.27988  ? 1085 VAL   B CG1  1 
ATOM   50   C  CG2  . VAL   A 1 33  ? -1.82645  -30.50814 -30.62498 1.000 17.12471  ? 1085 VAL   B CG2  1 
ATOM   51   N  N    . PHE   A 1 34  ? 1.03670   -31.95686 -30.48532 1.000 16.04350  ? 1086 PHE   B N    1 
ATOM   52   C  CA   . PHE   A 1 34  ? 1.66489   -32.80983 -29.48842 1.000 17.29811  ? 1086 PHE   B CA   1 
ATOM   53   C  C    . PHE   A 1 34  ? 1.90894   -32.00786 -28.22241 1.000 18.37870  ? 1086 PHE   B C    1 
ATOM   54   O  O    . PHE   A 1 34  ? 1.96182   -30.77285 -28.23437 1.000 18.37953  ? 1086 PHE   B O    1 
ATOM   55   C  CB   . PHE   A 1 34  ? 2.96390   -33.44469 -30.00157 1.000 13.59460  ? 1086 PHE   B CB   1 
ATOM   56   C  CG   . PHE   A 1 34  ? 4.00876   -32.45957 -30.45065 1.000 12.38813  ? 1086 PHE   B CG   1 
ATOM   57   C  CD1  . PHE   A 1 34  ? 4.02158   -31.98652 -31.74763 1.000 17.09287  ? 1086 PHE   B CD1  1 
ATOM   58   C  CD2  . PHE   A 1 34  ? 5.01680   -32.04950 -29.57973 1.000 16.26416  ? 1086 PHE   B CD2  1 
ATOM   59   C  CE1  . PHE   A 1 34  ? 5.00544   -31.09541 -32.17270 1.000 17.57457  ? 1086 PHE   B CE1  1 
ATOM   60   C  CE2  . PHE   A 1 34  ? 5.99968   -31.16339 -29.98280 1.000 14.03810  ? 1086 PHE   B CE2  1 
ATOM   61   C  CZ   . PHE   A 1 34  ? 5.99649   -30.68134 -31.29278 1.000 15.59861  ? 1086 PHE   B CZ   1 
ATOM   62   N  N    . ARG   A 1 35  ? 2.02412   -32.73588 -27.12145 1.000 17.03618  ? 1087 ARG   B N    1 
ATOM   63   C  CA   . ARG   A 1 35  ? 2.31120   -32.15690 -25.82246 1.000 18.36521  ? 1087 ARG   B CA   1 
ATOM   64   C  C    . ARG   A 1 35  ? 3.66030   -32.67879 -25.35262 1.000 16.81189  ? 1087 ARG   B C    1 
ATOM   65   O  O    . ARG   A 1 35  ? 4.23833   -33.58771 -25.95771 1.000 19.23320  ? 1087 ARG   B O    1 
ATOM   66   C  CB   . ARG   A 1 35  ? 1.19033   -32.47305 -24.81936 1.000 21.78085  ? 1087 ARG   B CB   1 
ATOM   67   C  CG   . ARG   A 1 35  ? 1.00251   -33.94308 -24.51339 1.000 21.53509  ? 1087 ARG   B CG   1 
ATOM   68   C  CD   . ARG   A 1 35  ? -0.32239  -34.19024 -23.77226 1.000 20.44040  ? 1087 ARG   B CD   1 
ATOM   69   N  NE   . ARG   A 1 35  ? -0.45634  -33.38229 -22.56522 1.000 19.34217  ? 1087 ARG   B NE   1 
ATOM   70   C  CZ   . ARG   A 1 35  ? 0.25579   -33.57526 -21.46630 1.000 27.99192  ? 1087 ARG   B CZ   1 
ATOM   71   N  NH1  . ARG   A 1 35  ? 1.18189   -34.52317 -21.40843 1.000 38.47713  ? 1087 ARG   B NH1  1 
ATOM   72   N  NH2  . ARG   A 1 35  ? 0.05282   -32.78732 -20.40925 1.000 19.38462  ? 1087 ARG   B NH2  1 
ATOM   73   N  N    . GLU   A 1 36  ? 4.18435   -32.07678 -24.28665 1.000 16.78507  ? 1088 GLU   B N    1 
ATOM   74   C  CA   . GLU   A 1 36  ? 5.49844   -32.47466 -23.78980 1.000 21.99419  ? 1088 GLU   B CA   1 
ATOM   75   C  C    . GLU   A 1 36  ? 5.45064   -33.88269 -23.20284 1.000 20.02155  ? 1088 GLU   B C    1 
ATOM   76   O  O    . GLU   A 1 36  ? 4.63476   -34.16880 -22.32277 1.000 21.19732  ? 1088 GLU   B O    1 
ATOM   77   C  CB   . GLU   A 1 36  ? 6.00745   -31.49965 -22.73082 1.000 21.43743  ? 1088 GLU   B CB   1 
ATOM   78   C  CG   . GLU   A 1 36  ? 7.35655   -31.92254 -22.15997 1.000 17.18100  ? 1088 GLU   B CG   1 
ATOM   79   C  CD   . GLU   A 1 36  ? 7.94955   -30.90052 -21.19599 1.000 23.76349  ? 1088 GLU   B CD   1 
ATOM   80   O  OE1  . GLU   A 1 36  ? 7.19852   -30.02461 -20.69088 1.000 17.92677  ? 1088 GLU   B OE1  1 
ATOM   81   O  OE2  . GLU   A 1 36  ? 9.17758   -30.97741 -20.95412 1.000 20.72924  ? 1088 GLU   B OE2  1 
ATOM   82   N  N    . ALA   A 1 37  ? 6.35468   -34.74158 -23.66997 1.000 19.40654  ? 1089 ALA   B N    1 
ATOM   83   C  CA   . ALA   A 1 37  ? 6.43786   -36.11359 -23.18903 1.000 19.31074  ? 1089 ALA   B CA   1 
ATOM   84   C  C    . ALA   A 1 37  ? 6.90701   -36.15960 -21.74008 1.000 30.18731  ? 1089 ALA   B C    1 
ATOM   85   O  O    . ALA   A 1 37  ? 7.64097   -35.28655 -21.27512 1.000 30.95728  ? 1089 ALA   B O    1 
ATOM   86   C  CB   . ALA   A 1 37  ? 7.39685   -36.92647 -24.06015 1.000 19.73037  ? 1089 ALA   B CB   1 
ATOM   87   N  N    . ASN   A 1 38  ? 6.47119   -37.19967 -21.02607 1.000 41.53592  ? 1090 ASN   B N    1 
ATOM   88   C  CA   . ASN   A 1 38  ? 6.90035   -37.46468 -19.65612 1.000 42.90747  ? 1090 ASN   B CA   1 
ATOM   89   C  C    . ASN   A 1 38  ? 6.09938   -36.66079 -18.63401 1.000 50.23133  ? 1090 ASN   B C    1 
ATOM   90   O  O    . ASN   A 1 38  ? 5.72554   -37.17887 -17.57599 1.000 58.26984  ? 1090 ASN   B O    1 
ATOM   91   C  CB   . ASN   A 1 38  ? 8.39534   -37.16054 -19.48927 1.000 46.25563  ? 1090 ASN   B CB   1 
ATOM   92   C  CG   . ASN   A 1 38  ? 9.25329   -37.79641 -20.58038 1.000 52.09290  ? 1090 ASN   B CG   1 
ATOM   93   O  OD1  . ASN   A 1 38  ? 9.01736   -38.93842 -20.98839 1.000 47.20834  ? 1090 ASN   B OD1  1 
ATOM   94   N  ND2  . ASN   A 1 38  ? 10.25517  -37.05230 -21.05845 1.000 38.04596  ? 1090 ASN   B ND2  1 
ATOM   95   N  N    . GLU   A 1 39  ? 5.81922   -35.40081 -18.94994 1.000 47.52561  ? 1091 GLU   B N    1 
ATOM   96   C  CA   . GLU   A 1 39  ? 5.45923   -34.40988 -17.94486 1.000 49.85145  ? 1091 GLU   B CA   1 
ATOM   97   C  C    . GLU   A 1 39  ? 3.95925   -34.38404 -17.69671 1.000 49.23481  ? 1091 GLU   B C    1 
ATOM   98   O  O    . GLU   A 1 39  ? 3.16315   -34.34408 -18.64263 1.000 43.51248  ? 1091 GLU   B O    1 
ATOM   99   C  CB   . GLU   A 1 39  ? 5.94605   -33.02382 -18.36886 1.000 32.88186  ? 1091 GLU   B CB   1 
ATOM   100  C  CG   . GLU   A 1 39  ? 7.46303   -32.91266 -18.45002 1.000 45.73029  ? 1091 GLU   B CG   1 
ATOM   101  C  CD   . GLU   A 1 39  ? 8.13919   -33.08465 -17.10509 1.000 50.29918  ? 1091 GLU   B CD   1 
ATOM   102  O  OE1  . GLU   A 1 39  ? 7.49626   -32.76675 -16.07901 1.000 53.13295  ? 1091 GLU   B OE1  1 
ATOM   103  O  OE2  . GLU   A 1 39  ? 9.31023   -33.53353 -17.08223 1.000 43.04102  ? 1091 GLU   B OE2  1 
ATOM   104  N  N    . ASP   A 1 40  ? 3.58739   -34.38612 -16.41267 1.000 49.83628  ? 1092 ASP   B N    1 
ATOM   105  C  CA   . ASP   A 1 40  ? 2.18641   -34.26827 -16.02152 1.000 51.21518  ? 1092 ASP   B CA   1 
ATOM   106  C  C    . ASP   A 1 40  ? 1.54323   -33.03231 -16.63841 1.000 38.89852  ? 1092 ASP   B C    1 
ATOM   107  O  O    . ASP   A 1 40  ? 0.46917   -33.11039 -17.24631 1.000 36.77154  ? 1092 ASP   B O    1 
ATOM   108  C  CB   . ASP   A 1 40  ? 2.08057   -34.22134 -14.49551 1.000 56.25864  ? 1092 ASP   B CB   1 
ATOM   109  C  CG   . ASP   A 1 40  ? 1.56475   -35.51541 -13.90350 1.000 77.35696  ? 1092 ASP   B CG   1 
ATOM   110  O  OD1  . ASP   A 1 40  ? 0.68675   -36.14847 -14.53344 1.000 79.46671  ? 1092 ASP   B OD1  1 
ATOM   111  O  OD2  . ASP   A 1 40  ? 2.03390   -35.89240 -12.80557 1.000 73.88190  ? 1092 ASP   B OD2  1 
ATOM   112  N  N    . GLU   A 1 41  ? 2.18113   -31.87625 -16.46844 1.000 38.44747  ? 1093 GLU   B N    1 
ATOM   113  C  CA   . GLU   A 1 41  ? 1.72395   -30.62228 -17.05434 1.000 33.07378  ? 1093 GLU   B CA   1 
ATOM   114  C  C    . GLU   A 1 41  ? 2.71980   -30.21814 -18.13143 1.000 25.62268  ? 1093 GLU   B C    1 
ATOM   115  O  O    . GLU   A 1 41  ? 3.90981   -30.05604 -17.84455 1.000 26.80091  ? 1093 GLU   B O    1 
ATOM   116  C  CB   . GLU   A 1 41  ? 1.59095   -29.52733 -15.99729 1.000 33.71766  ? 1093 GLU   B CB   1 
ATOM   117  C  CG   . GLU   A 1 41  ? 0.87112   -29.96545 -14.73423 1.000 35.38678  ? 1093 GLU   B CG   1 
ATOM   118  C  CD   . GLU   A 1 41  ? -0.01892  -28.87255 -14.16510 1.000 62.29435  ? 1093 GLU   B CD   1 
ATOM   119  O  OE1  . GLU   A 1 41  ? -0.96704  -28.44062 -14.86699 1.000 55.49164  ? 1093 GLU   B OE1  1 
ATOM   120  O  OE2  . GLU   A 1 41  ? 0.23515   -28.43957 -13.01811 1.000 57.94875  ? 1093 GLU   B OE2  1 
ATOM   121  N  N    . SER   A 1 42  ? 2.23166   -30.07014 -19.36338 1.000 21.24766  ? 1094 SER   B N    1 
ATOM   122  C  CA   . SER   A 1 42  ? 3.10352   -29.84302 -20.50846 1.000 20.87211  ? 1094 SER   B CA   1 
ATOM   123  C  C    . SER   A 1 42  ? 3.66839   -28.43097 -20.43746 1.000 15.78936  ? 1094 SER   B C    1 
ATOM   124  O  O    . SER   A 1 42  ? 2.91931   -27.46504 -20.26935 1.000 15.69818  ? 1094 SER   B O    1 
ATOM   125  C  CB   . SER   A 1 42  ? 2.32941   -30.06205 -21.80839 1.000 17.04805  ? 1094 SER   B CB   1 
ATOM   126  O  OG   . SER   A 1 42  ? 3.17228   -29.96592 -22.94347 1.000 21.20620  ? 1094 SER   B OG   1 
ATOM   127  N  N    . GLY   A 1 43  ? 4.98837   -28.31583 -20.54460 1.000 16.74083  ? 1095 GLY   B N    1 
ATOM   128  C  CA   . GLY   A 1 43  ? 5.63527   -27.03878 -20.28562 1.000 16.94873  ? 1095 GLY   B CA   1 
ATOM   129  C  C    . GLY   A 1 43  ? 6.40909   -26.41866 -21.43967 1.000 18.15240  ? 1095 GLY   B C    1 
ATOM   130  O  O    . GLY   A 1 43  ? 7.37604   -25.68957 -21.21275 1.000 11.66052  ? 1095 GLY   B O    1 
ATOM   131  N  N    . PHE   A 1 44  ? 6.01499   -26.70065 -22.67764 1.000 13.59530  ? 1096 PHE   B N    1 
ATOM   132  C  CA   . PHE   A 1 44  ? 6.57680   -25.97556 -23.80967 1.000 14.05152  ? 1096 PHE   B CA   1 
ATOM   133  C  C    . PHE   A 1 44  ? 6.35667   -24.47459 -23.62860 1.000 12.85672  ? 1096 PHE   B C    1 
ATOM   134  O  O    . PHE   A 1 44  ? 5.24366   -24.04071 -23.33447 1.000 14.60720  ? 1096 PHE   B O    1 
ATOM   135  C  CB   . PHE   A 1 44  ? 5.90671   -26.43558 -25.10262 1.000 13.37441  ? 1096 PHE   B CB   1 
ATOM   136  C  CG   . PHE   A 1 44  ? 6.18681   -27.85254 -25.47870 1.000 13.26517  ? 1096 PHE   B CG   1 
ATOM   137  C  CD1  . PHE   A 1 44  ? 7.42889   -28.42542 -25.24185 1.000 13.71712  ? 1096 PHE   B CD1  1 
ATOM   138  C  CD2  . PHE   A 1 44  ? 5.21482   -28.60561 -26.11963 1.000 19.49425  ? 1096 PHE   B CD2  1 
ATOM   139  C  CE1  . PHE   A 1 44  ? 7.68598   -29.73038 -25.62892 1.000 15.56561  ? 1096 PHE   B CE1  1 
ATOM   140  C  CE2  . PHE   A 1 44  ? 5.46491   -29.92057 -26.51370 1.000 14.25200  ? 1096 PHE   B CE2  1 
ATOM   141  C  CZ   . PHE   A 1 44  ? 6.69999   -30.48046 -26.25985 1.000 19.21628  ? 1096 PHE   B CZ   1 
ATOM   142  N  N    . THR   A 1 45  ? 7.41457   -23.67547 -23.83068 1.000 10.62588  ? 1097 THR   B N    1 
ATOM   143  C  CA   . THR   A 1 45  ? 7.31344   -22.22449 -23.75261 1.000 13.70411  ? 1097 THR   B CA   1 
ATOM   144  C  C    . THR   A 1 45  ? 7.73024   -21.49140 -25.02363 1.000 13.83970  ? 1097 THR   B C    1 
ATOM   145  O  O    . THR   A 1 45  ? 7.37411   -20.31943 -25.18155 1.000 15.89950  ? 1097 THR   B O    1 
ATOM   146  C  CB   . THR   A 1 45  ? 8.16151   -21.68345 -22.58368 1.000 14.37286  ? 1097 THR   B CB   1 
ATOM   147  O  OG1  . THR   A 1 45  ? 9.51854   -22.12331 -22.71684 1.000 12.78893  ? 1097 THR   B OG1  1 
ATOM   148  C  CG2  . THR   A 1 45  ? 7.61869   -22.18755 -21.25064 1.000 12.56360  ? 1097 THR   B CG2  1 
ATOM   149  N  N    . CYS   A 1 46  ? 8.47121   -22.12230 -25.91973 1.000 9.79317   ? 1098 CYS   B N    1 
ATOM   150  C  CA   . CYS   A 1 46  ? 8.95602   -21.38921 -27.08175 1.000 13.49602  ? 1098 CYS   B CA   1 
ATOM   151  C  C    . CYS   A 1 46  ? 9.54001   -22.39211 -28.05785 1.000 14.13292  ? 1098 CYS   B C    1 
ATOM   152  O  O    . CYS   A 1 46  ? 9.94416   -23.49009 -27.66893 1.000 16.30406  ? 1098 CYS   B O    1 
ATOM   153  C  CB   . CYS   A 1 46  ? 9.99595   -20.32712 -26.68682 1.000 14.11548  ? 1098 CYS   B CB   1 
ATOM   154  S  SG   . CYS   A 1 46  ? 11.44211  -20.96901 -25.75699 1.000 17.03504  ? 1098 CYS   B SG   1 
ATOM   155  N  N    . CYS   A 1 47  ? 9.60384   -22.00506 -29.32984 1.000 17.39600  ? 1099 CYS   B N    1 
ATOM   156  C  CA   . CYS   A 1 47  ? 9.97284   -22.98399 -30.33791 1.000 13.93569  ? 1099 CYS   B CA   1 
ATOM   157  C  C    . CYS   A 1 47  ? 10.67265  -22.32288 -31.51196 1.000 14.90567  ? 1099 CYS   B C    1 
ATOM   158  O  O    . CYS   A 1 47  ? 10.50951  -21.13188 -31.78190 1.000 17.86876  ? 1099 CYS   B O    1 
ATOM   159  C  CB   . CYS   A 1 47  ? 8.74586   -23.75209 -30.83282 1.000 11.02175  ? 1099 CYS   B CB   1 
ATOM   160  S  SG   . CYS   A 1 47  ? 7.43970   -22.67220 -31.38364 1.000 18.37215  ? 1099 CYS   B SG   1 
ATOM   161  N  N    . ALA   A 1 48  ? 11.44366  -23.14078 -32.22007 1.000 19.03193  ? 1100 ALA   B N    1 
ATOM   162  C  CA   . ALA   A 1 48  ? 12.05649  -22.76967 -33.48612 1.000 22.39131  ? 1100 ALA   B CA   1 
ATOM   163  C  C    . ALA   A 1 48  ? 12.38154  -24.05061 -34.24820 1.000 16.90319  ? 1100 ALA   B C    1 
ATOM   164  O  O    . ALA   A 1 48  ? 12.75170  -25.05660 -33.63527 1.000 13.66481  ? 1100 ALA   B O    1 
ATOM   165  C  CB   . ALA   A 1 48  ? 13.32143  -21.92755 -33.26322 1.000 17.97688  ? 1100 ALA   B CB   1 
ATOM   166  N  N    . PHE   A 1 49  ? 12.21440  -24.01258 -35.57218 1.000 9.52529   ? 1101 PHE   B N    1 
ATOM   167  C  CA   . PHE   A 1 49  ? 12.59743  -25.13951 -36.41226 1.000 17.83779  ? 1101 PHE   B CA   1 
ATOM   168  C  C    . PHE   A 1 49  ? 14.10644  -25.28936 -36.44242 1.000 17.45139  ? 1101 PHE   B C    1 
ATOM   169  O  O    . PHE   A 1 49  ? 14.84533  -24.30529 -36.53946 1.000 19.15956  ? 1101 PHE   B O    1 
ATOM   170  C  CB   . PHE   A 1 49  ? 12.07726  -24.94551 -37.83720 1.000 19.24612  ? 1101 PHE   B CB   1 
ATOM   171  C  CG   . PHE   A 1 49  ? 10.61527  -25.22565 -37.98506 1.000 19.01948  ? 1101 PHE   B CG   1 
ATOM   172  C  CD1  . PHE   A 1 49  ? 10.16938  -26.51968 -38.20906 1.000 16.77664  ? 1101 PHE   B CD1  1 
ATOM   173  C  CD2  . PHE   A 1 49  ? 9.68318   -24.19474 -37.88793 1.000 16.35706  ? 1101 PHE   B CD2  1 
ATOM   174  C  CE1  . PHE   A 1 49  ? 8.81239   -26.78681 -38.33393 1.000 17.84398  ? 1101 PHE   B CE1  1 
ATOM   175  C  CE2  . PHE   A 1 49  ? 8.33219   -24.44687 -38.01980 1.000 19.24338  ? 1101 PHE   B CE2  1 
ATOM   176  C  CZ   . PHE   A 1 49  ? 7.89230   -25.75191 -38.24380 1.000 18.99071  ? 1101 PHE   B CZ   1 
ATOM   177  N  N    . SER   A 1 50  ? 14.57257  -26.52432 -36.35952 1.000 20.50861  ? 1102 SER   B N    1 
ATOM   178  C  CA   . SER   A 1 50  ? 16.00558  -26.73418 -36.45267 1.000 27.76771  ? 1102 SER   B CA   1 
ATOM   179  C  C    . SER   A 1 50  ? 16.40545  -26.91708 -37.91372 1.000 24.85639  ? 1102 SER   B C    1 
ATOM   180  O  O    . SER   A 1 50  ? 15.56436  -27.00613 -38.80863 1.000 30.73291  ? 1102 SER   B O    1 
ATOM   181  C  CB   . SER   A 1 50  ? 16.43378  -27.92616 -35.59076 1.000 32.16773  ? 1102 SER   B CB   1 
ATOM   182  O  OG   . SER   A 1 50  ? 16.20384  -29.15416 -36.24678 1.000 31.36143  ? 1102 SER   B OG   1 
ATOM   183  N  N    . ALA   A 1 51  ? 17.71842  -26.95495 -38.15485 1.000 29.30914  ? 1103 ALA   B N    1 
ATOM   184  C  CA   . ALA   A 1 51  ? 18.20730  -27.11885 -39.52391 1.000 33.61493  ? 1103 ALA   B CA   1 
ATOM   185  C  C    . ALA   A 1 51  ? 17.79137  -28.46287 -40.11192 1.000 34.42159  ? 1103 ALA   B C    1 
ATOM   186  O  O    . ALA   A 1 51  ? 17.58426  -28.57484 -41.32490 1.000 45.91473  ? 1103 ALA   B O    1 
ATOM   187  C  CB   . ALA   A 1 51  ? 19.72828  -26.95970 -39.56406 1.000 25.53110  ? 1103 ALA   B CB   1 
ATOM   188  N  N    . ARG   A 1 52  ? 17.66956  -29.48791 -39.27494 1.000 35.99152  ? 1104 ARG   B N    1 
ATOM   189  C  CA   . ARG   A 1 52  ? 17.16564  -30.79694 -39.68694 1.000 36.04344  ? 1104 ARG   B CA   1 
ATOM   190  C  C    . ARG   A 1 52  ? 15.64164  -30.72810 -39.63678 1.000 45.35927  ? 1104 ARG   B C    1 
ATOM   191  O  O    . ARG   A 1 52  ? 15.00578  -31.03419 -38.62472 1.000 38.54433  ? 1104 ARG   B O    1 
ATOM   192  C  CB   . ARG   A 1 52  ? 17.73084  -31.89592 -38.78903 1.000 44.27159  ? 1104 ARG   B CB   1 
ATOM   193  C  CG   . ARG   A 1 52  ? 17.48693  -33.31893 -39.27906 1.000 50.89566  ? 1104 ARG   B CG   1 
ATOM   194  C  CD   . ARG   A 1 52  ? 18.63406  -34.26183 -38.89821 1.000 51.53040  ? 1104 ARG   B CD   1 
ATOM   195  N  NE   . ARG   A 1 52  ? 18.35227  -35.10290 -37.73521 1.000 65.82490  ? 1104 ARG   B NE   1 
ATOM   196  C  CZ   . ARG   A 1 52  ? 17.74038  -36.28196 -37.78319 1.000 66.23585  ? 1104 ARG   B CZ   1 
ATOM   197  N  NH1  . ARG   A 1 52  ? 17.25831  -36.76996 -38.91716 1.000 63.72585  ? 1104 ARG   B NH1  1 
ATOM   198  N  NH2  . ARG   A 1 52  ? 17.60956  -36.99401 -36.66421 1.000 56.50987  ? 1104 ARG   B NH2  1 
ATOM   199  N  N    . GLU   A 1 53  ? 15.03849  -30.28912 -40.73570 1.000 49.71701  ? 1105 GLU   B N    1 
ATOM   200  C  CA   . GLU   A 1 53  ? 13.60047  -30.09126 -40.72154 1.000 54.30794  ? 1105 GLU   B CA   1 
ATOM   201  C  C    . GLU   A 1 53  ? 12.89463  -31.41234 -40.41552 1.000 50.56887  ? 1105 GLU   B C    1 
ATOM   202  O  O    . GLU   A 1 53  ? 13.47873  -32.49728 -40.50662 1.000 52.52857  ? 1105 GLU   B O    1 
ATOM   203  C  CB   . GLU   A 1 53  ? 13.13127  -29.48925 -42.04447 1.000 61.62792  ? 1105 GLU   B CB   1 
ATOM   204  C  CG   . GLU   A 1 53  ? 12.13718  -28.34336 -41.88333 1.000 48.90313  ? 1105 GLU   B CG   1 
ATOM   205  C  CD   . GLU   A 1 53  ? 10.70724  -28.82650 -41.69920 1.000 57.95459  ? 1105 GLU   B CD   1 
ATOM   206  O  OE1  . GLU   A 1 53  ? 10.47742  -29.74056 -40.87421 1.000 52.46063  ? 1105 GLU   B OE1  1 
ATOM   207  O  OE2  . GLU   A 1 53  ? 9.81112   -28.29857 -42.39609 1.000 55.69445  ? 1105 GLU   B OE2  1 
ATOM   208  N  N    . ARG   A 1 54  ? 11.61866  -31.29648 -40.03938 1.000 44.55425  ? 1106 ARG   B N    1 
ATOM   209  C  CA   . ARG   A 1 54  ? 10.84683  -32.36357 -39.40834 1.000 44.14153  ? 1106 ARG   B CA   1 
ATOM   210  C  C    . ARG   A 1 54  ? 11.04097  -32.30061 -37.89836 1.000 32.97519  ? 1106 ARG   B C    1 
ATOM   211  O  O    . ARG   A 1 54  ? 10.22411  -32.83272 -37.13630 1.000 29.43009  ? 1106 ARG   B O    1 
ATOM   212  C  CB   . ARG   A 1 54  ? 11.22591  -33.74952 -39.94343 1.000 49.55151  ? 1106 ARG   B CB   1 
ATOM   213  C  CG   . ARG   A 1 54  ? 10.72779  -34.00752 -41.36039 1.000 64.98632  ? 1106 ARG   B CG   1 
ATOM   214  C  CD   . ARG   A 1 54  ? 11.22086  -35.33645 -41.92349 1.000 70.49941  ? 1106 ARG   B CD   1 
ATOM   215  N  NE   . ARG   A 1 54  ? 10.86873  -35.47143 -43.33346 1.000 85.73686  ? 1106 ARG   B NE   1 
ATOM   216  C  CZ   . ARG   A 1 54  ? 11.35774  -36.39635 -44.14754 1.000 88.89422  ? 1106 ARG   B CZ   1 
ATOM   217  N  NH1  . ARG   A 1 54  ? 12.22787  -37.30028 -43.72666 1.000 90.52712  ? 1106 ARG   B NH1  1 
ATOM   218  N  NH2  . ARG   A 1 54  ? 10.96761  -36.41434 -45.41950 1.000 83.44239  ? 1106 ARG   B NH2  1 
ATOM   219  N  N    . PHE   A 1 55  ? 12.10196  -31.63852 -37.45145 1.000 25.71537  ? 1107 PHE   B N    1 
ATOM   220  C  CA   . PHE   A 1 55  ? 12.36609  -31.50955 -36.02947 1.000 21.82570  ? 1107 PHE   B CA   1 
ATOM   221  C  C    . PHE   A 1 55  ? 12.25899  -30.05657 -35.59341 1.000 27.36350  ? 1107 PHE   B C    1 
ATOM   222  O  O    . PHE   A 1 55  ? 12.66383  -29.13651 -36.31341 1.000 26.10567  ? 1107 PHE   B O    1 
ATOM   223  C  CB   . PHE   A 1 55  ? 13.73218  -32.09543 -35.67263 1.000 21.93326  ? 1107 PHE   B CB   1 
ATOM   224  C  CG   . PHE   A 1 55  ? 13.83730  -33.56841 -35.97469 1.000 32.15357  ? 1107 PHE   B CG   1 
ATOM   225  C  CD1  . PHE   A 1 55  ? 14.15421  -34.00633 -37.25274 1.000 36.89000  ? 1107 PHE   B CD1  1 
ATOM   226  C  CD2  . PHE   A 1 55  ? 13.58449  -34.51447 -34.99070 1.000 33.49615  ? 1107 PHE   B CD2  1 
ATOM   227  C  CE1  . PHE   A 1 55  ? 14.23731  -35.35831 -37.54080 1.000 39.42198  ? 1107 PHE   B CE1  1 
ATOM   228  C  CE2  . PHE   A 1 55  ? 13.66659  -35.87245 -35.27276 1.000 36.93523  ? 1107 PHE   B CE2  1 
ATOM   229  C  CZ   . PHE   A 1 55  ? 13.99050  -36.29137 -36.55081 1.000 37.82108  ? 1107 PHE   B CZ   1 
ATOM   230  N  N    . LEU   A 1 56  ? 11.67509  -29.87367 -34.41934 1.000 20.96744  ? 1108 LEU   B N    1 
ATOM   231  C  CA   . LEU   A 1 56  ? 11.43603  -28.57972 -33.81427 1.000 14.97808  ? 1108 LEU   B CA   1 
ATOM   232  C  C    . LEU   A 1 56  ? 12.13117  -28.54770 -32.45734 1.000 16.22637  ? 1108 LEU   B C    1 
ATOM   233  O  O    . LEU   A 1 56  ? 12.07334  -29.52373 -31.70137 1.000 18.32292  ? 1108 LEU   B O    1 
ATOM   234  C  CB   . LEU   A 1 56  ? 9.92802   -28.33587 -33.65610 1.000 14.16114  ? 1108 LEU   B CB   1 
ATOM   235  C  CG   . LEU   A 1 56  ? 9.42594   -26.97594 -33.17100 1.000 14.73667  ? 1108 LEU   B CG   1 
ATOM   236  C  CD1  . LEU   A 1 56  ? 9.50072   -25.91589 -34.30697 1.000 17.55541  ? 1108 LEU   B CD1  1 
ATOM   237  C  CD2  . LEU   A 1 56  ? 8.00701   -27.12310 -32.62986 1.000 12.87375  ? 1108 LEU   B CD2  1 
ATOM   238  N  N    . MET   A 1 57  ? 12.80509  -27.43864 -32.16937 1.000 12.64551  ? 1109 MET   B N    1 
ATOM   239  C  CA   . MET   A 1 57  ? 13.38819  -27.17563 -30.86042 1.000 13.60324  ? 1109 MET   B CA   1 
ATOM   240  C  C    . MET   A 1 57  ? 12.38021  -26.41576 -30.00529 1.000 13.17028  ? 1109 MET   B C    1 
ATOM   241  O  O    . MET   A 1 57  ? 11.77806  -25.43781 -30.46619 1.000 17.36025  ? 1109 MET   B O    1 
ATOM   242  C  CB   . MET   A 1 57  ? 14.66210  -26.33950 -30.99652 1.000 13.97128  ? 1109 MET   B CB   1 
ATOM   243  C  CG   . MET   A 1 57  ? 15.81809  -27.00637 -31.71466 1.000 20.62234  ? 1109 MET   B CG   1 
ATOM   244  S  SD   . MET   A 1 57  ? 17.12893  -25.81222 -32.10875 1.000 40.00425  ? 1109 MET   B SD   1 
ATOM   245  C  CE   . MET   A 1 57  ? 16.50571  -25.08923 -33.61466 1.000 24.31572  ? 1109 MET   B CE   1 
ATOM   246  N  N    . LEU   A 1 58  ? 12.21038  -26.83983 -28.75728 1.000 11.47567  ? 1110 LEU   B N    1 
ATOM   247  C  CA   . LEU   A 1 58  ? 11.31640  -26.14095 -27.84117 1.000 12.67407  ? 1110 LEU   B CA   1 
ATOM   248  C  C    . LEU   A 1 58  ? 12.01152  -25.92193 -26.51023 1.000 14.13101  ? 1110 LEU   B C    1 
ATOM   249  O  O    . LEU   A 1 58  ? 12.65066  -26.83788 -25.98733 1.000 13.51831  ? 1110 LEU   B O    1 
ATOM   250  C  CB   . LEU   A 1 58  ? 10.01450  -26.91408 -27.62206 1.000 11.52321  ? 1110 LEU   B CB   1 
ATOM   251  C  CG   . LEU   A 1 58  ? 9.28741   -27.34811 -28.89200 1.000 12.91173  ? 1110 LEU   B CG   1 
ATOM   252  C  CD1  . LEU   A 1 58  ? 9.61852   -28.79506 -29.22209 1.000 10.31370  ? 1110 LEU   B CD1  1 
ATOM   253  C  CD2  . LEU   A 1 58  ? 7.77441   -27.15426 -28.76084 1.000 16.15305  ? 1110 LEU   B CD2  1 
ATOM   254  N  N    . GLY   A 1 59  ? 11.89645  -24.70096 -25.97417 1.000 14.24399  ? 1111 GLY   B N    1 
ATOM   255  C  CA   . GLY   A 1 59  ? 12.22857  -24.46798 -24.58620 1.000 11.58075  ? 1111 GLY   B CA   1 
ATOM   256  C  C    . GLY   A 1 59  ? 11.08871  -24.89012 -23.68010 1.000 15.04314  ? 1111 GLY   B C    1 
ATOM   257  O  O    . GLY   A 1 59  ? 9.95368   -25.05222 -24.12099 1.000 17.81928  ? 1111 GLY   B O    1 
ATOM   258  N  N    . THR   A 1 60  ? 11.39486  -25.11014 -22.40114 1.000 14.55888  ? 1112 THR   B N    1 
ATOM   259  C  CA   . THR   A 1 60  ? 10.38000  -25.51627 -21.43705 1.000 11.13136  ? 1112 THR   B CA   1 
ATOM   260  C  C    . THR   A 1 60  ? 10.44504  -24.63131 -20.20202 1.000 13.19314  ? 1112 THR   B C    1 
ATOM   261  O  O    . THR   A 1 60  ? 11.42900  -23.92422 -19.95710 1.000 10.79162  ? 1112 THR   B O    1 
ATOM   262  C  CB   . THR   A 1 60  ? 10.54719  -26.97227 -20.99212 1.000 15.06783  ? 1112 THR   B CB   1 
ATOM   263  O  OG1  . THR   A 1 60  ? 11.62729  -27.04920 -20.04523 1.000 14.65978  ? 1112 THR   B OG1  1 
ATOM   264  C  CG2  . THR   A 1 60  ? 10.82515  -27.86520 -22.18218 1.000 9.48004   ? 1112 THR   B CG2  1 
ATOM   265  N  N    . CYS   A 1 61  ? 9.39813   -24.73044 -19.38092 1.000 14.83940  ? 1113 CYS   B N    1 
ATOM   266  C  CA   . CYS   A 1 61  ? 9.33718   -23.93149 -18.16888 1.000 11.84317  ? 1113 CYS   B CA   1 
ATOM   267  C  C    . CYS   A 1 61  ? 10.32633  -24.39443 -17.11100 1.000 16.25636  ? 1113 CYS   B C    1 
ATOM   268  O  O    . CYS   A 1 61  ? 10.46337  -23.70846 -16.09099 1.000 16.03521  ? 1113 CYS   B O    1 
ATOM   269  C  CB   . CYS   A 1 61  ? 7.91824   -23.93665 -17.60374 1.000 18.44602  ? 1113 CYS   B CB   1 
ATOM   270  S  SG   . CYS   A 1 61  ? 7.36145   -25.56972 -17.10174 1.000 25.81258  ? 1113 CYS   B SG   1 
ATOM   271  N  N    . THR   A 1 62  ? 11.02642  -25.51836 -17.31811 1.000 15.67632  ? 1114 THR   B N    1 
ATOM   272  C  CA   . THR   A 1 62  ? 12.07056  -25.94929 -16.39024 1.000 19.79312  ? 1114 THR   B CA   1 
ATOM   273  C  C    . THR   A 1 62  ? 13.47248  -25.71513 -16.94537 1.000 21.16744  ? 1114 THR   B C    1 
ATOM   274  O  O    . THR   A 1 62  ? 14.43759  -26.31405 -16.46149 1.000 19.13977  ? 1114 THR   B O    1 
ATOM   275  C  CB   . THR   A 1 62  ? 11.89574  -27.41732 -16.01327 1.000 12.93498  ? 1114 THR   B CB   1 
ATOM   276  O  OG1  . THR   A 1 62  ? 12.03270  -28.23126 -17.17932 1.000 21.35020  ? 1114 THR   B OG1  1 
ATOM   277  C  CG2  . THR   A 1 62  ? 10.51883  -27.63648 -15.40214 1.000 22.66566  ? 1114 THR   B CG2  1 
ATOM   278  N  N    . GLY   A 1 63  ? 13.60429  -24.84108 -17.94135 1.000 17.81233  ? 1115 GLY   B N    1 
ATOM   279  C  CA   . GLY   A 1 63  ? 14.91421  -24.51193 -18.47148 1.000 15.55295  ? 1115 GLY   B CA   1 
ATOM   280  C  C    . GLY   A 1 63  ? 15.52322  -25.59484 -19.32558 1.000 17.16727  ? 1115 GLY   B C    1 
ATOM   281  O  O    . GLY   A 1 63  ? 16.74021  -25.61872 -19.50470 1.000 14.57520  ? 1115 GLY   B O    1 
ATOM   282  N  N    . GLN   A 1 64  ? 14.70826  -26.49390 -19.86453 1.000 13.03601  ? 1116 GLN   B N    1 
ATOM   283  C  CA   . GLN   A 1 64  ? 15.20127  -27.51982 -20.75962 1.000 16.84084  ? 1116 GLN   B CA   1 
ATOM   284  C  C    . GLN   A 1 64  ? 15.00707  -27.07879 -22.20658 1.000 15.16690  ? 1116 GLN   B C    1 
ATOM   285  O  O    . GLN   A 1 64  ? 14.04497  -26.38187 -22.54946 1.000 17.52881  ? 1116 GLN   B O    1 
ATOM   286  C  CB   . GLN   A 1 64  ? 14.49042  -28.85390 -20.51559 1.000 20.08643  ? 1116 GLN   B CB   1 
ATOM   287  C  CG   . GLN   A 1 64  ? 14.69962  -29.44293 -19.12163 1.000 19.27899  ? 1116 GLN   B CG   1 
ATOM   288  C  CD   . GLN   A 1 64  ? 16.15469  -29.84180 -18.83780 1.000 22.94177  ? 1116 GLN   B CD   1 
ATOM   289  O  OE1  . GLN   A 1 64  ? 16.77674  -29.33977 -17.89284 1.000 27.25418  ? 1116 GLN   B OE1  1 
ATOM   290  N  NE2  . GLN   A 1 64  ? 16.69070  -30.76272 -19.63989 1.000 25.83709  ? 1116 GLN   B NE2  1 
ATOM   291  N  N    . LEU   A 1 65  ? 15.95003  -27.47967 -23.04869 1.000 14.58752  ? 1117 LEU   B N    1 
ATOM   292  C  CA   . LEU   A 1 65  ? 15.80687  -27.40463 -24.49567 1.000 17.37697  ? 1117 LEU   B CA   1 
ATOM   293  C  C    . LEU   A 1 65  ? 15.52296  -28.81264 -25.00770 1.000 16.51454  ? 1117 LEU   B C    1 
ATOM   294  O  O    . LEU   A 1 65  ? 16.30007  -29.73157 -24.73481 1.000 17.16383  ? 1117 LEU   B O    1 
ATOM   295  C  CB   . LEU   A 1 65  ? 17.07075  -26.85448 -25.14978 1.000 18.07917  ? 1117 LEU   B CB   1 
ATOM   296  C  CG   . LEU   A 1 65  ? 16.84459  -26.76945 -26.65876 1.000 18.09803  ? 1117 LEU   B CG   1 
ATOM   297  C  CD1  . LEU   A 1 65  ? 16.36841  -25.37548 -26.99966 1.000 19.53136  ? 1117 LEU   B CD1  1 
ATOM   298  C  CD2  . LEU   A 1 65  ? 18.07054  -27.16230 -27.43890 1.000 19.99611  ? 1117 LEU   B CD2  1 
ATOM   299  N  N    . LYS   A 1 66  ? 14.42390  -28.98872 -25.74659 1.000 14.54944  ? 1118 LYS   B N    1 
ATOM   300  C  CA   . LYS   A 1 66  ? 14.04198  -30.30674 -26.24560 1.000 14.92940  ? 1118 LYS   B CA   1 
ATOM   301  C  C    . LYS   A 1 66  ? 13.88382  -30.31170 -27.76158 1.000 15.81201  ? 1118 LYS   B C    1 
ATOM   302  O  O    . LYS   A 1 66  ? 13.53266  -29.29871 -28.37351 1.000 21.39265  ? 1118 LYS   B O    1 
ATOM   303  C  CB   . LYS   A 1 66  ? 12.74709  -30.79189 -25.58848 1.000 12.36091  ? 1118 LYS   B CB   1 
ATOM   304  C  CG   . LYS   A 1 66  ? 12.90526  -30.99393 -24.09151 1.000 16.68116  ? 1118 LYS   B CG   1 
ATOM   305  C  CD   . LYS   A 1 66  ? 11.78941  -31.84606 -23.53342 1.000 22.51450  ? 1118 LYS   B CD   1 
ATOM   306  C  CE   . LYS   A 1 66  ? 12.08159  -32.24608 -22.09447 1.000 21.06485  ? 1118 LYS   B CE   1 
ATOM   307  N  NZ   . LYS   A 1 66  ? 10.91072  -32.91122 -21.46737 1.000 23.55101  ? 1118 LYS   B NZ   1 
ATOM   308  N  N    . LEU   A 1 67  ? 14.14787  -31.46965 -28.36165 1.000 18.38080  ? 1119 LEU   B N    1 
ATOM   309  C  CA   . LEU   A 1 67  ? 13.99875  -31.68361 -29.79664 1.000 16.91044  ? 1119 LEU   B CA   1 
ATOM   310  C  C    . LEU   A 1 67  ? 12.83981  -32.63572 -30.04756 1.000 16.35769  ? 1119 LEU   B C    1 
ATOM   311  O  O    . LEU   A 1 67  ? 12.78398  -33.71974 -29.45959 1.000 17.37299  ? 1119 LEU   B O    1 
ATOM   312  C  CB   . LEU   A 1 67  ? 15.27274  -32.27447 -30.40880 1.000 19.67246  ? 1119 LEU   B CB   1 
ATOM   313  C  CG   . LEU   A 1 67  ? 16.15056  -31.34635 -31.24485 1.000 29.64713  ? 1119 LEU   B CG   1 
ATOM   314  C  CD1  . LEU   A 1 67  ? 15.47240  -31.00637 -32.54077 1.000 24.29811  ? 1119 LEU   B CD1  1 
ATOM   315  C  CD2  . LEU   A 1 67  ? 16.47952  -30.08735 -30.46784 1.000 26.01510  ? 1119 LEU   B CD2  1 
ATOM   316  N  N    . TYR   A 1 68  ? 11.93968  -32.24977 -30.93445 1.000 15.33328  ? 1120 TYR   B N    1 
ATOM   317  C  CA   . TYR   A 1 68  ? 10.78273  -33.07788 -31.24336 1.000 19.31772  ? 1120 TYR   B CA   1 
ATOM   318  C  C    . TYR   A 1 68  ? 10.63660  -33.26384 -32.74635 1.000 17.11891  ? 1120 TYR   B C    1 
ATOM   319  O  O    . TYR   A 1 68  ? 10.90443  -32.34678 -33.53135 1.000 15.34287  ? 1120 TYR   B O    1 
ATOM   320  C  CB   . TYR   A 1 68  ? 9.49073   -32.46502 -30.67121 1.000 12.84766  ? 1120 TYR   B CB   1 
ATOM   321  C  CG   . TYR   A 1 68  ? 9.22692   -32.84610 -29.24019 1.000 14.47674  ? 1120 TYR   B CG   1 
ATOM   322  C  CD1  . TYR   A 1 68  ? 9.94697   -32.26007 -28.19725 1.000 13.38989  ? 1120 TYR   B CD1  1 
ATOM   323  C  CD2  . TYR   A 1 68  ? 8.25504   -33.79921 -28.92313 1.000 16.55696  ? 1120 TYR   B CD2  1 
ATOM   324  C  CE1  . TYR   A 1 68  ? 9.71314   -32.61414 -26.87324 1.000 11.93191  ? 1120 TYR   B CE1  1 
ATOM   325  C  CE2  . TYR   A 1 68  ? 8.00221   -34.15728 -27.60112 1.000 12.21935  ? 1120 TYR   B CE2  1 
ATOM   326  C  CZ   . TYR   A 1 68  ? 8.73126   -33.56025 -26.57917 1.000 19.24885  ? 1120 TYR   B CZ   1 
ATOM   327  O  OH   . TYR   A 1 68  ? 8.48643   -33.91132 -25.26816 1.000 19.16984  ? 1120 TYR   B OH   1 
ATOM   328  N  N    . ASN   A 1 69  ? 10.20768  -34.46186 -33.12835 1.000 15.90804  ? 1121 ASN   B N    1 
ATOM   329  C  CA   . ASN   A 1 69  ? 9.64856   -34.68687 -34.45130 1.000 20.30116  ? 1121 ASN   B CA   1 
ATOM   330  C  C    . ASN   A 1 69  ? 8.28449   -34.00800 -34.50114 1.000 18.89662  ? 1121 ASN   B C    1 
ATOM   331  O  O    . ASN   A 1 69  ? 7.38961   -34.36812 -33.72906 1.000 21.18336  ? 1121 ASN   B O    1 
ATOM   332  C  CB   . ASN   A 1 69  ? 9.52968   -36.19187 -34.71735 1.000 19.06324  ? 1121 ASN   B CB   1 
ATOM   333  C  CG   . ASN   A 1 69  ? 9.16857   -36.51686 -36.16832 1.000 21.39221  ? 1121 ASN   B CG   1 
ATOM   334  O  OD1  . ASN   A 1 69  ? 8.08049   -36.20695 -36.64620 1.000 21.60276  ? 1121 ASN   B OD1  1 
ATOM   335  N  ND2  . ASN   A 1 69  ? 10.08256  -37.16574 -36.86044 1.000 20.69147  ? 1121 ASN   B ND2  1 
ATOM   336  N  N    . VAL   A 1 70  ? 8.12730   -33.00599 -35.37509 1.000 18.92302  ? 1122 VAL   B N    1 
ATOM   337  C  CA   . VAL   A 1 70  ? 6.89223   -32.22411 -35.37093 1.000 21.35507  ? 1122 VAL   B CA   1 
ATOM   338  C  C    . VAL   A 1 70  ? 5.71625   -33.00320 -35.93184 1.000 23.37393  ? 1122 VAL   B C    1 
ATOM   339  O  O    . VAL   A 1 70  ? 4.56424   -32.66233 -35.63971 1.000 20.32088  ? 1122 VAL   B O    1 
ATOM   340  C  CB   . VAL   A 1 70  ? 7.03402   -30.91207 -36.16190 1.000 25.50681  ? 1122 VAL   B CB   1 
ATOM   341  C  CG1  . VAL   A 1 70  ? 8.07800   -30.03499 -35.53598 1.000 26.28387  ? 1122 VAL   B CG1  1 
ATOM   342  C  CG2  . VAL   A 1 70  ? 7.35590   -31.20098 -37.62594 1.000 23.57527  ? 1122 VAL   B CG2  1 
ATOM   343  N  N    . PHE   A 1 71  ? 5.97327   -34.04115 -36.73190 1.000 20.79239  ? 1123 PHE   B N    1 
ATOM   344  C  CA   . PHE   A 1 71  ? 4.91029   -34.85223 -37.30882 1.000 21.39507  ? 1123 PHE   B CA   1 
ATOM   345  C  C    . PHE   A 1 71  ? 4.46249   -35.98231 -36.38982 1.000 20.08773  ? 1123 PHE   B C    1 
ATOM   346  O  O    . PHE   A 1 71  ? 3.25953   -36.24943 -36.28571 1.000 22.41769  ? 1123 PHE   B O    1 
ATOM   347  C  CB   . PHE   A 1 71  ? 5.36420   -35.40714 -38.65689 1.000 19.88805  ? 1123 PHE   B CB   1 
ATOM   348  C  CG   . PHE   A 1 71  ? 5.77500   -34.33906 -39.61189 1.000 24.21437  ? 1123 PHE   B CG   1 
ATOM   349  C  CD1  . PHE   A 1 71  ? 4.81986   -33.54114 -40.22377 1.000 25.00280  ? 1123 PHE   B CD1  1 
ATOM   350  C  CD2  . PHE   A 1 71  ? 7.11395   -34.09492 -39.86802 1.000 28.12090  ? 1123 PHE   B CD2  1 
ATOM   351  C  CE1  . PHE   A 1 71  ? 5.18967   -32.54007 -41.08777 1.000 20.02792  ? 1123 PHE   B CE1  1 
ATOM   352  C  CE2  . PHE   A 1 71  ? 7.49476   -33.08885 -40.74603 1.000 26.94548  ? 1123 PHE   B CE2  1 
ATOM   353  C  CZ   . PHE   A 1 71  ? 6.53262   -32.31293 -41.35390 1.000 26.28965  ? 1123 PHE   B CZ   1 
ATOM   354  N  N    . SER   A 1 72  ? 5.38863   -36.64424 -35.69794 1.000 18.96183  ? 1124 SER   B N    1 
ATOM   355  C  CA   . SER   A 1 72  ? 4.97782   -37.73732 -34.81794 1.000 23.06584  ? 1124 SER   B CA   1 
ATOM   356  C  C    . SER   A 1 72  ? 4.68893   -37.28840 -33.39289 1.000 25.37213  ? 1124 SER   B C    1 
ATOM   357  O  O    . SER   A 1 72  ? 3.89506   -37.93550 -32.70183 1.000 25.52577  ? 1124 SER   B O    1 
ATOM   358  C  CB   . SER   A 1 72  ? 6.05194   -38.82321 -34.77409 1.000 19.74341  ? 1124 SER   B CB   1 
ATOM   359  O  OG   . SER   A 1 72  ? 7.21195   -38.32412 -34.13219 1.000 29.90864  ? 1124 SER   B OG   1 
ATOM   360  N  N    . GLY   A 1 73  ? 5.30487   -36.20135 -32.93391 1.000 20.94431  ? 1125 GLY   B N    1 
ATOM   361  C  CA   . GLY   A 1 73  ? 5.23198   -35.84741 -31.52889 1.000 19.93424  ? 1125 GLY   B CA   1 
ATOM   362  C  C    . GLY   A 1 73  ? 6.24314   -36.56134 -30.66402 1.000 21.38397  ? 1125 GLY   B C    1 
ATOM   363  O  O    . GLY   A 1 73  ? 6.12726   -36.55640 -29.43401 1.000 16.81094  ? 1125 GLY   B O    1 
ATOM   364  N  N    . GLN   A 1 74  ? 7.25013   -37.16622 -31.27515 1.000 21.08825  ? 1126 GLN   B N    1 
ATOM   365  C  CA   . GLN   A 1 74  ? 8.23228   -37.96715 -30.56128 1.000 22.98907  ? 1126 GLN   B CA   1 
ATOM   366  C  C    . GLN   A 1 74  ? 9.34825   -37.06406 -30.04636 1.000 17.00233  ? 1126 GLN   B C    1 
ATOM   367  O  O    . GLN   A 1 74  ? 10.01210  -36.37997 -30.83040 1.000 16.54612  ? 1126 GLN   B O    1 
ATOM   368  C  CB   . GLN   A 1 74  ? 8.78929   -39.04406 -31.49337 1.000 17.00608  ? 1126 GLN   B CB   1 
ATOM   369  C  CG   . GLN   A 1 74  ? 9.96043   -39.79597 -30.92352 1.000 22.66564  ? 1126 GLN   B CG   1 
ATOM   370  C  CD   . GLN   A 1 74  ? 9.52763   -40.82105 -29.90651 1.000 31.84177  ? 1126 GLN   B CD   1 
ATOM   371  O  OE1  . GLN   A 1 74  ? 9.04470   -41.89508 -30.26750 1.000 30.79601  ? 1126 GLN   B OE1  1 
ATOM   372  N  NE2  . GLN   A 1 74  ? 9.68273   -40.49608 -28.62352 1.000 36.19510  ? 1126 GLN   B NE2  1 
ATOM   373  N  N    . GLU   A 1 75  ? 9.56438   -37.06609 -28.73738 1.000 19.70183  ? 1127 GLU   B N    1 
ATOM   374  C  CA   . GLU   A 1 75  ? 10.71337  -36.35799 -28.18847 1.000 18.49684  ? 1127 GLU   B CA   1 
ATOM   375  C  C    . GLU   A 1 75  ? 12.00140  -37.06185 -28.61263 1.000 21.86286  ? 1127 GLU   B C    1 
ATOM   376  O  O    . GLU   A 1 75  ? 12.16354  -38.26084 -28.37669 1.000 25.82039  ? 1127 GLU   B O    1 
ATOM   377  C  CB   . GLU   A 1 75  ? 10.61752  -36.28706 -26.67446 1.000 13.41063  ? 1127 GLU   B CB   1 
ATOM   378  C  CG   . GLU   A 1 75  ? 11.81751  -35.57296 -26.03456 1.000 21.97913  ? 1127 GLU   B CG   1 
ATOM   379  C  CD   . GLU   A 1 75  ? 11.66065  -35.42103 -24.53554 1.000 21.29491  ? 1127 GLU   B CD   1 
ATOM   380  O  OE1  . GLU   A 1 75  ? 10.60265  -34.93615 -24.09741 1.000 18.70569  ? 1127 GLU   B OE1  1 
ATOM   381  O  OE2  . GLU   A 1 75  ? 12.58777  -35.81597 -23.80065 1.000 28.03216  ? 1127 GLU   B OE2  1 
ATOM   382  N  N    . GLU   A 1 76  ? 12.91526  -36.32174 -29.23870 1.000 20.09805  ? 1128 GLU   B N    1 
ATOM   383  C  CA   . GLU   A 1 76  ? 14.18826  -36.85860 -29.70185 1.000 19.10850  ? 1128 GLU   B CA   1 
ATOM   384  C  C    . GLU   A 1 76  ? 15.35134  -36.59152 -28.74796 1.000 26.93571  ? 1128 GLU   B C    1 
ATOM   385  O  O    . GLU   A 1 76  ? 16.24143  -37.43144 -28.61008 1.000 25.68227  ? 1128 GLU   B O    1 
ATOM   386  C  CB   . GLU   A 1 76  ? 14.52407  -36.29252 -31.07886 1.000 25.19347  ? 1128 GLU   B CB   1 
ATOM   387  C  CG   . GLU   A 1 76  ? 13.72702  -36.94555 -32.20081 1.000 36.95865  ? 1128 GLU   B CG   1 
ATOM   388  C  CD   . GLU   A 1 76  ? 14.06214  -38.41751 -32.35089 1.000 43.69631  ? 1128 GLU   B CD   1 
ATOM   389  O  OE1  . GLU   A 1 76  ? 15.26917  -38.75139 -32.41403 1.000 52.57069  ? 1128 GLU   B OE1  1 
ATOM   390  O  OE2  . GLU   A 1 76  ? 13.12322  -39.23761 -32.38583 1.000 44.39494  ? 1128 GLU   B OE2  1 
ATOM   391  N  N    . ALA   A 1 77  ? 15.38129  -35.43954 -28.08392 1.000 27.35972  ? 1129 ALA   B N    1 
ATOM   392  C  CA   . ALA   A 1 77  ? 16.49235  -35.11846 -27.19602 1.000 19.97769  ? 1129 ALA   B CA   1 
ATOM   393  C  C    . ALA   A 1 77  ? 16.02135  -34.08555 -26.18894 1.000 24.23628  ? 1129 ALA   B C    1 
ATOM   394  O  O    . ALA   A 1 77  ? 15.01426  -33.39864 -26.40081 1.000 17.24965  ? 1129 ALA   B O    1 
ATOM   395  C  CB   . ALA   A 1 77  ? 17.70922  -34.60532 -27.97413 1.000 19.43765  ? 1129 ALA   B CB   1 
ATOM   396  N  N    . SER   A 1 78  ? 16.76746  -33.99451 -25.08401 1.000 17.42777  ? 1130 SER   B N    1 
ATOM   397  C  CA   . SER   A 1 78  ? 16.53047  -33.03657 -24.01595 1.000 16.93727  ? 1130 SER   B CA   1 
ATOM   398  C  C    . SER   A 1 78  ? 17.87148  -32.56746 -23.47207 1.000 19.97501  ? 1130 SER   B C    1 
ATOM   399  O  O    . SER   A 1 78  ? 18.75459  -33.39038 -23.23119 1.000 17.52362  ? 1130 SER   B O    1 
ATOM   400  C  CB   . SER   A 1 78  ? 15.70465  -33.65770 -22.88789 1.000 18.40923  ? 1130 SER   B CB   1 
ATOM   401  O  OG   . SER   A 1 78  ? 15.56667  -32.74075 -21.81484 1.000 20.78480  ? 1130 SER   B OG   1 
ATOM   402  N  N    . TYR   A 1 79  ? 18.02837  -31.25145 -23.28504 1.000 15.00608  ? 1131 TYR   B N    1 
ATOM   403  C  CA   . TYR   A 1 79  ? 19.25537  -30.67635 -22.75515 1.000 15.87465  ? 1131 TYR   B CA   1 
ATOM   404  C  C    . TYR   A 1 79  ? 18.91238  -29.65142 -21.69307 1.000 19.71037  ? 1131 TYR   B C    1 
ATOM   405  O  O    . TYR   A 1 79  ? 17.96929  -28.86351 -21.84995 1.000 19.80303  ? 1131 TYR   B O    1 
ATOM   406  C  CB   . TYR   A 1 79  ? 20.09719  -30.00423 -23.84421 1.000 15.46458  ? 1131 TYR   B CB   1 
ATOM   407  C  CG   . TYR   A 1 79  ? 20.40516  -30.89116 -25.01327 1.000 19.07468  ? 1131 TYR   B CG   1 
ATOM   408  C  CD1  . TYR   A 1 79  ? 21.42726  -31.83206 -24.94341 1.000 22.89522  ? 1131 TYR   B CD1  1 
ATOM   409  C  CD2  . TYR   A 1 79  ? 19.67403  -30.79719 -26.18919 1.000 23.46248  ? 1131 TYR   B CD2  1 
ATOM   410  C  CE1  . TYR   A 1 79  ? 21.71223  -32.65599 -26.02747 1.000 24.14591  ? 1131 TYR   B CE1  1 
ATOM   411  C  CE2  . TYR   A 1 79  ? 19.94800  -31.61212 -27.27725 1.000 19.59275  ? 1131 TYR   B CE2  1 
ATOM   412  C  CZ   . TYR   A 1 79  ? 20.96910  -32.53802 -27.18839 1.000 23.16322  ? 1131 TYR   B CZ   1 
ATOM   413  O  OH   . TYR   A 1 79  ? 21.24707  -33.35096 -28.26045 1.000 25.92113  ? 1131 TYR   B OH   1 
ATOM   414  N  N    . ASN   A 1 80  ? 19.69949  -29.65639 -20.62615 1.000 14.43666  ? 1132 ASN   B N    1 
ATOM   415  C  CA   . ASN   A 1 80  ? 19.51151  -28.74444 -19.51310 1.000 19.50481  ? 1132 ASN   B CA   1 
ATOM   416  C  C    . ASN   A 1 80  ? 20.27236  -27.46436 -19.81713 1.000 22.04075  ? 1132 ASN   B C    1 
ATOM   417  O  O    . ASN   A 1 80  ? 21.50636  -27.44924 -19.77426 1.000 25.60720  ? 1132 ASN   B O    1 
ATOM   418  C  CB   . ASN   A 1 80  ? 19.99671  -29.37444 -18.21518 1.000 20.17687  ? 1132 ASN   B CB   1 
ATOM   419  C  CG   . ASN   A 1 80  ? 20.02873  -28.38648 -17.08614 1.000 29.54233  ? 1132 ASN   B CG   1 
ATOM   420  O  OD1  . ASN   A 1 80  ? 21.07377  -28.17240 -16.47324 1.000 40.29044  ? 1132 ASN   B OD1  1 
ATOM   421  N  ND2  . ASN   A 1 80  ? 18.88069  -27.75660 -16.80800 1.000 25.90179  ? 1132 ASN   B ND2  1 
ATOM   422  N  N    . CYS   A 1 81  ? 19.54322  -26.39342 -20.12902 1.000 15.89056  ? 1133 CYS   B N    1 
ATOM   423  C  CA   . CYS   A 1 81  ? 20.18206  -25.13634 -20.49604 1.000 18.05574  ? 1133 CYS   B CA   1 
ATOM   424  C  C    . CYS   A 1 81  ? 20.16407  -24.10239 -19.38300 1.000 11.62847  ? 1133 CYS   B C    1 
ATOM   425  O  O    . CYS   A 1 81  ? 21.15602  -23.39529 -19.20008 1.000 12.53294  ? 1133 CYS   B O    1 
ATOM   426  C  CB   . CYS   A 1 81  ? 19.53087  -24.54736 -21.75495 1.000 17.65878  ? 1133 CYS   B CB   1 
ATOM   427  S  SG   . CYS   A 1 81  ? 19.79582  -25.56328 -23.22802 1.000 17.76530  ? 1133 CYS   B SG   1 
ATOM   428  N  N    . HIS   A 1 82  ? 19.07114  -23.98552 -18.63188 1.000 13.41641  ? 1134 HIS   B N    1 
ATOM   429  C  CA   . HIS   A 1 82  ? 18.95214  -22.92857 -17.63283 1.000 18.75241  ? 1134 HIS   B CA   1 
ATOM   430  C  C    . HIS   A 1 82  ? 18.29432  -23.45768 -16.36579 1.000 17.33657  ? 1134 HIS   B C    1 
ATOM   431  O  O    . HIS   A 1 82  ? 17.66042  -24.51374 -16.36276 1.000 14.94108  ? 1134 HIS   B O    1 
ATOM   432  C  CB   . HIS   A 1 82  ? 18.14197  -21.74063 -18.15971 1.000 13.06873  ? 1134 HIS   B CB   1 
ATOM   433  C  CG   . HIS   A 1 82  ? 18.80578  -20.99052 -19.27175 1.000 13.94237  ? 1134 HIS   B CG   1 
ATOM   434  N  ND1  . HIS   A 1 82  ? 19.80271  -20.06143 -19.05482 1.000 13.96036  ? 1134 HIS   B ND1  1 
ATOM   435  C  CD2  . HIS   A 1 82  ? 18.59564  -21.00949 -20.60973 1.000 9.79046   ? 1134 HIS   B CD2  1 
ATOM   436  C  CE1  . HIS   A 1 82  ? 20.17954  -19.54435 -20.21284 1.000 14.67922  ? 1134 HIS   B CE1  1 
ATOM   437  N  NE2  . HIS   A 1 82  ? 19.45550  -20.09839 -21.17078 1.000 11.13849  ? 1134 HIS   B NE2  1 
ATOM   438  N  N    . ASN   A 1 83  ? 18.45636  -22.69670 -15.28378 1.000 11.15268  ? 1135 ASN   B N    1 
ATOM   439  C  CA   . ASN   A 1 83  ? 17.81551  -22.98081 -14.00672 1.000 16.57504  ? 1135 ASN   B CA   1 
ATOM   440  C  C    . ASN   A 1 83  ? 16.51046  -22.23194 -13.82956 1.000 19.84961  ? 1135 ASN   B C    1 
ATOM   441  O  O    . ASN   A 1 83  ? 16.06156  -22.06003 -12.69251 1.000 24.44209  ? 1135 ASN   B O    1 
ATOM   442  C  CB   . ASN   A 1 83  ? 18.75560  -22.64276 -12.84780 1.000 13.43334  ? 1135 ASN   B CB   1 
ATOM   443  C  CG   . ASN   A 1 83  ? 19.96869  -23.53464 -12.82096 1.000 19.13647  ? 1135 ASN   B CG   1 
ATOM   444  O  OD1  . ASN   A 1 83  ? 19.92475  -24.65463 -13.31900 1.000 20.69218  ? 1135 ASN   B OD1  1 
ATOM   445  N  ND2  . ASN   A 1 83  ? 21.06270  -23.04956 -12.24006 1.000 25.25748  ? 1135 ASN   B ND2  1 
ATOM   446  N  N    . SER   A 1 84  ? 15.91630  -21.74896 -14.91248 1.000 12.97805  ? 1136 SER   B N    1 
ATOM   447  C  CA   . SER   A 1 84  ? 14.58525  -21.16510 -14.85832 1.000 13.16301  ? 1136 SER   B CA   1 
ATOM   448  C  C    . SER   A 1 84  ? 13.99512  -21.30210 -16.24827 1.000 13.50040  ? 1136 SER   B C    1 
ATOM   449  O  O    . SER   A 1 84  ? 14.67706  -21.70400 -17.19035 1.000 14.10259  ? 1136 SER   B O    1 
ATOM   450  C  CB   . SER   A 1 84  ? 14.60815  -19.70211 -14.39627 1.000 12.12331  ? 1136 SER   B CB   1 
ATOM   451  O  OG   . SER   A 1 84  ? 15.46899  -18.91400 -15.20533 1.000 10.57122  ? 1136 SER   B OG   1 
ATOM   452  N  N    . ALA   A 1 85  ? 12.71608  -20.96923 -16.35612 1.000 13.05263  ? 1137 ALA   B N    1 
ATOM   453  C  CA   . ALA   A 1 85  ? 11.98497  -21.17025 -17.59806 1.000 13.46254  ? 1137 ALA   B CA   1 
ATOM   454  C  C    . ALA   A 1 85  ? 12.67578  -20.48714 -18.78210 1.000 14.00492  ? 1137 ALA   B C    1 
ATOM   455  O  O    . ALA   A 1 85  ? 13.11267  -19.33310 -18.69810 1.000 12.24223  ? 1137 ALA   B O    1 
ATOM   456  C  CB   . ALA   A 1 85  ? 10.55493  -20.64840 -17.43989 1.000 9.43378   ? 1137 ALA   B CB   1 
ATOM   457  N  N    . ILE   A 1 86  ? 12.77674  -21.20709 -19.89714 1.000 13.19025  ? 1138 ILE   B N    1 
ATOM   458  C  CA   A ILE   A 1 86  ? 13.23655  -20.58500 -21.12816 0.419 14.91947  ? 1138 ILE   B CA   1 
ATOM   459  C  CA   B ILE   A 1 86  ? 13.23155  -20.59400 -21.13616 0.581 14.95005  ? 1138 ILE   B CA   1 
ATOM   460  C  C    . ILE   A 1 86  ? 12.14340  -19.66509 -21.65502 1.000 14.95202  ? 1138 ILE   B C    1 
ATOM   461  O  O    . ILE   A 1 86  ? 10.97343  -20.05020 -21.74491 1.000 16.25567  ? 1138 ILE   B O    1 
ATOM   462  C  CB   A ILE   A 1 86  ? 13.62655  -21.64993 -22.16224 0.419 13.74112  ? 1138 ILE   B CB   1 
ATOM   463  C  CB   B ILE   A 1 86  ? 13.57655  -21.66793 -22.17724 0.581 13.75099  ? 1138 ILE   B CB   1 
ATOM   464  C  CG1  A ILE   A 1 86  ? 14.82068  -22.45783 -21.65139 0.419 13.71158  ? 1138 ILE   B CG1  1 
ATOM   465  C  CG1  B ILE   A 1 86  ? 14.45272  -22.75087 -21.55737 0.581 13.68402  ? 1138 ILE   B CG1  1 
ATOM   466  C  CG2  A ILE   A 1 86  ? 13.94534  -20.99085 -23.50025 0.419 12.83035  ? 1138 ILE   B CG2  1 
ATOM   467  C  CG2  B ILE   A 1 86  ? 14.26936  -21.02782 -23.37528 0.581 12.80022  ? 1138 ILE   B CG2  1 
ATOM   468  C  CD1  A ILE   A 1 86  ? 15.29469  -23.53575 -22.60448 0.419 13.79851  ? 1138 ILE   B CD1  1 
ATOM   469  C  CD1  B ILE   A 1 86  ? 15.87370  -22.32374 -21.33650 0.581 13.83177  ? 1138 ILE   B CD1  1 
ATOM   470  N  N    . THR   A 1 87  ? 12.51825  -18.43404 -21.98601 1.000 10.92388  ? 1139 THR   B N    1 
ATOM   471  C  CA   . THR   A 1 87  ? 11.54110  -17.48412 -22.49588 1.000 14.89104  ? 1139 THR   B CA   1 
ATOM   472  C  C    . THR   A 1 87  ? 11.54994  -17.38006 -24.00987 1.000 15.43116  ? 1139 THR   B C    1 
ATOM   473  O  O    . THR   A 1 87  ? 10.49485  -17.13214 -24.61176 1.000 16.37050  ? 1139 THR   B O    1 
ATOM   474  C  CB   . THR   A 1 87  ? 11.77603  -16.09012 -21.90385 1.000 13.74895  ? 1139 THR   B CB   1 
ATOM   475  O  OG1  . THR   A 1 87  ? 13.15197  -15.71698 -22.07098 1.000 16.44309  ? 1139 THR   B OG1  1 
ATOM   476  C  CG2  . THR   A 1 87  ? 11.40218  -16.07621 -20.40781 1.000 15.19956  ? 1139 THR   B CG2  1 
ATOM   477  N  N    . HIS   A 1 88  ? 12.70489  -17.58393 -24.63200 1.000 10.51113  ? 1140 HIS   B N    1 
ATOM   478  C  CA   . HIS   A 1 88  ? 12.83472  -17.26986 -26.04300 1.000 15.51203  ? 1140 HIS   B CA   1 
ATOM   479  C  C    . HIS   A 1 88  ? 14.09873  -17.93572 -26.54416 1.000 11.33677  ? 1140 HIS   B C    1 
ATOM   480  O  O    . HIS   A 1 88  ? 15.02583  -18.15866 -25.76326 1.000 11.87133  ? 1140 HIS   B O    1 
ATOM   481  C  CB   . HIS   A 1 88  ? 12.89555  -15.74985 -26.24895 1.000 14.02741  ? 1140 HIS   B CB   1 
ATOM   482  C  CG   . HIS   A 1 88  ? 13.20036  -15.33677 -27.65397 1.000 17.74664  ? 1140 HIS   B CG   1 
ATOM   483  N  ND1  . HIS   A 1 88  ? 14.48830  -15.13863 -28.11009 1.000 14.26338  ? 1140 HIS   B ND1  1 
ATOM   484  C  CD2  . HIS   A 1 88  ? 12.38323  -15.07381 -28.70188 1.000 18.60837  ? 1140 HIS   B CD2  1 
ATOM   485  C  CE1  . HIS   A 1 88  ? 14.45013  -14.77258 -29.38008 1.000 20.43336  ? 1140 HIS   B CE1  1 
ATOM   486  N  NE2  . HIS   A 1 88  ? 13.18509  -14.72569 -29.76295 1.000 18.50955  ? 1140 HIS   B NE2  1 
ATOM   487  N  N    . LEU   A 1 89  ? 14.13963  -18.24167 -27.84417 1.000 9.40606   ? 1141 LEU   B N    1 
ATOM   488  C  CA   . LEU   A 1 89  ? 15.33963  -18.85753 -28.40532 1.000 14.99484  ? 1141 LEU   B CA   1 
ATOM   489  C  C    . LEU   A 1 89  ? 15.42145  -18.57347 -29.90131 1.000 14.67402  ? 1141 LEU   B C    1 
ATOM   490  O  O    . LEU   A 1 89  ? 14.44035  -18.17254 -30.53020 1.000 14.34790  ? 1141 LEU   B O    1 
ATOM   491  C  CB   . LEU   A 1 89  ? 15.37981  -20.36654 -28.12637 1.000 9.14346   ? 1141 LEU   B CB   1 
ATOM   492  C  CG   . LEU   A 1 89  ? 14.22584  -21.23063 -28.61029 1.000 21.60060  ? 1141 LEU   B CG   1 
ATOM   493  C  CD1  . LEU   A 1 89  ? 14.34071  -21.45657 -30.10531 1.000 22.03041  ? 1141 LEU   B CD1  1 
ATOM   494  C  CD2  . LEU   A 1 89  ? 14.21405  -22.56666 -27.85633 1.000 20.30152  ? 1141 LEU   B CD2  1 
ATOM   495  N  N    . GLU   A 1 90  ? 16.62441  -18.75333 -30.45744 1.000 12.82800  ? 1142 GLU   B N    1 
ATOM   496  C  CA   . GLU   A 1 90  ? 16.87724  -18.45226 -31.86446 1.000 11.92189  ? 1142 GLU   B CA   1 
ATOM   497  C  C    . GLU   A 1 90  ? 18.01827  -19.32813 -32.35961 1.000 13.16576  ? 1142 GLU   B C    1 
ATOM   498  O  O    . GLU   A 1 90  ? 19.13032  -19.26304 -31.82072 1.000 13.36979  ? 1142 GLU   B O    1 
ATOM   499  C  CB   . GLU   A 1 90  ? 17.22807  -16.97121 -32.08944 1.000 15.86631  ? 1142 GLU   B CB   1 
ATOM   500  C  CG   . GLU   A 1 90  ? 17.25687  -16.56616 -33.59043 1.000 11.73024  ? 1142 GLU   B CG   1 
ATOM   501  C  CD   . GLU   A 1 90  ? 18.04172  -15.28207 -33.89946 1.000 17.07549  ? 1142 GLU   B CD   1 
ATOM   502  O  OE1  . GLU   A 1 90  ? 18.35773  -14.49807 -32.98447 1.000 16.02421  ? 1142 GLU   B OE1  1 
ATOM   503  O  OE2  . GLU   A 1 90  ? 18.36157  -15.05499 -35.09049 1.000 23.49825  ? 1142 GLU   B OE2  1 
ATOM   504  N  N    . PRO   A 1 91  ? 17.78825  -20.17011 -33.35862 1.000 15.68376  ? 1143 PRO   B N    1 
ATOM   505  C  CA   . PRO   A 1 91  ? 18.90026  -20.90698 -33.96576 1.000 11.03523  ? 1143 PRO   B CA   1 
ATOM   506  C  C    . PRO   A 1 91  ? 19.59007  -20.04788 -35.01080 1.000 15.16871  ? 1143 PRO   B C    1 
ATOM   507  O  O    . PRO   A 1 91  ? 18.98892  -19.13691 -35.58470 1.000 19.97439  ? 1143 PRO   B O    1 
ATOM   508  C  CB   . PRO   A 1 91  ? 18.20631  -22.11503 -34.60873 1.000 15.02007  ? 1143 PRO   B CB   1 
ATOM   509  C  CG   . PRO   A 1 91  ? 16.85023  -21.61215 -34.93457 1.000 19.35225  ? 1143 PRO   B CG   1 
ATOM   510  C  CD   . PRO   A 1 91  ? 16.48125  -20.63022 -33.85250 1.000 9.76526   ? 1143 PRO   B CD   1 
ATOM   511  N  N    . SER   A 1 92  ? 20.87407  -20.32274 -35.23994 1.000 14.26535  ? 1144 SER   B N    1 
ATOM   512  C  CA   . SER   A 1 92  ? 21.54689  -19.66064 -36.34898 1.000 20.94277  ? 1144 SER   B CA   1 
ATOM   513  C  C    . SER   A 1 92  ? 21.06582  -20.27064 -37.65796 1.000 21.90920  ? 1144 SER   B C    1 
ATOM   514  O  O    . SER   A 1 92  ? 20.60293  -21.41768 -37.70295 1.000 20.43299  ? 1144 SER   B O    1 
ATOM   515  C  CB   . SER   A 1 92  ? 23.07492  -19.76149 -36.23214 1.000 15.80049  ? 1144 SER   B CB   1 
ATOM   516  O  OG   . SER   A 1 92  ? 23.55304  -21.09644 -36.35024 1.000 17.11757  ? 1144 SER   B OG   1 
ATOM   517  N  N    . ARG   A 1 93  ? 21.14963  -19.48059 -38.72694 1.000 20.88529  ? 1145 ARG   B N    1 
ATOM   518  C  CA   . ARG   A 1 93  ? 20.67455  -19.97459 -40.01990 1.000 27.37407  ? 1145 ARG   B CA   1 
ATOM   519  C  C    . ARG   A 1 93  ? 21.42563  -21.22450 -40.45903 1.000 24.27552  ? 1145 ARG   B C    1 
ATOM   520  O  O    . ARG   A 1 93  ? 20.85064  -22.08053 -41.13400 1.000 20.85865  ? 1145 ARG   B O    1 
ATOM   521  C  CB   . ARG   A 1 93  ? 20.79133  -18.89454 -41.09288 1.000 23.77360  ? 1145 ARG   B CB   1 
ATOM   522  C  CG   . ARG   A 1 93  ? 19.75124  -17.79864 -40.97573 1.000 29.75479  ? 1145 ARG   B CG   1 
ATOM   523  C  CD   . ARG   A 1 93  ? 19.55003  -17.07462 -42.30768 1.000 30.98517  ? 1145 ARG   B CD   1 
ATOM   524  N  NE   . ARG   A 1 93  ? 20.75992  -16.38548 -42.73278 1.000 27.48766  ? 1145 ARG   B NE   1 
ATOM   525  C  CZ   . ARG   A 1 93  ? 21.18586  -15.24146 -42.21679 1.000 25.53000  ? 1145 ARG   B CZ   1 
ATOM   526  N  NH1  . ARG   A 1 93  ? 20.50590  -14.61756 -41.26369 1.000 24.85423  ? 1145 ARG   B NH1  1 
ATOM   527  N  NH2  . ARG   A 1 93  ? 22.32976  -14.72133 -42.65088 1.000 20.28114  ? 1145 ARG   B NH2  1 
ATOM   528  N  N    . ASP   A 1 94  ? 22.69868  -21.35939 -40.08916 1.000 20.06426  ? 1146 ASP   B N    1 
ATOM   529  C  CA   . ASP   A 1 94  ? 23.47474  -22.50830 -40.53228 1.000 24.35144  ? 1146 ASP   B CA   1 
ATOM   530  C  C    . ASP   A 1 94  ? 23.37796  -23.69734 -39.58032 1.000 26.81393  ? 1146 ASP   B C    1 
ATOM   531  O  O    . ASP   A 1 94  ? 24.08103  -24.69026 -39.78542 1.000 23.15040  ? 1146 ASP   B O    1 
ATOM   532  C  CB   . ASP   A 1 94  ? 24.93768  -22.10614 -40.74642 1.000 30.91760  ? 1146 ASP   B CB   1 
ATOM   533  C  CG   . ASP   A 1 94  ? 25.71780  -21.96111 -39.44449 1.000 35.22720  ? 1146 ASP   B CG   1 
ATOM   534  O  OD1  . ASP   A 1 94  ? 25.16394  -22.21821 -38.35045 1.000 31.64335  ? 1146 ASP   B OD1  1 
ATOM   535  O  OD2  . ASP   A 1 94  ? 26.90276  -21.58100 -39.52460 1.000 30.12751  ? 1146 ASP   B OD2  1 
ATOM   536  N  N    . GLY   A 1 95  ? 22.54006  -23.61246 -38.54323 1.000 29.85999  ? 1147 GLY   B N    1 
ATOM   537  C  CA   . GLY   A 1 95  ? 22.28726  -24.72852 -37.64624 1.000 26.21083  ? 1147 GLY   B CA   1 
ATOM   538  C  C    . GLY   A 1 95  ? 23.42439  -25.10744 -36.71937 1.000 31.36346  ? 1147 GLY   B C    1 
ATOM   539  O  O    . GLY   A 1 95  ? 23.35756  -26.15547 -36.06840 1.000 23.23528  ? 1147 GLY   B O    1 
ATOM   540  N  N    . SER   A 1 96  ? 24.47632  -24.29834 -36.63245 1.000 24.29246  ? 1148 SER   B N    1 
ATOM   541  C  CA   . SER   A 1 96  ? 25.57144  -24.62826 -35.73358 1.000 27.64763  ? 1148 SER   B CA   1 
ATOM   542  C  C    . SER   A 1 96  ? 25.44352  -23.98733 -34.35454 1.000 24.52774  ? 1148 SER   B C    1 
ATOM   543  O  O    . SER   A 1 96  ? 26.14666  -24.42029 -33.43163 1.000 20.61765  ? 1148 SER   B O    1 
ATOM   544  C  CB   . SER   A 1 96  ? 26.90934  -24.21211 -36.35270 1.000 25.40993  ? 1148 SER   B CB   1 
ATOM   545  O  OG   . SER   A 1 96  ? 26.94518  -22.81310 -36.58865 1.000 29.62615  ? 1148 SER   B OG   1 
ATOM   546  N  N    . LEU   A 1 97  ? 24.58144  -22.97442 -34.18541 1.000 18.11551  ? 1149 LEU   B N    1 
ATOM   547  C  CA   . LEU   A 1 97  ? 24.51550  -22.24347 -32.92538 1.000 17.44007  ? 1149 LEU   B CA   1 
ATOM   548  C  C    . LEU   A 1 97  ? 23.07452  -21.99262 -32.51322 1.000 19.85895  ? 1149 LEU   B C    1 
ATOM   549  O  O    . LEU   A 1 97  ? 22.15643  -21.94568 -33.33913 1.000 16.25363  ? 1149 LEU   B O    1 
ATOM   550  C  CB   . LEU   A 1 97  ? 25.24436  -20.90539 -32.99941 1.000 13.70361  ? 1149 LEU   B CB   1 
ATOM   551  C  CG   . LEU   A 1 97  ? 26.73334  -20.97924 -33.31856 1.000 20.38206  ? 1149 LEU   B CG   1 
ATOM   552  C  CD1  . LEU   A 1 97  ? 27.20016  -19.58618 -33.70856 1.000 13.95312  ? 1149 LEU   B CD1  1 
ATOM   553  C  CD2  . LEU   A 1 97  ? 27.53351  -21.53520 -32.12667 1.000 15.29896  ? 1149 LEU   B CD2  1 
ATOM   554  N  N    . LEU   A 1 98  ? 22.89563  -21.80169 -31.20620 1.000 15.63262  ? 1150 LEU   B N    1 
ATOM   555  C  CA   . LEU   A 1 98  ? 21.58766  -21.51384 -30.64005 1.000 18.71655  ? 1150 LEU   B CA   1 
ATOM   556  C  C    . LEU   A 1 98  ? 21.72868  -20.49587 -29.51403 1.000 15.45876  ? 1150 LEU   B C    1 
ATOM   557  O  O    . LEU   A 1 98  ? 22.64977  -20.58180 -28.69113 1.000 15.30443  ? 1150 LEU   B O    1 
ATOM   558  C  CB   . LEU   A 1 98  ? 20.92984  -22.80192 -30.13103 1.000 14.67552  ? 1150 LEU   B CB   1 
ATOM   559  C  CG   . LEU   A 1 98  ? 19.59290  -22.69808 -29.40889 1.000 15.20428  ? 1150 LEU   B CG   1 
ATOM   560  C  CD1  . LEU   A 1 98  ? 18.46678  -22.43515 -30.39677 1.000 13.12398  ? 1150 LEU   B CD1  1 
ATOM   561  C  CD2  . LEU   A 1 98  ? 19.34711  -23.97013 -28.61391 1.000 16.03196  ? 1150 LEU   B CD2  1 
ATOM   562  N  N    . LEU   A 1 99  ? 20.81858  -19.52296 -29.49390 1.000 13.68930  ? 1151 LEU   B N    1 
ATOM   563  C  CA   . LEU   A 1 99  ? 20.69261  -18.58801 -28.38786 1.000 11.88793  ? 1151 LEU   B CA   1 
ATOM   564  C  C    . LEU   A 1 99  ? 19.47473  -18.95016 -27.54674 1.000 17.25210  ? 1151 LEU   B C    1 
ATOM   565  O  O    . LEU   A 1 99  ? 18.40971  -19.27424 -28.07965 1.000 13.11942  ? 1151 LEU   B O    1 
ATOM   566  C  CB   . LEU   A 1 99  ? 20.57241  -17.14800 -28.89579 1.000 12.55684  ? 1151 LEU   B CB   1 
ATOM   567  C  CG   . LEU   A 1 99  ? 21.86830  -16.55085 -29.46190 1.000 15.76478  ? 1151 LEU   B CG   1 
ATOM   568  C  CD1  . LEU   A 1 99  ? 21.57508  -15.32385 -30.35983 1.000 12.22028  ? 1151 LEU   B CD1  1 
ATOM   569  C  CD2  . LEU   A 1 99  ? 22.85338  -16.18580 -28.34299 1.000 9.64671   ? 1151 LEU   B CD2  1 
ATOM   570  N  N    . THR   A 1 100 ? 19.64586  -18.92119 -26.22976 1.000 13.24796  ? 1152 THR   B N    1 
ATOM   571  C  CA   . THR   A 1 100 ? 18.54998  -19.12433 -25.29666 1.000 11.63232  ? 1152 THR   B CA   1 
ATOM   572  C  C    . THR   A 1 100 ? 18.52696  -17.96337 -24.32261 1.000 11.94746  ? 1152 THR   B C    1 
ATOM   573  O  O    . THR   A 1 100 ? 19.57494  -17.39828 -23.99070 1.000 12.05721  ? 1152 THR   B O    1 
ATOM   574  C  CB   . THR   A 1 100 ? 18.68919  -20.43235 -24.49672 1.000 11.38747  ? 1152 THR   B CB   1 
ATOM   575  O  OG1  . THR   A 1 100 ? 20.00825  -20.50824 -23.94486 1.000 13.38721  ? 1152 THR   B OG1  1 
ATOM   576  C  CG2  . THR   A 1 100 ? 18.43922  -21.64134 -25.37774 1.000 7.55828   ? 1152 THR   B CG2  1 
ATOM   577  N  N    . SER   A 1 101 ? 17.32297  -17.61350 -23.87147 1.000 8.69067   ? 1153 SER   B N    1 
ATOM   578  C  CA   . SER   A 1 101 ? 17.14100  -16.68556 -22.76942 1.000 8.73964   ? 1153 SER   B CA   1 
ATOM   579  C  C    . SER   A 1 101 ? 16.23817  -17.32969 -21.72735 1.000 11.14440  ? 1153 SER   B C    1 
ATOM   580  O  O    . SER   A 1 101 ? 15.29320  -18.04377 -22.06628 1.000 11.05873  ? 1153 SER   B O    1 
ATOM   581  C  CB   . SER   A 1 101 ? 16.55082  -15.36060 -23.24931 1.000 9.12108   ? 1153 SER   B CB   1 
ATOM   582  O  OG   . SER   A 1 101 ? 17.42866  -14.78548 -24.20038 1.000 11.93411  ? 1153 SER   B OG   1 
ATOM   583  N  N    . ALA   A 1 102 ? 16.52027  -17.06370 -20.45837 1.000 9.31483   ? 1154 ALA   B N    1 
ATOM   584  C  CA   . ALA   A 1 102 ? 15.78344  -17.66682 -19.36432 1.000 9.74149   ? 1154 ALA   B CA   1 
ATOM   585  C  C    . ALA   A 1 102 ? 14.93841  -16.59092 -18.68119 1.000 10.04467  ? 1154 ALA   B C    1 
ATOM   586  O  O    . ALA   A 1 102 ? 14.70224  -15.51993 -19.24713 1.000 18.83775  ? 1154 ALA   B O    1 
ATOM   587  C  CB   . ALA   A 1 102 ? 16.76661  -18.36475 -18.42144 1.000 10.18614  ? 1154 ALA   B CB   1 
ATOM   588  N  N    . THR   A 1 103 ? 14.46556  -16.88101 -17.47315 1.000 9.45073   ? 1155 THR   B N    1 
ATOM   589  C  CA   . THR   A 1 103 ? 13.52354  -15.99413 -16.79903 1.000 18.50647  ? 1155 THR   B CA   1 
ATOM   590  C  C    . THR   A 1 103 ? 14.19257  -15.13010 -15.73306 1.000 16.77932  ? 1155 THR   B C    1 
ATOM   591  O  O    . THR   A 1 103 ? 14.16644  -13.89910 -15.82202 1.000 13.33386  ? 1155 THR   B O    1 
ATOM   592  C  CB   . THR   A 1 103 ? 12.38368  -16.81526 -16.19294 1.000 14.64240  ? 1155 THR   B CB   1 
ATOM   593  O  OG1  . THR   A 1 103 ? 11.54662  -17.28831 -17.24887 1.000 16.84007  ? 1155 THR   B OG1  1 
ATOM   594  C  CG2  . THR   A 1 103 ? 11.55369  -15.95238 -15.27382 1.000 22.36087  ? 1155 THR   B CG2  1 
ATOM   595  N  N    . TRP   A 1 104 ? 14.79273  -15.74908 -14.71815 1.000 13.97104  ? 1156 TRP   B N    1 
ATOM   596  C  CA   . TRP   A 1 104 ? 15.44576  -14.97806 -13.66819 1.000 16.50907  ? 1156 TRP   B CA   1 
ATOM   597  C  C    . TRP   A 1 104 ? 16.84885  -15.45793 -13.31335 1.000 16.34121  ? 1156 TRP   B C    1 
ATOM   598  O  O    . TRP   A 1 104 ? 17.59584  -14.69088 -12.69640 1.000 19.10968  ? 1156 TRP   B O    1 
ATOM   599  C  CB   . TRP   A 1 104 ? 14.57589  -14.96519 -12.39810 1.000 20.15034  ? 1156 TRP   B CB   1 
ATOM   600  C  CG   . TRP   A 1 104 ? 14.37009  -16.31423 -11.80912 1.000 16.38492  ? 1156 TRP   B CG   1 
ATOM   601  C  CD1  . TRP   A 1 104 ? 13.29415  -17.13833 -11.99204 1.000 20.10506  ? 1156 TRP   B CD1  1 
ATOM   602  C  CD2  . TRP   A 1 104 ? 15.28024  -17.02117 -10.95624 1.000 16.05044  ? 1156 TRP   B CD2  1 
ATOM   603  N  NE1  . TRP   A 1 104 ? 13.48533  -18.32133 -11.31311 1.000 19.19430  ? 1156 TRP   B NE1  1 
ATOM   604  C  CE2  . TRP   A 1 104 ? 14.69240  -18.27124 -10.66323 1.000 16.11174  ? 1156 TRP   B CE2  1 
ATOM   605  C  CE3  . TRP   A 1 104 ? 16.53127  -16.71807 -10.41436 1.000 14.34034  ? 1156 TRP   B CE3  1 
ATOM   606  C  CZ2  . TRP   A 1 104 ? 15.31457  -19.21721 -9.84933  1.000 18.12201  ? 1156 TRP   B CZ2  1 
ATOM   607  C  CZ3  . TRP   A 1 104 ? 17.14944  -17.65604 -9.60546  1.000 14.67519  ? 1156 TRP   B CZ3  1 
ATOM   608  C  CH2  . TRP   A 1 104 ? 16.53959  -18.89610 -9.33444  1.000 17.16841  ? 1156 TRP   B CH2  1 
ATOM   609  N  N    . SER   A 1 105 ? 17.24393  -16.66788 -13.69743 1.000 14.27742  ? 1157 SER   B N    1 
ATOM   610  C  CA   . SER   A 1 105 ? 18.50803  -17.24377 -13.25258 1.000 14.86146  ? 1157 SER   B CA   1 
ATOM   611  C  C    . SER   A 1 105 ? 19.67189  -16.80762 -14.14169 1.000 16.74673  ? 1157 SER   B C    1 
ATOM   612  O  O    . SER   A 1 105 ? 19.52175  -16.61259 -15.35366 1.000 18.38086  ? 1157 SER   B O    1 
ATOM   613  C  CB   . SER   A 1 105 ? 18.41618  -18.77278 -13.22263 1.000 15.08627  ? 1157 SER   B CB   1 
ATOM   614  O  OG   . SER   A 1 105 ? 17.94711  -19.28978 -14.46260 1.000 14.34218  ? 1157 SER   B OG   1 
ATOM   615  N  N    . GLN   A 1 106 ? 20.84894  -16.63953 -13.51780 1.000 14.40644  ? 1158 GLN   B N    1 
ATOM   616  C  CA   . GLN   A 1 106 ? 21.97882  -16.30939 -14.36891 1.000 13.95161  ? 1158 GLN   B CA   1 
ATOM   617  C  C    . GLN   A 1 106 ? 22.78491  -17.56130 -14.69203 1.000 12.40515  ? 1158 GLN   B C    1 
ATOM   618  O  O    . GLN   A 1 106 ? 22.84709  -18.48932 -13.88707 1.000 14.54262  ? 1158 GLN   B O    1 
ATOM   619  C  CB   . GLN   A 1 106 ? 22.88879  -15.28432 -13.69396 1.000 13.51513  ? 1158 GLN   B CB   1 
ATOM   620  C  CG   . GLN   A 1 106 ? 22.19070  -13.98541 -13.31884 1.000 14.29026  ? 1158 GLN   B CG   1 
ATOM   621  C  CD   . GLN   A 1 106 ? 23.07271  -13.11235 -12.44690 1.000 19.28296  ? 1158 GLN   B CD   1 
ATOM   622  O  OE1  . GLN   A 1 106 ? 22.91159  -11.89237 -12.38984 1.000 17.07682  ? 1158 GLN   B OE1  1 
ATOM   623  N  NE2  . GLN   A 1 106 ? 24.01484  -13.74128 -11.76302 1.000 13.11746  ? 1158 GLN   B NE2  1 
ATOM   624  N  N    . PRO   A 1 107 ? 23.39879  -17.60520 -15.88110 1.000 13.31653  ? 1159 PRO   B N    1 
ATOM   625  C  CA   . PRO   A 1 107 ? 23.35859  -16.54416 -16.89306 1.000 10.50768  ? 1159 PRO   B CA   1 
ATOM   626  C  C    . PRO   A 1 107 ? 21.95651  -16.41828 -17.48291 1.000 15.26314  ? 1159 PRO   B C    1 
ATOM   627  O  O    . PRO   A 1 107 ? 21.31759  -17.43633 -17.74488 1.000 11.98930  ? 1159 PRO   B O    1 
ATOM   628  C  CB   . PRO   A 1 107 ? 24.40253  -17.00202 -17.91818 1.000 12.19758  ? 1159 PRO   B CB   1 
ATOM   629  C  CG   . PRO   A 1 107 ? 24.38169  -18.52303 -17.80823 1.000 13.93105  ? 1159 PRO   B CG   1 
ATOM   630  C  CD   . PRO   A 1 107 ? 24.16186  -18.78410 -16.33022 1.000 11.40915  ? 1159 PRO   B CD   1 
ATOM   631  N  N    . LEU   A 1 108 ? 21.45537  -15.19232 -17.71581 1.000 13.09779  ? 1160 LEU   B N    1 
ATOM   632  C  CA   . LEU   A 1 108 ? 20.12129  -15.03643 -18.29367 1.000 11.51754  ? 1160 LEU   B CA   1 
ATOM   633  C  C    . LEU   A 1 108 ? 20.07618  -15.41638 -19.77768 1.000 10.04619  ? 1160 LEU   B C    1 
ATOM   634  O  O    . LEU   A 1 108 ? 19.02717  -15.83446 -20.26959 1.000 11.34613  ? 1160 LEU   B O    1 
ATOM   635  C  CB   . LEU   A 1 108 ? 19.62118  -13.60549 -18.08157 1.000 11.51874  ? 1160 LEU   B CB   1 
ATOM   636  C  CG   . LEU   A 1 108 ? 19.16929  -13.28558 -16.64951 1.000 15.16545  ? 1160 LEU   B CG   1 
ATOM   637  C  CD1  . LEU   A 1 108 ? 19.00916  -11.77960 -16.45844 1.000 14.15437  ? 1160 LEU   B CD1  1 
ATOM   638  C  CD2  . LEU   A 1 108 ? 17.86240  -14.02972 -16.28240 1.000 12.88832  ? 1160 LEU   B CD2  1 
ATOM   639  N  N    . SER   A 1 109 ? 21.17509  -15.29725 -20.51479 1.000 11.10020  ? 1161 SER   B N    1 
ATOM   640  C  CA   . SER   A 1 109 ? 21.19100  -15.80519 -21.88281 1.000 9.44172   ? 1161 SER   B CA   1 
ATOM   641  C  C    . SER   A 1 109 ? 22.45606  -16.62006 -22.11597 1.000 9.47544   ? 1161 SER   B C    1 
ATOM   642  O  O    . SER   A 1 109 ? 23.46011  -16.45799 -21.42006 1.000 13.62672  ? 1161 SER   B O    1 
ATOM   643  C  CB   . SER   A 1 109 ? 21.08678  -14.67817 -22.92375 1.000 8.54363   ? 1161 SER   B CB   1 
ATOM   644  O  OG   . SER   A 1 109 ? 19.84373  -13.99729 -22.81260 1.000 11.82632  ? 1161 SER   B OG   1 
ATOM   645  N  N    . ALA   A 1 110 ? 22.39504  -17.50803 -23.10299 1.000 8.10650   ? 1162 ALA   B N    1 
ATOM   646  C  CA   . ALA   A 1 110 ? 23.54609  -18.34491 -23.41414 1.000 9.06884   ? 1162 ALA   B CA   1 
ATOM   647  C  C    . ALA   A 1 110 ? 23.59797  -18.63185 -24.90816 1.000 11.63165  ? 1162 ALA   B C    1 
ATOM   648  O  O    . ALA   A 1 110 ? 22.59988  -18.51292 -25.62405 1.000 10.16073  ? 1162 ALA   B O    1 
ATOM   649  C  CB   . ALA   A 1 110 ? 23.52430  -19.66294 -22.62819 1.000 9.49538   ? 1162 ALA   B CB   1 
ATOM   650  N  N    . LEU   A 1 111 ? 24.79196  -19.01372 -25.36129 1.000 12.28895  ? 1163 LEU   B N    1 
ATOM   651  C  CA   . LEU   A 1 111 ? 25.06286  -19.43464 -26.72934 1.000 13.59217  ? 1163 LEU   B CA   1 
ATOM   652  C  C    . LEU   A 1 111 ? 25.56400  -20.87459 -26.70044 1.000 12.38784  ? 1163 LEU   B C    1 
ATOM   653  O  O    . LEU   A 1 111 ? 26.52011  -21.18452 -25.98055 1.000 17.39525  ? 1163 LEU   B O    1 
ATOM   654  C  CB   . LEU   A 1 111 ? 26.09570  -18.51451 -27.38541 1.000 8.01713   ? 1163 LEU   B CB   1 
ATOM   655  C  CG   . LEU   A 1 111 ? 26.51459  -18.85042 -28.81846 1.000 12.67904  ? 1163 LEU   B CG   1 
ATOM   656  C  CD1  . LEU   A 1 111 ? 25.35346  -18.62150 -29.80734 1.000 13.70817  ? 1163 LEU   B CD1  1 
ATOM   657  C  CD2  . LEU   A 1 111 ? 27.77347  -18.05128 -29.23256 1.000 11.82379  ? 1163 LEU   B CD2  1 
ATOM   658  N  N    . TRP   A 1 112 ? 24.91101  -21.74963 -27.46740 1.000 13.99676  ? 1164 TRP   B N    1 
ATOM   659  C  CA   . TRP   A 1 112 ? 25.18915  -23.18560 -27.47148 1.000 17.20570  ? 1164 TRP   B CA   1 
ATOM   660  C  C    . TRP   A 1 112 ? 25.66906  -23.65050 -28.84355 1.000 20.69673  ? 1164 TRP   B C    1 
ATOM   661  O  O    . TRP   A 1 112 ? 25.15791  -23.19652 -29.87648 1.000 20.63367  ? 1164 TRP   B O    1 
ATOM   662  C  CB   . TRP   A 1 112 ? 23.93927  -23.98874 -27.07938 1.000 14.00651  ? 1164 TRP   B CB   1 
ATOM   663  C  CG   . TRP   A 1 112 ? 23.23634  -23.43085 -25.87029 1.000 15.88309  ? 1164 TRP   B CG   1 
ATOM   664  C  CD1  . TRP   A 1 112 ? 22.29725  -22.43894 -25.84916 1.000 16.57417  ? 1164 TRP   B CD1  1 
ATOM   665  C  CD2  . TRP   A 1 112 ? 23.44052  -23.81988 -24.50633 1.000 17.29752  ? 1164 TRP   B CD2  1 
ATOM   666  N  NE1  . TRP   A 1 112 ? 21.89935  -22.19403 -24.55211 1.000 17.41840  ? 1164 TRP   B NE1  1 
ATOM   667  C  CE2  . TRP   A 1 112 ? 22.58352  -23.03199 -23.71221 1.000 13.22018  ? 1164 TRP   B CE2  1 
ATOM   668  C  CE3  . TRP   A 1 112 ? 24.25868  -24.76582 -23.88245 1.000 16.26322  ? 1164 TRP   B CE3  1 
ATOM   669  C  CZ2  . TRP   A 1 112 ? 22.53368  -23.15305 -22.32221 1.000 12.49440  ? 1164 TRP   B CZ2  1 
ATOM   670  C  CZ3  . TRP   A 1 112 ? 24.19683  -24.88988 -22.50844 1.000 15.49963  ? 1164 TRP   B CZ3  1 
ATOM   671  C  CH2  . TRP   A 1 112 ? 23.34183  -24.08499 -21.74433 1.000 16.09455  ? 1164 TRP   B CH2  1 
ATOM   672  N  N    . GLY   A 1 113 ? 26.63615  -24.56441 -28.84668 1.000 19.35894  ? 1165 GLY   B N    1 
ATOM   673  C  CA   . GLY   A 1 113 ? 27.07908  -25.21332 -30.07075 1.000 15.46321  ? 1165 GLY   B CA   1 
ATOM   674  C  C    . GLY   A 1 113 ? 26.23718  -26.44239 -30.34971 1.000 30.92079  ? 1165 GLY   B C    1 
ATOM   675  O  O    . GLY   A 1 113 ? 25.96835  -27.23845 -29.44371 1.000 23.98002  ? 1165 GLY   B O    1 
ATOM   676  N  N    . MET   A 1 114 ? 25.82006  -26.58739 -31.61367 1.000 29.11875  ? 1166 MET   B N    1 
ATOM   677  C  CA   . MET   A 1 114 ? 24.92612  -27.67046 -32.01562 1.000 33.30074  ? 1166 MET   B CA   1 
ATOM   678  C  C    . MET   A 1 114 ? 25.58912  -28.61836 -33.00472 1.000 35.53567  ? 1166 MET   B C    1 
ATOM   679  O  O    . MET   A 1 114 ? 24.90213  -29.40140 -33.66668 1.000 44.74955  ? 1166 MET   B O    1 
ATOM   680  C  CB   . MET   A 1 114 ? 23.63601  -27.10257 -32.60547 1.000 31.20212  ? 1166 MET   B CB   1 
ATOM   681  C  CG   . MET   A 1 114 ? 23.05998  -25.97665 -31.76537 1.000 27.51149  ? 1166 MET   B CG   1 
ATOM   682  S  SD   . MET   A 1 114 ? 21.30805  -26.19684 -31.35819 1.000 34.76709  ? 1166 MET   B SD   1 
ATOM   683  C  CE   . MET   A 1 114 ? 20.54587  -26.08786 -32.94811 1.000 26.49252  ? 1166 MET   B CE   1 
ATOM   684  N  N    . LYS   A 1 115 ? 26.91010  -28.56323 -33.12686 1.000 35.12289  ? 1167 LYS   B N    1 
ATOM   685  C  CA   . LYS   A 1 115 ? 27.63610  -29.46212 -34.01296 1.000 38.12998  ? 1167 LYS   B CA   1 
ATOM   686  C  C    . LYS   A 1 115 ? 28.07630  -30.68111 -33.22005 1.000 49.14400  ? 1167 LYS   B C    1 
ATOM   687  O  O    . LYS   A 1 115 ? 28.73339  -30.54808 -32.18211 1.000 54.92302  ? 1167 LYS   B O    1 
ATOM   688  C  CB   . LYS   A 1 115 ? 28.84296  -28.75698 -34.63706 1.000 46.95091  ? 1167 LYS   B CB   1 
ATOM   689  C  CG   . LYS   A 1 115 ? 28.47975  -27.78398 -35.74199 1.000 44.89321  ? 1167 LYS   B CG   1 
ATOM   690  C  CD   . LYS   A 1 115 ? 29.69063  -27.34783 -36.55210 1.000 55.61474  ? 1167 LYS   B CD   1 
ATOM   691  C  CE   . LYS   A 1 115 ? 30.47459  -26.24478 -35.86014 1.000 49.38471  ? 1167 LYS   B CE   1 
ATOM   692  N  NZ   . LYS   A 1 115 ? 31.40443  -25.58465 -36.82121 1.000 46.82152  ? 1167 LYS   B NZ   1 
ATOM   693  N  N    . SER   A 1 116 ? 27.69936  -31.86313 -33.70306 1.000 40.90974  ? 1168 SER   B N    1 
ATOM   694  C  CA   . SER   A 1 116 ? 27.98856  -33.09913 -32.98913 1.000 51.80775  ? 1168 SER   B CA   1 
ATOM   695  C  C    . SER   A 1 116 ? 27.45970  -33.02423 -31.56107 1.000 49.42479  ? 1168 SER   B C    1 
ATOM   696  O  O    . SER   A 1 116 ? 26.33777  -33.46435 -31.28197 1.000 65.42195  ? 1168 SER   B O    1 
ATOM   697  C  CB   . SER   A 1 116 ? 29.49459  -33.39598 -32.99430 1.000 49.64772  ? 1168 SER   B CB   1 
ATOM   698  O  OG   . SER   A 1 116 ? 30.23155  -32.38293 -32.33033 1.000 56.79101  ? 1168 SER   B OG   1 
ATOM   699  N  N    . VAL   A 1 117 ? 28.24773  -32.45518 -30.65613 1.000 47.42916  ? 1169 VAL   B N    1 
ATOM   700  C  CA   . VAL   A 1 117 ? 27.88987  -32.38027 -29.24609 1.000 40.87565  ? 1169 VAL   B CA   1 
ATOM   701  C  C    . VAL   A 1 117 ? 27.29077  -31.00934 -28.94898 1.000 44.71326  ? 1169 VAL   B C    1 
ATOM   702  O  O    . VAL   A 1 117 ? 27.70561  -29.98828 -29.51899 1.000 39.43914  ? 1169 VAL   B O    1 
ATOM   703  C  CB   . VAL   A 1 117 ? 29.10899  -32.66418 -28.34923 1.000 48.05783  ? 1169 VAL   B CB   1 
ATOM   704  C  CG1  . VAL   A 1 117 ? 30.01288  -31.44110 -28.27928 1.000 47.46017  ? 1169 VAL   B CG1  1 
ATOM   705  C  CG2  . VAL   A 1 117 ? 28.65918  -33.10828 -26.96420 1.000 36.63274  ? 1169 VAL   B CG2  1 
ATOM   706  N  N    . PHE   A 1 118 ? 26.29986  -30.99847 -28.06188 1.000 36.47753  ? 1170 PHE   B N    1 
ATOM   707  C  CA   . PHE   A 1 118 ? 25.60178  -29.79855 -27.62977 1.000 29.59782  ? 1170 PHE   B CA   1 
ATOM   708  C  C    . PHE   A 1 118 ? 26.23687  -29.33254 -26.33081 1.000 30.79848  ? 1170 PHE   B C    1 
ATOM   709  O  O    . PHE   A 1 118 ? 26.32805  -30.10756 -25.37385 1.000 31.31973  ? 1170 PHE   B O    1 
ATOM   710  C  CB   . PHE   A 1 118 ? 24.11583  -30.09771 -27.43862 1.000 21.20466  ? 1170 PHE   B CB   1 
ATOM   711  C  CG   . PHE   A 1 118 ? 23.28176  -28.91580 -26.99850 1.000 21.30250  ? 1170 PHE   B CG   1 
ATOM   712  C  CD1  . PHE   A 1 118 ? 23.10287  -28.62987 -25.65147 1.000 20.46347  ? 1170 PHE   B CD1  1 
ATOM   713  C  CD2  . PHE   A 1 118 ? 22.60859  -28.14084 -27.93240 1.000 27.20016  ? 1170 PHE   B CD2  1 
ATOM   714  C  CE1  . PHE   A 1 118 ? 22.31081  -27.55996 -25.24835 1.000 22.15043  ? 1170 PHE   B CE1  1 
ATOM   715  C  CE2  . PHE   A 1 118 ? 21.80553  -27.07293 -27.53428 1.000 28.58002  ? 1170 PHE   B CE2  1 
ATOM   716  C  CZ   . PHE   A 1 118 ? 21.65964  -26.78099 -26.18625 1.000 14.16660  ? 1170 PHE   B CZ   1 
ATOM   717  N  N    . ASP   A 1 119 ? 26.69075  -28.08250 -26.29882 1.000 22.18338  ? 1171 ASP   B N    1 
ATOM   718  C  CA   . ASP   A 1 119 ? 27.23383  -27.54249 -25.06085 1.000 32.89371  ? 1171 ASP   B CA   1 
ATOM   719  C  C    . ASP   A 1 119 ? 27.34366  -26.02747 -25.19181 1.000 28.54715  ? 1171 ASP   B C    1 
ATOM   720  O  O    . ASP   A 1 119 ? 27.12650  -25.45745 -26.26377 1.000 20.07977  ? 1171 ASP   B O    1 
ATOM   721  C  CB   . ASP   A 1 119 ? 28.58392  -28.17737 -24.70901 1.000 29.76703  ? 1171 ASP   B CB   1 
ATOM   722  C  CG   . ASP   A 1 119 ? 29.60580  -28.02123 -25.80611 1.000 35.80330  ? 1171 ASP   B CG   1 
ATOM   723  O  OD1  . ASP   A 1 119 ? 29.46662  -27.09521 -26.63906 1.000 36.75720  ? 1171 ASP   B OD1  1 
ATOM   724  O  OD2  . ASP   A 1 119 ? 30.54487  -28.84313 -25.84224 1.000 45.68182  ? 1171 ASP   B OD2  1 
ATOM   725  N  N    . MET   A 1 120 ? 27.67172  -25.38448 -24.07482 1.000 18.87993  ? 1172 MET   B N    1 
ATOM   726  C  CA   . MET   A 1 120 ? 27.70958  -23.93148 -24.02577 1.000 23.67905  ? 1172 MET   B CA   1 
ATOM   727  C  C    . MET   A 1 120 ? 29.01047  -23.42733 -24.63589 1.000 21.57504  ? 1172 MET   B C    1 
ATOM   728  O  O    . MET   A 1 120 ? 30.08755  -23.94523 -24.33101 1.000 22.26456  ? 1172 MET   B O    1 
ATOM   729  C  CB   . MET   A 1 120 ? 27.56268  -23.44354 -22.58374 1.000 17.58585  ? 1172 MET   B CB   1 
ATOM   730  C  CG   . MET   A 1 120 ? 27.60155  -21.93855 -22.42469 1.000 13.45775  ? 1172 MET   B CG   1 
ATOM   731  S  SD   . MET   A 1 120 ? 27.44968  -21.48562 -20.70065 1.000 19.86817  ? 1172 MET   B SD   1 
ATOM   732  C  CE   . MET   A 1 120 ? 25.73070  -21.43980 -20.45848 1.000 15.01540  ? 1172 MET   B CE   1 
ATOM   733  N  N    . LYS   A 1 121 ? 28.90428  -22.44131 -25.52784 1.000 18.90664  ? 1173 LYS   B N    1 
ATOM   734  C  CA   . LYS   A 1 121 ? 30.08916  -21.75317 -26.02094 1.000 15.50389  ? 1173 LYS   B CA   1 
ATOM   735  C  C    . LYS   A 1 121 ? 30.35612  -20.49818 -25.20492 1.000 13.43959  ? 1173 LYS   B C    1 
ATOM   736  O  O    . LYS   A 1 121 ? 31.48614  -20.26708 -24.76903 1.000 16.46082  ? 1173 LYS   B O    1 
ATOM   737  C  CB   . LYS   A 1 121 ? 29.93297  -21.39213 -27.50291 1.000 17.99745  ? 1173 LYS   B CB   1 
ATOM   738  C  CG   . LYS   A 1 121 ? 29.67700  -22.57613 -28.41392 1.000 21.25411  ? 1173 LYS   B CG   1 
ATOM   739  C  CD   . LYS   A 1 121 ? 30.68713  -23.67504 -28.13807 1.000 41.62704  ? 1173 LYS   B CD   1 
ATOM   740  C  CE   . LYS   A 1 121 ? 31.71703  -23.78690 -29.25018 1.000 38.13545  ? 1173 LYS   B CE   1 
ATOM   741  N  NZ   . LYS   A 1 121 ? 31.06995  -24.26391 -30.49313 1.000 44.39589  ? 1173 LYS   B NZ   1 
ATOM   742  N  N    . HIS   A 1 122 ? 29.31907  -19.69629 -24.97578 1.000 15.31506  ? 1174 HIS   B N    1 
ATOM   743  C  CA   . HIS   A 1 122 ? 29.44502  -18.46230 -24.21175 1.000 15.02173  ? 1174 HIS   B CA   1 
ATOM   744  C  C    . HIS   A 1 122 ? 28.15208  -18.21045 -23.45261 1.000 16.80910  ? 1174 HIS   B C    1 
ATOM   745  O  O    . HIS   A 1 122 ? 27.11111  -18.81355 -23.73152 1.000 13.38646  ? 1174 HIS   B O    1 
ATOM   746  C  CB   . HIS   A 1 122 ? 29.77481  -17.26224 -25.10774 1.000 10.31700  ? 1174 HIS   B CB   1 
ATOM   747  C  CG   . HIS   A 1 122 ? 31.07775  -17.39308 -25.81988 1.000 12.45355  ? 1174 HIS   B CG   1 
ATOM   748  N  ND1  . HIS   A 1 122 ? 32.28482  -17.37999 -25.16000 1.000 14.41129  ? 1174 HIS   B ND1  1 
ATOM   749  C  CD2  . HIS   A 1 122 ? 31.36664  -17.56301 -27.13391 1.000 12.89685  ? 1174 HIS   B CD2  1 
ATOM   750  C  CE1  . HIS   A 1 122 ? 33.26375  -17.53686 -26.03411 1.000 17.69510  ? 1174 HIS   B CE1  1 
ATOM   751  N  NE2  . HIS   A 1 122 ? 32.73363  -17.64587 -27.24006 1.000 17.88726  ? 1174 HIS   B NE2  1 
ATOM   752  N  N    . SER   A 1 123 ? 28.23409  -17.30848 -22.48358 1.000 10.65956  ? 1175 SER   B N    1 
ATOM   753  C  CA   . SER   A 1 123 ? 27.08213  -16.95062 -21.67945 1.000 13.84510  ? 1175 SER   B CA   1 
ATOM   754  C  C    . SER   A 1 123 ? 27.07201  -15.43963 -21.49840 1.000 17.58303  ? 1175 SER   B C    1 
ATOM   755  O  O    . SER   A 1 123 ? 28.11894  -14.78653 -21.52748 1.000 11.38147  ? 1175 SER   B O    1 
ATOM   756  C  CB   . SER   A 1 123 ? 27.11034  -17.65667 -20.31848 1.000 17.92328  ? 1175 SER   B CB   1 
ATOM   757  O  OG   . SER   A 1 123 ? 28.30638  -17.32858 -19.62259 1.000 19.37056  ? 1175 SER   B OG   1 
ATOM   758  N  N    . PHE   A 1 124 ? 25.87697  -14.88676 -21.30025 1.000 16.13783  ? 1176 PHE   B N    1 
ATOM   759  C  CA   . PHE   A 1 124 ? 25.67784  -13.44278 -21.19018 1.000 17.64277  ? 1176 PHE   B CA   1 
ATOM   760  C  C    . PHE   A 1 124 ? 24.86095  -13.26591 -19.91909 1.000 14.61574  ? 1176 PHE   B C    1 
ATOM   761  O  O    . PHE   A 1 124 ? 23.63497  -13.39703 -19.93497 1.000 12.56417  ? 1176 PHE   B O    1 
ATOM   762  C  CB   . PHE   A 1 124 ? 24.96766  -12.88680 -22.42909 1.000 13.27403  ? 1176 PHE   B CB   1 
ATOM   763  C  CG   . PHE   A 1 124 ? 25.47358  -13.46171 -23.73616 1.000 10.95400  ? 1176 PHE   B CG   1 
ATOM   764  C  CD1  . PHE   A 1 124 ? 26.63047  -12.98057 -24.32426 1.000 12.03298  ? 1176 PHE   B CD1  1 
ATOM   765  C  CD2  . PHE   A 1 124 ? 24.77261  -14.46675 -24.38113 1.000 11.41330  ? 1176 PHE   B CD2  1 
ATOM   766  C  CE1  . PHE   A 1 124 ? 27.08340  -13.50648 -25.53233 1.000 12.60885  ? 1176 PHE   B CE1  1 
ATOM   767  C  CE2  . PHE   A 1 124 ? 25.21254  -14.99467 -25.58019 1.000 12.24633  ? 1176 PHE   B CE2  1 
ATOM   768  C  CZ   . PHE   A 1 124 ? 26.37044  -14.51753 -26.15729 1.000 18.85032  ? 1176 PHE   B CZ   1 
ATOM   769  N  N    . THR   A 1 125 ? 25.53604  -13.00388 -18.80315 1.000 16.36947  ? 1177 THR   B N    1 
ATOM   770  C  CA   . THR   A 1 125 ? 24.89820  -13.31399 -17.53110 1.000 17.63462  ? 1177 THR   B CA   1 
ATOM   771  C  C    . THR   A 1 125 ? 23.70614  -12.40412 -17.23994 1.000 14.05431  ? 1177 THR   B C    1 
ATOM   772  O  O    . THR   A 1 125 ? 22.72425  -12.86723 -16.65686 1.000 18.69059  ? 1177 THR   B O    1 
ATOM   773  C  CB   . THR   A 1 125 ? 25.92732  -13.29893 -16.37920 1.000 23.29157  ? 1177 THR   B CB   1 
ATOM   774  O  OG1  . THR   A 1 125 ? 25.64931  -12.23299 -15.46413 1.000 25.61407  ? 1177 THR   B OG1  1 
ATOM   775  C  CG2  . THR   A 1 125 ? 27.35226  -13.20877 -16.90335 1.000 14.56964  ? 1177 THR   B CG2  1 
ATOM   776  N  N    . GLU   A 1 126 ? 23.72898  -11.14010 -17.67090 1.000 12.08884  ? 1178 GLU   B N    1 
ATOM   777  C  CA   . GLU   A 1 126 ? 22.64892  -10.21922 -17.32275 1.000 16.70998  ? 1178 GLU   B CA   1 
ATOM   778  C  C    . GLU   A 1 126 ? 21.72577  -9.83027  -18.47665 1.000 16.15453  ? 1178 GLU   B C    1 
ATOM   779  O  O    . GLU   A 1 126 ? 20.78971  -9.05137  -18.25252 1.000 17.07214  ? 1178 GLU   B O    1 
ATOM   780  C  CB   . GLU   A 1 126 ? 23.23086  -8.94718  -16.69377 1.000 21.61227  ? 1178 GLU   B CB   1 
ATOM   781  C  CG   . GLU   A 1 126 ? 23.89202  -9.19717  -15.34984 1.000 18.88734  ? 1178 GLU   B CG   1 
ATOM   782  C  CD   . GLU   A 1 126 ? 24.11198  -7.91317  -14.57382 1.000 32.83517  ? 1178 GLU   B CD   1 
ATOM   783  O  OE1  . GLU   A 1 126 ? 24.85684  -7.04608  -15.08487 1.000 31.34539  ? 1178 GLU   B OE1  1 
ATOM   784  O  OE2  . GLU   A 1 126 ? 23.51808  -7.76627  -13.47675 1.000 33.43921  ? 1178 GLU   B OE2  1 
ATOM   785  N  N    . ASP   A 1 127 ? 21.93969  -10.33920 -19.69069 1.000 12.31185  ? 1179 ASP   B N    1 
ATOM   786  C  CA   . ASP   A 1 127 ? 21.06954  -9.99524  -20.82258 1.000 11.98237  ? 1179 ASP   B CA   1 
ATOM   787  C  C    . ASP   A 1 127 ? 19.83563  -10.90037 -20.81249 1.000 13.14528  ? 1179 ASP   B C    1 
ATOM   788  O  O    . ASP   A 1 127 ? 19.95973  -12.11535 -21.00855 1.000 10.90913  ? 1179 ASP   B O    1 
ATOM   789  C  CB   . ASP   A 1 127 ? 21.84042  -10.12512 -22.13667 1.000 9.83143   ? 1179 ASP   B CB   1 
ATOM   790  C  CG   . ASP   A 1 127 ? 23.04932  -9.21400  -22.18976 1.000 16.86916  ? 1179 ASP   B CG   1 
ATOM   791  O  OD1  . ASP   A 1 127 ? 22.86220  -7.99002  -22.22070 1.000 20.55371  ? 1179 ASP   B OD1  1 
ATOM   792  O  OD2  . ASP   A 1 127 ? 24.19038  -9.71089  -22.14589 1.000 24.11803  ? 1179 ASP   B OD2  1 
ATOM   793  N  N    A HIS   A 1 128 ? 18.65660  -10.30549 -20.56835 0.464 12.71985  ? 1180 HIS   B N    1 
ATOM   794  N  N    B HIS   A 1 128 ? 18.65060  -10.32449 -20.58735 0.536 12.70064  ? 1180 HIS   B N    1 
ATOM   795  C  CA   A HIS   A 1 128 ? 17.38767  -11.03561 -20.57624 0.464 12.85753  ? 1180 HIS   B CA   1 
ATOM   796  C  CA   B HIS   A 1 128 ? 17.41967  -11.11361 -20.58625 0.536 12.83995  ? 1180 HIS   B CA   1 
ATOM   797  C  C    A HIS   A 1 128 ? 16.96857  -11.46960 -21.98222 0.464 14.18496  ? 1180 HIS   B C    1 
ATOM   798  C  C    B HIS   A 1 128 ? 16.89056  -11.39361 -21.99121 0.536 14.19453  ? 1180 HIS   B C    1 
ATOM   799  O  O    A HIS   A 1 128 ? 16.10764  -12.34668 -22.11616 0.464 12.36255  ? 1180 HIS   B O    1 
ATOM   800  O  O    B HIS   A 1 128 ? 15.89161  -12.10870 -22.13313 0.536 12.25131  ? 1180 HIS   B O    1 
ATOM   801  C  CB   A HIS   A 1 128 ? 16.25265  -10.17575 -19.97510 0.464 13.49890  ? 1180 HIS   B CB   1 
ATOM   802  C  CB   B HIS   A 1 128 ? 16.32469  -10.42475 -19.74411 0.536 13.48010  ? 1180 HIS   B CB   1 
ATOM   803  C  CG   A HIS   A 1 128 ? 16.27079  -10.05280 -18.47609 0.464 16.54930  ? 1180 HIS   B CG   1 
ATOM   804  C  CG   B HIS   A 1 128 ? 16.02151  -9.01376  -20.15303 0.536 14.86693  ? 1180 HIS   B CG   1 
ATOM   805  N  ND1  A HIS   A 1 128 ? 15.45194  -10.80091 -17.65504 0.464 18.80824  ? 1180 HIS   B ND1  1 
ATOM   806  N  ND1  B HIS   A 1 128 ? 16.42448  -7.91975  -19.41403 0.536 17.79451  ? 1180 HIS   B ND1  1 
ATOM   807  C  CD2  A HIS   A 1 128 ? 16.96479  -9.22676  -17.65413 0.464 16.43100  ? 1180 HIS   B CD2  1 
ATOM   808  C  CD2  B HIS   A 1 128 ? 15.35035  -8.51679  -21.21894 0.536 12.97646  ? 1180 HIS   B CD2  1 
ATOM   809  C  CE1  A HIS   A 1 128 ? 15.66304  -10.46494 -16.39405 0.464 17.39232  ? 1180 HIS   B CE1  1 
ATOM   810  C  CE1  B HIS   A 1 128 ? 16.01831  -6.81277  -20.00995 0.536 10.67699  ? 1180 HIS   B CE1  1 
ATOM   811  N  NE2  A HIS   A 1 128 ? 16.57795  -9.51185  -16.36610 0.464 11.46308  ? 1180 HIS   B NE2  1 
ATOM   812  N  NE2  B HIS   A 1 128 ? 15.36423  -7.14679  -21.10589 0.536 11.48606  ? 1180 HIS   B NE2  1 
ATOM   813  N  N    . TYR   A 1 129 ? 17.53640  -10.86851 -23.02825 1.000 13.22128  ? 1181 TYR   B N    1 
ATOM   814  C  CA   . TYR   A 1 129 ? 17.12929  -11.13950 -24.40022 1.000 13.46517  ? 1181 TYR   B CA   1 
ATOM   815  C  C    . TYR   A 1 129 ? 18.34518  -11.02035 -25.30734 1.000 14.16609  ? 1181 TYR   B C    1 
ATOM   816  O  O    . TYR   A 1 129 ? 19.19212  -10.14627 -25.09340 1.000 12.11698  ? 1181 TYR   B O    1 
ATOM   817  C  CB   . TYR   A 1 129 ? 16.02514  -10.16259 -24.83707 1.000 12.26599  ? 1181 TYR   B CB   1 
ATOM   818  C  CG   . TYR   A 1 129 ? 15.49602  -10.37659 -26.24003 1.000 15.25276  ? 1181 TYR   B CG   1 
ATOM   819  C  CD1  . TYR   A 1 129 ? 14.44408  -11.24669 -26.48395 1.000 16.13487  ? 1181 TYR   B CD1  1 
ATOM   820  C  CD2  . TYR   A 1 129 ? 16.01984  -9.65950  -27.31505 1.000 15.75773  ? 1181 TYR   B CD2  1 
ATOM   821  C  CE1  . TYR   A 1 129 ? 13.95497  -11.43269 -27.77091 1.000 16.88684  ? 1181 TYR   B CE1  1 
ATOM   822  C  CE2  . TYR   A 1 129 ? 15.53373  -9.82751  -28.59501 1.000 14.47470  ? 1181 TYR   B CE2  1 
ATOM   823  C  CZ   . TYR   A 1 129 ? 14.50579  -10.71760 -28.82094 1.000 18.77422  ? 1181 TYR   B CZ   1 
ATOM   824  O  OH   . TYR   A 1 129 ? 14.02767  -10.88260 -30.10889 1.000 20.70992  ? 1181 TYR   B OH   1 
ATOM   825  N  N    . VAL   A 1 130 ? 18.43116  -11.89730 -26.31138 1.000 11.33197  ? 1182 VAL   B N    1 
ATOM   826  C  CA   . VAL   A 1 130 ? 19.54007  -11.90016 -27.26350 1.000 12.69670  ? 1182 VAL   B CA   1 
ATOM   827  C  C    . VAL   A 1 130 ? 19.04696  -12.27916 -28.65646 1.000 12.55833  ? 1182 VAL   B C    1 
ATOM   828  O  O    . VAL   A 1 130 ? 18.12002  -13.07924 -28.80739 1.000 11.22299  ? 1182 VAL   B O    1 
ATOM   829  C  CB   . VAL   A 1 130 ? 20.66321  -12.87007 -26.83465 1.000 10.17431  ? 1182 VAL   B CB   1 
ATOM   830  C  CG1  . VAL   A 1 130 ? 21.37127  -12.32604 -25.64270 1.000 6.60390   ? 1182 VAL   B CG1  1 
ATOM   831  C  CG2  . VAL   A 1 130 ? 20.07837  -14.24913 -26.53664 1.000 8.86189   ? 1182 VAL   B CG2  1 
ATOM   832  N  N    . GLU   A 1 131 ? 19.68980  -11.69606 -29.67950 1.000 8.77304   ? 1183 GLU   B N    1 
ATOM   833  C  CA   . GLU   A 1 131 ? 19.47569  -12.05103 -31.07449 1.000 9.55768   ? 1183 GLU   B CA   1 
ATOM   834  C  C    . GLU   A 1 131 ? 20.81563  -12.14087 -31.78864 1.000 11.94382  ? 1183 GLU   B C    1 
ATOM   835  O  O    . GLU   A 1 131 ? 21.77259  -11.44979 -31.42971 1.000 12.73057  ? 1183 GLU   B O    1 
ATOM   836  C  CB   . GLU   A 1 131 ? 18.63251  -11.02308 -31.84137 1.000 14.97371  ? 1183 GLU   B CB   1 
ATOM   837  C  CG   . GLU   A 1 131 ? 17.26254  -10.75124 -31.28822 1.000 17.13207  ? 1183 GLU   B CG   1 
ATOM   838  C  CD   . GLU   A 1 131 ? 16.54935  -9.66428  -32.08411 1.000 23.17691  ? 1183 GLU   B CD   1 
ATOM   839  O  OE1  . GLU   A 1 131 ? 17.19820  -9.03418  -32.97115 1.000 16.64148  ? 1183 GLU   B OE1  1 
ATOM   840  O  OE2  . GLU   A 1 131 ? 15.34736  -9.43241  -31.80898 1.000 19.16055  ? 1183 GLU   B OE2  1 
ATOM   841  N  N    . PHE   A 1 132 ? 20.87060  -12.98683 -32.81267 1.000 9.72163   ? 1184 PHE   B N    1 
ATOM   842  C  CA   . PHE   A 1 132 ? 21.99951  -12.95169 -33.72979 1.000 13.74078  ? 1184 PHE   B CA   1 
ATOM   843  C  C    . PHE   A 1 132 ? 21.97529  -11.68166 -34.57174 1.000 15.94380  ? 1184 PHE   B C    1 
ATOM   844  O  O    . PHE   A 1 132 ? 20.91621  -11.10775 -34.84361 1.000 12.30902  ? 1184 PHE   B O    1 
ATOM   845  C  CB   . PHE   A 1 132 ? 21.98653  -14.16065 -34.66583 1.000 10.27713  ? 1184 PHE   B CB   1 
ATOM   846  C  CG   . PHE   A 1 132 ? 22.35472  -15.45664 -33.99591 1.000 13.66134  ? 1184 PHE   B CG   1 
ATOM   847  C  CD1  . PHE   A 1 132 ? 23.62580  -15.64754 -33.47005 1.000 12.86117  ? 1184 PHE   B CD1  1 
ATOM   848  C  CD2  . PHE   A 1 132 ? 21.43084  -16.49474 -33.90086 1.000 15.00703  ? 1184 PHE   B CD2  1 
ATOM   849  C  CE1  . PHE   A 1 132 ? 23.97198  -16.86752 -32.83913 1.000 9.69605   ? 1184 PHE   B CE1  1 
ATOM   850  C  CE2  . PHE   A 1 132 ? 21.76902  -17.70672 -33.28193 1.000 15.19870  ? 1184 PHE   B CE2  1 
ATOM   851  C  CZ   . PHE   A 1 132 ? 23.03809  -17.88262 -32.75507 1.000 13.03203  ? 1184 PHE   B CZ   1 
ATOM   852  N  N    . SER   A 1 133 ? 23.16121  -11.24353 -34.99284 1.000 16.13833  ? 1185 SER   B N    1 
ATOM   853  C  CA   . SER   A 1 133 ? 23.20500  -10.33448 -36.12282 1.000 16.35021  ? 1185 SER   B CA   1 
ATOM   854  C  C    . SER   A 1 133 ? 22.54295  -11.01750 -37.31277 1.000 16.32832  ? 1185 SER   B C    1 
ATOM   855  O  O    . SER   A 1 133 ? 22.35807  -12.23852 -37.33580 1.000 13.28617  ? 1185 SER   B O    1 
ATOM   856  C  CB   . SER   A 1 133 ? 24.64393  -9.92633  -36.44595 1.000 14.67588  ? 1185 SER   B CB   1 
ATOM   857  O  OG   . SER   A 1 133 ? 25.48302  -11.05224 -36.59808 1.000 13.95500  ? 1185 SER   B OG   1 
ATOM   858  N  N    . LYS   A 1 134 ? 22.17577  -10.21850 -38.31071 1.000 15.57035  ? 1186 LYS   B N    1 
ATOM   859  C  CA   . LYS   A 1 134 ? 21.26171  -10.68855 -39.34763 1.000 17.45165  ? 1186 LYS   B CA   1 
ATOM   860  C  C    . LYS   A 1 134 ? 21.94561  -11.03744 -40.66471 1.000 22.36928  ? 1186 LYS   B C    1 
ATOM   861  O  O    . LYS   A 1 134 ? 21.57864  -12.03345 -41.29671 1.000 19.43506  ? 1186 LYS   B O    1 
ATOM   862  C  CB   . LYS   A 1 134 ? 20.16558  -9.64265  -39.59248 1.000 17.63538  ? 1186 LYS   B CB   1 
ATOM   863  C  CG   . LYS   A 1 134 ? 19.08469  -9.63280  -38.48537 1.000 16.32976  ? 1186 LYS   B CG   1 
ATOM   864  C  CD   . LYS   A 1 134 ? 18.07856  -8.51789  -38.71122 1.000 17.17100  ? 1186 LYS   B CD   1 
ATOM   865  C  CE   . LYS   A 1 134 ? 16.82766  -8.68504  -37.85010 1.000 23.72168  ? 1186 LYS   B CE   1 
ATOM   866  N  NZ   . LYS   A 1 134 ? 17.07577  -8.31007  -36.43011 1.000 20.31500  ? 1186 LYS   B NZ   1 
ATOM   867  N  N    . HIS   A 1 135 ? 22.93048  -10.26133 -41.10478 1.000 23.36605  ? 1187 HIS   B N    1 
ATOM   868  C  CA   . HIS   A 1 135 ? 23.54238  -10.56922 -42.38786 1.000 21.69413  ? 1187 HIS   B CA   1 
ATOM   869  C  C    . HIS   A 1 135 ? 24.56451  -11.68113 -42.22500 1.000 23.86314  ? 1187 HIS   B C    1 
ATOM   870  O  O    . HIS   A 1 135 ? 24.31359  -12.84114 -42.56202 1.000 26.30038  ? 1187 HIS   B O    1 
ATOM   871  C  CB   . HIS   A 1 135 ? 24.20820  -9.33513  -42.99788 1.000 28.37720  ? 1187 HIS   B CB   1 
ATOM   872  C  CG   . HIS   A 1 135 ? 24.77308  -9.58803  -44.35595 1.000 31.48258  ? 1187 HIS   B CG   1 
ATOM   873  N  ND1  . HIS   A 1 135 ? 23.97798  -9.71507  -45.47487 1.000 35.61135  ? 1187 HIS   B ND1  1 
ATOM   874  C  CD2  . HIS   A 1 135 ? 26.04606  -9.78489  -44.77309 1.000 27.17662  ? 1187 HIS   B CD2  1 
ATOM   875  C  CE1  . HIS   A 1 135 ? 24.73890  -9.95395  -46.52796 1.000 36.66123  ? 1187 HIS   B CE1  1 
ATOM   876  N  NE2  . HIS   A 1 135 ? 25.99794  -9.99684  -46.13009 1.000 34.16752  ? 1187 HIS   B NE2  1 
ATOM   877  N  N    . SER   A 1 136 ? 25.72953  -11.32603 -41.72111 1.000 29.02409  ? 1188 SER   B N    1 
ATOM   878  C  CA   . SER   A 1 136 ? 26.70367  -12.31395 -41.29225 1.000 30.08694  ? 1188 SER   B CA   1 
ATOM   879  C  C    . SER   A 1 136 ? 26.46784  -12.51603 -39.80423 1.000 28.18339  ? 1188 SER   B C    1 
ATOM   880  O  O    . SER   A 1 136 ? 26.63783  -11.58104 -39.00921 1.000 23.72678  ? 1188 SER   B O    1 
ATOM   881  C  CB   . SER   A 1 136 ? 28.12359  -11.84280 -41.60137 1.000 28.04906  ? 1188 SER   B CB   1 
ATOM   882  O  OG   . SER   A 1 136 ? 29.03073  -12.30675 -40.62348 1.000 44.17758  ? 1188 SER   B OG   1 
ATOM   883  N  N    . GLN   A 1 137 ? 26.02800  -13.71908 -39.43223 1.000 20.99367  ? 1189 GLN   B N    1 
ATOM   884  C  CA   . GLN   A 1 137 ? 25.63016  -14.00117 -38.05520 1.000 21.19067  ? 1189 GLN   B CA   1 
ATOM   885  C  C    . GLN   A 1 137 ? 26.86528  -14.27108 -37.19233 1.000 26.79109  ? 1189 GLN   B C    1 
ATOM   886  O  O    . GLN   A 1 137 ? 27.04744  -15.34709 -36.62639 1.000 21.05359  ? 1189 GLN   B O    1 
ATOM   887  C  CB   . GLN   A 1 137 ? 24.65628  -15.16927 -38.03114 1.000 19.61017  ? 1189 GLN   B CB   1 
ATOM   888  C  CG   . GLN   A 1 137 ? 23.44417  -14.93536 -38.91901 1.000 18.18444  ? 1189 GLN   B CG   1 
ATOM   889  C  CD   . GLN   A 1 137 ? 22.25329  -15.77849 -38.50891 1.000 23.06823  ? 1189 GLN   B CD   1 
ATOM   890  O  OE1  . GLN   A 1 137 ? 22.31141  -17.01048 -38.52597 1.000 18.06897  ? 1189 GLN   B OE1  1 
ATOM   891  N  NE2  . GLN   A 1 137 ? 21.16427  -15.11461 -38.13278 1.000 23.05293  ? 1189 GLN   B NE2  1 
ATOM   892  N  N    . ASP   A 1 138 ? 27.73619  -13.26200 -37.13139 1.000 19.23376  ? 1190 ASP   B N    1 
ATOM   893  C  CA   . ASP   A 1 138 ? 28.99527  -13.34290 -36.40752 1.000 20.68873  ? 1190 ASP   B CA   1 
ATOM   894  C  C    . ASP   A 1 138 ? 28.96433  -12.59095 -35.08449 1.000 20.94128  ? 1190 ASP   B C    1 
ATOM   895  O  O    . ASP   A 1 138 ? 29.98140  -12.54688 -34.38759 1.000 20.44841  ? 1190 ASP   B O    1 
ATOM   896  C  CB   . ASP   A 1 138 ? 30.14713  -12.81176 -37.28162 1.000 23.53325  ? 1190 ASP   B CB   1 
ATOM   897  C  CG   . ASP   A 1 138 ? 30.01395  -11.31076 -37.60255 1.000 32.73396  ? 1190 ASP   B CG   1 
ATOM   898  O  OD1  . ASP   A 1 138 ? 28.98092  -10.68887 -37.26542 1.000 31.94760  ? 1190 ASP   B OD1  1 
ATOM   899  O  OD2  . ASP   A 1 138 ? 30.95583  -10.74765 -38.19863 1.000 45.64356  ? 1190 ASP   B OD2  1 
ATOM   900  N  N    . ARG   A 1 139 ? 27.82431  -12.01008 -34.71135 1.000 20.00872  ? 1191 ARG   B N    1 
ATOM   901  C  CA   . ARG   A 1 139 ? 27.71437  -11.28814 -33.45431 1.000 18.72139  ? 1191 ARG   B CA   1 
ATOM   902  C  C    . ARG   A 1 139 ? 26.37047  -11.59129 -32.80819 1.000 17.88545  ? 1191 ARG   B C    1 
ATOM   903  O  O    . ARG   A 1 139 ? 25.47546  -12.17736 -33.42012 1.000 15.80490  ? 1191 ARG   B O    1 
ATOM   904  C  CB   . ARG   A 1 139 ? 27.90820  -9.78311  -33.65528 1.000 15.00589  ? 1191 ARG   B CB   1 
ATOM   905  C  CG   . ARG   A 1 139 ? 29.35913  -9.42595  -34.00141 1.000 22.95249  ? 1191 ARG   B CG   1 
ATOM   906  C  CD   . ARG   A 1 139 ? 29.52495  -7.97092  -34.38138 1.000 21.00854  ? 1191 ARG   B CD   1 
ATOM   907  N  NE   . ARG   A 1 139 ? 28.86179  -7.66894  -35.64730 1.000 30.41672  ? 1191 ARG   B NE   1 
ATOM   908  C  CZ   . ARG   A 1 139 ? 28.73762  -6.44994  -36.16424 1.000 35.18811  ? 1191 ARG   B CZ   1 
ATOM   909  N  NH1  . ARG   A 1 139 ? 29.21558  -5.38091  -35.54125 1.000 27.97024  ? 1191 ARG   B NH1  1 
ATOM   910  N  NH2  . ARG   A 1 139 ? 28.11848  -6.29896  -37.33317 1.000 28.72173  ? 1191 ARG   B NH2  1 
ATOM   911  N  N    . VAL   A 1 140 ? 26.26256  -11.19935 -31.53816 1.000 14.99933  ? 1192 VAL   B N    1 
ATOM   912  C  CA   . VAL   A 1 140 ? 25.07066  -11.36049 -30.71804 1.000 10.52579  ? 1192 VAL   B CA   1 
ATOM   913  C  C    . VAL   A 1 140 ? 24.77459  -9.99954  -30.11896 1.000 11.23974  ? 1192 VAL   B C    1 
ATOM   914  O  O    . VAL   A 1 140 ? 25.69556  -9.29347  -29.69903 1.000 15.18415  ? 1192 VAL   B O    1 
ATOM   915  C  CB   . VAL   A 1 140 ? 25.28388  -12.40251 -29.59310 1.000 12.17241  ? 1192 VAL   B CB   1 
ATOM   916  C  CG1  . VAL   A 1 140 ? 24.11298  -12.40466 -28.59998 1.000 8.87530   ? 1192 VAL   B CG1  1 
ATOM   917  C  CG2  . VAL   A 1 140 ? 25.55095  -13.78047 -30.16918 1.000 8.38466   ? 1192 VAL   B CG2  1 
ATOM   918  N  N    . ILE   A 1 141 ? 23.50355  -9.61767  -30.08782 1.000 11.31015  ? 1193 ILE   B N    1 
ATOM   919  C  CA   . ILE   A 1 141 ? 23.10850  -8.37573  -29.43173 1.000 12.39896  ? 1193 ILE   B CA   1 
ATOM   920  C  C    . ILE   A 1 141 ? 22.17865  -8.72887  -28.27665 1.000 12.90296  ? 1193 ILE   B C    1 
ATOM   921  O  O    . ILE   A 1 141 ? 21.10369  -9.30196  -28.48856 1.000 13.30825  ? 1193 ILE   B O    1 
ATOM   922  C  CB   . ILE   A 1 141 ? 22.44530  -7.38976  -30.40463 1.000 8.93267   ? 1193 ILE   B CB   1 
ATOM   923  C  CG1  . ILE   A 1 141 ? 22.21824  -6.04881  -29.69656 1.000 11.42567  ? 1193 ILE   B CG1  1 
ATOM   924  C  CG2  . ILE   A 1 141 ? 21.14530  -7.97487  -30.94152 1.000 9.68877   ? 1193 ILE   B CG2  1 
ATOM   925  C  CD1  . ILE   A 1 141 ? 21.99503  -4.86080  -30.64949 1.000 13.06347  ? 1193 ILE   B CD1  1 
ATOM   926  N  N    . GLY   A 1 142 ? 22.59174  -8.38087  -27.06268 1.000 8.96073   ? 1194 GLY   B N    1 
ATOM   927  C  CA   . GLY   A 1 142 ? 21.80789  -8.65399  -25.87361 1.000 10.34185  ? 1194 GLY   B CA   1 
ATOM   928  C  C    . GLY   A 1 142 ? 21.16582  -7.39107  -25.34150 1.000 13.02043  ? 1194 GLY   B C    1 
ATOM   929  O  O    . GLY   A 1 142 ? 21.61768  -6.28102  -25.65351 1.000 13.61520  ? 1194 GLY   B O    1 
ATOM   930  N  N    . THR   A 1 143 ? 20.10892  -7.54320  -24.55040 1.000 11.82245  ? 1195 THR   B N    1 
ATOM   931  C  CA   . THR   A 1 143 ? 19.41387  -6.41829  -23.94128 1.000 10.98624  ? 1195 THR   B CA   1 
ATOM   932  C  C    . THR   A 1 143 ? 19.36704  -6.61435  -22.43529 1.000 14.87677  ? 1195 THR   B C    1 
ATOM   933  O  O    . THR   A 1 143 ? 18.97120  -7.68641  -21.95728 1.000 13.71765  ? 1195 THR   B O    1 
ATOM   934  C  CB   . THR   A 1 143 ? 17.98680  -6.27342  -24.46313 1.000 13.37096  ? 1195 THR   B CB   1 
ATOM   935  O  OG1  . THR   A 1 143 ? 18.00865  -6.18136  -25.88913 1.000 14.09823  ? 1195 THR   B OG1  1 
ATOM   936  C  CG2  . THR   A 1 143 ? 17.34174  -5.00850  -23.86802 1.000 13.83821  ? 1195 THR   B CG2  1 
ATOM   937  N  N    . LYS   A 1 144 ? 19.77302  -5.58134  -21.70529 1.000 11.47734  ? 1196 LYS   B N    1 
ATOM   938  C  CA   . LYS   A 1 144 ? 19.64716  -5.51840  -20.24928 1.000 15.33538  ? 1196 LYS   B CA   1 
ATOM   939  C  C    . LYS   A 1 144 ? 18.93806  -4.20349  -19.93016 1.000 14.20646  ? 1196 LYS   B C    1 
ATOM   940  O  O    . LYS   A 1 144 ? 19.56796  -3.13942  -19.90518 1.000 16.88877  ? 1196 LYS   B O    1 
ATOM   941  C  CB   . LYS   A 1 144 ? 21.00524  -5.60430  -19.56142 1.000 17.52704  ? 1196 LYS   B CB   1 
ATOM   942  C  CG   . LYS   A 1 144 ? 20.89638  -5.47836  -18.05040 1.000 22.03287  ? 1196 LYS   B CG   1 
ATOM   943  C  CD   . LYS   A 1 144 ? 22.22942  -5.20425  -17.41153 1.000 26.47840  ? 1196 LYS   B CD   1 
ATOM   944  C  CE   . LYS   A 1 144 ? 22.04053  -4.82033  -15.94650 1.000 30.12103  ? 1196 LYS   B CE   1 
ATOM   945  N  NZ   . LYS   A 1 144 ? 23.33461  -4.81522  -15.23263 1.000 26.71241  ? 1196 LYS   B NZ   1 
ATOM   946  N  N    . GLY   A 1 145 ? 17.63310  -4.28362  -19.70202 1.000 11.57668  ? 1197 GLY   B N    1 
ATOM   947  C  CA   . GLY   A 1 145 ? 16.84801  -3.09371  -19.43590 1.000 12.46167  ? 1197 GLY   B CA   1 
ATOM   948  C  C    . GLY   A 1 145 ? 16.93579  -2.16866  -20.63188 1.000 16.87716  ? 1197 GLY   B C    1 
ATOM   949  O  O    . GLY   A 1 145 ? 16.56971  -2.53365  -21.75785 1.000 13.64823  ? 1197 GLY   B O    1 
ATOM   950  N  N    . ASP   A 1 146 ? 17.44570  -0.96462  -20.40188 1.000 14.94013  ? 1198 ASP   B N    1 
ATOM   951  C  CA   . ASP   A 1 146 ? 17.52249  0.06543   -21.43486 1.000 18.73167  ? 1198 ASP   B CA   1 
ATOM   952  C  C    . ASP   A 1 146 ? 18.77241  -0.04842  -22.29899 1.000 19.79706  ? 1198 ASP   B C    1 
ATOM   953  O  O    . ASP   A 1 146 ? 18.93024  0.74463   -23.24298 1.000 18.96545  ? 1198 ASP   B O    1 
ATOM   954  C  CB   . ASP   A 1 146 ? 17.49742  1.45340   -20.79580 1.000 15.76679  ? 1198 ASP   B CB   1 
ATOM   955  C  CG   . ASP   A 1 146 ? 16.20347  1.75525   -20.05966 1.000 21.33054  ? 1198 ASP   B CG   1 
ATOM   956  O  OD1  . ASP   A 1 146 ? 15.16151  1.08516   -20.29858 1.000 22.82881  ? 1198 ASP   B OD1  1 
ATOM   957  O  OD2  . ASP   A 1 146 ? 16.23346  2.70722   -19.24763 1.000 28.47031  ? 1198 ASP   B OD2  1 
ATOM   958  N  N    . ILE   A 1 147 ? 19.64854  -1.00834  -22.00111 1.000 14.79828  ? 1199 ILE   B N    1 
ATOM   959  C  CA   . ILE   A 1 147 ? 21.02249  -1.03019  -22.49225 1.000 12.49364  ? 1199 ILE   B CA   1 
ATOM   960  C  C    . ILE   A 1 147 ? 21.20550  -2.18814  -23.45932 1.000 14.32376  ? 1199 ILE   B C    1 
ATOM   961  O  O    . ILE   A 1 147 ? 20.73064  -3.30519  -23.20931 1.000 16.15265  ? 1199 ILE   B O    1 
ATOM   962  C  CB   . ILE   A 1 147 ? 22.01862  -1.13813  -21.32336 1.000 13.17201  ? 1199 ILE   B CB   1 
ATOM   963  C  CG1  . ILE   A 1 147 ? 21.86559  0.08882   -20.42730 1.000 18.45638  ? 1199 ILE   B CG1  1 
ATOM   964  C  CG2  . ILE   A 1 147 ? 23.45058  -1.27697  -21.84851 1.000 12.52091  ? 1199 ILE   B CG2  1 
ATOM   965  C  CD1  . ILE   A 1 147 ? 22.31776  -0.11919  -19.01235 1.000 19.95612  ? 1199 ILE   B CD1  1 
ATOM   966  N  N    . ALA   A 1 148 ? 21.90337  -1.92303  -24.55638 1.000 8.56458   ? 1200 ALA   B N    1 
ATOM   967  C  CA   . ALA   A 1 148 ? 22.22036  -2.93796  -25.54545 1.000 11.73153  ? 1200 ALA   B CA   1 
ATOM   968  C  C    . ALA   A 1 148 ? 23.68741  -3.33282  -25.43961 1.000 11.67992  ? 1200 ALA   B C    1 
ATOM   969  O  O    . ALA   A 1 148 ? 24.55735  -2.47574  -25.28167 1.000 14.10922  ? 1200 ALA   B O    1 
ATOM   970  C  CB   . ALA   A 1 148 ? 21.92917  -2.41794  -26.95440 1.000 11.75549  ? 1200 ALA   B CB   1 
ATOM   971  N  N    . HIS   A 1 149 ? 23.96853  -4.62479  -25.57769 1.000 13.94445  ? 1201 HIS   B N    1 
ATOM   972  C  CA   . HIS   A 1 149 ? 25.33657  -5.11865  -25.63185 1.000 13.73278  ? 1201 HIS   B CA   1 
ATOM   973  C  C    . HIS   A 1 149 ? 25.54451  -5.87158  -26.93589 1.000 10.90832  ? 1201 HIS   B C    1 
ATOM   974  O  O    . HIS   A 1 149 ? 24.70955  -6.68665  -27.31884 1.000 9.31446   ? 1201 HIS   B O    1 
ATOM   975  C  CB   . HIS   A 1 149 ? 25.64478  -6.04766  -24.45491 1.000 9.78376   ? 1201 HIS   B CB   1 
ATOM   976  C  CG   . HIS   A 1 149 ? 25.52085  -5.38872  -23.11987 1.000 14.58307  ? 1201 HIS   B CG   1 
ATOM   977  N  ND1  . HIS   A 1 149 ? 24.73201  -5.89684  -22.10981 1.000 12.23335  ? 1201 HIS   B ND1  1 
ATOM   978  C  CD2  . HIS   A 1 149 ? 26.07879  -4.25669  -22.62889 1.000 13.70843  ? 1201 HIS   B CD2  1 
ATOM   979  C  CE1  . HIS   A 1 149 ? 24.80804  -5.10587  -21.05479 1.000 11.79731  ? 1201 HIS   B CE1  1 
ATOM   980  N  NE2  . HIS   A 1 149 ? 25.61891  -4.10378  -21.34184 1.000 19.11915  ? 1201 HIS   B NE2  1 
ATOM   981  N  N    . ILE   A 1 150 ? 26.67542  -5.63245  -27.59400 1.000 12.89573  ? 1202 ILE   B N    1 
ATOM   982  C  CA   . ILE   A 1 150 ? 27.05737  -6.38237  -28.78207 1.000 14.05457  ? 1202 ILE   B CA   1 
ATOM   983  C  C    . ILE   A 1 150 ? 28.24249  -7.26327  -28.43722 1.000 15.43054  ? 1202 ILE   B C    1 
ATOM   984  O  O    . ILE   A 1 150 ? 29.25749  -6.76818  -27.93631 1.000 15.59872  ? 1202 ILE   B O    1 
ATOM   985  C  CB   . ILE   A 1 150 ? 27.40216  -5.45729  -29.95807 1.000 15.40076  ? 1202 ILE   B CB   1 
ATOM   986  C  CG1  . ILE   A 1 150 ? 26.16704  -4.65840  -30.38291 1.000 12.85208  ? 1202 ILE   B CG1  1 
ATOM   987  C  CG2  . ILE   A 1 150 ? 27.93112  -6.29220  -31.11515 1.000 11.69570  ? 1202 ILE   B CG2  1 
ATOM   988  C  CD1  . ILE   A 1 150 ? 26.43783  -3.70133  -31.50391 1.000 15.49125  ? 1202 ILE   B CD1  1 
ATOM   989  N  N    . TYR   A 1 151 ? 28.12859  -8.56027  -28.72426 1.000 13.40500  ? 1203 TYR   B N    1 
ATOM   990  C  CA   . TYR   A 1 151 ? 29.18471  -9.52017  -28.42940 1.000 13.21541  ? 1203 TYR   B CA   1 
ATOM   991  C  C    . TYR   A 1 151 ? 29.68165  -10.18508 -29.70347 1.000 14.40085  ? 1203 TYR   B C    1 
ATOM   992  O  O    . TYR   A 1 151 ? 28.92157  -10.39412 -30.65240 1.000 18.09009  ? 1203 TYR   B O    1 
ATOM   993  C  CB   . TYR   A 1 151 ? 28.70292  -10.61626 -27.47339 1.000 17.85668  ? 1203 TYR   B CB   1 
ATOM   994  C  CG   . TYR   A 1 151 ? 28.12000  -10.12336 -26.17631 1.000 12.63376  ? 1203 TYR   B CG   1 
ATOM   995  C  CD1  . TYR   A 1 151 ? 28.92410  -9.91032  -25.05939 1.000 13.54958  ? 1203 TYR   B CD1  1 
ATOM   996  C  CD2  . TYR   A 1 151 ? 26.76099  -9.88450  -26.06216 1.000 12.89185  ? 1203 TYR   B CD2  1 
ATOM   997  C  CE1  . TYR   A 1 151 ? 28.36918  -9.45542  -23.86631 1.000 13.83721  ? 1203 TYR   B CE1  1 
ATOM   998  C  CE2  . TYR   A 1 151 ? 26.20807  -9.43359  -24.88609 1.000 12.88021  ? 1203 TYR   B CE2  1 
ATOM   999  C  CZ   . TYR   A 1 151 ? 27.00816  -9.22455  -23.79717 1.000 11.15232  ? 1203 TYR   B CZ   1 
ATOM   1000 O  OH   . TYR   A 1 151 ? 26.43524  -8.78365  -22.63309 1.000 18.09479  ? 1203 TYR   B OH   1 
ATOM   1001 N  N    . ASP   A 1 152 ? 30.95868  -10.54795 -29.69362 1.000 16.96389  ? 1204 ASP   B N    1 
ATOM   1002 C  CA   . ASP   A 1 152 ? 31.53566  -11.36686 -30.74971 1.000 17.72265  ? 1204 ASP   B CA   1 
ATOM   1003 C  C    . ASP   A 1 152 ? 31.21983  -12.83790 -30.50073 1.000 18.88096  ? 1204 ASP   B C    1 
ATOM   1004 O  O    . ASP   A 1 152 ? 31.35899  -13.33493 -29.38376 1.000 14.72187  ? 1204 ASP   B O    1 
ATOM   1005 C  CB   . ASP   A 1 152 ? 33.05063  -11.14871 -30.80586 1.000 22.93478  ? 1204 ASP   B CB   1 
ATOM   1006 C  CG   . ASP   A 1 152 ? 33.71959  -11.91360 -31.94095 1.000 17.01699  ? 1204 ASP   B CG   1 
ATOM   1007 O  OD1  . ASP   A 1 152 ? 33.55043  -11.50958 -33.09792 1.000 21.14151  ? 1204 ASP   B OD1  1 
ATOM   1008 O  OD2  . ASP   A 1 152 ? 34.41271  -12.91254 -31.66906 1.000 23.85439  ? 1204 ASP   B OD2  1 
ATOM   1009 N  N    . ILE   A 1 153 ? 30.81779  -13.54890 -31.55371 1.000 14.93271  ? 1205 ILE   B N    1 
ATOM   1010 C  CA   . ILE   A 1 153 ? 30.41394  -14.93995 -31.36272 1.000 20.62710  ? 1205 ILE   B CA   1 
ATOM   1011 C  C    . ILE   A 1 153 ? 31.61706  -15.81884 -31.02188 1.000 25.05783  ? 1205 ILE   B C    1 
ATOM   1012 O  O    . ILE   A 1 153 ? 31.50824  -16.75888 -30.22390 1.000 22.46960  ? 1205 ILE   B O    1 
ATOM   1013 C  CB   . ILE   A 1 153 ? 29.66187  -15.45398 -32.60266 1.000 19.20411  ? 1205 ILE   B CB   1 
ATOM   1014 C  CG1  . ILE   A 1 153 ? 28.21882  -14.92812 -32.58050 1.000 20.92258  ? 1205 ILE   B CG1  1 
ATOM   1015 C  CG2  . ILE   A 1 153 ? 29.67801  -16.97297 -32.65772 1.000 19.30970  ? 1205 ILE   B CG2  1 
ATOM   1016 C  CD1  . ILE   A 1 153 ? 27.55168  -14.93113 -33.93643 1.000 29.97122  ? 1205 ILE   B CD1  1 
ATOM   1017 N  N    . GLN   A 1 154 ? 32.77998  -15.52971 -31.60799 1.000 17.66973  ? 1206 GLN   B N    1 
ATOM   1018 C  CA   . GLN   A 1 154 ? 33.93808  -16.38860 -31.39714 1.000 24.24690  ? 1206 GLN   B CA   1 
ATOM   1019 C  C    . GLN   A 1 154 ? 34.52421  -16.19259 -30.00519 1.000 21.87220  ? 1206 GLN   B C    1 
ATOM   1020 O  O    . GLN   A 1 154 ? 34.58438  -17.13462 -29.20723 1.000 18.81084  ? 1206 GLN   B O    1 
ATOM   1021 C  CB   . GLN   A 1 154 ? 34.98895  -16.13346 -32.47524 1.000 27.01875  ? 1206 GLN   B CB   1 
ATOM   1022 C  CG   . GLN   A 1 154 ? 34.94093  -17.16042 -33.58327 1.000 34.94928  ? 1206 GLN   B CG   1 
ATOM   1023 C  CD   . GLN   A 1 154 ? 36.26587  -17.28227 -34.30941 1.000 67.24119  ? 1206 GLN   B CD   1 
ATOM   1024 O  OE1  . GLN   A 1 154 ? 37.08099  -18.15620 -33.99852 1.000 65.20212  ? 1206 GLN   B OE1  1 
ATOM   1025 N  NE2  . GLN   A 1 154 ? 36.49168  -16.40121 -35.28340 1.000 64.63263  ? 1206 GLN   B NE2  1 
ATOM   1026 N  N    . THR   A 1 155 ? 34.93712  -14.96356 -29.68619 1.000 19.50404  ? 1207 THR   B N    1 
ATOM   1027 C  CA   . THR   A 1 155 ? 35.55422  -14.69655 -28.39324 1.000 18.91143  ? 1207 THR   B CA   1 
ATOM   1028 C  C    . THR   A 1 155 ? 34.55333  -14.53369 -27.25413 1.000 23.75084  ? 1207 THR   B C    1 
ATOM   1029 O  O    . THR   A 1 155 ? 34.94846  -14.64769 -26.08718 1.000 21.24670  ? 1207 THR   B O    1 
ATOM   1030 C  CB   . THR   A 1 155 ? 36.41309  -13.43746 -28.46228 1.000 17.08411  ? 1207 THR   B CB   1 
ATOM   1031 O  OG1  . THR   A 1 155 ? 35.57196  -12.29554 -28.67216 1.000 19.12220  ? 1207 THR   B OG1  1 
ATOM   1032 C  CG2  . THR   A 1 155 ? 37.42199  -13.54132 -29.60639 1.000 21.94898  ? 1207 THR   B CG2  1 
ATOM   1033 N  N    . GLY   A 1 156 ? 33.27927  -14.26080 -27.54499 1.000 21.86541  ? 1208 GLY   B N    1 
ATOM   1034 C  CA   . GLY   A 1 156 ? 32.35534  -13.88293 -26.48988 1.000 10.96224  ? 1208 GLY   B CA   1 
ATOM   1035 C  C    . GLY   A 1 156 ? 32.59327  -12.50693 -25.90086 1.000 18.09485  ? 1208 GLY   B C    1 
ATOM   1036 O  O    . GLY   A 1 156 ? 31.80031  -12.06604 -25.05876 1.000 14.33966  ? 1208 GLY   B O    1 
ATOM   1037 N  N    . ASN   A 1 157 ? 33.65415  -11.80881 -26.31994 1.000 18.29871  ? 1209 ASN   B N    1 
ATOM   1038 C  CA   . ASN   A 1 157 ? 33.93307  -10.46880 -25.81292 1.000 17.27567  ? 1209 ASN   B CA   1 
ATOM   1039 C  C    . ASN   A 1 157 ? 32.77496  -9.52191  -26.07577 1.000 13.17950  ? 1209 ASN   B C    1 
ATOM   1040 O  O    . ASN   A 1 157 ? 32.13885  -9.56393  -27.13070 1.000 15.25445  ? 1209 ASN   B O    1 
ATOM   1041 C  CB   . ASN   A 1 157 ? 35.18095  -9.87266  -26.47403 1.000 17.41561  ? 1209 ASN   B CB   1 
ATOM   1042 C  CG   . ASN   A 1 157 ? 36.44206  -10.63054 -26.15619 1.000 20.24988  ? 1209 ASN   B CG   1 
ATOM   1043 O  OD1  . ASN   A 1 157 ? 36.45623  -11.55657 -25.34422 1.000 21.24577  ? 1209 ASN   B OD1  1 
ATOM   1044 N  ND2  . ASN   A 1 157 ? 37.52295  -10.23041 -26.80328 1.000 29.18977  ? 1209 ASN   B ND2  1 
ATOM   1045 N  N    . LYS   A 1 158 ? 32.54296  -8.62296  -25.12671 1.000 13.37481  ? 1210 LYS   B N    1 
ATOM   1046 C  CA   . LYS   A 1 158 ? 31.65683  -7.49404  -25.36458 1.000 17.50049  ? 1210 LYS   B CA   1 
ATOM   1047 C  C    . LYS   A 1 158 ? 32.37364  -6.49094  -26.26362 1.000 21.64632  ? 1210 LYS   B C    1 
ATOM   1048 O  O    . LYS   A 1 158 ? 33.39462  -5.91085  -25.87670 1.000 22.96234  ? 1210 LYS   B O    1 
ATOM   1049 C  CB   . LYS   A 1 158 ? 31.24390  -6.85913  -24.03951 1.000 13.45276  ? 1210 LYS   B CB   1 
ATOM   1050 C  CG   . LYS   A 1 158 ? 30.30777  -5.68121  -24.23538 1.000 21.28299  ? 1210 LYS   B CG   1 
ATOM   1051 C  CD   . LYS   A 1 158 ? 29.57787  -5.35333  -22.96229 1.000 23.97636  ? 1210 LYS   B CD   1 
ATOM   1052 C  CE   . LYS   A 1 158 ? 30.47991  -4.71828  -21.92836 1.000 30.79954  ? 1210 LYS   B CE   1 
ATOM   1053 N  NZ   . LYS   A 1 158 ? 29.66700  -4.41441  -20.71326 1.000 36.74093  ? 1210 LYS   B NZ   1 
ATOM   1054 N  N    . LEU   A 1 159 ? 31.86250  -6.29895  -27.47756 1.000 18.45719  ? 1211 LEU   B N    1 
ATOM   1055 C  CA   . LEU   A 1 159 ? 32.45331  -5.35885  -28.41658 1.000 18.44377  ? 1211 LEU   B CA   1 
ATOM   1056 C  C    . LEU   A 1 159 ? 31.95219  -3.94191  -28.21448 1.000 23.14584  ? 1211 LEU   B C    1 
ATOM   1057 O  O    . LEU   A 1 159 ? 32.68607  -2.98783  -28.48152 1.000 22.54400  ? 1211 LEU   B O    1 
ATOM   1058 C  CB   . LEU   A 1 159 ? 32.16220  -5.79183  -29.86357 1.000 16.79266  ? 1211 LEU   B CB   1 
ATOM   1059 C  CG   . LEU   A 1 159 ? 32.66729  -7.18476  -30.28467 1.000 25.17228  ? 1211 LEU   B CG   1 
ATOM   1060 C  CD1  . LEU   A 1 159 ? 32.17419  -7.58176  -31.68564 1.000 15.29833  ? 1211 LEU   B CD1  1 
ATOM   1061 C  CD2  . LEU   A 1 159 ? 34.19431  -7.26362  -30.19983 1.000 17.19038  ? 1211 LEU   B CD2  1 
ATOM   1062 N  N    . LEU   A 1 160 ? 30.72822  -3.77605  -27.72635 1.000 22.99215  ? 1212 LEU   B N    1 
ATOM   1063 C  CA   . LEU   A 1 160 ? 30.12410  -2.45411  -27.67024 1.000 20.45230  ? 1212 LEU   B CA   1 
ATOM   1064 C  C    . LEU   A 1 160 ? 29.03821  -2.45325  -26.61313 1.000 22.02501  ? 1212 LEU   B C    1 
ATOM   1065 O  O    . LEU   A 1 160 ? 28.35833  -3.46133  -26.40510 1.000 17.87722  ? 1212 LEU   B O    1 
ATOM   1066 C  CB   . LEU   A 1 160 ? 29.50492  -2.05712  -29.01416 1.000 17.76866  ? 1212 LEU   B CB   1 
ATOM   1067 C  CG   . LEU   A 1 160 ? 30.27074  -1.25501  -30.05221 1.000 24.81144  ? 1212 LEU   B CG   1 
ATOM   1068 C  CD1  . LEU   A 1 160 ? 29.25758  -0.77307  -31.08809 1.000 19.91363  ? 1212 LEU   B CD1  1 
ATOM   1069 C  CD2  . LEU   A 1 160 ? 31.03169  -0.08196  -29.42725 1.000 22.15342  ? 1212 LEU   B CD2  1 
ATOM   1070 N  N    . THR   A 1 161 ? 28.87316  -1.30729  -25.96807 1.000 16.77291  ? 1213 THR   B N    1 
ATOM   1071 C  CA   . THR   A 1 161 ? 27.68121  -1.01944  -25.19294 1.000 16.85819  ? 1213 THR   B CA   1 
ATOM   1072 C  C    . THR   A 1 161 ? 27.01803  0.20752   -25.80183 1.000 18.51178  ? 1213 THR   B C    1 
ATOM   1073 O  O    . THR   A 1 161 ? 27.68491  1.21359   -26.04486 1.000 18.94265  ? 1213 THR   B O    1 
ATOM   1074 C  CB   . THR   A 1 161 ? 28.00334  -0.77846  -23.71596 1.000 20.08585  ? 1213 THR   B CB   1 
ATOM   1075 O  OG1  . THR   A 1 161 ? 28.48952  -1.99443  -23.12506 1.000 22.80330  ? 1213 THR   B OG1  1 
ATOM   1076 C  CG2  . THR   A 1 161 ? 26.74537  -0.35261  -22.99382 1.000 17.89732  ? 1213 THR   B CG2  1 
ATOM   1077 N  N    . LEU   A 1 162 ? 25.71601  0.12040   -26.06369 1.000 17.79934  ? 1214 LEU   B N    1 
ATOM   1078 C  CA   . LEU   A 1 162 ? 24.96384  1.21735   -26.66558 1.000 17.24641  ? 1214 LEU   B CA   1 
ATOM   1079 C  C    . LEU   A 1 162 ? 23.91590  1.68421   -25.67145 1.000 17.44112  ? 1214 LEU   B C    1 
ATOM   1080 O  O    . LEU   A 1 162 ? 22.90499  1.00710   -25.46237 1.000 15.36146  ? 1214 LEU   B O    1 
ATOM   1081 C  CB   . LEU   A 1 162 ? 24.31775  0.79333   -27.98853 1.000 16.07093  ? 1214 LEU   B CB   1 
ATOM   1082 C  CG   . LEU   A 1 162 ? 25.27066  0.47147   -29.14364 1.000 16.33274  ? 1214 LEU   B CG   1 
ATOM   1083 C  CD1  . LEU   A 1 162 ? 24.52057  0.06244   -30.40457 1.000 12.83727  ? 1214 LEU   B CD1  1 
ATOM   1084 C  CD2  . LEU   A 1 162 ? 26.17451  1.64857   -29.43469 1.000 23.09430  ? 1214 LEU   B CD2  1 
ATOM   1085 N  N    . PHE   A 1 163 ? 24.14784  2.84621   -25.07443 1.000 21.25715  ? 1215 PHE   B N    1 
ATOM   1086 C  CA   . PHE   A 1 163 ? 23.19689  3.41808   -24.13332 1.000 19.18181  ? 1215 PHE   B CA   1 
ATOM   1087 C  C    . PHE   A 1 163 ? 23.46075  4.90911   -24.01829 1.000 25.04149  ? 1215 PHE   B C    1 
ATOM   1088 O  O    . PHE   A 1 163 ? 24.61173  5.32621   -23.85739 1.000 27.73927  ? 1215 PHE   B O    1 
ATOM   1089 C  CB   . PHE   A 1 163 ? 23.30709  2.76904   -22.75335 1.000 16.73015  ? 1215 PHE   B CB   1 
ATOM   1090 C  CG   . PHE   A 1 163 ? 22.45013  3.43792   -21.71724 1.000 22.60263  ? 1215 PHE   B CG   1 
ATOM   1091 C  CD1  . PHE   A 1 163 ? 21.06512  3.41979   -21.83010 1.000 20.04945  ? 1215 PHE   B CD1  1 
ATOM   1092 C  CD2  . PHE   A 1 163 ? 23.02118  4.10994   -20.64927 1.000 27.88806  ? 1215 PHE   B CD2  1 
ATOM   1093 C  CE1  . PHE   A 1 163 ? 20.26516  4.04168   -20.89099 1.000 20.99725  ? 1215 PHE   B CE1  1 
ATOM   1094 C  CE2  . PHE   A 1 163 ? 22.22121  4.74183   -19.69817 1.000 32.64700  ? 1215 PHE   B CE2  1 
ATOM   1095 C  CZ   . PHE   A 1 163 ? 20.84520  4.70770   -19.82103 1.000 26.68442  ? 1215 PHE   B CZ   1 
ATOM   1096 N  N    . ASN   A 1 164 ? 22.40067  5.70200   -24.09215 1.000 27.39138  ? 1216 ASN   B N    1 
ATOM   1097 C  CA   . ASN   A 1 164 ? 22.50055  7.13301   -23.84211 1.000 22.29271  ? 1216 ASN   B CA   1 
ATOM   1098 C  C    . ASN   A 1 164 ? 21.32860  7.55986   -22.97097 1.000 26.33798  ? 1216 ASN   B C    1 
ATOM   1099 O  O    . ASN   A 1 164 ? 20.17555  7.56176   -23.42786 1.000 24.53044  ? 1216 ASN   B O    1 
ATOM   1100 C  CB   . ASN   A 1 164 ? 22.51034  7.92905   -25.13908 1.000 23.04105  ? 1216 ASN   B CB   1 
ATOM   1101 C  CG   . ASN   A 1 164 ? 22.55422  9.43605   -24.89303 1.000 40.05726  ? 1216 ASN   B CG   1 
ATOM   1102 O  OD1  . ASN   A 1 164 ? 22.21228  9.92298   -23.80798 1.000 38.27143  ? 1216 ASN   B OD1  1 
ATOM   1103 N  ND2  . ASN   A 1 164 ? 22.97604  10.18113  -25.90505 1.000 32.23085  ? 1216 ASN   B ND2  1 
ATOM   1104 N  N    . PRO   A 1 165 ? 21.58369  7.95084   -21.71999 1.000 29.48120  ? 1217 PRO   B N    1 
ATOM   1105 C  CA   . PRO   A 1 165 ? 20.47076  8.21370   -20.79986 1.000 34.77397  ? 1217 PRO   B CA   1 
ATOM   1106 C  C    . PRO   A 1 165 ? 19.64960  9.43263   -21.18473 1.000 32.51442  ? 1217 PRO   B C    1 
ATOM   1107 O  O    . PRO   A 1 165 ? 18.46863  9.49550   -20.81861 1.000 29.00380  ? 1217 PRO   B O    1 
ATOM   1108 C  CB   . PRO   A 1 165 ? 21.17088  8.39872   -19.44793 1.000 28.82925  ? 1217 PRO   B CB   1 
ATOM   1109 C  CG   . PRO   A 1 165 ? 22.51779  8.90286   -19.80905 1.000 30.83333  ? 1217 PRO   B CG   1 
ATOM   1110 C  CD   . PRO   A 1 165 ? 22.88872  8.28895   -21.12811 1.000 29.70329  ? 1217 PRO   B CD   1 
ATOM   1111 N  N    . ASP   A 1 166 ? 20.22243  10.38071  -21.93276 1.000 29.94470  ? 1218 ASP   B N    1 
ATOM   1112 C  CA   . ASP   A 1 166 ? 19.46527  11.53865  -22.38864 1.000 32.82617  ? 1218 ASP   B CA   1 
ATOM   1113 C  C    . ASP   A 1 166 ? 18.54718  11.22561  -23.56056 1.000 31.80413  ? 1218 ASP   B C    1 
ATOM   1114 O  O    . ASP   A 1 166 ? 17.59108  11.97052  -23.79143 1.000 31.57356  ? 1218 ASP   B O    1 
ATOM   1115 C  CB   . ASP   A 1 166 ? 20.41112  12.67376  -22.78270 1.000 33.83299  ? 1218 ASP   B CB   1 
ATOM   1116 C  CG   . ASP   A 1 166 ? 21.35019  13.05681  -21.66178 1.000 40.68210  ? 1218 ASP   B CG   1 
ATOM   1117 O  OD1  . ASP   A 1 166 ? 20.93933  12.94773  -20.48174 1.000 40.84657  ? 1218 ASP   B OD1  1 
ATOM   1118 O  OD2  . ASP   A 1 166 ? 22.50112  13.44894  -21.95888 1.000 49.65125  ? 1218 ASP   B OD2  1 
ATOM   1119 N  N    . LEU   A 1 167 ? 18.81021  10.15766  -24.31262 1.000 30.36776  ? 1219 LEU   B N    1 
ATOM   1120 C  CA   . LEU   A 1 167 ? 17.91413  9.76961   -25.39654 1.000 30.76703  ? 1219 LEU   B CA   1 
ATOM   1121 C  C    . LEU   A 1 167 ? 16.98428  8.61451   -25.03849 1.000 29.22197  ? 1219 LEU   B C    1 
ATOM   1122 O  O    . LEU   A 1 167 ? 16.01623  8.37544   -25.77040 1.000 34.01770  ? 1219 LEU   B O    1 
ATOM   1123 C  CB   . LEU   A 1 167 ? 18.71704  9.39474   -26.64964 1.000 29.45525  ? 1219 LEU   B CB   1 
ATOM   1124 C  CG   . LEU   A 1 167 ? 19.56387  10.47484  -27.31869 1.000 26.81611  ? 1219 LEU   B CG   1 
ATOM   1125 C  CD1  . LEU   A 1 167 ? 20.22480  9.89695   -28.55378 1.000 23.39651  ? 1219 LEU   B CD1  1 
ATOM   1126 C  CD2  . LEU   A 1 167 ? 18.74371  11.71878  -27.67756 1.000 25.56580  ? 1219 LEU   B CD2  1 
ATOM   1127 N  N    . ALA   A 1 168 ? 17.23547  7.90249   -23.93754 1.000 25.83186  ? 1220 ALA   B N    1 
ATOM   1128 C  CA   . ALA   A 1 168 ? 16.47162  6.69841   -23.62451 1.000 17.77666  ? 1220 ALA   B CA   1 
ATOM   1129 C  C    . ALA   A 1 168 ? 14.97359  6.98126   -23.60134 1.000 26.71847  ? 1220 ALA   B C    1 
ATOM   1130 O  O    . ALA   A 1 168 ? 14.53253  8.05120   -23.16826 1.000 21.69995  ? 1220 ALA   B O    1 
ATOM   1131 C  CB   . ALA   A 1 168 ? 16.90581  6.12840   -22.26957 1.000 15.71190  ? 1220 ALA   B CB   1 
ATOM   1132 N  N    . ASN   A 1 169 ? 14.18764  6.00720   -24.07330 1.000 15.50781  ? 1221 ASN   B N    1 
ATOM   1133 C  CA   . ASN   A 1 169 ? 12.74465  6.04805   -23.89415 1.000 20.97503  ? 1221 ASN   B CA   1 
ATOM   1134 C  C    . ASN   A 1 169 ? 12.28486  5.20896   -22.71513 1.000 15.23965  ? 1221 ASN   B C    1 
ATOM   1135 O  O    . ASN   A 1 169 ? 11.14689  5.37383   -22.26501 1.000 15.53580  ? 1221 ASN   B O    1 
ATOM   1136 C  CB   . ASN   A 1 169 ? 12.01657  5.58302   -25.16409 1.000 18.43382  ? 1221 ASN   B CB   1 
ATOM   1137 C  CG   . ASN   A 1 169 ? 12.00735  6.64106   -26.25805 1.000 17.04355  ? 1221 ASN   B CG   1 
ATOM   1138 O  OD1  . ASN   A 1 169 ? 11.69026  7.79602   -26.01298 1.000 20.50608  ? 1221 ASN   B OD1  1 
ATOM   1139 N  ND2  . ASN   A 1 169 ? 12.36927  6.24414   -27.46810 1.000 16.74909  ? 1221 ASN   B ND2  1 
ATOM   1140 N  N    . ASN   A 1 170 ? 13.14299  4.32303   -22.20425 1.000 19.17395  ? 1222 ASN   B N    1 
ATOM   1141 C  CA   . ASN   A 1 170 ? 12.82920  3.48896   -21.04825 1.000 15.51581  ? 1222 ASN   B CA   1 
ATOM   1142 C  C    . ASN   A 1 170 ? 11.63325  2.58685   -21.33216 1.000 15.18779  ? 1222 ASN   B C    1 
ATOM   1143 O  O    . ASN   A 1 170 ? 10.74436  2.43373   -20.49707 1.000 13.30154  ? 1222 ASN   B O    1 
ATOM   1144 C  CB   . ASN   A 1 170 ? 12.57924  4.34489   -19.80319 1.000 20.73312  ? 1222 ASN   B CB   1 
ATOM   1145 C  CG   . ASN   A 1 170 ? 13.56014  5.51798   -19.68425 1.000 26.60937  ? 1222 ASN   B CG   1 
ATOM   1146 O  OD1  . ASN   A 1 170 ? 13.15802  6.68994   -19.72317 1.000 22.00130  ? 1222 ASN   B OD1  1 
ATOM   1147 N  ND2  . ASN   A 1 170 ? 14.85418  5.20410   -19.54840 1.000 20.17781  ? 1222 ASN   B ND2  1 
ATOM   1148 N  N    . TYR   A 1 171 ? 11.59719  1.99989   -22.52718 1.000 12.11274  ? 1223 TYR   B N    1 
ATOM   1149 C  CA   . TYR   A 1 171 ? 10.53025  1.05980   -22.86410 1.000 16.52013  ? 1223 TYR   B CA   1 
ATOM   1150 C  C    . TYR   A 1 171 ? 10.57846  -0.15523  -21.93515 1.000 15.37956  ? 1223 TYR   B C    1 
ATOM   1151 O  O    . TYR   A 1 171 ? 11.63854  -0.75214  -21.72828 1.000 14.04746  ? 1223 TYR   B O    1 
ATOM   1152 C  CB   . TYR   A 1 171 ? 10.65314  0.61386   -24.32613 1.000 13.42912  ? 1223 TYR   B CB   1 
ATOM   1153 C  CG   . TYR   A 1 171 ? 10.20493  1.64685   -25.36605 1.000 9.21822   ? 1223 TYR   B CG   1 
ATOM   1154 C  CD1  . TYR   A 1 171 ? 8.87388   2.05073   -25.44290 1.000 11.50548  ? 1223 TYR   B CD1  1 
ATOM   1155 C  CD2  . TYR   A 1 171 ? 11.10779  2.18798   -26.28312 1.000 15.91734  ? 1223 TYR   B CD2  1 
ATOM   1156 C  CE1  . TYR   A 1 171 ? 8.45070   2.97372   -26.38982 1.000 12.84202  ? 1223 TYR   B CE1  1 
ATOM   1157 C  CE2  . TYR   A 1 171 ? 10.69659  3.12097   -27.25204 1.000 11.89176  ? 1223 TYR   B CE2  1 
ATOM   1158 C  CZ   . TYR   A 1 171 ? 9.36055   3.50784   -27.29389 1.000 11.23104  ? 1223 TYR   B CZ   1 
ATOM   1159 O  OH   . TYR   A 1 171 ? 8.91337   4.41283   -28.23681 1.000 12.09898  ? 1223 TYR   B OH   1 
ATOM   1160 N  N    . LYS   A 1 172 ? 9.42556   -0.53537  -21.37205 1.000 12.02572  ? 1224 LYS   B N    1 
ATOM   1161 C  CA   . LYS   A 1 172 ? 9.45676   -1.57540  -20.34109 1.000 14.43448  ? 1224 LYS   B CA   1 
ATOM   1162 C  C    . LYS   A 1 172 ? 9.83584   -2.93834  -20.90617 1.000 13.21613  ? 1224 LYS   B C    1 
ATOM   1163 O  O    . LYS   A 1 172 ? 10.40399  -3.75331  -20.17926 1.000 12.34889  ? 1224 LYS   B O    1 
ATOM   1164 C  CB   . LYS   A 1 172 ? 8.11485   -1.67156  -19.60895 1.000 15.76081  ? 1224 LYS   B CB   1 
ATOM   1165 C  CG   . LYS   A 1 172 ? 7.78081   -0.43062  -18.78987 1.000 20.21207  ? 1224 LYS   B CG   1 
ATOM   1166 C  CD   . LYS   A 1 172 ? 6.80796   -0.73176  -17.65278 1.000 33.67662  ? 1224 LYS   B CD   1 
ATOM   1167 C  CE   . LYS   A 1 172 ? 6.36390   0.57217   -16.96869 1.000 35.20933  ? 1224 LYS   B CE   1 
ATOM   1168 N  NZ   . LYS   A 1 172 ? 5.52004   0.36605   -15.75461 1.000 42.24515  ? 1224 LYS   B NZ   1 
ATOM   1169 N  N    . ARG   A 1 173 ? 9.53174   -3.21933  -22.17715 1.000 12.56322  ? 1225 ARG   B N    1 
ATOM   1170 C  CA   . ARG   A 1 173 ? 9.92779   -4.47426  -22.81824 1.000 12.53998  ? 1225 ARG   B CA   1 
ATOM   1171 C  C    . ARG   A 1 173 ? 10.89765  -4.19813  -23.95733 1.000 14.60635  ? 1225 ARG   B C    1 
ATOM   1172 O  O    . ARG   A 1 173 ? 10.77359  -4.74210  -25.05834 1.000 12.57732  ? 1225 ARG   B O    1 
ATOM   1173 C  CB   . ARG   A 1 173 ? 8.72082   -5.25936  -23.33214 1.000 14.73372  ? 1225 ARG   B CB   1 
ATOM   1174 C  CG   . ARG   A 1 173 ? 7.51592   -5.32152  -22.38102 1.000 16.40303  ? 1225 ARG   B CG   1 
ATOM   1175 C  CD   . ARG   A 1 173 ? 7.62014   -6.41954  -21.33407 1.000 21.37741  ? 1225 ARG   B CD   1 
ATOM   1176 N  NE   . ARG   A 1 173 ? 7.81321   -7.76851  -21.86814 1.000 29.59214  ? 1225 ARG   B NE   1 
ATOM   1177 C  CZ   . ARG   A 1 173 ? 6.85229   -8.67460  -22.01508 1.000 22.50823  ? 1225 ARG   B CZ   1 
ATOM   1178 N  NH1  . ARG   A 1 173 ? 5.58128   -8.38273  -21.79794 1.000 28.69274  ? 1225 ARG   B NH1  1 
ATOM   1179 N  NH2  . ARG   A 1 173 ? 7.17637   -9.91155  -22.37215 1.000 22.65119  ? 1225 ARG   B NH2  1 
ATOM   1180 N  N    . ASN   A 1 174 ? 11.85759  -3.31104  -23.70640 1.000 14.08573  ? 1226 ASN   B N    1 
ATOM   1181 C  CA   . ASN   A 1 174 ? 12.84245  -2.95591  -24.71348 1.000 13.44686  ? 1226 ASN   B CA   1 
ATOM   1182 C  C    . ASN   A 1 174 ? 13.55552  -4.19682  -25.22460 1.000 13.67233  ? 1226 ASN   B C    1 
ATOM   1183 O  O    . ASN   A 1 174 ? 13.95869  -5.05581  -24.43667 1.000 11.17735  ? 1226 ASN   B O    1 
ATOM   1184 C  CB   . ASN   A 1 174 ? 13.86442  -1.98583  -24.12055 1.000 13.50278  ? 1226 ASN   B CB   1 
ATOM   1185 C  CG   . ASN   A 1 174 ? 14.97029  -1.66369  -25.08666 1.000 13.18570  ? 1226 ASN   B CG   1 
ATOM   1186 O  OD1  . ASN   A 1 174 ? 14.71615  -1.49267  -26.27962 1.000 9.03270   ? 1226 ASN   B OD1  1 
ATOM   1187 N  ND2  . ASN   A 1 174 ? 16.21333  -1.60658  -24.59178 1.000 11.26434  ? 1226 ASN   B ND2  1 
ATOM   1188 N  N    . CYS   A 1 175 ? 13.73039  -4.27676  -26.55262 1.000 10.41384  ? 1227 CYS   B N    1 
ATOM   1189 C  CA   . CYS   A 1 175 ? 14.51743  -5.33566  -27.18774 1.000 10.90109  ? 1227 CYS   B CA   1 
ATOM   1190 C  C    . CYS   A 1 175 ? 15.40426  -4.72453  -28.26681 1.000 16.70026  ? 1227 CYS   B C    1 
ATOM   1191 O  O    . CYS   A 1 175 ? 14.90011  -4.26854  -29.30174 1.000 14.31627  ? 1227 CYS   B O    1 
ATOM   1192 C  CB   . CYS   A 1 175 ? 13.61948  -6.42672  -27.78369 1.000 11.01334  ? 1227 CYS   B CB   1 
ATOM   1193 S  SG   . CYS   A 1 175 ? 12.95572  -7.58983  -26.55666 1.000 25.95767  ? 1227 CYS   B SG   1 
ATOM   1194 N  N    . ALA   A 1 176 ? 16.72028  -4.73541  -28.03895 1.000 8.86252   ? 1228 ALA   B N    1 
ATOM   1195 C  CA   . ALA   A 1 176 ? 17.66913  -4.25528  -29.03403 1.000 9.99628   ? 1228 ALA   B CA   1 
ATOM   1196 C  C    . ALA   A 1 176 ? 17.79811  -5.24223  -30.18608 1.000 11.54538  ? 1228 ALA   B C    1 
ATOM   1197 O  O    . ALA   A 1 176 ? 17.72725  -6.45924  -30.00411 1.000 8.58221   ? 1228 ALA   B O    1 
ATOM   1198 C  CB   . ALA   A 1 176 ? 19.03918  -4.02417  -28.41516 1.000 9.88750   ? 1228 ALA   B CB   1 
ATOM   1199 N  N    . THR   A 1 177 ? 18.02394  -4.70416  -31.38008 1.000 10.87125  ? 1229 THR   B N    1 
ATOM   1200 C  CA   . THR   A 1 177 ? 17.98490  -5.52612  -32.57811 1.000 10.67913  ? 1229 THR   B CA   1 
ATOM   1201 C  C    . THR   A 1 177 ? 18.83472  -4.86900  -33.66617 1.000 14.13046  ? 1229 THR   B C    1 
ATOM   1202 O  O    . THR   A 1 177 ? 18.89159  -3.63599  -33.76713 1.000 14.48737  ? 1229 THR   B O    1 
ATOM   1203 C  CB   . THR   A 1 177 ? 16.52187  -5.71925  -33.03096 1.000 11.08132  ? 1229 THR   B CB   1 
ATOM   1204 O  OG1  . THR   A 1 177 ? 16.45983  -6.56821  -34.18399 1.000 10.66380  ? 1229 THR   B OG1  1 
ATOM   1205 C  CG2  . THR   A 1 177 ? 15.85770  -4.36330  -33.34984 1.000 14.19317  ? 1229 THR   B CG2  1 
ATOM   1206 N  N    . PHE   A 1 178 ? 19.52072  -5.69490  -34.44627 1.000 12.34700  ? 1230 PHE   B N    1 
ATOM   1207 C  CA   . PHE   A 1 178 ? 20.24656  -5.25179  -35.62433 1.000 13.56733  ? 1230 PHE   B CA   1 
ATOM   1208 C  C    . PHE   A 1 178 ? 19.27841  -5.02884  -36.78522 1.000 14.43828  ? 1230 PHE   B C    1 
ATOM   1209 O  O    . PHE   A 1 178 ? 18.21947  -5.64494  -36.84913 1.000 10.97255  ? 1230 PHE   B O    1 
ATOM   1210 C  CB   . PHE   A 1 178 ? 21.26761  -6.30467  -36.05947 1.000 14.81911  ? 1230 PHE   B CB   1 
ATOM   1211 C  CG   . PHE   A 1 178 ? 22.56669  -6.26357  -35.32060 1.000 12.90529  ? 1230 PHE   B CG   1 
ATOM   1212 C  CD1  . PHE   A 1 178 ? 23.49956  -5.26847  -35.58666 1.000 13.77377  ? 1230 PHE   B CD1  1 
ATOM   1213 C  CD2  . PHE   A 1 178 ? 22.88188  -7.25558  -34.40367 1.000 13.80778  ? 1230 PHE   B CD2  1 
ATOM   1214 C  CE1  . PHE   A 1 178 ? 24.70963  -5.24638  -34.91579 1.000 15.81822  ? 1230 PHE   B CE1  1 
ATOM   1215 C  CE2  . PHE   A 1 178 ? 24.09295  -7.24248  -33.72979 1.000 15.78664  ? 1230 PHE   B CE2  1 
ATOM   1216 C  CZ   . PHE   A 1 178 ? 25.00782  -6.24138  -33.98785 1.000 16.84365  ? 1230 PHE   B CZ   1 
ATOM   1217 N  N    . ASN   A 1 179 ? 19.68023  -4.16877  -37.73223 1.000 16.17137  ? 1231 ASN   B N    1 
ATOM   1218 C  CA   . ASN   A 1 179 ? 19.01109  -4.07779  -39.02916 1.000 11.85177  ? 1231 ASN   B CA   1 
ATOM   1219 C  C    . ASN   A 1 179 ? 19.53010  -5.16770  -39.96525 1.000 15.17099  ? 1231 ASN   B C    1 
ATOM   1220 O  O    . ASN   A 1 179 ? 20.51320  -5.84162  -39.66538 1.000 12.64898  ? 1231 ASN   B O    1 
ATOM   1221 C  CB   . ASN   A 1 179 ? 19.20789  -2.68275  -39.62913 1.000 14.39840  ? 1231 ASN   B CB   1 
ATOM   1222 C  CG   . ASN   A 1 179 ? 20.57981  -2.48159  -40.25926 1.000 20.97325  ? 1231 ASN   B CG   1 
ATOM   1223 O  OD1  . ASN   A 1 179 ? 21.58991  -3.02751  -39.80239 1.000 16.78769  ? 1231 ASN   B OD1  1 
ATOM   1224 N  ND2  . ASN   A 1 179 ? 20.61762  -1.68455  -41.32724 1.000 24.00063  ? 1231 ASN   B ND2  1 
ATOM   1225 N  N    . PRO   A 1 180 ? 18.87900  -5.37472  -41.12019 1.000 14.25742  ? 1232 PRO   B N    1 
ATOM   1226 C  CA   . PRO   A 1 180 ? 19.24803  -6.51966  -41.97427 1.000 14.81361  ? 1232 PRO   B CA   1 
ATOM   1227 C  C    . PRO   A 1 180 ? 20.71299  -6.56550  -42.39042 1.000 17.58947  ? 1232 PRO   B C    1 
ATOM   1228 O  O    . PRO   A 1 180 ? 21.23507  -7.66444  -42.62552 1.000 17.63867  ? 1232 PRO   B O    1 
ATOM   1229 C  CB   . PRO   A 1 180 ? 18.31989  -6.35370  -43.18417 1.000 15.58153  ? 1232 PRO   B CB   1 
ATOM   1230 C  CG   . PRO   A 1 180 ? 17.12088  -5.68584  -42.61902 1.000 12.96326  ? 1232 PRO   B CG   1 
ATOM   1231 C  CD   . PRO   A 1 180 ? 17.67089  -4.69682  -41.62204 1.000 17.12785  ? 1232 PRO   B CD   1 
ATOM   1232 N  N    . THR   A 1 181 ? 21.39787  -5.43143  -42.49045 1.000 15.80857  ? 1233 THR   B N    1 
ATOM   1233 C  CA   . THR   A 1 181 ? 22.81083  -5.42428  -42.85960 1.000 18.09732  ? 1233 THR   B CA   1 
ATOM   1234 C  C    . THR   A 1 181 ? 23.75293  -5.22323  -41.67069 1.000 23.41958  ? 1233 THR   B C    1 
ATOM   1235 O  O    . THR   A 1 181 ? 24.97791  -5.17810  -41.85981 1.000 18.56290  ? 1233 THR   B O    1 
ATOM   1236 C  CB   . THR   A 1 181 ? 23.06661  -4.36021  -43.93758 1.000 25.38241  ? 1233 THR   B CB   1 
ATOM   1237 O  OG1  . THR   A 1 181 ? 22.34553  -3.16229  -43.62747 1.000 22.83349  ? 1233 THR   B OG1  1 
ATOM   1238 C  CG2  . THR   A 1 181 ? 22.59352  -4.86821  -45.30155 1.000 18.37031  ? 1233 THR   B CG2  1 
ATOM   1239 N  N    . ASP   A 1 182 ? 23.22405  -5.13832  -40.44963 1.000 19.29744  ? 1234 ASP   B N    1 
ATOM   1240 C  CA   . ASP   A 1 182 ? 24.01317  -5.08629  -39.21771 1.000 19.15341  ? 1234 ASP   B CA   1 
ATOM   1241 C  C    . ASP   A 1 182 ? 24.79306  -3.79222  -39.05874 1.000 19.35171  ? 1234 ASP   B C    1 
ATOM   1242 O  O    . ASP   A 1 182 ? 25.61414  -3.69017  -38.13582 1.000 18.40606  ? 1234 ASP   B O    1 
ATOM   1243 C  CB   . ASP   A 1 182 ? 24.99030  -6.26620  -39.11385 1.000 22.53203  ? 1234 ASP   B CB   1 
ATOM   1244 C  CG   . ASP   A 1 182 ? 24.27942  -7.61527  -39.18083 1.000 26.09035  ? 1234 ASP   B CG   1 
ATOM   1245 O  OD1  . ASP   A 1 182 ? 23.09847  -7.67840  -38.75571 1.000 22.21247  ? 1234 ASP   B OD1  1 
ATOM   1246 O  OD2  . ASP   A 1 182 ? 24.89447  -8.59219  -39.66593 1.000 22.69549  ? 1234 ASP   B OD2  1 
ATOM   1247 N  N    . ASP   A 1 183 ? 24.58287  -2.80221  -39.92968 1.000 16.26171  ? 1235 ASP   B N    1 
ATOM   1248 C  CA   . ASP   A 1 183 ? 25.27677  -1.54115  -39.73771 1.000 16.59974  ? 1235 ASP   B CA   1 
ATOM   1249 C  C    . ASP   A 1 183 ? 24.55078  -0.61625  -38.77660 1.000 14.67425  ? 1235 ASP   B C    1 
ATOM   1250 O  O    . ASP   A 1 183 ? 25.16673  0.33779   -38.28763 1.000 17.68726  ? 1235 ASP   B O    1 
ATOM   1251 C  CB   . ASP   A 1 183 ? 25.48756  -0.82908  -41.06971 1.000 20.36225  ? 1235 ASP   B CB   1 
ATOM   1252 C  CG   . ASP   A 1 183 ? 24.20147  -0.64618  -41.84257 1.000 24.69127  ? 1235 ASP   B CG   1 
ATOM   1253 O  OD1  . ASP   A 1 183 ? 23.51454  -1.66023  -42.11053 1.000 22.61357  ? 1235 ASP   B OD1  1 
ATOM   1254 O  OD2  . ASP   A 1 183 ? 23.87432  0.51580   -42.17449 1.000 31.04738  ? 1235 ASP   B OD2  1 
ATOM   1255 N  N    . LEU   A 1 184 ? 23.27483  -0.86939  -38.49148 1.000 13.81353  ? 1236 LEU   B N    1 
ATOM   1256 C  CA   . LEU   A 1 184 ? 22.49485  -0.05050  -37.56937 1.000 16.24118  ? 1236 LEU   B CA   1 
ATOM   1257 C  C    . LEU   A 1 184 ? 21.93705  -0.91059  -36.44034 1.000 19.56116  ? 1236 LEU   B C    1 
ATOM   1258 O  O    . LEU   A 1 184 ? 21.74215  -2.11861  -36.58437 1.000 14.42408  ? 1236 LEU   B O    1 
ATOM   1259 C  CB   . LEU   A 1 184 ? 21.32570  0.65541   -38.28622 1.000 15.00829  ? 1236 LEU   B CB   1 
ATOM   1260 C  CG   . LEU   A 1 184 ? 21.69750  1.43050   -39.55423 1.000 18.36812  ? 1236 LEU   B CG   1 
ATOM   1261 C  CD1  . LEU   A 1 184 ? 20.45637  1.92440   -40.33409 1.000 14.86714  ? 1236 LEU   B CD1  1 
ATOM   1262 C  CD2  . LEU   A 1 184 ? 22.60242  2.59557   -39.19829 1.000 16.40445  ? 1236 LEU   B CD2  1 
ATOM   1263 N  N    . VAL   A 1 185 ? 21.66210  -0.27066  -35.30929 1.000 15.58022  ? 1237 VAL   B N    1 
ATOM   1264 C  CA   . VAL   A 1 185 ? 20.96328  -0.92177  -34.21024 1.000 16.19168  ? 1237 VAL   B CA   1 
ATOM   1265 C  C    . VAL   A 1 185 ? 19.80623  -0.03990  -33.78009 1.000 13.62358  ? 1237 VAL   B C    1 
ATOM   1266 O  O    . VAL   A 1 185 ? 19.94112  1.18511   -33.71806 1.000 16.80295  ? 1237 VAL   B O    1 
ATOM   1267 C  CB   . VAL   A 1 185 ? 21.88243  -1.20472  -32.99935 1.000 18.65946  ? 1237 VAL   B CB   1 
ATOM   1268 C  CG1  . VAL   A 1 185 ? 21.04657  -1.25085  -31.70926 1.000 9.63701   ? 1237 VAL   B CG1  1 
ATOM   1269 C  CG2  . VAL   A 1 185 ? 22.63654  -2.50764  -33.20047 1.000 10.89420  ? 1237 VAL   B CG2  1 
ATOM   1270 N  N    . LEU   A 1 186 ? 18.67333  -0.67102  -33.48600 1.000 10.50532  ? 1238 LEU   B N    1 
ATOM   1271 C  CA   . LEU   A 1 186 ? 17.55433  -0.03416  -32.81086 1.000 13.27663  ? 1238 LEU   B CA   1 
ATOM   1272 C  C    . LEU   A 1 186 ? 17.53853  -0.51821  -31.36088 1.000 11.57644  ? 1238 LEU   B C    1 
ATOM   1273 O  O    . LEU   A 1 186 ? 17.52467  -1.73022  -31.10692 1.000 11.58912  ? 1238 LEU   B O    1 
ATOM   1274 C  CB   . LEU   A 1 186 ? 16.24129  -0.36926  -33.52274 1.000 15.93780  ? 1238 LEU   B CB   1 
ATOM   1275 C  CG   . LEU   A 1 186 ? 15.06021  0.58362   -33.37158 1.000 20.19515  ? 1238 LEU   B CG   1 
ATOM   1276 C  CD1  . LEU   A 1 186 ? 15.42802  1.96568   -33.90857 1.000 16.43142  ? 1238 LEU   B CD1  1 
ATOM   1277 C  CD2  . LEU   A 1 186 ? 13.82220  -0.00047  -34.09348 1.000 14.66749  ? 1238 LEU   B CD2  1 
ATOM   1278 N  N    . ASN   A 1 187 ? 17.58953  0.41776   -30.41385 1.000 10.44721  ? 1239 ASN   B N    1 
ATOM   1279 C  CA   . ASN   A 1 187 ? 17.57671  0.07771   -28.98686 1.000 11.18633  ? 1239 ASN   B CA   1 
ATOM   1280 C  C    . ASN   A 1 187 ? 16.80669  1.14461   -28.22974 1.000 10.33013  ? 1239 ASN   B C    1 
ATOM   1281 O  O    . ASN   A 1 187 ? 17.17157  2.32764   -28.27174 1.000 12.94695  ? 1239 ASN   B O    1 
ATOM   1282 C  CB   . ASN   A 1 187 ? 18.99579  -0.05017  -28.40701 1.000 9.25269   ? 1239 ASN   B CB   1 
ATOM   1283 C  CG   . ASN   A 1 187 ? 18.98897  -0.33523  -26.89502 1.000 14.34602  ? 1239 ASN   B CG   1 
ATOM   1284 O  OD1  . ASN   A 1 187 ? 18.44911  -1.34830  -26.45300 1.000 13.95023  ? 1239 ASN   B OD1  1 
ATOM   1285 N  ND2  . ASN   A 1 187 ? 19.58796  0.55580   -26.10805 1.000 9.98974   ? 1239 ASN   B ND2  1 
ATOM   1286 N  N    . ASP   A 1 188 ? 15.74480  0.72948   -27.53865 1.000 10.67271  ? 1240 ASP   B N    1 
ATOM   1287 C  CA   . ASP   A 1 188 ? 14.94479  1.63437   -26.71753 1.000 12.82872  ? 1240 ASP   B CA   1 
ATOM   1288 C  C    . ASP   A 1 188 ? 14.44059  2.81835   -27.54244 1.000 13.73785  ? 1240 ASP   B C    1 
ATOM   1289 O  O    . ASP   A 1 188 ? 14.42353  3.95933   -27.08340 1.000 13.07500  ? 1240 ASP   B O    1 
ATOM   1290 C  CB   . ASP   A 1 188 ? 15.75487  2.10940   -25.51160 1.000 17.86793  ? 1240 ASP   B CB   1 
ATOM   1291 C  CG   . ASP   A 1 188 ? 14.88694  2.58828   -24.36649 1.000 20.59329  ? 1240 ASP   B CG   1 
ATOM   1292 O  OD1  . ASP   A 1 188 ? 13.72500  2.12316   -24.24539 1.000 16.29033  ? 1240 ASP   B OD1  1 
ATOM   1293 O  OD2  . ASP   A 1 188 ? 15.39594  3.42430   -23.57852 1.000 17.24259  ? 1240 ASP   B OD2  1 
ATOM   1294 N  N    . GLY   A 1 189 ? 14.05449  2.54736   -28.78441 1.000 15.25208  ? 1241 GLY   B N    1 
ATOM   1295 C  CA   . GLY   A 1 189 ? 13.53530  3.58934   -29.64732 1.000 13.76784  ? 1241 GLY   B CA   1 
ATOM   1296 C  C    . GLY   A 1 189 ? 14.57515  4.55546   -30.17039 1.000 16.03063  ? 1241 GLY   B C    1 
ATOM   1297 O  O    . GLY   A 1 189 ? 14.21200  5.62344   -30.66431 1.000 19.50948  ? 1241 GLY   B O    1 
ATOM   1298 N  N    . VAL   A 1 190 ? 15.85920  4.21358   -30.07653 1.000 9.54068   ? 1242 VAL   B N    1 
ATOM   1299 C  CA   . VAL   A 1 190 ? 16.95107  5.05870   -30.53662 1.000 14.28713  ? 1242 VAL   B CA   1 
ATOM   1300 C  C    . VAL   A 1 190 ? 17.71703  4.30082   -31.60872 1.000 14.92020  ? 1242 VAL   B C    1 
ATOM   1301 O  O    . VAL   A 1 190 ? 18.05917  3.12784   -31.41880 1.000 14.02706  ? 1242 VAL   B O    1 
ATOM   1302 C  CB   . VAL   A 1 190 ? 17.88015  5.46375   -29.37770 1.000 16.50804  ? 1242 VAL   B CB   1 
ATOM   1303 C  CG1  . VAL   A 1 190 ? 19.02501  6.34688   -29.87678 1.000 18.61917  ? 1242 VAL   B CG1  1 
ATOM   1304 C  CG2  . VAL   A 1 190 ? 17.08419  6.15364   -28.29459 1.000 18.25177  ? 1242 VAL   B CG2  1 
ATOM   1305 N  N    . LEU   A 1 191 ? 17.97285  4.96888   -32.73572 1.000 14.39388  ? 1243 LEU   B N    1 
ATOM   1306 C  CA   . LEU   A 1 191 ? 18.67979  4.37399   -33.86182 1.000 14.52232  ? 1243 LEU   B CA   1 
ATOM   1307 C  C    . LEU   A 1 191 ? 20.17578  4.65914   -33.74196 1.000 17.58961  ? 1243 LEU   B C    1 
ATOM   1308 O  O    . LEU   A 1 191 ? 20.58967  5.82117   -33.67296 1.000 15.24274  ? 1243 LEU   B O    1 
ATOM   1309 C  CB   . LEU   A 1 191 ? 18.13660  4.92399   -35.18074 1.000 14.63421  ? 1243 LEU   B CB   1 
ATOM   1310 C  CG   . LEU   A 1 191 ? 18.71453  4.31909   -36.46382 1.000 14.02702  ? 1243 LEU   B CG   1 
ATOM   1311 C  CD1  . LEU   A 1 191 ? 18.26066  2.86905   -36.62883 1.000 12.19347  ? 1243 LEU   B CD1  1 
ATOM   1312 C  CD2  . LEU   A 1 191 ? 18.31532  5.17210   -37.68675 1.000 20.02457  ? 1243 LEU   B CD2  1 
ATOM   1313 N  N    . TRP   A 1 192 ? 20.98288  3.60721   -33.73808 1.000 13.34664  ? 1244 TRP   B N    1 
ATOM   1314 C  CA   . TRP   A 1 192 ? 22.41789  3.74235   -33.55822 1.000 14.26525  ? 1244 TRP   B CA   1 
ATOM   1315 C  C    . TRP   A 1 192 ? 23.15780  3.31247   -34.81632 1.000 20.44949  ? 1244 TRP   B C    1 
ATOM   1316 O  O    . TRP   A 1 192 ? 22.77183  2.34245   -35.47831 1.000 17.00255  ? 1244 TRP   B O    1 
ATOM   1317 C  CB   . TRP   A 1 192 ? 22.90309  2.90635   -32.37730 1.000 15.45444  ? 1244 TRP   B CB   1 
ATOM   1318 C  CG   . TRP   A 1 192 ? 22.38818  3.34426   -31.05824 1.000 15.25276  ? 1244 TRP   B CG   1 
ATOM   1319 C  CD1  . TRP   A 1 192 ? 21.15826  3.06912   -30.52212 1.000 15.75259  ? 1244 TRP   B CD1  1 
ATOM   1320 C  CD2  . TRP   A 1 192 ? 23.09121  4.11429   -30.07728 1.000 16.66172  ? 1244 TRP   B CD2  1 
ATOM   1321 N  NE1  . TRP   A 1 192 ? 21.05034  3.63606   -29.27409 1.000 16.85376  ? 1244 TRP   B NE1  1 
ATOM   1322 C  CE2  . TRP   A 1 192 ? 22.22530  4.27616   -28.97319 1.000 22.21878  ? 1244 TRP   B CE2  1 
ATOM   1323 C  CE3  . TRP   A 1 192 ? 24.36616  4.68641   -30.02439 1.000 23.76396  ? 1244 TRP   B CE3  1 
ATOM   1324 C  CZ2  . TRP   A 1 192 ? 22.59435  4.99616   -27.82820 1.000 24.52334  ? 1244 TRP   B CZ2  1 
ATOM   1325 C  CZ3  . TRP   A 1 192 ? 24.73720  5.39241   -28.88140 1.000 24.44294  ? 1244 TRP   B CZ3  1 
ATOM   1326 C  CH2  . TRP   A 1 192 ? 23.85030  5.54628   -27.80331 1.000 19.93814  ? 1244 TRP   B CH2  1 
ATOM   1327 N  N    . ASP   A 1 193 ? 24.23370  4.03058   -35.12740 1.000 18.93236  ? 1245 ASP   B N    1 
ATOM   1328 C  CA   . ASP   A 1 193 ? 25.17263  3.61271   -36.15451 1.000 15.14182  ? 1245 ASP   B CA   1 
ATOM   1329 C  C    . ASP   A 1 193 ? 26.27078  2.79380   -35.48165 1.000 17.63249  ? 1245 ASP   B C    1 
ATOM   1330 O  O    . ASP   A 1 193 ? 26.96582  3.29183   -34.58571 1.000 21.62256  ? 1245 ASP   B O    1 
ATOM   1331 C  CB   . ASP   A 1 193 ? 25.74544  4.82180   -36.89053 1.000 12.31665  ? 1245 ASP   B CB   1 
ATOM   1332 C  CG   . ASP   A 1 193 ? 26.96739  4.46795   -37.72367 1.000 20.59574  ? 1245 ASP   B CG   1 
ATOM   1333 O  OD1  . ASP   A 1 193 ? 26.80834  3.86697   -38.79967 1.000 28.38407  ? 1245 ASP   B OD1  1 
ATOM   1334 O  OD2  . ASP   A 1 193 ? 28.09740  4.76804   -37.28577 1.000 19.76554  ? 1245 ASP   B OD2  1 
ATOM   1335 N  N    . VAL   A 1 194 ? 26.41786  1.53583   -35.89872 1.000 13.55647  ? 1246 VAL   B N    1 
ATOM   1336 C  CA   . VAL   A 1 194 ? 27.26203  0.60088   -35.15884 1.000 19.54878  ? 1246 VAL   B CA   1 
ATOM   1337 C  C    . VAL   A 1 194 ? 28.73798  0.98803   -35.26997 1.000 23.99061  ? 1246 VAL   B C    1 
ATOM   1338 O  O    . VAL   A 1 194 ? 29.45007  1.09306   -34.26004 1.000 18.00326  ? 1246 VAL   B O    1 
ATOM   1339 C  CB   . VAL   A 1 194 ? 27.01412  -0.83612  -35.64786 1.000 18.84567  ? 1246 VAL   B CB   1 
ATOM   1340 C  CG1  . VAL   A 1 194 ? 27.96829  -1.80106  -34.95900 1.000 16.07471  ? 1246 VAL   B CG1  1 
ATOM   1341 C  CG2  . VAL   A 1 194 ? 25.55319  -1.24528  -35.40573 1.000 12.93338  ? 1246 VAL   B CG2  1 
ATOM   1342 N  N    . ARG   A 1 195 ? 29.21983  1.19612   -36.49602 1.000 16.21430  ? 1247 ARG   B N    1 
ATOM   1343 C  CA   . ARG   A 1 195 ? 30.64479  1.43427   -36.72315 1.000 21.57749  ? 1247 ARG   B CA   1 
ATOM   1344 C  C    . ARG   A 1 195 ? 31.15575  2.62929   -35.92516 1.000 21.33726  ? 1247 ARG   B C    1 
ATOM   1345 O  O    . ARG   A 1 195 ? 32.28581  2.61438   -35.42428 1.000 20.97117  ? 1247 ARG   B O    1 
ATOM   1346 C  CB   . ARG   A 1 195 ? 30.89762  1.62235   -38.22217 1.000 23.03936  ? 1247 ARG   B CB   1 
ATOM   1347 C  CG   . ARG   A 1 195 ? 32.33254  1.99450   -38.59131 1.000 25.49029  ? 1247 ARG   B CG   1 
ATOM   1348 C  CD   . ARG   A 1 195 ? 32.65443  1.65359   -40.04335 1.000 31.68107  ? 1247 ARG   B CD   1 
ATOM   1349 N  NE   . ARG   A 1 195 ? 34.06937  1.85174   -40.34349 1.000 36.81232  ? 1247 ARG   B NE   1 
ATOM   1350 C  CZ   . ARG   A 1 195 ? 34.60726  1.75283   -41.55455 1.000 46.24089  ? 1247 ARG   B CZ   1 
ATOM   1351 N  NH1  . ARG   A 1 195 ? 33.87118  1.45580   -42.61848 1.000 39.29906  ? 1247 ARG   B NH1  1 
ATOM   1352 N  NH2  . ARG   A 1 195 ? 35.91422  1.96397   -41.70468 1.000 41.04641  ? 1247 ARG   B NH2  1 
ATOM   1353 N  N    . SER   A 1 196 ? 30.34466  3.66921   -35.78804 1.000 17.95835  ? 1248 SER   B N    1 
ATOM   1354 C  CA   . SER   A 1 196 ? 30.72163  4.85022   -35.02304 1.000 22.56915  ? 1248 SER   B CA   1 
ATOM   1355 C  C    . SER   A 1 196 ? 30.22878  4.81112   -33.58399 1.000 24.82021  ? 1248 SER   B C    1 
ATOM   1356 O  O    . SER   A 1 196 ? 30.55077  5.71412   -32.80799 1.000 27.20734  ? 1248 SER   B O    1 
ATOM   1357 C  CB   . SER   A 1 196 ? 30.19443  6.11919   -35.70394 1.000 23.17094  ? 1248 SER   B CB   1 
ATOM   1358 O  OG   . SER   A 1 196 ? 28.78444  6.23304   -35.53679 1.000 21.90149  ? 1248 SER   B OG   1 
ATOM   1359 N  N    . ALA   A 1 197 ? 29.44192  3.80303   -33.21194 1.000 27.26627  ? 1249 ALA   B N    1 
ATOM   1360 C  CA   . ALA   A 1 197 ? 28.83106  3.74192   -31.88488 1.000 23.25735  ? 1249 ALA   B CA   1 
ATOM   1361 C  C    . ALA   A 1 197 ? 28.15596  5.06684   -31.54177 1.000 26.44933  ? 1249 ALA   B C    1 
ATOM   1362 O  O    . ALA   A 1 197 ? 28.24603  5.56681   -30.41876 1.000 25.32301  ? 1249 ALA   B O    1 
ATOM   1363 C  CB   . ALA   A 1 197 ? 29.86020  3.35598   -30.82000 1.000 26.45115  ? 1249 ALA   B CB   1 
ATOM   1364 N  N    . GLN   A 1 198 ? 27.46681  5.64081   -32.52367 1.000 24.91435  ? 1250 GLN   B N    1 
ATOM   1365 C  CA   . GLN   A 1 198 ? 26.82169  6.93874   -32.37456 1.000 31.04669  ? 1250 GLN   B CA   1 
ATOM   1366 C  C    . GLN   A 1 198 ? 25.31268  6.83460   -32.57841 1.000 25.30577  ? 1250 GLN   B C    1 
ATOM   1367 O  O    . GLN   A 1 198 ? 24.83165  6.17758   -33.51338 1.000 21.50192  ? 1250 GLN   B O    1 
ATOM   1368 C  CB   . GLN   A 1 198 ? 27.40049  7.94783   -33.36558 1.000 31.17170  ? 1250 GLN   B CB   1 
ATOM   1369 C  CG   . GLN   A 1 198 ? 27.23640  9.38280   -32.92752 1.000 48.55092  ? 1250 GLN   B CG   1 
ATOM   1370 C  CD   . GLN   A 1 198 ? 28.52140  9.96190   -32.34963 1.000 58.32451  ? 1250 GLN   B CD   1 
ATOM   1371 O  OE1  . GLN   A 1 198 ? 29.56946  9.31401   -32.37076 1.000 46.55484  ? 1250 GLN   B OE1  1 
ATOM   1372 N  NE2  . GLN   A 1 198 ? 28.44433  11.18988  -31.83457 1.000 64.37319  ? 1250 GLN   B NE2  1 
ATOM   1373 N  N    . ALA   A 1 199 ? 24.56471  7.50049   -31.71031 1.000 19.87751  ? 1251 ALA   B N    1 
ATOM   1374 C  CA   . ALA   A 1 199 ? 23.11968  7.57036   -31.86816 1.000 23.21694  ? 1251 ALA   B CA   1 
ATOM   1375 C  C    . ALA   A 1 199 ? 22.79647  8.57036   -32.97109 1.000 31.92113  ? 1251 ALA   B C    1 
ATOM   1376 O  O    . ALA   A 1 199 ? 23.22837  9.72440   -32.90709 1.000 25.44195  ? 1251 ALA   B O    1 
ATOM   1377 C  CB   . ALA   A 1 199 ? 22.46178  7.97524   -30.55108 1.000 15.89935  ? 1251 ALA   B CB   1 
ATOM   1378 N  N    . ILE   A 1 200 ? 22.04141  8.14233   -33.98503 1.000 24.17005  ? 1252 ILE   B N    1 
ATOM   1379 C  CA   . ILE   A 1 200 ? 21.73221  9.04134   -35.09396 1.000 26.20698  ? 1252 ILE   B CA   1 
ATOM   1380 C  C    . ILE   A 1 200 ? 20.30716  9.60320   -35.06580 1.000 23.14217  ? 1252 ILE   B C    1 
ATOM   1381 O  O    . ILE   A 1 200 ? 20.05999  10.62920  -35.71173 1.000 24.55303  ? 1252 ILE   B O    1 
ATOM   1382 C  CB   . ILE   A 1 200 ? 22.01113  8.36941   -36.45802 1.000 20.73169  ? 1252 ILE   B CB   1 
ATOM   1383 C  CG1  . ILE   A 1 200 ? 21.41526  6.96736   -36.52801 1.000 20.56474  ? 1252 ILE   B CG1  1 
ATOM   1384 C  CG2  . ILE   A 1 200 ? 23.50611  8.30757   -36.71617 1.000 27.87015  ? 1252 ILE   B CG2  1 
ATOM   1385 C  CD1  . ILE   A 1 200 ? 21.63719  6.29043   -37.88305 1.000 24.40319  ? 1252 ILE   B CD1  1 
ATOM   1386 N  N    . HIS   A 1 201 ? 19.37329  8.97808   -34.34472 1.000 17.99915  ? 1253 HIS   B N    1 
ATOM   1387 C  CA   . HIS   A 1 201 ? 18.00125  9.47594   -34.28956 1.000 18.52461  ? 1253 HIS   B CA   1 
ATOM   1388 C  C    . HIS   A 1 201 ? 17.26943  8.85283   -33.10751 1.000 19.33903  ? 1253 HIS   B C    1 
ATOM   1389 O  O    . HIS   A 1 201 ? 17.41158  7.65883   -32.83757 1.000 14.57496  ? 1253 HIS   B O    1 
ATOM   1390 C  CB   . HIS   A 1 201 ? 17.23215  9.16791   -35.58550 1.000 17.45266  ? 1253 HIS   B CB   1 
ATOM   1391 C  CG   . HIS   A 1 201 ? 15.87708  9.80978   -35.65733 1.000 21.30579  ? 1253 HIS   B CG   1 
ATOM   1392 N  ND1  . HIS   A 1 201 ? 15.69992  11.15178  -35.92227 1.000 22.60435  ? 1253 HIS   B ND1  1 
ATOM   1393 C  CD2  . HIS   A 1 201 ? 14.63214  9.29366   -35.51022 1.000 25.15029  ? 1253 HIS   B CD2  1 
ATOM   1394 C  CE1  . HIS   A 1 201 ? 14.40889  11.43465  -35.93112 1.000 22.51401  ? 1253 HIS   B CE1  1 
ATOM   1395 N  NE2  . HIS   A 1 201 ? 13.73702  10.32357  -35.69110 1.000 18.85354  ? 1253 HIS   B NE2  1 
ATOM   1396 N  N    . LYS   A 1 202 ? 16.46542  9.65872   -32.42140 1.000 14.55615  ? 1254 LYS   B N    1 
ATOM   1397 C  CA   . LYS   A 1 202 ? 15.60758  9.16560   -31.35133 1.000 18.37671  ? 1254 LYS   B CA   1 
ATOM   1398 C  C    . LYS   A 1 202 ? 14.16153  9.24848   -31.80318 1.000 16.54525  ? 1254 LYS   B C    1 
ATOM   1399 O  O    . LYS   A 1 202 ? 13.66739  10.33944  -32.09709 1.000 14.30819  ? 1254 LYS   B O    1 
ATOM   1400 C  CB   . LYS   A 1 202 ? 15.79163  9.96757   -30.06732 1.000 23.12418  ? 1254 LYS   B CB   1 
ATOM   1401 C  CG   . LYS   A 1 202 ? 14.77978  9.58643   -28.99223 1.000 18.71990  ? 1254 LYS   B CG   1 
ATOM   1402 C  CD   . LYS   A 1 202 ? 14.87681  10.52440  -27.81421 1.000 30.64475  ? 1254 LYS   B CD   1 
ATOM   1403 C  CE   . LYS   A 1 202 ? 13.85895  10.18726  -26.75911 1.000 20.43010  ? 1254 LYS   B CE   1 
ATOM   1404 N  NZ   . LYS   A 1 202 ? 12.54791  9.95516   -27.40799 1.000 29.79181  ? 1254 LYS   B NZ   1 
ATOM   1405 N  N    . PHE   A 1 203 ? 13.48263  8.10741   -31.85215 1.000 14.53770  ? 1255 PHE   B N    1 
ATOM   1406 C  CA   . PHE   A 1 203 ? 12.06660  8.10928   -32.16900 1.000 9.87613   ? 1255 PHE   B CA   1 
ATOM   1407 C  C    . PHE   A 1 203 ? 11.26170  8.40516   -30.91491 1.000 15.34298  ? 1255 PHE   B C    1 
ATOM   1408 O  O    . PHE   A 1 203 ? 11.52986  7.85715   -29.84496 1.000 17.27859  ? 1255 PHE   B O    1 
ATOM   1409 C  CB   . PHE   A 1 203 ? 11.64467  6.77926   -32.78701 1.000 11.89967  ? 1255 PHE   B CB   1 
ATOM   1410 C  CG   . PHE   A 1 203 ? 12.25455  6.53737   -34.13708 1.000 11.11677  ? 1255 PHE   B CG   1 
ATOM   1411 C  CD1  . PHE   A 1 203 ? 11.66938  7.05736   -35.28200 1.000 12.44157  ? 1255 PHE   B CD1  1 
ATOM   1412 C  CD2  . PHE   A 1 203 ? 13.44561  5.83349   -34.25623 1.000 13.38728  ? 1255 PHE   B CD2  1 
ATOM   1413 C  CE1  . PHE   A 1 203 ? 12.23927  6.86546   -36.52707 1.000 9.37680   ? 1255 PHE   B CE1  1 
ATOM   1414 C  CE2  . PHE   A 1 203 ? 14.02150  5.62660   -35.49829 1.000 17.91363  ? 1255 PHE   B CE2  1 
ATOM   1415 C  CZ   . PHE   A 1 203 ? 13.42033  6.15158   -36.63821 1.000 18.10280  ? 1255 PHE   B CZ   1 
ATOM   1416 N  N    . ASP   A 1 204 ? 10.27360  9.28407   -31.05578 1.000 16.43506  ? 1256 ASP   B N    1 
ATOM   1417 C  CA   . ASP   A 1 204 ? 9.46267   9.69895   -29.92368 1.000 14.52831  ? 1256 ASP   B CA   1 
ATOM   1418 C  C    . ASP   A 1 204 ? 8.68885   8.51985   -29.35264 1.000 18.56632  ? 1256 ASP   B C    1 
ATOM   1419 O  O    . ASP   A 1 204 ? 8.37387   7.55184   -30.05465 1.000 18.65653  ? 1256 ASP   B O    1 
ATOM   1420 C  CB   . ASP   A 1 204 ? 8.49652   10.80987  -30.35254 1.000 16.74855  ? 1256 ASP   B CB   1 
ATOM   1421 C  CG   . ASP   A 1 204 ? 9.21036   12.12295  -30.63357 1.000 26.97298  ? 1256 ASP   B CG   1 
ATOM   1422 O  OD1  . ASP   A 1 204 ? 10.31240  12.32504  -30.06867 1.000 26.66408  ? 1256 ASP   B OD1  1 
ATOM   1423 O  OD2  . ASP   A 1 204 ? 8.67720   12.94692  -31.41048 1.000 29.80301  ? 1256 ASP   B OD2  1 
ATOM   1424 N  N    . LYS   A 1 205 ? 8.38297   8.61277   -28.05861 1.000 17.88224  ? 1257 LYS   B N    1 
ATOM   1425 C  CA   . LYS   A 1 205 ? 7.74616   7.53868   -27.30658 1.000 20.77274  ? 1257 LYS   B CA   1 
ATOM   1426 C  C    . LYS   A 1 205 ? 6.23113   7.69554   -27.35742 1.000 18.06703  ? 1257 LYS   B C    1 
ATOM   1427 O  O    . LYS   A 1 205 ? 5.69508   8.72747   -26.93433 1.000 17.40185  ? 1257 LYS   B O    1 
ATOM   1428 C  CB   . LYS   A 1 205 ? 8.22930   7.55668   -25.85763 1.000 18.69447  ? 1257 LYS   B CB   1 
ATOM   1429 C  CG   . LYS   A 1 205 ? 7.64650   6.45259   -24.96361 1.000 18.32251  ? 1257 LYS   B CG   1 
ATOM   1430 C  CD   . LYS   A 1 205 ? 8.20263   6.60759   -23.53766 1.000 14.38536  ? 1257 LYS   B CD   1 
ATOM   1431 C  CE   . LYS   A 1 205 ? 7.82184   5.43952   -22.64866 1.000 19.34501  ? 1257 LYS   B CE   1 
ATOM   1432 N  NZ   . LYS   A 1 205 ? 8.44397   5.56453   -21.29072 1.000 14.58700  ? 1257 LYS   B NZ   1 
ATOM   1433 N  N    . PHE   A 1 206 ? 5.54618   6.66649   -27.86239 1.000 14.19952  ? 1258 PHE   B N    1 
ATOM   1434 C  CA   . PHE   A 1 206 ? 4.09517   6.68635   -27.99024 1.000 17.71558  ? 1258 PHE   B CA   1 
ATOM   1435 C  C    . PHE   A 1 206 ? 3.42535   5.47526   -27.34721 1.000 16.98559  ? 1258 PHE   B C    1 
ATOM   1436 O  O    . PHE   A 1 206 ? 2.21335   5.29715   -27.51809 1.000 18.92322  ? 1258 PHE   B O    1 
ATOM   1437 C  CB   . PHE   A 1 206 ? 3.68701   6.80236   -29.46919 1.000 14.44788  ? 1258 PHE   B CB   1 
ATOM   1438 C  CG   . PHE   A 1 206 ? 4.06981   8.11542   -30.09818 1.000 20.54711  ? 1258 PHE   B CG   1 
ATOM   1439 C  CD1  . PHE   A 1 206 ? 3.43274   9.28935   -29.72107 1.000 25.67353  ? 1258 PHE   B CD1  1 
ATOM   1440 C  CD2  . PHE   A 1 206 ? 5.06671   8.18256   -31.05728 1.000 21.62194  ? 1258 PHE   B CD2  1 
ATOM   1441 C  CE1  . PHE   A 1 206 ? 3.78856   10.50740  -30.28607 1.000 17.24112  ? 1258 PHE   B CE1  1 
ATOM   1442 C  CE2  . PHE   A 1 206 ? 5.41353   9.39361   -31.63227 1.000 19.10304  ? 1258 PHE   B CE2  1 
ATOM   1443 C  CZ   . PHE   A 1 206 ? 4.77545   10.56053  -31.24317 1.000 15.35960  ? 1258 PHE   B CZ   1 
ATOM   1444 N  N    . ASN   A 1 207 ? 4.17551   4.63931   -26.62832 1.000 15.37307  ? 1259 ASN   B N    1 
ATOM   1445 C  CA   . ASN   A 1 207 ? 3.61970   3.54423   -25.84530 1.000 13.28741  ? 1259 ASN   B CA   1 
ATOM   1446 C  C    . ASN   A 1 207 ? 4.60984   3.23528   -24.73341 1.000 14.18430  ? 1259 ASN   B C    1 
ATOM   1447 O  O    . ASN   A 1 207 ? 5.71279   3.77639   -24.69851 1.000 14.08521  ? 1259 ASN   B O    1 
ATOM   1448 C  CB   . ASN   A 1 207 ? 3.35173   2.30723   -26.70332 1.000 11.43188  ? 1259 ASN   B CB   1 
ATOM   1449 C  CG   . ASN   A 1 207 ? 4.57081   1.40935   -26.81448 1.000 10.93446  ? 1259 ASN   B CG   1 
ATOM   1450 O  OD1  . ASN   A 1 207 ? 5.55270   1.75148   -27.48557 1.000 16.43433  ? 1259 ASN   B OD1  1 
ATOM   1451 N  ND2  . ASN   A 1 207 ? 4.51099   0.25433   -26.17451 1.000 7.92066   ? 1259 ASN   B ND2  1 
ATOM   1452 N  N    . MET   A 1 208 ? 4.21302   2.34721   -23.82341 1.000 12.18296  ? 1260 MET   B N    1 
ATOM   1453 C  CA   . MET   A 1 208 ? 5.01517   2.10825   -22.62950 1.000 15.62157  ? 1260 MET   B CA   1 
ATOM   1454 C  C    . MET   A 1 208 ? 5.98127   0.93235   -22.73264 1.000 18.50825  ? 1260 MET   B C    1 
ATOM   1455 O  O    . MET   A 1 208 ? 6.94336   0.88141   -21.95674 1.000 14.78141  ? 1260 MET   B O    1 
ATOM   1456 C  CB   . MET   A 1 208 ? 4.10932   1.87411   -21.41741 1.000 16.31356  ? 1260 MET   B CB   1 
ATOM   1457 C  CG   . MET   A 1 208 ? 3.40724   3.15103   -20.90729 1.000 25.01014  ? 1260 MET   B CG   1 
ATOM   1458 S  SD   . MET   A 1 208 ? 4.51814   4.55012   -20.54936 1.000 44.11017  ? 1260 MET   B SD   1 
ATOM   1459 C  CE   . MET   A 1 208 ? 4.47289   5.42818   -22.12432 1.000 32.46950  ? 1260 MET   B CE   1 
ATOM   1460 N  N    . ASN   A 1 209 ? 5.76027   -0.00464  -23.65565 1.000 13.61037  ? 1261 ASN   B N    1 
ATOM   1461 C  CA   . ASN   A 1 209 ? 6.44740   -1.29358  -23.62277 1.000 13.14946  ? 1261 ASN   B CA   1 
ATOM   1462 C  C    . ASN   A 1 209 ? 7.30030   -1.58345  -24.84987 1.000 12.96757  ? 1261 ASN   B C    1 
ATOM   1463 O  O    . ASN   A 1 209 ? 8.45936   -1.99834  -24.70100 1.000 13.96846  ? 1261 ASN   B O    1 
ATOM   1464 C  CB   . ASN   A 1 209 ? 5.40853   -2.40669  -23.43970 1.000 11.12683  ? 1261 ASN   B CB   1 
ATOM   1465 C  CG   . ASN   A 1 209 ? 4.60164   -2.22681  -22.17261 1.000 22.49863  ? 1261 ASN   B CG   1 
ATOM   1466 O  OD1  . ASN   A 1 209 ? 5.16472   -1.94879  -21.10666 1.000 19.77672  ? 1261 ASN   B OD1  1 
ATOM   1467 N  ND2  . ASN   A 1 209 ? 3.27864   -2.35994  -22.27948 1.000 16.30674  ? 1261 ASN   B ND2  1 
ATOM   1468 N  N    . ILE   A 1 210 ? 6.76316   -1.38746  -26.05580 1.000 12.34990  ? 1262 ILE   B N    1 
ATOM   1469 C  CA   . ILE   A 1 210 ? 7.35508   -1.90836  -27.28688 1.000 13.91129  ? 1262 ILE   B CA   1 
ATOM   1470 C  C    . ILE   A 1 210 ? 8.35593   -0.90824  -27.85795 1.000 17.40519  ? 1262 ILE   B C    1 
ATOM   1471 O  O    . ILE   A 1 210 ? 8.01579   0.25774   -28.09987 1.000 11.18162  ? 1262 ILE   B O    1 
ATOM   1472 C  CB   . ILE   A 1 210 ? 6.25301   -2.23443  -28.30878 1.000 19.91032  ? 1262 ILE   B CB   1 
ATOM   1473 C  CG1  . ILE   A 1 210 ? 5.35618   -3.35553  -27.76973 1.000 12.66448  ? 1262 ILE   B CG1  1 
ATOM   1474 C  CG2  . ILE   A 1 210 ? 6.85091   -2.62432  -29.65286 1.000 12.31393  ? 1262 ILE   B CG2  1 
ATOM   1475 C  CD1  . ILE   A 1 210 ? 6.07432   -4.64447  -27.59185 1.000 14.82981  ? 1262 ILE   B CD1  1 
ATOM   1476 N  N    . SER   A 1 211 ? 9.58695   -1.37211  -28.10809 1.000 12.62586  ? 1263 SER   B N    1 
ATOM   1477 C  CA   . SER   A 1 211 ? 10.64781  -0.50798  -28.61617 1.000 9.85640   ? 1263 SER   B CA   1 
ATOM   1478 C  C    . SER   A 1 211 ? 10.86866  -0.58691  -30.12820 1.000 11.46309  ? 1263 SER   B C    1 
ATOM   1479 O  O    . SER   A 1 211 ? 11.51452  0.30818   -30.67823 1.000 11.92344  ? 1263 SER   B O    1 
ATOM   1480 C  CB   . SER   A 1 211 ? 11.96591  -0.83488  -27.90932 1.000 17.64328  ? 1263 SER   B CB   1 
ATOM   1481 O  OG   . SER   A 1 211 ? 12.38801  -2.15683  -28.19741 1.000 11.63164  ? 1263 SER   B OG   1 
ATOM   1482 N  N    . GLY   A 1 212 ? 10.40169  -1.62293  -30.80719 1.000 16.32719  ? 1264 GLY   B N    1 
ATOM   1483 C  CA   . GLY   A 1 212 ? 10.36354  -1.58988  -32.25718 1.000 16.52265  ? 1264 GLY   B CA   1 
ATOM   1484 C  C    . GLY   A 1 212 ? 11.41356  -2.49275  -32.90532 1.000 15.53402  ? 1264 GLY   B C    1 
ATOM   1485 O  O    . GLY   A 1 212 ? 12.45965  -2.80667  -32.32944 1.000 13.22928  ? 1264 GLY   B O    1 
ATOM   1486 N  N    . VAL   A 1 213 ? 11.13047  -2.86574  -34.16431 1.000 12.90613  ? 1265 VAL   B N    1 
ATOM   1487 C  CA   . VAL   A 1 213 ? 11.99847  -3.69862  -34.99042 1.000 10.37533  ? 1265 VAL   B CA   1 
ATOM   1488 C  C    . VAL   A 1 213 ? 12.23026  -3.03555  -36.34942 1.000 17.38459  ? 1265 VAL   B C    1 
ATOM   1489 O  O    . VAL   A 1 213 ? 11.47013  -2.17161  -36.79731 1.000 15.19166  ? 1265 VAL   B O    1 
ATOM   1490 C  CB   . VAL   A 1 213 ? 11.40858  -5.10667  -35.22441 1.000 11.75332  ? 1265 VAL   B CB   1 
ATOM   1491 C  CG1  . VAL   A 1 213 ? 11.11179  -5.80475  -33.91041 1.000 13.89518  ? 1265 VAL   B CG1  1 
ATOM   1492 C  CG2  . VAL   A 1 213 ? 10.13348  -4.99776  -36.07628 1.000 9.77797   ? 1265 VAL   B CG2  1 
ATOM   1493 N  N    . PHE   A 1 214 ? 13.26824  -3.50342  -37.03055 1.000 9.25374   ? 1266 PHE   B N    1 
ATOM   1494 C  CA   . PHE   A 1 214 ? 13.49806  -3.15435  -38.42156 1.000 15.33104  ? 1266 PHE   B CA   1 
ATOM   1495 C  C    . PHE   A 1 214 ? 12.58504  -3.94941  -39.35549 1.000 17.16181  ? 1266 PHE   B C    1 
ATOM   1496 O  O    . PHE   A 1 214 ? 12.35918  -5.14943  -39.16251 1.000 13.16569  ? 1266 PHE   B O    1 
ATOM   1497 C  CB   . PHE   A 1 214 ? 14.96005  -3.41819  -38.78272 1.000 11.31137  ? 1266 PHE   B CB   1 
ATOM   1498 C  CG   . PHE   A 1 214 ? 15.93603  -2.46112  -38.12378 1.000 14.86949  ? 1266 PHE   B CG   1 
ATOM   1499 C  CD1  . PHE   A 1 214 ? 16.19684  -1.21208  -38.69177 1.000 15.89197  ? 1266 PHE   B CD1  1 
ATOM   1500 C  CD2  . PHE   A 1 214 ? 16.61318  -2.81810  -36.96387 1.000 12.40447  ? 1266 PHE   B CD2  1 
ATOM   1501 C  CE1  . PHE   A 1 214 ? 17.10782  -0.33001  -38.10383 1.000 11.34283  ? 1266 PHE   B CE1  1 
ATOM   1502 C  CE2  . PHE   A 1 214 ? 17.52516  -1.94503  -36.36593 1.000 12.71277  ? 1266 PHE   B CE2  1 
ATOM   1503 C  CZ   . PHE   A 1 214 ? 17.77097  -0.69998  -36.93591 1.000 13.84963  ? 1266 PHE   B CZ   1 
ATOM   1504 N  N    . HIS   A 1 215 ? 12.07487  -3.28242  -40.38542 1.000 13.54422  ? 1267 HIS   B N    1 
ATOM   1505 C  CA   . HIS   A 1 215 ? 11.44183  -4.01344  -41.47738 1.000 12.90069  ? 1267 HIS   B CA   1 
ATOM   1506 C  C    . HIS   A 1 215 ? 12.52082  -4.74131  -42.28452 1.000 15.41092  ? 1267 HIS   B C    1 
ATOM   1507 O  O    . HIS   A 1 215 ? 13.63976  -4.23419  -42.41661 1.000 13.30281  ? 1267 HIS   B O    1 
ATOM   1508 C  CB   . HIS   A 1 215 ? 10.65465  -3.05849  -42.37826 1.000 17.28074  ? 1267 HIS   B CB   1 
ATOM   1509 C  CG   . HIS   A 1 215 ? 9.83560   -3.73753  -43.43820 1.000 17.62859  ? 1267 HIS   B CG   1 
ATOM   1510 N  ND1  . HIS   A 1 215 ? 10.39856  -4.39143  -44.51729 1.000 16.56302  ? 1267 HIS   B ND1  1 
ATOM   1511 C  CD2  . HIS   A 1 215 ? 8.49260   -3.83265  -43.60207 1.000 13.45136  ? 1267 HIS   B CD2  1 
ATOM   1512 C  CE1  . HIS   A 1 215 ? 9.43953   -4.87550  -45.28720 1.000 16.76948  ? 1267 HIS   B CE1  1 
ATOM   1513 N  NE2  . HIS   A 1 215 ? 8.27255   -4.54663  -44.75707 1.000 19.10183  ? 1267 HIS   B NE2  1 
ATOM   1514 N  N    . PRO   A 1 216 ? 12.22689  -5.93832  -42.80153 1.000 14.39285  ? 1268 PRO   B N    1 
ATOM   1515 C  CA   . PRO   A 1 216 ? 13.24188  -6.68019  -43.57466 1.000 15.95866  ? 1268 PRO   B CA   1 
ATOM   1516 C  C    . PRO   A 1 216 ? 13.77668  -5.93309  -44.78669 1.000 19.62498  ? 1268 PRO   B C    1 
ATOM   1517 O  O    . PRO   A 1 216 ? 14.89367  -6.22697  -45.22781 1.000 13.00174  ? 1268 PRO   B O    1 
ATOM   1518 C  CB   . PRO   A 1 216 ? 12.49796  -7.95025  -44.00763 1.000 14.46197  ? 1268 PRO   B CB   1 
ATOM   1519 C  CG   . PRO   A 1 216 ? 11.41608  -8.11239  -43.00552 1.000 20.48717  ? 1268 PRO   B CG   1 
ATOM   1520 C  CD   . PRO   A 1 216 ? 11.01699  -6.73844  -42.55043 1.000 14.71889  ? 1268 PRO   B CD   1 
ATOM   1521 N  N    . ASN   A 1 217 ? 13.01253  -4.99915  -45.36058 1.000 15.61830  ? 1269 ASN   B N    1 
ATOM   1522 C  CA   . ASN   A 1 217 ? 13.50034  -4.27006  -46.52460 1.000 19.81593  ? 1269 ASN   B CA   1 
ATOM   1523 C  C    . ASN   A 1 217 ? 14.60428  -3.27696  -46.17568 1.000 20.49284  ? 1269 ASN   B C    1 
ATOM   1524 O  O    . ASN   A 1 217 ? 15.19213  -2.68587  -47.08572 1.000 24.80509  ? 1269 ASN   B O    1 
ATOM   1525 C  CB   . ASN   A 1 217 ? 12.33720  -3.54914  -47.22545 1.000 12.87149  ? 1269 ASN   B CB   1 
ATOM   1526 C  CG   . ASN   A 1 217 ? 11.74917  -2.41323  -46.39035 1.000 23.33546  ? 1269 ASN   B CG   1 
ATOM   1527 O  OD1  . ASN   A 1 217 ? 12.36822  -1.93721  -45.42440 1.000 17.65843  ? 1269 ASN   B OD1  1 
ATOM   1528 N  ND2  . ASN   A 1 217 ? 10.54309  -1.96134  -46.77221 1.000 14.95001  ? 1269 ASN   B ND2  1 
ATOM   1529 N  N    . GLY   A 1 218 ? 14.88639  -3.06498  -44.89470 1.000 19.37336  ? 1270 GLY   B N    1 
ATOM   1530 C  CA   . GLY   A 1 218 ? 15.95234  -2.17489  -44.49278 1.000 18.41233  ? 1270 GLY   B CA   1 
ATOM   1531 C  C    . GLY   A 1 218 ? 15.65219  -0.69292  -44.58269 1.000 18.21985  ? 1270 GLY   B C    1 
ATOM   1532 O  O    . GLY   A 1 218 ? 16.54014  0.11416   -44.28175 1.000 25.54978  ? 1270 GLY   B O    1 
ATOM   1533 N  N    . LEU   A 1 219 ? 14.44411  -0.29002  -44.98555 1.000 19.70270  ? 1271 LEU   B N    1 
ATOM   1534 C  CA   . LEU   A 1 219 ? 14.19294  1.12597   -45.25348 1.000 23.95290  ? 1271 LEU   B CA   1 
ATOM   1535 C  C    . LEU   A 1 219 ? 13.12797  1.73983   -44.34834 1.000 21.18093  ? 1271 LEU   B C    1 
ATOM   1536 O  O    . LEU   A 1 219 ? 12.77684  2.91880   -44.52926 1.000 12.78936  ? 1271 LEU   B O    1 
ATOM   1537 C  CB   . LEU   A 1 219 ? 13.83277  1.33598   -46.73543 1.000 23.69716  ? 1271 LEU   B CB   1 
ATOM   1538 C  CG   . LEU   A 1 219 ? 14.98168  1.17113   -47.75955 1.000 27.37469  ? 1271 LEU   B CG   1 
ATOM   1539 C  CD1  . LEU   A 1 219 ? 14.50851  1.40414   -49.19650 1.000 26.78151  ? 1271 LEU   B CD1  1 
ATOM   1540 C  CD2  . LEU   A 1 219 ? 16.18762  2.06124   -47.46165 1.000 18.21170  ? 1271 LEU   B CD2  1 
ATOM   1541 N  N    . GLU   A 1 220 ? 12.62415  0.98974   -43.36832 1.000 16.48142  ? 1272 GLU   B N    1 
ATOM   1542 C  CA   . GLU   A 1 220 ? 11.61119  1.51061   -42.46020 1.000 17.46366  ? 1272 GLU   B CA   1 
ATOM   1543 C  C    . GLU   A 1 220 ? 11.66240  0.71957   -41.15723 1.000 14.75579  ? 1272 GLU   B C    1 
ATOM   1544 O  O    . GLU   A 1 220 ? 12.23652  -0.37738  -41.09433 1.000 14.80480  ? 1272 GLU   B O    1 
ATOM   1545 C  CB   . GLU   A 1 220 ? 10.20813  1.47850   -43.10605 1.000 14.42000  ? 1272 GLU   B CB   1 
ATOM   1546 C  CG   . GLU   A 1 220 ? 9.62724   0.10245   -43.36604 1.000 14.63469  ? 1272 GLU   B CG   1 
ATOM   1547 C  CD   . GLU   A 1 220 ? 8.49413   0.12538   -44.40193 1.000 18.34087  ? 1272 GLU   B CD   1 
ATOM   1548 O  OE1  . GLU   A 1 220 ? 8.74597   0.54844   -45.54794 1.000 21.48314  ? 1272 GLU   B OE1  1 
ATOM   1549 O  OE2  . GLU   A 1 220 ? 7.35220   -0.27775  -44.08182 1.000 19.67441  ? 1272 GLU   B OE2  1 
ATOM   1550 N  N    . VAL   A 1 221 ? 11.08745  1.30447   -40.10815 1.000 14.92100  ? 1273 VAL   B N    1 
ATOM   1551 C  CA   . VAL   A 1 221 ? 11.04465  0.66842   -38.79317 1.000 15.70179  ? 1273 VAL   B CA   1 
ATOM   1552 C  C    . VAL   A 1 221 ? 9.61271   0.63226   -38.27802 1.000 18.36042  ? 1273 VAL   B C    1 
ATOM   1553 O  O    . VAL   A 1 221 ? 8.80559   1.53519   -38.53191 1.000 17.19677  ? 1273 VAL   B O    1 
ATOM   1554 C  CB   . VAL   A 1 221 ? 11.95569  1.35947   -37.75724 1.000 15.21551  ? 1273 VAL   B CB   1 
ATOM   1555 C  CG1  . VAL   A 1 221 ? 13.42068  1.10463   -38.07940 1.000 11.99147  ? 1273 VAL   B CG1  1 
ATOM   1556 C  CG2  . VAL   A 1 221 ? 11.65055  2.84844   -37.67215 1.000 15.57509  ? 1273 VAL   B CG2  1 
ATOM   1557 N  N    . ILE   A 1 222 ? 9.31389   -0.42479  -37.53403 1.000 15.19367  ? 1274 ILE   B N    1 
ATOM   1558 C  CA   . ILE   A 1 222 ? 7.98497   -0.71994  -37.01190 1.000 13.80025  ? 1274 ILE   B CA   1 
ATOM   1559 C  C    . ILE   A 1 222 ? 8.07511   -0.59199  -35.49691 1.000 14.12243  ? 1274 ILE   B C    1 
ATOM   1560 O  O    . ILE   A 1 222 ? 8.58827   -1.48996  -34.82799 1.000 17.25960  ? 1274 ILE   B O    1 
ATOM   1561 C  CB   . ILE   A 1 222 ? 7.51806   -2.11897  -37.42591 1.000 10.40245  ? 1274 ILE   B CB   1 
ATOM   1562 C  CG1  . ILE   A 1 222 ? 7.55692   -2.25691  -38.95292 1.000 17.15695  ? 1274 ILE   B CG1  1 
ATOM   1563 C  CG2  . ILE   A 1 222 ? 6.10915   -2.40513  -36.89477 1.000 13.36604  ? 1274 ILE   B CG2  1 
ATOM   1564 C  CD1  . ILE   A 1 222 ? 7.65201   -3.67789  -39.41498 1.000 19.59893  ? 1274 ILE   B CD1  1 
ATOM   1565 N  N    . ILE   A 1 223 ? 7.60506   0.51895   -34.94482 1.000 13.87705  ? 1275 ILE   B N    1 
ATOM   1566 C  CA   . ILE   A 1 223 ? 7.68618   0.77290   -33.50482 1.000 12.28449  ? 1275 ILE   B CA   1 
ATOM   1567 C  C    . ILE   A 1 223 ? 6.25223   0.83074   -33.00067 1.000 11.72716  ? 1275 ILE   B C    1 
ATOM   1568 O  O    . ILE   A 1 223 ? 5.61012   1.88068   -33.03057 1.000 12.79493  ? 1275 ILE   B O    1 
ATOM   1569 C  CB   . ILE   A 1 223 ? 8.44009   2.05796   -33.15985 1.000 11.81191  ? 1275 ILE   B CB   1 
ATOM   1570 C  CG1  . ILE   A 1 223 ? 9.83803   2.04412   -33.76799 1.000 15.06094  ? 1275 ILE   B CG1  1 
ATOM   1571 C  CG2  . ILE   A 1 223 ? 8.49423   2.23091   -31.62685 1.000 9.14476   ? 1275 ILE   B CG2  1 
ATOM   1572 C  CD1  . ILE   A 1 223 ? 10.70095  3.25519   -33.37204 1.000 13.05353  ? 1275 ILE   B CD1  1 
ATOM   1573 N  N    . ASN   A 1 224 ? 5.75039   -0.30132  -32.51566 1.000 13.30865  ? 1276 ASN   B N    1 
ATOM   1574 C  CA   . ASN   A 1 224 ? 4.38145   -0.42448  -32.01052 1.000 11.39626  ? 1276 ASN   B CA   1 
ATOM   1575 C  C    . ASN   A 1 224 ? 3.44830   -0.07953  -33.16042 1.000 13.03206  ? 1276 ASN   B C    1 
ATOM   1576 O  O    . ASN   A 1 224 ? 3.53326   -0.73448  -34.21345 1.000 12.78611  ? 1276 ASN   B O    1 
ATOM   1577 C  CB   . ASN   A 1 224 ? 4.21050   0.42346   -30.74548 1.000 14.84583  ? 1276 ASN   B CB   1 
ATOM   1578 C  CG   . ASN   A 1 224 ? 3.03563   -0.03568  -29.89837 1.000 13.55535  ? 1276 ASN   B CG   1 
ATOM   1579 O  OD1  . ASN   A 1 224 ? 2.92478   -1.21871  -29.57740 1.000 17.49031  ? 1276 ASN   B OD1  1 
ATOM   1580 N  ND2  . ASN   A 1 224 ? 2.12557   0.88921   -29.57524 1.000 14.23454  ? 1276 ASN   B ND2  1 
ATOM   1581 N  N    . THR   A 1 225 ? 2.56822   0.91038   -33.03029 1.000 11.48310  ? 1277 THR   B N    1 
ATOM   1582 C  CA   . THR   A 1 225 ? 1.65507   1.24633   -34.11318 1.000 16.33123  ? 1277 THR   B CA   1 
ATOM   1583 C  C    . THR   A 1 225 ? 2.25987   2.16843   -35.17221 1.000 12.55002  ? 1277 THR   B C    1 
ATOM   1584 O  O    . THR   A 1 225 ? 1.61975   2.37340   -36.19914 1.000 17.63125  ? 1277 THR   B O    1 
ATOM   1585 C  CB   . THR   A 1 225 ? 0.40107   1.89019   -33.52403 1.000 20.30851  ? 1277 THR   B CB   1 
ATOM   1586 O  OG1  . THR   A 1 225 ? 0.78504   3.02220   -32.73903 1.000 10.72792  ? 1277 THR   B OG1  1 
ATOM   1587 C  CG2  . THR   A 1 225 ? -0.31874  0.89009   -32.61499 1.000 14.98601  ? 1277 THR   B CG2  1 
ATOM   1588 N  N    . GLU   A 1 226 ? 3.45584   2.72854   -34.96031 1.000 11.60604  ? 1278 GLU   B N    1 
ATOM   1589 C  CA   . GLU   A 1 226 ? 4.04565   3.71063   -35.87334 1.000 14.36293  ? 1278 GLU   B CA   1 
ATOM   1590 C  C    . GLU   A 1 226 ? 5.00762   3.02476   -36.83946 1.000 18.23313  ? 1278 GLU   B C    1 
ATOM   1591 O  O    . GLU   A 1 226 ? 5.89074   2.27283   -36.41258 1.000 16.66997  ? 1278 GLU   B O    1 
ATOM   1592 C  CB   . GLU   A 1 226 ? 4.80862   4.80568   -35.11238 1.000 12.23209  ? 1278 GLU   B CB   1 
ATOM   1593 C  CG   . GLU   A 1 226 ? 3.94659   5.84357   -34.38625 1.000 13.65229  ? 1278 GLU   B CG   1 
ATOM   1594 C  CD   . GLU   A 1 226 ? 2.99376   5.22144   -33.37518 1.000 16.35546  ? 1278 GLU   B CD   1 
ATOM   1595 O  OE1  . GLU   A 1 226 ? 3.44291   4.83644   -32.27924 1.000 15.56417  ? 1278 GLU   B OE1  1 
ATOM   1596 O  OE2  . GLU   A 1 226 ? 1.79674   5.09833   -33.68906 1.000 18.05766  ? 1278 GLU   B OE2  1 
ATOM   1597 N  N    . ILE   A 1 227 ? 4.84346   3.30179   -38.13244 1.000 15.71864  ? 1279 ILE   B N    1 
ATOM   1598 C  CA   . ILE   A 1 227 ? 5.78539   2.88492   -39.17055 1.000 12.46192  ? 1279 ILE   B CA   1 
ATOM   1599 C  C    . ILE   A 1 227 ? 6.54423   4.12901   -39.60758 1.000 14.36934  ? 1279 ILE   B C    1 
ATOM   1600 O  O    . ILE   A 1 227 ? 5.94608   5.05597   -40.16649 1.000 13.07597  ? 1279 ILE   B O    1 
ATOM   1601 C  CB   . ILE   A 1 227 ? 5.07533   2.24790   -40.37650 1.000 11.77202  ? 1279 ILE   B CB   1 
ATOM   1602 C  CG1  . ILE   A 1 227 ? 4.12649   1.13179   -39.95344 1.000 16.37486  ? 1279 ILE   B CG1  1 
ATOM   1603 C  CG2  . ILE   A 1 227 ? 6.09027   1.78203   -41.39562 1.000 11.38132  ? 1279 ILE   B CG2  1 
ATOM   1604 C  CD1  . ILE   A 1 227 ? 4.78867   -0.00218  -39.21755 1.000 15.28896  ? 1279 ILE   B CD1  1 
ATOM   1605 N  N    . TRP   A 1 228 ? 7.84925   4.16413   -39.35871 1.000 10.98824  ? 1280 TRP   B N    1 
ATOM   1606 C  CA   . TRP   A 1 228 ? 8.66810   5.31822   -39.70276 1.000 11.06303  ? 1280 TRP   B CA   1 
ATOM   1607 C  C    . TRP   A 1 228 ? 9.57001   5.01235   -40.89586 1.000 17.88066  ? 1280 TRP   B C    1 
ATOM   1608 O  O    . TRP   A 1 228 ? 10.14610  3.92341   -40.99596 1.000 13.76929  ? 1280 TRP   B O    1 
ATOM   1609 C  CB   . TRP   A 1 228 ? 9.53918   5.76927   -38.52583 1.000 9.09299   ? 1280 TRP   B CB   1 
ATOM   1610 C  CG   . TRP   A 1 228 ? 8.81127   6.12515   -37.25774 1.000 13.35016  ? 1280 TRP   B CG   1 
ATOM   1611 C  CD1  . TRP   A 1 228 ? 8.75146   5.38110   -36.10476 1.000 13.27906  ? 1280 TRP   B CD1  1 
ATOM   1612 C  CD2  . TRP   A 1 228 ? 8.07818   7.33407   -36.99062 1.000 15.46736  ? 1280 TRP   B CD2  1 
ATOM   1613 N  NE1  . TRP   A 1 228 ? 8.02050   6.04999   -35.14666 1.000 14.69825  ? 1280 TRP   B NE1  1 
ATOM   1614 C  CE2  . TRP   A 1 228 ? 7.59333   7.24597   -35.66758 1.000 15.91893  ? 1280 TRP   B CE2  1 
ATOM   1615 C  CE3  . TRP   A 1 228 ? 7.77299   8.47406   -37.74655 1.000 15.91533  ? 1280 TRP   B CE3  1 
ATOM   1616 C  CZ2  . TRP   A 1 228 ? 6.82529   8.25688   -35.08546 1.000 19.52519  ? 1280 TRP   B CZ2  1 
ATOM   1617 C  CZ3  . TRP   A 1 228 ? 7.01295   9.47897   -37.16744 1.000 18.48146  ? 1280 TRP   B CZ3  1 
ATOM   1618 C  CH2  . TRP   A 1 228 ? 6.54310   9.35988   -35.84939 1.000 22.35749  ? 1280 TRP   B CH2  1 
ATOM   1619 N  N    . ASP   A 1 229 ? 9.69982   5.98940   -41.78884 1.000 14.70295  ? 1281 ASP   B N    1 
ATOM   1620 C  CA   . ASP   A 1 229 ? 10.59971  5.90153   -42.93093 1.000 16.40762  ? 1281 ASP   B CA   1 
ATOM   1621 C  C    . ASP   A 1 229 ? 12.02272  6.25165   -42.50007 1.000 15.91780  ? 1281 ASP   B C    1 
ATOM   1622 O  O    . ASP   A 1 229 ? 12.25268  7.32066   -41.92705 1.000 15.55791  ? 1281 ASP   B O    1 
ATOM   1623 C  CB   . ASP   A 1 229 ? 10.12451  6.87152   -44.01085 1.000 12.67457  ? 1281 ASP   B CB   1 
ATOM   1624 C  CG   . ASP   A 1 229 ? 10.73939  6.59863   -45.35992 1.000 18.60942  ? 1281 ASP   B CG   1 
ATOM   1625 O  OD1  . ASP   A 1 229 ? 11.76846  5.90073   -45.41705 1.000 15.52376  ? 1281 ASP   B OD1  1 
ATOM   1626 O  OD2  . ASP   A 1 229 ? 10.18024  7.08561   -46.36585 1.000 23.89418  ? 1281 ASP   B OD2  1 
ATOM   1627 N  N    . LEU   A 1 230 ? 12.98378  5.36076   -42.77320 1.000 14.51699  ? 1282 LEU   B N    1 
ATOM   1628 C  CA   . LEU   A 1 230 ? 14.37978  5.69788   -42.48533 1.000 15.02154  ? 1282 LEU   B CA   1 
ATOM   1629 C  C    . LEU   A 1 230 ? 14.99958  6.63998   -43.50936 1.000 16.22354  ? 1282 LEU   B C    1 
ATOM   1630 O  O    . LEU   A 1 230 ? 16.09055  7.16808   -43.25445 1.000 14.72427  ? 1282 LEU   B O    1 
ATOM   1631 C  CB   . LEU   A 1 230 ? 15.23791  4.43696   -42.39646 1.000 11.32387  ? 1282 LEU   B CB   1 
ATOM   1632 C  CG   . LEU   A 1 230 ? 14.97012  3.49590   -41.23047 1.000 17.27643  ? 1282 LEU   B CG   1 
ATOM   1633 C  CD1  . LEU   A 1 230 ? 15.75923  2.19898   -41.41760 1.000 13.21390  ? 1282 LEU   B CD1  1 
ATOM   1634 C  CD2  . LEU   A 1 230 ? 15.33519  4.17288   -39.92348 1.000 12.15639  ? 1282 LEU   B CD2  1 
ATOM   1635 N  N    . ARG   A 1 231 ? 14.37144  6.82096   -44.67729 1.000 15.27328  ? 1283 ARG   B N    1 
ATOM   1636 C  CA   . ARG   A 1 231 ? 14.83325  7.83204   -45.62730 1.000 18.08217  ? 1283 ARG   B CA   1 
ATOM   1637 C  C    . ARG   A 1 231 ? 14.64516  9.23700   -45.07023 1.000 18.63991  ? 1283 ARG   B C    1 
ATOM   1638 O  O    . ARG   A 1 231 ? 15.49706  10.11209  -45.27428 1.000 20.23922  ? 1283 ARG   B O    1 
ATOM   1639 C  CB   . ARG   A 1 231 ? 14.08812  7.69402   -46.96323 1.000 13.07844  ? 1283 ARG   B CB   1 
ATOM   1640 C  CG   . ARG   A 1 231 ? 14.48316  6.47009   -47.79731 1.000 22.39381  ? 1283 ARG   B CG   1 
ATOM   1641 C  CD   . ARG   A 1 231 ? 13.40208  6.14002   -48.84721 1.000 21.68910  ? 1283 ARG   B CD   1 
ATOM   1642 N  NE   . ARG   A 1 231 ? 12.40123  5.28490   -48.23214 1.000 36.54194  ? 1283 ARG   B NE   1 
ATOM   1643 C  CZ   . ARG   A 1 231 ? 11.96229  4.13987   -48.73314 1.000 30.29079  ? 1283 ARG   B CZ   1 
ATOM   1644 N  NH1  . ARG   A 1 231 ? 12.27220  3.75695   -49.96518 1.000 23.57232  ? 1283 ARG   B NH1  1 
ATOM   1645 N  NH2  . ARG   A 1 231 ? 11.18044  3.36777   -47.98508 1.000 40.45775  ? 1283 ARG   B NH2  1 
ATOM   1646 N  N    . THR   A 1 232 ? 13.53522  9.46687   -44.36111 1.000 15.07899  ? 1284 THR   B N    1 
ATOM   1647 C  CA   . THR   A 1 232 ? 13.09613  10.80381  -43.95201 1.000 17.52587  ? 1284 THR   B CA   1 
ATOM   1648 C  C    . THR   A 1 232 ? 12.67526  10.91572  -42.49396 1.000 22.69401  ? 1284 THR   B C    1 
ATOM   1649 O  O    . THR   A 1 232 ? 12.51120  12.04468  -42.01091 1.000 19.35690  ? 1284 THR   B O    1 
ATOM   1650 C  CB   . THR   A 1 232 ? 11.88600  11.24972  -44.77887 1.000 17.27849  ? 1284 THR   B CB   1 
ATOM   1651 O  OG1  . THR   A 1 232 ? 10.81511  10.33461  -44.52180 1.000 17.95212  ? 1284 THR   B OG1  1 
ATOM   1652 C  CG2  . THR   A 1 232 ? 12.19584  11.28281  -46.27690 1.000 18.59436  ? 1284 THR   B CG2  1 
ATOM   1653 N  N    . PHE   A 1 233 ? 12.42144  9.80467   -41.80198 1.000 18.33069  ? 1285 PHE   B N    1 
ATOM   1654 C  CA   . PHE   A 1 233 ? 11.77458  9.81456   -40.49191 1.000 15.57843  ? 1285 PHE   B CA   1 
ATOM   1655 C  C    . PHE   A 1 233 ? 10.35152  10.35342  -40.54875 1.000 14.19376  ? 1285 PHE   B C    1 
ATOM   1656 O  O    . PHE   A 1 233 ? 9.79259   10.73733  -39.51668 1.000 18.29561  ? 1285 PHE   B O    1 
ATOM   1657 C  CB   . PHE   A 1 233 ? 12.59660  10.60760  -39.47797 1.000 14.61591  ? 1285 PHE   B CB   1 
ATOM   1658 C  CG   . PHE   A 1 233 ? 14.02166  10.16674  -39.40213 1.000 21.95125  ? 1285 PHE   B CG   1 
ATOM   1659 C  CD1  . PHE   A 1 233 ? 14.33081  8.83176   -39.18921 1.000 17.10321  ? 1285 PHE   B CD1  1 
ATOM   1660 C  CD2  . PHE   A 1 233 ? 15.05255  11.06885  -39.59520 1.000 22.01562  ? 1285 PHE   B CD2  1 
ATOM   1661 C  CE1  . PHE   A 1 233 ? 15.63586  8.40489   -39.13036 1.000 20.53353  ? 1285 PHE   B CE1  1 
ATOM   1662 C  CE2  . PHE   A 1 233 ? 16.37059  10.64497  -39.54535 1.000 31.11627  ? 1285 PHE   B CE2  1 
ATOM   1663 C  CZ   . PHE   A 1 233 ? 16.66375  9.31499   -39.30943 1.000 20.99618  ? 1285 PHE   B CZ   1 
ATOM   1664 N  N    . HIS   A 1 234 ? 9.74039   10.39640  -41.73268 1.000 16.16719  ? 1286 HIS   B N    1 
ATOM   1665 C  CA   . HIS   A 1 234 ? 8.30836   10.64526  -41.80353 1.000 16.33937  ? 1286 HIS   B CA   1 
ATOM   1666 C  C    . HIS   A 1 234 ? 7.53653   9.41417   -41.34549 1.000 19.14708  ? 1286 HIS   B C    1 
ATOM   1667 O  O    . HIS   A 1 234 ? 8.02364   8.27722   -41.40558 1.000 15.25757  ? 1286 HIS   B O    1 
ATOM   1668 C  CB   . HIS   A 1 234 ? 7.87418   11.02627  -43.22747 1.000 14.96007  ? 1286 HIS   B CB   1 
ATOM   1669 C  CG   . HIS   A 1 234 ? 8.38800   12.35634  -43.68347 1.000 22.71700  ? 1286 HIS   B CG   1 
ATOM   1670 N  ND1  . HIS   A 1 234 ? 7.95482   12.96934  -44.84041 1.000 18.62201  ? 1286 HIS   B ND1  1 
ATOM   1671 C  CD2  . HIS   A 1 234 ? 9.30098   13.19041  -43.13254 1.000 21.62676  ? 1286 HIS   B CD2  1 
ATOM   1672 C  CE1  . HIS   A 1 234 ? 8.58069   14.12341  -44.98343 1.000 20.89163  ? 1286 HIS   B CE1  1 
ATOM   1673 N  NE2  . HIS   A 1 234 ? 9.40178   14.28145  -43.95851 1.000 22.79519  ? 1286 HIS   B NE2  1 
ATOM   1674 N  N    . LEU   A 1 235 ? 6.31855   9.66103   -40.87236 1.000 16.30871  ? 1287 LEU   B N    1 
ATOM   1675 C  CA   . LEU   A 1 235 ? 5.39870   8.60093   -40.48530 1.000 15.10779  ? 1287 LEU   B CA   1 
ATOM   1676 C  C    . LEU   A 1 235 ? 4.73762   8.04491   -41.74025 1.000 18.39963  ? 1287 LEU   B C    1 
ATOM   1677 O  O    . LEU   A 1 235 ? 3.94849   8.73786   -42.39315 1.000 12.30568  ? 1287 LEU   B O    1 
ATOM   1678 C  CB   . LEU   A 1 235 ? 4.34174   9.13379   -39.52217 1.000 10.87759  ? 1287 LEU   B CB   1 
ATOM   1679 C  CG   . LEU   A 1 235 ? 3.34089   8.07068   -39.08211 1.000 15.74055  ? 1287 LEU   B CG   1 
ATOM   1680 C  CD1  . LEU   A 1 235 ? 4.05908   7.02572   -38.22722 1.000 14.05326  ? 1287 LEU   B CD1  1 
ATOM   1681 C  CD2  . LEU   A 1 235 ? 2.16391   8.70154   -38.33597 1.000 12.55179  ? 1287 LEU   B CD2  1 
ATOM   1682 N  N    . LEU   A 1 236 ? 5.02871   6.78895   -42.06433 1.000 16.62024  ? 1288 LEU   B N    1 
ATOM   1683 C  CA   . LEU   A 1 236 ? 4.44965   6.16894   -43.24929 1.000 21.39838  ? 1288 LEU   B CA   1 
ATOM   1684 C  C    . LEU   A 1 236 ? 3.06974   5.56779   -43.00217 1.000 18.26013  ? 1288 LEU   B C    1 
ATOM   1685 O  O    . LEU   A 1 236 ? 2.20864   5.64074   -43.88308 1.000 12.92393  ? 1288 LEU   B O    1 
ATOM   1686 C  CB   . LEU   A 1 236 ? 5.39270   5.07905   -43.79143 1.000 14.24069  ? 1288 LEU   B CB   1 
ATOM   1687 C  CG   . LEU   A 1 236 ? 6.69259   5.59620   -44.44054 1.000 21.81124  ? 1288 LEU   B CG   1 
ATOM   1688 C  CD1  . LEU   A 1 236 ? 7.52866   4.42730   -44.88867 1.000 21.14751  ? 1288 LEU   B CD1  1 
ATOM   1689 C  CD2  . LEU   A 1 236 ? 6.38837   6.53121   -45.61548 1.000 21.74100  ? 1288 LEU   B CD2  1 
ATOM   1690 N  N    . HIS   A 1 237 ? 2.84592   4.94973   -41.84117 1.000 13.23162  ? 1289 HIS   B N    1 
ATOM   1691 C  CA   . HIS   A 1 237 ? 1.57401   4.28760   -41.58007 1.000 13.62561  ? 1289 HIS   B CA   1 
ATOM   1692 C  C    . HIS   A 1 237 ? 1.26115   4.34951   -40.09603 1.000 16.53109  ? 1289 HIS   B C    1 
ATOM   1693 O  O    . HIS   A 1 237 ? 2.16524   4.34457   -39.25612 1.000 13.43352  ? 1289 HIS   B O    1 
ATOM   1694 C  CB   . HIS   A 1 237 ? 1.57511   2.81661   -42.01312 1.000 13.17601  ? 1289 HIS   B CB   1 
ATOM   1695 C  CG   . HIS   A 1 237 ? 1.66898   2.61967   -43.49214 1.000 14.95087  ? 1289 HIS   B CG   1 
ATOM   1696 N  ND1  . HIS   A 1 237 ? 2.86194   2.36581   -44.13227 1.000 20.80992  ? 1289 HIS   B ND1  1 
ATOM   1697 C  CD2  . HIS   A 1 237 ? 0.72287   2.64862   -44.45604 1.000 16.14676  ? 1289 HIS   B CD2  1 
ATOM   1698 C  CE1  . HIS   A 1 237 ? 2.64581   2.24084   -45.43025 1.000 17.00899  ? 1289 HIS   B CE1  1 
ATOM   1699 N  NE2  . HIS   A 1 237 ? 1.35577   2.40772   -45.65311 1.000 17.98086  ? 1289 HIS   B NE2  1 
ATOM   1700 N  N    . THR   A 1 238 ? -0.02782  4.42237   -39.78790 1.000 13.38168  ? 1290 THR   B N    1 
ATOM   1701 C  CA   . THR   A 1 238 ? -0.54165  4.12627   -38.45585 1.000 17.44154  ? 1290 THR   B CA   1 
ATOM   1702 C  C    . THR   A 1 238 ? -1.23053  2.77421   -38.55283 1.000 17.18337  ? 1290 THR   B C    1 
ATOM   1703 O  O    . THR   A 1 238 ? -2.14360  2.60315   -39.36374 1.000 13.49385  ? 1290 THR   B O    1 
ATOM   1704 C  CB   . THR   A 1 238 ? -1.51271  5.20516   -37.95871 1.000 16.68396  ? 1290 THR   B CB   1 
ATOM   1705 O  OG1  . THR   A 1 238 ? -0.91585  6.50522   -38.09673 1.000 18.41138  ? 1290 THR   B OG1  1 
ATOM   1706 C  CG2  . THR   A 1 238 ? -1.83354  4.98408   -36.48569 1.000 15.99352  ? 1290 THR   B CG2  1 
ATOM   1707 N  N    . VAL   A 1 239 ? -0.76436  1.80323   -37.77491 1.000 14.69272  ? 1291 VAL   B N    1 
ATOM   1708 C  CA   . VAL   A 1 239 ? -1.36623  0.47117   -37.83790 1.000 16.17810  ? 1291 VAL   B CA   1 
ATOM   1709 C  C    . VAL   A 1 239 ? -1.88306  0.11807   -36.44886 1.000 14.47557  ? 1291 VAL   B C    1 
ATOM   1710 O  O    . VAL   A 1 239 ? -1.14892  -0.47589  -35.64896 1.000 14.38554  ? 1291 VAL   B O    1 
ATOM   1711 C  CB   . VAL   A 1 239 ? -0.37118  -0.58371  -38.35004 1.000 16.87070  ? 1291 VAL   B CB   1 
ATOM   1712 C  CG1  . VAL   A 1 239 ? -1.10408  -1.89777  -38.63701 1.000 13.75210  ? 1291 VAL   B CG1  1 
ATOM   1713 C  CG2  . VAL   A 1 239 ? 0.35064   -0.08460  -39.59710 1.000 14.13847  ? 1291 VAL   B CG2  1 
ATOM   1714 N  N    . PRO   A 1 240 ? -3.12206  0.47994   -36.10972 1.000 17.20225  ? 1292 PRO   B N    1 
ATOM   1715 C  CA   . PRO   A 1 240 ? -3.57489  0.28384   -34.72268 1.000 16.97010  ? 1292 PRO   B CA   1 
ATOM   1716 C  C    . PRO   A 1 240 ? -3.50771  -1.16117  -34.27674 1.000 16.84975  ? 1292 PRO   B C    1 
ATOM   1717 O  O    . PRO   A 1 240 ? -3.27156  -1.42519  -33.08977 1.000 16.49185  ? 1292 PRO   B O    1 
ATOM   1718 C  CB   . PRO   A 1 240 ? -5.01595  0.81870   -34.74351 1.000 18.72119  ? 1292 PRO   B CB   1 
ATOM   1719 C  CG   . PRO   A 1 240 ? -5.02616  1.83674   -35.85948 1.000 14.29315  ? 1292 PRO   B CG   1 
ATOM   1720 C  CD   . PRO   A 1 240 ? -4.09421  1.24487   -36.91459 1.000 14.94195  ? 1292 PRO   B CD   1 
ATOM   1721 N  N    . ALA   A 1 241 ? -3.68071  -2.11115  -35.19476 1.000 12.78919  ? 1293 ALA   B N    1 
ATOM   1722 C  CA   . ALA   A 1 241 ? -3.68753  -3.52017  -34.82381 1.000 14.43550  ? 1293 ALA   B CA   1 
ATOM   1723 C  C    . ALA   A 1 241 ? -2.35643  -3.99406  -34.25196 1.000 19.55873  ? 1293 ALA   B C    1 
ATOM   1724 O  O    . ALA   A 1 241 ? -2.32326  -5.04208  -33.59800 1.000 17.71667  ? 1293 ALA   B O    1 
ATOM   1725 C  CB   . ALA   A 1 241 ? -4.05957  -4.37916  -36.03480 1.000 18.96149  ? 1293 ALA   B CB   1 
ATOM   1726 N  N    . LEU   A 1 242 ? -1.26152  -3.26094  -34.47205 1.000 12.69043  ? 1294 LEU   B N    1 
ATOM   1727 C  CA   . LEU   A 1 242 ? 0.04457   -3.70583  -34.00620 1.000 14.23990  ? 1294 LEU   B CA   1 
ATOM   1728 C  C    . LEU   A 1 242 ? 0.33967   -3.27285  -32.58221 1.000 16.11381  ? 1294 LEU   B C    1 
ATOM   1729 O  O    . LEU   A 1 242 ? 1.46374   -3.47576  -32.12033 1.000 14.48378  ? 1294 LEU   B O    1 
ATOM   1730 C  CB   . LEU   A 1 242 ? 1.15443   -3.19369  -34.92929 1.000 15.00762  ? 1294 LEU   B CB   1 
ATOM   1731 C  CG   . LEU   A 1 242 ? 1.12234   -3.77564  -36.34031 1.000 15.30176  ? 1294 LEU   B CG   1 
ATOM   1732 C  CD1  . LEU   A 1 242 ? 2.20519   -3.17650  -37.20940 1.000 16.10330  ? 1294 LEU   B CD1  1 
ATOM   1733 C  CD2  . LEU   A 1 242 ? 1.26849   -5.28263  -36.26338 1.000 20.33400  ? 1294 LEU   B CD2  1 
ATOM   1734 N  N    . ASP   A 1 243 ? -0.62631  -2.67197  -31.88109 1.000 10.74621  ? 1295 ASP   B N    1 
ATOM   1735 C  CA   . ASP   A 1 243 ? -0.35422  -2.20599  -30.52610 1.000 12.22315  ? 1295 ASP   B CA   1 
ATOM   1736 C  C    . ASP   A 1 243 ? 0.04899   -3.37999  -29.63619 1.000 12.45843  ? 1295 ASP   B C    1 
ATOM   1737 O  O    . ASP   A 1 243 ? -0.62691  -4.41605  -29.60315 1.000 12.17338  ? 1295 ASP   B O    1 
ATOM   1738 C  CB   . ASP   A 1 243 ? -1.57323  -1.47713  -29.95595 1.000 11.34802  ? 1295 ASP   B CB   1 
ATOM   1739 C  CG   . ASP   A 1 243 ? -1.31115  -0.88416  -28.57396 1.000 14.88830  ? 1295 ASP   B CG   1 
ATOM   1740 O  OD1  . ASP   A 1 243 ? -0.21418  -0.32706  -28.36005 1.000 12.33209  ? 1295 ASP   B OD1  1 
ATOM   1741 O  OD2  . ASP   A 1 243 ? -2.20805  -0.96928  -27.70087 1.000 22.04561  ? 1295 ASP   B OD2  1 
ATOM   1742 N  N    . GLN   A 1 244 ? 1.17004   -3.21890  -28.93330 1.000 11.76665  ? 1296 GLN   B N    1 
ATOM   1743 C  CA   . GLN   A 1 244 ? 1.69924   -4.21788  -27.99639 1.000 14.94948  ? 1296 GLN   B CA   1 
ATOM   1744 C  C    . GLN   A 1 244 ? 2.00130   -5.55783  -28.67447 1.000 18.07903  ? 1296 GLN   B C    1 
ATOM   1745 O  O    . GLN   A 1 244 ? 1.99847   -6.61485  -28.02750 1.000 13.97356  ? 1296 GLN   B O    1 
ATOM   1746 C  CB   . GLN   A 1 244 ? 0.74638   -4.41402  -26.80830 1.000 17.89131  ? 1296 GLN   B CB   1 
ATOM   1747 C  CG   . GLN   A 1 244 ? 0.41033   -3.12508  -26.06721 1.000 18.09780  ? 1296 GLN   B CG   1 
ATOM   1748 C  CD   . GLN   A 1 244 ? 1.64430   -2.36198  -25.60131 1.000 22.47133  ? 1296 GLN   B CD   1 
ATOM   1749 O  OE1  . GLN   A 1 244 ? 2.48543   -2.89292  -24.87142 1.000 15.67177  ? 1296 GLN   B OE1  1 
ATOM   1750 N  NE2  . GLN   A 1 244 ? 1.76113   -1.10695  -26.03528 1.000 16.36781  ? 1296 GLN   B NE2  1 
ATOM   1751 N  N    . CYS   A 1 245 ? 2.26216   -5.53476  -29.98049 1.000 12.97179  ? 1297 CYS   B N    1 
ATOM   1752 C  CA   . CYS   A 1 245 ? 2.53121   -6.75770  -30.71756 1.000 12.33934  ? 1297 CYS   B CA   1 
ATOM   1753 C  C    . CYS   A 1 245 ? 4.02121   -7.00555  -30.88173 1.000 12.42352  ? 1297 CYS   B C    1 
ATOM   1754 O  O    . CYS   A 1 245 ? 4.82211   -6.07647  -31.00677 1.000 14.50376  ? 1297 CYS   B O    1 
ATOM   1755 C  CB   . CYS   A 1 245 ? 1.89006   -6.72772  -32.10250 1.000 12.81088  ? 1297 CYS   B CB   1 
ATOM   1756 S  SG   . CYS   A 1 245 ? 0.13909   -6.96189  -32.08832 1.000 16.40378  ? 1297 CYS   B SG   1 
ATOM   1757 N  N    . ARG   A 1 246 ? 4.37834   -8.27952  -30.86581 1.000 13.28548  ? 1298 ARG   B N    1 
ATOM   1758 C  CA   . ARG   A 1 246 ? 5.61433   -8.75938  -31.45095 1.000 11.16721  ? 1298 ARG   B CA   1 
ATOM   1759 C  C    . ARG   A 1 246 ? 5.29523   -9.23236  -32.86094 1.000 11.19545  ? 1298 ARG   B C    1 
ATOM   1760 O  O    . ARG   A 1 246 ? 4.15623   -9.59546  -33.16483 1.000 11.32851  ? 1298 ARG   B O    1 
ATOM   1761 C  CB   . ARG   A 1 246 ? 6.21453   -9.88235  -30.60205 1.000 12.03362  ? 1298 ARG   B CB   1 
ATOM   1762 C  CG   . ARG   A 1 246 ? 6.64262   -9.40236  -29.20508 1.000 11.45221  ? 1298 ARG   B CG   1 
ATOM   1763 C  CD   . ARG   A 1 246 ? 8.06056   -8.83722  -29.23121 1.000 16.33098  ? 1298 ARG   B CD   1 
ATOM   1764 N  NE   . ARG   A 1 246 ? 8.99963   -9.89711  -29.57834 1.000 14.24354  ? 1298 ARG   B NE   1 
ATOM   1765 C  CZ   . ARG   A 1 246 ? 10.28759  -9.72998  -29.84647 1.000 17.03173  ? 1298 ARG   B CZ   1 
ATOM   1766 N  NH1  . ARG   A 1 246 ? 10.86448  -8.53892  -29.77248 1.000 16.83274  ? 1298 ARG   B NH1  1 
ATOM   1767 N  NH2  . ARG   A 1 246 ? 11.01565  -10.78889 -30.20758 1.000 10.84782  ? 1298 ARG   B NH2  1 
ATOM   1768 N  N    . VAL   A 1 247 ? 6.29114   -9.18723  -33.73704 1.000 13.94066  ? 1299 VAL   B N    1 
ATOM   1769 C  CA   . VAL   A 1 247 ? 6.06302   -9.52520  -35.13503 1.000 17.71653  ? 1299 VAL   B CA   1 
ATOM   1770 C  C    . VAL   A 1 247 ? 7.18706   -10.40907 -35.64717 1.000 12.70409  ? 1299 VAL   B C    1 
ATOM   1771 O  O    . VAL   A 1 247 ? 8.32210   -10.35598 -35.16129 1.000 13.76817  ? 1299 VAL   B O    1 
ATOM   1772 C  CB   . VAL   A 1 247 ? 5.93881   -8.26318  -36.01697 1.000 14.60830  ? 1299 VAL   B CB   1 
ATOM   1773 C  CG1  . VAL   A 1 247 ? 4.70577   -7.43031  -35.59981 1.000 10.51512  ? 1299 VAL   B CG1  1 
ATOM   1774 C  CG2  . VAL   A 1 247 ? 7.21274   -7.44106  -35.94707 1.000 7.66254   ? 1299 VAL   B CG2  1 
ATOM   1775 N  N    . VAL   A 1 248 ? 6.85804   -11.22607 -36.64417 1.000 13.22145  ? 1300 VAL   B N    1 
ATOM   1776 C  CA   . VAL   A 1 248 ? 7.84303   -11.99194 -37.39530 1.000 14.20632  ? 1300 VAL   B CA   1 
ATOM   1777 C  C    . VAL   A 1 248 ? 7.40389   -12.04793 -38.85425 1.000 17.04263  ? 1300 VAL   B C    1 
ATOM   1778 O  O    . VAL   A 1 248 ? 6.21086   -12.02104 -39.16713 1.000 17.87218  ? 1300 VAL   B O    1 
ATOM   1779 C  CB   . VAL   A 1 248 ? 8.02723   -13.40994 -36.81337 1.000 14.97593  ? 1300 VAL   B CB   1 
ATOM   1780 C  CG1  . VAL   A 1 248 ? 6.74130   -14.20607 -36.95227 1.000 20.25307  ? 1300 VAL   B CG1  1 
ATOM   1781 C  CG2  . VAL   A 1 248 ? 9.18323   -14.11081 -37.50751 1.000 23.59616  ? 1300 VAL   B CG2  1 
ATOM   1782 N  N    . PHE   A 1 249 ? 8.38181   -12.12480 -39.74836 1.000 16.81588  ? 1301 PHE   B N    1 
ATOM   1783 C  CA   . PHE   A 1 249 ? 8.15866   -12.10277 -41.18833 1.000 23.34159  ? 1301 PHE   B CA   1 
ATOM   1784 C  C    . PHE   A 1 249 ? 8.39973   -13.47773 -41.79941 1.000 20.45476  ? 1301 PHE   B C    1 
ATOM   1785 O  O    . PHE   A 1 249 ? 9.26285   -14.22866 -41.34152 1.000 21.30571  ? 1301 PHE   B O    1 
ATOM   1786 C  CB   . PHE   A 1 249 ? 9.08549   -11.07866 -41.86239 1.000 16.71627  ? 1301 PHE   B CB   1 
ATOM   1787 C  CG   . PHE   A 1 249 ? 8.75838   -9.65870  -41.51531 1.000 17.13679  ? 1301 PHE   B CG   1 
ATOM   1788 C  CD1  . PHE   A 1 249 ? 9.22445   -9.09470  -40.34134 1.000 18.60101  ? 1301 PHE   B CD1  1 
ATOM   1789 C  CD2  . PHE   A 1 249 ? 7.96722   -8.88975  -42.35820 1.000 17.64406  ? 1301 PHE   B CD2  1 
ATOM   1790 C  CE1  . PHE   A 1 249 ? 8.91635   -7.78774  -40.02426 1.000 13.24125  ? 1301 PHE   B CE1  1 
ATOM   1791 C  CE2  . PHE   A 1 249 ? 7.65712   -7.58479  -42.05012 1.000 14.18549  ? 1301 PHE   B CE2  1 
ATOM   1792 C  CZ   . PHE   A 1 249 ? 8.13219   -7.03279  -40.88115 1.000 14.78230  ? 1301 PHE   B CZ   1 
ATOM   1793 N  N    . ASN   A 1 250 ? 7.63065   -13.80577 -42.83834 1.000 23.99857  ? 1302 ASN   B N    1 
ATOM   1794 C  CA   . ASN   A 1 250 ? 8.00368   -14.94770 -43.65442 1.000 17.47546  ? 1302 ASN   B CA   1 
ATOM   1795 C  C    . ASN   A 1 250 ? 9.32258   -14.63854 -44.35555 1.000 23.03975  ? 1302 ASN   B C    1 
ATOM   1796 O  O    . ASN   A 1 250 ? 9.75946   -13.48450 -44.44255 1.000 22.97013  ? 1302 ASN   B O    1 
ATOM   1797 C  CB   . ASN   A 1 250 ? 6.90661   -15.30577 -44.66732 1.000 18.96038  ? 1302 ASN   B CB   1 
ATOM   1798 C  CG   . ASN   A 1 250 ? 6.68040   -14.21575 -45.71226 1.000 25.06116  ? 1302 ASN   B CG   1 
ATOM   1799 O  OD1  . ASN   A 1 250 ? 7.33130   -13.17269 -45.69529 1.000 25.57099  ? 1302 ASN   B OD1  1 
ATOM   1800 N  ND2  . ASN   A 1 250 ? 5.75533   -14.46281 -46.63517 1.000 27.72513  ? 1302 ASN   B ND2  1 
ATOM   1801 N  N    . HIS   A 1 251 ? 9.96563   -15.69146 -44.85665 1.000 24.49042  ? 1303 HIS   B N    1 
ATOM   1802 C  CA   . HIS   A 1 251 ? 11.34757  -15.54531 -45.29579 1.000 26.74363  ? 1303 HIS   B CA   1 
ATOM   1803 C  C    . HIS   A 1 251 ? 11.47236  -14.76525 -46.59977 1.000 25.46345  ? 1303 HIS   B C    1 
ATOM   1804 O  O    . HIS   A 1 251 ? 12.55128  -14.25214 -46.89286 1.000 23.47534  ? 1303 HIS   B O    1 
ATOM   1805 C  CB   . HIS   A 1 251 ? 12.00070  -16.92824 -45.38990 1.000 24.11189  ? 1303 HIS   B CB   1 
ATOM   1806 C  CG   . HIS   A 1 251 ? 12.19690  -17.57627 -44.04995 1.000 31.41767  ? 1303 HIS   B CG   1 
ATOM   1807 N  ND1  . HIS   A 1 251 ? 11.16503  -18.16440 -43.34786 1.000 32.43355  ? 1303 HIS   B ND1  1 
ATOM   1808 C  CD2  . HIS   A 1 251 ? 13.29699  -17.69019 -43.26606 1.000 32.25202  ? 1303 HIS   B CD2  1 
ATOM   1809 C  CE1  . HIS   A 1 251 ? 11.62519  -18.63140 -42.19693 1.000 32.46380  ? 1303 HIS   B CE1  1 
ATOM   1810 N  NE2  . HIS   A 1 251 ? 12.91617  -18.35327 -42.12305 1.000 35.15935  ? 1303 HIS   B NE2  1 
ATOM   1811 N  N    . THR   A 1 252 ? 10.39827  -14.62533 -47.36766 1.000 23.34878  ? 1304 THR   B N    1 
ATOM   1812 C  CA   . THR   A 1 252 ? 10.45106  -13.72328 -48.51263 1.000 31.24661  ? 1304 THR   B CA   1 
ATOM   1813 C  C    . THR   A 1 252 ? 10.27296  -12.25931 -48.12356 1.000 32.46031  ? 1304 THR   B C    1 
ATOM   1814 O  O    . THR   A 1 252 ? 10.49079  -11.38026 -48.96555 1.000 31.01079  ? 1304 THR   B O    1 
ATOM   1815 C  CB   . THR   A 1 252 ? 9.38299   -14.10235 -49.54553 1.000 32.19408  ? 1304 THR   B CB   1 
ATOM   1816 O  OG1  . THR   A 1 252 ? 8.09005   -14.06550 -48.93140 1.000 27.98251  ? 1304 THR   B OG1  1 
ATOM   1817 C  CG2  . THR   A 1 252 ? 9.63707   -15.50031 -50.10861 1.000 26.82466  ? 1304 THR   B CG2  1 
ATOM   1818 N  N    . GLY   A 1 253 ? 9.87306   -11.97440 -46.88551 1.000 27.86801  ? 1305 GLY   B N    1 
ATOM   1819 C  CA   . GLY   A 1 253 ? 9.58797   -10.61144 -46.48043 1.000 20.84893  ? 1305 GLY   B CA   1 
ATOM   1820 C  C    . GLY   A 1 253 ? 8.30685   -10.03155 -47.04227 1.000 26.65615  ? 1305 GLY   B C    1 
ATOM   1821 O  O    . GLY   A 1 253 ? 8.19472   -8.80655  -47.16622 1.000 24.07835  ? 1305 GLY   B O    1 
ATOM   1822 N  N    . THR   A 1 254 ? 7.32890   -10.87863 -47.38321 1.000 29.09511  ? 1306 THR   B N    1 
ATOM   1823 C  CA   . THR   A 1 254 ? 6.06780   -10.43173 -47.97006 1.000 26.21167  ? 1306 THR   B CA   1 
ATOM   1824 C  C    . THR   A 1 254 ? 4.87390   -10.51388 -47.02994 1.000 26.50425  ? 1306 THR   B C    1 
ATOM   1825 O  O    . THR   A 1 254 ? 3.79782   -10.02198 -47.37981 1.000 19.66234  ? 1306 THR   B O    1 
ATOM   1826 C  CB   . THR   A 1 254 ? 5.72775   -11.25972 -49.21205 1.000 32.14067  ? 1306 THR   B CB   1 
ATOM   1827 O  OG1  . THR   A 1 254 ? 5.72992   -12.65073 -48.85610 1.000 29.01362  ? 1306 THR   B OG1  1 
ATOM   1828 C  CG2  . THR   A 1 254 ? 6.71461   -10.97858 -50.34015 1.000 23.24911  ? 1306 THR   B CG2  1 
ATOM   1829 N  N    . VAL   A 1 255 ? 5.01208   -11.16091 -45.88298 1.000 20.98820  ? 1307 VAL   B N    1 
ATOM   1830 C  CA   . VAL   A 1 255 ? 3.91519   -11.30105 -44.94287 1.000 18.18150  ? 1307 VAL   B CA   1 
ATOM   1831 C  C    . VAL   A 1 255 ? 4.47032   -11.11505 -43.54392 1.000 15.71333  ? 1307 VAL   B C    1 
ATOM   1832 O  O    . VAL   A 1 255 ? 5.57939   -11.55995 -43.23705 1.000 18.13084  ? 1307 VAL   B O    1 
ATOM   1833 C  CB   . VAL   A 1 255 ? 3.21131   -12.66012 -45.08285 1.000 26.12143  ? 1307 VAL   B CB   1 
ATOM   1834 C  CG1  . VAL   A 1 255 ? 2.17944   -12.82826 -43.97875 1.000 20.61940  ? 1307 VAL   B CG1  1 
ATOM   1835 C  CG2  . VAL   A 1 255 ? 2.56218   -12.75613 -46.44978 1.000 24.21824  ? 1307 VAL   B CG2  1 
ATOM   1836 N  N    . MET   A 1 256 ? 3.71034   -10.43115 -42.70482 1.000 20.32939  ? 1308 MET   B N    1 
ATOM   1837 C  CA   . MET   A 1 256 ? 4.09146   -10.20417 -41.32385 1.000 22.71392  ? 1308 MET   B CA   1 
ATOM   1838 C  C    . MET   A 1 256 ? 3.05661   -10.85430 -40.42077 1.000 17.97881  ? 1308 MET   B C    1 
ATOM   1839 O  O    . MET   A 1 256 ? 1.85257   -10.68441 -40.63764 1.000 18.47131  ? 1308 MET   B O    1 
ATOM   1840 C  CB   . MET   A 1 256 ? 4.20034   -8.70817  -41.03181 1.000 17.71004  ? 1308 MET   B CB   1 
ATOM   1841 C  CG   . MET   A 1 256 ? 4.90744   -8.39514  -39.73287 1.000 17.30157  ? 1308 MET   B CG   1 
ATOM   1842 S  SD   . MET   A 1 256 ? 5.00130   -6.62215  -39.38881 1.000 24.55600  ? 1308 MET   B SD   1 
ATOM   1843 C  CE   . MET   A 1 256 ? 3.27424   -6.14631  -39.52762 1.000 14.07994  ? 1308 MET   B CE   1 
ATOM   1844 N  N    . TYR   A 1 257 ? 3.53279   -11.61029 -39.43184 1.000 14.10009  ? 1309 TYR   B N    1 
ATOM   1845 C  CA   . TYR   A 1 257 ? 2.71295   -12.14441 -38.35478 1.000 15.12405  ? 1309 TYR   B CA   1 
ATOM   1846 C  C    . TYR   A 1 257 ? 2.83699   -11.25144 -37.12776 1.000 19.17827  ? 1309 TYR   B C    1 
ATOM   1847 O  O    . TYR   A 1 257 ? 3.92998   -10.78935 -36.79285 1.000 16.09559  ? 1309 TYR   B O    1 
ATOM   1848 C  CB   . TYR   A 1 257 ? 3.14413   -13.56238 -37.97287 1.000 20.19735  ? 1309 TYR   B CB   1 
ATOM   1849 C  CG   . TYR   A 1 257 ? 3.00712   -14.58336 -39.07290 1.000 21.89342  ? 1309 TYR   B CG   1 
ATOM   1850 C  CD1  . TYR   A 1 257 ? 3.92502   -14.64423 -40.11599 1.000 18.64363  ? 1309 TYR   B CD1  1 
ATOM   1851 C  CD2  . TYR   A 1 257 ? 1.97321   -15.50546 -39.05582 1.000 22.62745  ? 1309 TYR   B CD2  1 
ATOM   1852 C  CE1  . TYR   A 1 257 ? 3.80501   -15.59720 -41.11401 1.000 18.51763  ? 1309 TYR   B CE1  1 
ATOM   1853 C  CE2  . TYR   A 1 257 ? 1.83620   -16.44943 -40.05384 1.000 23.87712  ? 1309 TYR   B CE2  1 
ATOM   1854 C  CZ   . TYR   A 1 257 ? 2.74710   -16.48831 -41.07894 1.000 23.33757  ? 1309 TYR   B CZ   1 
ATOM   1855 O  OH   . TYR   A 1 257 ? 2.60409   -17.43729 -42.05996 1.000 26.23152  ? 1309 TYR   B OH   1 
ATOM   1856 N  N    . GLY   A 1 258 ? 1.72204   -11.02358 -36.45063 1.000 14.21587  ? 1310 GLY   B N    1 
ATOM   1857 C  CA   . GLY   A 1 258 ? 1.77109   -10.25662 -35.22561 1.000 14.38481  ? 1310 GLY   B CA   1 
ATOM   1858 C  C    . GLY   A 1 258 ? 0.83925   -10.81975 -34.17354 1.000 17.75998  ? 1310 GLY   B C    1 
ATOM   1859 O  O    . GLY   A 1 258 ? -0.26974  -11.24784 -34.50144 1.000 22.21636  ? 1310 GLY   B O    1 
ATOM   1860 N  N    . ALA   A 1 259 ? 1.28038   -10.84975 -32.91458 1.000 18.30593  ? 1311 ALA   B N    1 
ATOM   1861 C  CA   . ALA   A 1 259 ? 0.44354   -11.26387 -31.79751 1.000 18.43812  ? 1311 ALA   B CA   1 
ATOM   1862 C  C    . ALA   A 1 259 ? 0.62556   -10.27689 -30.65249 1.000 16.07815  ? 1311 ALA   B C    1 
ATOM   1863 O  O    . ALA   A 1 259 ? 1.73954   -9.80179  -30.39859 1.000 15.96086  ? 1311 ALA   B O    1 
ATOM   1864 C  CB   . ALA   A 1 259 ? 0.77773   -12.69285 -31.33460 1.000 17.00193  ? 1311 ALA   B CB   1 
ATOM   1865 N  N    . MET   A 1 260 ? -0.47840  -9.96403  -29.97337 1.000 11.74683  ? 1312 MET   B N    1 
ATOM   1866 C  CA   . MET   A 1 260 ? -0.51240  -8.91807  -28.96133 1.000 14.64990  ? 1312 MET   B CA   1 
ATOM   1867 C  C    . MET   A 1 260 ? -0.13121  -9.48108  -27.60039 1.000 16.62616  ? 1312 MET   B C    1 
ATOM   1868 O  O    . MET   A 1 260 ? -0.70006  -10.48015 -27.15137 1.000 15.22951  ? 1312 MET   B O    1 
ATOM   1869 C  CB   . MET   A 1 260 ? -1.90246  -8.27921  -28.89316 1.000 15.84455  ? 1312 MET   B CB   1 
ATOM   1870 C  CG   . MET   A 1 260 ? -2.05743  -7.32526  -27.71311 1.000 20.41735  ? 1312 MET   B CG   1 
ATOM   1871 S  SD   . MET   A 1 260 ? -3.63352  -6.42342  -27.70792 1.000 21.13735  ? 1312 MET   B SD   1 
ATOM   1872 C  CE   . MET   A 1 260 ? -3.03862  -4.80438  -27.18292 1.000 24.29215  ? 1312 MET   B CE   1 
ATOM   1873 N  N    . LEU   A 1 261 ? 0.84080   -8.84501  -26.95147 1.000 12.57028  ? 1313 LEU   B N    1 
ATOM   1874 C  CA   . LEU   A 1 261 ? 1.18598   -9.23702  -25.59451 1.000 16.79530  ? 1313 LEU   B CA   1 
ATOM   1875 C  C    . LEU   A 1 261 ? -0.03094  -9.12017  -24.67639 1.000 22.28567  ? 1313 LEU   B C    1 
ATOM   1876 O  O    . LEU   A 1 261 ? -0.87704  -8.23825  -24.84127 1.000 28.37845  ? 1313 LEU   B O    1 
ATOM   1877 C  CB   . LEU   A 1 261 ? 2.31195   -8.35993  -25.06060 1.000 14.74694  ? 1313 LEU   B CB   1 
ATOM   1878 C  CG   . LEU   A 1 261 ? 3.62788   -8.44677  -25.82274 1.000 13.09043  ? 1313 LEU   B CG   1 
ATOM   1879 C  CD1  . LEU   A 1 261 ? 4.50280   -7.27270  -25.44178 1.000 11.99976  ? 1313 LEU   B CD1  1 
ATOM   1880 C  CD2  . LEU   A 1 261 ? 4.33104   -9.78772  -25.52386 1.000 10.15491  ? 1313 LEU   B CD2  1 
ATOM   1881 N  N    . GLN   A 1 262 ? -0.12075  -10.02522 -23.70341 1.000 17.79344  ? 1314 GLN   B N    1 
ATOM   1882 C  CA   . GLN   A 1 262 ? -1.02766  -9.83935  -22.57831 1.000 30.53469  ? 1314 GLN   B CA   1 
ATOM   1883 C  C    . GLN   A 1 262 ? -0.33863  -8.99732  -21.50935 1.000 35.57150  ? 1314 GLN   B C    1 
ATOM   1884 O  O    . GLN   A 1 262 ? 0.83443   -9.21222  -21.18748 1.000 47.16340  ? 1314 GLN   B O    1 
ATOM   1885 C  CB   . GLN   A 1 262 ? -1.46146  -11.18641 -22.01031 1.000 36.69250  ? 1314 GLN   B CB   1 
ATOM   1886 C  CG   . GLN   A 1 262 ? -2.08249  -12.07543 -23.07228 1.000 33.02637  ? 1314 GLN   B CG   1 
ATOM   1887 C  CD   . GLN   A 1 262 ? -3.34837  -12.76657 -22.59918 1.000 45.31543  ? 1314 GLN   B CD   1 
ATOM   1888 O  OE1  . GLN   A 1 262 ? -3.30119  -13.65160 -21.73821 1.000 43.11874  ? 1314 GLN   B OE1  1 
ATOM   1889 N  NE2  . GLN   A 1 262 ? -4.48747  -12.36367 -23.15705 1.000 43.38594  ? 1314 GLN   B NE2  1 
ATOM   1890 N  N    . ALA   A 1 263 ? -1.07467  -8.03341  -20.95924 1.000 50.34586  ? 1315 ALA   B N    1 
ATOM   1891 C  CA   . ALA   A 1 263 ? -0.41671  -6.89537  -20.32427 1.000 51.75527  ? 1315 ALA   B CA   1 
ATOM   1892 C  C    . ALA   A 1 263 ? -0.77558  -6.66846  -18.86422 1.000 51.97464  ? 1315 ALA   B C    1 
ATOM   1893 O  O    . ALA   A 1 263 ? -0.14744  -7.23343  -17.96431 1.000 62.69392  ? 1315 ALA   B O    1 
ATOM   1894 C  CB   . ALA   A 1 263 ? -0.74092  -5.61637  -21.09919 1.000 54.06118  ? 1315 ALA   B CB   1 
ATOM   1895 N  N    . ASP   A 1 264 ? -1.77765  -5.81556  -18.63709 1.000 67.79888  ? 1316 ASP   B N    1 
ATOM   1896 C  CA   . ASP   A 1 264 ? -2.02357  -5.19064  -17.34304 1.000 69.25505  ? 1316 ASP   B CA   1 
ATOM   1897 C  C    . ASP   A 1 264 ? -0.70554  -4.82453  -16.67516 1.000 69.97414  ? 1316 ASP   B C    1 
ATOM   1898 O  O    . ASP   A 1 264 ? -0.14738  -5.61650  -15.90925 1.000 65.24201  ? 1316 ASP   B O    1 
ATOM   1899 C  CB   . ASP   A 1 264 ? -2.85639  -6.09575  -16.43399 1.000 67.89725  ? 1316 ASP   B CB   1 
ATOM   1900 C  CG   . ASP   A 1 264 ? -4.34743  -5.88189  -16.60883 1.000 76.52671  ? 1316 ASP   B CG   1 
ATOM   1901 O  OD1  . ASP   A 1 264 ? -4.93347  -6.48091  -17.53679 1.000 80.15805  ? 1316 ASP   B OD1  1 
ATOM   1902 O  OD2  . ASP   A 1 264 ? -4.93342  -5.11198  -15.81574 1.000 80.87201  ? 1316 ASP   B OD2  1 
ATOM   1903 N  N    . ASP   A 1 265 ? -0.18869  -3.63347  -16.98017 1.000 66.61946  ? 1317 ASP   B N    1 
ATOM   1904 C  CA   . ASP   A 1 265 ? 0.99534   -3.14838  -16.28027 1.000 73.92985  ? 1317 ASP   B CA   1 
ATOM   1905 C  C    . ASP   A 1 265 ? 0.75448   -3.09146  -14.77625 1.000 73.41521  ? 1317 ASP   B C    1 
ATOM   1906 O  O    . ASP   A 1 265 ? 1.68459   -3.30839  -13.98435 1.000 70.05528  ? 1317 ASP   B O    1 
ATOM   1907 C  CB   . ASP   A 1 265 ? 1.39215   -1.77332  -16.82127 1.000 68.59920  ? 1317 ASP   B CB   1 
ATOM   1908 C  CG   . ASP   A 1 265 ? 2.89411   -1.62517  -16.99441 1.000 68.78648  ? 1317 ASP   B CG   1 
ATOM   1909 O  OD1  . ASP   A 1 265 ? 3.63924   -1.98013  -16.05750 1.000 63.76945  ? 1317 ASP   B OD1  1 
ATOM   1910 O  OD2  . ASP   A 1 265 ? 3.32496   -1.15408  -18.07344 1.000 60.75339  ? 1317 ASP   B OD2  1 
ATOM   1911 N  N    . GLU   A 1 266 ? -0.49050  -2.81759  -14.36411 1.000 77.40320  ? 1318 GLU   B N    1 
ATOM   1912 C  CA   . GLU   A 1 266 ? -0.88036  -2.82468  -12.95807 1.000 81.47538  ? 1318 GLU   B CA   1 
ATOM   1913 C  C    . GLU   A 1 266 ? -0.86716  -4.21670  -12.34612 1.000 74.62224  ? 1318 GLU   B C    1 
ATOM   1914 O  O    . GLU   A 1 266 ? -1.23502  -4.36378  -11.17509 1.000 68.25331  ? 1318 GLU   B O    1 
ATOM   1915 C  CB   . GLU   A 1 266 ? -2.26540  -2.19082  -12.80391 1.000 81.38995  ? 1318 GLU   B CB   1 
ATOM   1916 C  CG   . GLU   A 1 266 ? -2.31258  -0.70582  -13.11885 1.000 77.63300  ? 1318 GLU   B CG   1 
ATOM   1917 C  CD   . GLU   A 1 266 ? -3.49671  -0.33490  -13.99571 1.000 96.50678  ? 1318 GLU   B CD   1 
ATOM   1918 O  OE1  . GLU   A 1 266 ? -4.05169  -1.23793  -14.66169 1.000 90.11525  ? 1318 GLU   B OE1  1 
ATOM   1919 O  OE2  . GLU   A 1 266 ? -3.86983  0.85906   -14.01663 1.000 101.94554 ? 1318 GLU   B OE2  1 
ATOM   1920 N  N    . ASP   A 1 267 ? -0.48014  -5.22764  -13.11720 1.000 76.29342  ? 1319 ASP   B N    1 
ATOM   1921 C  CA   . ASP   A 1 267 ? -0.23195  -6.54763  -12.56027 1.000 72.18984  ? 1319 ASP   B CA   1 
ATOM   1922 C  C    . ASP   A 1 267 ? 1.02714   -6.52854  -11.70740 1.000 73.00996  ? 1319 ASP   B C    1 
ATOM   1923 O  O    . ASP   A 1 267 ? 2.03304   -5.90843  -12.06648 1.000 73.54115  ? 1319 ASP   B O    1 
ATOM   1924 C  CB   . ASP   A 1 267 ? -0.07596  -7.58258  -13.67333 1.000 68.48566  ? 1319 ASP   B CB   1 
ATOM   1925 C  CG   . ASP   A 1 267 ? -1.39798  -8.01269  -14.26521 1.000 67.58349  ? 1319 ASP   B CG   1 
ATOM   1926 O  OD1  . ASP   A 1 267 ? -2.43501  -7.39780  -13.93108 1.000 73.80546  ? 1319 ASP   B OD1  1 
ATOM   1927 O  OD2  . ASP   A 1 267 ? -1.39697  -8.97166  -15.06424 1.000 59.65848  ? 1319 ASP   B OD2  1 
ATOM   1928 N  N    . ASP   A 1 268 ? 0.97532   -7.22159  -10.57742 1.000 69.26296  ? 1320 ASP   B N    1 
ATOM   1929 C  CA   . ASP   A 1 268 ? 2.15842   -7.41550  -9.75755  1.000 65.66441  ? 1320 ASP   B CA   1 
ATOM   1930 C  C    . ASP   A 1 268 ? 2.93149   -8.62740  -10.28467 1.000 63.09176  ? 1320 ASP   B C    1 
ATOM   1931 O  O    . ASP   A 1 268 ? 2.58044   -9.22240  -11.30866 1.000 62.50143  ? 1320 ASP   B O    1 
ATOM   1932 C  CB   . ASP   A 1 268 ? 1.77959   -7.55959  -8.28551  1.000 61.81869  ? 1320 ASP   B CB   1 
ATOM   1933 C  CG   . ASP   A 1 268 ? 1.18776   -8.92266  -7.95950  1.000 65.79659  ? 1320 ASP   B CG   1 
ATOM   1934 O  OD1  . ASP   A 1 268 ? 0.40872   -9.45071  -8.78144  1.000 63.15390  ? 1320 ASP   B OD1  1 
ATOM   1935 O  OD2  . ASP   A 1 268 ? 1.50592   -9.46567  -6.87656  1.000 65.44422  ? 1320 ASP   B OD2  1 
ATOM   1936 N  N    . LEU   A 1 269 ? 3.99460   -9.00733  -9.57679  1.000 66.05880  ? 1321 LEU   B N    1 
ATOM   1937 C  CA   . LEU   A 1 269 ? 4.83366   -10.11823 -10.01392 1.000 62.88734  ? 1321 LEU   B CA   1 
ATOM   1938 C  C    . LEU   A 1 269 ? 4.02678   -11.40430 -10.13388 1.000 58.95555  ? 1321 LEU   B C    1 
ATOM   1939 O  O    . LEU   A 1 269 ? 4.11674   -12.11426 -11.14092 1.000 62.10688  ? 1321 LEU   B O    1 
ATOM   1940 C  CB   . LEU   A 1 269 ? 6.00278   -10.31915 -9.04705  1.000 62.35394  ? 1321 LEU   B CB   1 
ATOM   1941 C  CG   . LEU   A 1 269 ? 7.02168   -9.17905  -8.96911  1.000 70.76898  ? 1321 LEU   B CG   1 
ATOM   1942 C  CD1  . LEU   A 1 269 ? 8.03157   -9.28391  -10.10122 1.000 57.93681  ? 1321 LEU   B CD1  1 
ATOM   1943 C  CD2  . LEU   A 1 269 ? 6.32054   -7.82912  -8.99299  1.000 71.24439  ? 1321 LEU   B CD2  1 
ATOM   1944 N  N    . MET   A 1 270 ? 3.23291   -11.72442 -9.10981  1.000 60.59884  ? 1322 MET   B N    1 
ATOM   1945 C  CA   . MET   A 1 270 ? 2.42903   -12.94250 -9.14078  1.000 60.76960  ? 1322 MET   B CA   1 
ATOM   1946 C  C    . MET   A 1 270 ? 1.45291   -12.92855 -10.31168 1.000 60.75359  ? 1322 MET   B C    1 
ATOM   1947 O  O    . MET   A 1 270 ? 1.30193   -13.92654 -11.02670 1.000 55.62438  ? 1322 MET   B O    1 
ATOM   1948 C  CB   . MET   A 1 270 ? 1.67218   -13.10062 -7.82170  1.000 56.24083  ? 1322 MET   B CB   1 
ATOM   1949 C  CG   . MET   A 1 270 ? 2.56730   -13.06757 -6.59980  1.000 63.43966  ? 1322 MET   B CG   1 
ATOM   1950 S  SD   . MET   A 1 270 ? 2.16855   -14.37466 -5.41480  1.000 61.37999  ? 1322 MET   B SD   1 
ATOM   1951 C  CE   . MET   A 1 270 ? 3.69865   -14.46154 -4.52196  1.000 37.71301  ? 1322 MET   B CE   1 
ATOM   1952 N  N    . GLU   A 1 271 ? 0.76678   -11.80061 -10.51456 1.000 61.00792  ? 1323 GLU   B N    1 
ATOM   1953 C  CA   . GLU   A 1 271 ? -0.21334  -11.71267 -11.58946 1.000 60.20888  ? 1323 GLU   B CA   1 
ATOM   1954 C  C    . GLU   A 1 271 ? 0.43653   -11.82355 -12.96153 1.000 58.65305  ? 1323 GLU   B C    1 
ATOM   1955 O  O    . GLU   A 1 271 ? -0.20852  -12.29258 -13.90248 1.000 55.96107  ? 1323 GLU   B O    1 
ATOM   1956 C  CB   . GLU   A 1 271 ? -1.00646  -10.41175 -11.46733 1.000 61.72159  ? 1323 GLU   B CB   1 
ATOM   1957 C  CG   . GLU   A 1 271 ? -2.11334  -10.47989 -10.42822 1.000 60.42134  ? 1323 GLU   B CG   1 
ATOM   1958 C  CD   . GLU   A 1 271 ? -2.50842  -9.11995  -9.89413  1.000 66.04510  ? 1323 GLU   B CD   1 
ATOM   1959 O  OE1  . GLU   A 1 271 ? -1.89757  -8.11488  -10.31716 1.000 67.07163  ? 1323 GLU   B OE1  1 
ATOM   1960 O  OE2  . GLU   A 1 271 ? -3.42534  -9.06107  -9.04703  1.000 64.81616  ? 1323 GLU   B OE2  1 
ATOM   1961 N  N    . GLU   A 1 272 ? 1.69947   -11.40842 -13.09965 1.000 59.52544  ? 1324 GLU   B N    1 
ATOM   1962 C  CA   . GLU   A 1 272 ? 2.38136   -11.57731 -14.37972 1.000 61.64134  ? 1324 GLU   B CA   1 
ATOM   1963 C  C    . GLU   A 1 272 ? 2.55747   -13.05328 -14.71579 1.000 61.02693  ? 1324 GLU   B C    1 
ATOM   1964 O  O    . GLU   A 1 272 ? 2.33339   -13.46326 -15.86079 1.000 55.34870  ? 1324 GLU   B O    1 
ATOM   1965 C  CB   . GLU   A 1 272 ? 3.73629   -10.86018 -14.37084 1.000 51.98560  ? 1324 GLU   B CB   1 
ATOM   1966 C  CG   . GLU   A 1 272 ? 3.67010   -9.38517  -14.74678 1.000 61.32302  ? 1324 GLU   B CG   1 
ATOM   1967 C  CD   . GLU   A 1 272 ? 5.01800   -8.82002  -15.18089 1.000 68.79764  ? 1324 GLU   B CD   1 
ATOM   1968 O  OE1  . GLU   A 1 272 ? 6.05610   -9.44993  -14.86902 1.000 57.83411  ? 1324 GLU   B OE1  1 
ATOM   1969 O  OE2  . GLU   A 1 272 ? 5.03683   -7.75700  -15.84286 1.000 61.89965  ? 1324 GLU   B OE2  1 
ATOM   1970 N  N    . ARG   A 1 273 ? 2.93865   -13.86928 -13.72386 1.000 63.70533  ? 1325 ARG   B N    1 
ATOM   1971 C  CA   . ARG   A 1 273 ? 3.13877   -15.29825 -13.95593 1.000 58.00830  ? 1325 ARG   B CA   1 
ATOM   1972 C  C    . ARG   A 1 273 ? 1.83880   -16.00937 -14.31383 1.000 54.25893  ? 1325 ARG   B C    1 
ATOM   1973 O  O    . ARG   A 1 273 ? 1.87283   -17.06034 -14.96887 1.000 48.85465  ? 1325 ARG   B O    1 
ATOM   1974 C  CB   . ARG   A 1 273 ? 3.75896   -15.95224 -12.72302 1.000 58.40260  ? 1325 ARG   B CB   1 
ATOM   1975 C  CG   . ARG   A 1 273 ? 5.13094   -15.43311 -12.34114 1.000 56.13603  ? 1325 ARG   B CG   1 
ATOM   1976 C  CD   . ARG   A 1 273 ? 5.55314   -16.05512 -11.02221 1.000 65.70173  ? 1325 ARG   B CD   1 
ATOM   1977 N  NE   . ARG   A 1 273 ? 4.55522   -15.82026 -9.98310  1.000 67.83149  ? 1325 ARG   B NE   1 
ATOM   1978 C  CZ   . ARG   A 1 273 ? 4.33641   -16.62332 -8.95011  1.000 56.28916  ? 1325 ARG   B CZ   1 
ATOM   1979 N  NH1  . ARG   A 1 273 ? 5.01454   -17.74925 -8.78822  1.000 42.38344  ? 1325 ARG   B NH1  1 
ATOM   1980 N  NH2  . ARG   A 1 273 ? 3.40647   -16.29444 -8.05800  1.000 61.22979  ? 1325 ARG   B NH2  1 
ATOM   1981 N  N    . MET   A 1 274 ? 0.69379   -15.46549 -13.88469 1.000 54.69014  ? 1326 MET   B N    1 
ATOM   1982 C  CA   . MET   A 1 274 ? -0.61119  -16.03161 -14.21858 1.000 53.93897  ? 1326 MET   B CA   1 
ATOM   1983 C  C    . MET   A 1 274 ? -0.91935  -15.97759 -15.70654 1.000 53.85963  ? 1326 MET   B C    1 
ATOM   1984 O  O    . MET   A 1 274 ? -1.88633  -16.61367 -16.14747 1.000 48.73293  ? 1326 MET   B O    1 
ATOM   1985 C  CB   . MET   A 1 274 ? -1.73319  -15.29475 -13.47143 1.000 49.44905  ? 1326 MET   B CB   1 
ATOM   1986 C  CG   . MET   A 1 274 ? -1.86400  -15.66681 -12.01243 1.000 56.88520  ? 1326 MET   B CG   1 
ATOM   1987 S  SD   . MET   A 1 274 ? -3.27999  -14.90898 -11.19526 1.000 69.84126  ? 1326 MET   B SD   1 
ATOM   1988 C  CE   . MET   A 1 274 ? -2.52604  -13.50094 -10.38829 1.000 51.49757  ? 1326 MET   B CE   1 
ATOM   1989 N  N    . LYS   A 1 275 ? -0.13850  -15.24048 -16.48460 1.000 50.52510  ? 1327 LYS   B N    1 
ATOM   1990 C  CA   . LYS   A 1 275 ? -0.48367  -14.96647 -17.86555 1.000 50.21031  ? 1327 LYS   B CA   1 
ATOM   1991 C  C    . LYS   A 1 275 ? 0.48330   -15.64834 -18.82767 1.000 43.08793  ? 1327 LYS   B C    1 
ATOM   1992 O  O    . LYS   A 1 275 ? 1.65935   -15.87023 -18.51980 1.000 34.97922  ? 1327 LYS   B O    1 
ATOM   1993 C  CB   . LYS   A 1 275 ? -0.51584  -13.45546 -18.11249 1.000 52.80114  ? 1327 LYS   B CB   1 
ATOM   1994 C  CG   . LYS   A 1 275 ? -1.55482  -12.74059 -17.25836 1.000 54.79477  ? 1327 LYS   B CG   1 
ATOM   1995 C  CD   . LYS   A 1 275 ? -1.90102  -11.37061 -17.81227 1.000 53.22236  ? 1327 LYS   B CD   1 
ATOM   1996 C  CE   . LYS   A 1 275 ? -3.04400  -10.74775 -17.02814 1.000 48.22456  ? 1327 LYS   B CE   1 
ATOM   1997 N  NZ   . LYS   A 1 275 ? -3.53618  -9.50977  -17.67704 1.000 53.89539  ? 1327 LYS   B NZ   1 
ATOM   1998 N  N    . SER   A 1 276 ? -0.05378  -16.02035 -19.98463 1.000 38.04360  ? 1328 SER   B N    1 
ATOM   1999 C  CA   . SER   A 1 276 ? 0.76214   -16.39423 -21.11673 1.000 24.80762  ? 1328 SER   B CA   1 
ATOM   2000 C  C    . SER   A 1 276 ? 1.37295   -15.14314 -21.73875 1.000 22.05279  ? 1328 SER   B C    1 
ATOM   2001 O  O    . SER   A 1 276 ? 0.88686   -14.02920 -21.52666 1.000 20.60632  ? 1328 SER   B O    1 
ATOM   2002 C  CB   . SER   A 1 276 ? -0.08689  -17.13527 -22.13367 1.000 21.91258  ? 1328 SER   B CB   1 
ATOM   2003 O  OG   . SER   A 1 276 ? -0.63172  -18.29335 -21.54166 1.000 33.81851  ? 1328 SER   B OG   1 
ATOM   2004 N  N    . PRO   A 1 277 ? 2.43789   -15.29201 -22.51686 1.000 16.07999  ? 1329 PRO   B N    1 
ATOM   2005 C  CA   . PRO   A 1 277 ? 3.03671   -14.09193 -23.12688 1.000 11.50510  ? 1329 PRO   B CA   1 
ATOM   2006 C  C    . PRO   A 1 277 ? 2.05954   -13.34899 -24.03075 1.000 15.38139  ? 1329 PRO   B C    1 
ATOM   2007 O  O    . PRO   A 1 277 ? 1.99742   -12.11600 -23.98770 1.000 14.07903  ? 1329 PRO   B O    1 
ATOM   2008 C  CB   . PRO   A 1 277 ? 4.24268   -14.64878 -23.90302 1.000 16.34425  ? 1329 PRO   B CB   1 
ATOM   2009 C  CG   . PRO   A 1 277 ? 4.49288   -16.03178 -23.30910 1.000 17.29743  ? 1329 PRO   B CG   1 
ATOM   2010 C  CD   . PRO   A 1 277 ? 3.13897   -16.53293 -22.88898 1.000 15.53815  ? 1329 PRO   B CD   1 
ATOM   2011 N  N    . PHE   A 1 278 ? 1.27553   -14.06404 -24.82970 1.000 16.86868  ? 1330 PHE   B N    1 
ATOM   2012 C  CA   . PHE   A 1 278 ? 0.42136   -13.45709 -25.83959 1.000 17.16282  ? 1330 PHE   B CA   1 
ATOM   2013 C  C    . PHE   A 1 278 ? -1.05358  -13.76724 -25.57645 1.000 21.75026  ? 1330 PHE   B C    1 
ATOM   2014 O  O    . PHE   A 1 278 ? -1.40641  -14.62731 -24.76144 1.000 17.54676  ? 1330 PHE   B O    1 
ATOM   2015 C  CB   . PHE   A 1 278 ? 0.83927   -13.93200 -27.24165 1.000 13.65456  ? 1330 PHE   B CB   1 
ATOM   2016 C  CG   . PHE   A 1 278 ? 2.23419   -13.52385 -27.60478 1.000 17.80579  ? 1330 PHE   B CG   1 
ATOM   2017 C  CD1  . PHE   A 1 278 ? 2.49002   -12.24980 -28.08776 1.000 15.99663  ? 1330 PHE   B CD1  1 
ATOM   2018 C  CD2  . PHE   A 1 278 ? 3.29829   -14.38475 -27.41292 1.000 16.09751  ? 1330 PHE   B CD2  1 
ATOM   2019 C  CE1  . PHE   A 1 278 ? 3.78295   -11.85067 -28.38288 1.000 16.13167  ? 1330 PHE   B CE1  1 
ATOM   2020 C  CE2  . PHE   A 1 278 ? 4.60422   -13.98861 -27.71304 1.000 13.65409  ? 1330 PHE   B CE2  1 
ATOM   2021 C  CZ   . PHE   A 1 278 ? 4.84305   -12.72357 -28.19802 1.000 15.87182  ? 1330 PHE   B CZ   1 
ATOM   2022 N  N    . GLY   A 1 279 ? -1.92172  -13.03630 -26.27533 1.000 19.37126  ? 1331 GLY   B N    1 
ATOM   2023 C  CA   . GLY   A 1 279 ? -3.33869  -13.34344 -26.29520 1.000 14.94407  ? 1331 GLY   B CA   1 
ATOM   2024 C  C    . GLY   A 1 279 ? -3.60365  -14.60044 -27.10522 1.000 25.63147  ? 1331 GLY   B C    1 
ATOM   2025 O  O    . GLY   A 1 279 ? -2.68560  -15.39934 -27.30934 1.000 21.41706  ? 1331 GLY   B O    1 
ATOM   2026 N  N    . SER   A 1 280 ? -4.83468  -14.79554 -27.58210 1.000 22.54856  ? 1332 SER   B N    1 
ATOM   2027 C  CA   . SER   A 1 280 ? -5.21163  -16.04755 -28.23310 1.000 26.34007  ? 1332 SER   B CA   1 
ATOM   2028 C  C    . SER   A 1 280 ? -5.31079  -15.93551 -29.74909 1.000 28.59174  ? 1332 SER   B C    1 
ATOM   2029 O  O    . SER   A 1 280 ? -5.64076  -16.92652 -30.41209 1.000 30.72177  ? 1332 SER   B O    1 
ATOM   2030 C  CB   . SER   A 1 280 ? -6.54152  -16.57470 -27.66499 1.000 25.02450  ? 1332 SER   B CB   1 
ATOM   2031 O  OG   . SER   A 1 280 ? -7.56762  -15.59980 -27.76785 1.000 30.29925  ? 1332 SER   B OG   1 
ATOM   2032 N  N    . SER   A 1 281 ? -5.01797  -14.77546 -30.32208 1.000 18.45989  ? 1333 SER   B N    1 
ATOM   2033 C  CA   . SER   A 1 281 ? -5.06313  -14.63341 -31.76407 1.000 27.42750  ? 1333 SER   B CA   1 
ATOM   2034 C  C    . SER   A 1 281 ? -3.76224  -14.02227 -32.25818 1.000 26.21812  ? 1333 SER   B C    1 
ATOM   2035 O  O    . SER   A 1 281 ? -3.04623  -13.33422 -31.52523 1.000 27.03095  ? 1333 SER   B O    1 
ATOM   2036 C  CB   . SER   A 1 281 ? -6.24326  -13.76351 -32.20392 1.000 27.06321  ? 1333 SER   B CB   1 
ATOM   2037 O  OG   . SER   A 1 281 ? -6.11133  -12.46352 -31.65988 1.000 29.36311  ? 1333 SER   B OG   1 
ATOM   2038 N  N    . PHE   A 1 282 ? -3.46034  -14.29019 -33.52222 1.000 20.77908  ? 1334 PHE   B N    1 
ATOM   2039 C  CA   . PHE   A 1 282 ? -2.43449  -13.55406 -34.23530 1.000 22.21427  ? 1334 PHE   B CA   1 
ATOM   2040 C  C    . PHE   A 1 282 ? -3.01367  -13.08907 -35.56022 1.000 27.13403  ? 1334 PHE   B C    1 
ATOM   2041 O  O    . PHE   A 1 282 ? -4.00967  -13.62315 -36.04914 1.000 23.01393  ? 1334 PHE   B O    1 
ATOM   2042 C  CB   . PHE   A 1 282 ? -1.17143  -14.39893 -34.45446 1.000 17.51154  ? 1334 PHE   B CB   1 
ATOM   2043 C  CG   . PHE   A 1 282 ? -1.38839  -15.62192 -35.30248 1.000 19.23638  ? 1334 PHE   B CG   1 
ATOM   2044 C  CD1  . PHE   A 1 282 ? -1.75622  -16.82798 -34.72549 1.000 22.69311  ? 1334 PHE   B CD1  1 
ATOM   2045 C  CD2  . PHE   A 1 282 ? -1.20354  -15.57685 -36.67650 1.000 22.48712  ? 1334 PHE   B CD2  1 
ATOM   2046 C  CE1  . PHE   A 1 282 ? -1.94519  -17.95397 -35.49851 1.000 15.21300  ? 1334 PHE   B CE1  1 
ATOM   2047 C  CE2  . PHE   A 1 282 ? -1.39851  -16.71385 -37.45952 1.000 23.50986  ? 1334 PHE   B CE2  1 
ATOM   2048 C  CZ   . PHE   A 1 282 ? -1.77033  -17.89990 -36.86352 1.000 21.13209  ? 1334 PHE   B CZ   1 
ATOM   2049 N  N    . ARG   A 1 283 ? -2.38583  -12.07499 -36.13525 1.000 24.67613  ? 1335 ARG   B N    1 
ATOM   2050 C  CA   . ARG   A 1 283 ? -2.83301  -11.52099 -37.40018 1.000 25.58404  ? 1335 ARG   B CA   1 
ATOM   2051 C  C    . ARG   A 1 283 ? -1.70111  -11.60184 -38.41030 1.000 20.06852  ? 1335 ARG   B C    1 
ATOM   2052 O  O    . ARG   A 1 283 ? -0.52208  -11.53374 -38.05042 1.000 21.93993  ? 1335 ARG   B O    1 
ATOM   2053 C  CB   . ARG   A 1 283 ? -3.29314  -10.06204 -37.23908 1.000 23.56903  ? 1335 ARG   B CB   1 
ATOM   2054 C  CG   . ARG   A 1 283 ? -4.63709  -9.86620  -36.53494 1.000 31.15440  ? 1335 ARG   B CG   1 
ATOM   2055 C  CD   . ARG   A 1 283 ? -4.84319  -8.39223  -36.14187 1.000 37.57364  ? 1335 ARG   B CD   1 
ATOM   2056 N  NE   . ARG   A 1 283 ? -6.24921  -8.02937  -35.97571 1.000 50.86758  ? 1335 ARG   B NE   1 
ATOM   2057 C  CZ   . ARG   A 1 283 ? -6.93137  -7.24041  -36.80061 1.000 52.19021  ? 1335 ARG   B CZ   1 
ATOM   2058 N  NH1  . ARG   A 1 283 ? -6.35453  -6.65332  -37.83865 1.000 36.23810  ? 1335 ARG   B NH1  1 
ATOM   2059 N  NH2  . ARG   A 1 283 ? -8.22737  -7.04155  -36.58247 1.000 51.65006  ? 1335 ARG   B NH2  1 
ATOM   2060 N  N    . THR   A 1 284 ? -2.06422  -11.75983 -39.67527 1.000 18.06378  ? 1336 THR   B N    1 
ATOM   2061 C  CA   . THR   A 1 284 ? -1.11835  -11.60470 -40.76336 1.000 17.82154  ? 1336 THR   B CA   1 
ATOM   2062 C  C    . THR   A 1 284 ? -1.42355  -10.30970 -41.50929 1.000 21.96295  ? 1336 THR   B C    1 
ATOM   2063 O  O    . THR   A 1 284 ? -2.57160  -9.85681  -41.57315 1.000 20.60029  ? 1336 THR   B O    1 
ATOM   2064 C  CB   . THR   A 1 284 ? -1.16233  -12.79767 -41.72540 1.000 20.01300  ? 1336 THR   B CB   1 
ATOM   2065 O  OG1  . THR   A 1 284 ? -2.50136  -12.99578 -42.18927 1.000 26.34633  ? 1336 THR   B OG1  1 
ATOM   2066 C  CG2  . THR   A 1 284 ? -0.69614  -14.04765 -41.03250 1.000 18.21396  ? 1336 THR   B CG2  1 
ATOM   2067 N  N    . PHE   A 1 285 ? -0.37767  -9.69858  -42.04437 1.000 19.22141  ? 1337 PHE   B N    1 
ATOM   2068 C  CA   . PHE   A 1 285 ? -0.49486  -8.44556  -42.76631 1.000 21.89984  ? 1337 PHE   B CA   1 
ATOM   2069 C  C    . PHE   A 1 285 ? 0.36202   -8.52944  -44.00640 1.000 19.68632  ? 1337 PHE   B C    1 
ATOM   2070 O  O    . PHE   A 1 285 ? 1.40508   -9.18833  -44.01454 1.000 20.14334  ? 1337 PHE   B O    1 
ATOM   2071 C  CB   . PHE   A 1 285 ? -0.02190  -7.22955  -41.95432 1.000 21.23164  ? 1337 PHE   B CB   1 
ATOM   2072 C  CG   . PHE   A 1 285 ? -0.61477  -7.13866  -40.59125 1.000 21.02564  ? 1337 PHE   B CG   1 
ATOM   2073 C  CD1  . PHE   A 1 285 ? -0.08359  -7.86664  -39.54633 1.000 22.19721  ? 1337 PHE   B CD1  1 
ATOM   2074 C  CD2  . PHE   A 1 285 ? -1.69583  -6.30777  -40.34611 1.000 26.07881  ? 1337 PHE   B CD2  1 
ATOM   2075 C  CE1  . PHE   A 1 285 ? -0.62747  -7.78674  -38.27928 1.000 17.69572  ? 1337 PHE   B CE1  1 
ATOM   2076 C  CE2  . PHE   A 1 285 ? -2.24470  -6.21187  -39.07905 1.000 20.14122  ? 1337 PHE   B CE2  1 
ATOM   2077 C  CZ   . PHE   A 1 285 ? -1.71053  -6.95285  -38.04513 1.000 23.58292  ? 1337 PHE   B CZ   1 
ATOM   2078 N  N    . ASN   A 1 286 ? -0.06316  -7.82544  -45.04334 1.000 21.95052  ? 1338 ASN   B N    1 
ATOM   2079 C  CA   . ASN   A 1 286 ? 0.81971   -7.63631  -46.17742 1.000 22.40733  ? 1338 ASN   B CA   1 
ATOM   2080 C  C    . ASN   A 1 286 ? 2.02167   -6.79821  -45.74151 1.000 21.21556  ? 1338 ASN   B C    1 
ATOM   2081 O  O    . ASN   A 1 286 ? 1.86862   -5.72125  -45.15646 1.000 20.21374  ? 1338 ASN   B O    1 
ATOM   2082 C  CB   . ASN   A 1 286 ? 0.07652   -6.97334  -47.32832 1.000 21.19101  ? 1338 ASN   B CB   1 
ATOM   2083 C  CG   . ASN   A 1 286 ? 0.90839   -6.92422  -48.57140 1.000 32.59819  ? 1338 ASN   B CG   1 
ATOM   2084 O  OD1  . ASN   A 1 286 ? 1.80230   -6.08712  -48.69346 1.000 31.89029  ? 1338 ASN   B OD1  1 
ATOM   2085 N  ND2  . ASN   A 1 286 ? 0.64638   -7.83821  -49.49841 1.000 40.58405  ? 1338 ASN   B ND2  1 
ATOM   2086 N  N    . ALA   A 1 287 ? 3.22269   -7.30908  -46.00865 1.000 19.81774  ? 1339 ALA   B N    1 
ATOM   2087 C  CA   . ALA   A 1 287 ? 4.42968   -6.65498  -45.52375 1.000 26.29442  ? 1339 ALA   B CA   1 
ATOM   2088 C  C    . ALA   A 1 287 ? 4.73947   -5.34293  -46.24074 1.000 24.25287  ? 1339 ALA   B C    1 
ATOM   2089 O  O    . ALA   A 1 287 ? 5.52745   -4.55087  -45.71579 1.000 18.30096  ? 1339 ALA   B O    1 
ATOM   2090 C  CB   . ALA   A 1 287 ? 5.62476   -7.60386  -45.64491 1.000 18.47712  ? 1339 ALA   B CB   1 
ATOM   2091 N  N    . THR   A 1 288 ? 4.16333   -5.08494  -47.41967 1.000 20.57162  ? 1340 THR   B N    1 
ATOM   2092 C  CA   . THR   A 1 288 ? 4.51114   -3.84088  -48.11066 1.000 25.54875  ? 1340 THR   B CA   1 
ATOM   2093 C  C    . THR   A 1 288 ? 3.62206   -2.66698  -47.69553 1.000 23.76928  ? 1340 THR   B C    1 
ATOM   2094 O  O    . THR   A 1 288 ? 4.09496   -1.52694  -47.60853 1.000 21.88455  ? 1340 THR   B O    1 
ATOM   2095 C  CB   . THR   A 1 288 ? 4.45400   -4.03083  -49.63366 1.000 23.98418  ? 1340 THR   B CB   1 
ATOM   2096 O  OG1  . THR   A 1 288 ? 3.11799   -4.32195  -50.02454 1.000 30.01341  ? 1340 THR   B OG1  1 
ATOM   2097 C  CG2  . THR   A 1 288 ? 5.34307   -5.18273  -50.07179 1.000 23.15444  ? 1340 THR   B CG2  1 
ATOM   2098 N  N    . ASP   A 1 289 ? 2.34411   -2.90412  -47.42040 1.000 20.32002  ? 1341 ASP   B N    1 
ATOM   2099 C  CA   . ASP   A 1 289 ? 1.44704   -1.80322  -47.10127 1.000 23.97669  ? 1341 ASP   B CA   1 
ATOM   2100 C  C    . ASP   A 1 289 ? 0.70019   -1.99534  -45.78820 1.000 26.09281  ? 1341 ASP   B C    1 
ATOM   2101 O  O    . ASP   A 1 289 ? -0.10985  -1.13643  -45.42609 1.000 24.21376  ? 1341 ASP   B O    1 
ATOM   2102 C  CB   . ASP   A 1 289 ? 0.44190   -1.58527  -48.24716 1.000 33.73717  ? 1341 ASP   B CB   1 
ATOM   2103 C  CG   . ASP   A 1 289 ? -0.40501  -2.81235  -48.52912 1.000 30.74827  ? 1341 ASP   B CG   1 
ATOM   2104 O  OD1  . ASP   A 1 289 ? -0.39383  -3.75838  -47.70815 1.000 32.79488  ? 1341 ASP   B OD1  1 
ATOM   2105 O  OD2  . ASP   A 1 289 ? -1.08411  -2.82938  -49.57805 1.000 36.51689  ? 1341 ASP   B OD2  1 
ATOM   2106 N  N    . TYR   A 1 290 ? 0.94937   -3.08734  -45.06827 1.000 23.72735  ? 1342 TYR   B N    1 
ATOM   2107 C  CA   . TYR   A 1 290 ? 0.38154   -3.37644  -43.75522 1.000 23.29931  ? 1342 TYR   B CA   1 
ATOM   2108 C  C    . TYR   A 1 290 ? -1.12644  -3.60059  -43.78407 1.000 23.09749  ? 1342 TYR   B C    1 
ATOM   2109 O  O    . TYR   A 1 290 ? -1.76833  -3.61369  -42.72001 1.000 26.58627  ? 1342 TYR   B O    1 
ATOM   2110 C  CB   . TYR   A 1 290 ? 0.72953   -2.27645  -42.74822 1.000 21.64350  ? 1342 TYR   B CB   1 
ATOM   2111 C  CG   . TYR   A 1 290 ? 2.22353   -2.11830  -42.58936 1.000 20.96263  ? 1342 TYR   B CG   1 
ATOM   2112 C  CD1  . TYR   A 1 290 ? 2.93870   -2.92827  -41.71647 1.000 15.97870  ? 1342 TYR   B CD1  1 
ATOM   2113 C  CD2  . TYR   A 1 290 ? 2.92236   -1.17521  -43.33740 1.000 27.98387  ? 1342 TYR   B CD2  1 
ATOM   2114 C  CE1  . TYR   A 1 290 ? 4.31670   -2.78214  -41.57060 1.000 19.90452  ? 1342 TYR   B CE1  1 
ATOM   2115 C  CE2  . TYR   A 1 290 ? 4.29436   -1.02508  -43.21154 1.000 20.04510  ? 1342 TYR   B CE2  1 
ATOM   2116 C  CZ   . TYR   A 1 290 ? 4.99353   -1.83004  -42.32564 1.000 23.60557  ? 1342 TYR   B CZ   1 
ATOM   2117 O  OH   . TYR   A 1 290 ? 6.36253   -1.67391  -42.20577 1.000 15.14560  ? 1342 TYR   B OH   1 
ATOM   2118 N  N    . LYS   A 1 291 ? -1.71355  -3.79960  -44.95702 1.000 21.65726  ? 1343 LYS   B N    1 
ATOM   2119 C  CA   . LYS   A 1 291 ? -3.11851  -4.17074  -45.00689 1.000 29.89711  ? 1343 LYS   B CA   1 
ATOM   2120 C  C    . LYS   A 1 291 ? -3.32131  -5.54078  -44.36592 1.000 23.10844  ? 1343 LYS   B C    1 
ATOM   2121 O  O    . LYS   A 1 291 ? -2.45924  -6.41870  -44.48204 1.000 21.82331  ? 1343 LYS   B O    1 
ATOM   2122 C  CB   . LYS   A 1 291 ? -3.62166  -4.18474  -46.44584 1.000 27.89806  ? 1343 LYS   B CB   1 
ATOM   2123 C  CG   . LYS   A 1 291 ? -4.02585  -2.81976  -46.95475 1.000 40.50538  ? 1343 LYS   B CG   1 
ATOM   2124 C  CD   . LYS   A 1 291 ? -4.04601  -2.77271  -48.48174 1.000 46.02131  ? 1343 LYS   B CD   1 
ATOM   2125 C  CE   . LYS   A 1 291 ? -4.50019  -1.39973  -48.97265 1.000 48.73186  ? 1343 LYS   B CE   1 
ATOM   2126 N  NZ   . LYS   A 1 291 ? -4.74717  -0.46880  -47.83159 1.000 48.06124  ? 1343 LYS   B NZ   1 
ATOM   2127 N  N    . PRO   A 1 292 ? -4.43722  -5.74892  -43.67781 1.000 25.91192  ? 1344 PRO   B N    1 
ATOM   2128 C  CA   . PRO   A 1 292 ? -4.66603  -7.03796  -43.01883 1.000 29.73677  ? 1344 PRO   B CA   1 
ATOM   2129 C  C    . PRO   A 1 292 ? -4.94702  -8.14296  -44.02285 1.000 24.44689  ? 1344 PRO   B C    1 
ATOM   2130 O  O    . PRO   A 1 292 ? -5.59815  -7.92798  -45.04577 1.000 29.56822  ? 1344 PRO   B O    1 
ATOM   2131 C  CB   . PRO   A 1 292 ? -5.88596  -6.77212  -42.13070 1.000 28.13109  ? 1344 PRO   B CB   1 
ATOM   2132 C  CG   . PRO   A 1 292 ? -5.90809  -5.29813  -41.94964 1.000 34.09833  ? 1344 PRO   B CG   1 
ATOM   2133 C  CD   . PRO   A 1 292 ? -5.41728  -4.73903  -43.25567 1.000 36.41215  ? 1344 PRO   B CD   1 
ATOM   2134 N  N    . ILE   A 1 293 ? -4.43988  -9.33692  -43.72094 1.000 25.65331  ? 1345 ILE   B N    1 
ATOM   2135 C  CA   . ILE   A 1 293 ? -4.73984  -10.51492 -44.52795 1.000 27.91033  ? 1345 ILE   B CA   1 
ATOM   2136 C  C    . ILE   A 1 293 ? -5.69267  -11.40404 -43.74289 1.000 33.50878  ? 1345 ILE   B C    1 
ATOM   2137 O  O    . ILE   A 1 293 ? -6.87670  -11.50214 -44.08077 1.000 35.58374  ? 1345 ILE   B O    1 
ATOM   2138 C  CB   . ILE   A 1 293 ? -3.46381  -11.27678 -44.93011 1.000 21.97342  ? 1345 ILE   B CB   1 
ATOM   2139 C  CG1  . ILE   A 1 293 ? -2.61399  -10.41466 -45.86317 1.000 18.65386  ? 1345 ILE   B CG1  1 
ATOM   2140 C  CG2  . ILE   A 1 293 ? -3.83075  -12.60979 -45.59012 1.000 16.18841  ? 1345 ILE   B CG2  1 
ATOM   2141 C  CD1  . ILE   A 1 293 ? -1.16195  -10.81752 -45.90733 1.000 17.39025  ? 1345 ILE   B CD1  1 
ATOM   2142 N  N    . ALA   A 1 294 ? -5.20350  -12.03103 -42.67296 1.000 27.99245  ? 1346 ALA   B N    1 
ATOM   2143 C  CA   . ALA   A 1 294 ? -6.01233  -12.96514 -41.90191 1.000 26.42637  ? 1346 ALA   B CA   1 
ATOM   2144 C  C    . ALA   A 1 294 ? -5.95121  -12.62818 -40.41990 1.000 27.22619  ? 1346 ALA   B C    1 
ATOM   2145 O  O    . ALA   A 1 294 ? -4.97122  -12.05311 -39.93398 1.000 24.23847  ? 1346 ALA   B O    1 
ATOM   2146 C  CB   . ALA   A 1 294 ? -5.55621  -14.41408 -42.11701 1.000 25.71996  ? 1346 ALA   B CB   1 
ATOM   2147 N  N    . THR   A 1 295 ? -7.02811  -12.97132 -39.71381 1.000 24.36961  ? 1347 THR   B N    1 
ATOM   2148 C  CA   . THR   A 1 295 ? -7.09396  -12.92538 -38.25680 1.000 19.91337  ? 1347 THR   B CA   1 
ATOM   2149 C  C    . THR   A 1 295 ? -7.40877  -14.33242 -37.77182 1.000 28.53113  ? 1347 THR   B C    1 
ATOM   2150 O  O    . THR   A 1 295 ? -8.49575  -14.85352 -38.03772 1.000 23.38534  ? 1347 THR   B O    1 
ATOM   2151 C  CB   . THR   A 1 295 ? -8.14901  -11.94150 -37.77165 1.000 27.63630  ? 1347 THR   B CB   1 
ATOM   2152 O  OG1  . THR   A 1 295 ? -7.70016  -10.59844 -37.99565 1.000 24.81321  ? 1347 THR   B OG1  1 
ATOM   2153 C  CG2  . THR   A 1 295 ? -8.39983  -12.15257 -36.27964 1.000 34.69179  ? 1347 THR   B CG2  1 
ATOM   2154 N  N    . ILE   A 1 296 ? -6.46564  -14.94636 -37.06394 1.000 25.28499  ? 1348 ILE   B N    1 
ATOM   2155 C  CA   . ILE   A 1 296 ? -6.56646  -16.34238 -36.65498 1.000 26.97754  ? 1348 ILE   B CA   1 
ATOM   2156 C  C    . ILE   A 1 296 ? -6.65830  -16.39945 -35.13897 1.000 30.74347  ? 1348 ILE   B C    1 
ATOM   2157 O  O    . ILE   A 1 296 ? -5.73027  -15.97438 -34.43705 1.000 29.86759  ? 1348 ILE   B O    1 
ATOM   2158 C  CB   . ILE   A 1 296 ? -5.37143  -17.16225 -37.15713 1.000 23.45232  ? 1348 ILE   B CB   1 
ATOM   2159 C  CG1  . ILE   A 1 296 ? -5.19561  -16.96817 -38.66414 1.000 26.46155  ? 1348 ILE   B CG1  1 
ATOM   2160 C  CG2  . ILE   A 1 296 ? -5.55125  -18.63128 -36.78916 1.000 25.70854  ? 1348 ILE   B CG2  1 
ATOM   2161 C  CD1  . ILE   A 1 296 ? -6.44966  -17.30927 -39.47402 1.000 29.74427  ? 1348 ILE   B CD1  1 
ATOM   2162 N  N    . ASP   A 1 297 ? -7.76920  -16.92957 -34.63187 1.000 28.43245  ? 1349 ASP   B N    1 
ATOM   2163 C  CA   . ASP   A 1 297 ? -7.96203  -17.13264 -33.19786 1.000 35.20054  ? 1349 ASP   B CA   1 
ATOM   2164 C  C    . ASP   A 1 297 ? -7.97185  -18.63065 -32.91891 1.000 41.44179  ? 1349 ASP   B C    1 
ATOM   2165 O  O    . ASP   A 1 297 ? -8.91882  -19.32973 -33.29784 1.000 46.48683  ? 1349 ASP   B O    1 
ATOM   2166 C  CB   . ASP   A 1 297 ? -9.25904  -16.49279 -32.70770 1.000 40.42879  ? 1349 ASP   B CB   1 
ATOM   2167 C  CG   . ASP   A 1 297 ? -9.35289  -16.46185 -31.19169 1.000 43.93435  ? 1349 ASP   B CG   1 
ATOM   2168 O  OD1  . ASP   A 1 297 ? -9.03872  -17.48984 -30.55676 1.000 47.73651  ? 1349 ASP   B OD1  1 
ATOM   2169 O  OD2  . ASP   A 1 297 ? -9.70594  -15.40291 -30.62862 1.000 51.01406  ? 1349 ASP   B OD2  1 
ATOM   2170 N  N    . VAL   A 1 298 ? -6.93174  -19.11758 -32.24704 1.000 33.98711  ? 1350 VAL   B N    1 
ATOM   2171 C  CA   . VAL   A 1 298 ? -6.81657  -20.53658 -31.92910 1.000 35.75159  ? 1350 VAL   B CA   1 
ATOM   2172 C  C    . VAL   A 1 298 ? -7.55040  -20.84470 -30.63004 1.000 33.96299  ? 1350 VAL   B C    1 
ATOM   2173 O  O    . VAL   A 1 298 ? -7.48424  -21.97271 -30.13209 1.000 36.68778  ? 1350 VAL   B O    1 
ATOM   2174 C  CB   . VAL   A 1 298 ? -5.34252  -20.96044 -31.84327 1.000 35.40527  ? 1350 VAL   B CB   1 
ATOM   2175 C  CG1  . VAL   A 1 298 ? -4.67967  -20.80132 -33.20033 1.000 32.97878  ? 1350 VAL   B CG1  1 
ATOM   2176 C  CG2  . VAL   A 1 298 ? -4.62149  -20.13240 -30.78831 1.000 33.57616  ? 1350 VAL   B CG2  1 
ATOM   2177 N  N    . LYS   A 1 299 ? -8.24544  -19.84578 -30.07893 1.000 32.25352  ? 1351 LYS   B N    1 
ATOM   2178 C  CA   . LYS   A 1 299 ? -9.07431  -19.94191 -28.87485 1.000 37.19340  ? 1351 LYS   B CA   1 
ATOM   2179 C  C    . LYS   A 1 299 ? -8.28914  -20.33088 -27.62694 1.000 35.47669  ? 1351 LYS   B C    1 
ATOM   2180 O  O    . LYS   A 1 299 ? -8.89301  -20.62697 -26.58889 1.000 45.29853  ? 1351 LYS   B O    1 
ATOM   2181 C  CB   . LYS   A 1 299 ? -10.23924 -20.91602 -29.06676 1.000 37.97610  ? 1351 LYS   B CB   1 
ATOM   2182 C  CG   . LYS   A 1 299 ? -11.32138 -20.41609 -30.01264 1.000 44.81748  ? 1351 LYS   B CG   1 
ATOM   2183 C  CD   . LYS   A 1 299 ? -10.97350 -20.70300 -31.46668 1.000 50.44746  ? 1351 LYS   B CD   1 
ATOM   2184 C  CE   . LYS   A 1 299 ? -12.20061 -20.55109 -32.36955 1.000 61.75352  ? 1351 LYS   B CE   1 
ATOM   2185 N  NZ   . LYS   A 1 299 ? -12.03268 -21.23703 -33.68559 1.000 51.58093  ? 1351 LYS   B NZ   1 
ATOM   2186 N  N    . ARG   A 1 300 ? -6.96315  -20.34474 -27.70508 1.000 33.69461  ? 1352 ARG   B N    1 
ATOM   2187 C  CA   . ARG   A 1 300 ? -6.07701  -20.61270 -26.58218 1.000 28.36615  ? 1352 ARG   B CA   1 
ATOM   2188 C  C    . ARG   A 1 300 ? -4.96011  -19.57459 -26.61126 1.000 27.47882  ? 1352 ARG   B C    1 
ATOM   2189 O  O    . ARG   A 1 300 ? -4.54927  -19.12951 -27.68928 1.000 25.79250  ? 1352 ARG   B O    1 
ATOM   2190 C  CB   . ARG   A 1 300 ? -5.47488  -22.04064 -26.65729 1.000 25.43272  ? 1352 ARG   B CB   1 
ATOM   2191 C  CG   . ARG   A 1 300 ? -6.47277  -23.19673 -26.76423 1.000 27.95527  ? 1352 ARG   B CG   1 
ATOM   2192 C  CD   . ARG   A 1 300 ? -5.76368  -24.52765 -27.11035 1.000 31.25789  ? 1352 ARG   B CD   1 
ATOM   2193 N  NE   . ARG   A 1 300 ? -5.61681  -24.73058 -28.54938 1.000 35.17925  ? 1352 ARG   B NE   1 
ATOM   2194 C  CZ   . ARG   A 1 300 ? -6.58785  -25.17565 -29.34129 1.000 52.50294  ? 1352 ARG   B CZ   1 
ATOM   2195 N  NH1  . ARG   A 1 300 ? -7.76376  -25.54778 -28.85019 1.000 39.58329  ? 1352 ARG   B NH1  1 
ATOM   2196 N  NH2  . ARG   A 1 300 ? -6.38098  -25.23158 -30.65932 1.000 26.47708  ? 1352 ARG   B NH2  1 
ATOM   2197 N  N    . ASN   A 1 301 ? -4.46203  -19.19358 -25.43430 1.000 17.62760  ? 1353 ASN   B N    1 
ATOM   2198 C  CA   . ASN   A 1 301 ? -3.42213  -18.16748 -25.37136 1.000 20.87538  ? 1353 ASN   B CA   1 
ATOM   2199 C  C    . ASN   A 1 301 ? -2.10113  -18.69633 -25.92052 1.000 20.35621  ? 1353 ASN   B C    1 
ATOM   2200 O  O    . ASN   A 1 301 ? -1.76000  -19.86931 -25.74960 1.000 17.07517  ? 1353 ASN   B O    1 
ATOM   2201 C  CB   . ASN   A 1 301 ? -3.22603  -17.67351 -23.94137 1.000 16.73251  ? 1353 ASN   B CB   1 
ATOM   2202 C  CG   . ASN   A 1 301 ? -4.43705  -16.91765 -23.41922 1.000 25.07160  ? 1353 ASN   B CG   1 
ATOM   2203 O  OD1  . ASN   A 1 301 ? -4.49196  -16.54470 -22.25520 1.000 32.77985  ? 1353 ASN   B OD1  1 
ATOM   2204 N  ND2  . ASN   A 1 301 ? -5.41816  -16.69872 -24.28311 1.000 24.31544  ? 1353 ASN   B ND2  1 
ATOM   2205 N  N    . ILE   A 1 302 ? -1.34128  -17.80123 -26.56757 1.000 16.59844  ? 1354 ILE   B N    1 
ATOM   2206 C  CA   . ILE   A 1 302 ? -0.16933  -18.16709 -27.36170 1.000 14.26669  ? 1354 ILE   B CA   1 
ATOM   2207 C  C    . ILE   A 1 302 ? 1.10772   -17.86599 -26.58882 1.000 16.20253  ? 1354 ILE   B C    1 
ATOM   2208 O  O    . ILE   A 1 302 ? 1.23868   -16.80700 -25.96279 1.000 13.24454  ? 1354 ILE   B O    1 
ATOM   2209 C  CB   . ILE   A 1 302 ? -0.18554  -17.43804 -28.72067 1.000 13.15289  ? 1354 ILE   B CB   1 
ATOM   2210 C  CG1  . ILE   A 1 302 ? -1.43258  -17.85614 -29.50256 1.000 15.69176  ? 1354 ILE   B CG1  1 
ATOM   2211 C  CG2  . ILE   A 1 302 ? 1.09441   -17.73089 -29.49181 1.000 15.31999  ? 1354 ILE   B CG2  1 
ATOM   2212 C  CD1  . ILE   A 1 302 ? -1.65678  -17.14411 -30.79851 1.000 16.74058  ? 1354 ILE   B CD1  1 
ATOM   2213 N  N    . PHE   A 1 303 ? 2.04681   -18.81590 -26.61695 1.000 14.45502  ? 1355 PHE   B N    1 
ATOM   2214 C  CA   . PHE   A 1 303 ? 3.36686   -18.65479 -26.02708 1.000 9.94480   ? 1355 PHE   B CA   1 
ATOM   2215 C  C    . PHE   A 1 303 ? 4.44272   -18.29365 -27.04618 1.000 14.55435  ? 1355 PHE   B C    1 
ATOM   2216 O  O    . PHE   A 1 303 ? 5.36468   -17.54157 -26.71124 1.000 14.68096  ? 1355 PHE   B O    1 
ATOM   2217 C  CB   . PHE   A 1 303 ? 3.78706   -19.94178 -25.30717 1.000 13.58984  ? 1355 PHE   B CB   1 
ATOM   2218 C  CG   . PHE   A 1 303 ? 3.40821   -19.98287 -23.84313 1.000 12.39592  ? 1355 PHE   B CG   1 
ATOM   2219 C  CD1  . PHE   A 1 303 ? 2.11128   -20.32101 -23.45401 1.000 12.40191  ? 1355 PHE   B CD1  1 
ATOM   2220 C  CD2  . PHE   A 1 303 ? 4.35728   -19.70881 -22.85922 1.000 15.61291  ? 1355 PHE   B CD2  1 
ATOM   2221 C  CE1  . PHE   A 1 303 ? 1.76043   -20.38009 -22.10698 1.000 13.06102  ? 1355 PHE   B CE1  1 
ATOM   2222 C  CE2  . PHE   A 1 303 ? 4.01443   -19.76389 -21.50519 1.000 13.54477  ? 1355 PHE   B CE2  1 
ATOM   2223 C  CZ   . PHE   A 1 303 ? 2.71250   -20.09503 -21.13406 1.000 13.49051  ? 1355 PHE   B CZ   1 
ATOM   2224 N  N    . ASP   A 1 304 ? 4.34864   -18.79961 -28.27519 1.000 15.11997  ? 1356 ASP   B N    1 
ATOM   2225 C  CA   . ASP   A 1 304 ? 5.35351   -18.56048 -29.30128 1.000 13.80532  ? 1356 ASP   B CA   1 
ATOM   2226 C  C    . ASP   A 1 304 ? 4.81042   -19.04248 -30.63824 1.000 17.88304  ? 1356 ASP   B C    1 
ATOM   2227 O  O    . ASP   A 1 304 ? 3.83549   -19.79858 -30.69517 1.000 12.77026  ? 1356 ASP   B O    1 
ATOM   2228 C  CB   . ASP   A 1 304 ? 6.66961   -19.28236 -28.98344 1.000 12.35006  ? 1356 ASP   B CB   1 
ATOM   2229 C  CG   . ASP   A 1 304 ? 7.88849   -18.56622 -29.54954 1.000 17.71942  ? 1356 ASP   B CG   1 
ATOM   2230 O  OD1  . ASP   A 1 304 ? 7.74832   -17.41822 -30.01548 1.000 16.63816  ? 1356 ASP   B OD1  1 
ATOM   2231 O  OD2  . ASP   A 1 304 ? 8.98855   -19.15711 -29.52967 1.000 15.18290  ? 1356 ASP   B OD2  1 
ATOM   2232 N  N    . LEU   A 1 305 ? 5.46427   -18.60638 -31.71129 1.000 13.65483  ? 1357 LEU   B N    1 
ATOM   2233 C  CA   . LEU   A 1 305 ? 5.18018   -19.14236 -33.03228 1.000 19.54001  ? 1357 LEU   B CA   1 
ATOM   2234 C  C    . LEU   A 1 305 ? 6.38907   -18.90421 -33.92540 1.000 18.88196  ? 1357 LEU   B C    1 
ATOM   2235 O  O    . LEU   A 1 305 ? 7.20001   -18.00614 -33.67145 1.000 23.09978  ? 1357 LEU   B O    1 
ATOM   2236 C  CB   . LEU   A 1 305 ? 3.90706   -18.53546 -33.64413 1.000 24.21101  ? 1357 LEU   B CB   1 
ATOM   2237 C  CG   . LEU   A 1 305 ? 3.78487   -17.10146 -34.16107 1.000 21.78987  ? 1357 LEU   B CG   1 
ATOM   2238 C  CD1  . LEU   A 1 305 ? 4.54571   -16.89734 -35.45714 1.000 20.33153  ? 1357 LEU   B CD1  1 
ATOM   2239 C  CD2  . LEU   A 1 305 ? 2.30881   -16.76659 -34.38190 1.000 24.03188  ? 1357 LEU   B CD2  1 
ATOM   2240 N  N    . CYS   A 1 306 ? 6.52105   -19.74516 -34.94344 1.000 15.67817  ? 1358 CYS   B N    1 
ATOM   2241 C  CA   . CYS   A 1 306 ? 7.64995   -19.67902 -35.85756 1.000 17.32659  ? 1358 CYS   B CA   1 
ATOM   2242 C  C    . CYS   A 1 306 ? 7.22787   -20.32201 -37.16954 1.000 18.87994  ? 1358 CYS   B C    1 
ATOM   2243 O  O    . CYS   A 1 306 ? 6.20494   -21.01311 -37.24446 1.000 17.97006  ? 1358 CYS   B O    1 
ATOM   2244 C  CB   . CYS   A 1 306 ? 8.91107   -20.36091 -35.27871 1.000 15.71109  ? 1358 CYS   B CB   1 
ATOM   2245 S  SG   . CYS   A 1 306 ? 8.78128   -22.18194 -34.96276 1.000 17.73301  ? 1358 CYS   B SG   1 
ATOM   2246 N  N    . THR   A 1 307 ? 8.01774   -20.06490 -38.20861 1.000 17.72365  ? 1359 THR   B N    1 
ATOM   2247 C  CA   . THR   A 1 307 ? 7.86667   -20.70886 -39.50462 1.000 20.97638  ? 1359 THR   B CA   1 
ATOM   2248 C  C    . THR   A 1 307 ? 9.17470   -21.38772 -39.88377 1.000 20.52536  ? 1359 THR   B C    1 
ATOM   2249 O  O    . THR   A 1 307 ? 10.23973  -21.08664 -39.32887 1.000 21.42529  ? 1359 THR   B O    1 
ATOM   2250 C  CB   . THR   A 1 307 ? 7.47646   -19.71386 -40.60354 1.000 19.77092  ? 1359 THR   B CB   1 
ATOM   2251 O  OG1  . THR   A 1 307 ? 8.49935   -18.71876 -40.71861 1.000 24.08156  ? 1359 THR   B OG1  1 
ATOM   2252 C  CG2  . THR   A 1 307 ? 6.15643   -19.04600 -40.27838 1.000 22.18198  ? 1359 THR   B CG2  1 
ATOM   2253 N  N    . ASP   A 1 308 ? 9.07770   -22.32470 -40.82480 1.000 23.35627  ? 1360 ASP   B N    1 
ATOM   2254 C  CA   . ASP   A 1 308 ? 10.27570  -22.93856 -41.36294 1.000 20.17142  ? 1360 ASP   B CA   1 
ATOM   2255 C  C    . ASP   A 1 308 ? 10.85550  -22.04846 -42.46797 1.000 24.83255  ? 1360 ASP   B C    1 
ATOM   2256 O  O    . ASP   A 1 308 ? 10.23736  -21.07651 -42.91087 1.000 20.48070  ? 1360 ASP   B O    1 
ATOM   2257 C  CB   . ASP   A 1 308 ? 9.97679   -24.35157 -41.86696 1.000 21.61045  ? 1360 ASP   B CB   1 
ATOM   2258 C  CG   . ASP   A 1 308 ? 8.89868   -24.38964 -42.94286 1.000 26.96222  ? 1360 ASP   B CG   1 
ATOM   2259 O  OD1  . ASP   A 1 308 ? 7.91062   -23.63474 -42.83973 1.000 28.18128  ? 1360 ASP   B OD1  1 
ATOM   2260 O  OD2  . ASP   A 1 308 ? 9.03666   -25.19059 -43.89690 1.000 34.99015  ? 1360 ASP   B OD2  1 
ATOM   2261 N  N    . THR   A 1 309 ? 12.06849  -22.37733 -42.90611 1.000 21.83420  ? 1361 THR   B N    1 
ATOM   2262 C  CA   . THR   A 1 309 ? 12.74730  -21.50623 -43.85815 1.000 24.48625  ? 1361 THR   B CA   1 
ATOM   2263 C  C    . THR   A 1 309 ? 11.98116  -21.39325 -45.16806 1.000 27.37788  ? 1361 THR   B C    1 
ATOM   2264 O  O    . THR   A 1 309 ? 12.11199  -20.38822 -45.87804 1.000 32.20650  ? 1361 THR   B O    1 
ATOM   2265 C  CB   . THR   A 1 309 ? 14.15433  -22.01508 -44.12631 1.000 25.76769  ? 1361 THR   B CB   1 
ATOM   2266 O  OG1  . THR   A 1 309 ? 14.06538  -23.27206 -44.80435 1.000 31.39727  ? 1361 THR   B OG1  1 
ATOM   2267 C  CG2  . THR   A 1 309 ? 14.89648  -22.20405 -42.81739 1.000 23.70771  ? 1361 THR   B CG2  1 
ATOM   2268 N  N    . LYS   A 1 310 ? 11.19322  -22.40532 -45.51902 1.000 27.41529  ? 1362 LYS   B N    1 
ATOM   2269 C  CA   . LYS   A 1 310 ? 10.42109  -22.36835 -46.75394 1.000 29.73852  ? 1362 LYS   B CA   1 
ATOM   2270 C  C    . LYS   A 1 310 ? 9.01806   -21.82749 -46.54777 1.000 25.63967  ? 1362 LYS   B C    1 
ATOM   2271 O  O    . LYS   A 1 310 ? 8.26895   -21.69653 -47.52169 1.000 20.17691  ? 1362 LYS   B O    1 
ATOM   2272 C  CB   . LYS   A 1 310 ? 10.34116  -23.76433 -47.38798 1.000 33.03682  ? 1362 LYS   B CB   1 
ATOM   2273 C  CG   . LYS   A 1 310 ? 11.69519  -24.38619 -47.69114 1.000 39.40625  ? 1362 LYS   B CG   1 
ATOM   2274 C  CD   . LYS   A 1 310 ? 11.65415  -25.23915 -48.95717 1.000 55.05469  ? 1362 LYS   B CD   1 
ATOM   2275 C  CE   . LYS   A 1 310 ? 12.52628  -26.49607 -48.83330 1.000 54.50720  ? 1362 LYS   B CE   1 
ATOM   2276 N  NZ   . LYS   A 1 310 ? 13.89631  -26.22195 -48.29543 1.000 55.59206  ? 1362 LYS   B NZ   1 
ATOM   2277 N  N    . ASP   A 1 311 ? 8.64515   -21.50158 -45.31172 1.000 19.26801  ? 1363 ASP   B N    1 
ATOM   2278 C  CA   . ASP   A 1 311 ? 7.32413   -20.94672 -45.03857 1.000 22.04919  ? 1363 ASP   B CA   1 
ATOM   2279 C  C    . ASP   A 1 311 ? 6.22217   -21.89381 -45.50649 1.000 20.34117  ? 1363 ASP   B C    1 
ATOM   2280 O  O    . ASP   A 1 311 ? 5.17508   -21.46789 -45.98937 1.000 23.03351  ? 1363 ASP   B O    1 
ATOM   2281 C  CB   . ASP   A 1 311 ? 7.16293   -19.56471 -45.67650 1.000 20.26842  ? 1363 ASP   B CB   1 
ATOM   2282 C  CG   . ASP   A 1 311 ? 8.12089   -18.53864 -45.09056 1.000 29.47742  ? 1363 ASP   B CG   1 
ATOM   2283 O  OD1  . ASP   A 1 311 ? 8.09299   -18.32168 -43.85355 1.000 24.77049  ? 1363 ASP   B OD1  1 
ATOM   2284 O  OD2  . ASP   A 1 311 ? 8.91075   -17.96153 -45.86862 1.000 34.45050  ? 1363 ASP   B OD2  1 
ATOM   2285 N  N    . CYS   A 1 312 ? 6.46232   -23.19679 -45.36156 1.000 23.74526  ? 1364 CYS   B N    1 
ATOM   2286 C  CA   . CYS   A 1 312 ? 5.41139   -24.19089 -45.54449 1.000 24.20872  ? 1364 CYS   B CA   1 
ATOM   2287 C  C    . CYS   A 1 312 ? 4.61855   -24.43801 -44.27542 1.000 22.71631  ? 1364 CYS   B C    1 
ATOM   2288 O  O    . CYS   A 1 312 ? 3.43557   -24.78512 -44.35631 1.000 26.77533  ? 1364 CYS   B O    1 
ATOM   2289 C  CB   . CYS   A 1 312 ? 6.00348   -25.51781 -46.02160 1.000 29.90343  ? 1364 CYS   B CB   1 
ATOM   2290 S  SG   . CYS   A 1 312 ? 6.66730   -25.45668 -47.68866 1.000 51.68602  ? 1364 CYS   B SG   1 
ATOM   2291 N  N    . TYR   A 1 313 ? 5.24365   -24.25999 -43.10648 1.000 27.17632  ? 1365 TYR   B N    1 
ATOM   2292 C  CA   . TYR   A 1 313 ? 4.66282   -24.65009 -41.83243 1.000 25.53604  ? 1365 TYR   B CA   1 
ATOM   2293 C  C    . TYR   A 1 313 ? 4.76181   -23.51412 -40.83340 1.000 23.70955  ? 1365 TYR   B C    1 
ATOM   2294 O  O    . TYR   A 1 313 ? 5.72374   -22.74202 -40.83247 1.000 21.93063  ? 1365 TYR   B O    1 
ATOM   2295 C  CB   . TYR   A 1 313 ? 5.35400   -25.88705 -41.23155 1.000 19.92204  ? 1365 TYR   B CB   1 
ATOM   2296 C  CG   . TYR   A 1 313 ? 5.20904   -27.12403 -42.08158 1.000 29.47268  ? 1365 TYR   B CG   1 
ATOM   2297 C  CD1  . TYR   A 1 313 ? 3.95507   -27.67414 -42.32747 1.000 28.85024  ? 1365 TYR   B CD1  1 
ATOM   2298 C  CD2  . TYR   A 1 313 ? 6.31904   -27.73990 -42.64871 1.000 34.13262  ? 1365 TYR   B CD2  1 
ATOM   2299 C  CE1  . TYR   A 1 313 ? 3.81110   -28.80713 -43.11649 1.000 28.93728  ? 1365 TYR   B CE1  1 
ATOM   2300 C  CE2  . TYR   A 1 313 ? 6.18207   -28.87889 -43.44474 1.000 35.96307  ? 1365 TYR   B CE2  1 
ATOM   2301 C  CZ   . TYR   A 1 313 ? 4.92310   -29.40100 -43.67163 1.000 33.56305  ? 1365 TYR   B CZ   1 
ATOM   2302 O  OH   . TYR   A 1 313 ? 4.77213   -30.52399 -44.45565 1.000 38.20698  ? 1365 TYR   B OH   1 
ATOM   2303 N  N    . LEU   A 1 314 ? 3.75289   -23.43925 -39.97829 1.000 18.07813  ? 1366 LEU   B N    1 
ATOM   2304 C  CA   . LEU   A 1 314 ? 3.73793   -22.56529 -38.82026 1.000 19.58504  ? 1366 LEU   B CA   1 
ATOM   2305 C  C    . LEU   A 1 314 ? 3.62114   -23.43935 -37.57928 1.000 19.93843  ? 1366 LEU   B C    1 
ATOM   2306 O  O    . LEU   A 1 314 ? 2.74423   -24.30644 -37.51522 1.000 18.23255  ? 1366 LEU   B O    1 
ATOM   2307 C  CB   . LEU   A 1 314 ? 2.57182   -21.58340 -38.91310 1.000 23.88962  ? 1366 LEU   B CB   1 
ATOM   2308 C  CG   . LEU   A 1 314 ? 2.33084   -20.59247 -37.78104 1.000 21.96352  ? 1366 LEU   B CG   1 
ATOM   2309 C  CD1  . LEU   A 1 314 ? 3.51576   -19.65636 -37.66813 1.000 26.26321  ? 1366 LEU   B CD1  1 
ATOM   2310 C  CD2  . LEU   A 1 314 ? 1.04474   -19.81358 -38.03988 1.000 21.61146  ? 1366 LEU   B CD2  1 
ATOM   2311 N  N    . ALA   A 1 315 ? 4.51522   -23.24230 -36.61436 1.000 13.27004  ? 1367 ALA   B N    1 
ATOM   2312 C  CA   . ALA   A 1 315 ? 4.41742   -23.91135 -35.32138 1.000 14.65116  ? 1367 ALA   B CA   1 
ATOM   2313 C  C    . ALA   A 1 315 ? 3.99642   -22.89243 -34.27530 1.000 15.55504  ? 1367 ALA   B C    1 
ATOM   2314 O  O    . ALA   A 1 315 ? 4.54732   -21.78738 -34.22231 1.000 13.53362  ? 1367 ALA   B O    1 
ATOM   2315 C  CB   . ALA   A 1 315 ? 5.73952   -24.56424 -34.91854 1.000 14.09028  ? 1367 ALA   B CB   1 
ATOM   2316 N  N    . VAL   A 1 316 ? 3.04255   -23.27456 -33.43321 1.000 12.99049  ? 1368 VAL   B N    1 
ATOM   2317 C  CA   . VAL   A 1 316 ? 2.45556   -22.38165 -32.44012 1.000 10.13451  ? 1368 VAL   B CA   1 
ATOM   2318 C  C    . VAL   A 1 316 ? 2.37977   -23.12870 -31.11114 1.000 13.00323  ? 1368 VAL   B C    1 
ATOM   2319 O  O    . VAL   A 1 316 ? 1.89289   -24.26275 -31.05413 1.000 9.94068   ? 1368 VAL   B O    1 
ATOM   2320 C  CB   . VAL   A 1 316 ? 1.06347   -21.89177 -32.88596 1.000 14.99579  ? 1368 VAL   B CB   1 
ATOM   2321 C  CG1  . VAL   A 1 316 ? 0.49347   -20.88786 -31.88987 1.000 11.30513  ? 1368 VAL   B CG1  1 
ATOM   2322 C  CG2  . VAL   A 1 316 ? 1.12526   -21.29871 -34.31395 1.000 15.03632  ? 1368 VAL   B CG2  1 
ATOM   2323 N  N    . ILE   A 1 317 ? 2.91182   -22.52469 -30.05817 1.000 16.57152  ? 1369 ILE   B N    1 
ATOM   2324 C  CA   . ILE   A 1 317 ? 2.76301   -23.05675 -28.70618 1.000 13.04711  ? 1369 ILE   B CA   1 
ATOM   2325 C  C    . ILE   A 1 317 ? 1.47201   -22.47890 -28.13502 1.000 18.04353  ? 1369 ILE   B C    1 
ATOM   2326 O  O    . ILE   A 1 317 ? 1.36992   -21.26392 -27.91797 1.000 15.15224  ? 1369 ILE   B O    1 
ATOM   2327 C  CB   . ILE   A 1 317 ? 3.95607   -22.71567 -27.81029 1.000 9.91819   ? 1369 ILE   B CB   1 
ATOM   2328 C  CG1  . ILE   A 1 317 ? 5.25507   -23.27752 -28.38844 1.000 15.02479  ? 1369 ILE   B CG1  1 
ATOM   2329 C  CG2  . ILE   A 1 317 ? 3.71627   -23.25175 -26.37828 1.000 11.48302  ? 1369 ILE   B CG2  1 
ATOM   2330 C  CD1  . ILE   A 1 317 ? 5.17118   -24.78152 -28.68149 1.000 16.55756  ? 1369 ILE   B CD1  1 
ATOM   2331 N  N    . GLU   A 1 318 ? 0.49513   -23.35301 -27.88495 1.000 11.57773  ? 1370 GLU   B N    1 
ATOM   2332 C  CA   . GLU   A 1 318 ? -0.82686  -22.96915 -27.41981 1.000 13.08138  ? 1370 GLU   B CA   1 
ATOM   2333 C  C    . GLU   A 1 318 ? -1.09367  -23.55823 -26.04280 1.000 16.64656  ? 1370 GLU   B C    1 
ATOM   2334 O  O    . GLU   A 1 318 ? -0.83652  -24.74221 -25.79587 1.000 15.37131  ? 1370 GLU   B O    1 
ATOM   2335 C  CB   . GLU   A 1 318 ? -1.89492  -23.42722 -28.40671 1.000 18.92296  ? 1370 GLU   B CB   1 
ATOM   2336 C  CG   . GLU   A 1 318 ? -1.65912  -22.87415 -29.80872 1.000 19.94122  ? 1370 GLU   B CG   1 
ATOM   2337 C  CD   . GLU   A 1 318 ? -2.70918  -23.32822 -30.80562 1.000 31.57841  ? 1370 GLU   B CD   1 
ATOM   2338 O  OE1  . GLU   A 1 318 ? -3.71307  -23.94033 -30.37754 1.000 25.50565  ? 1370 GLU   B OE1  1 
ATOM   2339 O  OE2  . GLU   A 1 318 ? -2.51933  -23.07815 -32.01864 1.000 29.96950  ? 1370 GLU   B OE2  1 
ATOM   2340 N  N    . ASN   A 1 319 ? -1.60666  -22.72831 -25.15272 1.000 14.91677  ? 1371 ASN   B N    1 
ATOM   2341 C  CA   . ASN   A 1 319 ? -1.91848  -23.14439 -23.79970 1.000 20.24391  ? 1371 ASN   B CA   1 
ATOM   2342 C  C    . ASN   A 1 319 ? -3.35942  -23.63553 -23.77557 1.000 22.47695  ? 1371 ASN   B C    1 
ATOM   2343 O  O    . ASN   A 1 319 ? -4.27354  -22.89161 -24.14445 1.000 27.39211  ? 1371 ASN   B O    1 
ATOM   2344 C  CB   . ASN   A 1 319 ? -1.70349  -21.96640 -22.85068 1.000 20.11474  ? 1371 ASN   B CB   1 
ATOM   2345 C  CG   . ASN   A 1 319 ? -1.94731  -22.31848 -21.39867 1.000 29.31837  ? 1371 ASN   B CG   1 
ATOM   2346 O  OD1  . ASN   A 1 319 ? -1.78215  -23.46648 -20.97273 1.000 25.20335  ? 1371 ASN   B OD1  1 
ATOM   2347 N  ND2  . ASN   A 1 319 ? -2.34433  -21.31755 -20.62459 1.000 28.88016  ? 1371 ASN   B ND2  1 
ATOM   2348 N  N    . GLN   A 1 320 ? -3.57126  -24.88857 -23.37159 1.000 14.82605  ? 1372 GLN   B N    1 
ATOM   2349 C  CA   . GLN   A 1 320 ? -4.94820  -25.32671 -23.16547 1.000 29.44471  ? 1372 GLN   B CA   1 
ATOM   2350 C  C    . GLN   A 1 320 ? -5.41706  -25.15881 -21.72141 1.000 29.71904  ? 1372 GLN   B C    1 
ATOM   2351 O  O    . GLN   A 1 320 ? -6.60802  -25.35494 -21.44530 1.000 29.93674  ? 1372 GLN   B O    1 
ATOM   2352 C  CB   . GLN   A 1 320 ? -5.14810  -26.77871 -23.63250 1.000 20.41964  ? 1372 GLN   B CB   1 
ATOM   2353 C  CG   . GLN   A 1 320 ? -4.06697  -27.76462 -23.29365 1.000 22.18008  ? 1372 GLN   B CG   1 
ATOM   2354 C  CD   . GLN   A 1 320 ? -4.43887  -29.20864 -23.66266 1.000 30.67360  ? 1372 GLN   B CD   1 
ATOM   2355 O  OE1  . GLN   A 1 320 ? -3.97471  -30.15862 -23.02974 1.000 23.25782  ? 1372 GLN   B OE1  1 
ATOM   2356 N  NE2  . GLN   A 1 320 ? -5.27496  -29.37369 -24.68758 1.000 18.31799  ? 1372 GLN   B NE2  1 
ATOM   2357 N  N    . GLY   A 1 321 ? -4.52601  -24.75976 -20.80749 1.000 31.19374  ? 1373 GLY   B N    1 
ATOM   2358 C  CA   . GLY   A 1 321 ? -4.87989  -24.49984 -19.42344 1.000 33.90792  ? 1373 GLY   B CA   1 
ATOM   2359 C  C    . GLY   A 1 321 ? -6.17895  -23.73397 -19.23128 1.000 37.56083  ? 1373 GLY   B C    1 
ATOM   2360 O  O    . GLY   A 1 321 ? -6.45712  -22.75098 -19.93222 1.000 31.26748  ? 1373 GLY   B O    1 
ATOM   2361 N  N    . SER   A 1 322 ? -6.97980  -24.18209 -18.25822 1.000 28.28126  ? 1374 SER   B N    1 
ATOM   2362 C  CA   . SER   A 1 322 ? -8.29384  -23.58722 -18.04406 1.000 33.92294  ? 1374 SER   B CA   1 
ATOM   2363 C  C    . SER   A 1 322 ? -8.20492  -22.18324 -17.44202 1.000 36.39305  ? 1374 SER   B C    1 
ATOM   2364 O  O    . SER   A 1 322 ? -9.08702  -21.34832 -17.69290 1.000 35.06912  ? 1374 SER   B O    1 
ATOM   2365 C  CB   . SER   A 1 322 ? -9.13466  -24.51434 -17.16401 1.000 28.68046  ? 1374 SER   B CB   1 
ATOM   2366 O  OG   . SER   A 1 322 ? -8.37850  -25.02030 -16.07410 1.000 29.64136  ? 1374 SER   B OG   1 
ATOM   2367 N  N    . MET   A 1 323 ? -7.15887  -21.89716 -16.66412 1.000 35.99050  ? 1375 MET   B N    1 
ATOM   2368 C  CA   . MET   A 1 323 ? -6.92594  -20.57616 -16.08509 1.000 37.04536  ? 1375 MET   B CA   1 
ATOM   2369 C  C    . MET   A 1 323 ? -5.65005  -19.94402 -16.63920 1.000 37.93947  ? 1375 MET   B C    1 
ATOM   2370 O  O    . MET   A 1 323 ? -4.87904  -19.30697 -15.91426 1.000 39.05092  ? 1375 MET   B O    1 
ATOM   2371 C  CB   . MET   A 1 323 ? -6.87277  -20.64621 -14.55810 1.000 29.20916  ? 1375 MET   B CB   1 
ATOM   2372 C  CG   . MET   A 1 323 ? -8.24269  -20.74037 -13.89196 1.000 37.32598  ? 1375 MET   B CG   1 
ATOM   2373 S  SD   . MET   A 1 323 ? -9.09884  -19.17146 -13.81282 1.000 43.39752  ? 1375 MET   B SD   1 
ATOM   2374 C  CE   . MET   A 1 323 ? -7.86885  -18.18437 -12.93591 1.000 36.12770  ? 1375 MET   B CE   1 
ATOM   2375 N  N    . ASP   A 1 324 ? -5.42217  -20.11295 -17.93623 1.000 37.61447  ? 1376 ASP   B N    1 
ATOM   2376 C  CA   . ASP   A 1 324 ? -4.27630  -19.51581 -18.64833 1.000 40.66990  ? 1376 ASP   B CA   1 
ATOM   2377 C  C    . ASP   A 1 324 ? -2.99018  -20.12970 -18.07748 1.000 36.89547  ? 1376 ASP   B C    1 
ATOM   2378 O  O    . ASP   A 1 324 ? -2.95704  -21.33971 -17.79453 1.000 32.48590  ? 1376 ASP   B O    1 
ATOM   2379 C  CB   . ASP   A 1 324 ? -4.35044  -17.99782 -18.57126 1.000 32.21313  ? 1376 ASP   B CB   1 
ATOM   2380 C  CG   . ASP   A 1 324 ? -3.53762  -17.31470 -19.67332 1.000 48.85120  ? 1376 ASP   B CG   1 
ATOM   2381 O  OD1  . ASP   A 1 324 ? -3.08365  -18.01462 -20.61939 1.000 36.09206  ? 1376 ASP   B OD1  1 
ATOM   2382 O  OD2  . ASP   A 1 324 ? -3.37074  -16.07369 -19.60829 1.000 46.89092  ? 1376 ASP   B OD2  1 
ATOM   2383 N  N    . ALA   A 1 325 ? -1.91325  -19.34560 -17.93356 1.000 35.99717  ? 1377 ALA   B N    1 
ATOM   2384 C  CA   . ALA   A 1 325 ? -0.62815  -19.82250 -17.42471 1.000 41.78883  ? 1377 ALA   B CA   1 
ATOM   2385 C  C    . ALA   A 1 325 ? -0.63996  -20.11255 -15.92472 1.000 42.43912  ? 1377 ALA   B C    1 
ATOM   2386 O  O    . ALA   A 1 325 ? 0.39513   -20.53447 -15.39084 1.000 38.80931  ? 1377 ALA   B O    1 
ATOM   2387 C  CB   . ALA   A 1 325 ? 0.47572   -18.80638 -17.74179 1.000 37.29790  ? 1377 ALA   B CB   1 
ATOM   2388 N  N    . LEU   A 1 326 ? -1.76092  -19.88169 -15.23060 1.000 39.33309  ? 1378 LEU   B N    1 
ATOM   2389 C  CA   . LEU   A 1 326 ? -1.87173  -20.32075 -13.84460 1.000 35.12926  ? 1378 LEU   B CA   1 
ATOM   2390 C  C    . LEU   A 1 326 ? -1.57257  -21.81372 -13.74869 1.000 42.65315  ? 1378 LEU   B C    1 
ATOM   2391 O  O    . LEU   A 1 326 ? -0.59147  -22.23065 -13.11480 1.000 37.83985  ? 1378 LEU   B O    1 
ATOM   2392 C  CB   . LEU   A 1 326 ? -3.26771  -19.99790 -13.30545 1.000 35.80535  ? 1378 LEU   B CB   1 
ATOM   2393 C  CG   . LEU   A 1 326 ? -3.49253  -20.17898 -11.79643 1.000 43.03514  ? 1378 LEU   B CG   1 
ATOM   2394 C  CD1  . LEU   A 1 326 ? -4.71056  -19.38412 -11.32228 1.000 32.16852  ? 1378 LEU   B CD1  1 
ATOM   2395 C  CD2  . LEU   A 1 326 ? -3.61235  -21.65101 -11.40147 1.000 38.62534  ? 1378 LEU   B CD2  1 
ATOM   2396 N  N    . ASN   A 1 327 ? -2.41256  -22.63378 -14.39463 1.000 29.41287  ? 1379 ASN   B N    1 
ATOM   2397 C  CA   . ASN   A 1 327 ? -2.15244  -24.06375 -14.57271 1.000 37.93294  ? 1379 ASN   B CA   1 
ATOM   2398 C  C    . ASN   A 1 327 ? -1.69656  -24.31365 -16.00976 1.000 37.12625  ? 1379 ASN   B C    1 
ATOM   2399 O  O    . ASN   A 1 327 ? -2.42360  -24.83769 -16.85371 1.000 35.66358  ? 1379 ASN   B O    1 
ATOM   2400 C  CB   . ASN   A 1 327 ? -3.39132  -24.88188 -14.22261 1.000 25.80178  ? 1379 ASN   B CB   1 
ATOM   2401 C  CG   . ASN   A 1 327 ? -4.59545  -24.52897 -15.09047 1.000 32.04906  ? 1379 ASN   B CG   1 
ATOM   2402 O  OD1  . ASN   A 1 327 ? -4.72461  -23.40396 -15.58642 1.000 27.42862  ? 1379 ASN   B OD1  1 
ATOM   2403 N  ND2  . ASN   A 1 327 ? -5.49137  -25.49905 -15.27142 1.000 36.58053  ? 1379 ASN   B ND2  1 
ATOM   2404 N  N    . MET   A 1 328 ? -0.45563  -23.91952 -16.27088 1.000 36.36506  ? 1380 MET   B N    1 
ATOM   2405 C  CA   . MET   A 1 328 ? 0.07924   -23.98342 -17.62093 1.000 35.23178  ? 1380 MET   B CA   1 
ATOM   2406 C  C    . MET   A 1 328 ? 0.04833   -25.41440 -18.15798 1.000 26.15639  ? 1380 MET   B C    1 
ATOM   2407 O  O    . MET   A 1 328 ? 0.48249   -26.35338 -17.48506 1.000 22.05225  ? 1380 MET   B O    1 
ATOM   2408 C  CB   . MET   A 1 328 ? 1.50319   -23.43628 -17.62506 1.000 32.94627  ? 1380 MET   B CB   1 
ATOM   2409 C  CG   . MET   A 1 328 ? 2.11003   -23.30917 -18.99212 1.000 25.46031  ? 1380 MET   B CG   1 
ATOM   2410 S  SD   . MET   A 1 328 ? 3.83701   -22.85101 -18.83728 1.000 29.06824  ? 1380 MET   B SD   1 
ATOM   2411 C  CE   . MET   A 1 328 ? 4.41788   -23.30389 -20.46436 1.000 17.52077  ? 1380 MET   B CE   1 
ATOM   2412 N  N    . ASP   A 1 329 ? -0.46778  -25.57441 -19.38194 1.000 19.66449  ? 1381 ASP   B N    1 
ATOM   2413 C  CA   . ASP   A 1 329 ? -0.53872  -26.89139 -20.02798 1.000 18.89486  ? 1381 ASP   B CA   1 
ATOM   2414 C  C    . ASP   A 1 329 ? -0.55690  -26.65034 -21.53997 1.000 19.04743  ? 1381 ASP   B C    1 
ATOM   2415 O  O    . ASP   A 1 329 ? -1.62198  -26.51542 -22.14885 1.000 17.32489  ? 1381 ASP   B O    1 
ATOM   2416 C  CB   . ASP   A 1 329 ? -1.76160  -27.67053 -19.56288 1.000 22.17638  ? 1381 ASP   B CB   1 
ATOM   2417 C  CG   . ASP   A 1 329 ? -1.72249  -29.13651 -19.96994 1.000 24.65464  ? 1381 ASP   B CG   1 
ATOM   2418 O  OD1  . ASP   A 1 329 ? -0.63943  -29.76341 -19.89407 1.000 24.20891  ? 1381 ASP   B OD1  1 
ATOM   2419 O  OD2  . ASP   A 1 329 ? -2.78848  -29.65760 -20.35685 1.000 27.54843  ? 1381 ASP   B OD2  1 
ATOM   2420 N  N    . THR   A 1 330 ? 0.63003   -26.59720 -22.13009 1.000 13.41616  ? 1382 THR   B N    1 
ATOM   2421 C  CA   . THR   A 1 330 ? 0.78785   -26.16014 -23.50309 1.000 13.60139  ? 1382 THR   B CA   1 
ATOM   2422 C  C    . THR   A 1 330 ? 0.93987   -27.35109 -24.43515 1.000 14.39117  ? 1382 THR   B C    1 
ATOM   2423 O  O    . THR   A 1 330 ? 1.47701   -28.40005 -24.06624 1.000 16.05003  ? 1382 THR   B O    1 
ATOM   2424 C  CB   . THR   A 1 330 ? 2.00674   -25.24501 -23.66118 1.000 14.32549  ? 1382 THR   B CB   1 
ATOM   2425 O  OG1  . THR   A 1 330 ? 3.17386   -25.92991 -23.18132 1.000 14.42808  ? 1382 THR   B OG1  1 
ATOM   2426 C  CG2  . THR   A 1 330 ? 1.80969   -23.91706 -22.90811 1.000 12.27533  ? 1382 THR   B CG2  1 
ATOM   2427 N  N    . VAL   A 1 331 ? 0.47273   -27.16309 -25.66309 1.000 12.21794  ? 1383 VAL   B N    1 
ATOM   2428 C  CA   . VAL   A 1 331 ? 0.74070   -28.06802 -26.76215 1.000 16.47251  ? 1383 VAL   B CA   1 
ATOM   2429 C  C    . VAL   A 1 331 ? 1.36451   -27.25592 -27.88419 1.000 17.46586  ? 1383 VAL   B C    1 
ATOM   2430 O  O    . VAL   A 1 331 ? 1.20138   -26.03493 -27.96912 1.000 19.79815  ? 1383 VAL   B O    1 
ATOM   2431 C  CB   . VAL   A 1 331 ? -0.53728  -28.77113 -27.25704 1.000 20.89523  ? 1383 VAL   B CB   1 
ATOM   2432 C  CG1  . VAL   A 1 331 ? -1.20609  -29.50924 -26.10100 1.000 13.95113  ? 1383 VAL   B CG1  1 
ATOM   2433 C  CG2  . VAL   A 1 331 ? -1.49544  -27.73420 -27.88091 1.000 14.88817  ? 1383 VAL   B CG2  1 
ATOM   2434 N  N    . CYS   A 1 332 ? 2.07849   -27.95482 -28.75128 1.000 11.33004  ? 1384 CYS   B N    1 
ATOM   2435 C  CA   . CYS   A 1 332 ? 2.56130   -27.39273 -29.99931 1.000 11.65747  ? 1384 CYS   B CA   1 
ATOM   2436 C  C    . CYS   A 1 332 ? 1.64323   -27.85478 -31.12024 1.000 17.93895  ? 1384 CYS   B C    1 
ATOM   2437 O  O    . CYS   A 1 332 ? 1.35734   -29.05080 -31.24825 1.000 18.72485  ? 1384 CYS   B O    1 
ATOM   2438 C  CB   . CYS   A 1 332 ? 4.00432   -27.81158 -30.27948 1.000 13.44292  ? 1384 CYS   B CB   1 
ATOM   2439 S  SG   . CYS   A 1 332 ? 4.56010   -27.31046 -31.91452 1.000 16.04029  ? 1384 CYS   B SG   1 
ATOM   2440 N  N    . ARG   A 1 333 ? 1.15506   -26.90280 -31.90015 1.000 15.12115  ? 1385 ARG   B N    1 
ATOM   2441 C  CA   . ARG   A 1 333 ? 0.36597   -27.17683 -33.08508 1.000 14.28122  ? 1385 ARG   B CA   1 
ATOM   2442 C  C    . ARG   A 1 333 ? 1.15680   -26.77871 -34.32015 1.000 17.20565  ? 1385 ARG   B C    1 
ATOM   2443 O  O    . ARG   A 1 333 ? 1.76869   -25.70165 -34.35817 1.000 12.83399  ? 1385 ARG   B O    1 
ATOM   2444 C  CB   . ARG   A 1 333 ? -0.96310  -26.42196 -33.03692 1.000 19.76043  ? 1385 ARG   B CB   1 
ATOM   2445 C  CG   . ARG   A 1 333 ? -2.10197  -27.31209 -32.60583 1.000 21.74933  ? 1385 ARG   B CG   1 
ATOM   2446 C  CD   . ARG   A 1 333 ? -3.30501  -26.51322 -32.19668 1.000 26.92512  ? 1385 ARG   B CD   1 
ATOM   2447 N  NE   . ARG   A 1 333 ? -3.94283  -27.12033 -31.03564 1.000 41.47950  ? 1385 ARG   B NE   1 
ATOM   2448 C  CZ   . ARG   A 1 333 ? -4.91975  -28.01042 -31.12457 1.000 39.44559  ? 1385 ARG   B CZ   1 
ATOM   2449 N  NH1  . ARG   A 1 333 ? -5.37683  -28.40342 -32.30053 1.000 26.42417  ? 1385 ARG   B NH1  1 
ATOM   2450 N  NH2  . ARG   A 1 333 ? -5.45459  -28.50851 -30.00853 1.000 26.86376  ? 1385 ARG   B NH2  1 
ATOM   2451 N  N    . LEU   A 1 334 ? 1.15779   -27.66267 -35.30718 1.000 14.16961  ? 1386 LEU   B N    1 
ATOM   2452 C  CA   . LEU   A 1 334 ? 1.78763   -27.42156 -36.59723 1.000 17.21786  ? 1386 LEU   B CA   1 
ATOM   2453 C  C    . LEU   A 1 334 ? 0.68350   -27.13964 -37.60211 1.000 19.83816  ? 1386 LEU   B C    1 
ATOM   2454 O  O    . LEU   A 1 334 ? -0.25244  -27.93672 -37.73504 1.000 19.21881  ? 1386 LEU   B O    1 
ATOM   2455 C  CB   . LEU   A 1 334 ? 2.62170   -28.62947 -37.02836 1.000 14.31495  ? 1386 LEU   B CB   1 
ATOM   2456 C  CG   . LEU   A 1 334 ? 3.52357   -28.51133 -38.26045 1.000 23.11228  ? 1386 LEU   B CG   1 
ATOM   2457 C  CD1  . LEU   A 1 334 ? 4.75051   -27.64422 -37.97555 1.000 20.95696  ? 1386 LEU   B CD1  1 
ATOM   2458 C  CD2  . LEU   A 1 334 ? 3.93966   -29.89928 -38.70955 1.000 20.84554  ? 1386 LEU   B CD2  1 
ATOM   2459 N  N    . TYR   A 1 335 ? 0.77032   -25.99860 -38.27208 1.000 16.35740  ? 1387 TYR   B N    1 
ATOM   2460 C  CA   . TYR   A 1 335 ? -0.20882  -25.60466 -39.26896 1.000 22.72790  ? 1387 TYR   B CA   1 
ATOM   2461 C  C    . TYR   A 1 335 ? 0.45503   -25.52055 -40.63003 1.000 23.48256  ? 1387 TYR   B C    1 
ATOM   2462 O  O    . TYR   A 1 335 ? 1.62298   -25.13443 -40.75314 1.000 19.92565  ? 1387 TYR   B O    1 
ATOM   2463 C  CB   . TYR   A 1 335 ? -0.84492  -24.25074 -38.95785 1.000 19.74765  ? 1387 TYR   B CB   1 
ATOM   2464 C  CG   . TYR   A 1 335 ? -1.63180  -24.20486 -37.68277 1.000 21.93482  ? 1387 TYR   B CG   1 
ATOM   2465 C  CD1  . TYR   A 1 335 ? -2.96675  -24.59799 -37.64764 1.000 17.71401  ? 1387 TYR   B CD1  1 
ATOM   2466 C  CD2  . TYR   A 1 335 ? -1.03972  -23.76084 -36.50681 1.000 16.63081  ? 1387 TYR   B CD2  1 
ATOM   2467 C  CE1  . TYR   A 1 335 ? -3.68964  -24.55211 -36.46257 1.000 20.54114  ? 1387 TYR   B CE1  1 
ATOM   2468 C  CE2  . TYR   A 1 335 ? -1.74460  -23.70296 -35.33274 1.000 20.46078  ? 1387 TYR   B CE2  1 
ATOM   2469 C  CZ   . TYR   A 1 335 ? -3.06656  -24.09909 -35.30362 1.000 24.60333  ? 1387 TYR   B CZ   1 
ATOM   2470 O  OH   . TYR   A 1 335 ? -3.74845  -24.03520 -34.10954 1.000 19.69645  ? 1387 TYR   B OH   1 
ATOM   2471 N  N    . GLU   A 1 336 ? -0.31304  -25.86159 -41.65196 1.000 22.91856  ? 1388 GLU   B N    1 
ATOM   2472 C  CA   . GLU   A 1 336 ? 0.13880   -25.70049 -43.02400 1.000 27.86001  ? 1388 GLU   B CA   1 
ATOM   2473 C  C    . GLU   A 1 336 ? -0.11438  -24.26850 -43.46593 1.000 28.89822  ? 1388 GLU   B C    1 
ATOM   2474 O  O    . GLU   A 1 336 ? -1.24242  -23.77362 -43.36179 1.000 29.72391  ? 1388 GLU   B O    1 
ATOM   2475 C  CB   . GLU   A 1 336 ? -0.58920  -26.67953 -43.92696 1.000 32.45273  ? 1388 GLU   B CB   1 
ATOM   2476 C  CG   . GLU   A 1 336 ? -0.09034  -26.69243 -45.33402 1.000 40.62568  ? 1388 GLU   B CG   1 
ATOM   2477 C  CD   . GLU   A 1 336 ? -0.72731  -27.81147 -46.11199 1.000 50.24803  ? 1388 GLU   B CD   1 
ATOM   2478 O  OE1  . GLU   A 1 336 ? -1.94835  -27.71458 -46.37486 1.000 40.37631  ? 1388 GLU   B OE1  1 
ATOM   2479 O  OE2  . GLU   A 1 336 ? -0.01524  -28.79839 -46.41610 1.000 47.68213  ? 1388 GLU   B OE2  1 
ATOM   2480 N  N    . VAL   A 1 337 ? 0.93250   -23.59238 -43.92801 1.000 27.37794  ? 1389 VAL   B N    1 
ATOM   2481 C  CA   . VAL   A 1 337 ? 0.78232   -22.22238 -44.40594 1.000 33.19210  ? 1389 VAL   B CA   1 
ATOM   2482 C  C    . VAL   A 1 337 ? 0.25218   -22.28338 -45.83589 1.000 39.17830  ? 1389 VAL   B C    1 
ATOM   2483 O  O    . VAL   A 1 337 ? 0.96612   -22.68428 -46.75898 1.000 38.30185  ? 1389 VAL   B O    1 
ATOM   2484 C  CB   . VAL   A 1 337 ? 2.09625   -21.44025 -44.33205 1.000 31.79318  ? 1389 VAL   B CB   1 
ATOM   2485 C  CG1  . VAL   A 1 337 ? 1.92005   -20.08125 -44.98498 1.000 30.31143  ? 1389 VAL   B CG1  1 
ATOM   2486 C  CG2  . VAL   A 1 337 ? 2.54538   -21.28626 -42.88709 1.000 25.41873  ? 1389 VAL   B CG2  1 
ATOM   2487 N  N    . GLY   A 1 338 ? -1.01288  -21.91950 -46.01175 1.000 34.90489  ? 1390 GLY   B N    1 
ATOM   2488 C  CA   . GLY   A 1 338 ? -1.58503  -21.74251 -47.33168 1.000 49.31910  ? 1390 GLY   B CA   1 
ATOM   2489 C  C    . GLY   A 1 338 ? -1.50021  -20.28048 -47.72764 1.000 63.66193  ? 1390 GLY   B C    1 
ATOM   2490 O  O    . GLY   A 1 338 ? -2.44427  -19.51158 -47.52851 1.000 68.61225  ? 1390 GLY   B O    1 
ATOM   2491 O  OXT  . GLY   A 1 338 ? -0.47231  -19.82336 -48.23773 1.000 58.35521  ? 1390 GLY   B OXT  1 
ATOM   2492 N  N    . VAL   B 2 26  ? 4.74385   -43.07091 19.72619  1.000 37.81081  ? 31   VAL   A N    1 
ATOM   2493 C  CA   . VAL   B 2 26  ? 3.89174   -41.91895 19.98603  1.000 38.32507  ? 31   VAL   A CA   1 
ATOM   2494 C  C    . VAL   B 2 26  ? 3.79682   -41.03602 18.73697  1.000 46.81058  ? 31   VAL   A C    1 
ATOM   2495 O  O    . VAL   B 2 26  ? 4.81185   -40.63199 18.16706  1.000 40.64023  ? 31   VAL   A O    1 
ATOM   2496 C  CB   . VAL   B 2 26  ? 4.40356   -41.10385 21.19704  1.000 48.69149  ? 31   VAL   A CB   1 
ATOM   2497 C  CG1  . VAL   B 2 26  ? 5.72655   -40.39378 20.86514  1.000 35.62639  ? 31   VAL   A CG1  1 
ATOM   2498 C  CG2  . VAL   B 2 26  ? 3.34644   -40.11089 21.66487  1.000 38.76567  ? 31   VAL   A CG2  1 
ATOM   2499 N  N    . LYS   B 2 27  ? 2.57085   -40.75513 18.30482  1.000 33.26978  ? 32   LYS   A N    1 
ATOM   2500 C  CA   . LYS   B 2 27  ? 2.32790   -39.82321 17.21775  1.000 31.20633  ? 32   LYS   A CA   1 
ATOM   2501 C  C    . LYS   B 2 27  ? 1.43977   -38.68924 17.70359  1.000 27.62631  ? 32   LYS   A C    1 
ATOM   2502 O  O    . LYS   B 2 27  ? 0.62569   -38.88524 18.60951  1.000 27.71308  ? 32   LYS   A O    1 
ATOM   2503 C  CB   . LYS   B 2 27  ? 1.65407   -40.50432 16.01971  1.000 28.41301  ? 32   LYS   A CB   1 
ATOM   2504 C  CG   . LYS   B 2 27  ? 2.53822   -41.49230 15.28786  1.000 31.15143  ? 32   LYS   A CG   1 
ATOM   2505 C  CD   . LYS   B 2 27  ? 1.83139   -41.97942 14.03481  1.000 39.57416  ? 32   LYS   A CD   1 
ATOM   2506 C  CE   . LYS   B 2 27  ? 2.18351   -43.42241 13.72693  1.000 43.91148  ? 32   LYS   A CE   1 
ATOM   2507 N  NZ   . LYS   B 2 27  ? 0.95358   -44.25250 13.58484  1.000 53.79400  ? 32   LYS   A NZ   1 
ATOM   2508 N  N    . PRO   B 2 28  ? 1.57575   -37.49426 17.13453  1.000 24.98141  ? 33   PRO   A N    1 
ATOM   2509 C  CA   . PRO   B 2 28  ? 0.65265   -36.41030 17.47238  1.000 21.92409  ? 33   PRO   A CA   1 
ATOM   2510 C  C    . PRO   B 2 28  ? -0.69827  -36.64543 16.81824  1.000 17.64777  ? 33   PRO   A C    1 
ATOM   2511 O  O    . PRO   B 2 28  ? -0.87112  -37.52549 15.98227  1.000 15.43108  ? 33   PRO   A O    1 
ATOM   2512 C  CB   . PRO   B 2 28  ? 1.34962   -35.15629 16.92838  1.000 22.04243  ? 33   PRO   A CB   1 
ATOM   2513 C  CG   . PRO   B 2 28  ? 2.21178   -35.66229 15.81050  1.000 17.97080  ? 33   PRO   A CG   1 
ATOM   2514 C  CD   . PRO   B 2 28  ? 2.62383   -37.06624 16.18762  1.000 22.48905  ? 33   PRO   A CD   1 
ATOM   2515 N  N    . ASN   B 2 29  ? -1.67436  -35.83847 17.21209  1.000 20.65757  ? 34   ASN   A N    1 
ATOM   2516 C  CA   . ASN   B 2 29  ? -2.99929  -35.92159 16.61096  1.000 17.80313  ? 34   ASN   A CA   1 
ATOM   2517 C  C    . ASN   B 2 29  ? -3.51235  -34.52565 16.30682  1.000 18.50690  ? 34   ASN   A C    1 
ATOM   2518 O  O    . ASN   B 2 29  ? -4.62842  -34.16170 16.67868  1.000 17.61500  ? 34   ASN   A O    1 
ATOM   2519 C  CB   . ASN   B 2 29  ? -3.98534  -36.66461 17.51189  1.000 14.80062  ? 34   ASN   A CB   1 
ATOM   2520 C  CG   . ASN   B 2 29  ? -4.14253  -36.00654 18.87884  1.000 23.37591  ? 34   ASN   A CG   1 
ATOM   2521 O  OD1  . ASN   B 2 29  ? -3.54063  -34.96549 19.15584  1.000 28.91503  ? 34   ASN   A OD1  1 
ATOM   2522 N  ND2  . ASN   B 2 29  ? -4.94958  -36.60955 19.73578  1.000 22.55013  ? 34   ASN   A ND2  1 
ATOM   2523 N  N    . TYR   B 2 30  ? -2.69234  -33.70963 15.63987  1.000 15.31165  ? 35   TYR   A N    1 
ATOM   2524 C  CA   . TYR   B 2 30  ? -3.14938  -32.37168 15.27074  1.000 15.55774  ? 35   TYR   A CA   1 
ATOM   2525 C  C    . TYR   B 2 30  ? -4.46030  -32.46081 14.50261  1.000 16.84774  ? 35   TYR   A C    1 
ATOM   2526 O  O    . TYR   B 2 30  ? -4.61915  -33.30687 13.61864  1.000 14.23691  ? 35   TYR   A O    1 
ATOM   2527 C  CB   . TYR   B 2 30  ? -2.09234  -31.64066 14.44081  1.000 13.51905  ? 35   TYR   A CB   1 
ATOM   2528 C  CG   . TYR   B 2 30  ? -0.95147  -31.14453 15.29491  1.000 15.50067  ? 35   TYR   A CG   1 
ATOM   2529 C  CD1  . TYR   B 2 30  ? -1.03062  -29.91550 15.93083  1.000 11.97968  ? 35   TYR   A CD1  1 
ATOM   2530 C  CD2  . TYR   B 2 30  ? 0.18656   -31.92445 15.49807  1.000 12.95198  ? 35   TYR   A CD2  1 
ATOM   2531 C  CE1  . TYR   B 2 30  ? 0.00027   -29.45839 16.72392  1.000 14.41191  ? 35   TYR   A CE1  1 
ATOM   2532 C  CE2  . TYR   B 2 30  ? 1.22445   -31.47633 16.29416  1.000 11.21897  ? 35   TYR   A CE2  1 
ATOM   2533 C  CZ   . TYR   B 2 30  ? 1.12530   -30.24030 16.90608  1.000 15.61928  ? 35   TYR   A CZ   1 
ATOM   2534 O  OH   . TYR   B 2 30  ? 2.14518   -29.77819 17.71017  1.000 15.85770  ? 35   TYR   A OH   1 
ATOM   2535 N  N    . ALA   B 2 31  ? -5.40939  -31.60085 14.87746  1.000 15.42217  ? 36   ALA   A N    1 
ATOM   2536 C  CA   . ALA   B 2 31  ? -6.69433  -31.50097 14.20531  1.000 17.29305  ? 36   ALA   A CA   1 
ATOM   2537 C  C    . ALA   B 2 31  ? -7.02340  -30.03301 13.96920  1.000 15.57690  ? 36   ALA   A C    1 
ATOM   2538 O  O    . ALA   B 2 31  ? -6.59154  -29.14494 14.71119  1.000 15.42381  ? 36   ALA   A O    1 
ATOM   2539 C  CB   . ALA   B 2 31  ? -7.81937  -32.17000 15.01223  1.000 15.80173  ? 36   ALA   A CB   1 
ATOM   2540 N  N    . LEU   B 2 32  ? -7.79330  -29.79412 12.92210  1.000 11.69086  ? 37   LEU   A N    1 
ATOM   2541 C  CA   . LEU   B 2 32  ? -8.07235  -28.43916 12.48399  1.000 15.29061  ? 37   LEU   A CA   1 
ATOM   2542 C  C    . LEU   B 2 32  ? -9.00950  -27.74917 13.46985  1.000 18.33120  ? 37   LEU   A C    1 
ATOM   2543 O  O    . LEU   B 2 32  ? -10.05350 -28.29722 13.83077  1.000 15.18155  ? 37   LEU   A O    1 
ATOM   2544 C  CB   . LEU   B 2 32  ? -8.68519  -28.48328 11.08993  1.000 11.80617  ? 37   LEU   A CB   1 
ATOM   2545 C  CG   . LEU   B 2 32  ? -9.05822  -27.12934 10.51581  1.000 15.09711  ? 37   LEU   A CG   1 
ATOM   2546 C  CD1  . LEU   B 2 32  ? -7.79226  -26.33026 10.34291  1.000 13.46096  ? 37   LEU   A CD1  1 
ATOM   2547 C  CD2  . LEU   B 2 32  ? -9.81307  -27.31646 9.20074   1.000 7.48266   ? 37   LEU   A CD2  1 
ATOM   2548 N  N    . LYS   B 2 33  ? -8.62363  -26.56012 13.92883  1.000 12.53803  ? 38   LYS   A N    1 
ATOM   2549 C  CA   . LYS   B 2 33  ? -9.43078  -25.79512 14.87370  1.000 18.50811  ? 38   LYS   A CA   1 
ATOM   2550 C  C    . LYS   B 2 33  ? -10.01780 -24.53019 14.27157  1.000 17.24060  ? 38   LYS   A C    1 
ATOM   2551 O  O    . LYS   B 2 33  ? -11.19284 -24.23726 14.49542  1.000 10.98050  ? 38   LYS   A O    1 
ATOM   2552 C  CB   . LYS   B 2 33  ? -8.60794  -25.43199 16.11477  1.000 13.27575  ? 38   LYS   A CB   1 
ATOM   2553 C  CG   . LYS   B 2 33  ? -7.95593  -26.62891 16.79691  1.000 17.97311  ? 38   LYS   A CG   1 
ATOM   2554 C  CD   . LYS   B 2 33  ? -8.99494  -27.52794 17.46884  1.000 18.17103  ? 38   LYS   A CD   1 
ATOM   2555 C  CE   . LYS   B 2 33  ? -9.55912  -26.85091 18.71275  1.000 16.83408  ? 38   LYS   A CE   1 
ATOM   2556 N  NZ   . LYS   B 2 33  ? -10.67114 -27.61195 19.31867  1.000 26.16778  ? 38   LYS   A NZ   1 
ATOM   2557 N  N    . PHE   B 2 34  ? -9.23976  -23.78818 13.48861  1.000 16.36370  ? 39   PHE   A N    1 
ATOM   2558 C  CA   . PHE   B 2 34  ? -9.71977  -22.58525 12.83049  1.000 14.22935  ? 39   PHE   A CA   1 
ATOM   2559 C  C    . PHE   B 2 34  ? -9.06364  -22.44128 11.46755  1.000 12.20506  ? 39   PHE   A C    1 
ATOM   2560 O  O    . PHE   B 2 34  ? -7.94158  -22.89722 11.25270  1.000 13.05876  ? 39   PHE   A O    1 
ATOM   2561 C  CB   . PHE   B 2 34  ? -9.40794  -21.32618 13.64745  1.000 17.20051  ? 39   PHE   A CB   1 
ATOM   2562 C  CG   . PHE   B 2 34  ? -9.90609  -21.38014 15.04840  1.000 21.42011  ? 39   PHE   A CG   1 
ATOM   2563 C  CD1  . PHE   B 2 34  ? -11.20615 -20.99021 15.35024  1.000 17.28336  ? 39   PHE   A CD1  1 
ATOM   2564 C  CD2  . PHE   B 2 34  ? -9.07617  -21.80503 16.07552  1.000 19.59017  ? 39   PHE   A CD2  1 
ATOM   2565 C  CE1  . PHE   B 2 34  ? -11.66929 -21.02917 16.64619  1.000 20.52112  ? 39   PHE   A CE1  1 
ATOM   2566 C  CE2  . PHE   B 2 34  ? -9.53531  -21.84198 17.39047  1.000 22.99221  ? 39   PHE   A CE2  1 
ATOM   2567 C  CZ   . PHE   B 2 34  ? -10.83037 -21.44905 17.67131  1.000 19.66016  ? 39   PHE   A CZ   1 
ATOM   2568 N  N    . THR   B 2 35  ? -9.77458  -21.78238 10.56244  1.000 13.73407  ? 40   THR   A N    1 
ATOM   2569 C  CA   . THR   B 2 35  ? -9.26247  -21.35642 9.26747   1.000 10.29662  ? 40   THR   A CA   1 
ATOM   2570 C  C    . THR   B 2 35  ? -9.41756  -19.84543 9.20137   1.000 14.09489  ? 40   THR   A C    1 
ATOM   2571 O  O    . THR   B 2 35  ? -10.52762 -19.32950 9.37022   1.000 12.70369  ? 40   THR   A O    1 
ATOM   2572 C  CB   . THR   B 2 35  ? -10.01630 -22.04053 8.12143   1.000 10.73780  ? 40   THR   A CB   1 
ATOM   2573 O  OG1  . THR   B 2 35  ? -9.82722  -23.45852 8.21053   1.000 11.97395  ? 40   THR   A OG1  1 
ATOM   2574 C  CG2  . THR   B 2 35  ? -9.51319  -21.54158 6.75445   1.000 8.26817   ? 40   THR   A CG2  1 
ATOM   2575 N  N    . LEU   B 2 36  ? -8.30559  -19.14337 8.98145   1.000 9.66516   ? 41   LEU   A N    1 
ATOM   2576 C  CA   . LEU   B 2 36  ? -8.24069  -17.68337 9.01238   1.000 10.96101  ? 41   LEU   A CA   1 
ATOM   2577 C  C    . LEU   B 2 36  ? -8.25657  -17.15945 7.57934   1.000 19.78788  ? 41   LEU   A C    1 
ATOM   2578 O  O    . LEU   B 2 36  ? -7.27348  -17.30642 6.83946   1.000 17.36644  ? 41   LEU   A O    1 
ATOM   2579 C  CB   . LEU   B 2 36  ? -6.97980  -17.20624 9.73948   1.000 12.15996  ? 41   LEU   A CB   1 
ATOM   2580 C  CG   . LEU   B 2 36  ? -6.90896  -17.28515 11.27850  1.000 14.41665  ? 41   LEU   A CG   1 
ATOM   2581 C  CD1  . LEU   B 2 36  ? -7.56693  -18.55317 11.78950  1.000 11.73625  ? 41   LEU   A CD1  1 
ATOM   2582 C  CD2  . LEU   B 2 36  ? -5.45502  -17.19303 11.76365  1.000 13.51200  ? 41   LEU   A CD2  1 
ATOM   2583 N  N    . ALA   B 2 37  ? -9.35757  -16.52854 7.19419   1.000 11.53176  ? 42   ALA   A N    1 
ATOM   2584 C  CA   . ALA   B 2 37  ? -9.47447  -15.91262 5.89014   1.000 11.96519  ? 42   ALA   A CA   1 
ATOM   2585 C  C    . ALA   B 2 37  ? -9.40559  -14.40261 6.05907   1.000 10.67274  ? 42   ALA   A C    1 
ATOM   2586 O  O    . ALA   B 2 37  ? -9.75974  -13.86357 7.11100   1.000 11.26064  ? 42   ALA   A O    1 
ATOM   2587 C  CB   . ALA   B 2 37  ? -10.77337 -16.34475 5.20203   1.000 12.56390  ? 42   ALA   A CB   1 
ATOM   2588 N  N    . GLY   B 2 38  ? -8.91052  -13.72063 5.03108   1.000 11.72117  ? 43   GLY   A N    1 
ATOM   2589 C  CA   . GLY   B 2 38  ? -8.73163  -12.28561 5.14002   1.000 9.84927   ? 43   GLY   A CA   1 
ATOM   2590 C  C    . GLY   B 2 38  ? -7.71256  -11.71960 4.16910   1.000 15.67713  ? 43   GLY   A C    1 
ATOM   2591 O  O    . GLY   B 2 38  ? -7.95657  -10.65765 3.58701   1.000 14.07529  ? 43   GLY   A O    1 
ATOM   2592 N  N    . HIS   B 2 39  ? -6.56150  -12.37953 4.00426   1.000 11.55304  ? 44   HIS   A N    1 
ATOM   2593 C  CA   . HIS   B 2 39  ? -5.63442  -11.96353 2.95834   1.000 11.29080  ? 44   HIS   A CA   1 
ATOM   2594 C  C    . HIS   B 2 39  ? -6.26926  -12.16265 1.58428   1.000 10.73997  ? 44   HIS   A C    1 
ATOM   2595 O  O    . HIS   B 2 39  ? -7.02817  -13.11271 1.36525   1.000 12.59240  ? 44   HIS   A O    1 
ATOM   2596 C  CB   . HIS   B 2 39  ? -4.31938  -12.73444 3.06752   1.000 12.48483  ? 44   HIS   A CB   1 
ATOM   2597 C  CG   . HIS   B 2 39  ? -3.43753  -12.24532 4.17459   1.000 9.58021   ? 44   HIS   A CG   1 
ATOM   2598 N  ND1  . HIS   B 2 39  ? -2.87461  -10.98728 4.17158   1.000 9.52417   ? 44   HIS   A ND1  1 
ATOM   2599 C  CD2  . HIS   B 2 39  ? -3.05962  -12.82423 5.33666   1.000 9.69944   ? 44   HIS   A CD2  1 
ATOM   2600 C  CE1  . HIS   B 2 39  ? -2.16174  -10.82217 5.27165   1.000 14.57830  ? 44   HIS   A CE1  1 
ATOM   2601 N  NE2  . HIS   B 2 39  ? -2.25875  -11.92214 5.99870   1.000 11.80830  ? 44   HIS   A NE2  1 
ATOM   2602 N  N    . THR   B 2 40  ? -5.97922  -11.24768 0.65626   1.000 10.46792  ? 45   THR   A N    1 
ATOM   2603 C  CA   . THR   B 2 40  ? -6.55007  -11.34580 -0.68880  1.000 17.40734  ? 45   THR   A CA   1 
ATOM   2604 C  C    . THR   B 2 40  ? -5.56792  -11.89579 -1.72266  1.000 18.49776  ? 45   THR   A C    1 
ATOM   2605 O  O    . THR   B 2 40  ? -5.90779  -11.96688 -2.91269  1.000 11.40623  ? 45   THR   A O    1 
ATOM   2606 C  CB   . THR   B 2 40  ? -7.07811  -9.98486  -1.14793  1.000 16.07331  ? 45   THR   A CB   1 
ATOM   2607 O  OG1  . THR   B 2 40  ? -6.00017  -9.04479  -1.18187  1.000 10.79484  ? 45   THR   A OG1  1 
ATOM   2608 C  CG2  . THR   B 2 40  ? -8.16724  -9.47787  -0.19107  1.000 9.42377   ? 45   THR   A CG2  1 
ATOM   2609 N  N    . LYS   B 2 41  ? -4.36594  -12.28268 -1.29851  1.000 13.24705  ? 46   LYS   A N    1 
ATOM   2610 C  CA   . LYS   B 2 41  ? -3.39780  -12.94667 -2.15437  1.000 15.95041  ? 46   LYS   A CA   1 
ATOM   2611 C  C    . LYS   B 2 41  ? -2.69282  -14.00557 -1.32023  1.000 14.64717  ? 46   LYS   A C    1 
ATOM   2612 O  O    . LYS   B 2 41  ? -2.98794  -14.17253 -0.12926  1.000 11.30649  ? 46   LYS   A O    1 
ATOM   2613 C  CB   . LYS   B 2 41  ? -2.40681  -11.94764 -2.75132  1.000 12.26897  ? 46   LYS   A CB   1 
ATOM   2614 C  CG   . LYS   B 2 41  ? -3.03776  -10.98573 -3.74444  1.000 20.19267  ? 46   LYS   A CG   1 
ATOM   2615 C  CD   . LYS   B 2 41  ? -2.02767  -10.61073 -4.82835  1.000 31.48757  ? 46   LYS   A CD   1 
ATOM   2616 C  CE   . LYS   B 2 41  ? -2.64162  -9.69483  -5.88047  1.000 48.33753  ? 46   LYS   A CE   1 
ATOM   2617 N  NZ   . LYS   B 2 41  ? -3.05577  -8.39482  -5.28859  1.000 52.92858  ? 46   LYS   A NZ   1 
ATOM   2618 N  N    . ALA   B 2 42  ? -1.75371  -14.72055 -1.94409  1.000 9.71475   ? 47   ALA   A N    1 
ATOM   2619 C  CA   . ALA   B 2 42  ? -1.03671  -15.78646 -1.25296  1.000 9.81539   ? 47   ALA   A CA   1 
ATOM   2620 C  C    . ALA   B 2 42  ? -0.49789  -15.28835 0.08507   1.000 8.81394   ? 47   ALA   A C    1 
ATOM   2621 O  O    . ALA   B 2 42  ? -0.07098  -14.13432 0.20705   1.000 9.26883   ? 47   ALA   A O    1 
ATOM   2622 C  CB   . ALA   B 2 42  ? 0.11242   -16.29943 -2.12680  1.000 11.02359  ? 47   ALA   A CB   1 
ATOM   2623 N  N    . VAL   B 2 43  ? -0.54394  -16.15830 1.09512   1.000 8.45882   ? 48   VAL   A N    1 
ATOM   2624 C  CA   . VAL   B 2 43  ? 0.03690   -15.87519 2.40716   1.000 7.71922   ? 48   VAL   A CA   1 
ATOM   2625 C  C    . VAL   B 2 43  ? 1.44494   -16.43909 2.41735   1.000 9.05853   ? 48   VAL   A C    1 
ATOM   2626 O  O    . VAL   B 2 43  ? 1.64405   -17.62709 2.14743   1.000 12.04548  ? 48   VAL   A O    1 
ATOM   2627 C  CB   . VAL   B 2 43  ? -0.79618  -16.49918 3.53811   1.000 10.06117  ? 48   VAL   A CB   1 
ATOM   2628 C  CG1  . VAL   B 2 43  ? -0.14634  -16.22106 4.90416   1.000 8.92383   ? 48   VAL   A CG1  1 
ATOM   2629 C  CG2  . VAL   B 2 43  ? -2.25121  -16.02328 3.48993   1.000 9.90959   ? 48   VAL   A CG2  1 
ATOM   2630 N  N    . SER   B 2 44  ? 2.42285   -15.60801 2.74640   1.000 7.89795   ? 49   SER   A N    1 
ATOM   2631 C  CA   . SER   B 2 44  ? 3.80889   -16.02792 2.61158   1.000 10.08001  ? 49   SER   A CA   1 
ATOM   2632 C  C    . SER   B 2 44  ? 4.43078   -16.52581 3.91267   1.000 11.10413  ? 49   SER   A C    1 
ATOM   2633 O  O    . SER   B 2 44  ? 5.30185   -17.39975 3.86981   1.000 10.79744  ? 49   SER   A O    1 
ATOM   2634 C  CB   . SER   B 2 44  ? 4.65087   -14.87590 2.03760   1.000 12.27933  ? 49   SER   A CB   1 
ATOM   2635 O  OG   . SER   B 2 44  ? 4.49571   -13.68887 2.80252   1.000 15.83477  ? 49   SER   A OG   1 
ATOM   2636 N  N    . SER   B 2 45  ? 3.99863   -16.03977 5.07060   1.000 11.31895  ? 50   SER   A N    1 
ATOM   2637 C  CA   A SER   B 2 45  ? 4.66752   -16.40966 6.30869   0.792 12.72573  ? 50   SER   A CA   1 
ATOM   2638 C  CA   B SER   B 2 45  ? 4.65852   -16.41966 6.31069   0.208 12.72805  ? 50   SER   A CA   1 
ATOM   2639 C  C    . SER   B 2 45  ? 3.71338   -16.21566 7.48658   1.000 16.19241  ? 50   SER   A C    1 
ATOM   2640 O  O    . SER   B 2 45  ? 2.98431   -15.21770 7.54644   1.000 13.93680  ? 50   SER   A O    1 
ATOM   2641 C  CB   A SER   B 2 45  ? 5.94644   -15.57257 6.48878   0.792 12.53295  ? 50   SER   A CB   1 
ATOM   2642 C  CB   B SER   B 2 45  ? 5.94244   -15.60756 6.51678   0.208 12.53068  ? 50   SER   A CB   1 
ATOM   2643 O  OG   A SER   B 2 45  ? 6.81337   -16.10645 7.48690   0.792 11.87318  ? 50   SER   A OG   1 
ATOM   2644 O  OG   B SER   B 2 45  ? 5.65434   -14.22058 6.57067   0.208 12.76616  ? 50   SER   A OG   1 
ATOM   2645 N  N    . VAL   B 2 46  ? 3.71734   -17.17261 8.40963   1.000 13.45010  ? 51   VAL   A N    1 
ATOM   2646 C  CA   . VAL   B 2 46  ? 2.99520   -17.04458 9.67155   1.000 10.69099  ? 51   VAL   A CA   1 
ATOM   2647 C  C    . VAL   B 2 46  ? 3.99009   -17.26245 10.80667  1.000 13.95301  ? 51   VAL   A C    1 
ATOM   2648 O  O    . VAL   B 2 46  ? 4.84416   -18.15640 10.73281  1.000 11.75570  ? 51   VAL   A O    1 
ATOM   2649 C  CB   . VAL   B 2 46  ? 1.80625   -18.03466 9.77047   1.000 21.71829  ? 51   VAL   A CB   1 
ATOM   2650 C  CG1  . VAL   B 2 46  ? 0.68833   -17.64679 8.79233   1.000 13.69249  ? 51   VAL   A CG1  1 
ATOM   2651 C  CG2  . VAL   B 2 46  ? 2.26338   -19.48564 9.52260   1.000 13.87183  ? 51   VAL   A CG2  1 
ATOM   2652 N  N    . LYS   B 2 47  ? 3.89392   -16.42640 11.84761  1.000 12.70718  ? 52   LYS   A N    1 
ATOM   2653 C  CA   . LYS   B 2 47  ? 4.83181   -16.45028 12.96571  1.000 10.63067  ? 52   LYS   A CA   1 
ATOM   2654 C  C    . LYS   B 2 47  ? 4.08965   -16.22925 14.28162  1.000 12.39781  ? 52   LYS   A C    1 
ATOM   2655 O  O    . LYS   B 2 47  ? 3.38257   -15.23029 14.43749  1.000 11.06570  ? 52   LYS   A O    1 
ATOM   2656 C  CB   . LYS   B 2 47  ? 5.91375   -15.37022 12.80077  1.000 10.73790  ? 52   LYS   A CB   1 
ATOM   2657 C  CG   . LYS   B 2 47  ? 6.77690   -15.50123 11.53887  1.000 14.26611  ? 52   LYS   A CG   1 
ATOM   2658 C  CD   . LYS   B 2 47  ? 7.72697   -16.68516 11.62303  1.000 11.49503  ? 52   LYS   A CD   1 
ATOM   2659 C  CE   . LYS   B 2 47  ? 8.57511   -16.79417 10.36713  1.000 11.21353  ? 52   LYS   A CE   1 
ATOM   2660 N  NZ   . LYS   B 2 47  ? 9.62304   -15.73411 10.30118  1.000 8.52703   ? 52   LYS   A NZ   1 
ATOM   2661 N  N    . PHE   B 2 48  ? 4.25861   -17.14619 15.23069  1.000 8.68654   ? 53   PHE   A N    1 
ATOM   2662 C  CA   . PHE   B 2 48  ? 3.73745   -16.91515 16.57962  1.000 12.80208  ? 53   PHE   A CA   1 
ATOM   2663 C  C    . PHE   B 2 48  ? 4.61530   -15.91905 17.32466  1.000 14.23546  ? 53   PHE   A C    1 
ATOM   2664 O  O    . PHE   B 2 48  ? 5.84631   -15.99597 17.27779  1.000 10.01909  ? 53   PHE   A O    1 
ATOM   2665 C  CB   . PHE   B 2 48  ? 3.65945   -18.22311 17.37568  1.000 7.62134   ? 53   PHE   A CB   1 
ATOM   2666 C  CG   . PHE   B 2 48  ? 2.51755   -19.10521 16.96361  1.000 15.02527  ? 53   PHE   A CG   1 
ATOM   2667 C  CD1  . PHE   B 2 48  ? 1.20049   -18.77928 17.31345  1.000 8.65944   ? 53   PHE   A CD1  1 
ATOM   2668 C  CD2  . PHE   B 2 48  ? 2.74571   -20.25423 16.22970  1.000 10.86336  ? 53   PHE   A CD2  1 
ATOM   2669 C  CE1  . PHE   B 2 48  ? 0.14959   -19.57637 16.92438  1.000 10.79115  ? 53   PHE   A CE1  1 
ATOM   2670 C  CE2  . PHE   B 2 48  ? 1.68280   -21.06433 15.84063  1.000 15.42288  ? 53   PHE   A CE2  1 
ATOM   2671 C  CZ   . PHE   B 2 48  ? 0.39475   -20.72439 16.17647  1.000 9.89932   ? 53   PHE   A CZ   1 
ATOM   2672 N  N    . SER   B 2 49  ? 3.97917   -14.98005 18.01554  1.000 12.52658  ? 54   SER   A N    1 
ATOM   2673 C  CA   . SER   B 2 49  ? 4.75102   -14.10495 18.87457  1.000 13.18450  ? 54   SER   A CA   1 
ATOM   2674 C  C    . SER   B 2 49  ? 5.39695   -14.94085 19.98069  1.000 11.01697  ? 54   SER   A C    1 
ATOM   2675 O  O    . SER   B 2 49  ? 4.86498   -15.98286 20.37369  1.000 12.42546  ? 54   SER   A O    1 
ATOM   2676 C  CB   . SER   B 2 49  ? 3.86288   -13.00798 19.46041  1.000 14.61716  ? 54   SER   A CB   1 
ATOM   2677 O  OG   . SER   B 2 49  ? 2.84783   -13.55300 20.27534  1.000 12.26802  ? 54   SER   A OG   1 
ATOM   2678 N  N    . PRO   B 2 50  ? 6.56487   -14.52974 20.47379  1.000 13.72235  ? 55   PRO   A N    1 
ATOM   2679 C  CA   . PRO   B 2 50  ? 7.23781   -15.32664 21.51491  1.000 14.88185  ? 55   PRO   A CA   1 
ATOM   2680 C  C    . PRO   B 2 50  ? 6.44968   -15.44862 22.81783  1.000 20.60491  ? 55   PRO   A C    1 
ATOM   2681 O  O    . PRO   B 2 50  ? 6.60267   -16.45657 23.52490  1.000 18.06053  ? 55   PRO   A O    1 
ATOM   2682 C  CB   . PRO   B 2 50  ? 8.56874   -14.58654 21.71501  1.000 13.30666  ? 55   PRO   A CB   1 
ATOM   2683 C  CG   . PRO   B 2 50  ? 8.79683   -13.87460 20.42399  1.000 19.10166  ? 55   PRO   A CG   1 
ATOM   2684 C  CD   . PRO   B 2 50  ? 7.44387   -13.49372 19.89983  1.000 12.51577  ? 55   PRO   A CD   1 
ATOM   2685 N  N    . ASN   B 2 51  ? 5.60558   -14.46766 23.15768  1.000 14.67971  ? 56   ASN   A N    1 
ATOM   2686 C  CA   . ASN   B 2 51  ? 4.77046   -14.58265 24.35060  1.000 20.09691  ? 56   ASN   A CA   1 
ATOM   2687 C  C    . ASN   B 2 51  ? 3.54454   -15.46974 24.13252  1.000 15.74956  ? 56   ASN   A C    1 
ATOM   2688 O  O    . ASN   B 2 51  ? 2.76045   -15.65774 25.06444  1.000 13.22073  ? 56   ASN   A O    1 
ATOM   2689 C  CB   . ASN   B 2 51  ? 4.32932   -13.18865 24.83647  1.000 14.62286  ? 56   ASN   A CB   1 
ATOM   2690 C  CG   . ASN   B 2 51  ? 3.32037   -12.51877 23.88633  1.000 18.29447  ? 56   ASN   A CG   1 
ATOM   2691 O  OD1  . ASN   B 2 51  ? 2.89952   -13.10285 22.89332  1.000 23.51832  ? 56   ASN   A OD1  1 
ATOM   2692 N  ND2  . ASN   B 2 51  ? 2.93926   -11.29478 24.19722  1.000 13.89347  ? 56   ASN   A ND2  1 
ATOM   2693 N  N    . GLY   B 2 52  ? 3.35971   -16.01482 22.93153  1.000 14.53297  ? 57   GLY   A N    1 
ATOM   2694 C  CA   . GLY   B 2 52  ? 2.32380   -17.00090 22.68847  1.000 14.97663  ? 57   GLY   A CA   1 
ATOM   2695 C  C    . GLY   B 2 52  ? 0.95179   -16.44601 22.38629  1.000 16.30896  ? 57   GLY   A C    1 
ATOM   2696 O  O    . GLY   B 2 52  ? 0.04388   -17.22709 22.04024  1.000 14.06926  ? 57   GLY   A O    1 
ATOM   2697 N  N    . GLU   B 2 53  ? 0.76670   -15.13002 22.48120  1.000 11.72742  ? 58   GLU   A N    1 
ATOM   2698 C  CA   . GLU   B 2 53  ? -0.56733  -14.55211 22.40002  1.000 16.85598  ? 58   GLU   A CA   1 
ATOM   2699 C  C    . GLU   B 2 53  ? -1.05219  -14.36322 20.96896  1.000 20.43899  ? 58   GLU   A C    1 
ATOM   2700 O  O    . GLU   B 2 53  ? -2.26316  -14.42932 20.72684  1.000 16.54206  ? 58   GLU   A O    1 
ATOM   2701 C  CB   . GLU   B 2 53  ? -0.59550  -13.20507 23.13395  1.000 13.43601  ? 58   GLU   A CB   1 
ATOM   2702 C  CG   . GLU   B 2 53  ? -0.42665  -13.32498 24.64297  1.000 20.58245  ? 58   GLU   A CG   1 
ATOM   2703 C  CD   . GLU   B 2 53  ? -1.53067  -14.16301 25.26390  1.000 27.56086  ? 58   GLU   A CD   1 
ATOM   2704 O  OE1  . GLU   B 2 53  ? -2.68770  -13.70409 25.25775  1.000 34.58301  ? 58   GLU   A OE1  1 
ATOM   2705 O  OE2  . GLU   B 2 53  ? -1.24964  -15.29297 25.72699  1.000 38.60462  ? 58   GLU   A OE2  1 
ATOM   2706 N  N    . TRP   B 2 54  ? -0.14410  -14.14122 20.01105  1.000 16.75547  ? 59   TRP   A N    1 
ATOM   2707 C  CA   . TRP   B 2 54  ? -0.53199  -13.67732 18.68298  1.000 19.21009  ? 59   TRP   A CA   1 
ATOM   2708 C  C    . TRP   B 2 54  ? 0.09918   -14.51833 17.57909  1.000 12.60962  ? 59   TRP   A C    1 
ATOM   2709 O  O    . TRP   B 2 54  ? 1.17320   -15.10525 17.74524  1.000 10.41895  ? 59   TRP   A O    1 
ATOM   2710 C  CB   . TRP   B 2 54  ? -0.13207  -12.19030 18.47194  1.000 16.34365  ? 59   TRP   A CB   1 
ATOM   2711 C  CG   . TRP   B 2 54  ? -0.64624  -11.29427 19.55583  1.000 17.83546  ? 59   TRP   A CG   1 
ATOM   2712 C  CD1  . TRP   B 2 54  ? 0.08161   -10.71617 20.57088  1.000 22.10340  ? 59   TRP   A CD1  1 
ATOM   2713 C  CD2  . TRP   B 2 54  ? -2.00129  -10.89035 19.75467  1.000 15.58807  ? 59   TRP   A CD2  1 
ATOM   2714 N  NE1  . TRP   B 2 54  ? -0.74253  -9.97818  21.38075  1.000 17.23774  ? 59   TRP   A NE1  1 
ATOM   2715 C  CE2  . TRP   B 2 54  ? -2.02747  -10.07029 20.90662  1.000 28.55007  ? 59   TRP   A CE2  1 
ATOM   2716 C  CE3  . TRP   B 2 54  ? -3.20020  -11.15047 19.08155  1.000 18.62106  ? 59   TRP   A CE3  1 
ATOM   2717 C  CZ2  . TRP   B 2 54  ? -3.20956  -9.50534  21.39446  1.000 22.23311  ? 59   TRP   A CZ2  1 
ATOM   2718 C  CZ3  . TRP   B 2 54  ? -4.37729  -10.58752 19.56339  1.000 23.67800  ? 59   TRP   A CZ3  1 
ATOM   2719 C  CH2  . TRP   B 2 54  ? -4.37047  -9.77046  20.70835  1.000 29.43169  ? 59   TRP   A CH2  1 
ATOM   2720 N  N    . LEU   B 2 55  ? -0.59169  -14.54944 16.44502  1.000 13.98048  ? 60   LEU   A N    1 
ATOM   2721 C  CA   . LEU   B 2 55  ? -0.05153  -14.96748 15.15810  1.000 12.67553  ? 60   LEU   A CA   1 
ATOM   2722 C  C    . LEU   B 2 55  ? 0.05949   -13.75152 14.24005  1.000 14.49922  ? 60   LEU   A C    1 
ATOM   2723 O  O    . LEU   B 2 55  ? -0.89155  -12.97859 14.11390  1.000 11.63326  ? 60   LEU   A O    1 
ATOM   2724 C  CB   . LEU   B 2 55  ? -0.94639  -16.02158 14.51207  1.000 8.90084   ? 60   LEU   A CB   1 
ATOM   2725 C  CG   . LEU   B 2 55  ? -0.40221  -16.68161 13.23416  1.000 13.35985  ? 60   LEU   A CG   1 
ATOM   2726 C  CD1  . LEU   B 2 55  ? 0.72482   -17.61352 13.58233  1.000 11.42848  ? 60   LEU   A CD1  1 
ATOM   2727 C  CD2  . LEU   B 2 55  ? -1.50508  -17.42873 12.49208  1.000 6.22909   ? 60   LEU   A CD2  1 
ATOM   2728 N  N    . ALA   B 2 56  ? 1.21954   -13.56648 13.62016  1.000 9.08918   ? 61   ALA   A N    1 
ATOM   2729 C  CA   . ALA   B 2 56  ? 1.37959   -12.56653 12.58012  1.000 10.95991  ? 61   ALA   A CA   1 
ATOM   2730 C  C    . ALA   B 2 56  ? 1.46578   -13.26760 11.23417  1.000 14.02141  ? 61   ALA   A C    1 
ATOM   2731 O  O    . ALA   B 2 56  ? 2.08786   -14.33056 11.11930  1.000 10.96601  ? 61   ALA   A O    1 
ATOM   2732 C  CB   . ALA   B 2 56  ? 2.62551   -11.70843 12.80921  1.000 9.05517   ? 61   ALA   A CB   1 
ATOM   2733 N  N    . SER   B 2 57  ? 0.83185   -12.68570 10.21907  1.000 8.40184   ? 62   SER   A N    1 
ATOM   2734 C  CA   . SER   B 2 57  ? 0.91803   -13.23077 8.87111   1.000 8.94269   ? 62   SER   A CA   1 
ATOM   2735 C  C    . SER   B 2 57  ? 1.28106   -12.12780 7.88709   1.000 12.30709  ? 62   SER   A C    1 
ATOM   2736 O  O    . SER   B 2 57  ? 0.78298   -11.00482 7.98897   1.000 12.90330  ? 62   SER   A O    1 
ATOM   2737 C  CB   . SER   B 2 57  ? -0.39988  -13.89988 8.45301   1.000 12.07133  ? 62   SER   A CB   1 
ATOM   2738 O  OG   . SER   B 2 57  ? -1.47394  -12.96595 8.41784   1.000 7.67321   ? 62   SER   A OG   1 
ATOM   2739 N  N    . SER   B 2 58  ? 2.12919   -12.46279 6.91720   1.000 13.47415  ? 63   SER   A N    1 
ATOM   2740 C  CA   . SER   B 2 58  ? 2.48925   -11.56783 5.83119   1.000 7.58043   ? 63   SER   A CA   1 
ATOM   2741 C  C    . SER   B 2 58  ? 1.95143   -12.14194 4.53216   1.000 9.03119   ? 63   SER   A C    1 
ATOM   2742 O  O    . SER   B 2 58  ? 1.66952   -13.33996 4.43420   1.000 10.10223  ? 63   SER   A O    1 
ATOM   2743 C  CB   . SER   B 2 58  ? 4.01024   -11.38074 5.74834   1.000 9.72731   ? 63   SER   A CB   1 
ATOM   2744 O  OG   . SER   B 2 58  ? 4.68536   -12.60571 5.44448   1.000 13.84488  ? 63   SER   A OG   1 
ATOM   2745 N  N    . SER   B 2 59  ? 1.79948   -11.28001 3.52610   1.000 10.85173  ? 64   SER   A N    1 
ATOM   2746 C  CA   . SER   B 2 59  ? 1.09163   -11.69612 2.32104   1.000 9.63696   ? 64   SER   A CA   1 
ATOM   2747 C  C    . SER   B 2 59  ? 1.60172   -10.95615 1.09306   1.000 11.09216  ? 64   SER   A C    1 
ATOM   2748 O  O    . SER   B 2 59  ? 2.09263   -9.82212  1.17805   1.000 10.93988  ? 64   SER   A O    1 
ATOM   2749 C  CB   . SER   B 2 59  ? -0.42140  -11.46821 2.45487   1.000 7.49614   ? 64   SER   A CB   1 
ATOM   2750 O  OG   . SER   B 2 59  ? -1.07424  -11.79732 1.24382   1.000 10.04724  ? 64   SER   A OG   1 
ATOM   2751 N  N    . ALA   B 2 60  ? 1.45288   -11.61123 -0.06192  1.000 10.88446  ? 65   ALA   A N    1 
ATOM   2752 C  CA   . ALA   B 2 60  ? 1.61198   -10.93129 -1.33794  1.000 10.49040  ? 65   ALA   A CA   1 
ATOM   2753 C  C    . ALA   B 2 60  ? 0.63892   -9.77536  -1.49311  1.000 11.22034  ? 65   ALA   A C    1 
ATOM   2754 O  O    . ALA   B 2 60  ? 0.83895   -8.93740  -2.37714  1.000 8.96222   ? 65   ALA   A O    1 
ATOM   2755 C  CB   . ALA   B 2 60  ? 1.44217   -11.91737 -2.49991  1.000 9.11023   ? 65   ALA   A CB   1 
ATOM   2756 N  N    . ASP   B 2 61  ? -0.39418  -9.69339  -0.66223  1.000 9.21980   ? 66   ASP   A N    1 
ATOM   2757 C  CA   . ASP   B 2 61  ? -1.28525  -8.54545  -0.75039  1.000 14.26299  ? 66   ASP   A CA   1 
ATOM   2758 C  C    . ASP   B 2 61  ? -0.71040  -7.30437  -0.06840  1.000 15.17498  ? 66   ASP   A C    1 
ATOM   2759 O  O    . ASP   B 2 61  ? -1.43348  -6.31741  0.09847   1.000 14.67257  ? 66   ASP   A O    1 
ATOM   2760 C  CB   . ASP   B 2 61  ? -2.66628  -8.89451  -0.17352  1.000 11.36763  ? 66   ASP   A CB   1 
ATOM   2761 C  CG   . ASP   B 2 61  ? -2.66944  -9.02042  1.35949   1.000 11.50023  ? 66   ASP   A CG   1 
ATOM   2762 O  OD1  . ASP   B 2 61  ? -1.65053  -8.69432  2.01858   1.000 9.38441   ? 66   ASP   A OD1  1 
ATOM   2763 O  OD2  . ASP   B 2 61  ? -3.70747  -9.46346  1.90140   1.000 14.73540  ? 66   ASP   A OD2  1 
ATOM   2764 N  N    . LYS   B 2 62  ? 0.56456   -7.33027  0.31974   1.000 11.75291  ? 67   LYS   A N    1 
ATOM   2765 C  CA   . LYS   B 2 62  ? 1.27942   -6.19719  0.88076   1.000 12.47468  ? 67   LYS   A CA   1 
ATOM   2766 C  C    . LYS   B 2 62  ? 0.91725   -5.94313  2.33570   1.000 15.47791  ? 67   LYS   A C    1 
ATOM   2767 O  O    . LYS   B 2 62  ? 1.35212   -4.91607  2.88669   1.000 15.70818  ? 67   LYS   A O    1 
ATOM   2768 C  CB   . LYS   B 2 62  ? 1.01642   -4.89925  0.11266   1.000 17.19290  ? 67   LYS   A CB   1 
ATOM   2769 C  CG   . LYS   B 2 62  ? 1.17459   -4.98232  -1.39932  1.000 16.56877  ? 67   LYS   A CG   1 
ATOM   2770 C  CD   . LYS   B 2 62  ? 0.60857   -3.70240  -2.03845  1.000 20.30297  ? 67   LYS   A CD   1 
ATOM   2771 C  CE   . LYS   B 2 62  ? 0.95172   -3.59845  -3.51242  1.000 25.92615  ? 67   LYS   A CE   1 
ATOM   2772 N  NZ   . LYS   B 2 62  ? 0.10873   -2.57255  -4.18757  1.000 34.17206  ? 67   LYS   A NZ   1 
ATOM   2773 N  N    . LEU   B 2 63  ? 0.12424   -6.80815  2.96467   1.000 11.68593  ? 68   LEU   A N    1 
ATOM   2774 C  CA   . LEU   B 2 63  ? -0.39192  -6.57011  4.30160   1.000 11.97611  ? 68   LEU   A CA   1 
ATOM   2775 C  C    . LEU   B 2 63  ? 0.19604   -7.54801  5.31072   1.000 16.31571  ? 68   LEU   A C    1 
ATOM   2776 O  O    . LEU   B 2 63  ? 0.52015   -8.69501  4.98581   1.000 11.11974  ? 68   LEU   A O    1 
ATOM   2777 C  CB   . LEU   B 2 63  ? -1.91892  -6.69221  4.33844   1.000 11.23938  ? 68   LEU   A CB   1 
ATOM   2778 C  CG   . LEU   B 2 63  ? -2.68189  -5.68031  3.48930   1.000 17.09967  ? 68   LEU   A CG   1 
ATOM   2779 C  CD1  . LEU   B 2 63  ? -4.16892  -5.77839  3.79115   1.000 15.47639  ? 68   LEU   A CD1  1 
ATOM   2780 C  CD2  . LEU   B 2 63  ? -2.14301  -4.24926  3.74128   1.000 16.85131  ? 68   LEU   A CD2  1 
ATOM   2781 N  N    . ILE   B 2 64  ? 0.31787   -7.07394  6.54670   1.000 11.36322  ? 69   ILE   A N    1 
ATOM   2782 C  CA   . ILE   B 2 64  ? 0.57080   -7.90985  7.70778   1.000 12.44092  ? 69   ILE   A CA   1 
ATOM   2783 C  C    . ILE   B 2 64  ? -0.71428  -7.92989  8.51164   1.000 11.48178  ? 69   ILE   A C    1 
ATOM   2784 O  O    . ILE   B 2 64  ? -1.30138  -6.86992  8.76352   1.000 14.41813  ? 69   ILE   A O    1 
ATOM   2785 C  CB   . ILE   B 2 64  ? 1.73168   -7.36473  8.55387   1.000 12.28448  ? 69   ILE   A CB   1 
ATOM   2786 C  CG1  . ILE   B 2 64  ? 3.04077   -7.42269  7.76701   1.000 17.53695  ? 69   ILE   A CG1  1 
ATOM   2787 C  CG2  . ILE   B 2 64  ? 1.86559   -8.13865  9.84993   1.000 11.25319  ? 69   ILE   A CG2  1 
ATOM   2788 C  CD1  . ILE   B 2 64  ? 4.12064   -6.52058  8.35108   1.000 13.04496  ? 69   ILE   A CD1  1 
ATOM   2789 N  N    . LYS   B 2 65  ? -1.16025  -9.11490  8.91366   1.000 8.91956   ? 70   LYS   A N    1 
ATOM   2790 C  CA   . LYS   B 2 65  ? -2.33233  -9.21093  9.78354   1.000 10.39240  ? 70   LYS   A CA   1 
ATOM   2791 C  C    . LYS   B 2 65  ? -1.97042  -9.92483  11.07962  1.000 15.64681  ? 70   LYS   A C    1 
ATOM   2792 O  O    . LYS   B 2 65  ? -1.14636  -10.84578 11.09176  1.000 15.86577  ? 70   LYS   A O    1 
ATOM   2793 C  CB   . LYS   B 2 65  ? -3.50021  -9.91605  9.09445   1.000 14.14186  ? 70   LYS   A CB   1 
ATOM   2794 C  CG   . LYS   B 2 65  ? -4.00513  -9.16215  7.85835   1.000 16.82110  ? 70   LYS   A CG   1 
ATOM   2795 C  CD   . LYS   B 2 65  ? -5.06600  -9.94026  7.09228   1.000 13.53542  ? 70   LYS   A CD   1 
ATOM   2796 C  CE   . LYS   B 2 65  ? -5.71594  -9.05737  6.01917   1.000 21.22941  ? 70   LYS   A CE   1 
ATOM   2797 N  NZ   . LYS   B 2 65  ? -6.45908  -7.89938  6.63102   1.000 18.62444  ? 70   LYS   A NZ   1 
ATOM   2798 N  N    . ILE   B 2 66  ? -2.58857  -9.48181  12.17052  1.000 12.10099  ? 71   ILE   A N    1 
ATOM   2799 C  CA   . ILE   B 2 66  ? -2.36968  -10.03473 13.49458  1.000 9.68525   ? 71   ILE   A CA   1 
ATOM   2800 C  C    . ILE   B 2 66  ? -3.63767  -10.76079 13.90248  1.000 15.62209  ? 71   ILE   A C    1 
ATOM   2801 O  O    . ILE   B 2 66  ? -4.74669  -10.24187 13.71734  1.000 17.17524  ? 71   ILE   A O    1 
ATOM   2802 C  CB   . ILE   B 2 66  ? -2.01286  -8.93065  14.50256  1.000 13.19064  ? 71   ILE   A CB   1 
ATOM   2803 C  CG1  . ILE   B 2 66  ? -0.87686  -8.06360  13.96363  1.000 11.88139  ? 71   ILE   A CG1  1 
ATOM   2804 C  CG2  . ILE   B 2 66  ? -1.67997  -9.53055  15.88263  1.000 17.11710  ? 71   ILE   A CG2  1 
ATOM   2805 C  CD1  . ILE   B 2 66  ? 0.47518   -8.72051  13.99281  1.000 13.48029  ? 71   ILE   A CD1  1 
ATOM   2806 N  N    . TRP   B 2 67  ? -3.47965  -11.96375 14.44257  1.000 12.17038  ? 72   TRP   A N    1 
ATOM   2807 C  CA   . TRP   B 2 67  ? -4.60764  -12.79080 14.84549  1.000 14.17559  ? 72   TRP   A CA   1 
ATOM   2808 C  C    . TRP   B 2 67  ? -4.37076  -13.30070 16.26255  1.000 15.92484  ? 72   TRP   A C    1 
ATOM   2809 O  O    . TRP   B 2 67  ? -3.22780  -13.41460 16.72168  1.000 13.29054  ? 72   TRP   A O    1 
ATOM   2810 C  CB   . TRP   B 2 67  ? -4.79946  -13.97987 13.88554  1.000 12.20292  ? 72   TRP   A CB   1 
ATOM   2811 C  CG   . TRP   B 2 67  ? -4.60332  -13.65594 12.40954  1.000 10.52184  ? 72   TRP   A CG   1 
ATOM   2812 C  CD1  . TRP   B 2 67  ? -3.41726  -13.43589 11.76266  1.000 12.79801  ? 72   TRP   A CD1  1 
ATOM   2813 C  CD2  . TRP   B 2 67  ? -5.62522  -13.55606 11.40943  1.000 14.78642  ? 72   TRP   A CD2  1 
ATOM   2814 N  NE1  . TRP   B 2 67  ? -3.63814  -13.18998 10.42262  1.000 11.63464  ? 72   TRP   A NE1  1 
ATOM   2815 C  CE2  . TRP   B 2 67  ? -4.98411  -13.26308 10.18048  1.000 17.88154  ? 72   TRP   A CE2  1 
ATOM   2816 C  CE3  . TRP   B 2 67  ? -7.01721  -13.68615 11.43128  1.000 13.54818  ? 72   TRP   A CE3  1 
ATOM   2817 C  CZ2  . TRP   B 2 67  ? -5.69299  -13.09620 8.99339   1.000 11.28255  ? 72   TRP   A CZ2  1 
ATOM   2818 C  CZ3  . TRP   B 2 67  ? -7.71710  -13.52026 10.25820  1.000 12.35486  ? 72   TRP   A CZ3  1 
ATOM   2819 C  CH2  . TRP   B 2 67  ? -7.05399  -13.22429 9.05325   1.000 17.35243  ? 72   TRP   A CH2  1 
ATOM   2820 N  N    . GLY   B 2 68  ? -5.46481  -13.62374 16.94645  1.000 13.17931  ? 73   GLY   A N    1 
ATOM   2821 C  CA   . GLY   B 2 68  ? -5.35891  -14.25866 18.25149  1.000 14.30195  ? 73   GLY   A CA   1 
ATOM   2822 C  C    . GLY   B 2 68  ? -4.85980  -15.68463 18.10663  1.000 13.81409  ? 73   GLY   A C    1 
ATOM   2823 O  O    . GLY   B 2 68  ? -5.38766  -16.46171 17.30161  1.000 11.63962  ? 73   GLY   A O    1 
ATOM   2824 N  N    . ALA   B 2 69  ? -3.84086  -16.04252 18.88676  1.000 13.38192  ? 74   ALA   A N    1 
ATOM   2825 C  CA   . ALA   B 2 69  ? -3.17775  -17.32049 18.63790  1.000 11.97347  ? 74   ALA   A CA   1 
ATOM   2826 C  C    . ALA   B 2 69  ? -4.00572  -18.50252 19.11588  1.000 16.64587  ? 74   ALA   A C    1 
ATOM   2827 O  O    . ALA   B 2 69  ? -3.76360  -19.62053 18.66196  1.000 15.47114  ? 74   ALA   A O    1 
ATOM   2828 C  CB   . ALA   B 2 69  ? -1.79881  -17.34836 19.29905  1.000 15.82841  ? 74   ALA   A CB   1 
ATOM   2829 N  N    . TYR   B 2 70  ? -4.97483  -18.28354 20.00876  1.000 13.71178  ? 75   TYR   A N    1 
ATOM   2830 C  CA   . TYR   B 2 70  ? -5.79482  -19.34356 20.58373  1.000 20.12156  ? 75   TYR   A CA   1 
ATOM   2831 C  C    . TYR   B 2 70  ? -7.19575  -19.38568 20.00058  1.000 18.47758  ? 75   TYR   A C    1 
ATOM   2832 O  O    . TYR   B 2 70  ? -7.74866  -20.47173 19.81858  1.000 21.96307  ? 75   TYR   A O    1 
ATOM   2833 C  CB   . TYR   B 2 70  ? -5.88899  -19.18248 22.10771  1.000 14.51646  ? 75   TYR   A CB   1 
ATOM   2834 C  CG   . TYR   B 2 70  ? -4.53206  -19.15535 22.75086  1.000 15.07106  ? 75   TYR   A CG   1 
ATOM   2835 C  CD1  . TYR   B 2 70  ? -3.76300  -20.30430 22.83900  1.000 20.41945  ? 75   TYR   A CD1  1 
ATOM   2836 C  CD2  . TYR   B 2 70  ? -4.00320  -17.97629 23.24985  1.000 23.54511  ? 75   TYR   A CD2  1 
ATOM   2837 C  CE1  . TYR   B 2 70  ? -2.49806  -20.27918 23.41214  1.000 19.61581  ? 75   TYR   A CE1  1 
ATOM   2838 C  CE2  . TYR   B 2 70  ? -2.74426  -17.94117 23.83698  1.000 15.28613  ? 75   TYR   A CE2  1 
ATOM   2839 C  CZ   . TYR   B 2 70  ? -1.99819  -19.08712 23.91012  1.000 20.66116  ? 75   TYR   A CZ   1 
ATOM   2840 O  OH   . TYR   B 2 70  ? -0.74126  -19.04201 24.48426  1.000 20.50708  ? 75   TYR   A OH   1 
ATOM   2841 N  N    . ASP   B 2 71  ? -7.77980  -18.23174 19.68346  1.000 16.95062  ? 76   ASP   A N    1 
ATOM   2842 C  CA   . ASP   B 2 71  ? -9.12074  -18.18486 19.12231  1.000 17.45125  ? 76   ASP   A CA   1 
ATOM   2843 C  C    . ASP   B 2 71  ? -9.14260  -17.91095 17.62229  1.000 17.02138  ? 76   ASP   A C    1 
ATOM   2844 O  O    . ASP   B 2 71  ? -10.20752 -18.01705 17.01018  1.000 17.30392  ? 76   ASP   A O    1 
ATOM   2845 C  CB   . ASP   B 2 71  ? -9.95589  -17.13487 19.86616  1.000 18.52806  ? 76   ASP   A CB   1 
ATOM   2846 C  CG   . ASP   B 2 71  ? -9.33498  -15.72984 19.81315  1.000 25.98761  ? 76   ASP   A CG   1 
ATOM   2847 O  OD1  . ASP   B 2 71  ? -8.44190  -15.48482 18.97723  1.000 21.88134  ? 76   ASP   A OD1  1 
ATOM   2848 O  OD2  . ASP   B 2 71  ? -9.75612  -14.86482 20.61606  1.000 19.45883  ? 76   ASP   A OD2  1 
ATOM   2849 N  N    . GLY   B 2 72  ? -7.99855  -17.59390 17.00740  1.000 21.42334  ? 77   GLY   A N    1 
ATOM   2850 C  CA   . GLY   B 2 72  ? -7.95642  -17.33098 15.57539  1.000 14.23821  ? 77   GLY   A CA   1 
ATOM   2851 C  C    . GLY   B 2 72  ? -8.65945  -16.06705 15.12424  1.000 21.97966  ? 77   GLY   A C    1 
ATOM   2852 O  O    . GLY   B 2 72  ? -8.84233  -15.86913 13.91621  1.000 19.49713  ? 77   GLY   A O    1 
ATOM   2853 N  N    . LYS   B 2 73  ? -9.04361  -15.19403 16.05115  1.000 21.69329  ? 78   LYS   A N    1 
ATOM   2854 C  CA   . LYS   B 2 73  ? -9.83465  -14.01210 15.72100  1.000 15.29280  ? 78   LYS   A CA   1 
ATOM   2855 C  C    . LYS   B 2 73  ? -8.94167  -12.89407 15.19503  1.000 16.80179  ? 78   LYS   A C    1 
ATOM   2856 O  O    . LYS   B 2 73  ? -7.92476  -12.56297 15.80912  1.000 12.63648  ? 78   LYS   A O    1 
ATOM   2857 C  CB   . LYS   B 2 73  ? -10.60082 -13.55008 16.95889  1.000 22.73698  ? 78   LYS   A CB   1 
ATOM   2858 C  CG   . LYS   B 2 73  ? -11.07991 -12.10611 16.93176  1.000 35.41550  ? 78   LYS   A CG   1 
ATOM   2859 C  CD   . LYS   B 2 73  ? -12.20303 -11.87413 17.96263  1.000 40.04704  ? 78   LYS   A CD   1 
ATOM   2860 C  CE   . LYS   B 2 73  ? -11.88921 -10.73005 18.92660  1.000 36.85060  ? 78   LYS   A CE   1 
ATOM   2861 N  NZ   . LYS   B 2 73  ? -10.87530 -11.13393 19.94973  1.000 42.32225  ? 78   LYS   A NZ   1 
ATOM   2862 N  N    . PHE   B 2 74  ? -9.32159  -12.31516 14.05296  1.000 13.44972  ? 79   PHE   A N    1 
ATOM   2863 C  CA   . PHE   B 2 74  ? -8.58760  -11.18414 13.48898  1.000 15.81340  ? 79   PHE   A CA   1 
ATOM   2864 C  C    . PHE   B 2 74  ? -8.42078  -10.04907 14.50193  1.000 21.45414  ? 79   PHE   A C    1 
ATOM   2865 O  O    . PHE   B 2 74  ? -9.36388  -9.67010  15.20381  1.000 19.97522  ? 79   PHE   A O    1 
ATOM   2866 C  CB   . PHE   B 2 74  ? -9.30650  -10.66526 12.24087  1.000 20.50079  ? 79   PHE   A CB   1 
ATOM   2867 C  CG   . PHE   B 2 74  ? -8.73953  -9.37825  11.71286  1.000 20.16245  ? 79   PHE   A CG   1 
ATOM   2868 C  CD1  . PHE   B 2 74  ? -7.55145  -9.37421  10.98899  1.000 14.67784  ? 79   PHE   A CD1  1 
ATOM   2869 C  CD2  . PHE   B 2 74  ? -9.38363  -8.17528  11.94272  1.000 18.93020  ? 79   PHE   A CD2  1 
ATOM   2870 C  CE1  . PHE   B 2 74  ? -7.01748  -8.19120  10.50098  1.000 18.13521  ? 79   PHE   A CE1  1 
ATOM   2871 C  CE2  . PHE   B 2 74  ? -8.85766  -6.99427  11.45371  1.000 25.43033  ? 79   PHE   A CE2  1 
ATOM   2872 C  CZ   . PHE   B 2 74  ? -7.67058  -7.00123  10.72984  1.000 17.18609  ? 79   PHE   A CZ   1 
ATOM   2873 N  N    . GLU   B 2 75  ? -7.20883  -9.50899  14.58103  1.000 18.73310  ? 80   GLU   A N    1 
ATOM   2874 C  CA   . GLU   B 2 75  ? -6.91400  -8.39892  15.48200  1.000 20.39868  ? 80   GLU   A CA   1 
ATOM   2875 C  C    . GLU   B 2 75  ? -6.69801  -7.08094  14.75395  1.000 22.50923  ? 80   GLU   A C    1 
ATOM   2876 O  O    . GLU   B 2 75  ? -7.26512  -6.06196  15.15183  1.000 22.30001  ? 80   GLU   A O    1 
ATOM   2877 C  CB   . GLU   B 2 75  ? -5.67207  -8.71179  16.33415  1.000 17.97951  ? 80   GLU   A CB   1 
ATOM   2878 C  CG   . GLU   B 2 75  ? -5.31525  -7.60271  17.31813  1.000 23.46379  ? 80   GLU   A CG   1 
ATOM   2879 C  CD   . GLU   B 2 75  ? -6.32938  -7.48971  18.44501  1.000 29.07461  ? 80   GLU   A CD   1 
ATOM   2880 O  OE1  . GLU   B 2 75  ? -7.25033  -8.34077  18.49996  1.000 29.56269  ? 80   GLU   A OE1  1 
ATOM   2881 O  OE2  . GLU   B 2 75  ? -6.21153  -6.55966  19.27197  1.000 26.50552  ? 80   GLU   A OE2  1 
ATOM   2882 N  N    . LYS   B 2 76  ? -5.86790  -7.06195  13.71104  1.000 16.43064  ? 81   LYS   A N    1 
ATOM   2883 C  CA   . LYS   B 2 76  ? -5.57091  -5.79996  13.05100  1.000 13.36196  ? 81   LYS   A CA   1 
ATOM   2884 C  C    . LYS   B 2 76  ? -4.74376  -6.05398  11.79710  1.000 20.75951  ? 81   LYS   A C    1 
ATOM   2885 O  O    . LYS   B 2 76  ? -4.11167  -7.10695  11.63323  1.000 11.88953  ? 81   LYS   A O    1 
ATOM   2886 C  CB   . LYS   B 2 76  ? -4.82807  -4.83386  13.98803  1.000 14.28751  ? 81   LYS   A CB   1 
ATOM   2887 C  CG   . LYS   B 2 76  ? -3.33106  -5.08076  14.04120  1.000 22.39996  ? 81   LYS   A CG   1 
ATOM   2888 C  CD   . LYS   B 2 76  ? -2.59121  -3.95467  14.74822  1.000 20.59715  ? 81   LYS   A CD   1 
ATOM   2889 C  CE   . LYS   B 2 76  ? -2.92237  -3.93661  16.23218  1.000 23.41872  ? 81   LYS   A CE   1 
ATOM   2890 N  NZ   . LYS   B 2 76  ? -2.10352  -2.92052  16.94621  1.000 26.57183  ? 81   LYS   A NZ   1 
ATOM   2891 N  N    . THR   B 2 77  ? -4.75873  -5.06203  10.91905  1.000 15.52837  ? 82   THR   A N    1 
ATOM   2892 C  CA   . THR   B 2 77  ? -3.97560  -5.04804  9.69813   1.000 11.64307  ? 82   THR   A CA   1 
ATOM   2893 C  C    . THR   B 2 77  ? -2.88468  -3.99197  9.82019   1.000 18.27116  ? 82   THR   A C    1 
ATOM   2894 O  O    . THR   B 2 77  ? -3.13281  -2.89395  10.32710  1.000 14.43224  ? 82   THR   A O    1 
ATOM   2895 C  CB   . THR   B 2 77  ? -4.86449  -4.72317  8.51302   1.000 18.62922  ? 82   THR   A CB   1 
ATOM   2896 O  OG1  . THR   B 2 77  ? -5.84941  -5.76024  8.37697   1.000 17.38116  ? 82   THR   A OG1  1 
ATOM   2897 C  CG2  . THR   B 2 77  ? -4.02437  -4.54419  7.21910   1.000 12.23593  ? 82   THR   A CG2  1 
ATOM   2898 N  N    . ILE   B 2 78  ? -1.68361  -4.33091  9.35933   1.000 14.58042  ? 83   ILE   A N    1 
ATOM   2899 C  CA   . ILE   B 2 78  ? -0.54267  -3.42384  9.34441   1.000 19.11006  ? 83   ILE   A CA   1 
ATOM   2900 C  C    . ILE   B 2 78  ? -0.09753  -3.24289  7.90044   1.000 15.84944  ? 83   ILE   A C    1 
ATOM   2901 O  O    . ILE   B 2 78  ? 0.12062   -4.22691  7.18152   1.000 15.43977  ? 83   ILE   A O    1 
ATOM   2902 C  CB   . ILE   B 2 78  ? 0.60827   -3.94271  10.22756  1.000 13.06143  ? 83   ILE   A CB   1 
ATOM   2903 C  CG1  . ILE   B 2 78  ? 0.16511   -3.89866  11.69051  1.000 15.32451  ? 83   ILE   A CG1  1 
ATOM   2904 C  CG2  . ILE   B 2 78  ? 1.84723   -3.08264  10.03664  1.000 15.59526  ? 83   ILE   A CG2  1 
ATOM   2905 C  CD1  . ILE   B 2 78  ? 1.14305   -4.49354  12.63665  1.000 14.63162  ? 83   ILE   A CD1  1 
ATOM   2906 N  N    . SER   B 2 79  ? 0.02844   -1.98690  7.47539   1.000 16.75600  ? 84   SER   A N    1 
ATOM   2907 C  CA   . SER   B 2 79  ? 0.19557   -1.67297  6.06439   1.000 17.09781  ? 84   SER   A CA   1 
ATOM   2908 C  C    . SER   B 2 79  ? 1.27752   -0.62091  5.88745   1.000 14.17297  ? 84   SER   A C    1 
ATOM   2909 O  O    . SER   B 2 79  ? 1.55337   0.16516   6.79743   1.000 16.57150  ? 84   SER   A O    1 
ATOM   2910 C  CB   . SER   B 2 79  ? -1.11140  -1.16709  5.44722   1.000 14.73792  ? 84   SER   A CB   1 
ATOM   2911 O  OG   . SER   B 2 79  ? -1.45755  0.06492   6.03011   1.000 19.96758  ? 84   SER   A OG   1 
ATOM   2912 N  N    . GLY   B 2 80  ? 1.88264   -0.61693  4.70051   1.000 12.69915  ? 85   GLY   A N    1 
ATOM   2913 C  CA   . GLY   B 2 80  ? 2.90161   0.35511   4.37457   1.000 12.84705  ? 85   GLY   A CA   1 
ATOM   2914 C  C    . GLY   B 2 80  ? 3.84776   -0.08788  3.27169   1.000 22.69374  ? 85   GLY   A C    1 
ATOM   2915 O  O    . GLY   B 2 80  ? 4.39578   0.76211   2.56470   1.000 19.59385  ? 85   GLY   A O    1 
ATOM   2916 N  N    . HIS   B 2 81  ? 4.07287   -1.39588  3.11179   1.000 15.01734  ? 86   HIS   A N    1 
ATOM   2917 C  CA   . HIS   B 2 81  ? 4.91701   -1.83988  2.01090   1.000 12.83341  ? 86   HIS   A CA   1 
ATOM   2918 C  C    . HIS   B 2 81  ? 4.24713   -1.51700  0.67481   1.000 17.28309  ? 86   HIS   A C    1 
ATOM   2919 O  O    . HIS   B 2 81  ? 3.01814   -1.37709  0.58067   1.000 17.45910  ? 86   HIS   A O    1 
ATOM   2920 C  CB   . HIS   B 2 81  ? 5.23010   -3.33786  2.13402   1.000 13.79013  ? 86   HIS   A CB   1 
ATOM   2921 C  CG   . HIS   B 2 81  ? 6.37402   -3.63473  3.05716   1.000 15.11514  ? 86   HIS   A CG   1 
ATOM   2922 N  ND1  . HIS   B 2 81  ? 7.66002   -3.18566  2.81727   1.000 14.47307  ? 86   HIS   A ND1  1 
ATOM   2923 C  CD2  . HIS   B 2 81  ? 6.42794   -4.31566  4.22920   1.000 11.11173  ? 86   HIS   A CD2  1 
ATOM   2924 C  CE1  . HIS   B 2 81  ? 8.45394   -3.58055  3.80038   1.000 13.22057  ? 86   HIS   A CE1  1 
ATOM   2925 N  NE2  . HIS   B 2 81  ? 7.73389   -4.27455  4.66534   1.000 12.39495  ? 86   HIS   A NE2  1 
ATOM   2926 N  N    . LYS   B 2 82  ? 5.06724   -1.36401  -0.36611  1.000 12.62642  ? 87   LYS   A N    1 
ATOM   2927 C  CA   . LYS   B 2 82  ? 4.53835   -0.99111  -1.67018  1.000 19.03902  ? 87   LYS   A CA   1 
ATOM   2928 C  C    . LYS   B 2 82  ? 4.27553   -2.19018  -2.56315  1.000 18.36741  ? 87   LYS   A C    1 
ATOM   2929 O  O    . LYS   B 2 82  ? 3.56463   -2.05328  -3.56623  1.000 18.03321  ? 87   LYS   A O    1 
ATOM   2930 C  CB   . LYS   B 2 82  ? 5.49136   -0.03109  -2.38414  1.000 20.03851  ? 87   LYS   A CB   1 
ATOM   2931 C  CG   . LYS   B 2 82  ? 5.52621   1.37094   -1.78521  1.000 31.81700  ? 87   LYS   A CG   1 
ATOM   2932 C  CD   . LYS   B 2 82  ? 6.28924   2.32894   -2.69918  1.000 43.61985  ? 87   LYS   A CD   1 
ATOM   2933 C  CE   . LYS   B 2 82  ? 7.56014   2.86107   -2.04107  1.000 56.00392  ? 87   LYS   A CE   1 
ATOM   2934 N  NZ   . LYS   B 2 82  ? 8.60122   3.23808   -3.05198  1.000 58.27164  ? 87   LYS   A NZ   1 
ATOM   2935 N  N    . LEU   B 2 83  ? 4.83457   -3.34913  -2.22702  1.000 11.24571  ? 88   LEU   A N    1 
ATOM   2936 C  CA   . LEU   B 2 83  ? 4.63773   -4.57318  -3.00397  1.000 16.98946  ? 88   LEU   A CA   1 
ATOM   2937 C  C    . LEU   B 2 83  ? 4.53170   -5.72713  -2.01892  1.000 13.38816  ? 88   LEU   A C    1 
ATOM   2938 O  O    . LEU   B 2 83  ? 4.54056   -5.52307  -0.79993  1.000 13.83978  ? 88   LEU   A O    1 
ATOM   2939 C  CB   . LEU   B 2 83  ? 5.77286   -4.80116  -4.01084  1.000 19.29668  ? 88   LEU   A CB   1 
ATOM   2940 C  CG   . LEU   B 2 83  ? 5.92993   -3.88222  -5.22687  1.000 28.22568  ? 88   LEU   A CG   1 
ATOM   2941 C  CD1  . LEU   B 2 83  ? 7.31401   -4.06416  -5.86971  1.000 14.60426  ? 88   LEU   A CD1  1 
ATOM   2942 C  CD2  . LEU   B 2 83  ? 4.80905   -4.12335  -6.25598  1.000 18.07369  ? 88   LEU   A CD2  1 
ATOM   2943 N  N    . GLY   B 2 84  ? 4.46284   -6.93917  -2.56386  1.000 14.21537  ? 89   GLY   A N    1 
ATOM   2944 C  CA   . GLY   B 2 84  ? 4.26484   -8.14214  -1.78781  1.000 15.36713  ? 89   GLY   A CA   1 
ATOM   2945 C  C    . GLY   B 2 84  ? 5.26173   -8.28501  -0.65270  1.000 19.27545  ? 89   GLY   A C    1 
ATOM   2946 O  O    . GLY   B 2 84  ? 6.40070   -7.79694  -0.73060  1.000 12.52361  ? 89   GLY   A O    1 
ATOM   2947 N  N    . ILE   B 2 85  ? 4.82566   -8.94198  0.41729   1.000 12.11071  ? 90   ILE   A N    1 
ATOM   2948 C  CA   . ILE   B 2 85  ? 5.66755   -9.21586  1.57340   1.000 11.57161  ? 90   ILE   A CA   1 
ATOM   2949 C  C    . ILE   B 2 85  ? 6.00965   -10.69284 1.56952   1.000 12.51366  ? 90   ILE   A C    1 
ATOM   2950 O  O    . ILE   B 2 85  ? 5.12272   -11.54790 1.43847   1.000 12.42602  ? 90   ILE   A O    1 
ATOM   2951 C  CB   . ILE   B 2 85  ? 4.97938   -8.80983  2.88630   1.000 16.52604  ? 90   ILE   A CB   1 
ATOM   2952 C  CG1  . ILE   B 2 85  ? 4.68728   -7.29585  2.87818   1.000 15.68804  ? 90   ILE   A CG1  1 
ATOM   2953 C  CG2  . ILE   B 2 85  ? 5.85728   -9.21371  4.06242   1.000 12.29699  ? 90   ILE   A CG2  1 
ATOM   2954 C  CD1  . ILE   B 2 85  ? 3.90412   -6.82484  4.08207   1.000 13.10909  ? 90   ILE   A CD1  1 
ATOM   2955 N  N    . SER   B 2 86  ? 7.29365   -10.98574 1.73067   1.000 11.04153  ? 91   SER   A N    1 
ATOM   2956 C  CA   . SER   B 2 86  ? 7.83075   -12.33271 1.66380   1.000 10.31847  ? 91   SER   A CA   1 
ATOM   2957 C  C    . SER   B 2 86  ? 7.97964   -12.98762 3.03385   1.000 10.54799  ? 91   SER   A C    1 
ATOM   2958 O  O    . SER   B 2 86  ? 7.86171   -14.21163 3.14291   1.000 13.52873  ? 91   SER   A O    1 
ATOM   2959 C  CB   . SER   B 2 86  ? 9.18482   -12.27766 0.93094   1.000 14.88262  ? 91   SER   A CB   1 
ATOM   2960 O  OG   . SER   B 2 86  ? 9.75792   -13.53963 0.75508   1.000 15.21550  ? 91   SER   A OG   1 
ATOM   2961 N  N    . ASP   B 2 87  ? 8.16148   -12.20955 4.09783   1.000 13.98140  ? 92   ASP   A N    1 
ATOM   2962 C  CA   . ASP   B 2 87  ? 8.46437   -12.77646 5.40190   1.000 11.28378  ? 92   ASP   A CA   1 
ATOM   2963 C  C    . ASP   B 2 87  ? 8.24219   -11.71941 6.47581   1.000 14.48942  ? 92   ASP   A C    1 
ATOM   2964 O  O    . ASP   B 2 87  ? 8.30914   -10.51142 6.21875   1.000 13.73430  ? 92   ASP   A O    1 
ATOM   2965 C  CB   . ASP   B 2 87  ? 9.90940   -13.28736 5.44108   1.000 10.53312  ? 92   ASP   A CB   1 
ATOM   2966 C  CG   . ASP   B 2 87  ? 10.20633  -14.14227 6.65816   1.000 15.21834  ? 92   ASP   A CG   1 
ATOM   2967 O  OD1  . ASP   B 2 87  ? 9.24130   -14.67130 7.28108   1.000 12.63350  ? 92   ASP   A OD1  1 
ATOM   2968 O  OD2  . ASP   B 2 87  ? 11.42630  -14.28017 6.97830   1.000 14.81372  ? 92   ASP   A OD2  1 
ATOM   2969 N  N    . VAL   B 2 88  ? 8.00009   -12.19236 7.69581   1.000 14.58351  ? 93   VAL   A N    1 
ATOM   2970 C  CA   . VAL   B 2 88  ? 7.80791   -11.30931 8.84174   1.000 15.64940  ? 93   VAL   A CA   1 
ATOM   2971 C  C    . VAL   B 2 88  ? 8.38382   -12.02820 10.06084  1.000 15.82540  ? 93   VAL   A C    1 
ATOM   2972 O  O    . VAL   B 2 88  ? 8.49591   -13.25920 10.07293  1.000 12.32808  ? 93   VAL   A O    1 
ATOM   2973 C  CB   . VAL   B 2 88  ? 6.30787   -10.92140 8.99456   1.000 12.91433  ? 93   VAL   A CB   1 
ATOM   2974 C  CG1  . VAL   B 2 88  ? 5.45591   -12.14144 9.34454   1.000 12.21549  ? 93   VAL   A CG1  1 
ATOM   2975 C  CG2  . VAL   B 2 88  ? 6.12768   -9.83236  10.02348  1.000 16.56744  ? 93   VAL   A CG2  1 
ATOM   2976 N  N    . ALA   B 2 89  ? 8.80466   -11.25412 11.07085  1.000 11.95565  ? 94   ALA   A N    1 
ATOM   2977 C  CA   . ALA   B 2 89  ? 9.45958   -11.82701 12.24395  1.000 14.25620  ? 94   ALA   A CA   1 
ATOM   2978 C  C    . ALA   B 2 89  ? 9.24139   -10.94296 13.47188  1.000 15.47182  ? 94   ALA   A C    1 
ATOM   2979 O  O    . ALA   B 2 89  ? 9.18232   -9.71597  13.36980  1.000 18.09060  ? 94   ALA   A O    1 
ATOM   2980 C  CB   . ALA   B 2 89  ? 10.96161  -12.01792 12.00812  1.000 15.48584  ? 94   ALA   A CB   1 
ATOM   2981 N  N    . TRP   B 2 90  ? 9.15630   -11.58090 14.63890  1.000 11.37078  ? 95   TRP   A N    1 
ATOM   2982 C  CA   . TRP   B 2 90  ? 8.88012   -10.90685 15.90384  1.000 13.28142  ? 95   TRP   A CA   1 
ATOM   2983 C  C    . TRP   B 2 90  ? 10.17702  -10.57672 16.64896  1.000 13.92456  ? 95   TRP   A C    1 
ATOM   2984 O  O    . TRP   B 2 90  ? 11.15708  -11.32166 16.58310  1.000 12.93253  ? 95   TRP   A O    1 
ATOM   2985 C  CB   . TRP   B 2 90  ? 8.01108   -11.77785 16.81679  1.000 9.52651   ? 95   TRP   A CB   1 
ATOM   2986 C  CG   . TRP   B 2 90  ? 6.57614   -12.00997 16.39065  1.000 10.96153  ? 95   TRP   A CG   1 
ATOM   2987 C  CD1  . TRP   B 2 90  ? 6.11230   -13.01305 15.59566  1.000 10.65491  ? 95   TRP   A CD1  1 
ATOM   2988 C  CD2  . TRP   B 2 90  ? 5.42305   -11.24903 16.79148  1.000 12.65622  ? 95   TRP   A CD2  1 
ATOM   2989 N  NE1  . TRP   B 2 90  ? 4.73330   -12.91915 15.46150  1.000 14.19372  ? 95   TRP   A NE1  1 
ATOM   2990 C  CE2  . TRP   B 2 90  ? 4.29015   -11.85313 16.19640  1.000 11.58455  ? 95   TRP   A CE2  1 
ATOM   2991 C  CE3  . TRP   B 2 90  ? 5.23789   -10.12099 17.60140  1.000 12.65151  ? 95   TRP   A CE3  1 
ATOM   2992 C  CZ2  . TRP   B 2 90  ? 3.00610   -11.35621 16.36123  1.000 15.33842  ? 95   TRP   A CZ2  1 
ATOM   2993 C  CZ3  . TRP   B 2 90  ? 3.95684   -9.63107  17.77624  1.000 16.95874  ? 95   TRP   A CZ3  1 
ATOM   2994 C  CH2  . TRP   B 2 90  ? 2.85594   -10.24618 17.15415  1.000 14.35611  ? 95   TRP   A CH2  1 
ATOM   2995 N  N    . SER   B 2 91  ? 10.17187  -9.45868  17.37389  1.000 16.82169  ? 96   SER   A N    1 
ATOM   2996 C  CA   . SER   B 2 91  ? 11.23675  -9.22555  18.34299  1.000 20.19498  ? 96   SER   A CA   1 
ATOM   2997 C  C    . SER   B 2 91  ? 11.00467  -10.08650 19.58702  1.000 16.87166  ? 96   SER   A C    1 
ATOM   2998 O  O    . SER   B 2 91  ? 9.89468   -10.56956 19.84393  1.000 14.23151  ? 96   SER   A O    1 
ATOM   2999 C  CB   . SER   B 2 91  ? 11.33361  -7.74553  18.72292  1.000 15.31536  ? 96   SER   A CB   1 
ATOM   3000 O  OG   . SER   B 2 91  ? 10.14151  -7.30057  19.35777  1.000 17.23794  ? 96   SER   A OG   1 
ATOM   3001 N  N    . SER   B 2 92  ? 12.07560  -10.28339 20.35914  1.000 13.52610  ? 97   SER   A N    1 
ATOM   3002 C  CA   . SER   B 2 92  ? 12.01955  -11.25133 21.45219  1.000 19.46477  ? 97   SER   A CA   1 
ATOM   3003 C  C    . SER   B 2 92  ? 10.94742  -10.89834 22.46906  1.000 16.41465  ? 97   SER   A C    1 
ATOM   3004 O  O    . SER   B 2 92  ? 10.38041  -11.79534 23.10205  1.000 17.10532  ? 97   SER   A O    1 
ATOM   3005 C  CB   . SER   B 2 92  ? 13.37848  -11.35920 22.14234  1.000 22.87881  ? 97   SER   A CB   1 
ATOM   3006 O  OG   . SER   B 2 92  ? 14.39060  -11.64918 21.19447  1.000 30.79351  ? 97   SER   A OG   1 
ATOM   3007 N  N    . ASP   B 2 93  ? 10.65031  -9.61435  22.63795  1.000 17.01919  ? 98   ASP   A N    1 
ATOM   3008 C  CA   . ASP   B 2 93  ? 9.67518   -9.17536  23.62682  1.000 17.59541  ? 98   ASP   A CA   1 
ATOM   3009 C  C    . ASP   B 2 93  ? 8.27523   -9.02449  23.05067  1.000 19.85157  ? 98   ASP   A C    1 
ATOM   3010 O  O    . ASP   B 2 93  ? 7.41012   -8.44851  23.71054  1.000 17.64204  ? 98   ASP   A O    1 
ATOM   3011 C  CB   . ASP   B 2 93  ? 10.11602  -7.84930  24.25580  1.000 18.03442  ? 98   ASP   A CB   1 
ATOM   3012 C  CG   . ASP   B 2 93  ? 9.95905   -6.66536  23.30671  1.000 21.66221  ? 98   ASP   A CG   1 
ATOM   3013 O  OD1  . ASP   B 2 93  ? 9.59419   -6.86545  22.12069  1.000 18.17606  ? 98   ASP   A OD1  1 
ATOM   3014 O  OD2  . ASP   B 2 93  ? 10.19292  -5.52232  23.75268  1.000 19.16690  ? 98   ASP   A OD2  1 
ATOM   3015 N  N    . SER   B 2 94  ? 8.04239   -9.48157  21.82367  1.000 14.96891  ? 99   SER   A N    1 
ATOM   3016 C  CA   . SER   B 2 94  ? 6.72346   -9.50469  21.20853  1.000 18.36453  ? 99   SER   A CA   1 
ATOM   3017 C  C    . SER   B 2 94  ? 6.17440   -8.11975  20.89939  1.000 21.06147  ? 99   SER   A C    1 
ATOM   3018 O  O    . SER   B 2 94  ? 4.99643   -8.00784  20.54126  1.000 20.96684  ? 99   SER   A O    1 
ATOM   3019 C  CB   . SER   B 2 94  ? 5.70642   -10.25271 22.08246  1.000 13.44937  ? 99   SER   A CB   1 
ATOM   3020 O  OG   . SER   B 2 94  ? 6.07649   -11.60868 22.24657  1.000 17.28556  ? 99   SER   A OG   1 
ATOM   3021 N  N    . ASN   B 2 95  ? 6.97832   -7.05569  21.00442  1.000 15.70562  ? 100  ASN   A N    1 
ATOM   3022 C  CA   . ASN   B 2 95  ? 6.42326   -5.72574  20.76028  1.000 25.33916  ? 100  ASN   A CA   1 
ATOM   3023 C  C    . ASN   B 2 95  ? 6.70337   -5.16680  19.36928  1.000 18.72004  ? 100  ASN   A C    1 
ATOM   3024 O  O    . ASN   B 2 95  ? 6.02135   -4.21886  18.95716  1.000 21.20530  ? 100  ASN   A O    1 
ATOM   3025 C  CB   . ASN   B 2 95  ? 6.92108   -4.73265  21.81628  1.000 20.74578  ? 100  ASN   A CB   1 
ATOM   3026 C  CG   . ASN   B 2 95  ? 6.20895   -4.90462  23.14821  1.000 26.24441  ? 100  ASN   A CG   1 
ATOM   3027 O  OD1  . ASN   B 2 95  ? 4.98895   -5.08570  23.19509  1.000 28.36792  ? 100  ASN   A OD1  1 
ATOM   3028 N  ND2  . ASN   B 2 95  ? 6.97083   -4.86351  24.23529  1.000 26.90182  ? 100  ASN   A ND2  1 
ATOM   3029 N  N    . LEU   B 2 96  ? 7.65749   -5.72777  18.63542  1.000 17.47556  ? 101  LEU   A N    1 
ATOM   3030 C  CA   . LEU   B 2 96  ? 8.01660   -5.25482  17.30543  1.000 17.91306  ? 101  LEU   A CA   1 
ATOM   3031 C  C    . LEU   B 2 96  ? 7.86678   -6.36889  16.27547  1.000 14.97652  ? 101  LEU   A C    1 
ATOM   3032 O  O    . LEU   B 2 96  ? 7.92883   -7.56087  16.59355  1.000 12.28500  ? 101  LEU   A O    1 
ATOM   3033 C  CB   . LEU   B 2 96  ? 9.46957   -4.74773  17.26256  1.000 17.90254  ? 101  LEU   A CB   1 
ATOM   3034 C  CG   . LEU   B 2 96  ? 9.94639   -3.64965  18.22155  1.000 18.18448  ? 101  LEU   A CG   1 
ATOM   3035 C  CD1  . LEU   B 2 96  ? 11.40840  -3.34756  17.96269  1.000 14.84964  ? 101  LEU   A CD1  1 
ATOM   3036 C  CD2  . LEU   B 2 96  ? 9.10833   -2.38471  18.06838  1.000 17.54697  ? 101  LEU   A CD2  1 
ATOM   3037 N  N    . LEU   B 2 97  ? 7.71289   -5.95897  15.02143  1.000 14.76480  ? 102  LEU   A N    1 
ATOM   3038 C  CA   . LEU   B 2 97  ? 7.81907   -6.84903  13.87450  1.000 15.40790  ? 102  LEU   A CA   1 
ATOM   3039 C  C    . LEU   B 2 97  ? 8.82814   -6.27102  12.89957  1.000 17.99031  ? 102  LEU   A C    1 
ATOM   3040 O  O    . LEU   B 2 97  ? 9.03506   -5.05301  12.84453  1.000 13.87565  ? 102  LEU   A O    1 
ATOM   3041 C  CB   . LEU   B 2 97  ? 6.48016   -7.03516  13.13236  1.000 11.44787  ? 102  LEU   A CB   1 
ATOM   3042 C  CG   . LEU   B 2 97  ? 5.39915   -7.87119  13.79829  1.000 19.53988  ? 102  LEU   A CG   1 
ATOM   3043 C  CD1  . LEU   B 2 97  ? 4.02521   -7.65232  13.10513  1.000 12.42968  ? 102  LEU   A CD1  1 
ATOM   3044 C  CD2  . LEU   B 2 97  ? 5.81125   -9.33817  13.74742  1.000 12.90837  ? 102  LEU   A CD2  1 
ATOM   3045 N  N    . VAL   B 2 98  ? 9.44828   -7.15602  12.12469  1.000 13.50960  ? 103  VAL   A N    1 
ATOM   3046 C  CA   . VAL   B 2 98  ? 10.17938  -6.76504  10.92574  1.000 15.55333  ? 103  VAL   A CA   1 
ATOM   3047 C  C    . VAL   B 2 98  ? 9.59456   -7.54214  9.75472   1.000 14.31102  ? 103  VAL   A C    1 
ATOM   3048 O  O    . VAL   B 2 98  ? 9.24362   -8.71716  9.89175   1.000 15.63169  ? 103  VAL   A O    1 
ATOM   3049 C  CB   . VAL   B 2 98  ? 11.70738  -6.98993  11.05492  1.000 16.19140  ? 103  VAL   A CB   1 
ATOM   3050 C  CG1  . VAL   B 2 98  ? 12.05844  -8.43588  11.41904  1.000 9.18809   ? 103  VAL   A CG1  1 
ATOM   3051 C  CG2  . VAL   B 2 98  ? 12.43349  -6.55895  9.77197   1.000 12.13382  ? 103  VAL   A CG2  1 
ATOM   3052 N  N    . SER   B 2 99  ? 9.44664   -6.86821  8.62267   1.000 12.98936  ? 104  SER   A N    1 
ATOM   3053 C  CA   . SER   B 2 99  ? 8.96781   -7.47631  7.39365   1.000 11.24416  ? 104  SER   A CA   1 
ATOM   3054 C  C    . SER   B 2 99  ? 9.99191   -7.26631  6.28775   1.000 15.92762  ? 104  SER   A C    1 
ATOM   3055 O  O    . SER   B 2 99  ? 10.70585  -6.25626  6.26677   1.000 16.82371  ? 104  SER   A O    1 
ATOM   3056 C  CB   . SER   B 2 99  ? 7.61882   -6.87743  6.96448   1.000 13.29098  ? 104  SER   A CB   1 
ATOM   3057 O  OG   . SER   B 2 99  ? 7.67472   -5.45443  6.93940   1.000 13.81300  ? 104  SER   A OG   1 
ATOM   3058 N  N    . ALA   B 2 100 ? 10.05308  -8.22136  5.36281   1.000 12.49804  ? 105  ALA   A N    1 
ATOM   3059 C  CA   . ALA   B 2 100 ? 10.91520  -8.14336  4.18690   1.000 12.73546  ? 105  ALA   A CA   1 
ATOM   3060 C  C    . ALA   B 2 100 ? 10.04133  -8.14449  2.93681   1.000 11.76892  ? 105  ALA   A C    1 
ATOM   3061 O  O    . ALA   B 2 100 ? 9.18141   -9.01656  2.77576   1.000 12.28317  ? 105  ALA   A O    1 
ATOM   3062 C  CB   . ALA   B 2 100 ? 11.90228  -9.31530  4.14707   1.000 10.04096  ? 105  ALA   A CB   1 
ATOM   3063 N  N    . SER   B 2 101 ? 10.27737  -7.20253  2.03478   1.000 13.06189  ? 106  SER   A N    1 
ATOM   3064 C  CA   . SER   B 2 101 ? 9.33447   -6.96965  0.94866   1.000 13.12052  ? 106  SER   A CA   1 
ATOM   3065 C  C    . SER   B 2 101 ? 10.00862  -7.04268  -0.41426  1.000 15.08714  ? 106  SER   A C    1 
ATOM   3066 O  O    . SER   B 2 101 ? 11.21062  -6.78161  -0.56314  1.000 11.94204  ? 106  SER   A O    1 
ATOM   3067 C  CB   . SER   B 2 101 ? 8.64036   -5.60169  1.09251   1.000 12.22649  ? 106  SER   A CB   1 
ATOM   3068 O  OG   . SER   B 2 101 ? 7.79246   -5.33081  -0.02059  1.000 9.20729   ? 106  SER   A OG   1 
ATOM   3069 N  N    . ASP   B 2 102 ? 9.19475   -7.40379  -1.40933  1.000 14.87968  ? 107  ASP   A N    1 
ATOM   3070 C  CA   . ASP   B 2 102 ? 9.57489   -7.27984  -2.81029  1.000 18.26975  ? 107  ASP   A CA   1 
ATOM   3071 C  C    . ASP   B 2 102 ? 9.85684   -5.84085  -3.21634  1.000 16.12929  ? 107  ASP   A C    1 
ATOM   3072 O  O    . ASP   B 2 102 ? 10.47994  -5.61886  -4.26129  1.000 18.87952  ? 107  ASP   A O    1 
ATOM   3073 C  CB   . ASP   B 2 102 ? 8.46902   -7.84897  -3.69038  1.000 13.76004  ? 107  ASP   A CB   1 
ATOM   3074 C  CG   . ASP   B 2 102 ? 8.44012   -9.35297  -3.66430  1.000 30.31312  ? 107  ASP   A CG   1 
ATOM   3075 O  OD1  . ASP   B 2 102 ? 9.38822   -9.97293  -4.17716  1.000 46.28233  ? 107  ASP   A OD1  1 
ATOM   3076 O  OD2  . ASP   B 2 102 ? 7.49710   -9.92100  -3.10337  1.000 26.10391  ? 107  ASP   A OD2  1 
ATOM   3077 N  N    . ASP   B 2 103 ? 9.40069   -4.86383  -2.43245  1.000 11.90705  ? 108  ASP   A N    1 
ATOM   3078 C  CA   . ASP   B 2 103 ? 9.73863   -3.47883  -2.70849  1.000 12.96714  ? 108  ASP   A CA   1 
ATOM   3079 C  C    . ASP   B 2 103 ? 11.19157  -3.14771  -2.34035  1.000 16.37687  ? 108  ASP   A C    1 
ATOM   3080 O  O    . ASP   B 2 103 ? 11.54450  -1.97069  -2.41838  1.000 16.15311  ? 108  ASP   A O    1 
ATOM   3081 C  CB   . ASP   B 2 103 ? 8.75949   -2.52785  -2.00065  1.000 13.68802  ? 108  ASP   A CB   1 
ATOM   3082 C  CG   . ASP   B 2 103 ? 8.89732   -2.52676  -0.45863  1.000 18.52234  ? 108  ASP   A CG   1 
ATOM   3083 O  OD1  . ASP   B 2 103 ? 9.89230   -3.04966  0.10151   1.000 18.31059  ? 108  ASP   A OD1  1 
ATOM   3084 O  OD2  . ASP   B 2 103 ? 7.98922   -1.97478  0.20324   1.000 19.05093  ? 108  ASP   A OD2  1 
ATOM   3085 N  N    . LYS   B 2 104 ? 12.01159  -4.12763  -1.95521  1.000 13.36467  ? 109  LYS   A N    1 
ATOM   3086 C  CA   . LYS   B 2 104 ? 13.45456  -4.00653  -1.76006  1.000 12.16583  ? 109  LYS   A CA   1 
ATOM   3087 C  C    . LYS   B 2 104 ? 13.81238  -3.43343  -0.39905  1.000 13.21020  ? 109  LYS   A C    1 
ATOM   3088 O  O    . LYS   B 2 104 ? 15.01333  -3.15033  -0.12594  1.000 10.77988  ? 109  LYS   A O    1 
ATOM   3089 C  CB   . LYS   B 2 104 ? 14.10862  -3.15355  -2.85004  1.000 14.87447  ? 109  LYS   A CB   1 
ATOM   3090 C  CG   . LYS   B 2 104 ? 13.81981  -3.65464  -4.25804  1.000 18.26697  ? 109  LYS   A CG   1 
ATOM   3091 C  CD   . LYS   B 2 104 ? 14.78887  -3.04364  -5.27597  1.000 17.75877  ? 109  LYS   A CD   1 
ATOM   3092 C  CE   . LYS   B 2 104 ? 14.34383  -1.66969  -5.70609  1.000 27.93429  ? 109  LYS   A CE   1 
ATOM   3093 N  NZ   . LYS   B 2 104 ? 14.87596  -1.35873  -7.06805  1.000 34.83822  ? 109  LYS   A NZ   1 
ATOM   3094 N  N    . THR   B 2 105 ? 12.83227  -3.24244  0.47383   1.000 13.73843  ? 110  THR   A N    1 
ATOM   3095 C  CA   . THR   B 2 105 ? 13.10209  -2.75035  1.81183   1.000 12.01787  ? 110  THR   A CA   1 
ATOM   3096 C  C    . THR   B 2 105 ? 12.61105  -3.76033  2.83184   1.000 17.29318  ? 110  THR   A C    1 
ATOM   3097 O  O    . THR   B 2 105 ? 11.82815  -4.66240  2.52080   1.000 17.50602  ? 110  THR   A O    1 
ATOM   3098 C  CB   . THR   B 2 105 ? 12.39698  -1.41138  2.08368   1.000 15.59931  ? 110  THR   A CB   1 
ATOM   3099 O  OG1  . THR   B 2 105 ? 11.00397  -1.66746  2.31355   1.000 15.85734  ? 110  THR   A OG1  1 
ATOM   3100 C  CG2  . THR   B 2 105 ? 12.53804  -0.48244  0.90665   1.000 10.82724  ? 110  THR   A CG2  1 
ATOM   3101 N  N    . LEU   B 2 106 ? 13.07291  -3.58223  4.05988   1.000 11.89822  ? 111  LEU   A N    1 
ATOM   3102 C  CA   . LEU   B 2 106 ? 12.42082  -4.13621  5.23084   1.000 9.76248   ? 111  LEU   A CA   1 
ATOM   3103 C  C    . LEU   B 2 106 ? 11.80966  -2.98620  6.02571   1.000 15.33921  ? 111  LEU   A C    1 
ATOM   3104 O  O    . LEU   B 2 106 ? 12.23559  -1.82918  5.91169   1.000 13.42192  ? 111  LEU   A O    1 
ATOM   3105 C  CB   . LEU   B 2 106 ? 13.40978  -4.92609  6.10699   1.000 12.17614  ? 111  LEU   A CB   1 
ATOM   3106 C  CG   . LEU   B 2 106 ? 14.28392  -6.01407  5.46514   1.000 8.76675   ? 111  LEU   A CG   1 
ATOM   3107 C  CD1  . LEU   B 2 106 ? 15.65193  -5.49700  5.07326   1.000 13.58866  ? 111  LEU   A CD1  1 
ATOM   3108 C  CD2  . LEU   B 2 106 ? 14.40590  -7.21701  6.41522   1.000 10.01394  ? 111  LEU   A CD2  1 
ATOM   3109 N  N    . LYS   B 2 107 ? 10.79759  -3.30722  6.82862   1.000 13.08933  ? 112  LYS   A N    1 
ATOM   3110 C  CA   . LYS   B 2 107 ? 10.18843  -2.32022  7.70650   1.000 16.30706  ? 112  LYS   A CA   1 
ATOM   3111 C  C    . LYS   B 2 107 ? 10.13932  -2.86514  9.11952   1.000 17.91691  ? 112  LYS   A C    1 
ATOM   3112 O  O    . LYS   B 2 107 ? 9.90237   -4.06114  9.32756   1.000 17.52499  ? 112  LYS   A O    1 
ATOM   3113 C  CB   . LYS   B 2 107 ? 8.77546   -1.91434  7.22932   1.000 12.53920  ? 112  LYS   A CB   1 
ATOM   3114 C  CG   . LYS   B 2 107 ? 8.83051   -0.86339  6.12227   1.000 12.05268  ? 112  LYS   A CG   1 
ATOM   3115 C  CD   . LYS   B 2 107 ? 7.53358   -0.72652  5.32912   1.000 13.08709  ? 112  LYS   A CD   1 
ATOM   3116 C  CE   . LYS   B 2 107 ? 7.68863   0.33342   4.21608   1.000 15.65436  ? 112  LYS   A CE   1 
ATOM   3117 N  NZ   . LYS   B 2 107 ? 7.86648   1.72447   4.77702   1.000 14.67242  ? 112  LYS   A NZ   1 
ATOM   3118 N  N    . ILE   B 2 108 ? 10.42016  -1.98307  10.08150  1.000 15.55314  ? 113  ILE   A N    1 
ATOM   3119 C  CA   . ILE   B 2 108 ? 10.28702  -2.28100  11.50051  1.000 17.23781  ? 113  ILE   A CA   1 
ATOM   3120 C  C    . ILE   B 2 108 ? 9.00493   -1.62906  11.97433  1.000 19.65487  ? 113  ILE   A C    1 
ATOM   3121 O  O    . ILE   B 2 108 ? 8.77188   -0.43909  11.70924  1.000 17.12943  ? 113  ILE   A O    1 
ATOM   3122 C  CB   . ILE   B 2 108 ? 11.49290  -1.76987  12.30561  1.000 17.33194  ? 113  ILE   A CB   1 
ATOM   3123 C  CG1  . ILE   B 2 108 ? 12.80900  -2.25382  11.69677  1.000 21.38761  ? 113  ILE   A CG1  1 
ATOM   3124 C  CG2  . ILE   B 2 108 ? 11.41778  -2.24280  13.74762  1.000 14.59592  ? 113  ILE   A CG2  1 
ATOM   3125 C  CD1  . ILE   B 2 108 ? 14.02188  -1.89169  12.55388  1.000 17.32256  ? 113  ILE   A CD1  1 
ATOM   3126 N  N    . TRP   B 2 109 ? 8.16791   -2.41007  12.65429  1.000 18.19739  ? 114  TRP   A N    1 
ATOM   3127 C  CA   . TRP   B 2 109 ? 6.83584   -1.98914  13.06712  1.000 16.41364  ? 114  TRP   A CA   1 
ATOM   3128 C  C    . TRP   B 2 109 ? 6.69868   -2.08506  14.57411  1.000 17.26399  ? 114  TRP   A C    1 
ATOM   3129 O  O    . TRP   B 2 109 ? 7.17068   -3.04700  15.18621  1.000 12.07505  ? 114  TRP   A O    1 
ATOM   3130 C  CB   . TRP   B 2 109 ? 5.75196   -2.86625  12.45305  1.000 12.75764  ? 114  TRP   A CB   1 
ATOM   3131 C  CG   . TRP   B 2 109 ? 5.86313   -3.12832  10.99208  1.000 12.30895  ? 114  TRP   A CG   1 
ATOM   3132 C  CD1  . TRP   B 2 109 ? 6.51627   -4.16831  10.39321  1.000 15.91192  ? 114  TRP   A CD1  1 
ATOM   3133 C  CD2  . TRP   B 2 109 ? 5.25320   -2.37442  9.93697   1.000 16.39073  ? 114  TRP   A CD2  1 
ATOM   3134 N  NE1  . TRP   B 2 109 ? 6.36041   -4.09840  9.02419   1.000 16.16796  ? 114  TRP   A NE1  1 
ATOM   3135 C  CE2  . TRP   B 2 109 ? 5.58337   -3.01247  8.71904   1.000 12.25196  ? 114  TRP   A CE2  1 
ATOM   3136 C  CE3  . TRP   B 2 109 ? 4.46412   -1.21547  9.90282   1.000 14.98158  ? 114  TRP   A CE3  1 
ATOM   3137 C  CZ2  . TRP   B 2 109 ? 5.16047   -2.52456  7.47797   1.000 15.59904  ? 114  TRP   A CZ2  1 
ATOM   3138 C  CZ3  . TRP   B 2 109 ? 4.03722   -0.73657  8.66775   1.000 13.60698  ? 114  TRP   A CZ3  1 
ATOM   3139 C  CH2  . TRP   B 2 109 ? 4.38640   -1.38861  7.47682   1.000 14.64332  ? 114  TRP   A CH2  1 
ATOM   3140 N  N    . ASP   B 2 110 ? 6.03955   -1.09608  15.16798  1.000 21.39794  ? 115  ASP   A N    1 
ATOM   3141 C  CA   . ASP   B 2 110 ? 5.55941   -1.21803  16.53694  1.000 17.50102  ? 115  ASP   A CA   1 
ATOM   3142 C  C    . ASP   B 2 110 ? 4.18946   -1.87812  16.48283  1.000 16.36540  ? 115  ASP   A C    1 
ATOM   3143 O  O    . ASP   B 2 110 ? 3.26049   -1.33522  15.87670  1.000 20.03884  ? 115  ASP   A O    1 
ATOM   3144 C  CB   . ASP   B 2 110 ? 5.48725   0.14200   17.22385  1.000 19.99051  ? 115  ASP   A CB   1 
ATOM   3145 C  CG   . ASP   B 2 110 ? 4.81211   0.07403   18.58779  1.000 21.88658  ? 115  ASP   A CG   1 
ATOM   3146 O  OD1  . ASP   B 2 110 ? 3.56410   0.11495   18.64565  1.000 29.39360  ? 115  ASP   A OD1  1 
ATOM   3147 O  OD2  . ASP   B 2 110 ? 5.52600   -0.03586  19.60287  1.000 27.98127  ? 115  ASP   A OD2  1 
ATOM   3148 N  N    . VAL   B 2 111 ? 4.06447   -3.04610  17.10488  1.000 16.76120  ? 116  VAL   A N    1 
ATOM   3149 C  CA   . VAL   B 2 111 ? 2.84354   -3.82919  16.93979  1.000 21.76121  ? 116  VAL   A CA   1 
ATOM   3150 C  C    . VAL   B 2 111 ? 1.63843   -3.10423  17.54462  1.000 24.58841  ? 116  VAL   A C    1 
ATOM   3151 O  O    . VAL   B 2 111 ? 0.55149   -3.07934  16.94650  1.000 19.71459  ? 116  VAL   A O    1 
ATOM   3152 C  CB   . VAL   B 2 111 ? 3.03457   -5.23714  17.53989  1.000 21.14213  ? 116  VAL   A CB   1 
ATOM   3153 C  CG1  . VAL   B 2 111 ? 1.79165   -6.08324  17.32381  1.000 17.96944  ? 116  VAL   A CG1  1 
ATOM   3154 C  CG2  . VAL   B 2 111 ? 4.21469   -5.92210  16.89206  1.000 22.29865  ? 116  VAL   A CG2  1 
ATOM   3155 N  N    . SER   B 2 112 ? 1.80326   -2.50816  18.73261  1.000 25.30759  ? 117  SER   A N    1 
ATOM   3156 C  CA   . SER   B 2 112 ? 0.66915   -1.87319  19.41345  1.000 27.47572  ? 117  SER   A CA   1 
ATOM   3157 C  C    . SER   B 2 112 ? 0.05317   -0.77328  18.56032  1.000 20.89332  ? 117  SER   A C    1 
ATOM   3158 O  O    . SER   B 2 112 ? -1.15681  -0.76838  18.31419  1.000 19.10440  ? 117  SER   A O    1 
ATOM   3159 C  CB   . SER   B 2 112 ? 1.10196   -1.30509  20.76946  1.000 24.17964  ? 117  SER   A CB   1 
ATOM   3160 O  OG   . SER   B 2 112 ? 1.71694   -2.29200  21.56959  1.000 32.84261  ? 117  SER   A OG   1 
ATOM   3161 N  N    . SER   B 2 113 ? 0.87515   0.17475   18.10436  1.000 18.40282  ? 118  SER   A N    1 
ATOM   3162 C  CA   . SER   B 2 113 ? 0.38516   1.29667   17.31324  1.000 26.08696  ? 118  SER   A CA   1 
ATOM   3163 C  C    . SER   B 2 113 ? 0.15934   0.95157   15.84624  1.000 23.63834  ? 118  SER   A C    1 
ATOM   3164 O  O    . SER   B 2 113 ? -0.56863  1.67949   15.16112  1.000 21.66055  ? 118  SER   A O    1 
ATOM   3165 C  CB   . SER   B 2 113 ? 1.37608   2.45974   17.39028  1.000 24.62663  ? 118  SER   A CB   1 
ATOM   3166 O  OG   . SER   B 2 113 ? 2.59417   2.12078   16.73543  1.000 21.35405  ? 118  SER   A OG   1 
ATOM   3167 N  N    . GLY   B 2 114 ? 0.80147   -0.10041  15.33037  1.000 22.30938  ? 119  GLY   A N    1 
ATOM   3168 C  CA   . GLY   B 2 114 ? 0.75364   -0.37050  13.90338  1.000 21.45247  ? 119  GLY   A CA   1 
ATOM   3169 C  C    . GLY   B 2 114 ? 1.60967   0.53051   13.03142  1.000 18.13534  ? 119  GLY   A C    1 
ATOM   3170 O  O    . GLY   B 2 114 ? 1.55081   0.40944   11.80542  1.000 17.36913  ? 119  GLY   A O    1 
ATOM   3171 N  N    . LYS   B 2 115 ? 2.42255   1.41060   13.61346  1.000 19.22116  ? 120  LYS   A N    1 
ATOM   3172 C  CA   . LYS   B 2 115 ? 3.19957   2.35861   12.82649  1.000 20.45746  ? 120  LYS   A CA   1 
ATOM   3173 C  C    . LYS   B 2 115 ? 4.55466   1.79867   12.39566  1.000 19.62880  ? 120  LYS   A C    1 
ATOM   3174 O  O    . LYS   B 2 115 ? 5.15464   0.95175   13.06777  1.000 13.69486  ? 120  LYS   A O    1 
ATOM   3175 C  CB   . LYS   B 2 115 ? 3.39540   3.65966   13.60743  1.000 26.52455  ? 120  LYS   A CB   1 
ATOM   3176 C  CG   . LYS   B 2 115 ? 2.23736   4.64957   13.39625  1.000 36.40642  ? 120  LYS   A CG   1 
ATOM   3177 C  CD   . LYS   B 2 115 ? 1.96517   5.51662   14.61818  1.000 37.17370  ? 120  LYS   A CD   1 
ATOM   3178 C  CE   . LYS   B 2 115 ? 0.62414   6.24853   14.48999  1.000 40.23829  ? 120  LYS   A CE   1 
ATOM   3179 N  NZ   . LYS   B 2 115 ? -0.53080  5.29645   14.46892  1.000 49.45786  ? 120  LYS   A NZ   1 
ATOM   3180 N  N    . CYS   B 2 116 ? 5.03075   2.29964   11.25669  1.000 17.86140  ? 121  CYS   A N    1 
ATOM   3181 C  CA   . CYS   B 2 116 ? 6.36082   1.99070   10.73685  1.000 18.64720  ? 121  CYS   A CA   1 
ATOM   3182 C  C    . CYS   B 2 116 ? 7.38969   2.86781   11.44191  1.000 21.82698  ? 121  CYS   A C    1 
ATOM   3183 O  O    . CYS   B 2 116 ? 7.38862   4.09580   11.28284  1.000 21.42456  ? 121  CYS   A O    1 
ATOM   3184 C  CB   . CYS   B 2 116 ? 6.40197   2.20462   9.22484   1.000 12.84445  ? 121  CYS   A CB   1 
ATOM   3185 S  SG   . CYS   B 2 116 ? 8.04107   1.93969   8.49503   1.000 19.26658  ? 121  CYS   A SG   1 
ATOM   3186 N  N    . LEU   B 2 117 ? 8.26765   2.23591   12.22404  1.000 22.77733  ? 122  LEU   A N    1 
ATOM   3187 C  CA   . LEU   B 2 117 ? 9.30452   2.94602   12.96411  1.000 21.23201  ? 122  LEU   A CA   1 
ATOM   3188 C  C    . LEU   B 2 117 ? 10.50559  3.24505   12.07922  1.000 21.87454  ? 122  LEU   A C    1 
ATOM   3189 O  O    . LEU   B 2 117 ? 11.10851  4.31809   12.18523  1.000 21.00844  ? 122  LEU   A O    1 
ATOM   3190 C  CB   . LEU   B 2 117 ? 9.75444   2.12212   14.17520  1.000 20.54988  ? 122  LEU   A CB   1 
ATOM   3191 C  CG   . LEU   B 2 117 ? 8.71137   1.64810   15.19312  1.000 24.20156  ? 122  LEU   A CG   1 
ATOM   3192 C  CD1  . LEU   B 2 117 ? 9.38929   0.88121   16.33723  1.000 21.97408  ? 122  LEU   A CD1  1 
ATOM   3193 C  CD2  . LEU   B 2 117 ? 7.87523   2.81908   15.74096  1.000 21.43495  ? 122  LEU   A CD2  1 
ATOM   3194 N  N    . LYS   B 2 118 ? 10.87075  2.30102   11.21431  1.000 23.57394  ? 123  LYS   A N    1 
ATOM   3195 C  CA   . LYS   B 2 118 ? 12.04783  2.42706   10.36843  1.000 23.00146  ? 123  LYS   A CA   1 
ATOM   3196 C  C    . LYS   B 2 118 ? 11.79602  1.67597   9.07145   1.000 14.42686  ? 123  LYS   A C    1 
ATOM   3197 O  O    . LYS   B 2 118 ? 11.12809  0.63892   9.05243   1.000 14.75259  ? 123  LYS   A O    1 
ATOM   3198 C  CB   . LYS   B 2 118 ? 13.31680  1.86518   11.05160  1.000 17.70591  ? 123  LYS   A CB   1 
ATOM   3199 C  CG   . LYS   B 2 118 ? 13.71061  2.52228   12.36460  1.000 21.38334  ? 123  LYS   A CG   1 
ATOM   3200 C  CD   . LYS   B 2 118 ? 14.23455  3.91730   12.11558  1.000 27.02942  ? 123  LYS   A CD   1 
ATOM   3201 C  CE   . LYS   B 2 118 ? 14.71137  4.56640   13.39260  1.000 29.32941  ? 123  LYS   A CE   1 
ATOM   3202 N  NZ   . LYS   B 2 118 ? 14.87329  6.03340   13.19853  1.000 32.32548  ? 123  LYS   A NZ   1 
ATOM   3203 N  N    . THR   B 2 119 ? 12.34310  2.20694   7.98548   1.000 19.23797  ? 124  THR   A N    1 
ATOM   3204 C  CA   . THR   B 2 119 ? 12.42729  1.50288   6.71052   1.000 17.02484  ? 124  THR   A CA   1 
ATOM   3205 C  C    . THR   B 2 119 ? 13.90033  1.25996   6.42770   1.000 19.88751  ? 124  THR   A C    1 
ATOM   3206 O  O    . THR   B 2 119 ? 14.69327  2.20801   6.42473   1.000 18.64913  ? 124  THR   A O    1 
ATOM   3207 C  CB   . THR   B 2 119 ? 11.78335  2.31977   5.59241   1.000 19.72813  ? 124  THR   A CB   1 
ATOM   3208 O  OG1  . THR   B 2 119 ? 10.43229  2.60270   5.95425   1.000 16.95345  ? 124  THR   A OG1  1 
ATOM   3209 C  CG2  . THR   B 2 119 ? 11.80155  1.54270   4.25645   1.000 16.47789  ? 124  THR   A CG2  1 
ATOM   3210 N  N    . LEU   B 2 120 ? 14.27544  -0.00403  6.22781   1.000 24.04835  ? 125  LEU   A N    1 
ATOM   3211 C  CA   . LEU   B 2 120 ? 15.66949  -0.36195  5.97998   1.000 17.86587  ? 125  LEU   A CA   1 
ATOM   3212 C  C    . LEU   B 2 120 ? 15.89965  -0.42402  4.48100   1.000 17.10875  ? 125  LEU   A C    1 
ATOM   3213 O  O    . LEU   B 2 120 ? 15.32978  -1.28209  3.78999   1.000 22.09850  ? 125  LEU   A O    1 
ATOM   3214 C  CB   . LEU   B 2 120 ? 16.02951  -1.69689  6.62909   1.000 19.15967  ? 125  LEU   A CB   1 
ATOM   3215 C  CG   . LEU   B 2 120 ? 15.51537  -1.88984  8.05804   1.000 24.63511  ? 125  LEU   A CG   1 
ATOM   3216 C  CD1  . LEU   B 2 120 ? 16.04139  -3.18877  8.65817   1.000 13.23792  ? 125  LEU   A CD1  1 
ATOM   3217 C  CD2  . LEU   B 2 120 ? 15.87120  -0.69777  8.91702   1.000 14.87641  ? 125  LEU   A CD2  1 
ATOM   3218 N  N    . LYS   B 2 121 ? 16.73865  0.47001   3.97704   1.000 15.55575  ? 126  LYS   A N    1 
ATOM   3219 C  CA   . LYS   B 2 121 ? 16.97179  0.59395   2.54706   1.000 19.35031  ? 126  LYS   A CA   1 
ATOM   3220 C  C    . LYS   B 2 121 ? 18.43184  0.29403   2.25724   1.000 25.83017  ? 126  LYS   A C    1 
ATOM   3221 O  O    . LYS   B 2 121 ? 19.31774  0.78613   2.96630   1.000 19.14774  ? 126  LYS   A O    1 
ATOM   3222 C  CB   . LYS   B 2 121 ? 16.59176  1.98789   2.04094   1.000 21.46379  ? 126  LYS   A CB   1 
ATOM   3223 C  CG   . LYS   B 2 121 ? 15.07676  2.17178   1.85677   1.000 32.24503  ? 126  LYS   A CG   1 
ATOM   3224 C  CD   . LYS   B 2 121 ? 14.73978  3.36671   0.95767   1.000 35.58693  ? 126  LYS   A CD   1 
ATOM   3225 C  CE   . LYS   B 2 121 ? 13.28984  3.31258   0.42752   1.000 46.66351  ? 126  LYS   A CE   1 
ATOM   3226 N  NZ   . LYS   B 2 121 ? 13.11203  2.51950   -0.84546  1.000 31.93485  ? 126  LYS   A NZ   1 
ATOM   3227 N  N    . GLY   B 2 122 ? 18.67401  -0.51402  1.22131   1.000 16.38989  ? 127  GLY   A N    1 
ATOM   3228 C  CA   . GLY   B 2 122 ? 20.02107  -0.89695  0.85147   1.000 17.81821  ? 127  GLY   A CA   1 
ATOM   3229 C  C    . GLY   B 2 122 ? 20.07526  -2.06400  -0.11046  1.000 22.54880  ? 127  GLY   A C    1 
ATOM   3230 O  O    . GLY   B 2 122 ? 20.92535  -2.09299  -1.00736  1.000 16.97266  ? 127  GLY   A O    1 
ATOM   3231 N  N    . HIS   B 2 123 ? 19.19230  -3.04704  0.07350   1.000 20.49822  ? 128  HIS   A N    1 
ATOM   3232 C  CA   . HIS   B 2 123 ? 19.12948  -4.13810  -0.88444  1.000 17.91407  ? 128  HIS   A CA   1 
ATOM   3233 C  C    . HIS   B 2 123 ? 18.76859  -3.60020  -2.26051  1.000 14.58474  ? 128  HIS   A C    1 
ATOM   3234 O  O    . HIS   B 2 123 ? 17.99054  -2.65226  -2.39665  1.000 13.04352  ? 128  HIS   A O    1 
ATOM   3235 C  CB   . HIS   B 2 123 ? 18.12150  -5.18814  -0.44349  1.000 12.53671  ? 128  HIS   A CB   1 
ATOM   3236 C  CG   . HIS   B 2 123 ? 18.67145  -6.14505  0.56262   1.000 15.42695  ? 128  HIS   A CG   1 
ATOM   3237 N  ND1  . HIS   B 2 123 ? 19.74354  -6.96700  0.28878   1.000 9.00353   ? 128  HIS   A ND1  1 
ATOM   3238 C  CD2  . HIS   B 2 123 ? 18.31133  -6.40100  1.84360   1.000 9.58292   ? 128  HIS   A CD2  1 
ATOM   3239 C  CE1  . HIS   B 2 123 ? 20.01347  -7.69992  1.35785   1.000 13.87673  ? 128  HIS   A CE1  1 
ATOM   3240 N  NE2  . HIS   B 2 123 ? 19.16335  -7.37092  2.31474   1.000 12.30674  ? 128  HIS   A NE2  1 
ATOM   3241 N  N    . SER   B 2 124 ? 19.35874  -4.19622  -3.28541  1.000 12.72844  ? 129  SER   A N    1 
ATOM   3242 C  CA   . SER   B 2 124 ? 19.13985  -3.73531  -4.64146  1.000 15.02315  ? 129  SER   A CA   1 
ATOM   3243 C  C    . SER   B 2 124 ? 18.08398  -4.55142  -5.36053  1.000 15.63202  ? 129  SER   A C    1 
ATOM   3244 O  O    . SER   B 2 124 ? 17.85410  -4.32550  -6.55157  1.000 13.45030  ? 129  SER   A O    1 
ATOM   3245 C  CB   . SER   B 2 124 ? 20.45794  -3.73627  -5.41432  1.000 15.39154  ? 129  SER   A CB   1 
ATOM   3246 O  OG   . SER   B 2 124 ? 21.03102  -5.02323  -5.42019  1.000 20.68323  ? 129  SER   A OG   1 
ATOM   3247 N  N    . ASN   B 2 125 ? 17.43797  -5.48943  -4.66755  1.000 13.40212  ? 130  ASN   A N    1 
ATOM   3248 C  CA   . ASN   B 2 125 ? 16.32708  -6.24753  -5.22663  1.000 13.47142  ? 130  ASN   A CA   1 
ATOM   3249 C  C    . ASN   B 2 125 ? 15.52600  -6.85552  -4.06968  1.000 11.71041  ? 130  ASN   A C    1 
ATOM   3250 O  O    . ASN   B 2 125 ? 15.73385  -6.51244  -2.89967  1.000 11.45434  ? 130  ASN   A O    1 
ATOM   3251 C  CB   . ASN   B 2 125 ? 16.82526  -7.29755  -6.22851  1.000 15.31114  ? 130  ASN   A CB   1 
ATOM   3252 C  CG   . ASN   B 2 125 ? 15.83540  -7.51968  -7.35961  1.000 16.79934  ? 130  ASN   A CG   1 
ATOM   3253 O  OD1  . ASN   B 2 125 ? 14.65236  -7.26075  -7.19775  1.000 20.26531  ? 130  ASN   A OD1  1 
ATOM   3254 N  ND2  . ASN   B 2 125 ? 16.31755  -7.96471  -8.51153  1.000 14.20780  ? 130  ASN   A ND2  1 
ATOM   3255 N  N    . TYR   B 2 126 ? 14.59809  -7.74960  -4.40173  1.000 13.36061  ? 131  TYR   A N    1 
ATOM   3256 C  CA   . TYR   B 2 126 ? 13.59902  -8.20361  -3.43281  1.000 16.56226  ? 131  TYR   A CA   1 
ATOM   3257 C  C    . TYR   B 2 126 ? 14.23692  -8.77850  -2.17071  1.000 10.17221  ? 131  TYR   A C    1 
ATOM   3258 O  O    . TYR   B 2 126 ? 15.18898  -9.55344  -2.23456  1.000 8.31370   ? 131  TYR   A O    1 
ATOM   3259 C  CB   . TYR   B 2 126 ? 12.70116  -9.28070  -4.04085  1.000 13.94856  ? 131  TYR   A CB   1 
ATOM   3260 C  CG   . TYR   B 2 126 ? 12.45631  -9.17180  -5.51488  1.000 17.17119  ? 131  TYR   A CG   1 
ATOM   3261 C  CD1  . TYR   B 2 126 ? 11.47830  -8.31590  -6.02403  1.000 16.80089  ? 131  TYR   A CD1  1 
ATOM   3262 C  CD2  . TYR   B 2 126 ? 13.17645  -9.95581  -6.40476  1.000 23.82716  ? 131  TYR   A CD2  1 
ATOM   3263 C  CE1  . TYR   B 2 126 ? 11.24244  -8.22999  -7.38106  1.000 17.08208  ? 131  TYR   A CE1  1 
ATOM   3264 C  CE2  . TYR   B 2 126 ? 12.95260  -9.87690  -7.76178  1.000 28.24440  ? 131  TYR   A CE2  1 
ATOM   3265 C  CZ   . TYR   B 2 126 ? 11.98859  -9.01199  -8.24694  1.000 26.55550  ? 131  TYR   A CZ   1 
ATOM   3266 O  OH   . TYR   B 2 126 ? 11.79173  -8.95208  -9.60096  1.000 28.86496  ? 131  TYR   A OH   1 
ATOM   3267 N  N    . VAL   B 2 127 ? 13.64978  -8.45547  -1.02679  1.000 11.32832  ? 132  VAL   A N    1 
ATOM   3268 C  CA   . VAL   B 2 127 ? 14.04868  -9.01638  0.26128   1.000 10.90111  ? 132  VAL   A CA   1 
ATOM   3269 C  C    . VAL   B 2 127 ? 13.13872  -10.19942 0.57025   1.000 10.82615  ? 132  VAL   A C    1 
ATOM   3270 O  O    . VAL   B 2 127 ? 11.91471  -10.05250 0.59911   1.000 8.38240   ? 132  VAL   A O    1 
ATOM   3271 C  CB   . VAL   B 2 127 ? 13.97849  -7.95632  1.36822   1.000 8.68601   ? 132  VAL   A CB   1 
ATOM   3272 C  CG1  . VAL   B 2 127 ? 14.77638  -8.40020  2.61133   1.000 9.66397   ? 132  VAL   A CG1  1 
ATOM   3273 C  CG2  . VAL   B 2 127 ? 14.50646  -6.64731  0.84420   1.000 9.63897   ? 132  VAL   A CG2  1 
ATOM   3274 N  N    . PHE   B 2 128 ? 13.72378  -11.38037 0.78238   1.000 11.12258  ? 133  PHE   A N    1 
ATOM   3275 C  CA   . PHE   B 2 128 ? 12.94384  -12.59941 0.98537   1.000 10.09715  ? 133  PHE   A CA   1 
ATOM   3276 C  C    . PHE   B 2 128 ? 12.85971  -13.04233 2.43938   1.000 8.69518   ? 133  PHE   A C    1 
ATOM   3277 O  O    . PHE   B 2 128 ? 11.90172  -13.73038 2.80532   1.000 14.76545  ? 133  PHE   A O    1 
ATOM   3278 C  CB   . PHE   B 2 128 ? 13.52000  -13.76542 0.17349   1.000 11.55589  ? 133  PHE   A CB   1 
ATOM   3279 C  CG   . PHE   B 2 128 ? 13.40815  -13.59451 -1.31653  1.000 10.67116  ? 133  PHE   A CG   1 
ATOM   3280 C  CD1  . PHE   B 2 128 ? 12.32017  -12.95161 -1.87968  1.000 11.25751  ? 133  PHE   A CD1  1 
ATOM   3281 C  CD2  . PHE   B 2 128 ? 14.40927  -14.06049 -2.15040  1.000 9.92886   ? 133  PHE   A CD2  1 
ATOM   3282 C  CE1  . PHE   B 2 128 ? 12.22831  -12.80069 -3.25570  1.000 18.34328  ? 133  PHE   A CE1  1 
ATOM   3283 C  CE2  . PHE   B 2 128 ? 14.32841  -13.91657 -3.53241  1.000 11.03535  ? 133  PHE   A CE2  1 
ATOM   3284 C  CZ   . PHE   B 2 128 ? 13.23843  -13.29067 -4.08556  1.000 18.93765  ? 133  PHE   A CZ   1 
ATOM   3285 N  N    . CYS   B 2 129 ? 13.82060  -12.68022 3.28546   1.000 7.05112   ? 134  CYS   A N    1 
ATOM   3286 C  CA   . CYS   B 2 129 ? 13.89149  -13.28414 4.60651   1.000 8.94620   ? 134  CYS   A CA   1 
ATOM   3287 C  C    . CYS   B 2 129 ? 14.43332  -12.27705 5.61051   1.000 10.67252  ? 134  CYS   A C    1 
ATOM   3288 O  O    . CYS   B 2 129 ? 15.22530  -11.39402 5.25954   1.000 8.49613   ? 134  CYS   A O    1 
ATOM   3289 C  CB   . CYS   B 2 129 ? 14.74658  -14.55409 4.55367   1.000 10.69209  ? 134  CYS   A CB   1 
ATOM   3290 S  SG   . CYS   B 2 129 ? 16.31068  -14.39604 3.60083   1.000 13.33988  ? 134  CYS   A SG   1 
ATOM   3291 N  N    . CYS   B 2 130 ? 13.96619  -12.38601 6.85746   1.000 11.49872  ? 135  CYS   A N    1 
ATOM   3292 C  CA   . CYS   B 2 130 ? 14.34102  -11.42393 7.89645   1.000 8.83147   ? 135  CYS   A CA   1 
ATOM   3293 C  C    . CYS   B 2 130 ? 14.19891  -12.06686 9.26747   1.000 9.60100   ? 135  CYS   A C    1 
ATOM   3294 O  O    . CYS   B 2 130 ? 13.42396  -13.00890 9.44844   1.000 11.14308  ? 135  CYS   A O    1 
ATOM   3295 C  CB   . CYS   B 2 130 ? 13.48994  -10.15899 7.82729   1.000 8.72952   ? 135  CYS   A CB   1 
ATOM   3296 S  SG   . CYS   B 2 130 ? 11.70095  -10.46611 7.89711   1.000 13.49940  ? 135  CYS   A SG   1 
ATOM   3297 N  N    . ASN   B 2 131 ? 14.94177  -11.52776 10.23752  1.000 10.55094  ? 136  ASN   A N    1 
ATOM   3298 C  CA   . ASN   B 2 131 ? 14.86665  -11.97769 11.62354  1.000 11.88685  ? 136  ASN   A CA   1 
ATOM   3299 C  C    . ASN   B 2 131 ? 15.55249  -10.97459 12.54256  1.000 15.47591  ? 136  ASN   A C    1 
ATOM   3300 O  O    . ASN   B 2 131 ? 16.55749  -10.36655 12.15563  1.000 13.71473  ? 136  ASN   A O    1 
ATOM   3301 C  CB   . ASN   B 2 131 ? 15.51373  -13.35664 11.78068  1.000 10.47027  ? 136  ASN   A CB   1 
ATOM   3302 C  CG   . ASN   B 2 131 ? 14.48779  -14.45470 11.86264  1.000 15.49849  ? 136  ASN   A CG   1 
ATOM   3303 O  OD1  . ASN   B 2 131 ? 13.50271  -14.33372 12.59852  1.000 11.12103  ? 136  ASN   A OD1  1 
ATOM   3304 N  ND2  . ASN   B 2 131 ? 14.69395  -15.52873 11.09472  1.000 10.48165  ? 136  ASN   A ND2  1 
ATOM   3305 N  N    . PHE   B 2 132 ? 14.99735  -10.79556 13.75449  1.000 12.78105  ? 137  PHE   A N    1 
ATOM   3306 C  CA   . PHE   B 2 132 ? 15.73719  -10.13545 14.82953  1.000 13.54561  ? 137  PHE   A CA   1 
ATOM   3307 C  C    . PHE   B 2 132 ? 16.73919  -11.11435 15.42769  1.000 14.07659  ? 137  PHE   A C    1 
ATOM   3308 O  O    . PHE   B 2 132 ? 16.56428  -12.33237 15.35474  1.000 17.25908  ? 137  PHE   A O    1 
ATOM   3309 C  CB   . PHE   B 2 132 ? 14.81803  -9.65945  15.97340  1.000 12.00812  ? 137  PHE   A CB   1 
ATOM   3310 C  CG   . PHE   B 2 132 ? 13.86700  -8.54653  15.60124  1.000 15.90185  ? 137  PHE   A CG   1 
ATOM   3311 C  CD1  . PHE   B 2 132 ? 12.60107  -8.83364  15.08112  1.000 15.74778  ? 137  PHE   A CD1  1 
ATOM   3312 C  CD2  . PHE   B 2 132 ? 14.21489  -7.21650  15.81920  1.000 12.63997  ? 137  PHE   A CD2  1 
ATOM   3313 C  CE1  . PHE   B 2 132 ? 11.70104  -7.80472  14.74697  1.000 16.23464  ? 137  PHE   A CE1  1 
ATOM   3314 C  CE2  . PHE   B 2 132 ? 13.32385  -6.18457  15.50005  1.000 20.19031  ? 137  PHE   A CE2  1 
ATOM   3315 C  CZ   . PHE   B 2 132 ? 12.06193  -6.48169  14.95793  1.000 14.44956  ? 137  PHE   A CZ   1 
ATOM   3316 N  N    . ASN   B 2 133 ? 17.75508  -10.60425 16.08177  1.000 12.11957  ? 138  ASN   A N    1 
ATOM   3317 C  CA   . ASN   B 2 133 ? 18.55705  -11.46615 16.94491  1.000 21.38488  ? 138  ASN   A CA   1 
ATOM   3318 C  C    . ASN   B 2 133 ? 17.90491  -11.55011 18.31384  1.000 14.83744  ? 138  ASN   A C    1 
ATOM   3319 O  O    . ASN   B 2 133 ? 17.00782  -10.77215 18.64970  1.000 14.12346  ? 138  ASN   A O    1 
ATOM   3320 C  CB   . ASN   B 2 133 ? 19.99901  -10.97705 17.01703  1.000 12.25924  ? 138  ASN   A CB   1 
ATOM   3321 C  CG   . ASN   B 2 133 ? 20.13185  -9.61500  17.68497  1.000 16.85300  ? 138  ASN   A CG   1 
ATOM   3322 O  OD1  . ASN   B 2 133 ? 19.14778  -8.91605  17.89683  1.000 16.57762  ? 138  ASN   A OD1  1 
ATOM   3323 N  ND2  . ASN   B 2 133 ? 21.37479  -9.22390  18.00208  1.000 14.44136  ? 138  ASN   A ND2  1 
ATOM   3324 N  N    . PRO   B 2 134 ? 18.32188  -12.52004 19.13994  1.000 14.22107  ? 139  PRO   A N    1 
ATOM   3325 C  CA   . PRO   B 2 134 ? 17.78574  -12.60300 20.51789  1.000 24.15753  ? 139  PRO   A CA   1 
ATOM   3326 C  C    . PRO   B 2 134 ? 17.82157  -11.28595 21.28082  1.000 19.88302  ? 139  PRO   A C    1 
ATOM   3327 O  O    . PRO   B 2 134 ? 16.84048  -10.92698 21.94869  1.000 17.46069  ? 139  PRO   A O    1 
ATOM   3328 C  CB   . PRO   B 2 134 ? 18.68774  -13.66290 21.17704  1.000 20.71137  ? 139  PRO   A CB   1 
ATOM   3329 C  CG   . PRO   B 2 134 ? 19.12792  -14.53894 20.03614  1.000 20.50718  ? 139  PRO   A CG   1 
ATOM   3330 C  CD   . PRO   B 2 134 ? 19.31398  -13.57699 18.86610  1.000 20.81947  ? 139  PRO   A CD   1 
ATOM   3331 N  N    . GLN   B 2 135 ? 18.93053  -10.55488 21.19789  1.000 15.78736  ? 140  GLN   A N    1 
ATOM   3332 C  CA   . GLN   B 2 135 ? 19.03037  -9.27084  21.87583  1.000 19.08783  ? 140  GLN   A CA   1 
ATOM   3333 C  C    . GLN   B 2 135 ? 18.06137  -8.24693  21.31267  1.000 22.63460  ? 140  GLN   A C    1 
ATOM   3334 O  O    . GLN   B 2 135 ? 17.70023  -7.29392  22.01558  1.000 24.46668  ? 140  GLN   A O    1 
ATOM   3335 C  CB   . GLN   B 2 135 ? 20.46835  -8.74775  21.77296  1.000 23.51305  ? 140  GLN   A CB   1 
ATOM   3336 C  CG   . GLN   B 2 135 ? 21.49333  -9.63664  22.46312  1.000 16.89727  ? 140  GLN   A CG   1 
ATOM   3337 C  CD   . GLN   B 2 135 ? 21.83650  -10.96066 21.71123  1.000 32.62646  ? 140  GLN   A CD   1 
ATOM   3338 O  OE1  . GLN   B 2 135 ? 21.46564  -11.17275 20.53220  1.000 16.19460  ? 140  GLN   A OE1  1 
ATOM   3339 N  NE2  . GLN   B 2 135 ? 22.54849  -11.85358 22.40836  1.000 22.81808  ? 140  GLN   A NE2  1 
ATOM   3340 N  N    . SER   B 2 136 ? 17.64451  -8.42103  20.06164  1.000 15.15625  ? 141  SER   A N    1 
ATOM   3341 C  CA   . SER   B 2 136 ? 16.68153  -7.56013  19.39349  1.000 16.03377  ? 141  SER   A CA   1 
ATOM   3342 C  C    . SER   B 2 136 ? 17.23547  -6.17911  19.07247  1.000 17.50473  ? 141  SER   A C    1 
ATOM   3343 O  O    . SER   B 2 136 ? 16.46243  -5.25418  18.82533  1.000 16.42075  ? 141  SER   A O    1 
ATOM   3344 C  CB   . SER   B 2 136 ? 15.39143  -7.43317  20.21634  1.000 18.89010  ? 141  SER   A CB   1 
ATOM   3345 O  OG   . SER   B 2 136 ? 14.61552  -8.61423  20.09932  1.000 23.61582  ? 141  SER   A OG   1 
ATOM   3346 N  N    . ASN   B 2 137 ? 18.56146  -6.01203  19.04260  1.000 13.46195  ? 142  ASN   A N    1 
ATOM   3347 C  CA   . ASN   B 2 137 ? 19.15343  -4.76502  18.57160  1.000 16.94168  ? 142  ASN   A CA   1 
ATOM   3348 C  C    . ASN   B 2 137 ? 19.62259  -4.85606  17.12365  1.000 16.29958  ? 142  ASN   A C    1 
ATOM   3349 O  O    . ASN   B 2 137 ? 19.96359  -3.82508  16.52663  1.000 15.99763  ? 142  ASN   A O    1 
ATOM   3350 C  CB   . ASN   B 2 137 ? 20.32430  -4.34289  19.48670  1.000 11.94364  ? 142  ASN   A CB   1 
ATOM   3351 C  CG   . ASN   B 2 137 ? 21.29635  -5.47881  19.74587  1.000 20.20022  ? 142  ASN   A CG   1 
ATOM   3352 O  OD1  . ASN   B 2 137 ? 21.53950  -6.30484  18.86294  1.000 19.82824  ? 142  ASN   A OD1  1 
ATOM   3353 N  ND2  . ASN   B 2 137 ? 21.84422  -5.53870  20.95693  1.000 17.71663  ? 142  ASN   A ND2  1 
ATOM   3354 N  N    . LEU   B 2 138 ? 19.61773  -6.05310  16.54072  1.000 12.99727  ? 143  LEU   A N    1 
ATOM   3355 C  CA   . LEU   B 2 138 ? 20.00489  -6.25515  15.15677  1.000 12.26368  ? 143  LEU   A CA   1 
ATOM   3356 C  C    . LEU   B 2 138 ? 18.88902  -6.95027  14.39169  1.000 15.31489  ? 143  LEU   A C    1 
ATOM   3357 O  O    . LEU   B 2 138 ? 18.11201  -7.73429  14.95265  1.000 13.72108  ? 143  LEU   A O    1 
ATOM   3358 C  CB   . LEU   B 2 138 ? 21.27096  -7.11907  15.03895  1.000 10.42929  ? 143  LEU   A CB   1 
ATOM   3359 C  CG   . LEU   B 2 138 ? 22.58487  -6.69895  15.68107  1.000 13.74173  ? 143  LEU   A CG   1 
ATOM   3360 C  CD1  . LEU   B 2 138 ? 23.63297  -7.76490  15.36724  1.000 12.28913  ? 143  LEU   A CD1  1 
ATOM   3361 C  CD2  . LEU   B 2 138 ? 23.00683  -5.32895  15.14904  1.000 14.51365  ? 143  LEU   A CD2  1 
ATOM   3362 N  N    . ILE   B 2 139 ? 18.84414  -6.67034  13.09567  1.000 16.87833  ? 144  ILE   A N    1 
ATOM   3363 C  CA   . ILE   B 2 139 ? 18.04930  -7.42445  12.13863  1.000 17.28313  ? 144  ILE   A CA   1 
ATOM   3364 C  C    . ILE   B 2 139 ? 18.99045  -7.96844  11.07676  1.000 17.10448  ? 144  ILE   A C    1 
ATOM   3365 O  O    . ILE   B 2 139 ? 19.96344  -7.30140  10.70782  1.000 15.64025  ? 144  ILE   A O    1 
ATOM   3366 C  CB   . ILE   B 2 139 ? 16.95031  -6.54656  11.50846  1.000 19.25357  ? 144  ILE   A CB   1 
ATOM   3367 C  CG1  . ILE   B 2 139 ? 15.82118  -6.34057  12.52833  1.000 16.70619  ? 144  ILE   A CG1  1 
ATOM   3368 C  CG2  . ILE   B 2 139 ? 16.45349  -7.14866  10.17744  1.000 16.28855  ? 144  ILE   A CG2  1 
ATOM   3369 C  CD1  . ILE   B 2 139 ? 14.88615  -5.23866  12.15516  1.000 17.65449  ? 144  ILE   A CD1  1 
ATOM   3370 N  N    . VAL   B 2 140 ? 18.71858  -9.19049  10.61480  1.000 12.93597  ? 145  VAL   A N    1 
ATOM   3371 C  CA   . VAL   B 2 140 ? 19.42974  -9.81350  9.50391   1.000 11.35925  ? 145  VAL   A CA   1 
ATOM   3372 C  C    . VAL   B 2 140 ? 18.42387  -10.04363 8.38081   1.000 11.29057  ? 145  VAL   A C    1 
ATOM   3373 O  O    . VAL   B 2 140 ? 17.25787  -10.36470 8.63670   1.000 11.44694  ? 145  VAL   A O    1 
ATOM   3374 C  CB   . VAL   B 2 140 ? 20.10678  -11.13643 9.92305   1.000 9.35568   ? 145  VAL   A CB   1 
ATOM   3375 C  CG1  . VAL   B 2 140 ? 19.04480  -12.16148 10.34900  1.000 9.77195   ? 145  VAL   A CG1  1 
ATOM   3376 C  CG2  . VAL   B 2 140 ? 20.97994  -11.68244 8.78918   1.000 14.31339  ? 145  VAL   A CG2  1 
ATOM   3377 N  N    . SER   B 2 141 ? 18.86599  -9.85467  7.13985   1.000 10.00685  ? 146  SER   A N    1 
ATOM   3378 C  CA   . SER   B 2 141 ? 17.98612  -9.89280  5.98076   1.000 10.00616  ? 146  SER   A CA   1 
ATOM   3379 C  C    . SER   B 2 141 ? 18.70829  -10.58881 4.84487   1.000 11.07086  ? 146  SER   A C    1 
ATOM   3380 O  O    . SER   B 2 141 ? 19.93629  -10.52273 4.76200   1.000 11.16868  ? 146  SER   A O    1 
ATOM   3381 C  CB   . SER   B 2 141 ? 17.58208  -8.48785  5.51163   1.000 12.50459  ? 146  SER   A CB   1 
ATOM   3382 O  OG   . SER   B 2 141 ? 18.72807  -7.74980  5.08472   1.000 10.07597  ? 146  SER   A OG   1 
ATOM   3383 N  N    . GLY   B 2 142 ? 17.93543  -11.24891 3.98083   1.000 12.79711  ? 147  GLY   A N    1 
ATOM   3384 C  CA   . GLY   B 2 142 ? 18.47860  -11.93394 2.81792   1.000 9.74820   ? 147  GLY   A CA   1 
ATOM   3385 C  C    . GLY   B 2 142 ? 17.65871  -11.60906 1.59182   1.000 9.51544   ? 147  GLY   A C    1 
ATOM   3386 O  O    . GLY   B 2 142 ? 16.45168  -11.37214 1.66267   1.000 10.19389  ? 147  GLY   A O    1 
ATOM   3387 N  N    . SER   B 2 143 ? 18.32883  -11.57708 0.43889   1.000 13.40253  ? 148  SER   A N    1 
ATOM   3388 C  CA   . SER   B 2 143 ? 17.76091  -10.93218 -0.73221  1.000 10.22443  ? 148  SER   A CA   1 
ATOM   3389 C  C    . SER   B 2 143 ? 18.09110  -11.69723 -2.00713  1.000 9.99291   ? 148  SER   A C    1 
ATOM   3390 O  O    . SER   B 2 143 ? 19.08416  -12.43017 -2.10098  1.000 8.81163   ? 148  SER   A O    1 
ATOM   3391 C  CB   . SER   B 2 143 ? 18.25783  -9.48116  -0.85024  1.000 9.45465   ? 148  SER   A CB   1 
ATOM   3392 O  OG   . SER   B 2 143 ? 18.01293  -8.95225  -2.13629  1.000 11.61372  ? 148  SER   A OG   1 
ATOM   3393 N  N    . PHE   B 2 144 ? 17.22919  -11.48335 -3.00124  1.000 9.36131   ? 149  PHE   A N    1 
ATOM   3394 C  CA   . PHE   B 2 144 ? 17.49637  -11.91641 -4.36818  1.000 8.45799   ? 149  PHE   A CA   1 
ATOM   3395 C  C    . PHE   B 2 144 ? 18.83138  -11.37634 -4.85907  1.000 10.67275  ? 149  PHE   A C    1 
ATOM   3396 O  O    . PHE   B 2 144 ? 19.46652  -11.98735 -5.73297  1.000 9.68812   ? 149  PHE   A O    1 
ATOM   3397 C  CB   . PHE   B 2 144 ? 16.33843  -11.45153 -5.26033  1.000 9.24712   ? 149  PHE   A CB   1 
ATOM   3398 C  CG   . PHE   B 2 144 ? 16.40662  -11.91761 -6.70230  1.000 11.93639  ? 149  PHE   A CG   1 
ATOM   3399 C  CD1  . PHE   B 2 144 ? 17.04967  -11.15362 -7.66027  1.000 13.57518  ? 149  PHE   A CD1  1 
ATOM   3400 C  CD2  . PHE   B 2 144 ? 15.76074  -13.08867 -7.10830  1.000 12.20897  ? 149  PHE   A CD2  1 
ATOM   3401 C  CE1  . PHE   B 2 144 ? 17.09084  -11.56169 -9.00625  1.000 15.48325  ? 149  PHE   A CE1  1 
ATOM   3402 C  CE2  . PHE   B 2 144 ? 15.79191  -13.50875 -8.43828  1.000 13.07208  ? 149  PHE   A CE2  1 
ATOM   3403 C  CZ   . PHE   B 2 144 ? 16.45096  -12.74075 -9.39425  1.000 13.73810  ? 149  PHE   A CZ   1 
ATOM   3404 N  N    . ASP   B 2 145 ? 19.27725  -10.22428 -4.31509  1.000 13.22809  ? 150  ASP   A N    1 
ATOM   3405 C  CA   . ASP   B 2 145 ? 20.55825  -9.62722  -4.73998  1.000 12.06827  ? 150  ASP   A CA   1 
ATOM   3406 C  C    . ASP   B 2 145 ? 21.75925  -10.38311 -4.20481  1.000 10.66995  ? 150  ASP   A C    1 
ATOM   3407 O  O    . ASP   B 2 145 ? 22.89424  -9.95005  -4.38871  1.000 13.95515  ? 150  ASP   A O    1 
ATOM   3408 C  CB   . ASP   B 2 145 ? 20.63911  -8.14020  -4.34906  1.000 12.92861  ? 150  ASP   A CB   1 
ATOM   3409 C  CG   . ASP   B 2 145 ? 20.77593  -7.90010  -2.82706  1.000 18.64354  ? 150  ASP   A CG   1 
ATOM   3410 O  OD1  . ASP   B 2 145 ? 21.11491  -8.83404  -2.05697  1.000 8.36498   ? 150  ASP   A OD1  1 
ATOM   3411 O  OD2  . ASP   B 2 145 ? 20.51481  -6.74210  -2.40615  1.000 13.39223  ? 150  ASP   A OD2  1 
ATOM   3412 N  N    . GLU   B 2 146 ? 21.54325  -11.51809 -3.54877  1.000 11.48822  ? 151  GLU   A N    1 
ATOM   3413 C  CA   . GLU   B 2 146 ? 22.56428  -12.50500 -3.20861  1.000 15.97836  ? 151  GLU   A CA   1 
ATOM   3414 C  C    . GLU   B 2 146 ? 23.38912  -12.06488 -1.99654  1.000 16.08972  ? 151  GLU   A C    1 
ATOM   3415 O  O    . GLU   B 2 146 ? 24.32013  -12.78680 -1.60240  1.000 13.77223  ? 151  GLU   A O    1 
ATOM   3416 C  CB   . GLU   B 2 146 ? 23.48643  -12.81401 -4.40249  1.000 12.34141  ? 151  GLU   A CB   1 
ATOM   3417 C  CG   . GLU   B 2 146 ? 22.69158  -13.04713 -5.68956  1.000 10.89893  ? 151  GLU   A CG   1 
ATOM   3418 C  CD   . GLU   B 2 146 ? 23.54174  -13.50614 -6.88645  1.000 14.95266  ? 151  GLU   A CD   1 
ATOM   3419 O  OE1  . GLU   B 2 146 ? 24.78673  -13.45106 -6.80432  1.000 17.64986  ? 151  GLU   A OE1  1 
ATOM   3420 O  OE2  . GLU   B 2 146 ? 22.95588  -13.91424 -7.92049  1.000 15.70046  ? 151  GLU   A OE2  1 
ATOM   3421 N  N    . SER   B 2 147 ? 23.05498  -10.94287 -1.36364  1.000 11.78976  ? 152  SER   A N    1 
ATOM   3422 C  CA   . SER   B 2 147 ? 23.73582  -10.50176 -0.15559  1.000 15.40027  ? 152  SER   A CA   1 
ATOM   3423 C  C    . SER   B 2 147 ? 22.91671  -10.83974 1.08634   1.000 11.02715  ? 152  SER   A C    1 
ATOM   3424 O  O    . SER   B 2 147 ? 21.70873  -11.07982 1.02422   1.000 10.50848  ? 152  SER   A O    1 
ATOM   3425 C  CB   . SER   B 2 147 ? 23.98672  -8.98374  -0.20265  1.000 11.00877  ? 152  SER   A CB   1 
ATOM   3426 O  OG   . SER   B 2 147 ? 22.78965  -8.27081  0.09018   1.000 11.38519  ? 152  SER   A OG   1 
ATOM   3427 N  N    . VAL   B 2 148 ? 23.60059  -10.83763 2.22441   1.000 16.77294  ? 153  VAL   A N    1 
ATOM   3428 C  CA   . VAL   B 2 148 ? 22.98544  -10.79760 3.54834   1.000 10.75130  ? 153  VAL   A CA   1 
ATOM   3429 C  C    . VAL   B 2 148 ? 23.39229  -9.47454  4.17931   1.000 13.13514  ? 153  VAL   A C    1 
ATOM   3430 O  O    . VAL   B 2 148 ? 24.55327  -9.05947  4.06541   1.000 13.69759  ? 153  VAL   A O    1 
ATOM   3431 C  CB   . VAL   B 2 148 ? 23.42343  -12.00752 4.40546   1.000 13.59168  ? 153  VAL   A CB   1 
ATOM   3432 C  CG1  . VAL   B 2 148 ? 23.05426  -11.82446 5.88541   1.000 11.98558  ? 153  VAL   A CG1  1 
ATOM   3433 C  CG2  . VAL   B 2 148 ? 22.79557  -13.30659 3.86646   1.000 9.72150   ? 153  VAL   A CG2  1 
ATOM   3434 N  N    . ARG   B 2 149 ? 22.43817  -8.78957  4.81017   1.000 13.09772  ? 154  ARG   A N    1 
ATOM   3435 C  CA   . ARG   B 2 149 ? 22.69802  -7.50851  5.45913   1.000 13.93960  ? 154  ARG   A CA   1 
ATOM   3436 C  C    . ARG   B 2 149 ? 22.31786  -7.55745  6.93309   1.000 14.24884  ? 154  ARG   A C    1 
ATOM   3437 O  O    . ARG   B 2 149 ? 21.34187  -8.21250  7.31302   1.000 13.27800  ? 154  ARG   A O    1 
ATOM   3438 C  CB   . ARG   B 2 149 ? 21.94802  -6.36360  4.75198   1.000 14.20485  ? 154  ARG   A CB   1 
ATOM   3439 C  CG   . ARG   B 2 149 ? 22.54514  -6.01564  3.40503   1.000 13.81082  ? 154  ARG   A CG   1 
ATOM   3440 C  CD   . ARG   B 2 149 ? 21.72215  -5.00973  2.64689   1.000 16.39146  ? 154  ARG   A CD   1 
ATOM   3441 N  NE   . ARG   B 2 149 ? 22.42825  -4.56775  1.44894   1.000 19.60896  ? 154  ARG   A NE   1 
ATOM   3442 C  CZ   . ARG   B 2 149 ? 23.05719  -3.40572  1.33294   1.000 21.85010  ? 154  ARG   A CZ   1 
ATOM   3443 N  NH1  . ARG   B 2 149 ? 23.06602  -2.52166  2.31989   1.000 26.64862  ? 154  ARG   A NH1  1 
ATOM   3444 N  NH2  . ARG   B 2 149 ? 23.68029  -3.11774  0.19099   1.000 15.45416  ? 154  ARG   A NH2  1 
ATOM   3445 N  N    . ILE   B 2 150 ? 23.09373  -6.85336  7.75814   1.000 13.37495  ? 155  ILE   A N    1 
ATOM   3446 C  CA   . ILE   B 2 150 ? 22.86557  -6.75929  9.20011   1.000 15.18179  ? 155  ILE   A CA   1 
ATOM   3447 C  C    . ILE   B 2 150 ? 22.57244  -5.30329  9.52899   1.000 19.15432  ? 155  ILE   A C    1 
ATOM   3448 O  O    . ILE   B 2 150 ? 23.35042  -4.41426  9.15903   1.000 16.98854  ? 155  ILE   A O    1 
ATOM   3449 C  CB   . ILE   B 2 150 ? 24.07752  -7.26617  10.00226  1.000 18.74262  ? 155  ILE   A CB   1 
ATOM   3450 C  CG1  . ILE   B 2 150 ? 24.39865  -8.71617  9.62438   1.000 19.11425  ? 155  ILE   A CG1  1 
ATOM   3451 C  CG2  . ILE   B 2 150 ? 23.82034  -7.11710  11.50223  1.000 17.54953  ? 155  ILE   A CG2  1 
ATOM   3452 C  CD1  . ILE   B 2 150 ? 25.60561  -9.27905  10.34954  1.000 19.75554  ? 155  ILE   A CD1  1 
ATOM   3453 N  N    . TRP   B 2 151 ? 21.45934  -5.05933  10.22286  1.000 15.13956  ? 156  TRP   A N    1 
ATOM   3454 C  CA   . TRP   B 2 151 ? 20.92424  -3.71435  10.40673  1.000 18.67922  ? 156  TRP   A CA   1 
ATOM   3455 C  C    . TRP   B 2 151 ? 20.83805  -3.35228  11.88070  1.000 15.60742  ? 156  TRP   A C    1 
ATOM   3456 O  O    . TRP   B 2 151 ? 20.56702  -4.20625  12.72772  1.000 13.48074  ? 156  TRP   A O    1 
ATOM   3457 C  CB   . TRP   B 2 151 ? 19.52129  -3.58748  9.79857   1.000 15.06608  ? 156  TRP   A CB   1 
ATOM   3458 C  CG   . TRP   B 2 151 ? 19.40948  -4.06557  8.36258   1.000 16.58113  ? 156  TRP   A CG   1 
ATOM   3459 C  CD1  . TRP   B 2 151 ? 19.30061  -5.36560  7.93064   1.000 12.62037  ? 156  TRP   A CD1  1 
ATOM   3460 C  CD2  . TRP   B 2 151 ? 19.35555  -3.24864  7.18153   1.000 15.61797  ? 156  TRP   A CD2  1 
ATOM   3461 N  NE1  . TRP   B 2 151 ? 19.19976  -5.40168  6.55864   1.000 13.18854  ? 156  TRP   A NE1  1 
ATOM   3462 C  CE2  . TRP   B 2 151 ? 19.22373  -4.12071  6.07357   1.000 14.06764  ? 156  TRP   A CE2  1 
ATOM   3463 C  CE3  . TRP   B 2 151 ? 19.41248  -1.86865  6.95046   1.000 14.15037  ? 156  TRP   A CE3  1 
ATOM   3464 C  CZ2  . TRP   B 2 151 ? 19.14784  -3.65479  4.75753   1.000 22.16935  ? 156  TRP   A CZ2  1 
ATOM   3465 C  CZ3  . TRP   B 2 151 ? 19.33759  -1.40772  5.64043   1.000 19.32766  ? 156  TRP   A CZ3  1 
ATOM   3466 C  CH2  . TRP   B 2 151 ? 19.19977  -2.29679  4.56046   1.000 18.82951  ? 156  TRP   A CH2  1 
ATOM   3467 N  N    . ASP   B 2 152 ? 21.04194  -2.06425  12.17165  1.000 19.61147  ? 157  ASP   A N    1 
ATOM   3468 C  CA   . ASP   B 2 152 ? 20.84076  -1.53519  13.51760  1.000 19.15170  ? 157  ASP   A CA   1 
ATOM   3469 C  C    . ASP   B 2 152 ? 19.35772  -1.23927  13.72742  1.000 21.00073  ? 157  ASP   A C    1 
ATOM   3470 O  O    . ASP   B 2 152 ? 18.78973  -0.37635  13.04731  1.000 18.19241  ? 157  ASP   A O    1 
ATOM   3471 C  CB   . ASP   B 2 152 ? 21.68365  -0.27212  13.71862  1.000 28.76732  ? 157  ASP   A CB   1 
ATOM   3472 C  CG   . ASP   B 2 152 ? 21.62846  0.26696   15.14958  1.000 28.49003  ? 157  ASP   A CG   1 
ATOM   3473 O  OD1  . ASP   B 2 152 ? 20.56940  0.17793   15.81747  1.000 23.77136  ? 157  ASP   A OD1  1 
ATOM   3474 O  OD2  . ASP   B 2 152 ? 22.66738  0.79005   15.60166  1.000 36.29398  ? 157  ASP   A OD2  1 
ATOM   3475 N  N    . VAL   B 2 153 ? 18.74066  -1.94626  14.68139  1.000 17.68034  ? 158  VAL   A N    1 
ATOM   3476 C  CA   . VAL   B 2 153 ? 17.30363  -1.82534  14.89923  1.000 22.37781  ? 158  VAL   A CA   1 
ATOM   3477 C  C    . VAL   B 2 153 ? 16.92550  -0.39235  15.25011  1.000 25.75660  ? 158  VAL   A C    1 
ATOM   3478 O  O    . VAL   B 2 153 ? 15.91851  0.13156   14.76398  1.000 29.18623  ? 158  VAL   A O    1 
ATOM   3479 C  CB   . VAL   B 2 153 ? 16.84458  -2.81831  15.98624  1.000 19.68196  ? 158  VAL   A CB   1 
ATOM   3480 C  CG1  . VAL   B 2 153 ? 15.43951  -2.49038  16.44807  1.000 19.57000  ? 158  VAL   A CG1  1 
ATOM   3481 C  CG2  . VAL   B 2 153 ? 16.91273  -4.25834  15.46033  1.000 13.82845  ? 158  VAL   A CG2  1 
ATOM   3482 N  N    . LYS   B 2 154 ? 17.72136  0.26675   16.08416  1.000 21.93752  ? 159  LYS   A N    1 
ATOM   3483 C  CA   . LYS   B 2 154 ? 17.35622  1.58475   16.58505  1.000 24.43927  ? 159  LYS   A CA   1 
ATOM   3484 C  C    . LYS   B 2 154 ? 17.73625  2.72773   15.64703  1.000 25.37986  ? 159  LYS   A C    1 
ATOM   3485 O  O    . LYS   B 2 154 ? 17.05518  3.75868   15.64189  1.000 20.20453  ? 159  LYS   A O    1 
ATOM   3486 C  CB   . LYS   B 2 154 ? 17.98306  1.80987   17.96710  1.000 23.89624  ? 159  LYS   A CB   1 
ATOM   3487 C  CG   . LYS   B 2 154 ? 17.59202  0.73890   18.99312  1.000 25.96629  ? 159  LYS   A CG   1 
ATOM   3488 C  CD   . LYS   B 2 154 ? 18.53089  0.76203   20.20722  1.000 42.86042  ? 159  LYS   A CD   1 
ATOM   3489 C  CE   . LYS   B 2 154 ? 18.44888  -0.52192  21.05328  1.000 47.33364  ? 159  LYS   A CE   1 
ATOM   3490 N  NZ   . LYS   B 2 154 ? 19.75393  -1.27284  21.06547  1.000 34.91215  ? 159  LYS   A NZ   1 
ATOM   3491 N  N    . THR   B 2 155 ? 18.78434  2.58175   14.83615  1.000 22.34732  ? 160  THR   A N    1 
ATOM   3492 C  CA   . THR   B 2 155 ? 19.08538  3.61272   13.85212  1.000 23.62088  ? 160  THR   A CA   1 
ATOM   3493 C  C    . THR   B 2 155 ? 18.43154  3.34660   12.51107  1.000 23.91291  ? 160  THR   A C    1 
ATOM   3494 O  O    . THR   B 2 155 ? 18.30757  4.27655   11.70300  1.000 25.12889  ? 160  THR   A O    1 
ATOM   3495 C  CB   . THR   B 2 155 ? 20.59440  3.74880   13.62128  1.000 24.09348  ? 160  THR   A CB   1 
ATOM   3496 O  OG1  . THR   B 2 155 ? 21.10654  2.53081   13.04840  1.000 26.40291  ? 160  THR   A OG1  1 
ATOM   3497 C  CG2  . THR   B 2 155 ? 21.32523  4.07693   14.92334  1.000 16.27860  ? 160  THR   A CG2  1 
ATOM   3498 N  N    . GLY   B 2 156 ? 18.01265  2.10756   12.25909  1.000 20.91118  ? 161  GLY   A N    1 
ATOM   3499 C  CA   . GLY   B 2 156 ? 17.49881  1.75545   10.95705  1.000 21.14216  ? 161  GLY   A CA   1 
ATOM   3500 C  C    . GLY   B 2 156 ? 18.55493  1.75146   9.88217   1.000 22.11806  ? 161  GLY   A C    1 
ATOM   3501 O  O    . GLY   B 2 156 ? 18.22606  1.76837   8.69613   1.000 24.77498  ? 161  GLY   A O    1 
ATOM   3502 N  N    . LYS   B 2 157 ? 19.82089  1.72157   10.26731  1.000 19.05008  ? 162  LYS   A N    1 
ATOM   3503 C  CA   . LYS   B 2 157 ? 20.92099  1.81159   9.32342   1.000 26.84568  ? 162  LYS   A CA   1 
ATOM   3504 C  C    . LYS   B 2 157 ? 21.56110  0.44762   9.12856   1.000 22.40164  ? 162  LYS   A C    1 
ATOM   3505 O  O    . LYS   B 2 157 ? 21.51606  -0.41134  10.01561  1.000 17.23858  ? 162  LYS   A O    1 
ATOM   3506 C  CB   . LYS   B 2 157 ? 21.96687  2.82268   9.80147   1.000 28.80185  ? 162  LYS   A CB   1 
ATOM   3507 C  CG   . LYS   B 2 157 ? 21.93987  4.10764   8.99740   1.000 34.45855  ? 162  LYS   A CG   1 
ATOM   3508 C  CD   . LYS   B 2 157 ? 21.99269  5.32969   9.87834   1.000 35.62962  ? 162  LYS   A CD   1 
ATOM   3509 C  CE   . LYS   B 2 157 ? 22.15870  6.59065   9.03228   1.000 53.00939  ? 162  LYS   A CE   1 
ATOM   3510 N  NZ   . LYS   B 2 157 ? 22.05253  7.84369   9.84320   1.000 55.30515  ? 162  LYS   A NZ   1 
ATOM   3511 N  N    . CYS   B 2 158 ? 22.14824  0.24959   7.94864   1.000 18.02829  ? 163  CYS   A N    1 
ATOM   3512 C  CA   . CYS   B 2 158 ? 22.82235  -1.00538  7.64778   1.000 18.64887  ? 163  CYS   A CA   1 
ATOM   3513 C  C    . CYS   B 2 158 ? 24.21028  -0.99925  8.28293   1.000 17.47224  ? 163  CYS   A C    1 
ATOM   3514 O  O    . CYS   B 2 158 ? 25.01625  -0.09921  8.03196   1.000 25.56783  ? 163  CYS   A O    1 
ATOM   3515 C  CB   . CYS   B 2 158 ? 22.90653  -1.22046  6.13880   1.000 18.02249  ? 163  CYS   A CB   1 
ATOM   3516 S  SG   . CYS   B 2 158 ? 23.58868  -2.82944  5.67996   1.000 17.54966  ? 163  CYS   A SG   1 
ATOM   3517 N  N    . LEU   B 2 159 ? 24.48326  -1.98719  9.12401   1.000 22.35709  ? 164  LEU   A N    1 
ATOM   3518 C  CA   . LEU   B 2 159 ? 25.79520  -2.10707  9.74216   1.000 21.91671  ? 164  LEU   A CA   1 
ATOM   3519 C  C    . LEU   B 2 159 ? 26.77435  -2.86305  8.85731   1.000 24.77890  ? 164  LEU   A C    1 
ATOM   3520 O  O    . LEU   B 2 159 ? 27.92633  -2.44698  8.72041   1.000 18.69362  ? 164  LEU   A O    1 
ATOM   3521 C  CB   . LEU   B 2 159 ? 25.67910  -2.80200  11.10019  1.000 20.41131  ? 164  LEU   A CB   1 
ATOM   3522 C  CG   . LEU   B 2 159 ? 24.89894  -2.03399  12.16806  1.000 25.34838  ? 164  LEU   A CG   1 
ATOM   3523 C  CD1  . LEU   B 2 159 ? 24.66986  -2.89394  13.39108  1.000 23.11248  ? 164  LEU   A CD1  1 
ATOM   3524 C  CD2  . LEU   B 2 159 ? 25.63681  -0.75292  12.54907  1.000 22.80175  ? 164  LEU   A CD2  1 
ATOM   3525 N  N    . LYS   B 2 160 ? 26.34848  -3.96611  8.24632   1.000 15.57312  ? 165  LYS   A N    1 
ATOM   3526 C  CA   . LYS   B 2 160 ? 27.24263  -4.75610  7.42146   1.000 19.27475  ? 165  LYS   A CA   1 
ATOM   3527 C  C    . LYS   B 2 160 ? 26.48679  -5.33022  6.23641   1.000 20.08272  ? 165  LYS   A C    1 
ATOM   3528 O  O    . LYS   B 2 160 ? 25.30680  -5.66729  6.33431   1.000 12.70983  ? 165  LYS   A O    1 
ATOM   3529 C  CB   . LYS   B 2 160 ? 27.89961  -5.88101  8.22860   1.000 22.69903  ? 165  LYS   A CB   1 
ATOM   3530 C  CG   . LYS   B 2 160 ? 28.93547  -5.36689  9.20368   1.000 30.22089  ? 165  LYS   A CG   1 
ATOM   3531 C  CD   . LYS   B 2 160 ? 30.07352  -6.34181  9.34086   1.000 35.68758  ? 165  LYS   A CD   1 
ATOM   3532 C  CE   . LYS   B 2 160 ? 29.68050  -7.46078  10.27188  1.000 31.96334  ? 165  LYS   A CE   1 
ATOM   3533 N  NZ   . LYS   B 2 160 ? 29.51032  -6.94571  11.65983  1.000 35.24900  ? 165  LYS   A NZ   1 
ATOM   3534 N  N    . THR   B 2 161 ? 27.18892  -5.43823  5.11250   1.000 16.66492  ? 166  THR   A N    1 
ATOM   3535 C  CA   . THR   B 2 161 ? 26.69209  -6.11233  3.91948   1.000 14.52902  ? 166  THR   A CA   1 
ATOM   3536 C  C    . THR   B 2 161 ? 27.57620  -7.31729  3.63564   1.000 18.74912  ? 166  THR   A C    1 
ATOM   3537 O  O    . THR   B 2 161 ? 28.76122  -7.15523  3.32876   1.000 19.64004  ? 166  THR   A O    1 
ATOM   3538 C  CB   . THR   B 2 161 ? 26.68516  -5.16340  2.72443   1.000 18.42792  ? 166  THR   A CB   1 
ATOM   3539 O  OG1  . THR   B 2 161 ? 25.74206  -4.11045  2.96727   1.000 22.68180  ? 166  THR   A OG1  1 
ATOM   3540 C  CG2  . THR   B 2 161 ? 26.31634  -5.91050  1.43843   1.000 12.25625  ? 166  THR   A CG2  1 
ATOM   3541 N  N    . LEU   B 2 162 ? 26.99427  -8.53132  3.71565   1.000 15.96406  ? 167  LEU   A N    1 
ATOM   3542 C  CA   . LEU   B 2 162 ? 27.81438  -9.71928  3.50680   1.000 16.36091  ? 167  LEU   A CA   1 
ATOM   3543 C  C    . LEU   B 2 162 ? 27.69156  -10.20337 2.06782   1.000 17.24072  ? 167  LEU   A C    1 
ATOM   3544 O  O    . LEU   B 2 162 ? 26.57463  -10.35347 1.56370   1.000 10.98361  ? 167  LEU   A O    1 
ATOM   3545 C  CB   . LEU   B 2 162 ? 27.40335  -10.83225 4.47082   1.000 13.30018  ? 167  LEU   A CB   1 
ATOM   3546 C  CG   . LEU   B 2 162 ? 27.28416  -10.45318 5.95979   1.000 15.98341  ? 167  LEU   A CG   1 
ATOM   3547 C  CD1  . LEU   B 2 162 ? 27.06715  -11.69515 6.79683   1.000 14.91979  ? 167  LEU   A CD1  1 
ATOM   3548 C  CD2  . LEU   B 2 162 ? 28.50306  -9.71907  6.45488   1.000 17.07838  ? 167  LEU   A CD2  1 
ATOM   3549 N  N    . PRO   B 2 163 ? 28.78965  -10.44334 1.36995   1.000 17.55918  ? 168  PRO   A N    1 
ATOM   3550 C  CA   . PRO   B 2 163 ? 28.69783  -10.96242 -0.00803  1.000 13.19210  ? 168  PRO   A CA   1 
ATOM   3551 C  C    . PRO   B 2 163 ? 28.49993  -12.47543 0.03003   1.000 17.37344  ? 168  PRO   A C    1 
ATOM   3552 O  O    . PRO   B 2 163 ? 29.33703  -13.28940 -0.38784  1.000 12.04534  ? 168  PRO   A O    1 
ATOM   3553 C  CB   . PRO   B 2 163 ? 30.03687  -10.53336 -0.60391  1.000 22.28667  ? 168  PRO   A CB   1 
ATOM   3554 C  CG   . PRO   B 2 163 ? 30.97475  -10.65224 0.55619   1.000 26.73292  ? 168  PRO   A CG   1 
ATOM   3555 C  CD   . PRO   B 2 163 ? 30.18359  -10.25122 1.79009   1.000 18.67563  ? 168  PRO   A CD   1 
ATOM   3556 N  N    . ALA   B 2 164 ? 27.32790  -12.86248 0.53392   1.000 14.09169  ? 169  ALA   A N    1 
ATOM   3557 C  CA   . ALA   B 2 164 ? 27.18592  -14.15245 1.18898   1.000 13.78000  ? 169  ALA   A CA   1 
ATOM   3558 C  C    . ALA   B 2 164 ? 27.18110  -15.30851 0.20105   1.000 10.89827  ? 169  ALA   A C    1 
ATOM   3559 O  O    . ALA   B 2 164 ? 27.66214  -16.39846 0.52716   1.000 8.56526   ? 169  ALA   A O    1 
ATOM   3560 C  CB   . ALA   B 2 164 ? 25.90483  -14.15549 2.02984   1.000 11.20857  ? 169  ALA   A CB   1 
ATOM   3561 N  N    . HIS   B 2 165 ? 26.67522  -15.08661 -1.01102  1.000 11.17056  ? 170  HIS   A N    1 
ATOM   3562 C  CA   . HIS   B 2 165 ? 26.28838  -16.17268 -1.89400  1.000 10.33803  ? 170  HIS   A CA   1 
ATOM   3563 C  C    . HIS   B 2 165 ? 26.40351  -15.70876 -3.33802  1.000 12.79787  ? 170  HIS   A C    1 
ATOM   3564 O  O    . HIS   B 2 165 ? 26.45546  -14.51077 -3.61908  1.000 15.00972  ? 170  HIS   A O    1 
ATOM   3565 C  CB   . HIS   B 2 165 ? 24.85138  -16.62576 -1.59513  1.000 8.06709   ? 170  HIS   A CB   1 
ATOM   3566 C  CG   . HIS   B 2 165 ? 24.71029  -17.37670 -0.31110  1.000 5.82902   ? 170  HIS   A CG   1 
ATOM   3567 N  ND1  . HIS   B 2 165 ? 25.12236  -18.68166 -0.16999  1.000 7.35990   ? 170  HIS   A ND1  1 
ATOM   3568 C  CD2  . HIS   B 2 165 ? 24.20014  -17.01167 0.89182   1.000 9.68285   ? 170  HIS   A CD2  1 
ATOM   3569 C  CE1  . HIS   B 2 165 ? 24.86526  -19.09761 1.06301   1.000 10.98335  ? 170  HIS   A CE1  1 
ATOM   3570 N  NE2  . HIS   B 2 165 ? 24.30712  -18.10261 1.72889   1.000 9.38929   ? 170  HIS   A NE2  1 
ATOM   3571 N  N    . SER   B 2 166 ? 26.41667  -16.67281 -4.25896  1.000 12.75047  ? 171  SER   A N    1 
ATOM   3572 C  CA   . SER   B 2 166 ? 26.43680  -16.37689 -5.69297  1.000 10.44775  ? 171  SER   A CA   1 
ATOM   3573 C  C    . SER   B 2 166 ? 25.07889  -16.59301 -6.35911  1.000 14.68591  ? 171  SER   A C    1 
ATOM   3574 O  O    . SER   B 2 166 ? 25.01403  -16.73909 -7.58311  1.000 11.78963  ? 171  SER   A O    1 
ATOM   3575 C  CB   . SER   B 2 166 ? 27.51094  -17.20585 -6.40181  1.000 8.96125   ? 171  SER   A CB   1 
ATOM   3576 O  OG   . SER   B 2 166 ? 27.43399  -18.59184 -6.08574  1.000 7.19352   ? 171  SER   A OG   1 
ATOM   3577 N  N    . ASP   B 2 167 ? 24.00281  -16.60504 -5.57422  1.000 14.87169  ? 172  ASP   A N    1 
ATOM   3578 C  CA   . ASP   B 2 167 ? 22.64187  -16.77816 -6.06636  1.000 13.13301  ? 172  ASP   A CA   1 
ATOM   3579 C  C    . ASP   B 2 167 ? 21.69672  -16.26616 -4.98649  1.000 13.56478  ? 172  ASP   A C    1 
ATOM   3580 O  O    . ASP   B 2 167 ? 22.13258  -15.96107 -3.86646  1.000 12.47600  ? 172  ASP   A O    1 
ATOM   3581 C  CB   . ASP   B 2 167 ? 22.34901  -18.25320 -6.40431  1.000 13.72469  ? 172  ASP   A CB   1 
ATOM   3582 C  CG   . ASP   B 2 167 ? 22.71418  -18.61325 -7.83925  1.000 19.75214  ? 172  ASP   A CG   1 
ATOM   3583 O  OD1  . ASP   B 2 167 ? 22.21824  -17.92934 -8.76234  1.000 15.92563  ? 172  ASP   A OD1  1 
ATOM   3584 O  OD2  . ASP   B 2 167 ? 23.50827  -19.56921 -8.04211  1.000 20.91136  ? 172  ASP   A OD2  1 
ATOM   3585 N  N    . PRO   B 2 168 ? 20.39875  -16.15826 -5.28764  1.000 11.44438  ? 173  PRO   A N    1 
ATOM   3586 C  CA   . PRO   B 2 168 ? 19.47260  -15.55627 -4.31477  1.000 13.44744  ? 173  PRO   A CA   1 
ATOM   3587 C  C    . PRO   B 2 168 ? 19.51650  -16.25719 -2.95872  1.000 15.37540  ? 173  PRO   A C    1 
ATOM   3588 O  O    . PRO   B 2 168 ? 19.71457  -17.47317 -2.86564  1.000 11.43693  ? 173  PRO   A O    1 
ATOM   3589 C  CB   . PRO   B 2 168 ? 18.10368  -15.69640 -4.99291  1.000 12.63669  ? 173  PRO   A CB   1 
ATOM   3590 C  CG   . PRO   B 2 168 ? 18.44884  -15.59546 -6.49888  1.000 10.19245  ? 173  PRO   A CG   1 
ATOM   3591 C  CD   . PRO   B 2 168 ? 19.78490  -16.30838 -6.62569  1.000 11.97082  ? 173  PRO   A CD   1 
ATOM   3592 N  N    . VAL   B 2 169 ? 19.35134  -15.45314 -1.90079  1.000 8.92448   ? 174  VAL   A N    1 
ATOM   3593 C  CA   . VAL   B 2 169 ? 19.33922  -15.92507 -0.51976  1.000 8.44495   ? 174  VAL   A CA   1 
ATOM   3594 C  C    . VAL   B 2 169 ? 17.89619  -16.21014 -0.10090  1.000 10.78607  ? 174  VAL   A C    1 
ATOM   3595 O  O    . VAL   B 2 169 ? 17.03214  -15.32420 -0.17904  1.000 8.78530   ? 174  VAL   A O    1 
ATOM   3596 C  CB   . VAL   B 2 169 ? 19.97005  -14.87597 0.41425   1.000 9.00561   ? 174  VAL   A CB   1 
ATOM   3597 C  CG1  . VAL   B 2 169 ? 19.94593  -15.40790 1.84227   1.000 8.80884   ? 174  VAL   A CG1  1 
ATOM   3598 C  CG2  . VAL   B 2 169 ? 21.40607  -14.54590 -0.01162  1.000 8.78211   ? 174  VAL   A CG2  1 
ATOM   3599 N  N    . SER   B 2 170 ? 17.63822  -17.43213 0.37614   1.000 7.30484   ? 175  SER   A N    1 
ATOM   3600 C  CA   . SER   B 2 170 ? 16.28721  -17.86120 0.72102   1.000 9.96583   ? 175  SER   A CA   1 
ATOM   3601 C  C    . SER   B 2 170 ? 15.95905  -17.76914 2.21098   1.000 10.94859  ? 175  SER   A C    1 
ATOM   3602 O  O    . SER   B 2 170 ? 14.77701  -17.68820 2.56285   1.000 11.30363  ? 175  SER   A O    1 
ATOM   3603 C  CB   . SER   B 2 170 ? 16.07436  -19.30624 0.25708   1.000 9.48338   ? 175  SER   A CB   1 
ATOM   3604 O  OG   . SER   B 2 170 ? 17.14136  -20.11814 0.71824   1.000 7.56742   ? 175  SER   A OG   1 
ATOM   3605 N  N    . ALA   B 2 171 ? 16.94996  -17.80802 3.09909   1.000 8.32964   ? 176  ALA   A N    1 
ATOM   3606 C  CA   . ALA   B 2 171 ? 16.64280  -17.75997 4.52505   1.000 9.79701   ? 176  ALA   A CA   1 
ATOM   3607 C  C    . ALA   B 2 171 ? 17.85668  -17.24684 5.29315   1.000 9.30257   ? 176  ALA   A C    1 
ATOM   3608 O  O    . ALA   B 2 171 ? 19.00174  -17.39279 4.84928   1.000 9.46668   ? 176  ALA   A O    1 
ATOM   3609 C  CB   . ALA   B 2 171 ? 16.20583  -19.13696 5.05808   1.000 6.42740   ? 176  ALA   A CB   1 
ATOM   3610 N  N    . VAL   B 2 172 ? 17.58452  -16.61080 6.43109   1.000 8.51788   ? 177  VAL   A N    1 
ATOM   3611 C  CA   . VAL   B 2 172 ? 18.61039  -16.11968 7.34817   1.000 7.30318   ? 177  VAL   A CA   1 
ATOM   3612 C  C    . VAL   B 2 172 ? 18.05725  -16.28064 8.75912   1.000 12.86005  ? 177  VAL   A C    1 
ATOM   3613 O  O    . VAL   B 2 172 ? 16.85321  -16.11570 8.98898   1.000 9.90829   ? 177  VAL   A O    1 
ATOM   3614 C  CB   . VAL   B 2 172 ? 19.01432  -14.64567 7.08413   1.000 7.81673   ? 177  VAL   A CB   1 
ATOM   3615 C  CG1  . VAL   B 2 172 ? 19.83445  -14.46968 5.77021   1.000 7.04868   ? 177  VAL   A CG1  1 
ATOM   3616 C  CG2  . VAL   B 2 172 ? 17.79326  -13.73775 7.09495   1.000 6.80183   ? 177  VAL   A CG2  1 
ATOM   3617 N  N    . HIS   B 2 173 ? 18.92917  -16.62753 9.69923   1.000 8.51918   ? 178  HIS   A N    1 
ATOM   3618 C  CA   . HIS   B 2 173 ? 18.46405  -16.94848 11.04520  1.000 16.37364  ? 178  HIS   A CA   1 
ATOM   3619 C  C    . HIS   B 2 173 ? 19.61693  -16.78135 12.02732  1.000 15.08916  ? 178  HIS   A C    1 
ATOM   3620 O  O    . HIS   B 2 173 ? 20.74599  -17.18629 11.73246  1.000 15.41786  ? 178  HIS   A O    1 
ATOM   3621 C  CB   . HIS   B 2 173 ? 17.90713  -18.38551 11.10022  1.000 9.51070   ? 178  HIS   A CB   1 
ATOM   3622 C  CG   . HIS   B 2 173 ? 17.25502  -18.74049 12.40417  1.000 13.62292  ? 178  HIS   A CG   1 
ATOM   3623 N  ND1  . HIS   B 2 173 ? 17.55302  -19.89743 13.09327  1.000 17.93674  ? 178  HIS   A ND1  1 
ATOM   3624 C  CD2  . HIS   B 2 173 ? 16.30590  -18.10151 13.13403  1.000 15.24782  ? 178  HIS   A CD2  1 
ATOM   3625 C  CE1  . HIS   B 2 173 ? 16.81991  -19.95641 14.19319  1.000 13.75923  ? 178  HIS   A CE1  1 
ATOM   3626 N  NE2  . HIS   B 2 173 ? 16.05683  -18.87846 14.24305  1.000 14.83016  ? 178  HIS   A NE2  1 
ATOM   3627 N  N    . PHE   B 2 174 ? 19.32976  -16.16930 13.18325  1.000 12.24108  ? 179  PHE   A N    1 
ATOM   3628 C  CA   . PHE   B 2 174 ? 20.29864  -16.07418 14.27535  1.000 13.37325  ? 179  PHE   A CA   1 
ATOM   3629 C  C    . PHE   B 2 174 ? 20.23363  -17.31913 15.15441  1.000 11.49792  ? 179  PHE   A C    1 
ATOM   3630 O  O    . PHE   B 2 174 ? 19.17666  -17.94520 15.29633  1.000 8.19727   ? 179  PHE   A O    1 
ATOM   3631 C  CB   . PHE   B 2 174 ? 20.03846  -14.85015 15.16425  1.000 12.22482  ? 179  PHE   A CB   1 
ATOM   3632 C  CG   . PHE   B 2 174 ? 20.56544  -13.55114 14.61124  1.000 13.07833  ? 179  PHE   A CG   1 
ATOM   3633 C  CD1  . PHE   B 2 174 ? 21.92841  -13.24305 14.67837  1.000 11.41942  ? 179  PHE   A CD1  1 
ATOM   3634 C  CD2  . PHE   B 2 174 ? 19.69643  -12.62023 14.06009  1.000 10.84482  ? 179  PHE   A CD2  1 
ATOM   3635 C  CE1  . PHE   B 2 174 ? 22.40438  -12.03404 14.18335  1.000 12.37667  ? 179  PHE   A CE1  1 
ATOM   3636 C  CE2  . PHE   B 2 174 ? 20.16141  -11.40323 13.57907  1.000 11.64058  ? 179  PHE   A CE2  1 
ATOM   3637 C  CZ   . PHE   B 2 174 ? 21.51538  -11.10413 13.63120  1.000 8.22365   ? 179  PHE   A CZ   1 
ATOM   3638 N  N    . ASN   B 2 175 ? 21.37059  -17.66402 15.76955  1.000 8.87126   ? 180  ASN   A N    1 
ATOM   3639 C  CA   . ASN   B 2 175 ? 21.37856  -18.75797 16.72162  1.000 11.30398  ? 180  ASN   A CA   1 
ATOM   3640 C  C    . ASN   B 2 175 ? 20.96337  -18.22992 18.09954  1.000 14.77654  ? 180  ASN   A C    1 
ATOM   3641 O  O    . ASN   B 2 175 ? 20.66928  -17.04793 18.27644  1.000 13.60347  ? 180  ASN   A O    1 
ATOM   3642 C  CB   . ASN   B 2 175 ? 22.74260  -19.45788 16.75180  1.000 14.89282  ? 180  ASN   A CB   1 
ATOM   3643 C  CG   . ASN   B 2 175 ? 23.81247  -18.65177 17.47287  1.000 14.43451  ? 180  ASN   A CG   1 
ATOM   3644 O  OD1  . ASN   B 2 175 ? 23.81739  -17.41577 17.45680  1.000 10.78199  ? 180  ASN   A OD1  1 
ATOM   3645 N  ND2  . ASN   B 2 175 ? 24.73545  -19.36067 18.10801  1.000 17.28455  ? 180  ASN   A ND2  1 
ATOM   3646 N  N    . ARG   B 2 176 ? 20.94532  -19.11587 19.09759  1.000 17.28797  ? 181  ARG   A N    1 
ATOM   3647 C  CA   . ARG   B 2 176 ? 20.22917  -18.79285 20.32849  1.000 24.09740  ? 181  ARG   A CA   1 
ATOM   3648 C  C    . ARG   B 2 176 ? 20.93401  -17.74175 21.17851  1.000 19.54346  ? 181  ARG   A C    1 
ATOM   3649 O  O    . ARG   B 2 176 ? 20.26188  -17.06575 21.96440  1.000 20.20545  ? 181  ARG   A O    1 
ATOM   3650 C  CB   . ARG   B 2 176 ? 19.97317  -20.05882 21.15154  1.000 24.08820  ? 181  ARG   A CB   1 
ATOM   3651 C  CG   . ARG   B 2 176 ? 21.20018  -20.83871 21.53371  1.000 30.88715  ? 181  ARG   A CG   1 
ATOM   3652 C  CD   . ARG   B 2 176 ? 20.99708  -21.52365 22.88173  1.000 37.44396  ? 181  ARG   A CD   1 
ATOM   3653 N  NE   . ARG   B 2 176 ? 20.85690  -20.53460 23.94666  1.000 53.70544  ? 181  ARG   A NE   1 
ATOM   3654 C  CZ   . ARG   B 2 176 ? 21.87279  -19.94150 24.56773  1.000 49.34620  ? 181  ARG   A CZ   1 
ATOM   3655 N  NH1  . ARG   B 2 176 ? 23.13284  -20.25543 24.30089  1.000 45.11594  ? 181  ARG   A NH1  1 
ATOM   3656 N  NH2  . ARG   B 2 176 ? 21.61763  -19.00147 25.47465  1.000 41.88403  ? 181  ARG   A NH2  1 
ATOM   3657 N  N    . ASP   B 2 177 ? 22.25201  -17.57667 21.05564  1.000 20.64052  ? 182  ASP   A N    1 
ATOM   3658 C  CA   . ASP   B 2 177 ? 22.92887  -16.47459 21.73065  1.000 20.44649  ? 182  ASP   A CA   1 
ATOM   3659 C  C    . ASP   B 2 177 ? 23.28689  -15.33862 20.78163  1.000 19.65725  ? 182  ASP   A C    1 
ATOM   3660 O  O    . ASP   B 2 177 ? 23.95279  -14.38555 21.20065  1.000 16.61220  ? 182  ASP   A O    1 
ATOM   3661 C  CB   . ASP   B 2 177 ? 24.16882  -16.96746 22.50381  1.000 23.07532  ? 182  ASP   A CB   1 
ATOM   3662 C  CG   . ASP   B 2 177 ? 25.30195  -17.46644 21.60196  1.000 26.77851  ? 182  ASP   A CG   1 
ATOM   3663 O  OD1  . ASP   B 2 177 ? 25.38105  -17.09750 20.41195  1.000 26.85226  ? 182  ASP   A OD1  1 
ATOM   3664 O  OD2  . ASP   B 2 177 ? 26.14494  -18.23535 22.11110  1.000 25.15978  ? 182  ASP   A OD2  1 
ATOM   3665 N  N    . GLY   B 2 178 ? 22.82303  -15.39472 19.52858  1.000 23.37157  ? 183  GLY   A N    1 
ATOM   3666 C  CA   . GLY   B 2 178 ? 22.98306  -14.29076 18.60354  1.000 15.13714  ? 183  GLY   A CA   1 
ATOM   3667 C  C    . GLY   B 2 178 ? 24.37811  -14.13170 18.04268  1.000 14.26479  ? 183  GLY   A C    1 
ATOM   3668 O  O    . GLY   B 2 178 ? 24.61413  -13.19673 17.26965  1.000 10.14154  ? 183  GLY   A O    1 
ATOM   3669 N  N    . SER   B 2 179 ? 25.31013  -15.01962 18.38983  1.000 12.56272  ? 184  SER   A N    1 
ATOM   3670 C  CA   . SER   B 2 179 ? 26.67517  -14.87955 17.89797  1.000 11.65509  ? 184  SER   A CA   1 
ATOM   3671 C  C    . SER   B 2 179 ? 26.84836  -15.40362 16.47802  1.000 12.82273  ? 184  SER   A C    1 
ATOM   3672 O  O    . SER   B 2 179 ? 27.85741  -15.08959 15.83711  1.000 8.64729   ? 184  SER   A O    1 
ATOM   3673 C  CB   . SER   B 2 179 ? 27.65612  -15.58744 18.84511  1.000 14.24768  ? 184  SER   A CB   1 
ATOM   3674 O  OG   . SER   B 2 179 ? 27.32519  -16.95645 18.98815  1.000 15.51270  ? 184  SER   A OG   1 
ATOM   3675 N  N    . LEU   B 2 180 ? 25.89147  -16.17071 15.96196  1.000 10.45130  ? 185  LEU   A N    1 
ATOM   3676 C  CA   . LEU   B 2 180 ? 26.00565  -16.74278 14.63000  1.000 17.10532  ? 185  LEU   A CA   1 
ATOM   3677 C  C    . LEU   B 2 180 ? 24.74771  -16.45591 13.82385  1.000 13.55546  ? 185  LEU   A C    1 
ATOM   3678 O  O    . LEU   B 2 180 ? 23.64365  -16.35495 14.36372  1.000 13.50429  ? 185  LEU   A O    1 
ATOM   3679 C  CB   . LEU   B 2 180 ? 26.25074  -18.26976 14.67111  1.000 9.04069   ? 185  LEU   A CB   1 
ATOM   3680 C  CG   . LEU   B 2 180 ? 27.55571  -18.75364 15.30928  1.000 14.88961  ? 185  LEU   A CG   1 
ATOM   3681 C  CD1  . LEU   B 2 180 ? 27.59880  -20.27963 15.37037  1.000 10.57059  ? 185  LEU   A CD1  1 
ATOM   3682 C  CD2  . LEU   B 2 180 ? 28.73576  -18.23360 14.54038  1.000 12.84117  ? 185  LEU   A CD2  1 
ATOM   3683 N  N    . ILE   B 2 181 ? 24.94885  -16.32697 12.51686  1.000 16.35730  ? 186  ILE   A N    1 
ATOM   3684 C  CA   . ILE   B 2 181 ? 23.89495  -16.25209 11.51775  1.000 11.31146  ? 186  ILE   A CA   1 
ATOM   3685 C  C    . ILE   B 2 181 ? 24.10413  -17.41013 10.55983  1.000 13.28332  ? 186  ILE   A C    1 
ATOM   3686 O  O    . ILE   B 2 181 ? 25.24119  -17.69708 10.15697  1.000 14.79718  ? 186  ILE   A O    1 
ATOM   3687 C  CB   . ILE   B 2 181 ? 23.93694  -14.91313 10.74768  1.000 14.69764  ? 186  ILE   A CB   1 
ATOM   3688 C  CG1  . ILE   B 2 181 ? 23.58777  -13.74411 11.66657  1.000 11.97365  ? 186  ILE   A CG1  1 
ATOM   3689 C  CG2  . ILE   B 2 181 ? 23.01208  -14.94026 9.51258   1.000 9.88298   ? 186  ILE   A CG2  1 
ATOM   3690 C  CD1  . ILE   B 2 181 ? 24.05474  -12.42211 11.12555  1.000 10.47462  ? 186  ILE   A CD1  1 
ATOM   3691 N  N    . VAL   B 2 182 ? 23.01921  -18.07523 10.19675  1.000 12.71277  ? 187  VAL   A N    1 
ATOM   3692 C  CA   . VAL   B 2 182 ? 23.04439  -19.09328 9.15781   1.000 13.34276  ? 187  VAL   A CA   1 
ATOM   3693 C  C    . VAL   B 2 182 ? 22.26648  -18.55440 7.96470   1.000 12.62567  ? 187  VAL   A C    1 
ATOM   3694 O  O    . VAL   B 2 182 ? 21.23042  -17.90046 8.13655   1.000 10.64933  ? 187  VAL   A O    1 
ATOM   3695 C  CB   . VAL   B 2 182 ? 22.46542  -20.42929 9.66183   1.000 9.81855   ? 187  VAL   A CB   1 
ATOM   3696 C  CG1  . VAL   B 2 182 ? 21.01436  -20.23836 10.13266  1.000 11.26419  ? 187  VAL   A CG1  1 
ATOM   3697 C  CG2  . VAL   B 2 182 ? 22.54161  -21.47035 8.57389   1.000 9.82168   ? 187  VAL   A CG2  1 
ATOM   3698 N  N    . SER   B 2 183 ? 22.78363  -18.78743 6.75977   1.000 12.44515  ? 188  SER   A N    1 
ATOM   3699 C  CA   . SER   B 2 183 ? 22.11173  -18.36255 5.53467   1.000 8.77661   ? 188  SER   A CA   1 
ATOM   3700 C  C    . SER   B 2 183 ? 22.03691  -19.52861 4.55673   1.000 13.64955  ? 188  SER   A C    1 
ATOM   3701 O  O    . SER   B 2 183 ? 22.87697  -20.43155 4.58587   1.000 9.72204   ? 188  SER   A O    1 
ATOM   3702 C  CB   . SER   B 2 183 ? 22.83372  -17.18354 4.87068   1.000 6.55581   ? 188  SER   A CB   1 
ATOM   3703 O  OG   . SER   B 2 183 ? 24.07481  -17.59348 4.32984   1.000 9.77869   ? 188  SER   A OG   1 
ATOM   3704 N  N    . SER   B 2 184 ? 21.01300  -19.51072 3.69162   1.000 7.73360   ? 189  SER   A N    1 
ATOM   3705 C  CA   . SER   B 2 184 ? 20.81618  -20.56179 2.70166   1.000 11.53264  ? 189  SER   A CA   1 
ATOM   3706 C  C    . SER   B 2 184 ? 20.55428  -19.91488 1.35059   1.000 9.64997   ? 189  SER   A C    1 
ATOM   3707 O  O    . SER   B 2 184 ? 19.96622  -18.83393 1.26947   1.000 8.27496   ? 189  SER   A O    1 
ATOM   3708 C  CB   . SER   B 2 184 ? 19.65220  -21.48985 3.06658   1.000 6.98068   ? 189  SER   A CB   1 
ATOM   3709 O  OG   . SER   B 2 184 ? 18.44914  -20.74992 3.15241   1.000 6.45493   ? 189  SER   A OG   1 
ATOM   3710 N  N    . SER   B 2 185 ? 20.98844  -20.57991 0.28367   1.000 8.27526   ? 190  SER   A N    1 
ATOM   3711 C  CA   . SER   B 2 185 ? 20.95454  -19.91399 -1.01237  1.000 10.73542  ? 190  SER   A CA   1 
ATOM   3712 C  C    . SER   B 2 185 ? 20.67972  -20.90607 -2.13134  1.000 11.83093  ? 190  SER   A C    1 
ATOM   3713 O  O    . SER   B 2 185 ? 21.04079  -22.08704 -2.04424  1.000 11.70847  ? 190  SER   A O    1 
ATOM   3714 C  CB   . SER   B 2 185 ? 22.28352  -19.18292 -1.29226  1.000 9.39175   ? 190  SER   A CB   1 
ATOM   3715 O  OG   . SER   B 2 185 ? 22.39064  -18.77198 -2.65328  1.000 10.92633  ? 190  SER   A OG   1 
ATOM   3716 N  N    . TYR   B 2 186 ? 20.08180  -20.38617 -3.21043  1.000 6.87928   ? 191  TYR   A N    1 
ATOM   3717 C  CA   . TYR   B 2 186 ? 19.96399  -21.11025 -4.46541  1.000 9.04981   ? 191  TYR   A CA   1 
ATOM   3718 C  C    . TYR   B 2 186 ? 21.30408  -21.54319 -5.04024  1.000 13.66187  ? 191  TYR   A C    1 
ATOM   3719 O  O    . TYR   B 2 186 ? 21.31523  -22.35124 -5.98419  1.000 9.06294   ? 191  TYR   A O    1 
ATOM   3720 C  CB   . TYR   B 2 186 ? 19.22904  -20.26035 -5.50353  1.000 9.78722   ? 191  TYR   A CB   1 
ATOM   3721 C  CG   . TYR   B 2 186 ? 17.72405  -20.45045 -5.46668  1.000 11.16555  ? 191  TYR   A CG   1 
ATOM   3722 C  CD1  . TYR   B 2 186 ? 16.97290  -19.98544 -4.38379  1.000 11.99580  ? 191  TYR   A CD1  1 
ATOM   3723 C  CD2  . TYR   B 2 186 ? 17.05521  -21.10555 -6.50372  1.000 9.58006   ? 191  TYR   A CD2  1 
ATOM   3724 C  CE1  . TYR   B 2 186 ? 15.59091  -20.16153 -4.34093  1.000 12.97836  ? 191  TYR   A CE1  1 
ATOM   3725 C  CE2  . TYR   B 2 186 ? 15.69321  -21.29264 -6.46685  1.000 9.31120   ? 191  TYR   A CE2  1 
ATOM   3726 C  CZ   . TYR   B 2 186 ? 14.96107  -20.81363 -5.38096  1.000 14.09985  ? 191  TYR   A CZ   1 
ATOM   3727 O  OH   . TYR   B 2 186 ? 13.59807  -20.97872 -5.32910  1.000 13.91983  ? 191  TYR   A OH   1 
ATOM   3728 N  N    . ASP   B 2 187 ? 22.42599  -21.01609 -4.52915  1.000 8.94233   ? 192  ASP   A N    1 
ATOM   3729 C  CA   . ASP   B 2 187 ? 23.73007  -21.51903 -4.97498  1.000 12.53846  ? 192  ASP   A CA   1 
ATOM   3730 C  C    . ASP   B 2 187 ? 24.05510  -22.90797 -4.40287  1.000 13.55324  ? 192  ASP   A C    1 
ATOM   3731 O  O    . ASP   B 2 187 ? 25.14816  -23.41891 -4.64972  1.000 11.36780  ? 192  ASP   A O    1 
ATOM   3732 C  CB   . ASP   B 2 187 ? 24.84997  -20.51993 -4.63291  1.000 7.23456   ? 192  ASP   A CB   1 
ATOM   3733 C  CG   . ASP   B 2 187 ? 25.13080  -20.39883 -3.12789  1.000 11.36986  ? 192  ASP   A CG   1 
ATOM   3734 O  OD1  . ASP   B 2 187 ? 24.56476  -21.16182 -2.30491  1.000 11.89034  ? 192  ASP   A OD1  1 
ATOM   3735 O  OD2  . ASP   B 2 187 ? 25.94370  -19.51876 -2.77185  1.000 11.43582  ? 192  ASP   A OD2  1 
ATOM   3736 N  N    . GLY   B 2 188 ? 23.14206  -23.52699 -3.65693  1.000 12.39933  ? 193  GLY   A N    1 
ATOM   3737 C  CA   . GLY   B 2 188 ? 23.35609  -24.84995 -3.10783  1.000 8.64358   ? 193  GLY   A CA   1 
ATOM   3738 C  C    . GLY   B 2 188 ? 24.07495  -24.89282 -1.77075  1.000 9.54151   ? 193  GLY   A C    1 
ATOM   3739 O  O    . GLY   B 2 188 ? 24.33897  -25.98878 -1.25666  1.000 9.70607   ? 193  GLY   A O    1 
ATOM   3740 N  N    . LEU   B 2 189 ? 24.40681  -23.75177 -1.19278  1.000 7.70296   ? 194  LEU   A N    1 
ATOM   3741 C  CA   . LEU   B 2 189 ? 25.21068  -23.70665 0.01530   1.000 11.62682  ? 194  LEU   A CA   1 
ATOM   3742 C  C    . LEU   B 2 189 ? 24.39052  -23.20864 1.19019   1.000 11.17048  ? 194  LEU   A C    1 
ATOM   3743 O  O    . LEU   B 2 189 ? 23.47648  -22.40071 1.02904   1.000 8.89205   ? 194  LEU   A O    1 
ATOM   3744 C  CB   . LEU   B 2 189 ? 26.41063  -22.77158 -0.15962  1.000 9.43862   ? 194  LEU   A CB   1 
ATOM   3745 C  CG   . LEU   B 2 189 ? 27.32378  -23.01658 -1.35451  1.000 11.92396  ? 194  LEU   A CG   1 
ATOM   3746 C  CD1  . LEU   B 2 189 ? 28.50371  -22.05350 -1.28244  1.000 9.55292   ? 194  LEU   A CD1  1 
ATOM   3747 C  CD2  . LEU   B 2 189 ? 27.78888  -24.48455 -1.35038  1.000 12.56085  ? 194  LEU   A CD2  1 
ATOM   3748 N  N    A CYS   B 2 190 ? 24.69243  -23.74455 2.36625   0.697 12.47051  ? 195  CYS   A N    1 
ATOM   3749 N  N    B CYS   B 2 190 ? 24.75242  -23.68455 2.37925   0.303 12.47962  ? 195  CYS   A N    1 
ATOM   3750 C  CA   A CYS   B 2 190 ? 24.40225  -23.07550 3.62418   0.697 13.27843  ? 195  CYS   A CA   1 
ATOM   3751 C  CA   B CYS   B 2 190 ? 24.36225  -23.07350 3.64218   0.303 13.23144  ? 195  CYS   A CA   1 
ATOM   3752 C  C    A CYS   B 2 190 ? 25.70415  -22.47839 4.13229   0.697 12.97440  ? 195  CYS   A C    1 
ATOM   3753 C  C    B CYS   B 2 190 ? 25.62714  -22.57038 4.32528   0.303 12.96783  ? 195  CYS   A C    1 
ATOM   3754 O  O    A CYS   B 2 190 ? 26.77121  -23.06333 3.94343   0.697 11.92201  ? 195  CYS   A O    1 
ATOM   3755 O  O    B CYS   B 2 190 ? 26.60118  -23.31931 4.44843   0.303 12.85521  ? 195  CYS   A O    1 
ATOM   3756 C  CB   A CYS   B 2 190 ? 23.82920  -24.03448 4.66617   0.697 13.42947  ? 195  CYS   A CB   1 
ATOM   3757 C  CB   B CYS   B 2 190 ? 23.62522  -24.06750 4.54215   0.303 13.29809  ? 195  CYS   A CB   1 
ATOM   3758 S  SG   A CYS   B 2 190 ? 22.22929  -24.70161 4.25404   0.697 15.81948  ? 195  CYS   A SG   1 
ATOM   3759 S  SG   B CYS   B 2 190 ? 23.62100  -23.60940 6.28913   0.303 13.98228  ? 195  CYS   A SG   1 
ATOM   3760 N  N    . ARG   B 2 191 ? 25.61901  -21.30736 4.75321   1.000 10.84491  ? 196  ARG   A N    1 
ATOM   3761 C  CA   . ARG   B 2 191 ? 26.80591  -20.66125 5.29230   1.000 12.84263  ? 196  ARG   A CA   1 
ATOM   3762 C  C    . ARG   B 2 191 ? 26.50272  -20.11619 6.68224   1.000 13.96484  ? 196  ARG   A C    1 
ATOM   3763 O  O    . ARG   B 2 191 ? 25.38467  -19.67325 6.94410   1.000 10.57178  ? 196  ARG   A O    1 
ATOM   3764 C  CB   . ARG   B 2 191 ? 27.31194  -19.55527 4.34030   1.000 10.52604  ? 196  ARG   A CB   1 
ATOM   3765 C  CG   . ARG   B 2 191 ? 28.18410  -20.14227 3.18942   1.000 15.55317  ? 196  ARG   A CG   1 
ATOM   3766 C  CD   . ARG   B 2 191 ? 28.74514  -19.12829 2.21143   1.000 10.11465  ? 196  ARG   A CD   1 
ATOM   3767 N  NE   . ARG   B 2 191 ? 29.68628  -19.75728 1.28456   1.000 12.45830  ? 196  ARG   A NE   1 
ATOM   3768 C  CZ   . ARG   B 2 191 ? 29.99538  -19.29033 0.07857   1.000 9.14161   ? 196  ARG   A CZ   1 
ATOM   3769 N  NH1  . ARG   B 2 191 ? 29.45536  -18.18239 -0.39555  1.000 7.61133   ? 196  ARG   A NH1  1 
ATOM   3770 N  NH2  . ARG   B 2 191 ? 30.85850  -19.96231 -0.67430  1.000 9.16995   ? 196  ARG   A NH2  1 
ATOM   3771 N  N    . ILE   B 2 192 ? 27.50663  -20.17708 7.56635   1.000 15.48239  ? 197  ILE   A N    1 
ATOM   3772 C  CA   . ILE   B 2 192 ? 27.45245  -19.64100 8.92632   1.000 13.45424  ? 197  ILE   A CA   1 
ATOM   3773 C  C    . ILE   B 2 192 ? 28.34736  -18.40794 8.99134   1.000 15.79725  ? 197  ILE   A C    1 
ATOM   3774 O  O    . ILE   B 2 192 ? 29.45642  -18.40890 8.44546   1.000 15.57748  ? 197  ILE   A O    1 
ATOM   3775 C  CB   . ILE   B 2 192 ? 27.91041  -20.68891 9.96242   1.000 11.68953  ? 197  ILE   A CB   1 
ATOM   3776 C  CG1  . ILE   B 2 192 ? 27.15352  -22.00697 9.78642   1.000 13.08453  ? 197  ILE   A CG1  1 
ATOM   3777 C  CG2  . ILE   B 2 192 ? 27.74622  -20.15785 11.39038  1.000 15.96220  ? 197  ILE   A CG2  1 
ATOM   3778 C  CD1  . ILE   B 2 192 ? 25.79845  -21.99703 10.37827  1.000 21.00204  ? 197  ILE   A CD1  1 
ATOM   3779 N  N    . TRP   B 2 193 ? 27.88122  -17.37093 9.68124   1.000 11.91658  ? 198  TRP   A N    1 
ATOM   3780 C  CA   . TRP   B 2 193 ? 28.57313  -16.09188 9.73824   1.000 9.76099   ? 198  TRP   A CA   1 
ATOM   3781 C  C    . TRP   B 2 193 ? 28.74694  -15.65279 11.18723  1.000 12.96060  ? 198  TRP   A C    1 
ATOM   3782 O  O    . TRP   B 2 193 ? 27.86287  -15.87580 12.01715  1.000 13.92966  ? 198  TRP   A O    1 
ATOM   3783 C  CB   . TRP   B 2 193 ? 27.79514  -15.00598 8.96309   1.000 10.56160  ? 198  TRP   A CB   1 
ATOM   3784 C  CG   . TRP   B 2 193 ? 27.47432  -15.42108 7.56708   1.000 13.34465  ? 198  TRP   A CG   1 
ATOM   3785 C  CD1  . TRP   B 2 193 ? 26.38341  -16.15817 7.14801   1.000 10.74101  ? 198  TRP   A CD1  1 
ATOM   3786 C  CD2  . TRP   B 2 193 ? 28.25243  -15.15609 6.39015   1.000 19.05780  ? 198  TRP   A CD2  1 
ATOM   3787 N  NE1  . TRP   B 2 193 ? 26.44557  -16.35124 5.78302   1.000 16.12717  ? 198  TRP   A NE1  1 
ATOM   3788 C  CE2  . TRP   B 2 193 ? 27.57958  -15.74920 5.29511   1.000 12.90134  ? 198  TRP   A CE2  1 
ATOM   3789 C  CE3  . TRP   B 2 193 ? 29.45741  -14.47302 6.15324   1.000 16.04923  ? 198  TRP   A CE3  1 
ATOM   3790 C  CZ2  . TRP   B 2 193 ? 28.06772  -15.67324 3.98816   1.000 13.19456  ? 198  TRP   A CZ2  1 
ATOM   3791 C  CZ3  . TRP   B 2 193 ? 29.94254  -14.40806 4.85529   1.000 14.34223  ? 198  TRP   A CZ3  1 
ATOM   3792 C  CH2  . TRP   B 2 193 ? 29.24470  -15.00217 3.79025   1.000 11.40707  ? 198  TRP   A CH2  1 
ATOM   3793 N  N    . ASP   B 2 194 ? 29.89087  -15.02270 11.48532  1.000 13.20298  ? 199  ASP   A N    1 
ATOM   3794 C  CA   . ASP   B 2 194 ? 30.10669  -14.39261 12.78431  1.000 11.74426  ? 199  ASP   A CA   1 
ATOM   3795 C  C    . ASP   B 2 194 ? 29.38160  -13.05466 12.80816  1.000 13.58123  ? 199  ASP   A C    1 
ATOM   3796 O  O    . ASP   B 2 194 ? 29.71462  -12.14568 12.03414  1.000 14.04543  ? 199  ASP   A O    1 
ATOM   3797 C  CB   . ASP   B 2 194 ? 31.59965  -14.18650 13.06046  1.000 17.18470  ? 199  ASP   A CB   1 
ATOM   3798 C  CG   . ASP   B 2 194 ? 31.85346  -13.58440 14.43545  1.000 15.71000  ? 199  ASP   A CG   1 
ATOM   3799 O  OD1  . ASP   B 2 194 ? 31.85240  -14.34135 15.42549  1.000 15.75515  ? 199  ASP   A OD1  1 
ATOM   3800 O  OD2  . ASP   B 2 194 ? 31.99036  -12.34839 14.54440  1.000 18.55976  ? 199  ASP   A OD2  1 
ATOM   3801 N  N    . THR   B 2 195 ? 28.38250  -12.93668 13.68204  1.000 16.27911  ? 200  THR   A N    1 
ATOM   3802 C  CA   . THR   B 2 195 ? 27.58841  -11.71272 13.74689  1.000 13.17063  ? 200  THR   A CA   1 
ATOM   3803 C  C    . THR   B 2 195 ? 28.47432  -10.47166 13.84291  1.000 17.69203  ? 200  THR   A C    1 
ATOM   3804 O  O    . THR   B 2 195 ? 28.28433  -9.49271  13.11184  1.000 21.31784  ? 200  THR   A O    1 
ATOM   3805 C  CB   . THR   B 2 195 ? 26.63229  -11.77972 14.93479  1.000 18.07598  ? 200  THR   A CB   1 
ATOM   3806 O  OG1  . THR   B 2 195 ? 25.76238  -12.92379 14.80076  1.000 12.07014  ? 200  THR   A OG1  1 
ATOM   3807 C  CG2  . THR   B 2 195 ? 25.80219  -10.49577 15.01163  1.000 11.67369  ? 200  THR   A CG2  1 
ATOM   3808 N  N    . ALA   B 2 196 ? 29.45622  -10.50155 14.73302  1.000 16.20586  ? 201  ALA   A N    1 
ATOM   3809 C  CA   . ALA   B 2 196 ? 30.19911  -9.29248  15.05303  1.000 15.47097  ? 201  ALA   A CA   1 
ATOM   3810 C  C    . ALA   B 2 196 ? 31.17320  -8.90948  13.94812  1.000 21.09106  ? 201  ALA   A C    1 
ATOM   3811 O  O    . ALA   B 2 196 ? 31.25716  -7.73249  13.58106  1.000 20.91993  ? 201  ALA   A O    1 
ATOM   3812 C  CB   . ALA   B 2 196 ? 30.93898  -9.48236  16.38312  1.000 16.56769  ? 201  ALA   A CB   1 
ATOM   3813 N  N    . SER   B 2 197 ? 31.91432  -9.87746  13.41025  1.000 17.56185  ? 202  SER   A N    1 
ATOM   3814 C  CA   . SER   B 2 197 ? 32.90041  -9.56945  12.38334  1.000 17.29198  ? 202  SER   A CA   1 
ATOM   3815 C  C    . SER   B 2 197 ? 32.33557  -9.65456  10.97428  1.000 15.65162  ? 202  SER   A C    1 
ATOM   3816 O  O    . SER   B 2 197 ? 32.82962  -8.96558  10.07830  1.000 15.51159  ? 202  SER   A O    1 
ATOM   3817 C  CB   . SER   B 2 197 ? 34.10146  -10.50736 12.50152  1.000 16.73598  ? 202  SER   A CB   1 
ATOM   3818 O  OG   . SER   B 2 197 ? 33.75659  -11.83341 12.14356  1.000 19.72193  ? 202  SER   A OG   1 
ATOM   3819 N  N    . GLY   B 2 198 ? 31.29465  -10.45665 10.76022  1.000 17.09560  ? 203  GLY   A N    1 
ATOM   3820 C  CA   . GLY   B 2 198 ? 30.81281  -10.71075 9.42018   1.000 18.63616  ? 203  GLY   A CA   1 
ATOM   3821 C  C    . GLY   B 2 198 ? 31.62195  -11.73774 8.67532   1.000 17.02226  ? 203  GLY   A C    1 
ATOM   3822 O  O    . GLY   B 2 198 ? 31.36510  -11.96982 7.48631   1.000 18.22561  ? 203  GLY   A O    1 
ATOM   3823 N  N    . GLN   B 2 199 ? 32.58992  -12.36264 9.33646   1.000 16.02533  ? 204  GLN   A N    1 
ATOM   3824 C  CA   . GLN   B 2 199 ? 33.39206  -13.38162 8.67960   1.000 19.33060  ? 204  GLN   A CA   1 
ATOM   3825 C  C    . GLN   B 2 199 ? 32.56617  -14.64569 8.48359   1.000 16.04540  ? 204  GLN   A C    1 
ATOM   3826 O  O    . GLN   B 2 199 ? 31.77410  -15.03469 9.34752   1.000 18.17950  ? 204  GLN   A O    1 
ATOM   3827 C  CB   . GLN   B 2 199 ? 34.65800  -13.68849 9.49176   1.000 18.14881  ? 204  GLN   A CB   1 
ATOM   3828 C  CG   . GLN   B 2 199 ? 35.14211  -15.13847 9.31389   1.000 23.38978  ? 204  GLN   A CG   1 
ATOM   3829 C  CD   . GLN   B 2 199 ? 36.45205  -15.48034 10.05705  1.000 43.42181  ? 204  GLN   A CD   1 
ATOM   3830 O  OE1  . GLN   B 2 199 ? 36.59291  -15.26427 11.27205  1.000 36.81676  ? 204  GLN   A OE1  1 
ATOM   3831 N  NE2  . GLN   B 2 199 ? 37.41017  -16.03532 9.31618   1.000 30.21952  ? 204  GLN   A NE2  1 
ATOM   3832 N  N    . CYS   B 2 200 ? 32.73633  -15.28274 7.32664   1.000 16.84141  ? 205  CYS   A N    1 
ATOM   3833 C  CA   . CYS   B 2 200 ? 32.12944  -16.58779 7.10165   1.000 17.29360  ? 205  CYS   A CA   1 
ATOM   3834 C  C    . CYS   B 2 200 ? 32.87643  -17.64570 7.90479   1.000 16.91749  ? 205  CYS   A C    1 
ATOM   3835 O  O    . CYS   B 2 200 ? 34.10445  -17.75162 7.81593   1.000 16.77297  ? 205  CYS   A O    1 
ATOM   3836 C  CB   . CYS   B 2 200 ? 32.14163  -16.93488 5.61167   1.000 11.34989  ? 205  CYS   A CB   1 
ATOM   3837 S  SG   . CYS   B 2 200 ? 31.18177  -18.42196 5.23965   1.000 14.25138  ? 205  CYS   A SG   1 
ATOM   3838 N  N    . LEU   B 2 201 ? 32.13640  -18.43571 8.68875   1.000 13.45024  ? 206  LEU   A N    1 
ATOM   3839 C  CA   . LEU   B 2 201 ? 32.73437  -19.42262 9.58187   1.000 15.41214  ? 206  LEU   A CA   1 
ATOM   3840 C  C    . LEU   B 2 201 ? 32.52151  -20.86565 9.14093   1.000 22.51255  ? 206  LEU   A C    1 
ATOM   3841 O  O    . LEU   B 2 201 ? 33.15151  -21.76958 9.70005   1.000 27.72796  ? 206  LEU   A O    1 
ATOM   3842 C  CB   . LEU   B 2 201 ? 32.18420  -19.26457 11.00380  1.000 12.73644  ? 206  LEU   A CB   1 
ATOM   3843 C  CG   . LEU   B 2 201 ? 32.40904  -17.94352 11.73475  1.000 23.94815  ? 206  LEU   A CG   1 
ATOM   3844 C  CD1  . LEU   B 2 201 ? 31.69890  -17.99449 13.08568  1.000 21.71847  ? 206  LEU   A CD1  1 
ATOM   3845 C  CD2  . LEU   B 2 201 ? 33.89600  -17.64141 11.90390  1.000 22.21649  ? 206  LEU   A CD2  1 
ATOM   3846 N  N    . LYS   B 2 202 ? 31.64963  -21.11477 8.17385   1.000 15.70435  ? 207  LYS   A N    1 
ATOM   3847 C  CA   . LYS   B 2 202 ? 31.39177  -22.48681 7.76290   1.000 15.11639  ? 207  LYS   A CA   1 
ATOM   3848 C  C    . LYS   B 2 202 ? 30.64891  -22.45593 6.43882   1.000 19.28494  ? 207  LYS   A C    1 
ATOM   3849 O  O    . LYS   B 2 202 ? 29.80087  -21.58600 6.22368   1.000 13.73618  ? 207  LYS   A O    1 
ATOM   3850 C  CB   . LYS   B 2 202 ? 30.55870  -23.22980 8.81885   1.000 14.05622  ? 207  LYS   A CB   1 
ATOM   3851 C  CG   . LYS   B 2 202 ? 30.72080  -24.74079 8.79795   1.000 20.72541  ? 207  LYS   A CG   1 
ATOM   3852 C  CD   . LYS   B 2 202 ? 31.91074  -25.15867 9.65210   1.000 26.99543  ? 207  LYS   A CD   1 
ATOM   3853 C  CE   . LYS   B 2 202 ? 32.52788  -26.46465 9.16224   1.000 46.06098  ? 207  LYS   A CE   1 
ATOM   3854 N  NZ   . LYS   B 2 202 ? 34.02987  -26.48055 9.28140   1.000 47.37515  ? 207  LYS   A NZ   1 
ATOM   3855 N  N    . THR   B 2 203 ? 30.95906  -23.40896 5.56390   1.000 15.84158  ? 208  THR   A N    1 
ATOM   3856 C  CA   . THR   B 2 203 ? 30.18621  -23.62408 4.34483   1.000 13.35046  ? 208  THR   A CA   1 
ATOM   3857 C  C    . THR   B 2 203 ? 29.80331  -25.09110 4.32487   1.000 14.54088  ? 208  THR   A C    1 
ATOM   3858 O  O    . THR   B 2 203 ? 30.67837  -25.96405 4.31602   1.000 16.21169  ? 208  THR   A O    1 
ATOM   3859 C  CB   . THR   B 2 203 ? 30.97332  -23.22409 3.08989   1.000 13.16309  ? 208  THR   A CB   1 
ATOM   3860 O  OG1  . THR   B 2 203 ? 31.08323  -21.79409 3.03083   1.000 12.62464  ? 208  THR   A OG1  1 
ATOM   3861 C  CG2  . THR   B 2 203 ? 30.29949  -23.74321 1.80685   1.000 10.05590  ? 208  THR   A CG2  1 
ATOM   3862 N  N    . LEU   B 2 204 ? 28.50632  -25.36219 4.39475   1.000 14.19388  ? 209  LEU   A N    1 
ATOM   3863 C  CA   . LEU   B 2 204 ? 28.00340  -26.72622 4.45077   1.000 17.63183  ? 209  LEU   A CA   1 
ATOM   3864 C  C    . LEU   B 2 204 ? 27.56358  -27.14632 3.05875   1.000 17.69300  ? 209  LEU   A C    1 
ATOM   3865 O  O    . LEU   B 2 204 ? 26.81260  -26.42741 2.40063   1.000 15.33919  ? 209  LEU   A O    1 
ATOM   3866 C  CB   . LEU   B 2 204 ? 26.84031  -26.85624 5.43265   1.000 19.37204  ? 209  LEU   A CB   1 
ATOM   3867 C  CG   . LEU   B 2 204 ? 27.13013  -26.56914 6.90767   1.000 20.91180  ? 209  LEU   A CG   1 
ATOM   3868 C  CD1  . LEU   B 2 204 ? 25.91407  -26.96917 7.71656   1.000 20.99742  ? 209  LEU   A CD1  1 
ATOM   3869 C  CD2  . LEU   B 2 204 ? 28.38212  -27.31703 7.40184   1.000 20.34498  ? 209  LEU   A CD2  1 
ATOM   3870 N  N    . ILE   B 2 205 ? 28.05370  -28.29432 2.60886   1.000 16.78266  ? 210  ILE   A N    1 
ATOM   3871 C  CA   . ILE   B 2 205 ? 27.60788  -28.90141 1.36085   1.000 19.69382  ? 210  ILE   A CA   1 
ATOM   3872 C  C    . ILE   B 2 205 ? 27.81096  -30.39639 1.49195   1.000 21.92839  ? 210  ILE   A C    1 
ATOM   3873 O  O    . ILE   B 2 205 ? 28.76392  -30.84229 2.13908   1.000 27.50772  ? 210  ILE   A O    1 
ATOM   3874 C  CB   . ILE   B 2 205 ? 28.35297  -28.32743 0.13690   1.000 23.68116  ? 210  ILE   A CB   1 
ATOM   3875 C  CG1  . ILE   B 2 205 ? 28.02616  -29.14052 -1.11009  1.000 21.93116  ? 210  ILE   A CG1  1 
ATOM   3876 C  CG2  . ILE   B 2 205 ? 29.87094  -28.28532 0.36106   1.000 15.05371  ? 210  ILE   A CG2  1 
ATOM   3877 C  CD1  . ILE   B 2 205 ? 28.47025  -28.47157 -2.37208  1.000 22.81341  ? 210  ILE   A CD1  1 
ATOM   3878 N  N    . ASP   B 2 206 ? 26.89508  -31.16549 0.90590   1.000 15.54885  ? 211  ASP   A N    1 
ATOM   3879 C  CA   . ASP   B 2 206 ? 26.89816  -32.62148 1.00898   1.000 27.18038  ? 211  ASP   A CA   1 
ATOM   3880 C  C    . ASP   B 2 206 ? 27.39534  -33.22252 -0.30293  1.000 28.29841  ? 211  ASP   A C    1 
ATOM   3881 O  O    . ASP   B 2 206 ? 28.32637  -32.69249 -0.91586  1.000 29.95849  ? 211  ASP   A O    1 
ATOM   3882 C  CB   . ASP   B 2 206 ? 25.48716  -33.14456 1.34586   1.000 27.87533  ? 211  ASP   A CB   1 
ATOM   3883 C  CG   . ASP   B 2 206 ? 25.50617  -34.47451 2.10794   1.000 35.29718  ? 211  ASP   A CG   1 
ATOM   3884 O  OD1  . ASP   B 2 206 ? 26.59919  -35.06743 2.25909   1.000 37.55349  ? 211  ASP   A OD1  1 
ATOM   3885 O  OD2  . ASP   B 2 206 ? 24.42415  -34.92156 2.56784   1.000 38.79322  ? 211  ASP   A OD2  1 
ATOM   3886 N  N    . ASP   B 2 207 ? 26.76746  -34.31559 -0.75194  1.000 33.34862  ? 212  ASP   A N    1 
ATOM   3887 C  CA   . ASP   B 2 207 ? 27.15064  -35.00263 -1.98186  1.000 29.80141  ? 212  ASP   A CA   1 
ATOM   3888 C  C    . ASP   B 2 207 ? 26.69773  -34.27173 -3.23895  1.000 32.51070  ? 212  ASP   A C    1 
ATOM   3889 O  O    . ASP   B 2 207 ? 27.10687  -34.65477 -4.33888  1.000 30.99464  ? 212  ASP   A O    1 
ATOM   3890 C  CB   . ASP   B 2 207 ? 26.57374  -36.41567 -2.00084  1.000 29.15546  ? 212  ASP   A CB   1 
ATOM   3891 C  CG   . ASP   B 2 207 ? 25.07577  -36.42779 -2.31000  1.000 55.33658  ? 212  ASP   A CG   1 
ATOM   3892 O  OD1  . ASP   B 2 207 ? 24.27165  -35.88480 -1.50212  1.000 38.08216  ? 212  ASP   A OD1  1 
ATOM   3893 O  OD2  . ASP   B 2 207 ? 24.70592  -36.96887 -3.38001  1.000 60.04646  ? 212  ASP   A OD2  1 
ATOM   3894 N  N    . ASP   B 2 208 ? 25.86465  -33.24378 -3.10110  1.000 32.46479  ? 213  ASP   A N    1 
ATOM   3895 C  CA   . ASP   B 2 208 ? 25.32372  -32.49188 -4.22520  1.000 29.61838  ? 213  ASP   A CA   1 
ATOM   3896 C  C    . ASP   B 2 208 ? 25.01357  -31.08587 -3.72231  1.000 29.50596  ? 213  ASP   A C    1 
ATOM   3897 O  O    . ASP   B 2 208 ? 25.17442  -30.79279 -2.53231  1.000 28.49179  ? 213  ASP   A O    1 
ATOM   3898 C  CB   . ASP   B 2 208 ? 24.08482  -33.18999 -4.78929  1.000 23.80946  ? 213  ASP   A CB   1 
ATOM   3899 C  CG   . ASP   B 2 208 ? 23.77895  -32.76809 -6.20435  1.000 39.58607  ? 213  ASP   A CG   1 
ATOM   3900 O  OD1  . ASP   B 2 208 ? 24.61296  -32.05207 -6.80330  1.000 37.33402  ? 213  ASP   A OD1  1 
ATOM   3901 O  OD2  . ASP   B 2 208 ? 22.71203  -33.15419 -6.72344  1.000 47.70532  ? 213  ASP   A OD2  1 
ATOM   3902 N  N    . ASN   B 2 209 ? 24.56561  -30.20095 -4.61940  1.000 23.53210  ? 214  ASN   A N    1 
ATOM   3903 C  CA   . ASN   B 2 209 ? 24.20847  -28.83595 -4.21952  1.000 24.28574  ? 214  ASN   A CA   1 
ATOM   3904 C  C    . ASN   B 2 209 ? 22.98352  -28.32908 -4.98668  1.000 19.02540  ? 214  ASN   A C    1 
ATOM   3905 O  O    . ASN   B 2 209 ? 23.03453  -27.30911 -5.68173  1.000 15.87402  ? 214  ASN   A O    1 
ATOM   3906 C  CB   . ASN   B 2 209 ? 25.41043  -27.89888 -4.37044  1.000 24.54294  ? 214  ASN   A CB   1 
ATOM   3907 C  CG   . ASN   B 2 209 ? 25.70256  -27.53494 -5.80143  1.000 19.67194  ? 214  ASN   A CG   1 
ATOM   3908 O  OD1  . ASN   B 2 209 ? 25.82271  -28.39698 -6.66937  1.000 19.28924  ? 214  ASN   A OD1  1 
ATOM   3909 N  ND2  . ASN   B 2 209 ? 25.81150  -26.23195 -6.06049  1.000 24.08686  ? 214  ASN   A ND2  1 
ATOM   3910 N  N    . PRO   B 2 210 ? 21.84455  -29.00414 -4.84076  1.000 17.68547  ? 215  PRO   A N    1 
ATOM   3911 C  CA   . PRO   B 2 210 ? 20.57256  -28.41225 -5.29893  1.000 14.77916  ? 215  PRO   A CA   1 
ATOM   3912 C  C    . PRO   B 2 210 ? 20.23539  -27.18223 -4.47604  1.000 15.04465  ? 215  PRO   A C    1 
ATOM   3913 O  O    . PRO   B 2 210 ? 20.68326  -27.06014 -3.32200  1.000 12.26197  ? 215  PRO   A O    1 
ATOM   3914 C  CB   . PRO   B 2 210 ? 19.55861  -29.53931 -5.05798  1.000 12.56042  ? 215  PRO   A CB   1 
ATOM   3915 C  CG   . PRO   B 2 210 ? 20.12353  -30.26820 -3.85288  1.000 19.10328  ? 215  PRO   A CG   1 
ATOM   3916 C  CD   . PRO   B 2 210 ? 21.63655  -30.26112 -4.09372  1.000 11.77895  ? 215  PRO   A CD   1 
ATOM   3917 N  N    . PRO   B 2 211 ? 19.44539  -26.25031 -5.01117  1.000 12.20591  ? 216  PRO   A N    1 
ATOM   3918 C  CA   . PRO   B 2 211 ? 19.14122  -25.02329 -4.26428  1.000 10.45449  ? 216  PRO   A CA   1 
ATOM   3919 C  C    . PRO   B 2 211 ? 18.77009  -25.32623 -2.82330  1.000 11.61442  ? 216  PRO   A C    1 
ATOM   3920 O  O    . PRO   B 2 211 ? 17.98812  -26.23827 -2.55133  1.000 10.72643  ? 216  PRO   A O    1 
ATOM   3921 C  CB   . PRO   B 2 211 ? 17.95627  -24.43541 -5.03444  1.000 12.64426  ? 216  PRO   A CB   1 
ATOM   3922 C  CG   . PRO   B 2 211 ? 18.18145  -24.89447 -6.43239  1.000 15.00836  ? 216  PRO   A CG   1 
ATOM   3923 C  CD   . PRO   B 2 211 ? 18.80553  -26.25743 -6.33824  1.000 10.19416  ? 216  PRO   A CD   1 
ATOM   3924 N  N    . VAL   B 2 212 ? 19.33794  -24.56214 -1.89128  1.000 10.18979  ? 217  VAL   A N    1 
ATOM   3925 C  CA   . VAL   B 2 212 ? 18.93679  -24.65109 -0.49132  1.000 9.56317   ? 217  VAL   A CA   1 
ATOM   3926 C  C    . VAL   B 2 212 ? 17.83670  -23.61815 -0.26249  1.000 10.97713  ? 217  VAL   A C    1 
ATOM   3927 O  O    . VAL   B 2 212 ? 18.08762  -22.41214 -0.28453  1.000 8.99535   ? 217  VAL   A O    1 
ATOM   3928 C  CB   . VAL   B 2 212 ? 20.11468  -24.44796 0.46380   1.000 9.01400   ? 217  VAL   A CB   1 
ATOM   3929 C  CG1  . VAL   B 2 212 ? 19.68055  -24.82491 1.87077   1.000 5.06616   ? 217  VAL   A CG1  1 
ATOM   3930 C  CG2  . VAL   B 2 212 ? 21.32178  -25.29891 0.01197   1.000 8.02814   ? 217  VAL   A CG2  1 
ATOM   3931 N  N    . SER   B 2 213 ? 16.60771  -24.10222 -0.06860  1.000 10.20218  ? 218  SER   A N    1 
ATOM   3932 C  CA   . SER   B 2 213 ? 15.40966  -23.27530 -0.05177  1.000 9.67203   ? 218  SER   A CA   1 
ATOM   3933 C  C    . SER   B 2 213 ? 15.02348  -22.81225 1.34616   1.000 10.44265  ? 218  SER   A C    1 
ATOM   3934 O  O    . SER   B 2 213 ? 14.15740  -21.93830 1.47602   1.000 6.31054   ? 218  SER   A O    1 
ATOM   3935 C  CB   . SER   B 2 213 ? 14.24278  -24.05142 -0.67786  1.000 10.50590  ? 218  SER   A CB   1 
ATOM   3936 O  OG   . SER   B 2 213 ? 14.10579  -25.31639 -0.05480  1.000 9.04630   ? 218  SER   A OG   1 
ATOM   3937 N  N    . PHE   B 2 214 ? 15.63740  -23.36515 2.38726   1.000 6.96978   ? 219  PHE   A N    1 
ATOM   3938 C  CA   . PHE   B 2 214 ? 15.32123  -22.94510 3.74220   1.000 8.54252   ? 219  PHE   A CA   1 
ATOM   3939 C  C    . PHE   B 2 214 ? 16.38016  -23.46297 4.70334   1.000 8.58939   ? 219  PHE   A C    1 
ATOM   3940 O  O    . PHE   B 2 214 ? 16.89225  -24.57195 4.52546   1.000 8.86102   ? 219  PHE   A O    1 
ATOM   3941 C  CB   . PHE   B 2 214 ? 13.94721  -23.45716 4.17908   1.000 6.05919   ? 219  PHE   A CB   1 
ATOM   3942 C  CG   . PHE   B 2 214 ? 13.69404  -23.26210 5.64104   1.000 8.39533   ? 219  PHE   A CG   1 
ATOM   3943 C  CD1  . PHE   B 2 214 ? 13.17291  -22.06711 6.10992   1.000 8.67776   ? 219  PHE   A CD1  1 
ATOM   3944 C  CD2  . PHE   B 2 214 ? 14.00701  -24.26003 6.54413   1.000 11.07568  ? 219  PHE   A CD2  1 
ATOM   3945 C  CE1  . PHE   B 2 214 ? 12.95476  -21.86105 7.46088   1.000 11.01558  ? 219  PHE   A CE1  1 
ATOM   3946 C  CE2  . PHE   B 2 214 ? 13.79185  -24.06797 7.90810   1.000 17.37666  ? 219  PHE   A CE2  1 
ATOM   3947 C  CZ   . PHE   B 2 214 ? 13.26873  -22.86198 8.36397   1.000 12.17901  ? 219  PHE   A CZ   1 
ATOM   3948 N  N    . VAL   B 2 215 ? 16.64999  -22.68490 5.75533   1.000 9.18664   ? 220  VAL   A N    1 
ATOM   3949 C  CA   . VAL   B 2 215 ? 17.52191  -23.14678 6.83345   1.000 10.72145  ? 220  VAL   A CA   1 
ATOM   3950 C  C    . VAL   B 2 215 ? 17.19272  -22.39473 8.11237   1.000 11.36764  ? 220  VAL   A C    1 
ATOM   3951 O  O    . VAL   B 2 215 ? 16.80465  -21.22476 8.08026   1.000 9.88384   ? 220  VAL   A O    1 
ATOM   3952 C  CB   . VAL   B 2 215 ? 19.01594  -22.97970 6.46160   1.000 12.39518  ? 220  VAL   A CB   1 
ATOM   3953 C  CG1  . VAL   B 2 215 ? 19.40284  -21.49867 6.46956   1.000 7.86394   ? 220  VAL   A CG1  1 
ATOM   3954 C  CG2  . VAL   B 2 215 ? 19.87589  -23.79759 7.41573   1.000 14.43364  ? 220  VAL   A CG2  1 
ATOM   3955 N  N    . LYS   B 2 216 ? 17.37064  -23.06965 9.24743   1.000 11.63769  ? 221  LYS   A N    1 
ATOM   3956 C  CA   . LYS   B 2 216 ? 17.35346  -22.40758 10.54239  1.000 11.37245  ? 221  LYS   A CA   1 
ATOM   3957 C  C    . LYS   B 2 216 ? 18.18141  -23.21947 11.53952  1.000 12.86408  ? 221  LYS   A C    1 
ATOM   3958 O  O    . LYS   B 2 216 ? 18.42951  -24.41547 11.34961  1.000 12.86524  ? 221  LYS   A O    1 
ATOM   3959 C  CB   . LYS   B 2 216 ? 15.92239  -22.22365 11.05722  1.000 9.26952   ? 221  LYS   A CB   1 
ATOM   3960 C  CG   . LYS   B 2 216 ? 15.38640  -23.45965 11.73023  1.000 11.68848  ? 221  LYS   A CG   1 
ATOM   3961 C  CD   . LYS   B 2 216 ? 13.85940  -23.46175 11.76007  1.000 20.02110  ? 221  LYS   A CD   1 
ATOM   3962 C  CE   . LYS   B 2 216 ? 13.27623  -22.35774 12.63995  1.000 12.62544  ? 221  LYS   A CE   1 
ATOM   3963 N  NZ   . LYS   B 2 216 ? 11.78024  -22.51983 12.70479  1.000 19.29350  ? 221  LYS   A NZ   1 
ATOM   3964 N  N    . PHE   B 2 217 ? 18.60225  -22.54738 12.61453  1.000 9.44619   ? 222  PHE   A N    1 
ATOM   3965 C  CA   . PHE   B 2 217 ? 19.21917  -23.21628 13.75363  1.000 16.02966  ? 222  PHE   A CA   1 
ATOM   3966 C  C    . PHE   B 2 217 ? 18.19013  -23.98930 14.56756  1.000 19.44096  ? 222  PHE   A C    1 
ATOM   3967 O  O    . PHE   B 2 217 ? 17.03109  -23.57637 14.70442  1.000 17.15533  ? 222  PHE   A O    1 
ATOM   3968 C  CB   . PHE   B 2 217 ? 19.88600  -22.20918 14.69165  1.000 13.52684  ? 222  PHE   A CB   1 
ATOM   3969 C  CG   . PHE   B 2 217 ? 21.18702  -21.67812 14.18776  1.000 11.60116  ? 222  PHE   A CG   1 
ATOM   3970 C  CD1  . PHE   B 2 217 ? 22.32407  -22.45205 14.23692  1.000 11.52320  ? 222  PHE   A CD1  1 
ATOM   3971 C  CD2  . PHE   B 2 217 ? 21.26999  -20.39715 13.68769  1.000 10.99588  ? 222  PHE   A CD2  1 
ATOM   3972 C  CE1  . PHE   B 2 217 ? 23.52208  -21.95799 13.79602  1.000 10.48159  ? 222  PHE   A CE1  1 
ATOM   3973 C  CE2  . PHE   B 2 217 ? 22.46401  -19.89509 13.23880  1.000 16.21365  ? 222  PHE   A CE2  1 
ATOM   3974 C  CZ   . PHE   B 2 217 ? 23.59605  -20.67902 13.29096  1.000 14.85881  ? 222  PHE   A CZ   1 
ATOM   3975 N  N    . SER   B 2 218 ? 18.64214  -25.10124 15.15868  1.000 17.88975  ? 223  SER   A N    1 
ATOM   3976 C  CA   . SER   B 2 218 ? 17.83008  -25.77224 16.16663  1.000 23.58647  ? 223  SER   A CA   1 
ATOM   3977 C  C    . SER   B 2 218 ? 17.75189  -24.92817 17.44257  1.000 21.86202  ? 223  SER   A C    1 
ATOM   3978 O  O    . SER   B 2 218 ? 18.60880  -24.07010 17.70061  1.000 15.77111  ? 223  SER   A O    1 
ATOM   3979 C  CB   . SER   B 2 218 ? 18.37714  -27.16718 16.48576  1.000 17.99651  ? 223  SER   A CB   1 
ATOM   3980 O  OG   . SER   B 2 218 ? 19.66407  -27.11307 17.05990  1.000 17.39122  ? 223  SER   A OG   1 
ATOM   3981 N  N    . PRO   B 2 219 ? 16.71182  -25.14420 18.25147  1.000 17.58668  ? 224  PRO   A N    1 
ATOM   3982 C  CA   . PRO   B 2 219 ? 16.55063  -24.33114 19.46941  1.000 21.86462  ? 224  PRO   A CA   1 
ATOM   3983 C  C    . PRO   B 2 219 ? 17.72953  -24.41401 20.42854  1.000 20.72383  ? 224  PRO   A C    1 
ATOM   3984 O  O    . PRO   B 2 219 ? 17.97839  -23.44995 21.16351  1.000 22.45439  ? 224  PRO   A O    1 
ATOM   3985 C  CB   . PRO   B 2 219 ? 15.26060  -24.89119 20.08930  1.000 19.92149  ? 224  PRO   A CB   1 
ATOM   3986 C  CG   . PRO   B 2 219 ? 14.49076  -25.40630 18.93325  1.000 17.89055  ? 224  PRO   A CG   1 
ATOM   3987 C  CD   . PRO   B 2 219 ? 15.52890  -25.97629 17.97839  1.000 20.27739  ? 224  PRO   A CD   1 
ATOM   3988 N  N    . ASN   B 2 220 ? 18.47461  -25.51796 20.43968  1.000 22.78168  ? 225  ASN   A N    1 
ATOM   3989 C  CA   . ASN   B 2 220 ? 19.64852  -25.61183 21.29781  1.000 28.85408  ? 225  ASN   A CA   1 
ATOM   3990 C  C    . ASN   B 2 220 ? 20.88955  -24.99778 20.66091  1.000 30.06478  ? 225  ASN   A C    1 
ATOM   3991 O  O    . ASN   B 2 220 ? 21.92247  -24.88368 21.33102  1.000 32.45625  ? 225  ASN   A O    1 
ATOM   3992 C  CB   . ASN   B 2 220 ? 19.91758  -27.07679 21.66692  1.000 28.32653  ? 225  ASN   A CB   1 
ATOM   3993 C  CG   . ASN   B 2 220 ? 20.52475  -27.87282 20.52303  1.000 35.91463  ? 225  ASN   A CG   1 
ATOM   3994 O  OD1  . ASN   B 2 220 ? 20.51785  -27.43488 19.36901  1.000 34.28632  ? 225  ASN   A OD1  1 
ATOM   3995 N  ND2  . ASN   B 2 220 ? 21.04780  -29.05776 20.83615  1.000 37.21998  ? 225  ASN   A ND2  1 
ATOM   3996 N  N    . GLY   B 2 221 ? 20.81966  -24.60286 19.38988  1.000 28.00755  ? 226  GLY   A N    1 
ATOM   3997 C  CA   . GLY   B 2 221 ? 21.95369  -24.00682 18.71397  1.000 24.66332  ? 226  GLY   A CA   1 
ATOM   3998 C  C    . GLY   B 2 221 ? 22.95982  -24.98979 18.16013  1.000 28.68142  ? 226  GLY   A C    1 
ATOM   3999 O  O    . GLY   B 2 221 ? 23.87387  -24.57077 17.43121  1.000 26.34211  ? 226  GLY   A O    1 
ATOM   4000 N  N    . LYS   B 2 222 ? 22.81587  -26.28378 18.46119  1.000 25.81708  ? 227  LYS   A N    1 
ATOM   4001 C  CA   . LYS   B 2 222 ? 23.79798  -27.27374 18.03335  1.000 33.30654  ? 227  LYS   A CA   1 
ATOM   4002 C  C    . LYS   B 2 222 ? 23.61117  -27.69983 16.57635  1.000 29.39159  ? 227  LYS   A C    1 
ATOM   4003 O  O    . LYS   B 2 222 ? 24.58626  -28.08480 15.91848  1.000 22.61247  ? 227  LYS   A O    1 
ATOM   4004 C  CB   . LYS   B 2 222 ? 23.72796  -28.49669 18.95741  1.000 37.90179  ? 227  LYS   A CB   1 
ATOM   4005 C  CG   . LYS   B 2 222 ? 25.07098  -29.16659 19.20259  1.000 44.73594  ? 227  LYS   A CG   1 
ATOM   4006 C  CD   . LYS   B 2 222 ? 25.02891  -30.07652 20.43164  1.000 50.82425  ? 227  LYS   A CD   1 
ATOM   4007 C  CE   . LYS   B 2 222 ? 24.60904  -31.49957 20.07667  1.000 43.98690  ? 227  LYS   A CE   1 
ATOM   4008 N  NZ   . LYS   B 2 222 ? 25.55919  -32.14056 19.11381  1.000 49.17651  ? 227  LYS   A NZ   1 
ATOM   4009 N  N    . TYR   B 2 223 ? 22.39422  -27.63494 16.04722  1.000 25.45987  ? 228  TYR   A N    1 
ATOM   4010 C  CA   . TYR   B 2 223 ? 22.12940  -28.14803 14.71022  1.000 20.26262  ? 228  TYR   A CA   1 
ATOM   4011 C  C    . TYR   B 2 223 ? 21.60542  -27.06312 13.77610  1.000 18.67437  ? 228  TYR   A C    1 
ATOM   4012 O  O    . TYR   B 2 223 ? 21.20431  -25.96812 14.18100  1.000 17.83621  ? 228  TYR   A O    1 
ATOM   4013 C  CB   . TYR   B 2 223 ? 21.13147  -29.31610 14.74718  1.000 18.55599  ? 228  TYR   A CB   1 
ATOM   4014 C  CG   . TYR   B 2 223 ? 21.45342  -30.33002 15.80627  1.000 28.75530  ? 228  TYR   A CG   1 
ATOM   4015 C  CD1  . TYR   B 2 223 ? 22.62948  -31.07094 15.75044  1.000 28.60051  ? 228  TYR   A CD1  1 
ATOM   4016 C  CD2  . TYR   B 2 223 ? 20.59332  -30.54201 16.87119  1.000 27.72574  ? 228  TYR   A CD2  1 
ATOM   4017 C  CE1  . TYR   B 2 223 ? 22.93043  -31.99987 16.72352  1.000 38.81642  ? 228  TYR   A CE1  1 
ATOM   4018 C  CE2  . TYR   B 2 223 ? 20.88228  -31.46794 17.84827  1.000 33.64687  ? 228  TYR   A CE2  1 
ATOM   4019 C  CZ   . TYR   B 2 223 ? 22.04934  -32.19487 17.77144  1.000 40.70607  ? 228  TYR   A CZ   1 
ATOM   4020 O  OH   . TYR   B 2 223 ? 22.33829  -33.11979 18.74952  1.000 41.80475  ? 228  TYR   A OH   1 
ATOM   4021 N  N    . ILE   B 2 224 ? 21.61658  -27.43419 12.50312  1.000 16.73592  ? 229  ILE   A N    1 
ATOM   4022 C  CA   . ILE   B 2 224 ? 21.04765  -26.68429 11.39602  1.000 19.48166  ? 229  ILE   A CA   1 
ATOM   4023 C  C    . ILE   B 2 224 ? 20.02679  -27.59840 10.71896  1.000 14.26879  ? 229  ILE   A C    1 
ATOM   4024 O  O    . ILE   B 2 224 ? 20.30789  -28.78039 10.49306  1.000 15.35959  ? 229  ILE   A O    1 
ATOM   4025 C  CB   . ILE   B 2 224 ? 22.17573  -26.23927 10.43512  1.000 21.23366  ? 229  ILE   A CB   1 
ATOM   4026 C  CG1  . ILE   B 2 224 ? 22.67159  -24.84621 10.81909  1.000 20.81063  ? 229  ILE   A CG1  1 
ATOM   4027 C  CG2  . ILE   B 2 224 ? 21.83190  -26.40437 8.94909   1.000 17.55676  ? 229  ILE   A CG2  1 
ATOM   4028 C  CD1  . ILE   B 2 224 ? 21.62147  -24.01125 11.43293  1.000 24.47099  ? 229  ILE   A CD1  1 
ATOM   4029 N  N    . LEU   B 2 225 ? 18.83278  -27.07149 10.44481  1.000 13.03001  ? 230  LEU   A N    1 
ATOM   4030 C  CA   . LEU   B 2 225 ? 17.81291  -27.77160 9.67274   1.000 12.54271  ? 230  LEU   A CA   1 
ATOM   4031 C  C    . LEU   B 2 225 ? 17.69601  -27.10368 8.30869   1.000 16.77446  ? 230  LEU   A C    1 
ATOM   4032 O  O    . LEU   B 2 225 ? 17.40394  -25.90071 8.22659   1.000 13.38986  ? 230  LEU   A O    1 
ATOM   4033 C  CB   . LEU   B 2 225 ? 16.46983  -27.75365 10.39759  1.000 16.82267  ? 230  LEU   A CB   1 
ATOM   4034 C  CG   . LEU   B 2 225 ? 15.27795  -28.32177 9.62949   1.000 16.22028  ? 230  LEU   A CG   1 
ATOM   4035 C  CD1  . LEU   B 2 225 ? 15.44908  -29.81677 9.37760   1.000 13.76754  ? 230  LEU   A CD1  1 
ATOM   4036 C  CD2  . LEU   B 2 225 ? 13.98985  -28.03581 10.39334  1.000 18.79980  ? 230  LEU   A CD2  1 
ATOM   4037 N  N    . ALA   B 2 226 ? 17.91918  -27.87373 7.23875   1.000 11.32420  ? 231  ALA   A N    1 
ATOM   4038 C  CA   . ALA   B 2 226 ? 17.98828  -27.27880 5.90873   1.000 12.17630  ? 231  ALA   A CA   1 
ATOM   4039 C  C    . ALA   B 2 226 ? 17.11044  -28.03391 4.92367   1.000 9.70980   ? 231  ALA   A C    1 
ATOM   4040 O  O    . ALA   B 2 226 ? 17.11952  -29.26991 4.88274   1.000 14.31524  ? 231  ALA   A O    1 
ATOM   4041 C  CB   . ALA   B 2 226 ? 19.43134  -27.24873 5.37588   1.000 9.99671   ? 231  ALA   A CB   1 
ATOM   4042 N  N    . ALA   B 2 227 ? 16.37047  -27.28401 4.11755   1.000 8.20399   ? 232  ALA   A N    1 
ATOM   4043 C  CA   . ALA   B 2 227 ? 15.58963  -27.85112 3.02950   1.000 12.20879  ? 232  ALA   A CA   1 
ATOM   4044 C  C    . ALA   B 2 227 ? 16.28876  -27.63115 1.69256   1.000 9.84373   ? 232  ALA   A C    1 
ATOM   4045 O  O    . ALA   B 2 227 ? 16.81072  -26.54113 1.41956   1.000 6.81491   ? 232  ALA   A O    1 
ATOM   4046 C  CB   . ALA   B 2 227 ? 14.19259  -27.23221 2.98232   1.000 7.08540   ? 232  ALA   A CB   1 
ATOM   4047 N  N    . THR   B 2 228 ? 16.26392  -28.65120 0.84062   1.000 5.40430   ? 233  THR   A N    1 
ATOM   4048 C  CA   . THR   B 2 228 ? 16.73105  -28.47024 -0.52334  1.000 11.54843  ? 233  THR   A CA   1 
ATOM   4049 C  C    . THR   B 2 228 ? 15.62718  -28.82337 -1.51344  1.000 11.49699  ? 233  THR   A C    1 
ATOM   4050 O  O    . THR   B 2 228 ? 14.73520  -29.62841 -1.22449  1.000 10.41666  ? 233  THR   A O    1 
ATOM   4051 C  CB   . THR   B 2 228 ? 18.00514  -29.30117 -0.79716  1.000 10.80986  ? 233  THR   A CB   1 
ATOM   4052 O  OG1  . THR   B 2 228 ? 17.91415  -30.56114 -0.13510  1.000 13.22989  ? 233  THR   A OG1  1 
ATOM   4053 C  CG2  . THR   B 2 228 ? 19.23303  -28.57806 -0.27007  1.000 11.04963  ? 233  THR   A CG2  1 
ATOM   4054 N  N    . LEU   B 2 229 ? 15.68227  -28.19643 -2.69147  1.000 9.60945   ? 234  LEU   A N    1 
ATOM   4055 C  CA   . LEU   B 2 229 ? 14.65239  -28.39256 -3.70557  1.000 8.63612   ? 234  LEU   A CA   1 
ATOM   4056 C  C    . LEU   B 2 229 ? 14.77355  -29.73059 -4.42448  1.000 15.38757  ? 234  LEU   A C    1 
ATOM   4057 O  O    . LEU   B 2 229 ? 14.56269  -29.80967 -5.63450  1.000 11.75801  ? 234  LEU   A O    1 
ATOM   4058 C  CB   . LEU   B 2 229 ? 14.68942  -27.23061 -4.69863  1.000 11.62534  ? 234  LEU   A CB   1 
ATOM   4059 C  CG   . LEU   B 2 229 ? 14.19726  -25.91061 -4.09076  1.000 12.65327  ? 234  LEU   A CG   1 
ATOM   4060 C  CD1  . LEU   B 2 229 ? 13.95031  -24.84568 -5.15884  1.000 11.47497  ? 234  LEU   A CD1  1 
ATOM   4061 C  CD2  . LEU   B 2 229 ? 12.94819  -26.14664 -3.25488  1.000 10.10707  ? 234  LEU   A CD2  1 
ATOM   4062 N  N    . ASP   B 2 230 ? 15.14555  -30.78652 -3.69938  1.000 15.85321  ? 235  ASP   A N    1 
ATOM   4063 C  CA   . ASP   B 2 230 ? 15.06969  -32.16156 -4.17431  1.000 17.60026  ? 235  ASP   A CA   1 
ATOM   4064 C  C    . ASP   B 2 230 ? 14.16764  -32.96856 -3.24937  1.000 18.88774  ? 235  ASP   A C    1 
ATOM   4065 O  O    . ASP   B 2 230 ? 14.41269  -34.15153 -2.99927  1.000 15.09959  ? 235  ASP   A O    1 
ATOM   4066 C  CB   . ASP   B 2 230 ? 16.46274  -32.79847 -4.27913  1.000 12.50714  ? 235  ASP   A CB   1 
ATOM   4067 C  CG   . ASP   B 2 230 ? 17.24160  -32.70434 -2.98505  1.000 18.09886  ? 235  ASP   A CG   1 
ATOM   4068 O  OD1  . ASP   B 2 230 ? 16.69845  -32.12433 -2.01814  1.000 16.77999  ? 235  ASP   A OD1  1 
ATOM   4069 O  OD2  . ASP   B 2 230 ? 18.40062  -33.18827 -2.93390  1.000 22.16140  ? 235  ASP   A OD2  1 
ATOM   4070 N  N    . ASN   B 2 231 ? 13.14054  -32.31360 -2.69951  1.000 13.82863  ? 236  ASN   A N    1 
ATOM   4071 C  CA   . ASN   B 2 231 ? 12.17849  -32.97962 -1.82958  1.000 16.70904  ? 236  ASN   A CA   1 
ATOM   4072 C  C    . ASN   B 2 231 ? 12.83539  -33.51250 -0.55948  1.000 12.45009  ? 236  ASN   A C    1 
ATOM   4073 O  O    . ASN   B 2 231 ? 12.52841  -34.61050 -0.10345  1.000 15.89853  ? 236  ASN   A O    1 
ATOM   4074 C  CB   . ASN   B 2 231 ? 11.47565  -34.10970 -2.58059  1.000 12.85794  ? 236  ASN   A CB   1 
ATOM   4075 C  CG   . ASN   B 2 231 ? 11.10277  -33.70581 -3.98065  1.000 23.86489  ? 236  ASN   A CG   1 
ATOM   4076 O  OD1  . ASN   B 2 231 ? 10.24373  -32.83188 -4.18280  1.000 17.43337  ? 236  ASN   A OD1  1 
ATOM   4077 N  ND2  . ASN   B 2 231 ? 11.76492  -34.31482 -4.97055  1.000 13.40787  ? 236  ASN   A ND2  1 
ATOM   4078 N  N    . THR   B 2 232 ? 13.75028  -32.74341 0.02858   1.000 15.89781  ? 237  THR   A N    1 
ATOM   4079 C  CA   . THR   B 2 232 ? 14.56220  -33.29329 1.10969   1.000 16.07911  ? 237  THR   A CA   1 
ATOM   4080 C  C    . THR   B 2 232 ? 14.86801  -32.26021 2.18767   1.000 16.41132  ? 237  THR   A C    1 
ATOM   4081 O  O    . THR   B 2 232 ? 15.24297  -31.12121 1.87765   1.000 13.54961  ? 237  THR   A O    1 
ATOM   4082 C  CB   . THR   B 2 232 ? 15.87729  -33.86124 0.55987   1.000 16.35812  ? 237  THR   A CB   1 
ATOM   4083 O  OG1  . THR   B 2 232 ? 15.60246  -34.88931 -0.40011  1.000 24.03970  ? 237  THR   A OG1  1 
ATOM   4084 C  CG2  . THR   B 2 232 ? 16.70521  -34.44512 1.67499   1.000 18.26783  ? 237  THR   A CG2  1 
ATOM   4085 N  N    . LEU   B 2 233 ? 14.70990  -32.67815 3.44968   1.000 13.17069  ? 238  LEU   A N    1 
ATOM   4086 C  CA   A LEU   B 2 233 ? 15.14573  -31.92106 4.61468   0.618 15.42116  ? 238  LEU   A CA   1 
ATOM   4087 C  CA   B LEU   B 2 233 ? 15.14573  -31.92106 4.61668   0.382 15.39183  ? 238  LEU   A CA   1 
ATOM   4088 C  C    . LEU   B 2 233 ? 16.27870  -32.66495 5.30384   1.000 12.94215  ? 238  LEU   A C    1 
ATOM   4089 O  O    . LEU   B 2 233 ? 16.26778  -33.89894 5.37291   1.000 16.48470  ? 238  LEU   A O    1 
ATOM   4090 C  CB   A LEU   B 2 233 ? 14.00661  -31.71608 5.61255   0.618 15.57740  ? 238  LEU   A CB   1 
ATOM   4091 C  CB   B LEU   B 2 233 ? 14.01561  -31.71508 5.62855   0.382 15.53915  ? 238  LEU   A CB   1 
ATOM   4092 C  CG   A LEU   B 2 233 ? 12.92958  -30.70917 5.24437   0.618 14.39697  ? 238  LEU   A CG   1 
ATOM   4093 C  CG   B LEU   B 2 233 ? 13.12054  -30.49715 5.47038   0.382 14.25626  ? 238  LEU   A CG   1 
ATOM   4094 C  CD1  A LEU   B 2 233 ? 11.61554  -31.12922 5.88726   0.618 12.59237  ? 238  LEU   A CD1  1 
ATOM   4095 C  CD1  B LEU   B 2 233 ? 12.24469  -30.69127 4.25830   0.382 15.07435  ? 238  LEU   A CD1  1 
ATOM   4096 C  CD2  A LEU   B 2 233 ? 13.34744  -29.31412 5.70434   0.618 13.65221  ? 238  LEU   A CD2  1 
ATOM   4097 C  CD2  B LEU   B 2 233 ? 12.28139  -30.28013 6.73128   0.382 13.07683  ? 238  LEU   A CD2  1 
ATOM   4098 N  N    . LYS   B 2 234 ? 17.23960  -31.91185 5.82690   1.000 10.78444  ? 239  LYS   A N    1 
ATOM   4099 C  CA   . LYS   B 2 234 ? 18.40957  -32.49174 6.46906   1.000 18.90636  ? 239  LYS   A CA   1 
ATOM   4100 C  C    . LYS   B 2 234 ? 18.74338  -31.74365 7.75006   1.000 16.72926  ? 239  LYS   A C    1 
ATOM   4101 O  O    . LYS   B 2 234 ? 18.69629  -30.50965 7.79598   1.000 15.84692  ? 239  LYS   A O    1 
ATOM   4102 C  CB   . LYS   B 2 234 ? 19.62367  -32.47071 5.53919   1.000 13.80394  ? 239  LYS   A CB   1 
ATOM   4103 C  CG   . LYS   B 2 234 ? 19.50186  -33.37179 4.31123   1.000 19.54729  ? 239  LYS   A CG   1 
ATOM   4104 C  CD   . LYS   B 2 234 ? 20.78794  -33.31075 3.49836   1.000 21.99353  ? 239  LYS   A CD   1 
ATOM   4105 C  CE   . LYS   B 2 234 ? 20.73513  -34.11782 2.21340   1.000 24.09529  ? 239  LYS   A CE   1 
ATOM   4106 N  NZ   . LYS   B 2 234 ? 22.02420  -33.93978 1.43253   1.000 25.60324  ? 239  LYS   A NZ   1 
ATOM   4107 N  N    . LEU   B 2 235 ? 19.10132  -32.49957 8.77814   1.000 10.36544  ? 240  LEU   A N    1 
ATOM   4108 C  CA   . LEU   B 2 235 ? 19.56415  -31.94646 10.04016  1.000 11.06532  ? 240  LEU   A CA   1 
ATOM   4109 C  C    . LEU   B 2 235 ? 21.08015  -32.09036 10.10333  1.000 17.30427  ? 240  LEU   A C    1 
ATOM   4110 O  O    . LEU   B 2 235 ? 21.60723  -33.20733 10.09945  1.000 16.21415  ? 240  LEU   A O    1 
ATOM   4111 C  CB   . LEU   B 2 235 ? 18.90207  -32.66444 11.21013  1.000 10.13688  ? 240  LEU   A CB   1 
ATOM   4112 C  CG   . LEU   B 2 235 ? 19.19289  -32.20234 12.63713  1.000 14.08972  ? 240  LEU   A CG   1 
ATOM   4113 C  CD1  . LEU   B 2 235 ? 18.55977  -30.83637 12.90399  1.000 16.00162  ? 240  LEU   A CD1  1 
ATOM   4114 C  CD2  . LEU   B 2 235 ? 18.67785  -33.24532 13.60913  1.000 20.79928  ? 240  LEU   A CD2  1 
ATOM   4115 N  N    . TRP   B 2 236 ? 21.77607  -30.96131 10.15734  1.000 21.58155  ? 241  TRP   A N    1 
ATOM   4116 C  CA   . TRP   B 2 236 ? 23.22807  -30.92622 10.13749  1.000 20.79405  ? 241  TRP   A CA   1 
ATOM   4117 C  C    . TRP   B 2 236 ? 23.76290  -30.61510 11.52953  1.000 24.60514  ? 241  TRP   A C    1 
ATOM   4118 O  O    . TRP   B 2 236 ? 23.20877  -29.77310 12.24543  1.000 16.59727  ? 241  TRP   A O    1 
ATOM   4119 C  CB   . TRP   B 2 236 ? 23.73510  -29.86124 9.16449   1.000 18.48364  ? 241  TRP   A CB   1 
ATOM   4120 C  CG   . TRP   B 2 236 ? 23.57528  -30.19433 7.72349   1.000 24.65508  ? 241  TRP   A CG   1 
ATOM   4121 C  CD1  . TRP   B 2 236 ? 22.41636  -30.18644 6.99136   1.000 24.88495  ? 241  TRP   A CD1  1 
ATOM   4122 C  CD2  . TRP   B 2 236 ? 24.61740  -30.56931 6.81962   1.000 24.16059  ? 241  TRP   A CD2  1 
ATOM   4123 N  NE1  . TRP   B 2 236 ? 22.67552  -30.54750 5.69041   1.000 18.35758  ? 241  TRP   A NE1  1 
ATOM   4124 C  CE2  . TRP   B 2 236 ? 24.02055  -30.78742 5.55857   1.000 26.51287  ? 241  TRP   A CE2  1 
ATOM   4125 C  CE3  . TRP   B 2 236 ? 26.00440  -30.75921 6.95878   1.000 26.10364  ? 241  TRP   A CE3  1 
ATOM   4126 C  CZ2  . TRP   B 2 236 ? 24.76570  -31.17243 4.43367   1.000 27.61615  ? 241  TRP   A CZ2  1 
ATOM   4127 C  CZ3  . TRP   B 2 236 ? 26.74355  -31.14322 5.84588   1.000 21.75612  ? 241  TRP   A CZ3  1 
ATOM   4128 C  CH2  . TRP   B 2 236 ? 26.12269  -31.34233 4.59783   1.000 27.18630  ? 241  TRP   A CH2  1 
ATOM   4129 N  N    . ASP   B 2 237 ? 24.84590  -31.29201 11.90669  1.000 25.98585  ? 242  ASP   A N    1 
ATOM   4130 C  CA   . ASP   B 2 237 ? 25.74376  -30.77589 12.93475  1.000 19.88526  ? 242  ASP   A CA   1 
ATOM   4131 C  C    . ASP   B 2 237 ? 26.71778  -29.85987 12.20781  1.000 26.70139  ? 242  ASP   A C    1 
ATOM   4132 O  O    . ASP   B 2 237 ? 27.67388  -30.32284 11.57494  1.000 27.48447  ? 242  ASP   A O    1 
ATOM   4133 C  CB   . ASP   B 2 237 ? 26.45776  -31.90080 13.67389  1.000 26.98041  ? 242  ASP   A CB   1 
ATOM   4134 C  CG   . ASP   B 2 237 ? 27.36560  -31.38268 14.78696  1.000 31.48954  ? 242  ASP   A CG   1 
ATOM   4135 O  OD1  . ASP   B 2 237 ? 28.22157  -30.51264 14.51401  1.000 25.06243  ? 242  ASP   A OD1  1 
ATOM   4136 O  OD2  . ASP   B 2 237 ? 27.21051  -31.83263 15.93997  1.000 37.01957  ? 242  ASP   A OD2  1 
ATOM   4137 N  N    . TYR   B 2 238 ? 26.46868  -28.55188 12.28271  1.000 21.76974  ? 243  TYR   A N    1 
ATOM   4138 C  CA   . TYR   B 2 238 ? 27.25271  -27.61487 11.48274  1.000 29.03706  ? 243  TYR   A CA   1 
ATOM   4139 C  C    . TYR   B 2 238 ? 28.69665  -27.51975 11.98089  1.000 25.10390  ? 243  TYR   A C    1 
ATOM   4140 O  O    . TYR   B 2 238 ? 29.62372  -27.35773 11.17698  1.000 33.22675  ? 243  TYR   A O    1 
ATOM   4141 C  CB   . TYR   B 2 238 ? 26.58362  -26.23792 11.45659  1.000 21.45111  ? 243  TYR   A CB   1 
ATOM   4142 C  CG   . TYR   B 2 238 ? 26.49343  -25.55385 12.79354  1.000 22.23227  ? 243  TYR   A CG   1 
ATOM   4143 C  CD1  . TYR   B 2 238 ? 27.57633  -24.86575 13.30762  1.000 20.98457  ? 243  TYR   A CD1  1 
ATOM   4144 C  CD2  . TYR   B 2 238 ? 25.32435  -25.58989 13.54042  1.000 21.65007  ? 243  TYR   A CD2  1 
ATOM   4145 C  CE1  . TYR   B 2 238 ? 27.51216  -24.23769 14.53058  1.000 25.72385  ? 243  TYR   A CE1  1 
ATOM   4146 C  CE2  . TYR   B 2 238 ? 25.24418  -24.95382 14.78138  1.000 19.78701  ? 243  TYR   A CE2  1 
ATOM   4147 C  CZ   . TYR   B 2 238 ? 26.35308  -24.27972 15.26446  1.000 26.09286  ? 243  TYR   A CZ   1 
ATOM   4148 O  OH   . TYR   B 2 238 ? 26.32291  -23.63566 16.48442  1.000 38.03360  ? 243  TYR   A OH   1 
ATOM   4149 N  N    . SER   B 2 239 ? 28.91751  -27.61066 13.29992  1.000 24.51590  ? 244  SER   A N    1 
ATOM   4150 C  CA   . SER   B 2 239 ? 30.29046  -27.66154 13.81007  1.000 26.16861  ? 244  SER   A CA   1 
ATOM   4151 C  C    . SER   B 2 239 ? 31.07460  -28.80553 13.17522  1.000 28.23793  ? 244  SER   A C    1 
ATOM   4152 O  O    . SER   B 2 239 ? 32.20264  -28.61648 12.70333  1.000 37.53496  ? 244  SER   A O    1 
ATOM   4153 C  CB   . SER   B 2 239 ? 30.29631  -27.80646 15.33108  1.000 31.44969  ? 244  SER   A CB   1 
ATOM   4154 O  OG   . SER   B 2 239 ? 29.90416  -26.60245 15.96597  1.000 47.62047  ? 244  SER   A OG   1 
ATOM   4155 N  N    . LYS   B 2 240 ? 30.50268  -30.01056 13.17322  1.000 22.81281  ? 245  LYS   A N    1 
ATOM   4156 C  CA   . LYS   B 2 240 ? 31.20882  -31.15855 12.61936  1.000 26.51309  ? 245  LYS   A CA   1 
ATOM   4157 C  C    . LYS   B 2 240 ? 31.12399  -31.21964 11.10536  1.000 28.55109  ? 245  LYS   A C    1 
ATOM   4158 O  O    . LYS   B 2 240 ? 31.86810  -31.99062 10.49248  1.000 32.63311  ? 245  LYS   A O    1 
ATOM   4159 C  CB   . LYS   B 2 240 ? 30.67984  -32.46955 13.22638  1.000 29.85854  ? 245  LYS   A CB   1 
ATOM   4160 C  CG   . LYS   B 2 240 ? 31.22471  -32.74643 14.63845  1.000 42.48598  ? 245  LYS   A CG   1 
ATOM   4161 C  CD   . LYS   B 2 240 ? 30.59871  -33.96944 15.33145  1.000 47.15127  ? 245  LYS   A CD   1 
ATOM   4162 C  CE   . LYS   B 2 240 ? 31.18686  -35.29643 14.83659  1.000 57.80046  ? 245  LYS   A CE   1 
ATOM   4163 N  NZ   . LYS   B 2 240 ? 32.68085  -35.36532 14.93076  1.000 53.97646  ? 245  LYS   A NZ   1 
ATOM   4164 N  N    . GLY   B 2 241 ? 30.26400  -30.41073 10.49122  1.000 35.47721  ? 246  GLY   A N    1 
ATOM   4165 C  CA   . GLY   B 2 241 ? 30.01916  -30.50982 9.06420   1.000 25.23932  ? 246  GLY   A CA   1 
ATOM   4166 C  C    . GLY   B 2 241 ? 29.35029  -31.79789 8.63720   1.000 28.70179  ? 246  GLY   A C    1 
ATOM   4167 O  O    . GLY   B 2 241 ? 29.61144  -32.27594 7.52925   1.000 36.70196  ? 246  GLY   A O    1 
ATOM   4168 N  N    . LYS   B 2 242 ? 28.47524  -32.36790 9.47414   1.000 27.24269  ? 247  LYS   A N    1 
ATOM   4169 C  CA   . LYS   B 2 242 ? 27.89835  -33.68896 9.23015   1.000 28.43616  ? 247  LYS   A CA   1 
ATOM   4170 C  C    . LYS   B 2 242 ? 26.37736  -33.63306 9.14098   1.000 26.50187  ? 247  LYS   A C    1 
ATOM   4171 O  O    . LYS   B 2 242 ? 25.71423  -33.06606 10.01788  1.000 21.33792  ? 247  LYS   A O    1 
ATOM   4172 C  CB   . LYS   B 2 242 ? 28.28430  -34.67687 10.33624  1.000 27.27505  ? 247  LYS   A CB   1 
ATOM   4173 C  CG   . LYS   B 2 242 ? 29.78829  -34.87476 10.53342  1.000 45.69316  ? 247  LYS   A CG   1 
ATOM   4174 C  CD   . LYS   B 2 242 ? 30.11034  -36.31471 10.93953  1.000 46.37106  ? 247  LYS   A CD   1 
ATOM   4175 C  CE   . LYS   B 2 242 ? 29.00629  -36.92174 11.82645  1.000 47.62528  ? 247  LYS   A CE   1 
ATOM   4176 N  NZ   . LYS   B 2 242 ? 28.56511  -36.05370 12.96635  1.000 51.17188  ? 247  LYS   A NZ   1 
ATOM   4177 N  N    . CYS   B 2 243 ? 25.83251  -34.27116 8.10996   1.000 25.89819  ? 248  CYS   A N    1 
ATOM   4178 C  CA   . CYS   B 2 243 ? 24.39754  -34.50526 8.00782   1.000 22.37872  ? 248  CYS   A CA   1 
ATOM   4179 C  C    . CYS   B 2 243 ? 24.02952  -35.69423 8.88984   1.000 24.62197  ? 248  CYS   A C    1 
ATOM   4180 O  O    . CYS   B 2 243 ? 24.60661  -36.77320 8.74597   1.000 27.73586  ? 248  CYS   A O    1 
ATOM   4181 C  CB   . CYS   B 2 243 ? 24.01671  -34.76036 6.55079   1.000 21.73975  ? 248  CYS   A CB   1 
ATOM   4182 S  SG   . CYS   B 2 243 ? 22.32777  -35.33849 6.32964   1.000 31.38380  ? 248  CYS   A SG   1 
ATOM   4183 N  N    . LEU   B 2 244 ? 23.08141  -35.49724 9.80673   1.000 20.99399  ? 249  LEU   A N    1 
ATOM   4184 C  CA   . LEU   B 2 244 ? 22.71437  -36.48221 10.81975  1.000 20.53857  ? 249  LEU   A CA   1 
ATOM   4185 C  C    . LEU   B 2 244 ? 21.35543  -37.13531 10.59664  1.000 24.30163  ? 249  LEU   A C    1 
ATOM   4186 O  O    . LEU   B 2 244 ? 21.15747  -38.28430 11.00568  1.000 27.60749  ? 249  LEU   A O    1 
ATOM   4187 C  CB   . LEU   B 2 244 ? 22.69017  -35.83114 12.21171  1.000 18.74063  ? 249  LEU   A CB   1 
ATOM   4188 C  CG   . LEU   B 2 244 ? 23.95407  -35.16102 12.73881  1.000 23.75824  ? 249  LEU   A CG   1 
ATOM   4189 C  CD1  . LEU   B 2 244 ? 23.59089  -34.09399 13.75571  1.000 28.31135  ? 249  LEU   A CD1  1 
ATOM   4190 C  CD2  . LEU   B 2 244 ? 24.85407  -36.18493 13.36196  1.000 21.77665  ? 249  LEU   A CD2  1 
ATOM   4191 N  N    . LYS   B 2 245 ? 20.40445  -36.42241 10.00650  1.000 15.79682  ? 250  LYS   A N    1 
ATOM   4192 C  CA   . LYS   B 2 245 ? 19.07251  -36.94251 9.75038   1.000 14.79929  ? 250  LYS   A CA   1 
ATOM   4193 C  C    . LYS   B 2 245 ? 18.61562  -36.41762 8.40030   1.000 17.72537  ? 250  LYS   A C    1 
ATOM   4194 O  O    . LYS   B 2 245 ? 18.89658  -35.26662 8.04627   1.000 17.09072  ? 250  LYS   A O    1 
ATOM   4195 C  CB   . LYS   B 2 245 ? 18.05737  -36.51252 10.82325  1.000 12.26771  ? 250  LYS   A CB   1 
ATOM   4196 C  CG   . LYS   B 2 245 ? 18.40724  -36.88142 12.25431  1.000 15.52048  ? 250  LYS   A CG   1 
ATOM   4197 C  CD   . LYS   B 2 245 ? 18.19031  -38.36842 12.54637  1.000 22.94857  ? 250  LYS   A CD   1 
ATOM   4198 C  CE   . LYS   B 2 245 ? 18.51817  -38.69531 14.00542  1.000 30.40867  ? 250  LYS   A CE   1 
ATOM   4199 N  NZ   . LYS   B 2 245 ? 18.48824  -40.16930 14.28550  1.000 33.28614  ? 250  LYS   A NZ   1 
ATOM   4200 N  N    . THR   B 2 246 ? 17.92276  -37.26371 7.65428   1.000 16.71893  ? 251  THR   A N    1 
ATOM   4201 C  CA   . THR   B 2 246 ? 17.25186  -36.88182 6.42318   1.000 19.27821  ? 251  THR   A CA   1 
ATOM   4202 C  C    . THR   B 2 246 ? 15.76087  -37.17291 6.55404   1.000 18.11996  ? 251  THR   A C    1 
ATOM   4203 O  O    . THR   B 2 246 ? 15.37289  -38.23491 7.04906   1.000 20.93476  ? 251  THR   A O    1 
ATOM   4204 C  CB   . THR   B 2 246 ? 17.83104  -37.63785 5.23729   1.000 15.41674  ? 251  THR   A CB   1 
ATOM   4205 O  OG1  . THR   B 2 246 ? 19.23603  -37.36376 5.14242   1.000 22.39702  ? 251  THR   A OG1  1 
ATOM   4206 C  CG2  . THR   B 2 246 ? 17.14215  -37.21196 3.96119   1.000 19.67207  ? 251  THR   A CG2  1 
ATOM   4207 N  N    . TYR   B 2 247 ? 14.92885  -36.23199 6.11190   1.000 17.18237  ? 252  TYR   A N    1 
ATOM   4208 C  CA   . TYR   B 2 247 ? 13.47586  -36.36808 6.18375   1.000 15.39345  ? 252  TYR   A CA   1 
ATOM   4209 C  C    . TYR   B 2 247 ? 12.91600  -36.24120 4.77768   1.000 15.13965  ? 252  TYR   A C    1 
ATOM   4210 O  O    . TYR   B 2 247 ? 13.18901  -35.25322 4.08866   1.000 11.55047  ? 252  TYR   A O    1 
ATOM   4211 C  CB   . TYR   B 2 247 ? 12.86469  -35.31707 7.11462   1.000 14.27310  ? 252  TYR   A CB   1 
ATOM   4212 C  CG   . TYR   B 2 247 ? 13.54454  -35.28095 8.45970   1.000 11.20514  ? 252  TYR   A CG   1 
ATOM   4213 C  CD1  . TYR   B 2 247 ? 13.12648  -36.11392 9.49670   1.000 15.20325  ? 252  TYR   A CD1  1 
ATOM   4214 C  CD2  . TYR   B 2 247 ? 14.61946  -34.43887 8.68776   1.000 12.74608  ? 252  TYR   A CD2  1 
ATOM   4215 C  CE1  . TYR   B 2 247 ? 13.75535  -36.09781 10.74076  1.000 11.94303  ? 252  TYR   A CE1  1 
ATOM   4216 C  CE2  . TYR   B 2 247 ? 15.26533  -34.41876 9.92383   1.000 12.51360  ? 252  TYR   A CE2  1 
ATOM   4217 C  CZ   . TYR   B 2 247 ? 14.83427  -35.24573 10.94383  1.000 13.94279  ? 252  TYR   A CZ   1 
ATOM   4218 O  OH   . TYR   B 2 247 ? 15.48114  -35.21862 12.17090  1.000 13.35357  ? 252  TYR   A OH   1 
ATOM   4219 N  N    . THR   B 2 248 ? 12.17311  -37.25527 4.33666   1.000 14.04613  ? 253  THR   A N    1 
ATOM   4220 C  CA   . THR   B 2 248 ? 11.61726  -37.26138 2.99160   1.000 16.94614  ? 253  THR   A CA   1 
ATOM   4221 C  C    . THR   B 2 248 ? 10.19629  -37.79348 3.05048   1.000 15.78822  ? 253  THR   A C    1 
ATOM   4222 O  O    . THR   B 2 248 ? 9.68920   -38.17845 4.11544   1.000 16.19508  ? 253  THR   A O    1 
ATOM   4223 C  CB   . THR   B 2 248 ? 12.46642  -38.09738 2.02474   1.000 19.17178  ? 253  THR   A CB   1 
ATOM   4224 O  OG1  . THR   B 2 248 ? 12.52346  -39.44935 2.49082   1.000 23.40726  ? 253  THR   A OG1  1 
ATOM   4225 C  CG2  . THR   B 2 248 ? 13.86839  -37.55329 1.94586   1.000 21.64677  ? 253  THR   A CG2  1 
ATOM   4226 N  N    . GLY   B 2 249 ? 9.56241   -37.83358 1.88241   1.000 14.83276  ? 254  GLY   A N    1 
ATOM   4227 C  CA   . GLY   B 2 249 ? 8.17446   -38.22768 1.74528   1.000 16.82198  ? 254  GLY   A CA   1 
ATOM   4228 C  C    . GLY   B 2 249 ? 7.27544   -37.12877 1.21813   1.000 19.86992  ? 254  GLY   A C    1 
ATOM   4229 O  O    . GLY   B 2 249 ? 6.19051   -37.42887 0.70003   1.000 20.31483  ? 254  GLY   A O    1 
ATOM   4230 N  N    . HIS   B 2 250 ? 7.69734   -35.86374 1.31710   1.000 15.94036  ? 255  HIS   A N    1 
ATOM   4231 C  CA   . HIS   B 2 250 ? 6.91932   -34.72081 0.87095   1.000 16.95520  ? 255  HIS   A CA   1 
ATOM   4232 C  C    . HIS   B 2 250 ? 7.40043   -34.25286 -0.50502  1.000 16.97805  ? 255  HIS   A C    1 
ATOM   4233 O  O    . HIS   B 2 250 ? 8.31154   -34.82583 -1.10389  1.000 20.96236  ? 255  HIS   A O    1 
ATOM   4234 C  CB   . HIS   B 2 250 ? 7.01213   -33.58875 1.89790   1.000 15.22358  ? 255  HIS   A CB   1 
ATOM   4235 C  CG   . HIS   B 2 250 ? 8.38808   -33.02265 2.04202   1.000 13.34519  ? 255  HIS   A CG   1 
ATOM   4236 N  ND1  . HIS   B 2 250 ? 9.50512   -33.81757 2.18518   1.000 14.15178  ? 255  HIS   A ND1  1 
ATOM   4237 C  CD2  . HIS   B 2 250 ? 8.82899   -31.74062 2.07199   1.000 16.44618  ? 255  HIS   A CD2  1 
ATOM   4238 C  CE1  . HIS   B 2 250 ? 10.57605  -33.04849 2.29625   1.000 14.97833  ? 255  HIS   A CE1  1 
ATOM   4239 N  NE2  . HIS   B 2 250 ? 10.19198  -31.78452 2.23314   1.000 14.70698  ? 255  HIS   A NE2  1 
ATOM   4240 N  N    . LYS   B 2 251 ? 6.77542   -33.18793 -1.00615  1.000 15.16180  ? 256  LYS   A N    1 
ATOM   4241 C  CA   . LYS   B 2 251 ? 7.04352   -32.64599 -2.33615  1.000 14.89181  ? 256  LYS   A CA   1 
ATOM   4242 C  C    . LYS   B 2 251 ? 7.57541   -31.22194 -2.18317  1.000 18.51170  ? 256  LYS   A C    1 
ATOM   4243 O  O    . LYS   B 2 251 ? 6.87130   -30.33796 -1.67830  1.000 14.95011  ? 256  LYS   A O    1 
ATOM   4244 C  CB   . LYS   B 2 251 ? 5.76562   -32.67712 -3.19328  1.000 16.61324  ? 256  LYS   A CB   1 
ATOM   4245 C  CG   . LYS   B 2 251 ? 5.98977   -32.53519 -4.70727  1.000 31.06530  ? 256  LYS   A CG   1 
ATOM   4246 C  CD   . LYS   B 2 251 ? 5.41474   -31.22026 -5.26140  1.000 35.25655  ? 256  LYS   A CD   1 
ATOM   4247 C  CE   . LYS   B 2 251 ? 5.98887   -30.85530 -6.65536  1.000 42.39985  ? 256  LYS   A CE   1 
ATOM   4248 N  NZ   . LYS   B 2 251 ? 5.90581   -29.36832 -7.00545  1.000 28.35131  ? 256  LYS   A NZ   1 
ATOM   4249 N  N    . ASN   B 2 252 ? 8.81944   -30.99788 -2.60305  1.000 11.31030  ? 257  ASN   A N    1 
ATOM   4250 C  CA   . ASN   B 2 252 ? 9.39034   -29.65584 -2.48506  1.000 11.58419  ? 257  ASN   A CA   1 
ATOM   4251 C  C    . ASN   B 2 252 ? 10.46145  -29.49983 -3.56596  1.000 13.01713  ? 257  ASN   A C    1 
ATOM   4252 O  O    . ASN   B 2 252 ? 11.63045  -29.84174 -3.35181  1.000 11.49928  ? 257  ASN   A O    1 
ATOM   4253 C  CB   . ASN   B 2 252 ? 9.96318   -29.41472 -1.09802  1.000 13.51038  ? 257  ASN   A CB   1 
ATOM   4254 C  CG   . ASN   B 2 252 ? 10.37106  -27.97268 -0.88705  1.000 8.70667   ? 257  ASN   A CG   1 
ATOM   4255 O  OD1  . ASN   B 2 252 ? 9.92008   -27.07075 -1.61115  1.000 9.25300   ? 257  ASN   A OD1  1 
ATOM   4256 N  ND2  . ASN   B 2 252 ? 11.20893  -27.73857 0.11502   1.000 7.42779   ? 257  ASN   A ND2  1 
ATOM   4257 N  N    . GLU   B 2 253 ? 10.04654  -28.97092 -4.71703  1.000 8.92208   ? 258  GLU   A N    1 
ATOM   4258 C  CA   . GLU   B 2 253 ? 10.95664  -28.74492 -5.82795  1.000 15.05136  ? 258  GLU   A CA   1 
ATOM   4259 C  C    . GLU   B 2 253 ? 10.86161  -27.34196 -6.40604  1.000 14.31789  ? 258  GLU   A C    1 
ATOM   4260 O  O    . GLU   B 2 253 ? 11.60069  -27.02796 -7.33997  1.000 15.65875  ? 258  GLU   A O    1 
ATOM   4261 C  CB   . GLU   B 2 253 ? 10.70283  -29.76800 -6.95192  1.000 16.05300  ? 258  GLU   A CB   1 
ATOM   4262 C  CG   . GLU   B 2 253 ? 10.89688  -31.21996 -6.53281  1.000 25.69329  ? 258  GLU   A CG   1 
ATOM   4263 C  CD   . GLU   B 2 253 ? 10.72407  -32.20404 -7.68778  1.000 33.24168  ? 258  GLU   A CD   1 
ATOM   4264 O  OE1  . GLU   B 2 253 ? 9.94515   -31.90414 -8.63488  1.000 26.13183  ? 258  GLU   A OE1  1 
ATOM   4265 O  OE2  . GLU   B 2 253 ? 11.37513  -33.27699 -7.63865  1.000 20.77658  ? 258  GLU   A OE2  1 
ATOM   4266 N  N    . LYS   B 2 254 ? 9.97550   -26.51499 -5.91818  1.000 12.64845  ? 259  LYS   A N    1 
ATOM   4267 C  CA   . LYS   B 2 254 ? 9.88048   -25.20503 -6.53626  1.000 14.37088  ? 259  LYS   A CA   1 
ATOM   4268 C  C    . LYS   B 2 254 ? 9.86230   -24.06598 -5.52933  1.000 18.44337  ? 259  LYS   A C    1 
ATOM   4269 O  O    . LYS   B 2 254 ? 10.52825  -23.04494 -5.75431  1.000 18.53710  ? 259  LYS   A O    1 
ATOM   4270 C  CB   . LYS   B 2 254 ? 8.61957   -25.14416 -7.42440  1.000 13.15114  ? 259  LYS   A CB   1 
ATOM   4271 C  CG   . LYS   B 2 254 ? 8.36055   -23.76922 -8.05050  1.000 18.03835  ? 259  LYS   A CG   1 
ATOM   4272 C  CD   . LYS   B 2 254 ? 7.13165   -23.78835 -8.97463  1.000 23.10388  ? 259  LYS   A CD   1 
ATOM   4273 C  CE   . LYS   B 2 254 ? 6.76661   -22.37640 -9.46275  1.000 23.65239  ? 259  LYS   A CE   1 
ATOM   4274 N  NZ   . LYS   B 2 254 ? 5.52270   -22.38453 -10.29388 1.000 31.89473  ? 259  LYS   A NZ   1 
ATOM   4275 N  N    . TYR   B 2 255 ? 9.11719   -24.20597 -4.43940  1.000 11.03046  ? 260  TYR   A N    1 
ATOM   4276 C  CA   . TYR   B 2 255 ? 8.88402   -23.11093 -3.51348  1.000 10.19577  ? 260  TYR   A CA   1 
ATOM   4277 C  C    . TYR   B 2 255 ? 9.80289   -23.19280 -2.29938  1.000 13.03646  ? 260  TYR   A C    1 
ATOM   4278 O  O    . TYR   B 2 255 ? 10.32192  -24.25475 -1.93827  1.000 7.29080   ? 260  TYR   A O    1 
ATOM   4279 C  CB   . TYR   B 2 255 ? 7.42097   -23.10900 -3.07964  1.000 14.72132  ? 260  TYR   A CB   1 
ATOM   4280 C  CG   . TYR   B 2 255 ? 6.51206   -22.69412 -4.20776  1.000 15.02626  ? 260  TYR   A CG   1 
ATOM   4281 C  CD1  . TYR   B 2 255 ? 6.27000   -21.34615 -4.45786  1.000 11.75795  ? 260  TYR   A CD1  1 
ATOM   4282 C  CD2  . TYR   B 2 255 ? 5.91522   -23.63821 -5.04377  1.000 19.41794  ? 260  TYR   A CD2  1 
ATOM   4283 C  CE1  . TYR   B 2 255 ? 5.45609   -20.94127 -5.50197  1.000 14.81579  ? 260  TYR   A CE1  1 
ATOM   4284 C  CE2  . TYR   B 2 255 ? 5.08130   -23.24133 -6.10288  1.000 15.55810  ? 260  TYR   A CE2  1 
ATOM   4285 C  CZ   . TYR   B 2 255 ? 4.85224   -21.88635 -6.31398  1.000 23.42381  ? 260  TYR   A CZ   1 
ATOM   4286 O  OH   . TYR   B 2 255 ? 4.03332   -21.45646 -7.33910  1.000 20.98351  ? 260  TYR   A OH   1 
ATOM   4287 N  N    . CYS   B 2 256 ? 10.01675  -22.03675 -1.67242  1.000 12.33339  ? 261  CYS   A N    1 
ATOM   4288 C  CA   . CYS   B 2 256 ? 10.85962  -21.98763 -0.48933  1.000 9.05166   ? 261  CYS   A CA   1 
ATOM   4289 C  C    . CYS   B 2 256 ? 9.95350   -22.16562 0.71858   1.000 8.09045   ? 261  CYS   A C    1 
ATOM   4290 O  O    . CYS   B 2 256 ? 9.44837   -21.21162 1.30847   1.000 9.54998   ? 261  CYS   A O    1 
ATOM   4291 C  CB   . CYS   B 2 256 ? 11.68853  -20.70857 -0.46032  1.000 10.47542  ? 261  CYS   A CB   1 
ATOM   4292 S  SG   . CYS   B 2 256 ? 13.03067  -20.79555 -1.69217  1.000 11.21214  ? 261  CYS   A SG   1 
ATOM   4293 N  N    . ILE   B 2 257 ? 9.76554   -23.42261 1.09063   1.000 9.94174   ? 262  ILE   A N    1 
ATOM   4294 C  CA   . ILE   B 2 257 ? 8.88645   -23.79661 2.18656   1.000 12.03983  ? 262  ILE   A CA   1 
ATOM   4295 C  C    . ILE   B 2 257 ? 9.62430   -23.68049 3.51663   1.000 13.08431  ? 262  ILE   A C    1 
ATOM   4296 O  O    . ILE   B 2 257 ? 10.71432  -24.23941 3.69078   1.000 13.14187  ? 262  ILE   A O    1 
ATOM   4297 C  CB   . ILE   B 2 257 ? 8.35457   -25.21766 1.96458   1.000 15.48330  ? 262  ILE   A CB   1 
ATOM   4298 C  CG1  . ILE   B 2 257 ? 7.71172   -25.29878 0.57151   1.000 14.91174  ? 262  ILE   A CG1  1 
ATOM   4299 C  CG2  . ILE   B 2 257 ? 7.37148   -25.57266 3.04949   1.000 11.33031  ? 262  ILE   A CG2  1 
ATOM   4300 C  CD1  . ILE   B 2 257 ? 7.03485   -26.63584 0.26251   1.000 14.14415  ? 262  ILE   A CD1  1 
ATOM   4301 N  N    . PHE   B 2 258 ? 9.02215   -22.95947 4.46352   1.000 10.44729  ? 263  PHE   A N    1 
ATOM   4302 C  CA   . PHE   B 2 258 ? 9.52100   -22.85337 5.83057   1.000 12.50481  ? 263  PHE   A CA   1 
ATOM   4303 C  C    . PHE   B 2 258 ? 9.38601   -24.20033 6.56363   1.000 15.13689  ? 263  PHE   A C    1 
ATOM   4304 O  O    . PHE   B 2 258 ? 8.56110   -25.04641 6.21759   1.000 26.27062  ? 263  PHE   A O    1 
ATOM   4305 C  CB   . PHE   B 2 258 ? 8.74484   -21.75838 6.57043   1.000 10.16181  ? 263  PHE   A CB   1 
ATOM   4306 C  CG   . PHE   B 2 258 ? 9.51968   -21.09426 7.67347   1.000 13.15091  ? 263  PHE   A CG   1 
ATOM   4307 C  CD1  . PHE   B 2 258 ? 9.46258   -21.57619 8.96849   1.000 14.25963  ? 263  PHE   A CD1  1 
ATOM   4308 C  CD2  . PHE   B 2 258 ? 10.28363  -19.96423 7.41949   1.000 14.57924  ? 263  PHE   A CD2  1 
ATOM   4309 C  CE1  . PHE   B 2 258 ? 10.16742  -20.95309 10.00453  1.000 10.91885  ? 263  PHE   A CE1  1 
ATOM   4310 C  CE2  . PHE   B 2 258 ? 10.99348  -19.33812 8.44753   1.000 16.22182  ? 263  PHE   A CE2  1 
ATOM   4311 C  CZ   . PHE   B 2 258 ? 10.93438  -19.84205 9.73955   1.000 12.53335  ? 263  PHE   A CZ   1 
ATOM   4312 N  N    . ALA   B 2 259 ? 10.21391  -24.40622 7.58473   1.000 13.29845  ? 264  ALA   A N    1 
ATOM   4313 C  CA   . ALA   B 2 259 ? 10.14491  -25.63018 8.38179   1.000 13.93590  ? 264  ALA   A CA   1 
ATOM   4314 C  C    . ALA   B 2 259 ? 10.50073  -25.30908 9.83281   1.000 11.85861  ? 264  ALA   A C    1 
ATOM   4315 O  O    . ALA   B 2 259 ? 11.02863  -24.23302 10.14381  1.000 13.50994  ? 264  ALA   A O    1 
ATOM   4316 C  CB   . ALA   B 2 259 ? 11.05704  -26.72715 7.80595   1.000 13.31718  ? 264  ALA   A CB   1 
ATOM   4317 N  N    . ASN   B 2 260 ? 10.21570  -26.25505 10.72984  1.000 9.55447   ? 265  ASN   A N    1 
ATOM   4318 C  CA   . ASN   B 2 260 ? 10.30452  -25.95196 12.15483  1.000 14.02062  ? 265  ASN   A CA   1 
ATOM   4319 C  C    . ASN   B 2 260 ? 10.69352  -27.17189 12.97394  1.000 12.22311  ? 265  ASN   A C    1 
ATOM   4320 O  O    . ASN   B 2 260 ? 10.44063  -28.32093 12.59497  1.000 7.90688   ? 265  ASN   A O    1 
ATOM   4321 C  CB   . ASN   B 2 260 ? 8.97043   -25.42902 12.72466  1.000 12.14853  ? 265  ASN   A CB   1 
ATOM   4322 C  CG   . ASN   B 2 260 ? 8.34645   -24.36011 11.87253  1.000 16.04360  ? 265  ASN   A CG   1 
ATOM   4323 O  OD1  . ASN   B 2 260 ? 7.48956   -24.64321 11.02545  1.000 20.87515  ? 265  ASN   A OD1  1 
ATOM   4324 N  ND2  . ASN   B 2 260 ? 8.77534   -23.11607 12.08151  1.000 14.38578  ? 265  ASN   A ND2  1 
ATOM   4325 N  N    . PHE   B 2 261 ? 11.26437  -26.88679 14.14598  1.000 12.55175  ? 266  PHE   A N    1 
ATOM   4326 C  CA   . PHE   B 2 261 ? 11.35832  -27.84772 15.23605  1.000 8.51549   ? 266  PHE   A CA   1 
ATOM   4327 C  C    . PHE   B 2 261 ? 10.13221  -27.66375 16.11990  1.000 16.27492  ? 266  PHE   A C    1 
ATOM   4328 O  O    . PHE   B 2 261 ? 9.89308   -26.56674 16.63482  1.000 15.68152  ? 266  PHE   A O    1 
ATOM   4329 C  CB   . PHE   B 2 261 ? 12.63422  -27.64259 16.06117  1.000 11.90311  ? 266  PHE   A CB   1 
ATOM   4330 C  CG   . PHE   B 2 261 ? 13.90131  -27.82455 15.28132  1.000 17.65546  ? 266  PHE   A CG   1 
ATOM   4331 C  CD1  . PHE   B 2 261 ? 14.41433  -26.78956 14.51132  1.000 15.75685  ? 266  PHE   A CD1  1 
ATOM   4332 C  CD2  . PHE   B 2 261 ? 14.58739  -29.02850 15.32246  1.000 14.66604  ? 266  PHE   A CD2  1 
ATOM   4333 C  CE1  . PHE   B 2 261 ? 15.58841  -26.95252 13.79445  1.000 15.62434  ? 266  PHE   A CE1  1 
ATOM   4334 C  CE2  . PHE   B 2 261 ? 15.75548  -29.20046 14.59359  1.000 16.57258  ? 266  PHE   A CE2  1 
ATOM   4335 C  CZ   . PHE   B 2 261 ? 16.25649  -28.16047 13.83659  1.000 13.44154  ? 266  PHE   A CZ   1 
ATOM   4336 N  N    . SER   B 2 262 ? 9.35426   -28.72479 16.29088  1.000 12.82886  ? 267  SER   A N    1 
ATOM   4337 C  CA   . SER   B 2 262 ? 8.25016   -28.72281 17.24076  1.000 14.53626  ? 267  SER   A CA   1 
ATOM   4338 C  C    . SER   B 2 262 ? 8.76206   -29.28970 18.56885  1.000 15.45241  ? 267  SER   A C    1 
ATOM   4339 O  O    . SER   B 2 262 ? 9.22513   -30.43467 18.62196  1.000 16.01224  ? 267  SER   A O    1 
ATOM   4340 C  CB   . SER   B 2 262 ? 7.08628   -29.54392 16.68868  1.000 12.02924  ? 267  SER   A CB   1 
ATOM   4341 O  OG   . SER   B 2 262 ? 5.94018   -29.40295 17.49955  1.000 15.90997  ? 267  SER   A OG   1 
ATOM   4342 N  N    . VAL   B 2 263 ? 8.72289   -28.48765 19.62780  1.000 13.55966  ? 268  VAL   A N    1 
ATOM   4343 C  CA   . VAL   B 2 263 ? 9.37978   -28.90154 20.86089  1.000 16.34887  ? 268  VAL   A CA   1 
ATOM   4344 C  C    . VAL   B 2 263 ? 8.49564   -28.78653 22.10379  1.000 22.42419  ? 268  VAL   A C    1 
ATOM   4345 O  O    . VAL   B 2 263 ? 8.98453   -28.95643 23.22885  1.000 23.22885  ? 268  VAL   A O    1 
ATOM   4346 C  CB   . VAL   B 2 263 ? 10.68471  -28.10444 21.06399  1.000 19.62767  ? 268  VAL   A CB   1 
ATOM   4347 C  CG1  . VAL   B 2 263 ? 11.52385  -28.09145 19.77208  1.000 20.47559  ? 268  VAL   A CG1  1 
ATOM   4348 C  CG2  . VAL   B 2 263 ? 10.38756  -26.69743 21.55988  1.000 17.83178  ? 268  VAL   A CG2  1 
ATOM   4349 N  N    . THR   B 2 264 ? 7.19664   -28.50962 21.94164  1.000 17.20721  ? 269  THR   A N    1 
ATOM   4350 C  CA   . THR   B 2 264 ? 6.35351   -28.38561 23.12654  1.000 18.35082  ? 269  THR   A CA   1 
ATOM   4351 C  C    . THR   B 2 264 ? 5.83154   -29.72062 23.64156  1.000 19.11235  ? 269  THR   A C    1 
ATOM   4352 O  O    . THR   B 2 264 ? 5.50942   -29.82457 24.83653  1.000 25.03263  ? 269  THR   A O    1 
ATOM   4353 C  CB   . THR   B 2 264 ? 5.16248   -27.45071 22.84436  1.000 18.63315  ? 269  THR   A CB   1 
ATOM   4354 O  OG1  . THR   B 2 264 ? 4.46063   -27.92182 21.69531  1.000 13.85930  ? 269  THR   A OG1  1 
ATOM   4355 C  CG2  . THR   B 2 264 ? 5.64041   -26.02269 22.59333  1.000 17.41819  ? 269  THR   A CG2  1 
ATOM   4356 N  N    . GLY   B 2 265 ? 5.73870   -30.72967 22.78160  1.000 15.70763  ? 270  GLY   A N    1 
ATOM   4357 C  CA   . GLY   B 2 265 ? 5.26975   -32.04668 23.16763  1.000 18.64347  ? 270  GLY   A CA   1 
ATOM   4358 C  C    . GLY   B 2 265 ? 6.24087   -33.09764 22.67979  1.000 19.27422  ? 270  GLY   A C    1 
ATOM   4359 O  O    . GLY   B 2 265 ? 7.39082   -33.11754 23.11491  1.000 19.91412  ? 270  GLY   A O    1 
ATOM   4360 N  N    . GLY   B 2 266 ? 5.81002   -33.96972 21.77479  1.000 19.71460  ? 271  GLY   A N    1 
ATOM   4361 C  CA   . GLY   B 2 266 ? 6.76015   -34.80470 21.06194  1.000 25.86468  ? 271  GLY   A CA   1 
ATOM   4362 C  C    . GLY   B 2 266 ? 7.74319   -33.97868 20.24800  1.000 22.81707  ? 271  GLY   A C    1 
ATOM   4363 O  O    . GLY   B 2 266 ? 7.47015   -32.84172 19.85091  1.000 19.09615  ? 271  GLY   A O    1 
ATOM   4364 N  N    . LYS   B 2 267 ? 8.91825   -34.56461 19.99816  1.000 16.95579  ? 272  LYS   A N    1 
ATOM   4365 C  CA   . LYS   B 2 267 ? 9.98029   -33.88859 19.24824  1.000 13.11974  ? 272  LYS   A CA   1 
ATOM   4366 C  C    . LYS   B 2 267 ? 9.75846   -34.13868 17.76223  1.000 18.01918  ? 272  LYS   A C    1 
ATOM   4367 O  O    . LYS   B 2 267 ? 10.06659  -35.22169 17.25232  1.000 17.90475  ? 272  LYS   A O    1 
ATOM   4368 C  CB   . LYS   B 2 267 ? 11.34928  -34.39447 19.68241  1.000 19.04025  ? 272  LYS   A CB   1 
ATOM   4369 C  CG   . LYS   B 2 267 ? 12.01711  -33.59537 20.77944  1.000 19.90969  ? 272  LYS   A CG   1 
ATOM   4370 C  CD   . LYS   B 2 267 ? 11.03196  -32.92738 21.69630  1.000 22.34150  ? 272  LYS   A CD   1 
ATOM   4371 C  CE   . LYS   B 2 267 ? 11.76980  -32.08427 22.72133  1.000 25.20796  ? 272  LYS   A CE   1 
ATOM   4372 N  NZ   . LYS   B 2 267 ? 10.81965  -31.31229 23.57718  1.000 29.26472  ? 272  LYS   A NZ   1 
ATOM   4373 N  N    . TRP   B 2 268 ? 9.22548   -33.14576 17.05211  1.000 14.73986  ? 273  TRP   A N    1 
ATOM   4374 C  CA   . TRP   B 2 268 ? 8.93664   -33.33986 15.63709  1.000 15.83597  ? 273  TRP   A CA   1 
ATOM   4375 C  C    . TRP   B 2 268 ? 9.77067   -32.40585 14.77213  1.000 14.28536  ? 273  TRP   A C    1 
ATOM   4376 O  O    . TRP   B 2 268 ? 10.36256  -31.43178 15.24414  1.000 14.23523  ? 273  TRP   A O    1 
ATOM   4377 C  CB   . TRP   B 2 268 ? 7.45066   -33.11497 15.31592  1.000 12.75763  ? 273  TRP   A CB   1 
ATOM   4378 C  CG   . TRP   B 2 268 ? 6.48658   -33.58098 16.36384  1.000 22.05835  ? 273  TRP   A CG   1 
ATOM   4379 C  CD1  . TRP   B 2 268 ? 5.57445   -32.80800 17.04070  1.000 14.66314  ? 273  TRP   A CD1  1 
ATOM   4380 C  CD2  . TRP   B 2 268 ? 6.31661   -34.92396 16.85090  1.000 17.42123  ? 273  TRP   A CD2  1 
ATOM   4381 N  NE1  . TRP   B 2 268 ? 4.86041   -33.58900 17.92267  1.000 17.69489  ? 273  TRP   A NE1  1 
ATOM   4382 C  CE2  . TRP   B 2 268 ? 5.29551   -34.88598 17.83079  1.000 19.24911  ? 273  TRP   A CE2  1 
ATOM   4383 C  CE3  . TRP   B 2 268 ? 6.93473   -36.14794 16.56603  1.000 12.41678  ? 273  TRP   A CE3  1 
ATOM   4384 C  CZ2  . TRP   B 2 268 ? 4.87651   -36.02897 18.52381  1.000 18.60501  ? 273  TRP   A CZ2  1 
ATOM   4385 C  CZ3  . TRP   B 2 268 ? 6.51073   -37.28193 17.24805  1.000 21.09272  ? 273  TRP   A CZ3  1 
ATOM   4386 C  CH2  . TRP   B 2 268 ? 5.48862   -37.21194 18.21594  1.000 21.19923  ? 273  TRP   A CH2  1 
ATOM   4387 N  N    . ILE   B 2 269 ? 9.78883   -32.72992 13.48215  1.000 17.29322  ? 274  ILE   A N    1 
ATOM   4388 C  CA   . ILE   B 2 269 ? 10.08888  -31.79196 12.40613  1.000 15.85155  ? 274  ILE   A CA   1 
ATOM   4389 C  C    . ILE   B 2 269 ? 8.79095   -31.51409 11.65498  1.000 13.70470  ? 274  ILE   A C    1 
ATOM   4390 O  O    . ILE   B 2 269 ? 8.02304   -32.43916 11.35494  1.000 12.36034  ? 274  ILE   A O    1 
ATOM   4391 C  CB   . ILE   B 2 269 ? 11.16702  -32.34394 11.45428  1.000 11.01996  ? 274  ILE   A CB   1 
ATOM   4392 C  CG1  . ILE   B 2 269 ? 12.48196  -32.59181 12.20843  1.000 9.82842   ? 274  ILE   A CG1  1 
ATOM   4393 C  CG2  . ILE   B 2 269 ? 11.35709  -31.41200 10.25625  1.000 8.01021   ? 274  ILE   A CG2  1 
ATOM   4394 C  CD1  . ILE   B 2 269 ? 13.15582  -31.34074 12.73243  1.000 11.28752  ? 274  ILE   A CD1  1 
ATOM   4395 N  N    . VAL   B 2 270 ? 8.54289   -30.24012 11.35288  1.000 17.08527  ? 275  VAL   A N    1 
ATOM   4396 C  CA   . VAL   B 2 270 ? 7.31093   -29.80124 10.70472  1.000 9.60327   ? 275  VAL   A CA   1 
ATOM   4397 C  C    . VAL   B 2 270 ? 7.64002   -29.03929 9.43071   1.000 10.82922  ? 275  VAL   A C    1 
ATOM   4398 O  O    . VAL   B 2 270 ? 8.49496   -28.14723 9.43276   1.000 10.55884  ? 275  VAL   A O    1 
ATOM   4399 C  CB   . VAL   B 2 270 ? 6.47478   -28.90824 11.63758  1.000 14.07537  ? 275  VAL   A CB   1 
ATOM   4400 C  CG1  . VAL   B 2 270 ? 5.23382   -28.37937 10.90042  1.000 9.88274   ? 275  VAL   A CG1  1 
ATOM   4401 C  CG2  . VAL   B 2 270 ? 6.11269   -29.66120 12.89458  1.000 10.57987  ? 275  VAL   A CG2  1 
ATOM   4402 N  N    . SER   B 2 271 ? 6.91516   -29.34440 8.35465   1.000 14.44288  ? 276  SER   A N    1 
ATOM   4403 C  CA   . SER   B 2 271 ? 7.11624   -28.60345 7.12263   1.000 12.56059  ? 276  SER   A CA   1 
ATOM   4404 C  C    . SER   B 2 271 ? 5.87934   -28.70158 6.24151   1.000 15.56422  ? 276  SER   A C    1 
ATOM   4405 O  O    . SER   B 2 271 ? 5.16441   -29.71163 6.25349   1.000 12.73790  ? 276  SER   A O    1 
ATOM   4406 C  CB   . SER   B 2 271 ? 8.34536   -29.11341 6.36279   1.000 12.44284  ? 276  SER   A CB   1 
ATOM   4407 O  OG   . SER   B 2 271 ? 8.51144   -28.41647 5.13577   1.000 12.29908  ? 276  SER   A OG   1 
ATOM   4408 N  N    . GLY   B 2 272 ? 5.65835   -27.64364 5.45842   1.000 8.36551   ? 277  GLY   A N    1 
ATOM   4409 C  CA   . GLY   B 2 272 ? 4.69047   -27.67077 4.38732   1.000 8.08091   ? 277  GLY   A CA   1 
ATOM   4410 C  C    . GLY   B 2 272 ? 5.20265   -28.45680 3.20042   1.000 9.99753   ? 277  GLY   A C    1 
ATOM   4411 O  O    . GLY   B 2 272 ? 6.28469   -29.03973 3.21157   1.000 13.44482  ? 277  GLY   A O    1 
ATOM   4412 N  N    . SER   B 2 273 ? 4.41077   -28.45691 2.13733   1.000 11.48049  ? 278  SER   A N    1 
ATOM   4413 C  CA   . SER   B 2 273 ? 4.63194   -29.38396 1.03941   1.000 10.85242  ? 278  SER   A CA   1 
ATOM   4414 C  C    . SER   B 2 273 ? 3.85304   -28.91408 -0.17370  1.000 12.66820  ? 278  SER   A C    1 
ATOM   4415 O  O    . SER   B 2 273 ? 2.80799   -28.27614 -0.04185  1.000 14.19901  ? 278  SER   A O    1 
ATOM   4416 C  CB   . SER   B 2 273 ? 4.21400   -30.81096 1.41444   1.000 13.15086  ? 278  SER   A CB   1 
ATOM   4417 O  OG   . SER   B 2 273 ? 4.43918   -31.70801 0.32352   1.000 15.37531  ? 278  SER   A OG   1 
ATOM   4418 N  N    . GLU   B 2 274 ? 4.36519   -29.25611 -1.35463  1.000 10.40055  ? 279  GLU   A N    1 
ATOM   4419 C  CA   . GLU   B 2 274 ? 3.74630   -28.81022 -2.58972  1.000 12.92116  ? 279  GLU   A CA   1 
ATOM   4420 C  C    . GLU   B 2 274 ? 2.59040   -29.69832 -3.02279  1.000 11.00888  ? 279  GLU   A C    1 
ATOM   4421 O  O    . GLU   B 2 274 ? 2.00550   -29.44942 -4.08287  1.000 14.20281  ? 279  GLU   A O    1 
ATOM   4422 C  CB   . GLU   B 2 274 ? 4.80441   -28.70521 -3.68361  1.000 10.68576  ? 279  GLU   A CB   1 
ATOM   4423 C  CG   . GLU   B 2 274 ? 5.70731   -27.47314 -3.50658  1.000 16.53822  ? 279  GLU   A CG   1 
ATOM   4424 C  CD   . GLU   B 2 274 ? 7.07239   -27.60709 -4.18743  1.000 18.97297  ? 279  GLU   A CD   1 
ATOM   4425 O  OE1  . GLU   B 2 274 ? 7.31253   -28.62911 -4.87034  1.000 13.50580  ? 279  GLU   A OE1  1 
ATOM   4426 O  OE2  . GLU   B 2 274 ? 7.90731   -26.68802 -4.02639  1.000 15.88260  ? 279  GLU   A OE2  1 
ATOM   4427 N  N    . ASP   B 2 275 ? 2.26439   -30.73530 -2.24477  1.000 11.40866  ? 280  ASP   A N    1 
ATOM   4428 C  CA   . ASP   B 2 275 ? 1.00945   -31.46539 -2.37286  1.000 12.79628  ? 280  ASP   A CA   1 
ATOM   4429 C  C    . ASP   B 2 275 ? -0.05069  -30.94640 -1.40901  1.000 13.04175  ? 280  ASP   A C    1 
ATOM   4430 O  O    . ASP   B 2 275 ? -1.04367  -31.63446 -1.17107  1.000 9.66229   ? 280  ASP   A O    1 
ATOM   4431 C  CB   . ASP   B 2 275 ? 1.22753   -32.97536 -2.17075  1.000 8.14803   ? 280  ASP   A CB   1 
ATOM   4432 C  CG   . ASP   B 2 275 ? 1.81140   -33.31625 -0.80167  1.000 18.93531  ? 280  ASP   A CG   1 
ATOM   4433 O  OD1  . ASP   B 2 275 ? 1.97125   -32.39719 0.05129   1.000 12.87441  ? 280  ASP   A OD1  1 
ATOM   4434 O  OD2  . ASP   B 2 275 ? 2.11746   -34.51221 -0.57657  1.000 15.14404  ? 280  ASP   A OD2  1 
ATOM   4435 N  N    . ASN   B 2 276 ? 0.15617   -29.75736 -0.83005  1.000 9.39105   ? 281  ASN   A N    1 
ATOM   4436 C  CA   . ASN   B 2 276 ? -0.84896  -29.03938 -0.04420  1.000 10.88217  ? 281  ASN   A CA   1 
ATOM   4437 C  C    . ASN   B 2 276 ? -1.06007  -29.62632 1.34681   1.000 10.48687  ? 281  ASN   A C    1 
ATOM   4438 O  O    . ASN   B 2 276 ? -2.05916  -29.30835 2.00769   1.000 10.44028  ? 281  ASN   A O    1 
ATOM   4439 C  CB   . ASN   B 2 276 ? -2.19889  -28.97351 -0.76835  1.000 10.51416  ? 281  ASN   A CB   1 
ATOM   4440 C  CG   . ASN   B 2 276 ? -2.07177  -28.46858 -2.19136  1.000 14.85515  ? 281  ASN   A CG   1 
ATOM   4441 O  OD1  . ASN   B 2 276 ? -1.03977  -27.89254 -2.58328  1.000 11.50673  ? 281  ASN   A OD1  1 
ATOM   4442 N  ND2  . ASN   B 2 276 ? -3.12467  -28.68470 -2.98246  1.000 16.04948  ? 281  ASN   A ND2  1 
ATOM   4443 N  N    . LEU   B 2 277 ? -0.14107  -30.45623 1.81896   1.000 14.11648  ? 282  LEU   A N    1 
ATOM   4444 C  CA   . LEU   B 2 277 ? -0.21817  -31.07516 3.13098   1.000 11.84924  ? 282  LEU   A CA   1 
ATOM   4445 C  C    . LEU   B 2 277 ? 0.81669   -30.45504 4.05706   1.000 13.38134  ? 282  LEU   A C    1 
ATOM   4446 O  O    . LEU   B 2 277 ? 1.86171   -29.98000 3.61115   1.000 10.70684  ? 282  LEU   A O    1 
ATOM   4447 C  CB   . LEU   B 2 277 ? 0.01894   -32.58515 3.04309   1.000 10.86856  ? 282  LEU   A CB   1 
ATOM   4448 C  CG   . LEU   B 2 277 ? -0.93891  -33.38126 2.14604   1.000 15.53004  ? 282  LEU   A CG   1 
ATOM   4449 C  CD1  . LEU   B 2 277 ? -0.54981  -34.85524 2.10216   1.000 11.54898  ? 282  LEU   A CD1  1 
ATOM   4450 C  CD2  . LEU   B 2 277 ? -2.37897  -33.22333 2.63187   1.000 11.59758  ? 282  LEU   A CD2  1 
ATOM   4451 N  N    . VAL   B 2 278 ? 0.51655   -30.45599 5.35403   1.000 10.68410  ? 283  VAL   A N    1 
ATOM   4452 C  CA   . VAL   B 2 278 ? 1.54843   -30.27786 6.36313   1.000 12.51380  ? 283  VAL   A CA   1 
ATOM   4453 C  C    . VAL   B 2 278 ? 2.08248   -31.65481 6.73926   1.000 14.47138  ? 283  VAL   A C    1 
ATOM   4454 O  O    . VAL   B 2 278 ? 1.30251   -32.56684 7.03623   1.000 16.76569  ? 283  VAL   A O    1 
ATOM   4455 C  CB   . VAL   B 2 278 ? 1.00225   -29.53683 7.58703   1.000 9.75899   ? 283  VAL   A CB   1 
ATOM   4456 C  CG1  . VAL   B 2 278 ? 2.04013   -29.52770 8.71214   1.000 11.14015  ? 283  VAL   A CG1  1 
ATOM   4457 C  CG2  . VAL   B 2 278 ? 0.60920   -28.11788 7.18591   1.000 14.39938  ? 283  VAL   A CG2  1 
ATOM   4458 N  N    . TYR   B 2 279 ? 3.40850   -31.81172 6.70841   1.000 10.24043  ? 284  TYR   A N    1 
ATOM   4459 C  CA   . TYR   B 2 279 ? 4.06854   -33.05966 7.08855   1.000 9.90590   ? 284  TYR   A CA   1 
ATOM   4460 C  C    . TYR   B 2 279 ? 4.69038   -32.92254 8.47261   1.000 11.13147  ? 284  TYR   A C    1 
ATOM   4461 O  O    . TYR   B 2 279 ? 5.25828   -31.87848 8.81662   1.000 11.89266  ? 284  TYR   A O    1 
ATOM   4462 C  CB   . TYR   B 2 279 ? 5.15767   -33.44764 6.08069   1.000 12.06982  ? 284  TYR   A CB   1 
ATOM   4463 C  CG   . TYR   B 2 279 ? 4.63785   -34.08975 4.81667   1.000 8.65255   ? 284  TYR   A CG   1 
ATOM   4464 C  CD1  . TYR   B 2 279 ? 3.94290   -33.34684 3.86756   1.000 10.33699  ? 284  TYR   A CD1  1 
ATOM   4465 C  CD2  . TYR   B 2 279 ? 4.83797   -35.44275 4.57177   1.000 13.53709  ? 284  TYR   A CD2  1 
ATOM   4466 C  CE1  . TYR   B 2 279 ? 3.45907   -33.94594 2.70754   1.000 11.20772  ? 284  TYR   A CE1  1 
ATOM   4467 C  CE2  . TYR   B 2 279 ? 4.36113   -36.05084 3.42075   1.000 11.07813  ? 284  TYR   A CE2  1 
ATOM   4468 C  CZ   . TYR   B 2 279 ? 3.67418   -35.30194 2.49064   1.000 14.82853  ? 284  TYR   A CZ   1 
ATOM   4469 O  OH   . TYR   B 2 279 ? 3.20435   -35.90803 1.34062   1.000 16.39248  ? 284  TYR   A OH   1 
ATOM   4470 N  N    . ILE   B 2 280 ? 4.57537   -33.97050 9.27266   1.000 11.65586  ? 285  ILE   A N    1 
ATOM   4471 C  CA   . ILE   B 2 280 ? 5.20823   -34.00439 10.58573  1.000 15.58569  ? 285  ILE   A CA   1 
ATOM   4472 C  C    . ILE   B 2 280 ? 5.99730   -35.30133 10.69089  1.000 19.04206  ? 285  ILE   A C    1 
ATOM   4473 O  O    . ILE   B 2 280 ? 5.46540   -36.38238 10.39789  1.000 15.25210  ? 285  ILE   A O    1 
ATOM   4474 C  CB   . ILE   B 2 280 ? 4.18110   -33.87239 11.72661  1.000 8.87082   ? 285  ILE   A CB   1 
ATOM   4475 C  CG1  . ILE   B 2 280 ? 3.32303   -32.61746 11.51945  1.000 9.90052   ? 285  ILE   A CG1  1 
ATOM   4476 C  CG2  . ILE   B 2 280 ? 4.89894   -33.77027 13.07168  1.000 12.23116  ? 285  ILE   A CG2  1 
ATOM   4477 C  CD1  . ILE   B 2 280 ? 2.21591   -32.43147 12.58632  1.000 11.71522  ? 285  ILE   A CD1  1 
ATOM   4478 N  N    . TRP   B 2 281 ? 7.27625   -35.19122 11.05602  1.000 13.09921  ? 286  TRP   A N    1 
ATOM   4479 C  CA   . TRP   B 2 281 ? 8.15832   -36.34516 11.18518  1.000 19.49046  ? 286  TRP   A CA   1 
ATOM   4480 C  C    . TRP   B 2 281 ? 8.60517   -36.47605 12.62923  1.000 18.35110  ? 286  TRP   A C    1 
ATOM   4481 O  O    . TRP   B 2 281 ? 8.68303   -35.47900 13.35519  1.000 14.57066  ? 286  TRP   A O    1 
ATOM   4482 C  CB   . TRP   B 2 281 ? 9.43240   -36.23112 10.33531  1.000 16.81728  ? 286  TRP   A CB   1 
ATOM   4483 C  CG   . TRP   B 2 281 ? 9.30556   -36.23321 8.85229   1.000 15.49817  ? 286  TRP   A CG   1 
ATOM   4484 C  CD1  . TRP   B 2 281 ? 9.47272   -37.30725 8.01537   1.000 14.26643  ? 286  TRP   A CD1  1 
ATOM   4485 C  CD2  . TRP   B 2 281 ? 9.07158   -35.09327 8.00521   1.000 15.40237  ? 286  TRP   A CD2  1 
ATOM   4486 N  NE1  . TRP   B 2 281 ? 9.34584   -36.90633 6.69734   1.000 15.76037  ? 286  TRP   A NE1  1 
ATOM   4487 C  CE2  . TRP   B 2 281 ? 9.09875   -35.55535 6.66323   1.000 19.17071  ? 286  TRP   A CE2  1 
ATOM   4488 C  CE3  . TRP   B 2 281 ? 8.84346   -33.73228 8.24710   1.000 14.62344  ? 286  TRP   A CE3  1 
ATOM   4489 C  CZ2  . TRP   B 2 281 ? 8.89581   -34.70042 5.57116   1.000 18.01753  ? 286  TRP   A CZ2  1 
ATOM   4490 C  CZ3  . TRP   B 2 281 ? 8.64952   -32.88135 7.16104   1.000 13.40181  ? 286  TRP   A CZ3  1 
ATOM   4491 C  CH2  . TRP   B 2 281 ? 8.68269   -33.37142 5.83707   1.000 15.34892  ? 286  TRP   A CH2  1 
ATOM   4492 N  N    . ASN   B 2 282 ? 8.90121   -37.71800 13.03233  1.000 18.52057  ? 287  ASN   A N    1 
ATOM   4493 C  CA   . ASN   B 2 282 ? 9.61309   -37.96989 14.28042  1.000 13.48750  ? 287  ASN   A CA   1 
ATOM   4494 C  C    . ASN   B 2 282 ? 11.07009  -37.57880 14.07156  1.000 18.09918  ? 287  ASN   A C    1 
ATOM   4495 O  O    . ASN   B 2 282 ? 11.71922  -38.07681 13.14466  1.000 16.47816  ? 287  ASN   A O    1 
ATOM   4496 C  CB   . ASN   B 2 282 ? 9.46915   -39.44488 14.67249  1.000 17.48294  ? 287  ASN   A CB   1 
ATOM   4497 C  CG   . ASN   B 2 282 ? 10.21704  -39.80675 15.94859  1.000 18.27103  ? 287  ASN   A CG   1 
ATOM   4498 O  OD1  . ASN   B 2 282 ? 11.36899  -39.43167 16.14469  1.000 20.39376  ? 287  ASN   A OD1  1 
ATOM   4499 N  ND2  . ASN   B 2 282 ? 9.56199   -40.56375 16.81356  1.000 14.82221  ? 287  ASN   A ND2  1 
ATOM   4500 N  N    . LEU   B 2 283 ? 11.57594  -36.65172 14.89056  1.000 12.78005  ? 288  LEU   A N    1 
ATOM   4501 C  CA   . LEU   B 2 283 ? 12.91093  -36.11465 14.63167  1.000 18.75230  ? 288  LEU   A CA   1 
ATOM   4502 C  C    . LEU   B 2 283 ? 13.97300  -37.21058 14.69185  1.000 26.90122  ? 288  LEU   A C    1 
ATOM   4503 O  O    . LEU   B 2 283 ? 14.84910  -37.28557 13.81995  1.000 21.12436  ? 288  LEU   A O    1 
ATOM   4504 C  CB   . LEU   B 2 283 ? 13.23375  -34.98457 15.61765  1.000 18.54463  ? 288  LEU   A CB   1 
ATOM   4505 C  CG   . LEU   B 2 283 ? 14.59972  -34.27549 15.49175  1.000 21.13586  ? 288  LEU   A CG   1 
ATOM   4506 C  CD1  . LEU   B 2 283 ? 14.57656  -32.86246 16.08767  1.000 15.65272  ? 288  LEU   A CD1  1 
ATOM   4507 C  CD2  . LEU   B 2 283 ? 15.75771  -35.09438 16.11192  1.000 18.18757  ? 288  LEU   A CD2  1 
ATOM   4508 N  N    . GLN   B 2 284 ? 13.89595  -38.08352 15.69789  1.000 20.30950  ? 289  GLN   A N    1 
ATOM   4509 C  CA   . GLN   B 2 284 ? 14.91100  -39.11745 15.87306  1.000 23.69287  ? 289  GLN   A CA   1 
ATOM   4510 C  C    . GLN   B 2 284 ? 14.79118  -40.20851 14.81510  1.000 24.04072  ? 289  GLN   A C    1 
ATOM   4511 O  O    . GLN   B 2 284 ? 15.78428  -40.56848 14.17223  1.000 25.84904  ? 289  GLN   A O    1 
ATOM   4512 C  CB   . GLN   B 2 284 ? 14.81589  -39.71238 17.28108  1.000 24.86748  ? 289  GLN   A CB   1 
ATOM   4513 C  CG   . GLN   B 2 284 ? 15.21570  -38.72729 18.36707  1.000 27.98055  ? 289  GLN   A CG   1 
ATOM   4514 C  CD   . GLN   B 2 284 ? 16.68269  -38.30320 18.25720  1.000 42.23642  ? 289  GLN   A CD   1 
ATOM   4515 O  OE1  . GLN   B 2 284 ? 17.08456  -37.25414 18.77219  1.000 37.17776  ? 289  GLN   A OE1  1 
ATOM   4516 N  NE2  . GLN   B 2 284 ? 17.48781  -39.12918 17.59033  1.000 38.18903  ? 289  GLN   A NE2  1 
ATOM   4517 N  N    . THR   B 2 285 ? 13.59024  -40.75061 14.61001  1.000 24.16973  ? 290  THR   A N    1 
ATOM   4518 C  CA   . THR   B 2 285 ? 13.45741  -41.89966 13.72306  1.000 18.65479  ? 290  THR   A CA   1 
ATOM   4519 C  C    . THR   B 2 285 ? 13.27555  -41.52276 12.25502  1.000 26.68612  ? 290  THR   A C    1 
ATOM   4520 O  O    . THR   B 2 285 ? 13.43870  -42.38680 11.38308  1.000 21.55517  ? 290  THR   A O    1 
ATOM   4521 C  CB   . THR   B 2 285 ? 12.28743  -42.78672 14.16098  1.000 21.32587  ? 290  THR   A CB   1 
ATOM   4522 O  OG1  . THR   B 2 285 ? 11.04944  -42.21882 13.71082  1.000 20.33167  ? 290  THR   A OG1  1 
ATOM   4523 C  CG2  . THR   B 2 285 ? 12.25427  -42.92763 15.67198  1.000 15.56032  ? 290  THR   A CG2  1 
ATOM   4524 N  N    . LYS   B 2 286 ? 12.92550  -40.27180 11.95591  1.000 22.28956  ? 291  LYS   A N    1 
ATOM   4525 C  CA   . LYS   B 2 286 ? 12.77661  -39.78188 10.59186  1.000 19.46978  ? 291  LYS   A CA   1 
ATOM   4526 C  C    . LYS   B 2 286 ? 11.53172  -40.31501 9.89376   1.000 18.42700  ? 291  LYS   A C    1 
ATOM   4527 O  O    . LYS   B 2 286 ? 11.39184  -40.14408 8.66874   1.000 15.86256  ? 291  LYS   A O    1 
ATOM   4528 C  CB   . LYS   B 2 286 ? 14.00772  -40.11485 9.74102   1.000 24.02047  ? 291  LYS   A CB   1 
ATOM   4529 C  CG   . LYS   B 2 286 ? 15.30463  -39.51873 10.26112  1.000 27.06459  ? 291  LYS   A CG   1 
ATOM   4530 C  CD   . LYS   B 2 286 ? 16.51574  -40.12369 9.55229   1.000 25.84646  ? 291  LYS   A CD   1 
ATOM   4531 C  CE   . LYS   B 2 286 ? 16.70679  -41.57066 9.97239   1.000 28.96730  ? 291  LYS   A CE   1 
ATOM   4532 N  NZ   . LYS   B 2 286 ? 17.78392  -42.23163 9.18254   1.000 36.40662  ? 291  LYS   A NZ   1 
ATOM   4533 N  N    . GLU   B 2 287 ? 10.61968  -40.95603 10.61370  1.000 18.97976  ? 292  GLU   A N    1 
ATOM   4534 C  CA   . GLU   B 2 287 ? 9.39178   -41.43514 9.99459   1.000 17.81124  ? 292  GLU   A CA   1 
ATOM   4535 C  C    . GLU   B 2 287 ? 8.31070   -40.36321 10.07842  1.000 12.29394  ? 292  GLU   A C    1 
ATOM   4536 O  O    . GLU   B 2 287 ? 8.23955   -39.60816 11.05337  1.000 17.92573  ? 292  GLU   A O    1 
ATOM   4537 C  CB   . GLU   B 2 287 ? 8.92380   -42.73214 10.65762  1.000 20.60405  ? 292  GLU   A CB   1 
ATOM   4538 C  CG   . GLU   B 2 287 ? 8.46863   -42.56209 12.10056  1.000 24.93047  ? 292  GLU   A CG   1 
ATOM   4539 C  CD   . GLU   B 2 287 ? 8.53663   -43.86804 12.90664  1.000 56.51209  ? 292  GLU   A CD   1 
ATOM   4540 O  OE1  . GLU   B 2 287 ? 8.51877   -44.96007 12.28170  1.000 47.79477  ? 292  GLU   A OE1  1 
ATOM   4541 O  OE2  . GLU   B 2 287 ? 8.60849   -43.79696 14.16664  1.000 33.81602  ? 292  GLU   A OE2  1 
ATOM   4542 N  N    . ILE   B 2 288 ? 7.50181   -40.27732 9.02233   1.000 16.93949  ? 293  ILE   A N    1 
ATOM   4543 C  CA   . ILE   B 2 288 ? 6.33775   -39.40440 9.02715   1.000 20.74624  ? 293  ILE   A CA   1 
ATOM   4544 C  C    . ILE   B 2 288 ? 5.36167   -39.87340 10.09507  1.000 20.49754  ? 293  ILE   A C    1 
ATOM   4545 O  O    . ILE   B 2 288 ? 4.99974   -41.05642 10.15210  1.000 17.81189  ? 293  ILE   A O    1 
ATOM   4546 C  CB   . ILE   B 2 288 ? 5.67990   -39.40352 7.64108   1.000 21.72167  ? 293  ILE   A CB   1 
ATOM   4547 C  CG1  . ILE   B 2 288 ? 6.68299   -38.99151 6.56117   1.000 16.33726  ? 293  ILE   A CG1  1 
ATOM   4548 C  CG2  . ILE   B 2 288 ? 4.42984   -38.51860 7.64190   1.000 17.96755  ? 293  ILE   A CG2  1 
ATOM   4549 C  CD1  . ILE   B 2 288 ? 6.10114   -39.04963 5.15011   1.000 14.41401  ? 293  ILE   A CD1  1 
ATOM   4550 N  N    . VAL   B 2 289 ? 4.93451   -38.95238 10.95898  1.000 15.31268  ? 294  VAL   A N    1 
ATOM   4551 C  CA   . VAL   B 2 289 ? 3.97442   -39.28639 12.00689  1.000 15.99831  ? 294  VAL   A CA   1 
ATOM   4552 C  C    . VAL   B 2 289 ? 2.60341   -38.66449 11.77371  1.000 17.33903  ? 294  VAL   A C    1 
ATOM   4553 O  O    . VAL   B 2 289 ? 1.64836   -39.04952 12.46063  1.000 19.56262  ? 294  VAL   A O    1 
ATOM   4554 C  CB   . VAL   B 2 289 ? 4.49825   -38.90728 13.40993  1.000 18.30474  ? 294  VAL   A CB   1 
ATOM   4555 C  CG1  . VAL   B 2 289 ? 5.75826   -39.74817 13.78411  1.000 13.04347  ? 294  VAL   A CG1  1 
ATOM   4556 C  CG2  . VAL   B 2 289 ? 4.76114   -37.38525 13.51287  1.000 16.80495  ? 294  VAL   A CG2  1 
ATOM   4557 N  N    . GLN   B 2 290 ? 2.46745   -37.73555 10.82964  1.000 18.98512  ? 295  GLN   A N    1 
ATOM   4558 C  CA   . GLN   B 2 290 ? 1.16445   -37.16966 10.50347  1.000 20.36945  ? 295  GLN   A CA   1 
ATOM   4559 C  C    . GLN   B 2 290 ? 1.28553   -36.34172 9.23544   1.000 10.74960  ? 295  GLN   A C    1 
ATOM   4560 O  O    . GLN   B 2 290 ? 2.34452   -35.77567 8.94852   1.000 14.11758  ? 295  GLN   A O    1 
ATOM   4561 C  CB   . GLN   B 2 290 ? 0.60926   -36.29763 11.64536  1.000 13.30427  ? 295  GLN   A CB   1 
ATOM   4562 C  CG   . GLN   B 2 290 ? -0.69376  -36.81369 12.23125  1.000 14.45522  ? 295  GLN   A CG   1 
ATOM   4563 C  CD   . GLN   B 2 290 ? -1.47392  -35.75869 13.02411  1.000 21.78067  ? 295  GLN   A CD   1 
ATOM   4564 O  OE1  . GLN   B 2 290 ? -0.91105  -35.02461 13.83013  1.000 13.20889  ? 295  GLN   A OE1  1 
ATOM   4565 N  NE2  . GLN   B 2 290 ? -2.78190  -35.68579 12.78397  1.000 17.19911  ? 295  GLN   A NE2  1 
ATOM   4566 N  N    . LYS   B 2 291 ? 0.18060   -36.26384 8.49732   1.000 12.18948  ? 296  LYS   A N    1 
ATOM   4567 C  CA   . LYS   B 2 291 ? 0.01366   -35.33791 7.38225   1.000 21.59050  ? 296  LYS   A CA   1 
ATOM   4568 C  C    . LYS   B 2 291 ? -1.32741  -34.63099 7.54206   1.000 16.89512  ? 296  LYS   A C    1 
ATOM   4569 O  O    . LYS   B 2 291 ? -2.36437  -35.28605 7.62099   1.000 17.17156  ? 296  LYS   A O    1 
ATOM   4570 C  CB   . LYS   B 2 291 ? 0.08285   -36.07598 6.04430   1.000 17.39357  ? 296  LYS   A CB   1 
ATOM   4571 C  CG   . LYS   B 2 291 ? 1.39392   -36.82590 5.84848   1.000 18.04387  ? 296  LYS   A CG   1 
ATOM   4572 C  CD   . LYS   B 2 291 ? 1.16908   -38.16596 5.17553   1.000 20.03891  ? 296  LYS   A CD   1 
ATOM   4573 C  CE   . LYS   B 2 291 ? 0.99523   -38.02105 3.68150   1.000 28.78347  ? 296  LYS   A CE   1 
ATOM   4574 N  NZ   . LYS   B 2 291 ? 0.98039   -39.37209 3.02858   1.000 33.36366  ? 296  LYS   A NZ   1 
ATOM   4575 N  N    . LEU   B 2 292 ? -1.31350  -33.30299 7.57199   1.000 18.03872  ? 297  LEU   A N    1 
ATOM   4576 C  CA   . LEU   B 2 292 ? -2.51358  -32.51605 7.84982   1.000 13.35859  ? 297  LEU   A CA   1 
ATOM   4577 C  C    . LEU   B 2 292 ? -3.15446  -32.10117 6.53173   1.000 16.97404  ? 297  LEU   A C    1 
ATOM   4578 O  O    . LEU   B 2 292 ? -2.54843  -31.36317 5.75075   1.000 12.69952  ? 297  LEU   A O    1 
ATOM   4579 C  CB   . LEU   B 2 292 ? -2.17675  -31.29198 8.69979   1.000 12.79496  ? 297  LEU   A CB   1 
ATOM   4580 C  CG   . LEU   B 2 292 ? -1.33287  -31.53485 9.96089   1.000 15.67657  ? 297  LEU   A CG   1 
ATOM   4581 C  CD1  . LEU   B 2 292 ? -1.26005  -30.27980 10.82983  1.000 11.44494  ? 297  LEU   A CD1  1 
ATOM   4582 C  CD2  . LEU   B 2 292 ? -1.88588  -32.72185 10.75990  1.000 17.98421  ? 297  LEU   A CD2  1 
ATOM   4583 N  N    . GLN   B 2 293 ? -4.37541  -32.57126 6.28562   1.000 16.90004  ? 298  GLN   A N    1 
ATOM   4584 C  CA   . GLN   B 2 293 ? -5.08730  -32.25738 5.05253   1.000 16.78861  ? 298  GLN   A CA   1 
ATOM   4585 C  C    . GLN   B 2 293 ? -6.05939  -31.09643 5.25536   1.000 19.14450  ? 298  GLN   A C    1 
ATOM   4586 O  O    . GLN   B 2 293 ? -6.71151  -30.99242 6.29928   1.000 17.65691  ? 298  GLN   A O    1 
ATOM   4587 C  CB   . GLN   B 2 293 ? -5.85016  -33.47946 4.54151   1.000 24.70002  ? 298  GLN   A CB   1 
ATOM   4588 C  CG   . GLN   B 2 293 ? -6.67405  -33.16958 3.28141   1.000 43.85078  ? 298  GLN   A CG   1 
ATOM   4589 C  CD   . GLN   B 2 293 ? -7.79095  -34.16467 3.05134   1.000 46.40631  ? 298  GLN   A CD   1 
ATOM   4590 O  OE1  . GLN   B 2 293 ? -7.56687  -35.37865 3.05644   1.000 52.20919  ? 298  GLN   A OE1  1 
ATOM   4591 N  NE2  . GLN   B 2 293 ? -9.01197  -33.65476 2.87418   1.000 48.66853  ? 298  GLN   A NE2  1 
ATOM   4592 N  N    . GLY   B 2 294 ? -6.15934  -30.22949 4.24630   1.000 14.55277  ? 299  GLY   A N    1 
ATOM   4593 C  CA   . GLY   B 2 294 ? -7.11442  -29.14155 4.30014   1.000 16.22963  ? 299  GLY   A CA   1 
ATOM   4594 C  C    . GLY   B 2 294 ? -6.81740  -27.99059 3.36210   1.000 13.89599  ? 299  GLY   A C    1 
ATOM   4595 O  O    . GLY   B 2 294 ? -7.72938  -27.39468 2.78597   1.000 16.37385  ? 299  GLY   A O    1 
ATOM   4596 N  N    . HIS   B 2 295 ? -5.54940  -27.65751 3.19022   1.000 13.04185  ? 300  HIS   A N    1 
ATOM   4597 C  CA   . HIS   B 2 295 ? -5.21637  -26.58254 2.27420   1.000 11.95994  ? 300  HIS   A CA   1 
ATOM   4598 C  C    . HIS   B 2 295 ? -5.45419  -27.00964 0.83119   1.000 11.62550  ? 300  HIS   A C    1 
ATOM   4599 O  O    . HIS   B 2 295 ? -5.39908  -28.19665 0.49427   1.000 16.22992  ? 300  HIS   A O    1 
ATOM   4600 C  CB   . HIS   B 2 295 ? -3.76442  -26.15243 2.47633   1.000 8.02766   ? 300  HIS   A CB   1 
ATOM   4601 C  CG   . HIS   B 2 295 ? -3.54761  -25.38935 3.74431   1.000 13.09996  ? 300  HIS   A CG   1 
ATOM   4602 N  ND1  . HIS   B 2 295 ? -3.96671  -24.08537 3.90519   1.000 12.50500  ? 300  HIS   A ND1  1 
ATOM   4603 C  CD2  . HIS   B 2 295 ? -2.96471  -25.74524 4.91739   1.000 10.47290  ? 300  HIS   A CD2  1 
ATOM   4604 C  CE1  . HIS   B 2 295 ? -3.64487  -23.66828 5.11820   1.000 9.77312   ? 300  HIS   A CE1  1 
ATOM   4605 N  NE2  . HIS   B 2 295 ? -3.03888  -24.65820 5.75332   1.000 8.98403   ? 300  HIS   A NE2  1 
ATOM   4606 N  N    . THR   B 2 296 ? -5.71116  -26.01970 -0.02889  1.000 8.49721   ? 301  THR   A N    1 
ATOM   4607 C  CA   . THR   B 2 296 ? -5.96400  -26.24280 -1.45190  1.000 15.83651  ? 301  THR   A CA   1 
ATOM   4608 C  C    . THR   B 2 296 ? -4.83393  -25.73577 -2.35081  1.000 14.60281  ? 301  THR   A C    1 
ATOM   4609 O  O    . THR   B 2 296 ? -4.99480  -25.69785 -3.57883  1.000 10.55484  ? 301  THR   A O    1 
ATOM   4610 C  CB   . THR   B 2 296 ? -7.28400  -25.57991 -1.87108  1.000 13.13733  ? 301  THR   A CB   1 
ATOM   4611 O  OG1  . THR   B 2 296 ? -7.21912  -24.17989 -1.58015  1.000 16.41137  ? 301  THR   A OG1  1 
ATOM   4612 C  CG2  . THR   B 2 296 ? -8.47204  -26.18495 -1.12918  1.000 8.19591   ? 301  THR   A CG2  1 
ATOM   4613 N  N    . ASP   B 2 297 ? -3.70602  -25.33567 -1.77471  1.000 11.12174  ? 302  ASP   A N    1 
ATOM   4614 C  CA   . ASP   B 2 297 ? -2.54197  -24.89963 -2.53761  1.000 12.10255  ? 302  ASP   A CA   1 
ATOM   4615 C  C    . ASP   B 2 297 ? -1.30004  -25.21850 -1.71846  1.000 11.52793  ? 302  ASP   A C    1 
ATOM   4616 O  O    . ASP   B 2 297 ? -1.38813  -25.67945 -0.57244  1.000 9.99716   ? 302  ASP   A O    1 
ATOM   4617 C  CB   . ASP   B 2 297 ? -2.61803  -23.40266 -2.86870  1.000 10.32569  ? 302  ASP   A CB   1 
ATOM   4618 C  CG   . ASP   B 2 297 ? -1.80893  -23.02967 -4.10264  1.000 13.45556  ? 302  ASP   A CG   1 
ATOM   4619 O  OD1  . ASP   B 2 297 ? -1.08281  -23.89665 -4.62551  1.000 14.35920  ? 302  ASP   A OD1  1 
ATOM   4620 O  OD2  . ASP   B 2 297 ? -1.91695  -21.86970 -4.55571  1.000 12.19960  ? 302  ASP   A OD2  1 
ATOM   4621 N  N    . VAL   B 2 298 ? -0.13699  -24.95146 -2.31535  1.000 11.18840  ? 303  VAL   A N    1 
ATOM   4622 C  CA   . VAL   B 2 298 ? 1.13396   -25.20534 -1.65220  1.000 11.71388  ? 303  VAL   A CA   1 
ATOM   4623 C  C    . VAL   B 2 298 ? 1.10477   -24.63826 -0.23823  1.000 11.15611  ? 303  VAL   A C    1 
ATOM   4624 O  O    . VAL   B 2 298 ? 0.71467   -23.48828 -0.02434  1.000 9.91575   ? 303  VAL   A O    1 
ATOM   4625 C  CB   . VAL   B 2 298 ? 2.28300   -24.59831 -2.47411  1.000 12.10481  ? 303  VAL   A CB   1 
ATOM   4626 C  CG1  . VAL   B 2 298 ? 3.62595   -24.86118 -1.78295  1.000 10.25034  ? 303  VAL   A CG1  1 
ATOM   4627 C  CG2  . VAL   B 2 298 ? 2.27920   -25.14339 -3.92808  1.000 10.45817  ? 303  VAL   A CG2  1 
ATOM   4628 N  N    . VAL   B 2 299 ? 1.51272   -25.45018 0.73186   1.000 9.48506   ? 304  VAL   A N    1 
ATOM   4629 C  CA   . VAL   B 2 299 ? 1.68454   -24.99509 2.11185   1.000 11.84979  ? 304  VAL   A CA   1 
ATOM   4630 C  C    . VAL   B 2 299 ? 3.10949   -24.45699 2.21097   1.000 15.85592  ? 304  VAL   A C    1 
ATOM   4631 O  O    . VAL   B 2 299 ? 4.07052   -25.21592 2.37312   1.000 12.59962  ? 304  VAL   A O    1 
ATOM   4632 C  CB   . VAL   B 2 299 ? 1.42450   -26.11605 3.11788   1.000 10.22325  ? 304  VAL   A CB   1 
ATOM   4633 C  CG1  . VAL   B 2 299 ? 1.73832   -25.65695 4.53489   1.000 11.66449  ? 304  VAL   A CG1  1 
ATOM   4634 C  CG2  . VAL   B 2 299 ? -0.03045  -26.60316 3.00475   1.000 8.85335   ? 304  VAL   A CG2  1 
ATOM   4635 N  N    . ILE   B 2 300 ? 3.25642   -23.13999 2.07891   1.000 10.04924  ? 305  ILE   A N    1 
ATOM   4636 C  CA   . ILE   B 2 300 ? 4.59239   -22.56690 2.03003   1.000 9.67769   ? 305  ILE   A CA   1 
ATOM   4637 C  C    . ILE   B 2 300 ? 5.12921   -22.18679 3.41306   1.000 12.86685  ? 305  ILE   A C    1 
ATOM   4638 O  O    . ILE   B 2 300 ? 6.34118   -21.99470 3.56418   1.000 10.80471  ? 305  ILE   A O    1 
ATOM   4639 C  CB   . ILE   B 2 300 ? 4.61241   -21.35696 1.07896   1.000 10.41125  ? 305  ILE   A CB   1 
ATOM   4640 C  CG1  . ILE   B 2 300 ? 6.00246   -21.17690 0.48510   1.000 13.07030  ? 305  ILE   A CG1  1 
ATOM   4641 C  CG2  . ILE   B 2 300 ? 4.16425   -20.07795 1.79284   1.000 12.16787  ? 305  ILE   A CG2  1 
ATOM   4642 C  CD1  . ILE   B 2 300 ? 6.02953   -20.30296 -0.72395  1.000 13.52692  ? 305  ILE   A CD1  1 
ATOM   4643 N  N    . SER   B 2 301 ? 4.27710   -22.08779 4.42697   1.000 9.93470   ? 306  SER   A N    1 
ATOM   4644 C  CA   . SER   B 2 301 ? 4.75093   -21.66369 5.73699   1.000 11.71600  ? 306  SER   A CA   1 
ATOM   4645 C  C    . SER   B 2 301 ? 4.02986   -22.44467 6.82196   1.000 11.25878  ? 306  SER   A C    1 
ATOM   4646 O  O    . SER   B 2 301 ? 2.83990   -22.73576 6.69485   1.000 11.55777  ? 306  SER   A O    1 
ATOM   4647 C  CB   . SER   B 2 301 ? 4.53881   -20.15169 5.94289   1.000 10.18112  ? 306  SER   A CB   1 
ATOM   4648 O  OG   . SER   B 2 301 ? 4.92964   -19.73559 7.24590   1.000 13.45930  ? 306  SER   A OG   1 
ATOM   4649 N  N    . THR   B 2 302 ? 4.76777   -22.79457 7.87206   1.000 7.82887   ? 307  THR   A N    1 
ATOM   4650 C  CA   . THR   B 2 302 ? 4.21568   -23.37054 9.08503   1.000 15.18085  ? 307  THR   A CA   1 
ATOM   4651 C  C    . THR   B 2 302 ? 4.92651   -22.76142 10.28307  1.000 14.38027  ? 307  THR   A C    1 
ATOM   4652 O  O    . THR   B 2 302 ? 6.05549   -22.26735 10.18017  1.000 12.35384  ? 307  THR   A O    1 
ATOM   4653 C  CB   . THR   B 2 302 ? 4.36978   -24.89052 9.13613   1.000 16.24550  ? 307  THR   A CB   1 
ATOM   4654 O  OG1  . THR   B 2 302 ? 5.72083   -25.22145 8.80429   1.000 13.45285  ? 307  THR   A OG1  1 
ATOM   4655 C  CG2  . THR   B 2 302 ? 3.40793   -25.58264 8.16607   1.000 12.76100  ? 307  THR   A CG2  1 
ATOM   4656 N  N    . ALA   B 2 303 ? 4.25639   -22.81140 11.43200  1.000 12.43037  ? 308  ALA   A N    1 
ATOM   4657 C  CA   . ALA   B 2 303 ? 4.82423   -22.26230 12.65603  1.000 11.44700  ? 308  ALA   A CA   1 
ATOM   4658 C  C    . ALA   B 2 303 ? 4.35815   -23.09526 13.83503  1.000 12.41442  ? 308  ALA   A C    1 
ATOM   4659 O  O    . ALA   B 2 303 ? 3.21718   -23.56434 13.85293  1.000 14.54564  ? 308  ALA   A O    1 
ATOM   4660 C  CB   . ALA   B 2 303 ? 4.41511   -20.79631 12.85491  1.000 12.41265  ? 308  ALA   A CB   1 
ATOM   4661 N  N    . CYS   B 2 304 ? 5.23906   -23.26515 14.82113  1.000 11.96871  ? 309  CYS   A N    1 
ATOM   4662 C  CA   . CYS   B 2 304 ? 4.92498   -24.02310 16.02514  1.000 14.28699  ? 309  CYS   A CA   1 
ATOM   4663 C  C    . CYS   B 2 304 ? 4.81479   -23.07704 17.21608  1.000 16.39443  ? 309  CYS   A C    1 
ATOM   4664 O  O    . CYS   B 2 304 ? 5.75571   -22.33396 17.52114  1.000 12.67752  ? 309  CYS   A O    1 
ATOM   4665 C  CB   . CYS   B 2 304 ? 5.97603   -25.10502 16.27532  1.000 16.26929  ? 309  CYS   A CB   1 
ATOM   4666 S  SG   . CYS   B 2 304 ? 6.09725   -26.27009 14.90339  1.000 16.26879  ? 309  CYS   A SG   1 
ATOM   4667 N  N    . HIS   B 2 305 ? 3.66772   -23.11608 17.87996  1.000 14.89391  ? 310  HIS   A N    1 
ATOM   4668 C  CA   . HIS   B 2 305 ? 3.43154   -22.27003 19.03388  1.000 14.48541  ? 310  HIS   A CA   1 
ATOM   4669 C  C    . HIS   B 2 305 ? 4.50844   -22.49490 20.09601  1.000 18.72493  ? 310  HIS   A C    1 
ATOM   4670 O  O    . HIS   B 2 305 ? 4.95850   -23.63186 20.30012  1.000 13.45190  ? 310  HIS   A O    1 
ATOM   4671 C  CB   . HIS   B 2 305 ? 2.05850   -22.56109 19.62975  1.000 17.13373  ? 310  HIS   A CB   1 
ATOM   4672 C  CG   . HIS   B 2 305 ? 1.60732   -21.53407 20.61765  1.000 18.62083  ? 310  HIS   A CG   1 
ATOM   4673 N  ND1  . HIS   B 2 305 ? 1.88718   -21.62397 21.96568  1.000 16.82087  ? 310  HIS   A ND1  1 
ATOM   4674 C  CD2  . HIS   B 2 305 ? 0.89826   -20.39412 20.45551  1.000 13.72481  ? 310  HIS   A CD2  1 
ATOM   4675 C  CE1  . HIS   B 2 305 ? 1.36905   -20.58397 22.59157  1.000 13.05994  ? 310  HIS   A CE1  1 
ATOM   4676 N  NE2  . HIS   B 2 305 ? 0.76509   -19.82206 21.69846  1.000 13.59649  ? 310  HIS   A NE2  1 
ATOM   4677 N  N    . PRO   B 2 306 ? 4.91630   -21.44583 20.81200  1.000 11.50048  ? 311  PRO   A N    1 
ATOM   4678 C  CA   . PRO   B 2 306 ? 6.05721   -21.58271 21.73113  1.000 14.29785  ? 311  PRO   A CA   1 
ATOM   4679 C  C    . PRO   B 2 306 ? 5.76112   -22.35366 23.01214  1.000 22.68368  ? 311  PRO   A C    1 
ATOM   4680 O  O    . PRO   B 2 306 ? 6.71609   -22.85656 23.61827  1.000 18.02481  ? 311  PRO   A O    1 
ATOM   4681 C  CB   . PRO   B 2 306 ? 6.44808   -20.12567 22.03209  1.000 14.84138  ? 311  PRO   A CB   1 
ATOM   4682 C  CG   . PRO   B 2 306 ? 5.22305   -19.32676 21.75391  1.000 12.75004  ? 311  PRO   A CG   1 
ATOM   4683 C  CD   . PRO   B 2 306 ? 4.49922   -20.04387 20.63988  1.000 13.18591  ? 311  PRO   A CD   1 
ATOM   4684 N  N    . THR   B 2 307 ? 4.49908   -22.47572 23.45401  1.000 18.20474  ? 312  THR   A N    1 
ATOM   4685 C  CA   . THR   B 2 307 ? 4.25200   -23.21866 24.69403  1.000 22.56499  ? 312  THR   A CA   1 
ATOM   4686 C  C    . THR   B 2 307 ? 3.23309   -24.34874 24.55798  1.000 19.67340  ? 312  THR   A C    1 
ATOM   4687 O  O    . THR   B 2 307 ? 3.28907   -25.30769 25.33304  1.000 18.11319  ? 312  THR   A O    1 
ATOM   4688 C  CB   . THR   B 2 307 ? 3.82981   -22.27563 25.83693  1.000 20.11696  ? 312  THR   A CB   1 
ATOM   4689 O  OG1  . THR   B 2 307 ? 2.69180   -21.48072 25.45876  1.000 14.60915  ? 312  THR   A OG1  1 
ATOM   4690 C  CG2  . THR   B 2 307 ? 4.98571   -21.35753 26.21400  1.000 19.32877  ? 312  THR   A CG2  1 
ATOM   4691 N  N    . GLU   B 2 308 ? 2.31018   -24.27285 23.60288  1.000 16.23276  ? 313  GLU   A N    1 
ATOM   4692 C  CA   . GLU   B 2 308 ? 1.32227   -25.32893 23.40383  1.000 15.02455  ? 313  GLU   A CA   1 
ATOM   4693 C  C    . GLU   B 2 308 ? 1.55347   -26.05699 22.08089  1.000 18.24564  ? 313  GLU   A C    1 
ATOM   4694 O  O    . GLU   B 2 308 ? 2.22553   -25.55399 21.17894  1.000 15.58271  ? 313  GLU   A O    1 
ATOM   4695 C  CB   . GLU   B 2 308 ? -0.10077  -24.76102 23.43064  1.000 16.39241  ? 313  GLU   A CB   1 
ATOM   4696 C  CG   . GLU   B 2 308 ? -0.26894  -23.59298 24.35856  1.000 20.34853  ? 313  GLU   A CG   1 
ATOM   4697 C  CD   . GLU   B 2 308 ? -0.11407  -23.98889 25.81360  1.000 28.93087  ? 313  GLU   A CD   1 
ATOM   4698 O  OE1  . GLU   B 2 308 ? -0.70505  -25.01191 26.20959  1.000 23.92173  ? 313  GLU   A OE1  1 
ATOM   4699 O  OE2  . GLU   B 2 308 ? 0.60780   -23.28280 26.55664  1.000 35.70181  ? 313  GLU   A OE2  1 
ATOM   4700 N  N    . ASN   B 2 309 ? 0.99056   -27.26603 21.97790  1.000 17.91831  ? 314  ASN   A N    1 
ATOM   4701 C  CA   . ASN   B 2 309 ? 1.05074   -28.06809 20.74995  1.000 20.14814  ? 314  ASN   A CA   1 
ATOM   4702 C  C    . ASN   B 2 309 ? 0.03781   -27.49822 19.75681  1.000 15.08342  ? 314  ASN   A C    1 
ATOM   4703 O  O    . ASN   B 2 309 ? -1.05613  -28.03330 19.55072  1.000 16.22971  ? 314  ASN   A O    1 
ATOM   4704 C  CB   . ASN   B 2 309 ? 0.77281   -29.54310 21.03300  1.000 16.29532  ? 314  ASN   A CB   1 
ATOM   4705 C  CG   . ASN   B 2 309 ? 1.61473   -30.09798 22.15713  1.000 18.69804  ? 314  ASN   A CG   1 
ATOM   4706 O  OD1  . ASN   B 2 309 ? 2.80169   -29.78989 22.28524  1.000 23.23211  ? 314  ASN   A OD1  1 
ATOM   4707 N  ND2  . ASN   B 2 309 ? 1.00369   -30.93397 22.98511  1.000 25.45214  ? 314  ASN   A ND2  1 
ATOM   4708 N  N    . ILE   B 2 310 ? 0.40380   -26.36423 19.16779  1.000 12.69783  ? 315  ILE   A N    1 
ATOM   4709 C  CA   . ILE   B 2 310 ? -0.40814  -25.65833 18.18366  1.000 13.28074  ? 315  ILE   A CA   1 
ATOM   4710 C  C    . ILE   B 2 310 ? 0.46397   -25.36434 16.97574  1.000 13.56441  ? 315  ILE   A C    1 
ATOM   4711 O  O    . ILE   B 2 310 ? 1.60892   -24.91426 17.12084  1.000 13.36122  ? 315  ILE   A O    1 
ATOM   4712 C  CB   . ILE   B 2 310 ? -0.99329  -24.34134 18.73453  1.000 12.67235  ? 315  ILE   A CB   1 
ATOM   4713 C  CG1  . ILE   B 2 310 ? -1.96940  -24.60534 19.88744  1.000 19.02858  ? 315  ILE   A CG1  1 
ATOM   4714 C  CG2  . ILE   B 2 310 ? -1.71622  -23.59945 17.63041  1.000 12.49331  ? 315  ILE   A CG2  1 
ATOM   4715 C  CD1  . ILE   B 2 310 ? -2.60654  -23.33435 20.45630  1.000 12.24703  ? 315  ILE   A CD1  1 
ATOM   4716 N  N    . ILE   B 2 311 ? -0.07989  -25.60845 15.78769  1.000 14.02248  ? 316  ILE   A N    1 
ATOM   4717 C  CA   . ILE   B 2 311 ? 0.61023   -25.36347 14.52775  1.000 13.90182  ? 316  ILE   A CA   1 
ATOM   4718 C  C    . ILE   B 2 311 ? -0.21375  -24.39357 13.69561  1.000 13.76552  ? 316  ILE   A C    1 
ATOM   4719 O  O    . ILE   B 2 311 ? -1.43773  -24.53366 13.59649  1.000 14.86364  ? 316  ILE   A O    1 
ATOM   4720 C  CB   . ILE   B 2 311 ? 0.84040   -26.66750 13.74085  1.000 11.80455  ? 316  ILE   A CB   1 
ATOM   4721 C  CG1  . ILE   B 2 311 ? 1.92439   -27.52639 14.39002  1.000 9.38288   ? 316  ILE   A CG1  1 
ATOM   4722 C  CG2  . ILE   B 2 311 ? 1.22653   -26.35455 12.31388  1.000 11.14913  ? 316  ILE   A CG2  1 
ATOM   4723 C  CD1  . ILE   B 2 311 ? 2.03655   -28.88842 13.75010  1.000 10.91821  ? 316  ILE   A CD1  1 
ATOM   4724 N  N    . ALA   B 2 312 ? 0.45725   -23.41656 13.09063  1.000 10.69819  ? 317  ALA   A N    1 
ATOM   4725 C  CA   . ALA   B 2 312 ? -0.15469  -22.56966 12.07952  1.000 12.34939  ? 317  ALA   A CA   1 
ATOM   4726 C  C    . ALA   B 2 312 ? 0.42448   -22.92270 10.71660  1.000 12.20910  ? 317  ALA   A C    1 
ATOM   4727 O  O    . ALA   B 2 312 ? 1.64550   -23.08962 10.57274  1.000 13.09195  ? 317  ALA   A O    1 
ATOM   4728 C  CB   . ALA   B 2 312 ? 0.07118   -21.08263 12.37246  1.000 11.23167  ? 317  ALA   A CB   1 
ATOM   4729 N  N    . SER   B 2 313 ? -0.44841  -23.03181 9.71651   1.000 8.12986   ? 318  SER   A N    1 
ATOM   4730 C  CA   . SER   B 2 313 ? -0.01125  -23.26786 8.34857   1.000 9.46415   ? 318  SER   A CA   1 
ATOM   4731 C  C    . SER   B 2 313 ? -0.61722  -22.21795 7.42945   1.000 12.70152  ? 318  SER   A C    1 
ATOM   4732 O  O    . SER   B 2 313 ? -1.69128  -21.67800 7.70330   1.000 14.75043  ? 318  SER   A O    1 
ATOM   4733 C  CB   . SER   B 2 313 ? -0.38610  -24.67691 7.87861   1.000 10.00631  ? 318  SER   A CB   1 
ATOM   4734 O  OG   . SER   B 2 313 ? -1.79010  -24.86300 7.96447   1.000 13.77293  ? 318  SER   A OG   1 
ATOM   4735 N  N    . ALA   B 2 314 ? 0.07288   -21.92996 6.33050   1.000 7.73952   ? 319  ALA   A N    1 
ATOM   4736 C  CA   . ALA   B 2 314 ? -0.39509  -20.91305 5.40240   1.000 10.53098  ? 319  ALA   A CA   1 
ATOM   4737 C  C    . ALA   B 2 314 ? -0.09490  -21.34111 3.97045   1.000 10.10230  ? 319  ALA   A C    1 
ATOM   4738 O  O    . ALA   B 2 314 ? 0.94617   -21.95405 3.70560   1.000 9.07337   ? 319  ALA   A O    1 
ATOM   4739 C  CB   . ALA   B 2 314 ? 0.25179   -19.55799 5.71939   1.000 9.13766   ? 319  ALA   A CB   1 
ATOM   4740 N  N    . ALA   B 2 315 ? -0.99983  -21.00022 3.04234   1.000 7.98032   ? 320  ALA   A N    1 
ATOM   4741 C  CA   . ALA   B 2 315 ? -0.93965  -21.50829 1.67137   1.000 15.02094  ? 320  ALA   A CA   1 
ATOM   4742 C  C    . ALA   B 2 315 ? -0.96061  -20.36735 0.64631   1.000 11.14955  ? 320  ALA   A C    1 
ATOM   4743 O  O    . ALA   B 2 315 ? -1.24272  -19.20835 0.97121   1.000 7.79832   ? 320  ALA   A O    1 
ATOM   4744 C  CB   . ALA   B 2 315 ? -2.08355  -22.49638 1.40731   1.000 8.68862   ? 320  ALA   A CB   1 
ATOM   4745 N  N    . LEU   B 2 316 ? -0.66745  -20.71840 -0.61464  1.000 9.59109   ? 321  LEU   A N    1 
ATOM   4746 C  CA   . LEU   B 2 316 ? -0.39941  -19.73844 -1.66467  1.000 12.66675  ? 321  LEU   A CA   1 
ATOM   4747 C  C    . LEU   B 2 316 ? -1.69436  -19.28557 -2.35183  1.000 10.22016  ? 321  LEU   A C    1 
ATOM   4748 O  O    . LEU   B 2 316 ? -2.79141  -19.45061 -1.82094  1.000 10.16338  ? 321  LEU   A O    1 
ATOM   4749 C  CB   . LEU   B 2 316 ? 0.59874   -20.31643 -2.67153  1.000 9.77678   ? 321  LEU   A CB   1 
ATOM   4750 C  CG   . LEU   B 2 316 ? 1.98970   -20.60831 -2.13836  1.000 9.06856   ? 321  LEU   A CG   1 
ATOM   4751 C  CD1  . LEU   B 2 316 ? 2.85086   -21.16231 -3.25324  1.000 13.75651  ? 321  LEU   A CD1  1 
ATOM   4752 C  CD2  . LEU   B 2 316 ? 2.58856   -19.33524 -1.57937  1.000 7.89236   ? 321  LEU   A CD2  1 
ATOM   4753 N  N    . GLU   B 2 317 ? -1.57126  -18.76563 -3.57585  1.000 10.37871  ? 322  GLU   A N    1 
ATOM   4754 C  CA   . GLU   B 2 317 ? -2.58026  -17.87873 -4.16301  1.000 13.07419  ? 322  GLU   A CA   1 
ATOM   4755 C  C    . GLU   B 2 317 ? -3.94020  -18.54883 -4.34611  1.000 13.96205  ? 322  GLU   A C    1 
ATOM   4756 O  O    . GLU   B 2 317 ? -4.97025  -17.86589 -4.30926  1.000 13.54564  ? 322  GLU   A O    1 
ATOM   4757 C  CB   . GLU   B 2 317 ? -2.07215  -17.35877 -5.51698  1.000 16.94327  ? 322  GLU   A CB   1 
ATOM   4758 C  CG   . GLU   B 2 317 ? -2.86316  -16.18185 -6.11513  1.000 21.61520  ? 322  GLU   A CG   1 
ATOM   4759 C  CD   . GLU   B 2 317 ? -2.54033  -14.83379 -5.43317  1.000 35.12332  ? 322  GLU   A CD   1 
ATOM   4760 O  OE1  . GLU   B 2 317 ? -1.55541  -14.77168 -4.64707  1.000 29.05033  ? 322  GLU   A OE1  1 
ATOM   4761 O  OE2  . GLU   B 2 317 ? -3.26736  -13.84186 -5.69530  1.000 31.41567  ? 322  GLU   A OE2  1 
ATOM   4762 N  N    . ASN   B 2 318 ? -3.97508  -19.85784 -4.59105  1.000 12.68891  ? 323  ASN   A N    1 
ATOM   4763 C  CA   . ASN   B 2 318 ? -5.23001  -20.56094 -4.84014  1.000 17.99717  ? 323  ASN   A CA   1 
ATOM   4764 C  C    . ASN   B 2 318 ? -5.88912  -21.03291 -3.56219  1.000 21.28296  ? 323  ASN   A C    1 
ATOM   4765 O  O    . ASN   B 2 318 ? -6.89506  -21.75098 -3.62125  1.000 17.86265  ? 323  ASN   A O    1 
ATOM   4766 C  CB   . ASN   B 2 318 ? -4.99983  -21.74198 -5.78705  1.000 13.10992  ? 323  ASN   A CB   1 
ATOM   4767 C  CG   . ASN   B 2 318 ? -4.49171  -21.29002 -7.13902  1.000 24.37007  ? 323  ASN   A CG   1 
ATOM   4768 O  OD1  . ASN   B 2 318 ? -4.96972  -20.29108 -7.68013  1.000 28.08706  ? 323  ASN   A OD1  1 
ATOM   4769 N  ND2  . ASN   B 2 318 ? -3.50461  -21.99698 -7.67788  1.000 20.62076  ? 323  ASN   A ND2  1 
ATOM   4770 N  N    . ASP   B 2 319 ? -5.34527  -20.64181 -2.41115  1.000 15.12702  ? 324  ASP   A N    1 
ATOM   4771 C  CA   . ASP   B 2 319 ? -5.89838  -21.03178 -1.12519  1.000 14.60435  ? 324  ASP   A CA   1 
ATOM   4772 C  C    . ASP   B 2 319 ? -6.14855  -19.77575 -0.30128  1.000 13.70847  ? 324  ASP   A C    1 
ATOM   4773 O  O    . ASP   B 2 319 ? -7.29960  -19.46281 0.00058   1.000 10.18093  ? 324  ASP   A O    1 
ATOM   4774 C  CB   . ASP   B 2 319 ? -4.96239  -22.00867 -0.41503  1.000 11.59286  ? 324  ASP   A CB   1 
ATOM   4775 C  CG   . ASP   B 2 319 ? -5.48451  -22.43763 0.94794   1.000 13.47480  ? 324  ASP   A CG   1 
ATOM   4776 O  OD1  . ASP   B 2 319 ? -5.87465  -21.56161 1.75585   1.000 13.54848  ? 324  ASP   A OD1  1 
ATOM   4777 O  OD2  . ASP   B 2 319 ? -5.50845  -23.65962 1.20600   1.000 13.58234  ? 324  ASP   A OD2  1 
ATOM   4778 N  N    . LYS   B 2 320 ? -5.09664  -19.03566 0.04479   1.000 13.27374  ? 325  LYS   A N    1 
ATOM   4779 C  CA   . LYS   B 2 320 ? -5.17879  -17.72863 0.70271   1.000 12.47272  ? 325  LYS   A CA   1 
ATOM   4780 C  C    . LYS   B 2 320 ? -5.52395  -17.80257 2.19667   1.000 9.79659   ? 325  LYS   A C    1 
ATOM   4781 O  O    . LYS   B 2 320 ? -5.69209  -16.73454 2.82460   1.000 11.99573  ? 325  LYS   A O    1 
ATOM   4782 C  CB   . LYS   B 2 320 ? -6.20078  -16.79473 0.01454   1.000 14.49574  ? 325  LYS   A CB   1 
ATOM   4783 C  CG   . LYS   B 2 320 ? -5.81065  -16.43679 -1.41543  1.000 12.76598  ? 325  LYS   A CG   1 
ATOM   4784 C  CD   . LYS   B 2 320 ? -6.80065  -15.44689 -2.01659  1.000 12.94112  ? 325  LYS   A CD   1 
ATOM   4785 C  CE   . LYS   B 2 320 ? -6.43052  -15.05194 -3.44958  1.000 12.27386  ? 325  LYS   A CE   1 
ATOM   4786 N  NZ   . LYS   B 2 320 ? -7.38753  -14.05304 -4.00474  1.000 14.33374  ? 325  LYS   A NZ   1 
ATOM   4787 N  N    . THR   B 2 321 ? -5.62093  -18.98154 2.79373   1.000 13.04650  ? 326  THR   A N    1 
ATOM   4788 C  CA   . THR   B 2 321 ? -6.03508  -19.08849 4.17969   1.000 8.20092   ? 326  THR   A CA   1 
ATOM   4789 C  C    . THR   B 2 321 ? -4.91614  -19.60537 5.07284   1.000 11.44303  ? 326  THR   A C    1 
ATOM   4790 O  O    . THR   B 2 321 ? -3.93705  -20.21633 4.62998   1.000 13.53366  ? 326  THR   A O    1 
ATOM   4791 C  CB   . THR   B 2 321 ? -7.27103  -19.99856 4.32261   1.000 10.20240  ? 326  THR   A CB   1 
ATOM   4792 O  OG1  . THR   B 2 321 ? -6.92591  -21.34856 4.01672   1.000 10.47351  ? 326  THR   A OG1  1 
ATOM   4793 C  CG2  . THR   B 2 321 ? -8.39496  -19.54369 3.40546   1.000 16.43803  ? 326  THR   A CG2  1 
ATOM   4794 N  N    . ILE   B 2 322 ? -5.08729  -19.32930 6.35781   1.000 11.22138  ? 327  ILE   A N    1 
ATOM   4795 C  CA   . ILE   B 2 322 ? -4.20738  -19.78819 7.41593   1.000 10.78888  ? 327  ILE   A CA   1 
ATOM   4796 C  C    . ILE   B 2 322 ? -4.99340  -20.78619 8.25290   1.000 14.32805  ? 327  ILE   A C    1 
ATOM   4797 O  O    . ILE   B 2 322 ? -6.16245  -20.54525 8.56876   1.000 13.64247  ? 327  ILE   A O    1 
ATOM   4798 C  CB   . ILE   B 2 322 ? -3.73255  -18.59011 8.25991   1.000 12.90698  ? 327  ILE   A CB   1 
ATOM   4799 C  CG1  . ILE   B 2 322 ? -2.93152  -17.59110 7.39494   1.000 14.64341  ? 327  ILE   A CG1  1 
ATOM   4800 C  CG2  . ILE   B 2 322 ? -2.98865  -19.05599 9.49802   1.000 12.12444  ? 327  ILE   A CG2  1 
ATOM   4801 C  CD1  . ILE   B 2 322 ? -2.85968  -16.14507 7.99387   1.000 10.89819  ? 327  ILE   A CD1  1 
ATOM   4802 N  N    . LYS   B 2 323 ? -4.37536  -21.91313 8.59403   1.000 11.79021  ? 328  LYS   A N    1 
ATOM   4803 C  CA   . LYS   B 2 323 ? -5.03938  -22.91413 9.41501   1.000 9.06629   ? 328  LYS   A CA   1 
ATOM   4804 C  C    . LYS   B 2 323 ? -4.30351  -23.09901 10.73410  1.000 12.59645  ? 328  LYS   A C    1 
ATOM   4805 O  O    . LYS   B 2 323 ? -3.06653  -23.01892 10.79823  1.000 11.59390  ? 328  LYS   A O    1 
ATOM   4806 C  CB   . LYS   B 2 323 ? -5.19021  -24.24318 8.66207   1.000 9.58943   ? 328  LYS   A CB   1 
ATOM   4807 C  CG   . LYS   B 2 323 ? -6.23910  -24.11432 7.53995   1.000 8.34810   ? 328  LYS   A CG   1 
ATOM   4808 C  CD   . LYS   B 2 323 ? -6.30992  -25.28737 6.57801   1.000 11.51531  ? 328  LYS   A CD   1 
ATOM   4809 C  CE   . LYS   B 2 323 ? -7.29182  -24.96950 5.42788   1.000 12.26738  ? 328  LYS   A CE   1 
ATOM   4810 N  NZ   . LYS   B 2 323 ? -8.73185  -25.13558 5.81374   1.000 10.63952  ? 328  LYS   A NZ   1 
ATOM   4811 N  N    . LEU   B 2 324 ? -5.09361  -23.29600 11.78703  1.000 10.86322  ? 329  LEU   A N    1 
ATOM   4812 C  CA   . LEU   B 2 324 ? -4.60875  -23.49489 13.14409  1.000 12.25292  ? 329  LEU   A CA   1 
ATOM   4813 C  C    . LEU   B 2 324 ? -4.99970  -24.89690 13.57613  1.000 16.61071  ? 329  LEU   A C    1 
ATOM   4814 O  O    . LEU   B 2 324 ? -6.18167  -25.25298 13.53302  1.000 15.43276  ? 329  LEU   A O    1 
ATOM   4815 C  CB   . LEU   B 2 324 ? -5.19592  -22.45288 14.09797  1.000 15.60936  ? 329  LEU   A CB   1 
ATOM   4816 C  CG   . LEU   B 2 324 ? -4.63600  -21.03485 13.97695  1.000 17.27128  ? 329  LEU   A CG   1 
ATOM   4817 C  CD1  . LEU   B 2 324 ? -5.42316  -20.03985 14.84781  1.000 16.34849  ? 329  LEU   A CD1  1 
ATOM   4818 C  CD2  . LEU   B 2 324 ? -3.17804  -21.04273 14.37711  1.000 16.06511  ? 329  LEU   A CD2  1 
ATOM   4819 N  N    . TRP   B 2 325 ? -4.00569  -25.69381 13.97028  1.000 14.82465  ? 330  TRP   A N    1 
ATOM   4820 C  CA   . TRP   B 2 325 ? -4.19864  -27.07880 14.36733  1.000 12.77601  ? 330  TRP   A CA   1 
ATOM   4821 C  C    . TRP   B 2 325 ? -3.69778  -27.26269 15.79140  1.000 13.32719  ? 330  TRP   A C    1 
ATOM   4822 O  O    . TRP   B 2 325 ? -2.72687  -26.62460 16.20547  1.000 14.21990  ? 330  TRP   A O    1 
ATOM   4823 C  CB   . TRP   B 2 325 ? -3.44048  -28.04080 13.44947  1.000 10.32305  ? 330  TRP   A CB   1 
ATOM   4824 C  CG   . TRP   B 2 325 ? -3.43635  -27.65188 12.02245  1.000 12.00503  ? 330  TRP   A CG   1 
ATOM   4825 C  CD1  . TRP   B 2 325 ? -2.79436  -26.57887 11.45546  1.000 13.02067  ? 330  TRP   A CD1  1 
ATOM   4826 C  CD2  . TRP   B 2 325 ? -4.06919  -28.35398 10.95042  1.000 11.97121  ? 330  TRP   A CD2  1 
ATOM   4827 N  NE1  . TRP   B 2 325 ? -3.00721  -26.56696 10.09543  1.000 10.41842  ? 330  TRP   A NE1  1 
ATOM   4828 C  CE2  . TRP   B 2 325 ? -3.79011  -27.64403 9.76241   1.000 11.52944  ? 330  TRP   A CE2  1 
ATOM   4829 C  CE3  . TRP   B 2 325 ? -4.86410  -29.50404 10.88240  1.000 14.78872  ? 330  TRP   A CE3  1 
ATOM   4830 C  CZ2  . TRP   B 2 325 ? -4.27595  -28.04713 8.52038   1.000 15.92092  ? 330  TRP   A CZ2  1 
ATOM   4831 C  CZ3  . TRP   B 2 325 ? -5.34394  -29.90314 9.64537   1.000 18.49618  ? 330  TRP   A CZ3  1 
ATOM   4832 C  CH2  . TRP   B 2 325 ? -5.05187  -29.17618 8.48236   1.000 15.56559  ? 330  TRP   A CH2  1 
ATOM   4833 N  N    . LYS   B 2 326 ? -4.35980  -28.14869 16.53338  1.000 14.52864  ? 331  LYS   A N    1 
ATOM   4834 C  CA   . LYS   B 2 326 ? -4.03793  -28.39959 17.93142  1.000 17.83224  ? 331  LYS   A CA   1 
ATOM   4835 C  C    . LYS   B 2 326 ? -3.90486  -29.89757 18.16152  1.000 14.23750  ? 331  LYS   A C    1 
ATOM   4836 O  O    . LYS   B 2 326 ? -4.69975  -30.68165 17.64448  1.000 13.98594  ? 331  LYS   A O    1 
ATOM   4837 C  CB   . LYS   B 2 326 ? -5.11107  -27.81761 18.87728  1.000 19.05120  ? 331  LYS   A CB   1 
ATOM   4838 C  CG   . LYS   B 2 326 ? -4.72923  -27.89950 20.38032  1.000 17.84661  ? 331  LYS   A CG   1 
ATOM   4839 C  CD   . LYS   B 2 326 ? -5.87936  -27.45453 21.27817  1.000 31.91783  ? 331  LYS   A CD   1 
ATOM   4840 C  CE   . LYS   B 2 326 ? -5.44653  -27.24141 22.74321  1.000 23.55691  ? 331  LYS   A CE   1 
ATOM   4841 N  NZ   . LYS   B 2 326 ? -5.16052  -28.51836 23.44831  1.000 25.91808  ? 331  LYS   A NZ   1 
ATOM   4842 N  N    . SER   B 2 327 ? -2.90392  -30.29046 18.94665  1.000 14.77277  ? 332  SER   A N    1 
ATOM   4843 C  CA   . SER   B 2 327 ? -2.63685  -31.69542 19.22176  1.000 15.37348  ? 332  SER   A CA   1 
ATOM   4844 C  C    . SER   B 2 327 ? -2.51700  -31.92333 20.72478  1.000 19.46011  ? 332  SER   A C    1 
ATOM   4845 O  O    . SER   B 2 327 ? -2.11814  -31.02926 21.46878  1.000 14.33605  ? 332  SER   A O    1 
ATOM   4846 C  CB   . SER   B 2 327 ? -1.34975  -32.15938 18.52092  1.000 16.45508  ? 332  SER   A CB   1 
ATOM   4847 O  OG   . SER   B 2 327 ? -0.90872  -33.40632 19.02604  1.000 15.56086  ? 332  SER   A OG   1 
ATOM   4848 N  N    . ASP   B 2 328 ? -2.85097  -33.14433 21.16182  1.000 15.71993  ? 333  ASP   A N    1 
ATOM   4849 C  CA   . ASP   B 2 328 ? -2.76209  -33.49425 22.57385  1.000 18.84737  ? 333  ASP   A CA   1 
ATOM   4850 C  C    . ASP   B 2 328 ? -1.33712  -33.81613 23.02402  1.000 26.24330  ? 333  ASP   A C    1 
ATOM   4851 O  O    . ASP   B 2 328 ? -1.09325  -33.87304 24.23605  1.000 23.16500  ? 333  ASP   A O    1 
ATOM   4852 C  CB   . ASP   B 2 328 ? -3.69605  -34.67629 22.88081  1.000 16.65388  ? 333  ASP   A CB   1 
ATOM   4853 C  CG   . ASP   B 2 328 ? -5.18606  -34.30240 22.75663  1.000 18.60679  ? 333  ASP   A CG   1 
ATOM   4854 O  OD1  . ASP   B 2 328 ? -5.58618  -33.22240 23.24653  1.000 19.45903  ? 333  ASP   A OD1  1 
ATOM   4855 O  OD2  . ASP   B 2 328 ? -5.95694  -35.07648 22.15459  1.000 24.35718  ? 333  ASP   A OD2  1 
ATOM   4856 N  N    . CYS   B 2 329 ? -0.39901  -34.01712 22.09213  1.000 24.88874  ? 334  CYS   A N    1 
ATOM   4857 C  CA   . CYS   B 2 329 ? 1.01397   -34.27500 22.41929  1.000 22.32995  ? 334  CYS   A CA   1 
ATOM   4858 C  C    . CYS   B 2 329 ? 1.94906   -33.76200 21.32037  1.000 28.79016  ? 334  CYS   A C    1 
ATOM   4859 O  O    . CYS   B 2 329 ? 1.52311   -33.07608 20.38628  1.000 21.11500  ? 334  CYS   A O    1 
ATOM   4860 C  CB   . CYS   B 2 329 ? 1.26905   -35.77097 22.63741  1.000 15.08710  ? 334  CYS   A CB   1 
ATOM   4861 S  SG   . CYS   B 2 329 ? 0.96128   -36.82208 21.16443  1.000 29.78964  ? 334  CYS   A SG   1 
ATOM   4862 O  OXT  . CYS   B 2 329 ? 3.15707   -34.03492 21.33151  1.000 28.77105  ? 334  CYS   A OXT  1 
HETATM 4863 C  C10  . A1BAF C 3 .   ? 8.31500   -14.02600 -23.86700 1.000 13.57988  ? 1401 A1BAF B C10  1 
HETATM 4864 C  C11  . A1BAF C 3 .   ? 8.21900   -14.36500 -25.29900 1.000 18.69000  ? 1401 A1BAF B C11  1 
HETATM 4865 C  C12  . A1BAF C 3 .   ? 8.46200   -13.53700 -26.39900 1.000 18.05942  ? 1401 A1BAF B C12  1 
HETATM 4866 C  C13  . A1BAF C 3 .   ? 8.25400   -14.27600 -27.59000 1.000 18.00585  ? 1401 A1BAF B C13  1 
HETATM 4867 C  C14  . A1BAF C 3 .   ? 7.88400   -15.58400 -27.22500 1.000 16.18417  ? 1401 A1BAF B C14  1 
HETATM 4868 C  C15  . A1BAF C 3 .   ? 8.84200   -12.04600 -26.27700 1.000 14.01636  ? 1401 A1BAF B C15  1 
HETATM 4869 C  C16  . A1BAF C 3 .   ? 10.00600  -11.55700 -26.64700 1.000 14.62978  ? 1401 A1BAF B C16  1 
HETATM 4870 C  C17  . A1BAF C 3 .   ? 10.26600  -10.05300 -26.47900 1.000 19.41154  ? 1401 A1BAF B C17  1 
HETATM 4871 C  C18  . A1BAF C 3 .   ? 9.31400   -9.28800  -25.96700 1.000 19.87431  ? 1401 A1BAF B C18  1 
HETATM 4872 C  C19  . A1BAF C 3 .   ? 7.96900   -9.85900  -25.54600 1.000 13.86100  ? 1401 A1BAF B C19  1 
HETATM 4873 C  C20  . A1BAF C 3 .   ? 7.74800   -11.15000 -25.68800 1.000 17.11376  ? 1401 A1BAF B C20  1 
HETATM 4874 C  C21  . A1BAF C 3 .   ? 8.38100   -13.70500 -29.00900 1.000 18.91001  ? 1401 A1BAF B C21  1 
HETATM 4875 C  C22  . A1BAF C 3 .   ? 8.27900   -13.97600 -31.47200 1.000 16.75127  ? 1401 A1BAF B C22  1 
HETATM 4876 C  C23  . A1BAF C 3 .   ? 8.92000   -14.92900 -32.46000 1.000 20.79897  ? 1401 A1BAF B C23  1 
HETATM 4877 C  C24  . A1BAF C 3 .   ? 6.89100   -13.75000 -32.00900 1.000 15.13459  ? 1401 A1BAF B C24  1 
HETATM 4878 C  C25  . A1BAF C 3 .   ? 6.68000   -12.99100 -33.09000 1.000 11.99742  ? 1401 A1BAF B C25  1 
HETATM 4879 C  C26  . A1BAF C 3 .   ? 5.26200   -12.83000 -33.62200 1.000 13.13414  ? 1401 A1BAF B C26  1 
HETATM 4880 C  C01  . A1BAF C 3 .   ? 11.72800  -17.00300 2.10300   1.000 10.57504  ? 1401 A1BAF B C01  1 
HETATM 4881 C  C02  . A1BAF C 3 .   ? 10.98700  -16.68400 3.42200   1.000 9.59347   ? 1401 A1BAF B C02  1 
HETATM 4882 C  C03  . A1BAF C 3 .   ? 11.95000  -16.93400 4.59800   1.000 10.96525  ? 1401 A1BAF B C03  1 
HETATM 4883 C  C04  . A1BAF C 3 .   ? 9.04100   -17.19900 4.77100   1.000 10.50342  ? 1401 A1BAF B C04  1 
HETATM 4884 C  C05  . A1BAF C 3 .   ? 8.89100   -17.24400 2.35700   1.000 6.58709   ? 1401 A1BAF B C05  1 
HETATM 4885 C  C06  . A1BAF C 3 .   ? 7.61400   -18.10500 2.38100   1.000 13.27433  ? 1401 A1BAF B C06  1 
HETATM 4886 C  C07  . A1BAF C 3 .   ? 9.65200   -17.53700 1.04500   1.000 9.66219   ? 1401 A1BAF B C07  1 
HETATM 4887 C  C08  . A1BAF C 3 .   ? 8.22700   -14.25400 -21.30700 1.000 26.88937  ? 1401 A1BAF B C08  1 
HETATM 4888 C  C09  . A1BAF C 3 .   ? 8.12600   -14.73500 -22.71600 1.000 30.26931  ? 1401 A1BAF B C09  1 
HETATM 4889 C  C27  . A1BAF C 3 .   ? 4.26400   -13.45400 -33.01700 1.000 12.11875  ? 1401 A1BAF B C27  1 
HETATM 4890 C  C28  . A1BAF C 3 .   ? 4.52600   -14.33400 -31.78100 1.000 14.30391  ? 1401 A1BAF B C28  1 
HETATM 4891 C  C29  . A1BAF C 3 .   ? 5.74700   -14.47500 -31.31800 1.000 15.02436  ? 1401 A1BAF B C29  1 
HETATM 4892 C  C30  . A1BAF C 3 .   ? 10.36700  -15.10700 -31.99100 1.000 25.13673  ? 1401 A1BAF B C30  1 
HETATM 4893 C  C31  . A1BAF C 3 .   ? 13.19300  -17.62600 -1.82600  1.000 9.88822   ? 1401 A1BAF B C31  1 
HETATM 4894 C  C32  . A1BAF C 3 .   ? 12.67100  -17.56100 -0.59200  1.000 9.42975   ? 1401 A1BAF B C32  1 
HETATM 4895 C  C33  . A1BAF C 3 .   ? 11.44900  -16.80400 -0.32400  1.000 9.60324   ? 1401 A1BAF B C33  1 
HETATM 4896 C  C34  . A1BAF C 3 .   ? 10.76100  -16.16400 -1.37500  1.000 10.56511  ? 1401 A1BAF B C34  1 
HETATM 4897 C  C35  . A1BAF C 3 .   ? 11.37200  -16.23100 -2.79800  1.000 10.38461  ? 1401 A1BAF B C35  1 
HETATM 4898 C  C36  . A1BAF C 3 .   ? 12.50700  -16.91500 -2.97100  1.000 11.64387  ? 1401 A1BAF B C36  1 
HETATM 4899 C  C37  . A1BAF C 3 .   ? 13.08800  -17.07300 -4.41400  1.000 13.47045  ? 1401 A1BAF B C37  1 
HETATM 4900 C  C38  . A1BAF C 3 .   ? 8.33900   -15.73700 -2.01700  1.000 12.21259  ? 1401 A1BAF B C38  1 
HETATM 4901 C  C39  . A1BAF C 3 .   ? 7.25800   -14.66800 -1.99000  1.000 13.12413  ? 1401 A1BAF B C39  1 
HETATM 4902 C  C40  . A1BAF C 3 .   ? 7.74500   -13.34100 -2.31700  1.000 15.28414  ? 1401 A1BAF B C40  1 
HETATM 4903 C  C41  . A1BAF C 3 .   ? 5.51900   -12.42100 -2.12200  1.000 16.53586  ? 1401 A1BAF B C41  1 
HETATM 4904 C  C42  . A1BAF C 3 .   ? 4.98500   -13.74400 -1.80400  1.000 13.18329  ? 1401 A1BAF B C42  1 
HETATM 4905 C  C43  . A1BAF C 3 .   ? 5.83200   -14.84600 -1.75000  1.000 18.84781  ? 1401 A1BAF B C43  1 
HETATM 4906 C  C44  . A1BAF C 3 .   ? 12.19300  -17.32500 -5.34400  1.000 15.01689  ? 1401 A1BAF B C44  1 
HETATM 4907 C  C45  . A1BAF C 3 .   ? 12.63900  -17.53600 -6.76900  1.000 20.15656  ? 1401 A1BAF B C45  1 
HETATM 4908 C  C46  . A1BAF C 3 .   ? 13.91500  -17.50100 -7.07800  1.000 16.99504  ? 1401 A1BAF B C46  1 
HETATM 4909 C  C47  . A1BAF C 3 .   ? 14.94300  -17.24600 -5.98100  1.000 20.38107  ? 1401 A1BAF B C47  1 
HETATM 4910 C  C48  . A1BAF C 3 .   ? 14.55300  -17.06200 -4.73300  1.000 11.58544  ? 1401 A1BAF B C48  1 
HETATM 4911 C  C49  . A1BAF C 3 .   ? 11.54600  -17.79800 -7.81900  1.000 31.82834  ? 1401 A1BAF B C49  1 
HETATM 4912 C  C50  . A1BAF C 3 .   ? 9.32800   -18.78100 -8.30200  1.000 33.78500  ? 1401 A1BAF B C50  1 
HETATM 4913 C  C51  . A1BAF C 3 .   ? 8.02000   -19.03800 -7.54100  1.000 30.35045  ? 1401 A1BAF B C51  1 
HETATM 4914 C  C52  . A1BAF C 3 .   ? 7.64000   -17.08200 -6.16000  1.000 27.97730  ? 1401 A1BAF B C52  1 
HETATM 4915 C  C53  . A1BAF C 3 .   ? 6.36800   -16.40300 -5.63500  1.000 37.35264  ? 1401 A1BAF B C53  1 
HETATM 4916 C  C54  . A1BAF C 3 .   ? 6.60600   -14.05200 -5.52000  1.000 45.60580  ? 1401 A1BAF B C54  1 
HETATM 4917 C  C55  . A1BAF C 3 .   ? 6.19200   -12.70000 -6.13000  1.000 50.94111  ? 1401 A1BAF B C55  1 
HETATM 4918 C  C56  . A1BAF C 3 .   ? 8.08700   -11.55800 -7.14100  1.000 54.72930  ? 1401 A1BAF B C56  1 
HETATM 4919 C  C57  . A1BAF C 3 .   ? 9.24400   -12.26500 -6.41700  1.000 38.53899  ? 1401 A1BAF B C57  1 
HETATM 4920 C  C58  . A1BAF C 3 .   ? 10.51900  -14.29700 -6.48500  1.000 40.18313  ? 1401 A1BAF B C58  1 
HETATM 4921 C  C59  . A1BAF C 3 .   ? 11.84200  -13.79800 -7.08200  1.000 36.93605  ? 1401 A1BAF B C59  1 
HETATM 4922 C  C60  . A1BAF C 3 .   ? 11.47200  -14.38300 -9.38300  1.000 40.07125  ? 1401 A1BAF B C60  1 
HETATM 4923 C  C61  . A1BAF C 3 .   ? 11.01900  -13.71600 -10.66700 1.000 50.78174  ? 1401 A1BAF B C61  1 
HETATM 4924 C  C62  . A1BAF C 3 .   ? 11.53000  -11.91500 -12.06000 1.000 51.49391  ? 1401 A1BAF B C62  1 
HETATM 4925 C  C63  . A1BAF C 3 .   ? 12.20300  -12.51900 -13.31100 1.000 59.81332  ? 1401 A1BAF B C63  1 
HETATM 4926 C  C64  . A1BAF C 3 .   ? 12.30900  -10.61400 -14.76500 1.000 71.61040  ? 1401 A1BAF B C64  1 
HETATM 4927 C  C65  . A1BAF C 3 .   ? 11.27800  -9.47400  -14.70900 1.000 81.62626  ? 1401 A1BAF B C65  1 
HETATM 4928 C  C66  . A1BAF C 3 .   ? 9.58800   -10.15900 -16.23100 1.000 80.86802  ? 1401 A1BAF B C66  1 
HETATM 4929 C  C67  . A1BAF C 3 .   ? 9.25100   -10.11900 -17.72400 1.000 73.98213  ? 1401 A1BAF B C67  1 
HETATM 4930 C  C68  . A1BAF C 3 .   ? 9.91500   -11.20900 -19.75400 1.000 62.24919  ? 1401 A1BAF B C68  1 
HETATM 4931 C  C69  . A1BAF C 3 .   ? 8.97600   -12.42500 -19.76200 1.000 53.02195  ? 1401 A1BAF B C69  1 
HETATM 4932 C  C70  . A1BAF C 3 .   ? 5.31400   -16.26700 -1.44100  1.000 17.93214  ? 1401 A1BAF B C70  1 
HETATM 4933 F  F01  . A1BAF C 3 .   ? 10.97700  -12.34200 -27.18000 1.000 16.13774  ? 1401 A1BAF B F01  1 
HETATM 4934 F  F02  . A1BAF C 3 .   ? 2.99900   -13.31400 -33.48700 1.000 15.69560  ? 1401 A1BAF B F02  1 
HETATM 4935 F  F03  . A1BAF C 3 .   ? 15.43200  -16.81900 -3.73900  1.000 17.58084  ? 1401 A1BAF B F03  1 
HETATM 4936 F  F04  . A1BAF C 3 .   ? 4.05200   -16.20100 -0.95800  1.000 18.02829  ? 1401 A1BAF B F04  1 
HETATM 4937 F  F05  . A1BAF C 3 .   ? 5.33000   -16.99100 -2.61200  1.000 21.06092  ? 1401 A1BAF B F05  1 
HETATM 4938 F  F06  . A1BAF C 3 .   ? 6.11300   -16.86300 -0.51400  1.000 18.19767  ? 1401 A1BAF B F06  1 
HETATM 4939 N  N01  . A1BAF C 3 .   ? 10.87100  -16.74400 0.95500   1.000 11.60178  ? 1401 A1BAF B N01  1 
HETATM 4940 N  N02  . A1BAF C 3 .   ? 9.75900   -17.50400 3.52900   1.000 9.46516   ? 1401 A1BAF B N02  1 
HETATM 4941 N  N03  . A1BAF C 3 .   ? 7.85800   -15.64600 -25.80100 1.000 16.90242  ? 1401 A1BAF B N03  1 
HETATM 4942 N  N04  . A1BAF C 3 .   ? 8.17700   -14.57700 -30.16100 1.000 16.51364  ? 1401 A1BAF B N04  1 
HETATM 4943 N  N05  . A1BAF C 3 .   ? 10.76000  -16.40400 -31.50400 1.000 32.50519  ? 1401 A1BAF B N05  1 
HETATM 4944 N  N06  . A1BAF C 3 .   ? 9.55200   -15.32400 -1.35200  1.000 11.32893  ? 1401 A1BAF B N06  1 
HETATM 4945 N  N07  . A1BAF C 3 .   ? 6.85600   -12.22700 -2.36100  1.000 18.94119  ? 1401 A1BAF B N07  1 
HETATM 4946 N  N08  . A1BAF C 3 .   ? 10.45200  -18.52800 -7.40500  1.000 23.96096  ? 1401 A1BAF B N08  1 
HETATM 4947 N  N09  . A1BAF C 3 .   ? 8.87800   -13.02500 -21.10300 1.000 35.17829  ? 1401 A1BAF B N09  1 
HETATM 4948 O  O01  . A1BAF C 3 .   ? 7.73500   -14.92400 -20.36800 1.000 43.45098  ? 1401 A1BAF B O01  1 
HETATM 4949 O  O02  . A1BAF C 3 .   ? 8.59900   -12.55300 -29.16300 1.000 15.03364  ? 1401 A1BAF B O02  1 
HETATM 4950 O  O03  . A1BAF C 3 .   ? 11.10200  -14.16900 -32.01300 1.000 28.33166  ? 1401 A1BAF B O03  1 
HETATM 4951 O  O04  . A1BAF C 3 .   ? 8.24400   -16.77500 -2.58100  1.000 12.24487  ? 1401 A1BAF B O04  1 
HETATM 4952 O  O05  . A1BAF C 3 .   ? 4.69800   -11.29900 -2.17700  1.000 20.94417  ? 1401 A1BAF B O05  1 
HETATM 4953 O  O06  . A1BAF C 3 .   ? 11.63400  -17.35500 -8.93000  1.000 38.90331  ? 1401 A1BAF B O06  1 
HETATM 4954 O  O07  . A1BAF C 3 .   ? 7.27700   -17.84800 -7.30300  1.000 31.86460  ? 1401 A1BAF B O07  1 
HETATM 4955 O  O08  . A1BAF C 3 .   ? 6.11000   -15.15500 -6.26500  1.000 48.98065  ? 1401 A1BAF B O08  1 
HETATM 4956 O  O09  . A1BAF C 3 .   ? 6.92500   -12.37400 -7.30500  1.000 60.42715  ? 1401 A1BAF B O09  1 
HETATM 4957 O  O10  . A1BAF C 3 .   ? 9.42000   -13.55200 -6.99000  1.000 49.70861  ? 1401 A1BAF B O10  1 
HETATM 4958 O  O11  . A1BAF C 3 .   ? 11.63500  -13.35500 -8.41100  1.000 42.85091  ? 1401 A1BAF B O11  1 
HETATM 4959 O  O12  . A1BAF C 3 .   ? 11.92500  -12.65900 -10.93500 1.000 43.11237  ? 1401 A1BAF B O12  1 
HETATM 4960 O  O13  . A1BAF C 3 .   ? 11.71200  -11.88300 -14.48400 1.000 71.75454  ? 1401 A1BAF B O13  1 
HETATM 4961 O  O14  . A1BAF C 3 .   ? 10.66500  -9.27300  -15.97300 1.000 91.21254  ? 1401 A1BAF B O14  1 
HETATM 4962 O  O15  . A1BAF C 3 .   ? 10.24600  -10.86000 -18.42000 1.000 75.78443  ? 1401 A1BAF B O15  1 
HETATM 4963 CL CL01 . A1BAF C 3 .   ? 9.59300   -7.55300  -25.76300 1.000 25.65660  ? 1401 A1BAF B CL01 1 
HETATM 4964 CL CL02 . A1BAF C 3 .   ? 3.19000   -15.17400 -30.95800 1.000 24.90438  ? 1401 A1BAF B CL02 1 
HETATM 4965 H  H17  . A1BAF C 3 .   ? 9.11100   -13.30100 -23.71900 1.000 16.28300  ? 1401 A1BAF B H17  1 
HETATM 4966 H  H18  . A1BAF C 3 .   ? 7.65500   -16.39900 -27.90700 1.000 19.40815  ? 1401 A1BAF B H18  1 
HETATM 4967 H  H20  . A1BAF C 3 .   ? 11.22000  -9.62200  -26.77500 1.000 23.28099  ? 1401 A1BAF B H20  1 
HETATM 4968 H  H21  . A1BAF C 3 .   ? 7.20100   -9.21100  -25.12800 1.000 16.62034  ? 1401 A1BAF B H21  1 
HETATM 4969 H  H22  . A1BAF C 3 .   ? 6.79200   -11.57700 -25.39200 1.000 20.52366  ? 1401 A1BAF B H22  1 
HETATM 4970 H  H24  . A1BAF C 3 .   ? 8.83200   -13.03800 -31.42600 1.000 20.08866  ? 1401 A1BAF B H24  1 
HETATM 4971 H  H26  . A1BAF C 3 .   ? 8.90000   -14.50100 -33.46200 1.000 24.94590  ? 1401 A1BAF B H26  1 
HETATM 4972 H  H25  . A1BAF C 3 .   ? 8.40100   -15.88700 -32.44900 1.000 24.94590  ? 1401 A1BAF B H25  1 
HETATM 4973 H  H27  . A1BAF C 3 .   ? 7.51100   -12.48400 -33.57700 1.000 14.38405  ? 1401 A1BAF B H27  1 
HETATM 4974 H  H28  . A1BAF C 3 .   ? 5.07200   -12.21300 -34.49800 1.000 15.74811  ? 1401 A1BAF B H28  1 
HETATM 4975 H  H02  . A1BAF C 3 .   ? 12.61900  -16.37800 2.03300   1.000 12.67718  ? 1401 A1BAF B H02  1 
HETATM 4976 H  H01  . A1BAF C 3 .   ? 12.02000  -18.05300 2.10200   1.000 12.67718  ? 1401 A1BAF B H01  1 
HETATM 4977 H  H03  . A1BAF C 3 .   ? 10.70200  -15.63100 3.41500   1.000 11.49930  ? 1401 A1BAF B H03  1 
HETATM 4978 H  H05  . A1BAF C 3 .   ? 11.98100  -18.00000 4.82200   1.000 13.14544  ? 1401 A1BAF B H05  1 
HETATM 4979 H  H04  . A1BAF C 3 .   ? 11.60200  -16.38900 5.47400   1.000 13.14544  ? 1401 A1BAF B H04  1 
HETATM 4980 H  H06  . A1BAF C 3 .   ? 12.94800  -16.59100 4.32900   1.000 13.14544  ? 1401 A1BAF B H06  1 
HETATM 4981 H  H09  . A1BAF C 3 .   ? 9.62800   -17.54000 5.62300   1.000 12.59125  ? 1401 A1BAF B H09  1 
HETATM 4982 H  H07  . A1BAF C 3 .   ? 8.07800   -17.70700 4.76800   1.000 12.59125  ? 1401 A1BAF B H07  1 
HETATM 4983 H  H08  . A1BAF C 3 .   ? 8.88400   -16.12300 4.84500   1.000 12.59125  ? 1401 A1BAF B H08  1 
HETATM 4984 H  H10  . A1BAF C 3 .   ? 8.60600   -16.19100 2.36400   1.000 7.89165   ? 1401 A1BAF B H10  1 
HETATM 4985 H  H12  . A1BAF C 3 .   ? 7.77000   -18.96900 3.02600   1.000 15.91633  ? 1401 A1BAF B H12  1 
HETATM 4986 H  H13  . A1BAF C 3 .   ? 7.38500   -18.44200 1.37200   1.000 15.91633  ? 1401 A1BAF B H13  1 
HETATM 4987 H  H11  . A1BAF C 3 .   ? 6.78400   -17.51200 2.76300   1.000 15.91633  ? 1401 A1BAF B H11  1 
HETATM 4988 H  H15  . A1BAF C 3 .   ? 9.91300   -18.59600 1.01300   1.000 11.58177  ? 1401 A1BAF B H15  1 
HETATM 4989 H  H14  . A1BAF C 3 .   ? 9.01000   -17.29800 0.20100   1.000 11.58177  ? 1401 A1BAF B H14  1 
HETATM 4990 H  H16  . A1BAF C 3 .   ? 8.60900   -15.70600 -22.80400 1.000 36.31031  ? 1401 A1BAF B H16  1 
HETATM 4991 H  H29  . A1BAF C 3 .   ? 5.93600   -15.09500 -30.44600 1.000 18.01637  ? 1401 A1BAF B H29  1 
HETATM 4992 H  H32  . A1BAF C 3 .   ? 14.11000  -18.18500 -2.00200  1.000 11.85301  ? 1401 A1BAF B H32  1 
HETATM 4993 H  H33  . A1BAF C 3 .   ? 13.17000  -18.07500 0.22600   1.000 11.30284  ? 1401 A1BAF B H33  1 
HETATM 4994 H  H34  . A1BAF C 3 .   ? 10.77900  -15.93800 -3.65700  1.000 12.44867  ? 1401 A1BAF B H34  1 
HETATM 4995 H  H36  . A1BAF C 3 .   ? 8.80500   -13.19000 -2.50600  1.000 18.32811  ? 1401 A1BAF B H36  1 
HETATM 4996 H  H38  . A1BAF C 3 .   ? 3.91900   -13.86900 -1.62200  1.000 15.80709  ? 1401 A1BAF B H38  1 
HETATM 4997 H  H39  . A1BAF C 3 .   ? 11.13800  -17.35500 -5.09200  1.000 18.00741  ? 1401 A1BAF B H39  1 
HETATM 4998 H  H40  . A1BAF C 3 .   ? 14.23600  -17.65300 -8.10700  1.000 20.38119  ? 1401 A1BAF B H40  1 
HETATM 4999 H  H41  . A1BAF C 3 .   ? 16.00300  -17.22800 -6.22600  1.000 24.44442  ? 1401 A1BAF B H41  1 
HETATM 5000 H  H44  . A1BAF C 3 .   ? 9.55600   -19.65200 -8.91600  1.000 40.52914  ? 1401 A1BAF B H44  1 
HETATM 5001 H  H43  . A1BAF C 3 .   ? 9.19400   -17.91800 -8.95100  1.000 40.52914  ? 1401 A1BAF B H43  1 
HETATM 5002 H  H46  . A1BAF C 3 .   ? 8.25600   -19.50100 -6.58400  1.000 36.40767  ? 1401 A1BAF B H46  1 
HETATM 5003 H  H45  . A1BAF C 3 .   ? 7.40500   -19.72500 -8.12200  1.000 36.40767  ? 1401 A1BAF B H45  1 
HETATM 5004 H  H47  . A1BAF C 3 .   ? 8.05400   -17.73500 -5.39300  1.000 33.55990  ? 1401 A1BAF B H47  1 
HETATM 5005 H  H48  . A1BAF C 3 .   ? 8.37100   -16.33000 -6.43800  1.000 33.55990  ? 1401 A1BAF B H48  1 
HETATM 5006 H  H49  . A1BAF C 3 .   ? 6.47400   -16.24000 -4.56800  1.000 44.81031  ? 1401 A1BAF B H49  1 
HETATM 5007 H  H50  . A1BAF C 3 .   ? 5.52000   -17.06500 -5.80700  1.000 44.81031  ? 1401 A1BAF B H50  1 
HETATM 5008 H  H52  . A1BAF C 3 .   ? 6.22300   -14.11200 -4.50600  1.000 54.71410  ? 1401 A1BAF B H52  1 
HETATM 5009 H  H51  . A1BAF C 3 .   ? 7.68900   -14.10700 -5.49000  1.000 54.71410  ? 1401 A1BAF B H51  1 
HETATM 5010 H  H53  . A1BAF C 3 .   ? 6.35200   -11.91900 -5.39000  1.000 61.11648  ? 1401 A1BAF B H53  1 
HETATM 5011 H  H54  . A1BAF C 3 .   ? 5.13100   -12.73700 -6.37800  1.000 61.11648  ? 1401 A1BAF B H54  1 
HETATM 5012 H  H56  . A1BAF C 3 .   ? 8.43300   -11.24500 -8.12500  1.000 65.66230  ? 1401 A1BAF B H56  1 
HETATM 5013 H  H55  . A1BAF C 3 .   ? 7.81100   -10.67200 -6.57100  1.000 65.66230  ? 1401 A1BAF B H55  1 
HETATM 5014 H  H58  . A1BAF C 3 .   ? 9.00700   -12.36500 -5.36100  1.000 46.23393  ? 1401 A1BAF B H58  1 
HETATM 5015 H  H57  . A1BAF C 3 .   ? 10.15800  -11.68400 -6.53400  1.000 46.23393  ? 1401 A1BAF B H57  1 
HETATM 5016 H  H59  . A1BAF C 3 .   ? 10.55400  -14.19300 -5.40200  1.000 48.20689  ? 1401 A1BAF B H59  1 
HETATM 5017 H  H60  . A1BAF C 3 .   ? 10.38600  -15.34400 -6.73800  1.000 48.20689  ? 1401 A1BAF B H60  1 
HETATM 5018 H  H61  . A1BAF C 3 .   ? 12.56700  -14.60800 -7.08100  1.000 44.31039  ? 1401 A1BAF B H61  1 
HETATM 5019 H  H62  . A1BAF C 3 .   ? 12.22200  -12.97200 -6.48000  1.000 44.31039  ? 1401 A1BAF B H62  1 
HETATM 5020 H  H64  . A1BAF C 3 .   ? 12.42000  -14.89500 -9.54500  1.000 48.07264  ? 1401 A1BAF B H64  1 
HETATM 5021 H  H63  . A1BAF C 3 .   ? 10.72000  -15.09200 -9.04900  1.000 48.07264  ? 1401 A1BAF B H63  1 
HETATM 5022 H  H65  . A1BAF C 3 .   ? 10.01200  -13.31900 -10.54300 1.000 60.92522  ? 1401 A1BAF B H65  1 
HETATM 5023 H  H66  . A1BAF C 3 .   ? 11.03600  -14.43500 -11.48400 1.000 60.92522  ? 1401 A1BAF B H66  1 
HETATM 5024 H  H68  . A1BAF C 3 .   ? 10.44700  -11.96200 -12.16800 1.000 61.77984  ? 1401 A1BAF B H68  1 
HETATM 5025 H  H67  . A1BAF C 3 .   ? 11.84200  -10.87800 -11.94100 1.000 61.77984  ? 1401 A1BAF B H67  1 
HETATM 5026 H  H70  . A1BAF C 3 .   ? 11.98400  -13.58500 -13.36000 1.000 71.76312  ? 1401 A1BAF B H70  1 
HETATM 5027 H  H69  . A1BAF C 3 .   ? 13.28100  -12.37500 -13.24600 1.000 71.76312  ? 1401 A1BAF B H69  1 
HETATM 5028 H  H72  . A1BAF C 3 .   ? 13.09200  -10.42000 -14.03300 1.000 85.91961  ? 1401 A1BAF B H72  1 
HETATM 5029 H  H71  . A1BAF C 3 .   ? 12.75200  -10.64300 -15.76000 1.000 85.91961  ? 1401 A1BAF B H71  1 
HETATM 5030 H  H74  . A1BAF C 3 .   ? 11.77900  -8.55500  -14.40500 1.000 97.93866  ? 1401 A1BAF B H74  1 
HETATM 5031 H  H73  . A1BAF C 3 .   ? 10.51200  -9.72200  -13.97700 1.000 97.93866  ? 1401 A1BAF B H73  1 
HETATM 5032 H  H76  . A1BAF C 3 .   ? 9.87300   -11.17000 -15.95000 1.000 97.02876  ? 1401 A1BAF B H76  1 
HETATM 5033 H  H75  . A1BAF C 3 .   ? 8.71700   -9.85200  -15.65200 1.000 97.02876  ? 1401 A1BAF B H75  1 
HETATM 5034 H  H78  . A1BAF C 3 .   ? 9.24800   -9.08700  -18.07400 1.000 88.76569  ? 1401 A1BAF B H78  1 
HETATM 5035 H  H77  . A1BAF C 3 .   ? 8.27300   -10.56700 -17.89300 1.000 88.76569  ? 1401 A1BAF B H77  1 
HETATM 5036 H  H79  . A1BAF C 3 .   ? 9.41900   -10.36700 -20.23500 1.000 74.68617  ? 1401 A1BAF B H79  1 
HETATM 5037 H  H80  . A1BAF C 3 .   ? 10.82600  -11.45200 -20.30000 1.000 74.68617  ? 1401 A1BAF B H80  1 
HETATM 5038 H  H82  . A1BAF C 3 .   ? 9.35600   -13.17200 -19.06500 1.000 63.61348  ? 1401 A1BAF B H82  1 
HETATM 5039 H  H81  . A1BAF C 3 .   ? 7.98400   -12.11000 -19.44000 1.000 63.61348  ? 1401 A1BAF B H81  1 
HETATM 5040 H  H19  . A1BAF C 3 .   ? 7.62800   -16.45400 -25.24900 1.000 20.27004  ? 1401 A1BAF B H19  1 
HETATM 5041 H  H23  . A1BAF C 3 .   ? 8.25800   -15.57400 -30.05700 1.000 19.80351  ? 1401 A1BAF B H23  1 
HETATM 5042 H  H30  . A1BAF C 3 .   ? 10.17500  -17.20400 -31.67500 1.000 38.99337  ? 1401 A1BAF B H30  1 
HETATM 5043 H  H31  . A1BAF C 3 .   ? 11.60600  -16.50500 -30.96900 1.000 38.99337  ? 1401 A1BAF B H31  1 
HETATM 5044 H  H35  . A1BAF C 3 .   ? 9.57100   -14.44500 -0.86300  1.000 13.58185  ? 1401 A1BAF B H35  1 
HETATM 5045 H  H37  . A1BAF C 3 .   ? 7.20300   -11.30900 -2.58300  1.000 22.71657  ? 1401 A1BAF B H37  1 
HETATM 5046 H  H42  . A1BAF C 3 .   ? 10.43200  -18.90100 -6.47200  1.000 28.74029  ? 1401 A1BAF B H42  1 
HETATM 5047 H  H83  . A1BAF C 3 .   ? 9.28500   -12.54700 -21.88700 1.000 42.20109  ? 1401 A1BAF B H83  1 
HETATM 5048 O  O    . HOH   D 4 .   ? -2.16700  -13.17000 -20.24100 1.000 51.45703  ? 1501 HOH   B O    1 
HETATM 5049 O  O    . HOH   D 4 .   ? 16.98200  -26.99600 -16.38200 1.000 7.31911   ? 1502 HOH   B O    1 
HETATM 5050 O  O    . HOH   D 4 .   ? -2.45400  -28.28000 -16.35800 1.000 48.47910  ? 1503 HOH   B O    1 
HETATM 5051 O  O    . HOH   D 4 .   ? -5.90400  -20.60000 -44.31000 1.000 44.77022  ? 1504 HOH   B O    1 
HETATM 5052 O  O    . HOH   D 4 .   ? 28.80800  -27.91200 -29.31800 1.000 36.11292  ? 1505 HOH   B O    1 
HETATM 5053 O  O    . HOH   D 4 .   ? 10.46400  5.04200   -29.95900 1.000 16.05613  ? 1506 HOH   B O    1 
HETATM 5054 O  O    . HOH   D 4 .   ? -7.81600  -24.93400 -23.48000 1.000 28.74613  ? 1507 HOH   B O    1 
HETATM 5055 O  O    . HOH   D 4 .   ? 1.03400   -35.78500 -35.48100 1.000 16.36032  ? 1508 HOH   B O    1 
HETATM 5056 O  O    . HOH   D 4 .   ? 10.09500  -18.66400 -32.09200 1.000 27.86137  ? 1509 HOH   B O    1 
HETATM 5057 O  O    . HOH   D 4 .   ? -9.56000  -18.94000 -17.70600 1.000 40.73848  ? 1510 HOH   B O    1 
HETATM 5058 O  O    . HOH   D 4 .   ? 14.51900  -13.29900 -20.29600 1.000 26.01780  ? 1511 HOH   B O    1 
HETATM 5059 O  O    . HOH   D 4 .   ? 13.26900  -27.85700 -39.08200 1.000 45.16219  ? 1512 HOH   B O    1 
HETATM 5060 O  O    . HOH   D 4 .   ? 24.16000  -15.40400 -9.87900  1.000 1.17200   ? 1513 HOH   B O    1 
HETATM 5061 O  O    . HOH   D 4 .   ? 5.17800   -3.33900  -14.57600 1.000 39.64644  ? 1514 HOH   B O    1 
HETATM 5062 O  O    . HOH   D 4 .   ? -7.00300  -9.77300  -34.28900 1.000 45.56240  ? 1515 HOH   B O    1 
HETATM 5063 O  O    . HOH   D 4 .   ? 19.07900  -16.71000 -36.89700 1.000 17.75388  ? 1516 HOH   B O    1 
HETATM 5064 O  O    . HOH   D 4 .   ? 5.90000   4.35400   -31.75500 1.000 11.51866  ? 1517 HOH   B O    1 
HETATM 5065 O  O    . HOH   D 4 .   ? 6.446     10.794    -25.618   1.000 27.60838  ? 1518 HOH   B O    1 
HETATM 5066 O  O    . HOH   D 4 .   ? 27.94500  1.04300   -38.71500 1.000 21.81551  ? 1519 HOH   B O    1 
HETATM 5067 O  O    . HOH   D 4 .   ? 2.58300   3.64400   -30.17000 1.000 11.18442  ? 1520 HOH   B O    1 
HETATM 5068 O  O    . HOH   D 4 .   ? 6.01300   -29.13400 -16.68100 1.000 34.26490  ? 1521 HOH   B O    1 
HETATM 5069 O  O    . HOH   D 4 .   ? 14.37500  0.39700   -30.16700 1.000 24.43279  ? 1522 HOH   B O    1 
HETATM 5070 O  O    . HOH   D 4 .   ? 13.30300  -17.40600 -32.72600 1.000 25.30944  ? 1523 HOH   B O    1 
HETATM 5071 O  O    . HOH   D 4 .   ? 8.91800   9.49600   -46.07500 1.000 21.31918  ? 1524 HOH   B O    1 
HETATM 5072 O  O    . HOH   D 4 .   ? 21.73700  -20.22200 -12.30600 1.000 27.32741  ? 1525 HOH   B O    1 
HETATM 5073 O  O    . HOH   D 4 .   ? 28.15900  -3.55700  -37.63300 1.000 25.36115  ? 1526 HOH   B O    1 
HETATM 5074 O  O    . HOH   D 4 .   ? 2.96200   -10.30500 -22.20400 1.000 20.70207  ? 1527 HOH   B O    1 
HETATM 5075 O  O    . HOH   D 4 .   ? 23.70000  12.53700  -19.83200 1.000 33.12953  ? 1528 HOH   B O    1 
HETATM 5076 O  O    . HOH   D 4 .   ? 12.79000  -35.68600 -21.19400 1.000 26.49203  ? 1529 HOH   B O    1 
HETATM 5077 O  O    . HOH   D 4 .   ? 16.26700  -8.45200  -44.97600 1.000 20.19121  ? 1530 HOH   B O    1 
HETATM 5078 O  O    . HOH   D 4 .   ? 7.73700   -17.88600 -24.25500 1.000 17.39171  ? 1531 HOH   B O    1 
HETATM 5079 O  O    . HOH   D 4 .   ? 4.989     -36.083   -27.105   1.000 20.01990  ? 1532 HOH   B O    1 
HETATM 5080 O  O    . HOH   D 4 .   ? 7.83200   11.99500  -33.72100 1.000 30.59658  ? 1533 HOH   B O    1 
HETATM 5081 O  O    . HOH   D 4 .   ? 10.53000  -20.02300 3.72000   1.000 8.80376   ? 1534 HOH   B O    1 
HETATM 5082 O  O    . HOH   D 4 .   ? 16.75700  -14.96100 -26.75000 1.000 29.68812  ? 1535 HOH   B O    1 
HETATM 5083 O  O    . HOH   D 4 .   ? -2.80600  -5.01000  -30.98000 1.000 15.24684  ? 1536 HOH   B O    1 
HETATM 5084 O  O    . HOH   D 4 .   ? 20.04300  -19.20600 -16.24600 1.000 14.74499  ? 1537 HOH   B O    1 
HETATM 5085 O  O    . HOH   D 4 .   ? 13.27800  -7.79800  -31.52200 1.000 15.95351  ? 1538 HOH   B O    1 
HETATM 5086 O  O    . HOH   D 4 .   ? 13.62400  -1.13900  -20.01100 1.000 24.81759  ? 1539 HOH   B O    1 
HETATM 5087 O  O    . HOH   D 4 .   ? 18.05000  3.40500   -23.44400 1.000 18.32144  ? 1540 HOH   B O    1 
HETATM 5088 O  O    . HOH   D 4 .   ? 18.69600  -12.35100 -35.61700 1.000 14.79862  ? 1541 HOH   B O    1 
HETATM 5089 O  O    . HOH   D 4 .   ? -3.02500  -10.69200 -31.21700 1.000 26.47656  ? 1542 HOH   B O    1 
HETATM 5090 O  O    . HOH   D 4 .   ? 14.16900  -1.86900  -30.19600 1.000 14.07521  ? 1543 HOH   B O    1 
HETATM 5091 O  O    . HOH   D 4 .   ? 10.06000  -4.23800  -27.57500 1.000 11.62343  ? 1544 HOH   B O    1 
HETATM 5092 O  O    . HOH   D 4 .   ? 12.08700  12.27200  -33.02900 1.000 29.85346  ? 1545 HOH   B O    1 
HETATM 5093 O  O    . HOH   D 4 .   ? -0.064    6.456     -28.292   1.000 17.02969  ? 1546 HOH   B O    1 
HETATM 5094 O  O    . HOH   D 4 .   ? 7.21100   -2.86300  -32.99700 1.000 11.32959  ? 1547 HOH   B O    1 
HETATM 5095 O  O    . HOH   D 4 .   ? 13.66700  9.06700   -20.83200 1.000 31.69165  ? 1548 HOH   B O    1 
HETATM 5096 O  O    . HOH   D 4 .   ? 33.65700  -21.36200 -25.88800 1.000 23.78693  ? 1549 HOH   B O    1 
HETATM 5097 O  O    . HOH   D 4 .   ? 28.69000  -1.95700  -20.26100 1.000 30.46986  ? 1550 HOH   B O    1 
HETATM 5098 O  O    . HOH   D 4 .   ? 23.97500  -26.98700 -18.82600 1.000 23.34654  ? 1551 HOH   B O    1 
HETATM 5099 O  O    . HOH   D 4 .   ? 10.71600  -29.79900 -18.92300 1.000 28.05982  ? 1552 HOH   B O    1 
HETATM 5100 O  O    . HOH   D 4 .   ? 32.85300  -28.24500 -24.59700 1.000 30.67832  ? 1553 HOH   B O    1 
HETATM 5101 O  O    . HOH   D 4 .   ? 24.27400  -32.14000 -32.39400 1.000 52.51613  ? 1554 HOH   B O    1 
HETATM 5102 O  O    . HOH   D 4 .   ? 16.39600  -13.92600 -31.22000 1.000 32.15258  ? 1555 HOH   B O    1 
HETATM 5103 O  O    . HOH   D 4 .   ? 30.83600  -4.51600  -33.56100 1.000 24.30348  ? 1556 HOH   B O    1 
HETATM 5104 O  O    . HOH   D 4 .   ? 27.57100  -9.03300  -38.87200 1.000 30.76762  ? 1557 HOH   B O    1 
HETATM 5105 O  O    . HOH   D 4 .   ? 4.63800   -17.84500 -43.79600 1.000 29.14846  ? 1558 HOH   B O    1 
HETATM 5106 O  O    . HOH   D 4 .   ? -2.58900  -12.02700 -28.69500 1.000 28.77754  ? 1559 HOH   B O    1 
HETATM 5107 O  O    . HOH   D 4 .   ? 6.35100   4.13100   -29.06300 1.000 12.43238  ? 1560 HOH   B O    1 
HETATM 5108 O  O    . HOH   D 4 .   ? 19.40600  -8.61600  -34.48600 1.000 8.89611   ? 1561 HOH   B O    1 
HETATM 5109 O  O    . HOH   D 4 .   ? 18.91700  -7.82100  -27.87800 1.000 10.25040  ? 1562 HOH   B O    1 
HETATM 5110 O  O    . HOH   D 4 .   ? 14.61300  -1.73300  -42.01600 1.000 23.58925  ? 1563 HOH   B O    1 
HETATM 5111 O  O    . HOH   D 4 .   ? 11.55100  -18.28400 -29.32600 1.000 13.66747  ? 1564 HOH   B O    1 
HETATM 5112 O  O    . HOH   D 4 .   ? 0.72500   6.50700   -35.93100 1.000 18.04341  ? 1565 HOH   B O    1 
HETATM 5113 O  O    . HOH   D 4 .   ? 7.98500   3.05500   -20.34100 1.000 17.45139  ? 1566 HOH   B O    1 
HETATM 5114 O  O    . HOH   D 4 .   ? -0.62100  -5.74400  -23.77400 1.000 31.34457  ? 1567 HOH   B O    1 
HETATM 5115 O  O    . HOH   D 4 .   ? 14.77600  -9.12800  -35.20800 1.000 16.01558  ? 1568 HOH   B O    1 
HETATM 5116 O  O    . HOH   D 4 .   ? 27.564    -17.261   -16.993   1.000 23.25543  ? 1569 HOH   B O    1 
HETATM 5117 O  O    . HOH   D 4 .   ? 14.90600  -36.99000 -24.65100 1.000 23.00142  ? 1570 HOH   B O    1 
HETATM 5118 O  O    . HOH   D 4 .   ? -2.01200  -1.12900  -24.97800 1.000 28.97267  ? 1571 HOH   B O    1 
HETATM 5119 O  O    . HOH   D 4 .   ? 17.69700  -11.95200 -12.66600 1.000 20.08017  ? 1572 HOH   B O    1 
HETATM 5120 O  O    . HOH   D 4 .   ? 14.72800  -5.70900  -36.27800 1.000 13.66499  ? 1573 HOH   B O    1 
HETATM 5121 O  O    . HOH   D 4 .   ? 2.69000   6.32400   -46.51000 1.000 17.85388  ? 1574 HOH   B O    1 
HETATM 5122 O  O    . HOH   D 4 .   ? 19.23500  3.50100   -26.86600 1.000 16.66667  ? 1575 HOH   B O    1 
HETATM 5123 O  O    . HOH   D 4 .   ? 11.74400  -21.66800 -36.96900 1.000 26.61069  ? 1576 HOH   B O    1 
HETATM 5124 O  O    . HOH   D 4 .   ? -4.58900  -1.76300  -37.78900 1.000 22.50970  ? 1577 HOH   B O    1 
HETATM 5125 O  O    . HOH   D 4 .   ? 14.734    -2.420    -49.806   1.000 30.44890  ? 1578 HOH   B O    1 
HETATM 5126 O  O    . HOH   D 4 .   ? 10.61500  7.70500   -20.15600 1.000 27.42195  ? 1579 HOH   B O    1 
HETATM 5127 O  O    . HOH   D 4 .   ? 14.64100  -4.53500  -21.69100 1.000 15.06891  ? 1580 HOH   B O    1 
HETATM 5128 O  O    . HOH   D 4 .   ? 25.37500  -9.48700  -19.18700 1.000 21.95005  ? 1581 HOH   B O    1 
HETATM 5129 O  O    . HOH   D 4 .   ? -0.469    3.909     -30.412   1.000 21.42369  ? 1582 HOH   B O    1 
HETATM 5130 O  O    . HOH   D 4 .   ? 9.50600   15.55900  -31.93100 1.000 33.49492  ? 1583 HOH   B O    1 
HETATM 5131 O  O    . HOH   D 4 .   ? 19.48500  -8.56700  -15.83500 1.000 20.65242  ? 1584 HOH   B O    1 
HETATM 5132 O  O    . HOH   D 4 .   ? 31.18900  -2.24100  -23.85500 1.000 27.57915  ? 1585 HOH   B O    1 
HETATM 5133 O  O    . HOH   D 4 .   ? 4.24100   -3.63000  -32.50500 1.000 25.77062  ? 1586 HOH   B O    1 
HETATM 5134 O  O    . HOH   D 4 .   ? 14.05200  2.32000   -17.52200 1.000 26.66594  ? 1587 HOH   B O    1 
HETATM 5135 O  O    . HOH   D 4 .   ? 1.82200   -35.75300 -33.00100 1.000 22.38375  ? 1588 HOH   B O    1 
HETATM 5136 O  O    . HOH   D 4 .   ? 19.67300  -2.93900  -44.46800 1.000 22.43507  ? 1589 HOH   B O    1 
HETATM 5137 O  O    . HOH   D 4 .   ? 8.19300   5.79700   -32.24600 1.000 11.21910  ? 1590 HOH   B O    1 
HETATM 5138 O  O    . HOH   D 4 .   ? 26.45400  -2.42100  -19.23000 1.000 27.38978  ? 1591 HOH   B O    1 
HETATM 5139 O  O    . HOH   D 4 .   ? 8.37700   3.01800   -48.16000 1.000 30.82731  ? 1592 HOH   B O    1 
HETATM 5140 O  O    . HOH   D 4 .   ? -1.97100  -15.00200 -44.11800 1.000 31.83611  ? 1593 HOH   B O    1 
HETATM 5141 O  O    . HOH   D 4 .   ? 31.08000  0.45400   -25.72000 1.000 22.59879  ? 1594 HOH   B O    1 
HETATM 5142 O  O    . HOH   D 4 .   ? 24.24100  -18.93700 -39.32100 1.000 22.35338  ? 1595 HOH   B O    1 
HETATM 5143 O  O    . HOH   D 4 .   ? 19.61200  5.21900   -24.94700 1.000 22.94942  ? 1596 HOH   B O    1 
HETATM 5144 O  O    . HOH   D 4 .   ? 8.16900   -28.79300 -18.30700 1.000 30.04420  ? 1597 HOH   B O    1 
HETATM 5145 O  O    . HOH   D 4 .   ? 20.13800  -10.13200 -43.55100 1.000 26.88665  ? 1598 HOH   B O    1 
HETATM 5146 O  O    . HOH   D 4 .   ? 9.00800   5.76600   -48.61800 1.000 24.46925  ? 1599 HOH   B O    1 
HETATM 5147 O  O    . HOH   D 4 .   ? 32.78300  -13.88200 -34.50400 1.000 27.00748  ? 1600 HOH   B O    1 
HETATM 5148 O  O    . HOH   D 4 .   ? 12.65700  -5.28000  -30.76700 1.000 22.75663  ? 1601 HOH   B O    1 
HETATM 5149 O  O    . HOH   D 4 .   ? 22.84900  -21.75000 -17.57400 1.000 19.07764  ? 1602 HOH   B O    1 
HETATM 5150 O  O    . HOH   D 4 .   ? 9.65300   -17.15300 -34.89900 1.000 21.93998  ? 1603 HOH   B O    1 
HETATM 5151 O  O    . HOH   D 4 .   ? 1.62700   -5.05700  -23.17600 1.000 22.26087  ? 1604 HOH   B O    1 
HETATM 5152 O  O    . HOH   D 4 .   ? 1.57500   1.18900   -23.73900 1.000 28.32146  ? 1605 HOH   B O    1 
HETATM 5153 O  O    . HOH   D 4 .   ? 19.82800  -2.05400  -17.24100 1.000 22.93636  ? 1606 HOH   B O    1 
HETATM 5154 O  O    . HOH   D 4 .   ? 31.08600  -17.63800 -20.35000 1.000 28.89592  ? 1607 HOH   B O    1 
HETATM 5155 O  O    . HOH   D 4 .   ? 20.77900  -25.31500 -16.11300 1.000 24.08284  ? 1608 HOH   B O    1 
HETATM 5156 O  O    . HOH   D 4 .   ? 16.53100  12.47000  -33.12500 1.000 30.34478  ? 1609 HOH   B O    1 
HETATM 5157 O  O    . HOH   D 4 .   ? 16.85700  -5.49900  -47.23900 1.000 18.27631  ? 1610 HOH   B O    1 
HETATM 5158 O  O    . HOH   D 4 .   ? 36.22000  -19.52000 -28.89100 1.000 23.02961  ? 1611 HOH   B O    1 
HETATM 5159 O  O    . HOH   D 4 .   ? 12.00700  -11.65600 -44.12800 1.000 25.34078  ? 1612 HOH   B O    1 
HETATM 5160 O  O    . HOH   D 4 .   ? 19.41700  -26.32700 -35.86700 1.000 26.94064  ? 1613 HOH   B O    1 
HETATM 5161 O  O    . HOH   D 4 .   ? 18.07800  6.33200   -41.28500 1.000 17.71110  ? 1614 HOH   B O    1 
HETATM 5162 O  O    . HOH   D 4 .   ? 7.19300   -17.62000 -21.39500 1.000 19.81082  ? 1615 HOH   B O    1 
HETATM 5163 O  O    . HOH   D 4 .   ? 18.18500  -0.14000  -17.67500 1.000 23.66600  ? 1616 HOH   B O    1 
HETATM 5164 O  O    . HOH   D 4 .   ? 13.48100  -31.94900 -43.40800 1.000 46.39079  ? 1617 HOH   B O    1 
HETATM 5165 O  O    . HOH   D 4 .   ? 26.86900  4.03900   -25.67200 1.000 21.40078  ? 1618 HOH   B O    1 
HETATM 5166 O  O    . HOH   D 4 .   ? 9.46500   11.16400  -26.96100 1.000 23.10698  ? 1619 HOH   B O    1 
HETATM 5167 O  O    . HOH   D 4 .   ? 11.18000  -19.89400 -14.03000 1.000 17.33534  ? 1620 HOH   B O    1 
HETATM 5168 O  O    . HOH   D 4 .   ? -2.240    -34.250   -40.933   1.000 23.36023  ? 1621 HOH   B O    1 
HETATM 5169 O  O    . HOH   D 4 .   ? -4.16200  -27.58500 -16.98100 1.000 32.56356  ? 1622 HOH   B O    1 
HETATM 5170 O  O    . HOH   D 4 .   ? 8.73500   -7.92500  -32.50300 1.000 12.28127  ? 1623 HOH   B O    1 
HETATM 5171 O  O    . HOH   D 4 .   ? 25.78200  9.20200   -29.53700 1.000 26.45391  ? 1624 HOH   B O    1 
HETATM 5172 O  O    . HOH   D 4 .   ? 0.646     6.782     -31.459   1.000 17.58856  ? 1625 HOH   B O    1 
HETATM 5173 O  O    . HOH   D 4 .   ? 8.88700   -18.97600 -19.82900 1.000 15.46576  ? 1626 HOH   B O    1 
HETATM 5174 O  O    . HOH   D 4 .   ? 8.06600   -14.54800 -9.52100  1.000 41.49498  ? 1627 HOH   B O    1 
HETATM 5175 O  O    . HOH   D 4 .   ? 10.12500  -17.96500 -37.44700 1.000 17.23554  ? 1628 HOH   B O    1 
HETATM 5176 O  O    . HOH   D 4 .   ? -1.77300  4.43400   -42.32000 1.000 22.18385  ? 1629 HOH   B O    1 
HETATM 5177 O  O    . HOH   D 4 .   ? 17.05900  -31.71100 -15.94900 1.000 38.31165  ? 1630 HOH   B O    1 
HETATM 5178 O  O    . HOH   D 4 .   ? 27.986    -11.211   -19.404   1.000 24.68394  ? 1631 HOH   B O    1 
HETATM 5179 O  O    . HOH   D 4 .   ? -5.70700  -16.45500 -15.03900 1.000 31.79668  ? 1632 HOH   B O    1 
HETATM 5180 O  O    . HOH   D 4 .   ? 9.82400   10.36400  -33.92800 1.000 21.10553  ? 1633 HOH   B O    1 
HETATM 5181 O  O    . HOH   D 4 .   ? 19.62600  -14.35300 -10.36900 1.000 16.56361  ? 1634 HOH   B O    1 
HETATM 5182 O  O    . HOH   D 4 .   ? 10.86600  -12.02100 -34.48200 1.000 30.31197  ? 1635 HOH   B O    1 
HETATM 5183 O  O    . HOH   D 4 .   ? 7.74500   -5.29700  -31.76000 1.000 12.52471  ? 1636 HOH   B O    1 
HETATM 5184 O  O    . HOH   D 4 .   ? 32.34100  -26.52500 -27.70700 1.000 32.87414  ? 1637 HOH   B O    1 
HETATM 5185 O  O    . HOH   D 4 .   ? 31.45500  -19.87900 -30.22400 1.000 27.91999  ? 1638 HOH   B O    1 
HETATM 5186 O  O    . HOH   D 4 .   ? 29.63600  -26.76100 -31.86200 1.000 31.38869  ? 1639 HOH   B O    1 
HETATM 5187 O  O    . HOH   D 4 .   ? 14.76100  -26.03200 -13.28800 1.000 36.03633  ? 1640 HOH   B O    1 
HETATM 5188 O  O    . HOH   D 4 .   ? 12.87600  -7.82300  -37.47000 1.000 34.06860  ? 1641 HOH   B O    1 
HETATM 5189 O  O    . HOH   D 4 .   ? -8.20100  -6.10400  -45.54900 1.000 31.41257  ? 1642 HOH   B O    1 
HETATM 5190 O  O    . HOH   D 4 .   ? 36.48500  -6.01600  -26.79900 1.000 28.32484  ? 1643 HOH   B O    1 
HETATM 5191 O  O    . HOH   D 4 .   ? 21.40600  -21.36200 -15.34600 1.000 13.97094  ? 1644 HOH   B O    1 
HETATM 5192 O  O    . HOH   D 4 .   ? 11.53600  -18.49600 -33.89200 1.000 26.70529  ? 1645 HOH   B O    1 
HETATM 5193 O  O    . HOH   D 4 .   ? 28.62300  4.73000   -27.25200 1.000 30.59401  ? 1646 HOH   B O    1 
HETATM 5194 O  O    . HOH   D 4 .   ? 13.38200  -25.17300 -41.72700 1.000 32.15832  ? 1647 HOH   B O    1 
HETATM 5195 O  O    . HOH   D 4 .   ? 33.163    -24.575   -25.432   1.000 30.24423  ? 1648 HOH   B O    1 
HETATM 5196 O  O    . HOH   D 4 .   ? 17.88000  -15.64900 -39.47600 1.000 26.89294  ? 1649 HOH   B O    1 
HETATM 5197 O  O    . HOH   D 4 .   ? 9.81900   -5.36700  -30.01600 1.000 13.79101  ? 1650 HOH   B O    1 
HETATM 5198 O  O    . HOH   D 4 .   ? 23.78100  -10.71000 -9.34600  1.000 20.01580  ? 1651 HOH   B O    1 
HETATM 5199 O  O    . HOH   D 4 .   ? 1.01000   -25.77500 -48.13200 1.000 44.60948  ? 1652 HOH   B O    1 
HETATM 5200 O  O    . HOH   D 4 .   ? 18.15200  12.83200  -37.56100 1.000 41.01573  ? 1653 HOH   B O    1 
HETATM 5201 O  O    . HOH   D 4 .   ? 11.27200  -9.02500  -33.11200 1.000 21.99541  ? 1654 HOH   B O    1 
HETATM 5202 O  O    . HOH   D 4 .   ? 14.67600  -12.84800 -33.08500 1.000 26.68295  ? 1655 HOH   B O    1 
HETATM 5203 O  O    . HOH   D 4 .   ? -3.16700  -33.14700 -18.73800 1.000 27.73998  ? 1656 HOH   B O    1 
HETATM 5204 O  O    . HOH   D 4 .   ? 26.40700  -10.81200 -49.67500 1.000 40.22911  ? 1657 HOH   B O    1 
HETATM 5205 O  O    . HOH   D 4 .   ? 6.64700   -4.08300  -15.80300 1.000 41.09548  ? 1658 HOH   B O    1 
HETATM 5206 O  O    . HOH   D 4 .   ? 32.99200  -15.53600 -36.14300 1.000 36.26460  ? 1659 HOH   B O    1 
HETATM 5207 O  O    . HOH   D 4 .   ? 15.87500  0.28300   -16.42800 1.000 27.73876  ? 1660 HOH   B O    1 
HETATM 5208 O  O    . HOH   D 4 .   ? 11.55100  -7.54700  -21.92400 1.000 29.73122  ? 1661 HOH   B O    1 
HETATM 5209 O  O    . HOH   D 4 .   ? 15.89700  -11.69900 -35.35200 1.000 28.16046  ? 1662 HOH   B O    1 
HETATM 5210 O  O    . HOH   D 4 .   ? 20.70000  -25.37600 -9.27400  1.000 29.39010  ? 1663 HOH   B O    1 
HETATM 5211 O  O    . HOH   D 4 .   ? 2.95900   -3.19100  -53.64200 1.000 33.39528  ? 1664 HOH   B O    1 
HETATM 5212 O  O    . HOH   D 4 .   ? 5.00600   -26.87700 -16.08600 1.000 36.81957  ? 1665 HOH   B O    1 
HETATM 5213 O  O    . HOH   D 4 .   ? 17.84500  -25.73900 -10.28600 1.000 26.16116  ? 1666 HOH   B O    1 
HETATM 5214 O  O    . HOH   D 4 .   ? -10.33500 -19.95000 -21.09600 1.000 37.73193  ? 1667 HOH   B O    1 
HETATM 5215 O  O    . HOH   D 4 .   ? 35.86800  -19.77400 -26.24700 1.000 31.98439  ? 1668 HOH   B O    1 
HETATM 5216 O  O    . HOH   D 4 .   ? 13.67200  4.75500   -15.83800 1.000 32.51936  ? 1669 HOH   B O    1 
HETATM 5217 O  O    . HOH   D 4 .   ? 22.97900  -31.59600 -16.67400 1.000 31.60839  ? 1670 HOH   B O    1 
HETATM 5218 O  O    . HOH   D 4 .   ? 24.07200  -29.65000 -21.82100 1.000 30.11941  ? 1671 HOH   B O    1 
HETATM 5219 O  O    . HOH   D 4 .   ? -10.751   -28.217   -28.732   1.000 35.56154  ? 1672 HOH   B O    1 
HETATM 5220 O  O    . HOH   D 4 .   ? 10.00100  -31.40800 -13.14500 1.000 40.97511  ? 1673 HOH   B O    1 
HETATM 5221 O  O    . HOH   D 4 .   ? 29.45900  -1.84900  -39.25700 1.000 25.29709  ? 1674 HOH   B O    1 
HETATM 5222 O  O    . HOH   D 4 .   ? 12.23100  -15.01600 -38.52100 1.000 35.52354  ? 1675 HOH   B O    1 
HETATM 5223 O  O    . HOH   D 4 .   ? 15.283    14.728    -40.234   1.000 37.88628  ? 1676 HOH   B O    1 
HETATM 5224 O  O    . HOH   D 4 .   ? 11.31200  -1.19800  -16.73700 1.000 23.70858  ? 1677 HOH   B O    1 
HETATM 5225 O  O    . HOH   D 4 .   ? 13.70800  -5.72400  -49.93500 1.000 36.46968  ? 1678 HOH   B O    1 
HETATM 5226 O  O    . HOH   D 4 .   ? -7.68300  -24.03200 -36.70900 1.000 31.27446  ? 1679 HOH   B O    1 
HETATM 5227 O  O    . HOH   D 4 .   ? 13.44200  14.39300  -38.31700 1.000 30.69851  ? 1680 HOH   B O    1 
HETATM 5228 O  O    . HOH   D 4 .   ? 25.26400  -22.74500 -16.98000 1.000 17.14211  ? 1681 HOH   B O    1 
HETATM 5229 O  O    . HOH   D 4 .   ? -2.20600  -17.98600 -10.87800 1.000 51.46555  ? 1682 HOH   B O    1 
HETATM 5230 O  O    . HOH   D 4 .   ? -2.46600  -3.79000  -23.21500 1.000 31.49934  ? 1683 HOH   B O    1 
HETATM 5231 O  O    . HOH   D 4 .   ? 12.86500  -10.76000 -41.56300 1.000 31.39570  ? 1684 HOH   B O    1 
HETATM 5232 O  O    . HOH   D 4 .   ? 15.86100  -28.55000 -11.35800 1.000 39.36618  ? 1685 HOH   B O    1 
HETATM 5233 O  O    . HOH   D 4 .   ? 21.81200  5.58000   -16.01200 1.000 32.50712  ? 1686 HOH   B O    1 
HETATM 5234 O  O    . HOH   D 4 .   ? 39.35600  7.39600   -34.32700 1.000 40.11533  ? 1687 HOH   B O    1 
HETATM 5235 O  O    . HOH   E 4 .   ? 23.89000  -30.12200 -7.39900  1.000 36.05318  ? 401  HOH   A O    1 
HETATM 5236 O  O    . HOH   E 4 .   ? 22.91500  -5.28900  -0.63600  1.000 18.91090  ? 402  HOH   A O    1 
HETATM 5237 O  O    . HOH   E 4 .   ? 30.56100  -5.72600  14.40100  1.000 24.55440  ? 403  HOH   A O    1 
HETATM 5238 O  O    . HOH   E 4 .   ? 28.08300  -19.71000 -4.15200  1.000 7.16208   ? 404  HOH   A O    1 
HETATM 5239 O  O    . HOH   E 4 .   ? 0.50900   -16.89000 25.59400  1.000 13.88667  ? 405  HOH   A O    1 
HETATM 5240 O  O    . HOH   E 4 .   ? -10.53900 -16.13000 12.22600  1.000 19.89454  ? 406  HOH   A O    1 
HETATM 5241 O  O    . HOH   E 4 .   ? 6.17000   -24.71000 6.08000   1.000 19.85772  ? 407  HOH   A O    1 
HETATM 5242 O  O    . HOH   E 4 .   ? 3.04900   -4.63100  21.76900  1.000 29.56177  ? 408  HOH   A O    1 
HETATM 5243 O  O    . HOH   E 4 .   ? 9.36500   -1.93500  15.36400  1.000 39.75742  ? 409  HOH   A O    1 
HETATM 5244 O  O    . HOH   E 4 .   ? 11.03500  -26.39300 -9.66900  1.000 27.86869  ? 410  HOH   A O    1 
HETATM 5245 O  O    . HOH   E 4 .   ? 27.96200  -35.29800 -6.59000  1.000 32.97729  ? 411  HOH   A O    1 
HETATM 5246 O  O    . HOH   E 4 .   ? 10.38100  -36.65500 -0.17500  1.000 25.91016  ? 412  HOH   A O    1 
HETATM 5247 O  O    . HOH   E 4 .   ? 22.54300  -25.04200 -6.64000  1.000 18.87907  ? 413  HOH   A O    1 
HETATM 5248 O  O    . HOH   E 4 .   ? -5.06800  -17.90400 -8.46500  1.000 30.11027  ? 414  HOH   A O    1 
HETATM 5249 O  O    . HOH   E 4 .   ? -3.12400  -29.02700 4.27000   1.000 13.34750  ? 415  HOH   A O    1 
HETATM 5250 O  O    . HOH   E 4 .   ? 11.68400  -29.02500 2.24700   1.000 25.15221  ? 416  HOH   A O    1 
HETATM 5251 O  O    . HOH   E 4 .   ? 4.52300   -25.96200 19.38700  1.000 11.42351  ? 417  HOH   A O    1 
HETATM 5252 O  O    . HOH   E 4 .   ? 1.68600   -28.14200 -6.23900  1.000 31.92231  ? 418  HOH   A O    1 
HETATM 5253 O  O    . HOH   E 4 .   ? 25.80600  -24.32100 -7.75500  1.000 30.22662  ? 419  HOH   A O    1 
HETATM 5254 O  O    . HOH   E 4 .   ? 7.39200   -18.59500 7.47900   1.000 12.13724  ? 420  HOH   A O    1 
HETATM 5255 O  O    . HOH   E 4 .   ? -12.14900 -14.82700 21.51100  1.000 16.24710  ? 421  HOH   A O    1 
HETATM 5256 O  O    . HOH   E 4 .   ? 5.83600   -30.88100 20.00900  1.000 12.61600  ? 422  HOH   A O    1 
HETATM 5257 O  O    . HOH   E 4 .   ? 22.234    1.808     17.910    1.000 29.11226  ? 423  HOH   A O    1 
HETATM 5258 O  O    . HOH   E 4 .   ? -5.56700  -7.79700  1.31300   1.000 16.23726  ? 424  HOH   A O    1 
HETATM 5259 O  O    . HOH   E 4 .   ? 5.90300   -8.76500  -4.75600  1.000 35.20840  ? 425  HOH   A O    1 
HETATM 5260 O  O    . HOH   E 4 .   ? -4.35400  -13.94800 22.17300  1.000 24.98102  ? 426  HOH   A O    1 
HETATM 5261 O  O    . HOH   E 4 .   ? 17.45900  -1.11600  -6.92300  1.000 35.83552  ? 427  HOH   A O    1 
HETATM 5262 O  O    . HOH   E 4 .   ? -5.806    -27.637   -5.108    1.000 10.16094  ? 428  HOH   A O    1 
HETATM 5263 O  O    . HOH   E 4 .   ? -5.46200  -8.17700  -3.57300  1.000 31.65346  ? 429  HOH   A O    1 
HETATM 5264 O  O    . HOH   E 4 .   ? 11.83000  -25.42600 1.19900   1.000 9.12764   ? 430  HOH   A O    1 
HETATM 5265 O  O    . HOH   E 4 .   ? 12.44900  -22.16300 -7.34000  1.000 14.65300  ? 431  HOH   A O    1 
HETATM 5266 O  O    . HOH   E 4 .   ? -10.10300 -9.18900  3.34100   1.000 21.80166  ? 432  HOH   A O    1 
HETATM 5267 O  O    . HOH   E 4 .   ? 3.36000   -31.74000 19.08100  1.000 19.23879  ? 433  HOH   A O    1 
HETATM 5268 O  O    . HOH   E 4 .   ? -2.68400  -26.22200 24.98300  1.000 23.41613  ? 434  HOH   A O    1 
HETATM 5269 O  O    . HOH   E 4 .   ? -7.34100  -6.17400  4.86000   1.000 27.13016  ? 435  HOH   A O    1 
HETATM 5270 O  O    . HOH   E 4 .   ? 11.37900  -15.87600 12.65000  1.000 14.97847  ? 436  HOH   A O    1 
HETATM 5271 O  O    . HOH   E 4 .   ? 19.79100  -1.38500  17.78000  1.000 24.55745  ? 437  HOH   A O    1 
HETATM 5272 O  O    . HOH   E 4 .   ? 7.04600   -19.83100 10.28100  1.000 11.35594  ? 438  HOH   A O    1 
HETATM 5273 O  O    . HOH   E 4 .   ? 35.395    -13.872   13.159    1.000 29.80140  ? 439  HOH   A O    1 
HETATM 5274 O  O    . HOH   E 4 .   ? 11.50700  -13.63800 17.79900  1.000 21.34891  ? 440  HOH   A O    1 
HETATM 5275 O  O    . HOH   E 4 .   ? 19.52900  -21.64700 18.20000  1.000 15.48826  ? 441  HOH   A O    1 
HETATM 5276 O  O    . HOH   E 4 .   ? 11.96300  -39.61800 6.14000   1.000 21.67776  ? 442  HOH   A O    1 
HETATM 5277 O  O    . HOH   E 4 .   ? 10.30800  -10.56700 -1.76800  1.000 27.52177  ? 443  HOH   A O    1 
HETATM 5278 O  O    . HOH   E 4 .   ? 3.38700   3.57300   9.60500   1.000 20.17967  ? 444  HOH   A O    1 
HETATM 5279 O  O    . HOH   E 4 .   ? -8.30700  -4.79100  8.07800   1.000 27.46020  ? 445  HOH   A O    1 
HETATM 5280 O  O    . HOH   E 4 .   ? 8.04200   -16.27300 15.79800  1.000 16.80857  ? 446  HOH   A O    1 
HETATM 5281 O  O    . HOH   E 4 .   ? 15.05700  4.29200   17.32800  1.000 27.04562  ? 447  HOH   A O    1 
HETATM 5282 O  O    . HOH   E 4 .   ? 3.91100   -27.67600 17.31200  1.000 15.64289  ? 448  HOH   A O    1 
HETATM 5283 O  O    . HOH   E 4 .   ? -8.49300  -31.84900 11.35000  1.000 22.70319  ? 449  HOH   A O    1 
HETATM 5284 O  O    . HOH   E 4 .   ? 26.16700  -19.56100 -8.40300  1.000 13.16092  ? 450  HOH   A O    1 
HETATM 5285 O  O    . HOH   E 4 .   ? 21.584    -2.454    22.633    1.000 24.07382  ? 451  HOH   A O    1 
HETATM 5286 O  O    . HOH   E 4 .   ? 16.59300  -1.03200  -0.61800  1.000 11.49511  ? 452  HOH   A O    1 
HETATM 5287 O  O    . HOH   E 4 .   ? -2.076    -24.427   28.450    1.000 27.59256  ? 453  HOH   A O    1 
HETATM 5288 O  O    . HOH   E 4 .   ? 8.06000   -23.36900 18.45600  1.000 24.74776  ? 454  HOH   A O    1 
HETATM 5289 O  O    . HOH   E 4 .   ? 31.88500  -10.62600 5.20300   1.000 17.47840  ? 455  HOH   A O    1 
HETATM 5290 O  O    . HOH   E 4 .   ? -8.27900  -15.09000 2.71700   1.000 12.56514  ? 456  HOH   A O    1 
HETATM 5291 O  O    . HOH   E 4 .   ? 17.57000  -17.26600 22.17100  1.000 25.09328  ? 457  HOH   A O    1 
HETATM 5292 O  O    . HOH   E 4 .   ? 23.63500  -10.73500 17.83000  1.000 11.25539  ? 458  HOH   A O    1 
HETATM 5293 O  O    . HOH   E 4 .   ? 24.28700  -0.14300  2.75100   1.000 36.53906  ? 459  HOH   A O    1 
HETATM 5294 O  O    . HOH   E 4 .   ? 2.93300   -18.78500 25.56500  1.000 22.39203  ? 460  HOH   A O    1 
HETATM 5295 O  O    . HOH   E 4 .   ? 12.11000  -37.36900 17.73700  1.000 25.23458  ? 461  HOH   A O    1 
HETATM 5296 O  O    . HOH   E 4 .   ? 10.30500  -6.78200  -10.25500 1.000 31.71036  ? 462  HOH   A O    1 
HETATM 5297 O  O    . HOH   E 4 .   ? 24.12600  -30.34100 -0.07100  1.000 28.19148  ? 463  HOH   A O    1 
HETATM 5298 O  O    . HOH   E 4 .   ? 0.06600   -20.91200 -6.14200  1.000 21.16370  ? 464  HOH   A O    1 
HETATM 5299 O  O    . HOH   E 4 .   ? -3.11200  -4.18200  0.15500   1.000 24.79287  ? 465  HOH   A O    1 
HETATM 5300 O  O    . HOH   E 4 .   ? 24.49000  -27.25100 1.25500   1.000 21.15032  ? 466  HOH   A O    1 
HETATM 5301 O  O    . HOH   E 4 .   ? -4.81500  -30.56500 1.90000   1.000 14.25421  ? 467  HOH   A O    1 
HETATM 5302 O  O    . HOH   E 4 .   ? -5.86500  -31.02300 21.66000  1.000 29.23285  ? 468  HOH   A O    1 
HETATM 5303 O  O    . HOH   E 4 .   ? 33.84800  -11.60200 16.39800  1.000 16.94613  ? 469  HOH   A O    1 
HETATM 5304 O  O    . HOH   E 4 .   ? -9.960    -27.565   5.632     1.000 21.28993  ? 470  HOH   A O    1 
HETATM 5305 O  O    . HOH   E 4 .   ? 22.67300  -28.10200 -1.73600  1.000 13.02691  ? 471  HOH   A O    1 
HETATM 5306 O  O    . HOH   E 4 .   ? -4.01300  -25.18500 -6.08000  1.000 23.07926  ? 472  HOH   A O    1 
HETATM 5307 O  O    . HOH   E 4 .   ? 24.70600  -22.12000 18.33300  1.000 28.25521  ? 473  HOH   A O    1 
HETATM 5308 O  O    . HOH   E 4 .   ? 18.27100  1.95400   5.96000   1.000 29.08897  ? 474  HOH   A O    1 
HETATM 5309 O  O    . HOH   E 4 .   ? 33.206    -24.817   6.268     1.000 14.46543  ? 475  HOH   A O    1 
HETATM 5310 O  O    . HOH   E 4 .   ? 18.45600  -30.61100 2.55800   1.000 14.17110  ? 476  HOH   A O    1 
HETATM 5311 O  O    . HOH   E 4 .   ? 4.15900   -2.48000  20.32400  1.000 29.85590  ? 477  HOH   A O    1 
HETATM 5312 O  O    . HOH   E 4 .   ? 16.81100  -3.15800  1.95700   1.000 13.66158  ? 478  HOH   A O    1 
HETATM 5313 O  O    . HOH   E 4 .   ? 8.18100   0.51700   20.06900  1.000 28.24089  ? 479  HOH   A O    1 
HETATM 5314 O  O    . HOH   E 4 .   ? 2.02400   -8.93500  23.11200  1.000 28.23158  ? 480  HOH   A O    1 
HETATM 5315 O  O    . HOH   E 4 .   ? 7.26800   -20.02500 17.52000  1.000 20.79665  ? 481  HOH   A O    1 
HETATM 5316 O  O    . HOH   E 4 .   ? 7.30900   -26.12200 19.43000  1.000 15.24816  ? 482  HOH   A O    1 
HETATM 5317 O  O    . HOH   E 4 .   ? -9.66900  -12.49200 -3.96800  1.000 17.48960  ? 483  HOH   A O    1 
HETATM 5318 O  O    . HOH   E 4 .   ? 10.48500  -3.13700  22.38500  1.000 27.76675  ? 484  HOH   A O    1 
HETATM 5319 O  O    . HOH   E 4 .   ? 2.90900   -3.65200  4.79400   1.000 17.59392  ? 485  HOH   A O    1 
HETATM 5320 O  O    . HOH   E 4 .   ? -0.29800  0.13100   9.75900   1.000 14.77388  ? 486  HOH   A O    1 
HETATM 5321 O  O    . HOH   E 4 .   ? 21.84600  2.01600   5.83300   1.000 30.65356  ? 487  HOH   A O    1 
HETATM 5322 O  O    . HOH   E 4 .   ? 9.01200   -17.84100 23.62100  1.000 25.18470  ? 488  HOH   A O    1 
HETATM 5323 O  O    . HOH   E 4 .   ? 10.76500  -20.40000 -4.92900  1.000 12.55703  ? 489  HOH   A O    1 
HETATM 5324 O  O    . HOH   E 4 .   ? 21.70600  -36.45400 -0.58300  1.000 40.63973  ? 490  HOH   A O    1 
HETATM 5325 O  O    . HOH   E 4 .   ? -0.60600  -27.29800 -5.27000  1.000 21.58934  ? 491  HOH   A O    1 
HETATM 5326 O  O    . HOH   E 4 .   ? 22.05800  1.22800   3.24100   1.000 20.32046  ? 492  HOH   A O    1 
HETATM 5327 O  O    . HOH   E 4 .   ? 13.18500  -20.02000 3.25500   1.000 7.69039   ? 493  HOH   A O    1 
HETATM 5328 O  O    . HOH   E 4 .   ? 10.98200  -4.45200  -6.75000  1.000 23.56799  ? 494  HOH   A O    1 
HETATM 5329 O  O    . HOH   E 4 .   ? 5.38000   -17.95100 25.55000  1.000 18.82094  ? 495  HOH   A O    1 
HETATM 5330 O  O    . HOH   E 4 .   ? 13.16200  -12.59500 14.86400  1.000 15.61104  ? 496  HOH   A O    1 
HETATM 5331 O  O    . HOH   E 4 .   ? 24.25800  -18.13400 -10.66900 1.000 24.20412  ? 497  HOH   A O    1 
HETATM 5332 O  O    . HOH   E 4 .   ? 14.47900  -40.41900 5.54000   1.000 23.93627  ? 498  HOH   A O    1 
HETATM 5333 O  O    . HOH   E 4 .   ? -8.01100  -11.11700 18.21400  1.000 24.59158  ? 499  HOH   A O    1 
HETATM 5334 O  O    . HOH   E 4 .   ? 12.50600  -15.75900 9.11000   1.000 12.95883  ? 500  HOH   A O    1 
HETATM 5335 O  O    . HOH   E 4 .   ? 27.781    -22.542   -5.092    1.000 15.87531  ? 501  HOH   A O    1 
HETATM 5336 O  O    . HOH   E 4 .   ? -5.28400  -30.15100 -1.93000  1.000 17.55193  ? 502  HOH   A O    1 
HETATM 5337 O  O    . HOH   E 4 .   ? 7.90200   -11.84200 24.44100  1.000 17.51854  ? 503  HOH   A O    1 
HETATM 5338 O  O    . HOH   E 4 .   ? 15.05400  -19.18800 8.93500   1.000 9.41687   ? 504  HOH   A O    1 
HETATM 5339 O  O    . HOH   E 4 .   ? 13.48100  -18.07400 11.10700  1.000 17.85316  ? 505  HOH   A O    1 
HETATM 5340 O  O    . HOH   E 4 .   ? 11.81900  -30.89500 17.60900  1.000 22.34550  ? 506  HOH   A O    1 
HETATM 5341 O  O    . HOH   E 4 .   ? 27.07300  -11.82500 -3.00500  1.000 15.41205  ? 507  HOH   A O    1 
HETATM 5342 O  O    . HOH   E 4 .   ? 5.48300   2.86000   5.78100   1.000 21.23770  ? 508  HOH   A O    1 
HETATM 5343 O  O    . HOH   E 4 .   ? 19.33200  -33.79100 -5.53500  1.000 33.04374  ? 509  HOH   A O    1 
HETATM 5344 O  O    . HOH   E 4 .   ? 11.63400  -14.17500 23.97600  1.000 21.29983  ? 510  HOH   A O    1 
HETATM 5345 O  O    . HOH   E 4 .   ? -1.40300  -20.70200 26.68200  1.000 28.47865  ? 511  HOH   A O    1 
HETATM 5346 O  O    . HOH   E 4 .   ? 9.33100   -14.40200 14.43700  1.000 10.01711  ? 512  HOH   A O    1 
HETATM 5347 O  O    . HOH   E 4 .   ? -12.18600 -9.84300  14.97500  1.000 25.63077  ? 513  HOH   A O    1 
HETATM 5348 O  O    . HOH   E 4 .   ? 29.77200  -13.00900 16.82200  1.000 20.53946  ? 514  HOH   A O    1 
HETATM 5349 O  O    . HOH   E 4 .   ? 22.61300  0.07300   -1.72800  1.000 40.31146  ? 515  HOH   A O    1 
HETATM 5350 O  O    . HOH   E 4 .   ? 10.89000  -27.16500 4.20800   1.000 15.65273  ? 516  HOH   A O    1 
HETATM 5351 O  O    . HOH   E 4 .   ? 0.96700   -2.12900  2.42100   1.000 13.64375  ? 517  HOH   A O    1 
HETATM 5352 O  O    . HOH   E 4 .   ? -12.79100 -19.74500 7.68400   1.000 14.61427  ? 518  HOH   A O    1 
HETATM 5353 O  O    . HOH   E 4 .   ? 3.50600   -0.18800  -5.73100  1.000 23.73239  ? 519  HOH   A O    1 
HETATM 5354 O  O    . HOH   E 4 .   ? 26.80200  -11.90900 -5.48900  1.000 20.10523  ? 520  HOH   A O    1 
HETATM 5355 O  O    . HOH   E 4 .   ? 13.26900  0.71800   15.66500  1.000 20.78857  ? 521  HOH   A O    1 
HETATM 5356 O  O    . HOH   E 4 .   ? 9.98700   5.05100   7.36800   1.000 26.52522  ? 522  HOH   A O    1 
HETATM 5357 O  O    . HOH   E 4 .   ? -11.86900 -24.49400 9.93800   1.000 10.34777  ? 523  HOH   A O    1 
HETATM 5358 O  O    . HOH   E 4 .   ? 29.32200  -13.27100 -3.25800  1.000 20.45494  ? 524  HOH   A O    1 
HETATM 5359 O  O    . HOH   E 4 .   ? -5.89700  -15.16400 5.22700   1.000 14.81294  ? 525  HOH   A O    1 
HETATM 5360 O  O    . HOH   E 4 .   ? 9.49200   -22.28400 23.12000  1.000 27.35652  ? 526  HOH   A O    1 
HETATM 5361 O  O    . HOH   E 4 .   ? 29.72000  -4.06200  5.17800   1.000 30.72219  ? 527  HOH   A O    1 
HETATM 5362 O  O    . HOH   E 4 .   ? 8.10500   -22.35100 14.78900  1.000 12.11898  ? 528  HOH   A O    1 
HETATM 5363 O  O    . HOH   E 4 .   ? 33.980    -27.690   6.651     1.000 16.91280  ? 529  HOH   A O    1 
HETATM 5364 O  O    . HOH   E 4 .   ? 8.96100   0.60800   1.10000   1.000 27.39135  ? 530  HOH   A O    1 
HETATM 5365 O  O    . HOH   E 4 .   ? 20.15200  -19.55100 -9.99900  1.000 30.43487  ? 531  HOH   A O    1 
HETATM 5366 O  O    . HOH   E 4 .   ? 12.82500  -7.73400  22.23000  1.000 21.85260  ? 532  HOH   A O    1 
HETATM 5367 O  O    . HOH   E 4 .   ? 2.23400   -14.85500 27.80500  1.000 29.27006  ? 533  HOH   A O    1 
HETATM 5368 O  O    . HOH   E 4 .   ? 27.65800  -35.33800 6.11900   1.000 26.22924  ? 534  HOH   A O    1 
HETATM 5369 O  O    . HOH   E 4 .   ? -10.280   -26.077   2.347     1.000 20.84283  ? 535  HOH   A O    1 
HETATM 5370 O  O    . HOH   E 4 .   ? 15.20000  -36.60200 -4.35000  1.000 27.65166  ? 536  HOH   A O    1 
HETATM 5371 O  O    . HOH   E 4 .   ? 9.06500   -19.57900 -2.91200  1.000 8.62257   ? 537  HOH   A O    1 
HETATM 5372 O  O    . HOH   E 4 .   ? 4.76200   -39.83000 1.55900   1.000 28.34421  ? 538  HOH   A O    1 
HETATM 5373 O  O    . HOH   E 4 .   ? 26.35600  -37.20700 4.24900   1.000 47.70725  ? 539  HOH   A O    1 
HETATM 5374 O  O    . HOH   E 4 .   ? 9.42900   -37.28900 20.96100  1.000 22.82636  ? 540  HOH   A O    1 
HETATM 5375 O  O    . HOH   E 4 .   ? -5.26400  -15.10900 25.24900  1.000 41.30961  ? 541  HOH   A O    1 
HETATM 5376 O  O    . HOH   E 4 .   ? 21.15000  -29.97200 3.25000   1.000 12.32898  ? 542  HOH   A O    1 
HETATM 5377 O  O    . HOH   E 4 .   ? 21.01400  -16.00900 -10.63600 1.000 20.35296  ? 543  HOH   A O    1 
HETATM 5378 O  O    . HOH   E 4 .   ? -5.56900  -21.89100 18.13100  1.000 22.18745  ? 544  HOH   A O    1 
HETATM 5379 O  O    . HOH   E 4 .   ? -6.00100  -33.67200 11.03900  1.000 26.12274  ? 545  HOH   A O    1 
HETATM 5380 O  O    . HOH   E 4 .   ? 0.41700   -23.50400 -7.13800  1.000 34.93399  ? 546  HOH   A O    1 
HETATM 5381 O  O    . HOH   E 4 .   ? -6.11900  -15.84900 21.23500  1.000 22.03877  ? 547  HOH   A O    1 
HETATM 5382 O  O    . HOH   E 4 .   ? 16.87800  -15.18400 14.60400  1.000 17.96326  ? 548  HOH   A O    1 
HETATM 5383 O  O    . HOH   E 4 .   ? -0.34300  2.09700   8.01500   1.000 24.17437  ? 549  HOH   A O    1 
HETATM 5384 O  O    . HOH   E 4 .   ? -6.69100  -2.85300  11.37100  1.000 14.87896  ? 550  HOH   A O    1 
HETATM 5385 O  O    . HOH   E 4 .   ? 9.69100   -41.07200 4.80200   1.000 23.12139  ? 551  HOH   A O    1 
HETATM 5386 O  O    . HOH   E 4 .   ? 13.41700  4.97800   8.21800   1.000 26.18310  ? 552  HOH   A O    1 
HETATM 5387 O  O    . HOH   E 4 .   ? 7.91700   -42.10700 6.70200   1.000 21.19530  ? 553  HOH   A O    1 
HETATM 5388 O  O    . HOH   E 4 .   ? 6.73500   -18.78700 14.88700  1.000 15.48188  ? 554  HOH   A O    1 
HETATM 5389 O  O    . HOH   E 4 .   ? -1.62900  -38.62600 8.81000   1.000 25.78525  ? 555  HOH   A O    1 
HETATM 5390 O  O    . HOH   E 4 .   ? -5.69400  -34.02800 8.54400   1.000 21.26712  ? 556  HOH   A O    1 
HETATM 5391 O  O    . HOH   E 4 .   ? 16.09300  3.88000   8.53000   1.000 29.44053  ? 557  HOH   A O    1 
HETATM 5392 O  O    . HOH   E 4 .   ? -3.57200  -28.81200 -5.95300  1.000 19.59440  ? 558  HOH   A O    1 
HETATM 5393 O  O    . HOH   E 4 .   ? -6.53100  -32.81900 18.72600  1.000 33.36313  ? 559  HOH   A O    1 
HETATM 5394 O  O    . HOH   E 4 .   ? -8.11400  -12.36800 21.05600  1.000 24.85524  ? 560  HOH   A O    1 
HETATM 5395 O  O    . HOH   E 4 .   ? 20.91400  -6.65300  -7.96500  1.000 18.56832  ? 561  HOH   A O    1 
HETATM 5396 O  O    . HOH   E 4 .   ? 28.55400  -19.71700 19.33400  1.000 33.60780  ? 562  HOH   A O    1 
HETATM 5397 O  O    . HOH   E 4 .   ? 14.62700  -8.59700  -10.96200 1.000 28.91821  ? 563  HOH   A O    1 
HETATM 5398 O  O    . HOH   E 4 .   ? 18.10400  -19.68200 17.55800  1.000 22.46968  ? 564  HOH   A O    1 
HETATM 5399 O  O    . HOH   E 4 .   ? -9.05100  -9.24400  7.51100   1.000 20.37942  ? 565  HOH   A O    1 
HETATM 5400 O  O    . HOH   E 4 .   ? 14.43500  -16.75900 7.24200   1.000 12.42483  ? 566  HOH   A O    1 
HETATM 5401 O  O    . HOH   E 4 .   ? 19.28800  -8.66300  -8.65100  1.000 23.79910  ? 567  HOH   A O    1 
HETATM 5402 O  O    . HOH   E 4 .   ? -12.74300 -21.32300 11.17300  1.000 26.22695  ? 568  HOH   A O    1 
HETATM 5403 O  O    . HOH   E 4 .   ? 12.87600  -5.26800  -8.71200  1.000 28.87325  ? 569  HOH   A O    1 
HETATM 5404 O  O    . HOH   E 4 .   ? 28.871    -32.541   -5.700    1.000 34.23707  ? 570  HOH   A O    1 
HETATM 5405 O  O    . HOH   E 4 .   ? 14.43600  -35.94800 19.63300  1.000 30.63305  ? 571  HOH   A O    1 
HETATM 5406 O  O    . HOH   E 4 .   ? 8.00200   -20.18300 12.62900  1.000 16.14802  ? 572  HOH   A O    1 
HETATM 5407 O  O    . HOH   E 4 .   ? 22.44900  -30.88500 1.39500   1.000 26.79041  ? 573  HOH   A O    1 
HETATM 5408 O  O    . HOH   E 4 .   ? 20.00600  -41.59500 12.00300  1.000 38.52983  ? 574  HOH   A O    1 
HETATM 5409 O  O    . HOH   E 4 .   ? 7.79800   -5.68700  27.10200  1.000 28.57762  ? 575  HOH   A O    1 
HETATM 5410 O  O    . HOH   E 4 .   ? 20.70700  -22.66800 -9.02000  1.000 29.77171  ? 576  HOH   A O    1 
HETATM 5411 O  O    . HOH   E 4 .   ? -0.91500  -28.19100 24.28800  1.000 17.73840  ? 577  HOH   A O    1 
HETATM 5412 O  O    . HOH   E 4 .   ? 7.23000   -18.06300 19.19800  1.000 20.04809  ? 578  HOH   A O    1 
HETATM 5413 O  O    . HOH   E 4 .   ? -11.85000 -13.32300 12.48200  1.000 23.08133  ? 579  HOH   A O    1 
HETATM 5414 O  O    . HOH   E 4 .   ? 30.15300  -31.72900 17.04900  1.000 47.63426  ? 580  HOH   A O    1 
HETATM 5415 O  O    . HOH   E 4 .   ? 29.62600  -2.24300  11.37200  1.000 33.26581  ? 581  HOH   A O    1 
HETATM 5416 O  O    . HOH   E 4 .   ? 4.05500   -34.92700 24.27400  1.000 29.35292  ? 582  HOH   A O    1 
HETATM 5417 O  O    . HOH   E 4 .   ? -10.43500 -31.19200 4.36300   1.000 28.55433  ? 583  HOH   A O    1 
HETATM 5418 O  O    . HOH   E 4 .   ? -10.49900 -11.05900 8.54600   1.000 27.18030  ? 584  HOH   A O    1 
HETATM 5419 O  O    . HOH   E 4 .   ? 26.995    -6.539    13.663    1.000 25.51431  ? 585  HOH   A O    1 
HETATM 5420 O  O    . HOH   E 4 .   ? 3.57100   1.53700   21.68300  1.000 39.40787  ? 586  HOH   A O    1 
HETATM 5421 O  O    . HOH   E 4 .   ? -13.49100 -12.50400 21.36300  1.000 34.44970  ? 587  HOH   A O    1 
HETATM 5422 O  O    . HOH   E 4 .   ? 19.28200  -35.19500 17.44900  1.000 29.51389  ? 588  HOH   A O    1 
HETATM 5423 O  O    . HOH   E 4 .   ? 26.85200  -14.89900 -9.61600  1.000 22.38619  ? 589  HOH   A O    1 
HETATM 5424 O  O    . HOH   E 4 .   ? 14.23800  -16.44200 15.54200  1.000 28.89531  ? 590  HOH   A O    1 
HETATM 5425 O  O    . HOH   E 4 .   ? 20.41900  -10.65600 24.76900  1.000 34.87957  ? 591  HOH   A O    1 
HETATM 5426 O  O    . HOH   E 4 .   ? 27.83600  -26.82400 18.70800  1.000 33.74505  ? 592  HOH   A O    1 
HETATM 5427 O  O    . HOH   E 4 .   ? 15.25300  -15.12700 16.93100  1.000 32.27239  ? 593  HOH   A O    1 
HETATM 5428 O  O    . HOH   E 4 .   ? 7.86400   -14.09200 25.82600  1.000 22.38338  ? 594  HOH   A O    1 
HETATM 5429 O  O    . HOH   E 4 .   ? 24.53500  0.38000   0.23700   1.000 31.66167  ? 595  HOH   A O    1 
HETATM 5430 O  O    . HOH   E 4 .   ? 9.93600   -15.81600 25.16300  1.000 27.12967  ? 596  HOH   A O    1 
HETATM 5431 O  O    . HOH   E 4 .   ? 19.24800  0.60800   -3.84800  1.000 34.45027  ? 597  HOH   A O    1 
HETATM 5432 O  O    . HOH   E 4 .   ? -3.73500  -23.84400 24.23400  1.000 24.62589  ? 598  HOH   A O    1 
HETATM 5433 O  O    . HOH   E 4 .   ? 19.94000  -8.17700  25.07800  1.000 18.44504  ? 599  HOH   A O    1 
HETATM 5434 O  O    . HOH   E 4 .   ? 1.61800   -18.04200 27.96400  1.000 27.10826  ? 600  HOH   A O    1 
HETATM 5435 O  O    . HOH   E 4 .   ? -6.57800  -24.25100 19.67700  1.000 28.52004  ? 601  HOH   A O    1 
HETATM 5436 O  O    . HOH   E 4 .   ? 15.59000  -14.38000 23.85900  1.000 32.40562  ? 602  HOH   A O    1 
HETATM 5437 O  O    . HOH   E 4 .   ? -4.28800  3.91000   14.05600  1.000 39.41570  ? 603  HOH   A O    1 
HETATM 5438 O  O    . HOH   E 4 .   ? -2.77500  -37.86500 2.81000   1.000 26.57687  ? 604  HOH   A O    1 
HETATM 5439 O  O    . HOH   E 4 .   ? -9.152    -32.599   21.371    1.000 25.33752  ? 605  HOH   A O    1 
HETATM 5440 O  O    . HOH   E 4 .   ? 8.58000   -39.71300 -1.68700  1.000 31.01370  ? 606  HOH   A O    1 
HETATM 5441 O  O    . HOH   E 4 .   ? 9.71500   -20.07300 24.31800  1.000 29.00145  ? 607  HOH   A O    1 
HETATM 5442 O  O    . HOH   E 4 .   ? 13.84700  -23.83700 -8.84600  1.000 23.49177  ? 608  HOH   A O    1 
HETATM 5443 O  O    . HOH   E 4 .   ? 6.01600   -37.61300 23.83300  1.000 36.86942  ? 609  HOH   A O    1 
HETATM 5444 O  O    . HOH   E 4 .   ? 14.34500  -30.71700 25.81000  1.000 40.23166  ? 610  HOH   A O    1 
HETATM 5445 O  O    . HOH   E 4 .   ? 26.65300  -9.63700  -6.75700  1.000 28.57161  ? 611  HOH   A O    1 
HETATM 5446 O  O    . HOH   E 4 .   ? -7.252    -29.626   -3.443    1.000 21.58431  ? 612  HOH   A O    1 
HETATM 5447 O  O    . HOH   E 4 .   ? 6.96700   5.41600   6.89900   1.000 29.06691  ? 613  HOH   A O    1 
HETATM 5448 O  O    . HOH   E 4 .   ? 19.56500  -37.56200 0.80700   1.000 33.89095  ? 614  HOH   A O    1 
HETATM 5449 O  O    . HOH   E 4 .   ? 16.91200  -30.28500 18.30000  1.000 25.00633  ? 615  HOH   A O    1 
HETATM 5450 O  O    . HOH   E 4 .   ? 9.66400   -20.38000 16.96700  1.000 24.46375  ? 616  HOH   A O    1 
HETATM 5451 O  O    . HOH   E 4 .   ? 15.21700  -33.37900 19.92300  1.000 30.03885  ? 617  HOH   A O    1 
HETATM 5452 O  O    . HOH   E 4 .   ? 10.40800  -2.17300  -7.12700  1.000 30.12694  ? 618  HOH   A O    1 
HETATM 5453 O  O    . HOH   E 4 .   ? -13.96100 -16.15500 19.63000  1.000 17.67341  ? 619  HOH   A O    1 
HETATM 5454 O  O    . HOH   E 4 .   ? 12.88700  -0.11400  18.11800  1.000 21.02375  ? 620  HOH   A O    1 
HETATM 5455 O  O    . HOH   E 4 .   ? -1.50200  -1.44500  1.24300   1.000 22.73222  ? 621  HOH   A O    1 
HETATM 5456 O  O    . HOH   E 4 .   ? 17.64000  -32.74000 19.70200  1.000 29.55597  ? 622  HOH   A O    1 
HETATM 5457 O  O    . HOH   E 4 .   ? 10.52700  -16.07500 17.23000  1.000 26.72891  ? 623  HOH   A O    1 
HETATM 5458 O  O    . HOH   E 4 .   ? 17.10900  -40.53300 1.63800   1.000 34.97490  ? 624  HOH   A O    1 
HETATM 5459 O  O    . HOH   E 4 .   ? 12.39600  -20.71100 18.60700  1.000 27.23897  ? 625  HOH   A O    1 
HETATM 5460 O  O    . HOH   E 4 .   ? -9.85000  -0.29000  12.94100  1.000 32.01118  ? 626  HOH   A O    1 
HETATM 5461 O  O    . HOH   E 4 .   ? -15.49800 -6.51700  14.67800  1.000 36.09949  ? 627  HOH   A O    1 
HETATM 5462 O  O    . HOH   E 4 .   ? -2.03100  -46.91800 20.71200  1.000 37.76370  ? 628  HOH   A O    1 
HETATM 5463 O  O    . HOH   E 4 .   ? 2.46000   -50.14000 22.27700  1.000 32.98216  ? 629  HOH   A O    1 
HETATM 5464 O  O    . HOH   E 4 .   ? -8.19800  3.94700   11.56700  1.000 36.87806  ? 630  HOH   A O    1 
HETATM 5465 O  O    . HOH   E 4 .   ? 4.23100   -49.28800 26.27400  1.000 31.22701  ? 631  HOH   A O    1 
HETATM 5466 O  O    . HOH   E 4 .   ? -6.53800  -48.52200 3.00600   1.000 39.76162  ? 632  HOH   A O    1 
# 
