data_9B9H
# 
_entry.id   9B9H 
# 
_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   9B9H         pdb_00009b9h 10.2210/pdb9b9h/pdb 
WWPDB D_1000282921 ?            ?                   
# 
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                        9B9H 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-02 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_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 
'Wilson, B.J.'   2 0009-0003-1132-8095 
'Alvarez, H.G.'  3 0000-0001-6990-169X 
'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'-({(17E)-18-[(3P)-4-{[(1S)-3-amino-1-(3-chloro-4-fluorophenyl)-3-oxopropyl]carbamoyl}-3-(4-chloro-2-fluorophenyl)-1H-pyrrol-2-yl]-16-oxo-3,6,9,12-tetraoxa-15-azaoctadec-17-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
;
1255.093  1   ?        ? ?                    ? 
4 water       nat water 18.015    310 ?        ? ?                    ? 
# 
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'-({(17E)-18-[(3P)-4-{[(1S)-3-amino-1-(3-chloro-4-fluorophenyl)-3-oxopropyl]carbamoyl}-3-(4-chloro-2-fluorophenyl)-1H-pyrrol-2-yl]-16-oxo-3,6,9,12-tetraoxa-15-azaoctadec-17-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
;
A1AM2 
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 ? ? ? ? ? ? ? ? 
'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
A1AM2 non-polymer         . 
;N-{(1P)-5'-({(17E)-18-[(3P)-4-{[(1S)-3-amino-1-(3-chloro-4-fluorophenyl)-3-oxopropyl]carbamoyl}-3-(4-chloro-2-fluorophenyl)-1H-pyrrol-2-yl]-16-oxo-3,6,9,12-tetraoxa-15-azaoctadec-17-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-40333 'C60 H63 Cl2 F6 N9 O10' 1255.093 
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 1079 ALA ALA 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   28   PRO PRO A . n 
B 2 24  THR 24  29   29   THR THR A . n 
B 2 25  PRO 25  30   30   PRO PRO 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        A1AM2 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AM2 
_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 A1AM2 1   1401 1401 A1AM2 OIC A . 
D 4 HOH   1   1401 153  HOH   HOH B . 
D 4 HOH   2   1402 232  HOH   HOH B . 
D 4 HOH   3   1403 244  HOH   HOH B . 
D 4 HOH   4   1404 312  HOH   HOH B . 
D 4 HOH   5   1405 207  HOH   HOH B . 
D 4 HOH   6   1406 292  HOH   HOH B . 
D 4 HOH   7   1407 149  HOH   HOH B . 
D 4 HOH   8   1408 291  HOH   HOH B . 
D 4 HOH   9   1409 48   HOH   HOH B . 
D 4 HOH   10  1410 101  HOH   HOH B . 
D 4 HOH   11  1411 264  HOH   HOH B . 
D 4 HOH   12  1412 253  HOH   HOH B . 
D 4 HOH   13  1413 36   HOH   HOH B . 
D 4 HOH   14  1414 166  HOH   HOH B . 
D 4 HOH   15  1415 31   HOH   HOH B . 
D 4 HOH   16  1416 47   HOH   HOH B . 
D 4 HOH   17  1417 103  HOH   HOH B . 
D 4 HOH   18  1418 235  HOH   HOH B . 
D 4 HOH   19  1419 75   HOH   HOH B . 
D 4 HOH   20  1420 126  HOH   HOH B . 
D 4 HOH   21  1421 96   HOH   HOH B . 
D 4 HOH   22  1422 73   HOH   HOH B . 
D 4 HOH   23  1423 190  HOH   HOH B . 
D 4 HOH   24  1424 305  HOH   HOH B . 
D 4 HOH   25  1425 59   HOH   HOH B . 
D 4 HOH   26  1426 104  HOH   HOH B . 
D 4 HOH   27  1427 15   HOH   HOH B . 
D 4 HOH   28  1428 60   HOH   HOH B . 
D 4 HOH   29  1429 156  HOH   HOH B . 
D 4 HOH   30  1430 22   HOH   HOH B . 
D 4 HOH   31  1431 77   HOH   HOH B . 
D 4 HOH   32  1432 117  HOH   HOH B . 
D 4 HOH   33  1433 4    HOH   HOH B . 
D 4 HOH   34  1434 119  HOH   HOH B . 
D 4 HOH   35  1435 338  HOH   HOH B . 
D 4 HOH   36  1436 42   HOH   HOH B . 
D 4 HOH   37  1437 339  HOH   HOH B . 
D 4 HOH   38  1438 124  HOH   HOH B . 
D 4 HOH   39  1439 69   HOH   HOH B . 
D 4 HOH   40  1440 102  HOH   HOH B . 
D 4 HOH   41  1441 313  HOH   HOH B . 
D 4 HOH   42  1442 37   HOH   HOH B . 
D 4 HOH   43  1443 94   HOH   HOH B . 
D 4 HOH   44  1444 201  HOH   HOH B . 
D 4 HOH   45  1445 335  HOH   HOH B . 
D 4 HOH   46  1446 240  HOH   HOH B . 
D 4 HOH   47  1447 53   HOH   HOH B . 
D 4 HOH   48  1448 20   HOH   HOH B . 
D 4 HOH   49  1449 121  HOH   HOH B . 
D 4 HOH   50  1450 252  HOH   HOH B . 
D 4 HOH   51  1451 35   HOH   HOH B . 
D 4 HOH   52  1452 151  HOH   HOH B . 
D 4 HOH   53  1453 189  HOH   HOH B . 
D 4 HOH   54  1454 181  HOH   HOH B . 
D 4 HOH   55  1455 195  HOH   HOH B . 
D 4 HOH   56  1456 197  HOH   HOH B . 
D 4 HOH   57  1457 125  HOH   HOH B . 
D 4 HOH   58  1458 6    HOH   HOH B . 
D 4 HOH   59  1459 309  HOH   HOH B . 
D 4 HOH   60  1460 172  HOH   HOH B . 
D 4 HOH   61  1461 141  HOH   HOH B . 
D 4 HOH   62  1462 24   HOH   HOH B . 
D 4 HOH   63  1463 78   HOH   HOH B . 
D 4 HOH   64  1464 283  HOH   HOH B . 
D 4 HOH   65  1465 263  HOH   HOH B . 
D 4 HOH   66  1466 55   HOH   HOH B . 
D 4 HOH   67  1467 310  HOH   HOH B . 
D 4 HOH   68  1468 154  HOH   HOH B . 
D 4 HOH   69  1469 182  HOH   HOH B . 
D 4 HOH   70  1470 336  HOH   HOH B . 
D 4 HOH   71  1471 204  HOH   HOH B . 
D 4 HOH   72  1472 89   HOH   HOH B . 
D 4 HOH   73  1473 30   HOH   HOH B . 
D 4 HOH   74  1474 133  HOH   HOH B . 
D 4 HOH   75  1475 66   HOH   HOH B . 
D 4 HOH   76  1476 170  HOH   HOH B . 
D 4 HOH   77  1477 306  HOH   HOH B . 
D 4 HOH   78  1478 241  HOH   HOH B . 
D 4 HOH   79  1479 198  HOH   HOH B . 
D 4 HOH   80  1480 215  HOH   HOH B . 
D 4 HOH   81  1481 85   HOH   HOH B . 
D 4 HOH   82  1482 112  HOH   HOH B . 
D 4 HOH   83  1483 245  HOH   HOH B . 
D 4 HOH   84  1484 62   HOH   HOH B . 
D 4 HOH   85  1485 158  HOH   HOH B . 
D 4 HOH   86  1486 39   HOH   HOH B . 
D 4 HOH   87  1487 81   HOH   HOH B . 
D 4 HOH   88  1488 279  HOH   HOH B . 
D 4 HOH   89  1489 7    HOH   HOH B . 
D 4 HOH   90  1490 345  HOH   HOH B . 
D 4 HOH   91  1491 281  HOH   HOH B . 
D 4 HOH   92  1492 243  HOH   HOH B . 
D 4 HOH   93  1493 27   HOH   HOH B . 
D 4 HOH   94  1494 290  HOH   HOH B . 
D 4 HOH   95  1495 164  HOH   HOH B . 
D 4 HOH   96  1496 237  HOH   HOH B . 
D 4 HOH   97  1497 332  HOH   HOH B . 
D 4 HOH   98  1498 220  HOH   HOH B . 
D 4 HOH   99  1499 134  HOH   HOH B . 
D 4 HOH   100 1500 300  HOH   HOH B . 
D 4 HOH   101 1501 280  HOH   HOH B . 
D 4 HOH   102 1502 32   HOH   HOH B . 
D 4 HOH   103 1503 317  HOH   HOH B . 
D 4 HOH   104 1504 150  HOH   HOH B . 
D 4 HOH   105 1505 324  HOH   HOH B . 
D 4 HOH   106 1506 239  HOH   HOH B . 
D 4 HOH   107 1507 334  HOH   HOH B . 
D 4 HOH   108 1508 328  HOH   HOH B . 
D 4 HOH   109 1509 265  HOH   HOH B . 
D 4 HOH   110 1510 167  HOH   HOH B . 
D 4 HOH   111 1511 308  HOH   HOH B . 
D 4 HOH   112 1512 288  HOH   HOH B . 
D 4 HOH   113 1513 185  HOH   HOH B . 
D 4 HOH   114 1514 347  HOH   HOH B . 
D 4 HOH   115 1515 295  HOH   HOH B . 
D 4 HOH   116 1516 250  HOH   HOH B . 
D 4 HOH   117 1517 350  HOH   HOH B . 
D 4 HOH   118 1518 323  HOH   HOH B . 
D 4 HOH   119 1519 203  HOH   HOH B . 
D 4 HOH   120 1520 299  HOH   HOH B . 
D 4 HOH   121 1521 351  HOH   HOH B . 
D 4 HOH   122 1522 139  HOH   HOH B . 
D 4 HOH   123 1523 140  HOH   HOH B . 
D 4 HOH   124 1524 318  HOH   HOH B . 
D 4 HOH   125 1525 260  HOH   HOH B . 
D 4 HOH   126 1526 230  HOH   HOH B . 
D 4 HOH   127 1527 261  HOH   HOH B . 
D 4 HOH   128 1528 311  HOH   HOH B . 
D 4 HOH   129 1529 267  HOH   HOH B . 
D 4 HOH   130 1530 171  HOH   HOH B . 
D 4 HOH   131 1531 127  HOH   HOH B . 
D 4 HOH   132 1532 297  HOH   HOH B . 
D 4 HOH   133 1533 217  HOH   HOH B . 
D 4 HOH   134 1534 272  HOH   HOH B . 
D 4 HOH   135 1535 319  HOH   HOH B . 
D 4 HOH   136 1536 168  HOH   HOH B . 
D 4 HOH   137 1537 314  HOH   HOH B . 
D 4 HOH   138 1538 348  HOH   HOH B . 
D 4 HOH   139 1539 268  HOH   HOH B . 
D 4 HOH   140 1540 344  HOH   HOH B . 
D 4 HOH   141 1541 285  HOH   HOH B . 
D 4 HOH   142 1542 58   HOH   HOH B . 
D 4 HOH   143 1543 271  HOH   HOH B . 
E 4 HOH   1   1501 67   HOH   HOH A . 
E 4 HOH   2   1502 256  HOH   HOH A . 
E 4 HOH   3   1503 303  HOH   HOH A . 
E 4 HOH   4   1504 109  HOH   HOH A . 
E 4 HOH   5   1505 254  HOH   HOH A . 
E 4 HOH   6   1506 61   HOH   HOH A . 
E 4 HOH   7   1507 349  HOH   HOH A . 
E 4 HOH   8   1508 49   HOH   HOH A . 
E 4 HOH   9   1509 179  HOH   HOH A . 
E 4 HOH   10  1510 14   HOH   HOH A . 
E 4 HOH   11  1511 100  HOH   HOH A . 
E 4 HOH   12  1512 229  HOH   HOH A . 
E 4 HOH   13  1513 270  HOH   HOH A . 
E 4 HOH   14  1514 114  HOH   HOH A . 
E 4 HOH   15  1515 296  HOH   HOH A . 
E 4 HOH   16  1516 132  HOH   HOH A . 
E 4 HOH   17  1517 98   HOH   HOH A . 
E 4 HOH   18  1518 65   HOH   HOH A . 
E 4 HOH   19  1519 3    HOH   HOH A . 
E 4 HOH   20  1520 72   HOH   HOH A . 
E 4 HOH   21  1521 212  HOH   HOH A . 
E 4 HOH   22  1522 68   HOH   HOH A . 
E 4 HOH   23  1523 46   HOH   HOH A . 
E 4 HOH   24  1524 259  HOH   HOH A . 
E 4 HOH   25  1525 2    HOH   HOH A . 
E 4 HOH   26  1526 108  HOH   HOH A . 
E 4 HOH   27  1527 273  HOH   HOH A . 
E 4 HOH   28  1528 23   HOH   HOH A . 
E 4 HOH   29  1529 143  HOH   HOH A . 
E 4 HOH   30  1530 337  HOH   HOH A . 
E 4 HOH   31  1531 18   HOH   HOH A . 
E 4 HOH   32  1532 180  HOH   HOH A . 
E 4 HOH   33  1533 52   HOH   HOH A . 
E 4 HOH   34  1534 294  HOH   HOH A . 
E 4 HOH   35  1535 202  HOH   HOH A . 
E 4 HOH   36  1536 342  HOH   HOH A . 
E 4 HOH   37  1537 16   HOH   HOH A . 
E 4 HOH   38  1538 206  HOH   HOH A . 
E 4 HOH   39  1539 63   HOH   HOH A . 
E 4 HOH   40  1540 242  HOH   HOH A . 
E 4 HOH   41  1541 187  HOH   HOH A . 
E 4 HOH   42  1542 113  HOH   HOH A . 
E 4 HOH   43  1543 115  HOH   HOH A . 
E 4 HOH   44  1544 209  HOH   HOH A . 
E 4 HOH   45  1545 188  HOH   HOH A . 
E 4 HOH   46  1546 157  HOH   HOH A . 
E 4 HOH   47  1547 118  HOH   HOH A . 
E 4 HOH   48  1548 74   HOH   HOH A . 
E 4 HOH   49  1549 97   HOH   HOH A . 
E 4 HOH   50  1550 26   HOH   HOH A . 
E 4 HOH   51  1551 231  HOH   HOH A . 
E 4 HOH   52  1552 90   HOH   HOH A . 
E 4 HOH   53  1553 205  HOH   HOH A . 
E 4 HOH   54  1554 40   HOH   HOH A . 
E 4 HOH   55  1555 11   HOH   HOH A . 
E 4 HOH   56  1556 95   HOH   HOH A . 
E 4 HOH   57  1557 71   HOH   HOH A . 
E 4 HOH   58  1558 54   HOH   HOH A . 
E 4 HOH   59  1559 34   HOH   HOH A . 
E 4 HOH   60  1560 144  HOH   HOH A . 
E 4 HOH   61  1561 111  HOH   HOH A . 
E 4 HOH   62  1562 84   HOH   HOH A . 
E 4 HOH   63  1563 9    HOH   HOH A . 
E 4 HOH   64  1564 44   HOH   HOH A . 
E 4 HOH   65  1565 120  HOH   HOH A . 
E 4 HOH   66  1566 105  HOH   HOH A . 
E 4 HOH   67  1567 200  HOH   HOH A . 
E 4 HOH   68  1568 70   HOH   HOH A . 
E 4 HOH   69  1569 148  HOH   HOH A . 
E 4 HOH   70  1570 56   HOH   HOH A . 
E 4 HOH   71  1571 211  HOH   HOH A . 
E 4 HOH   72  1572 45   HOH   HOH A . 
E 4 HOH   73  1573 129  HOH   HOH A . 
E 4 HOH   74  1574 38   HOH   HOH A . 
E 4 HOH   75  1575 12   HOH   HOH A . 
E 4 HOH   76  1576 106  HOH   HOH A . 
E 4 HOH   77  1577 196  HOH   HOH A . 
E 4 HOH   78  1578 161  HOH   HOH A . 
E 4 HOH   79  1579 92   HOH   HOH A . 
E 4 HOH   80  1580 214  HOH   HOH A . 
E 4 HOH   81  1581 159  HOH   HOH A . 
E 4 HOH   82  1582 146  HOH   HOH A . 
E 4 HOH   83  1583 138  HOH   HOH A . 
E 4 HOH   84  1584 228  HOH   HOH A . 
E 4 HOH   85  1585 131  HOH   HOH A . 
E 4 HOH   86  1586 176  HOH   HOH A . 
E 4 HOH   87  1587 186  HOH   HOH A . 
E 4 HOH   88  1588 274  HOH   HOH A . 
E 4 HOH   89  1589 223  HOH   HOH A . 
E 4 HOH   90  1590 25   HOH   HOH A . 
E 4 HOH   91  1591 116  HOH   HOH A . 
E 4 HOH   92  1592 43   HOH   HOH A . 
E 4 HOH   93  1593 277  HOH   HOH A . 
E 4 HOH   94  1594 225  HOH   HOH A . 
E 4 HOH   95  1595 142  HOH   HOH A . 
E 4 HOH   96  1596 136  HOH   HOH A . 
E 4 HOH   97  1597 208  HOH   HOH A . 
E 4 HOH   98  1598 88   HOH   HOH A . 
E 4 HOH   99  1599 80   HOH   HOH A . 
E 4 HOH   100 1600 222  HOH   HOH A . 
E 4 HOH   101 1601 236  HOH   HOH A . 
E 4 HOH   102 1602 33   HOH   HOH A . 
E 4 HOH   103 1603 340  HOH   HOH A . 
E 4 HOH   104 1604 175  HOH   HOH A . 
E 4 HOH   105 1605 107  HOH   HOH A . 
E 4 HOH   106 1606 163  HOH   HOH A . 
E 4 HOH   107 1607 160  HOH   HOH A . 
E 4 HOH   108 1608 329  HOH   HOH A . 
E 4 HOH   109 1609 28   HOH   HOH A . 
E 4 HOH   110 1610 99   HOH   HOH A . 
E 4 HOH   111 1611 123  HOH   HOH A . 
E 4 HOH   112 1612 257  HOH   HOH A . 
E 4 HOH   113 1613 57   HOH   HOH A . 
E 4 HOH   114 1614 287  HOH   HOH A . 
E 4 HOH   115 1615 79   HOH   HOH A . 
E 4 HOH   116 1616 29   HOH   HOH A . 
E 4 HOH   117 1617 93   HOH   HOH A . 
E 4 HOH   118 1618 183  HOH   HOH A . 
E 4 HOH   119 1619 87   HOH   HOH A . 
E 4 HOH   120 1620 173  HOH   HOH A . 
E 4 HOH   121 1621 83   HOH   HOH A . 
E 4 HOH   122 1622 210  HOH   HOH A . 
E 4 HOH   123 1623 145  HOH   HOH A . 
E 4 HOH   124 1624 219  HOH   HOH A . 
E 4 HOH   125 1625 199  HOH   HOH A . 
E 4 HOH   126 1626 50   HOH   HOH A . 
E 4 HOH   127 1627 221  HOH   HOH A . 
E 4 HOH   128 1628 226  HOH   HOH A . 
E 4 HOH   129 1629 82   HOH   HOH A . 
E 4 HOH   130 1630 321  HOH   HOH A . 
E 4 HOH   131 1631 137  HOH   HOH A . 
E 4 HOH   132 1632 13   HOH   HOH A . 
E 4 HOH   133 1633 128  HOH   HOH A . 
E 4 HOH   134 1634 289  HOH   HOH A . 
E 4 HOH   135 1635 307  HOH   HOH A . 
E 4 HOH   136 1636 193  HOH   HOH A . 
E 4 HOH   137 1637 51   HOH   HOH A . 
E 4 HOH   138 1638 326  HOH   HOH A . 
E 4 HOH   139 1639 330  HOH   HOH A . 
E 4 HOH   140 1640 169  HOH   HOH A . 
E 4 HOH   141 1641 275  HOH   HOH A . 
E 4 HOH   142 1642 233  HOH   HOH A . 
E 4 HOH   143 1643 110  HOH   HOH A . 
E 4 HOH   144 1644 269  HOH   HOH A . 
E 4 HOH   145 1645 298  HOH   HOH A . 
E 4 HOH   146 1646 76   HOH   HOH A . 
E 4 HOH   147 1647 258  HOH   HOH A . 
E 4 HOH   148 1648 246  HOH   HOH A . 
E 4 HOH   149 1649 286  HOH   HOH A . 
E 4 HOH   150 1650 218  HOH   HOH A . 
E 4 HOH   151 1651 278  HOH   HOH A . 
E 4 HOH   152 1652 224  HOH   HOH A . 
E 4 HOH   153 1653 341  HOH   HOH A . 
E 4 HOH   154 1654 262  HOH   HOH A . 
E 4 HOH   155 1655 234  HOH   HOH A . 
E 4 HOH   156 1656 316  HOH   HOH A . 
E 4 HOH   157 1657 216  HOH   HOH A . 
E 4 HOH   158 1658 135  HOH   HOH A . 
E 4 HOH   159 1659 122  HOH   HOH A . 
E 4 HOH   160 1660 227  HOH   HOH A . 
E 4 HOH   161 1661 174  HOH   HOH A . 
E 4 HOH   162 1662 184  HOH   HOH A . 
E 4 HOH   163 1663 191  HOH   HOH A . 
E 4 HOH   164 1664 302  HOH   HOH A . 
E 4 HOH   165 1665 322  HOH   HOH A . 
E 4 HOH   166 1666 284  HOH   HOH A . 
E 4 HOH   167 1667 315  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_5207 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS       ? ? ? .         2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? pointless ? ? ? .         3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER    ? ? ? .         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                     9B9H 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     84.213 
_cell.length_a_esd                 ? 
_cell.length_b                     85.143 
_cell.length_b_esd                 ? 
_cell.length_c                     111.644 
_cell.length_c_esd                 ? 
_cell.volume                       800503.943 
_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                         9B9H 
_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                   9B9H 
_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             2.89 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          57.49 
_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              ? 
_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    '5% w/v 1-ethyl-3-methylimidazolium ethyl sulfate, 15% w/v polyethylene glycol 20,000, pH 7.9' 
_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 PILATUS3 S 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-02-14 
_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   1.1808 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'CLSI BEAMLINE 08B1-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.1808 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   08B1-1 
_diffrn_source.pdbx_synchrotron_site       CLSI 
# 
_reflns.B_iso_Wilson_estimate                          37.78 
_reflns.entry_id                                       9B9H 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.06 
_reflns.d_resolution_low                               42.57 
_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                                     49405 
_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                           95.17 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          25.11 
_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                                0.02298 
_reflns.pdbx_Rpim_I_all                                0.01625 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1 
_reflns.pdbx_CC_star                                   1 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.01625 
_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                                    2.06 
_reflns_shell.d_res_low                                     2.10 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.05 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2399 
_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                               0.9062 
_reflns_shell.pdbx_Rpim_I_all                               0.6408 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.952 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.6408 
_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                               46.56 
_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                                 9B9H 
_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                            2.06 
_refine.ls_d_res_low                             42.57 
_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                     47891 
_refine.ls_number_reflns_R_free                  2395 
_refine.ls_number_reflns_R_work                  45496 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.18 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2117 
_refine.ls_R_factor_R_free                       0.2291 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2108 
_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                 27.7492 
_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                            0.2828 
_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                       2.06 
_refine_hist.d_res_low                        42.57 
_refine_hist.number_atoms_solvent             310 
_refine_hist.number_atoms_total               5256 
_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        4946 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_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' ? 0.6576  ? 5033 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.8364  ? 6820 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0523  ? 760  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0389  ? 871  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 13.9745 ? 1794 ? 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' 2.06 2.10  . . 106 1885 68.18  . . . . 0.5275 . . . . . . . . . . . 0.5826 
'X-RAY DIFFRACTION' 2.10 2.15  . . 152 2662 96.50  . . . . 0.3019 . . . . . . . . . . . 0.2933 
'X-RAY DIFFRACTION' 2.15 2.20  . . 160 2694 98.28  . . . . 0.2677 . . . . . . . . . . . 0.3307 
'X-RAY DIFFRACTION' 2.20 2.25  . . 103 2096 75.31  . . . . 0.3978 . . . . . . . . . . . 0.3864 
'X-RAY DIFFRACTION' 2.25 2.31  . . 136 2390 86.48  . . . . 0.2957 . . . . . . . . . . . 0.3415 
'X-RAY DIFFRACTION' 2.31 2.38  . . 133 2810 100.00 . . . . 0.2361 . . . . . . . . . . . 0.2906 
'X-RAY DIFFRACTION' 2.38 2.46  . . 154 2762 100.00 . . . . 0.2363 . . . . . . . . . . . 0.2553 
'X-RAY DIFFRACTION' 2.46 2.55  . . 111 2828 100.00 . . . . 0.2465 . . . . . . . . . . . 0.2952 
'X-RAY DIFFRACTION' 2.55 2.65  . . 136 2747 97.66  . . . . 0.2541 . . . . . . . . . . . 0.2777 
'X-RAY DIFFRACTION' 2.65 2.77  . . 127 2730 97.74  . . . . 0.2526 . . . . . . . . . . . 0.2846 
'X-RAY DIFFRACTION' 2.77 2.91  . . 176 2786 99.93  . . . . 0.2296 . . . . . . . . . . . 0.2620 
'X-RAY DIFFRACTION' 2.91 3.10  . . 143 2802 100.00 . . . . 0.2376 . . . . . . . . . . . 0.2338 
'X-RAY DIFFRACTION' 3.10 3.34  . . 162 2806 99.90  . . . . 0.2141 . . . . . . . . . . . 0.2300 
'X-RAY DIFFRACTION' 3.34 3.67  . . 149 2793 98.53  . . . . 0.2007 . . . . . . . . . . . 0.1996 
'X-RAY DIFFRACTION' 3.67 4.20  . . 151 2804 98.99  . . . . 0.1722 . . . . . . . . . . . 0.1969 
'X-RAY DIFFRACTION' 4.20 5.29  . . 131 2905 99.97  . . . . 0.1451 . . . . . . . . . . . 0.1583 
'X-RAY DIFFRACTION' 5.29 42.57 . . 165 2996 99.68  . . . . 0.1909 . . . . . . . . . . . 0.1848 
# 
_struct.entry_id                     9B9H 
_struct.title                        'Crystal structure of the ternary complex of DCAF1 and WDR5 with PROTAC, OICR-40333' 
_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        9B9H 
_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 9B9H B 28 ? 338 ? Q9Y4B6 1080 ? 1390 ? 1080 1390 
2 2 9B9H 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 9B9H MET B 1  ? UNP Q9Y4B6 ? ? 'initiating methionine' 1053 1  
1 9B9H GLY B 2  ? UNP Q9Y4B6 ? ? 'expression tag'        1054 2  
1 9B9H SER B 3  ? UNP Q9Y4B6 ? ? 'expression tag'        1055 3  
1 9B9H SER B 4  ? UNP Q9Y4B6 ? ? 'expression tag'        1056 4  
1 9B9H HIS B 5  ? UNP Q9Y4B6 ? ? 'expression tag'        1057 5  
1 9B9H HIS B 6  ? UNP Q9Y4B6 ? ? 'expression tag'        1058 6  
1 9B9H HIS B 7  ? UNP Q9Y4B6 ? ? 'expression tag'        1059 7  
1 9B9H HIS B 8  ? UNP Q9Y4B6 ? ? 'expression tag'        1060 8  
1 9B9H HIS B 9  ? UNP Q9Y4B6 ? ? 'expression tag'        1061 9  
1 9B9H HIS B 10 ? UNP Q9Y4B6 ? ? 'expression tag'        1062 10 
1 9B9H SER B 11 ? UNP Q9Y4B6 ? ? 'expression tag'        1063 11 
1 9B9H SER B 12 ? UNP Q9Y4B6 ? ? 'expression tag'        1064 12 
1 9B9H GLY B 13 ? UNP Q9Y4B6 ? ? 'expression tag'        1065 13 
1 9B9H ARG B 14 ? UNP Q9Y4B6 ? ? 'expression tag'        1066 14 
1 9B9H GLU B 15 ? UNP Q9Y4B6 ? ? 'expression tag'        1067 15 
1 9B9H ASN B 16 ? UNP Q9Y4B6 ? ? 'expression tag'        1068 16 
1 9B9H LEU B 17 ? UNP Q9Y4B6 ? ? 'expression tag'        1069 17 
1 9B9H TYR B 18 ? UNP Q9Y4B6 ? ? 'expression tag'        1070 18 
1 9B9H PHE B 19 ? UNP Q9Y4B6 ? ? 'expression tag'        1071 19 
1 9B9H GLN B 20 ? UNP Q9Y4B6 ? ? 'expression tag'        1072 20 
1 9B9H GLY B 21 ? UNP Q9Y4B6 ? ? 'expression tag'        1073 21 
1 9B9H SER B 22 ? UNP Q9Y4B6 ? ? 'expression tag'        1074 22 
1 9B9H SER B 23 ? UNP Q9Y4B6 ? ? 'expression tag'        1075 23 
1 9B9H ARG B 24 ? UNP Q9Y4B6 ? ? 'expression tag'        1076 24 
1 9B9H ALA B 25 ? UNP Q9Y4B6 ? ? 'expression tag'        1077 25 
1 9B9H SER B 26 ? UNP Q9Y4B6 ? ? 'expression tag'        1078 26 
1 9B9H ALA B 27 ? UNP Q9Y4B6 ? ? 'expression tag'        1079 27 
2 9B9H MET A 1  ? UNP P61964 ? ? 'initiating methionine' 6    28 
2 9B9H HIS A 2  ? UNP P61964 ? ? 'expression tag'        7    29 
2 9B9H HIS A 3  ? UNP P61964 ? ? 'expression tag'        8    30 
2 9B9H HIS A 4  ? UNP P61964 ? ? 'expression tag'        9    31 
2 9B9H HIS A 5  ? UNP P61964 ? ? 'expression tag'        10   32 
2 9B9H HIS A 6  ? UNP P61964 ? ? 'expression tag'        11   33 
2 9B9H HIS A 7  ? UNP P61964 ? ? 'expression tag'        12   34 
2 9B9H SER A 8  ? UNP P61964 ? ? 'expression tag'        13   35 
2 9B9H SER A 9  ? UNP P61964 ? ? 'expression tag'        14   36 
2 9B9H GLY A 10 ? UNP P61964 ? ? 'expression tag'        15   37 
2 9B9H ARG A 11 ? UNP P61964 ? ? 'expression tag'        16   38 
2 9B9H GLU A 12 ? UNP P61964 ? ? 'expression tag'        17   39 
2 9B9H ASN A 13 ? UNP P61964 ? ? 'expression tag'        18   40 
2 9B9H LEU A 14 ? UNP P61964 ? ? 'expression tag'        19   41 
2 9B9H TYR A 15 ? UNP P61964 ? ? 'expression tag'        20   42 
2 9B9H PHE A 16 ? UNP P61964 ? ? 'expression tag'        21   43 
2 9B9H GLN A 17 ? UNP P61964 ? ? 'expression tag'        22   44 
2 9B9H 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_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 
# 
_struct_conf.conf_type_id            HELX_P 
_struct_conf.id                      HELX_P1 
_struct_conf.pdbx_PDB_helix_id       AA1 
_struct_conf.beg_label_comp_id       PRO 
_struct_conf.beg_label_asym_id       A 
_struct_conf.beg_label_seq_id        240 
_struct_conf.pdbx_beg_PDB_ins_code   ? 
_struct_conf.end_label_comp_id       ASP 
_struct_conf.end_label_asym_id       A 
_struct_conf.end_label_seq_id        243 
_struct_conf.pdbx_end_PDB_ins_code   ? 
_struct_conf.beg_auth_comp_id        PRO 
_struct_conf.beg_auth_asym_id        B 
_struct_conf.beg_auth_seq_id         1292 
_struct_conf.end_auth_comp_id        ASP 
_struct_conf.end_auth_asym_id        B 
_struct_conf.end_auth_seq_id         1295 
_struct_conf.pdbx_PDB_helix_class    5 
_struct_conf.details                 ? 
_struct_conf.pdbx_PDB_helix_length   4 
# 
_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       1.55 
# 
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 PHE A 28  ? ARG A 35  ? PHE B 1080 ARG B 1087 
AA1 2 THR A 330 ? VAL A 337 ? THR B 1382 VAL B 1389 
AA1 3 TYR A 313 ? ASN A 319 ? TYR B 1365 ASN B 1371 
AA1 4 ASN A 301 ? THR A 307 ? ASN B 1353 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 ILE A 86  ? PRO A 91  ? ILE B 1138 PRO B 1143 
AA3 2 LEU A 97  ? ALA A 102 ? LEU B 1149 ALA B 1154 
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 TYR B 30  ? LEU B 36  ? TYR A 35   LEU A 41   
AA8 2 ILE B 322 ? SER B 327 ? ILE A 327  SER A 332  
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 ILE B 64  ? GLY B 68  ? ILE A 69   GLY A 73   
AA9 4 PHE B 74  ? ILE B 78  ? PHE A 79   ILE A 83   
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 PHE A 34  ? N PHE B 1086 O CYS A 332 ? O CYS B 1384 
AA1 2 3 O VAL A 331 ? O VAL B 1383 N GLU A 318 ? N GLU B 1370 
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 GLY A 113 ? N GLY B 1165 O ASP A 119 ? O ASP B 1171 
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 LEU A 191 ? N LEU B 1243 O ILE A 200 ? O ILE B 1252 
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 66  ? N ILE A 71   O GLU B 75  ? O GLU A 80   
AB1 1 2 N ALA B 89  ? N ALA A 94   O VAL B 98  ? O VAL A 103  
AB1 2 3 N LEU B 97  ? N LEU A 102  O TRP B 109 ? O TRP A 114  
AB1 3 4 N ILE B 108 ? N ILE A 113  O LYS B 118 ? O LYS A 123  
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 CYS B 190 ? N CYS A 195  O LEU B 204 ? O LEU A 209  
AB4 1 2 N LYS B 216 ? N LYS A 221  O LEU B 225 ? O LEU A 230  
AB4 2 3 N ALA B 226 ? N ALA A 231  O LYS B 234 ? O LYS A 239  
AB4 3 4 N ASP B 237 ? N ASP A 242  O LYS B 242 ? O LYS A 247  
AB5 1 2 N SER B 262 ? N SER A 267  O TRP B 268 ? O TRP A 273  
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                   9B9H 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   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 O B HOH 1438 ? ? O B HOH 1491 ? ? 1.99 
2 1 O B HOH 1474 ? ? O B HOH 1533 ? ? 2.11 
3 1 O B HOH 1401 ? ? O B HOH 1512 ? ? 2.17 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 OD1 B ASP 1317 ? ? 1_555 NZ A LYS 227  ? ? 3_544 2.09 
2 1 O   B HOH 1463 ? ? 1_555 O  B HOH 1479 ? ? 4_545 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 ARG B 1106 ? ? 82.85   -1.54   
2  1 TRP B 1156 ? ? -156.85 66.13   
3  1 SER B 1168 ? ? 62.55   -99.79  
4  1 HIS B 1187 ? ? -70.58  -73.14  
5  1 PHE B 1215 ? ? -173.07 139.19  
6  1 HIS B 1253 ? ? -170.29 137.64  
7  1 ASN B 1261 ? ? -121.74 -51.17  
8  1 ASN B 1276 ? ? 53.18   -119.65 
9  1 PHE B 1285 ? ? 59.55   14.66   
10 1 ASP B 1317 ? ? 55.05   -133.52 
11 1 GLU B 1318 ? ? -154.17 -97.59  
12 1 ASP B 1319 ? ? -87.50  43.15   
13 1 GLU B 1323 ? ? 69.21   -27.50  
14 1 MET B 1326 ? ? 61.44   -112.96 
15 1 LYS B 1327 ? ? 72.58   -27.88  
16 1 TYR B 1342 ? ? 58.85   15.03   
17 1 ASN A 214  ? ? -118.10 62.38   
18 1 LEU A 234  ? ? -73.96  38.75   
19 1 LEU A 321  ? ? -90.10  -153.12 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     181 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.256 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
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 1542 ? 7.27 . 
2 1 O ? B HOH 1543 ? 7.58 . 
3 1 O ? A HOH 1666 ? 6.41 . 
4 1 O ? A HOH 1667 ? 7.10 . 
# 
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 A MET 6    ? B MET 1  
28 1 Y 1 A HIS 7    ? B HIS 2  
29 1 Y 1 A HIS 8    ? B HIS 3  
30 1 Y 1 A HIS 9    ? B HIS 4  
31 1 Y 1 A HIS 10   ? B HIS 5  
32 1 Y 1 A HIS 11   ? B HIS 6  
33 1 Y 1 A HIS 12   ? B HIS 7  
34 1 Y 1 A SER 13   ? B SER 8  
35 1 Y 1 A SER 14   ? B SER 9  
36 1 Y 1 A GLY 15   ? B GLY 10 
37 1 Y 1 A ARG 16   ? B ARG 11 
38 1 Y 1 A GLU 17   ? B GLU 12 
39 1 Y 1 A ASN 18   ? B ASN 13 
40 1 Y 1 A LEU 19   ? B LEU 14 
41 1 Y 1 A TYR 20   ? B TYR 15 
42 1 Y 1 A PHE 21   ? B PHE 16 
43 1 Y 1 A GLN 22   ? B GLN 17 
44 1 Y 1 A GLY 23   ? B GLY 18 
45 1 Y 1 A THR 24   ? B THR 19 
46 1 Y 1 A GLN 25   ? B GLN 20 
47 1 Y 1 A SER 26   ? B SER 21 
48 1 Y 1 A LYS 27   ? B LYS 22 
# 
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 
A1AM2 C01  C  N N 1   
A1AM2 C03  C  N S 2   
A1AM2 C04  C  N N 3   
A1AM2 C06  C  Y N 4   
A1AM2 C07  C  Y N 5   
A1AM2 C08  C  Y N 6   
A1AM2 C09  C  Y N 7   
A1AM2 C10  C  Y N 8   
A1AM2 C11  C  Y N 9   
A1AM2 C13  C  Y N 10  
A1AM2 C14  C  Y N 11  
A1AM2 C15  C  Y N 12  
A1AM2 C16  C  N N 13  
A1AM2 C19  C  N N 14  
A1AM2 C20  C  N N 15  
A1AM2 C22  C  N N 16  
A1AM2 C23  C  N N 17  
A1AM2 C25  C  N N 18  
A1AM2 C26  C  N N 19  
A1AM2 C28  C  N N 20  
A1AM2 C29  C  N N 21  
A1AM2 C31  C  N N 22  
A1AM2 C32  C  N N 23  
A1AM2 C34  C  N N 24  
A1AM2 C36  C  N N 25  
A1AM2 C37  C  N N 26  
A1AM2 C38  C  Y N 27  
A1AM2 C39  C  Y N 28  
A1AM2 C40  C  Y N 29  
A1AM2 C41  C  Y N 30  
A1AM2 C43  C  Y N 31  
A1AM2 C44  C  Y N 32  
A1AM2 C46  C  Y N 33  
A1AM2 C47  C  Y N 34  
A1AM2 C48  C  Y N 35  
A1AM2 C49  C  N N 36  
A1AM2 C52  C  N S 37  
A1AM2 C53  C  Y N 38  
A1AM2 C54  C  Y N 39  
A1AM2 C55  C  Y N 40  
A1AM2 C56  C  Y N 41  
A1AM2 C58  C  Y N 42  
A1AM2 C60  C  Y N 43  
A1AM2 C61  C  N N 44  
A1AM2 C62  C  N N 45  
A1AM2 C65  C  Y N 46  
A1AM2 C67  C  Y N 47  
A1AM2 C68  C  Y N 48  
A1AM2 C69  C  Y N 49  
A1AM2 C71  C  N N 50  
A1AM2 C73  C  N N 51  
A1AM2 C74  C  N N 52  
A1AM2 C75  C  N N 53  
A1AM2 C79  C  N N 54  
A1AM2 C80  C  N N 55  
A1AM2 C83  C  N N 56  
A1AM2 C84  C  N N 57  
A1AM2 C85  C  N R 58  
A1AM2 C86  C  N N 59  
A1AM2 C87  C  N N 60  
A1AM2 F12  F  N N 61  
A1AM2 F42  F  N N 62  
A1AM2 F57  F  N N 63  
A1AM2 F76  F  N N 64  
A1AM2 F77  F  N N 65  
A1AM2 F78  F  N N 66  
A1AM2 N02  N  N N 67  
A1AM2 N05  N  N N 68  
A1AM2 N18  N  N N 69  
A1AM2 N33  N  N N 70  
A1AM2 N51  N  N N 71  
A1AM2 N64  N  N N 72  
A1AM2 N66  N  Y N 73  
A1AM2 N70  N  N N 74  
A1AM2 N82  N  N N 75  
A1AM2 O17  O  N N 76  
A1AM2 O21  O  N N 77  
A1AM2 O24  O  N N 78  
A1AM2 O27  O  N N 79  
A1AM2 O30  O  N N 80  
A1AM2 O35  O  N N 81  
A1AM2 O50  O  N N 82  
A1AM2 O63  O  N N 83  
A1AM2 O72  O  N N 84  
A1AM2 O81  O  N N 85  
A1AM2 CL45 CL N N 86  
A1AM2 CL59 CL N N 87  
A1AM2 H013 H  N N 88  
A1AM2 H012 H  N N 89  
A1AM2 H011 H  N N 90  
A1AM2 H031 H  N N 91  
A1AM2 H041 H  N N 92  
A1AM2 H042 H  N N 93  
A1AM2 H071 H  N N 94  
A1AM2 H081 H  N N 95  
A1AM2 H131 H  N N 96  
A1AM2 H141 H  N N 97  
A1AM2 H191 H  N N 98  
A1AM2 H192 H  N N 99  
A1AM2 H202 H  N N 100 
A1AM2 H201 H  N N 101 
A1AM2 H222 H  N N 102 
A1AM2 H221 H  N N 103 
A1AM2 H232 H  N N 104 
A1AM2 H231 H  N N 105 
A1AM2 H252 H  N N 106 
A1AM2 H251 H  N N 107 
A1AM2 H262 H  N N 108 
A1AM2 H261 H  N N 109 
A1AM2 H282 H  N N 110 
A1AM2 H281 H  N N 111 
A1AM2 H291 H  N N 112 
A1AM2 H292 H  N N 113 
A1AM2 H312 H  N N 114 
A1AM2 H311 H  N N 115 
A1AM2 H321 H  N N 116 
A1AM2 H322 H  N N 117 
A1AM2 H361 H  N N 118 
A1AM2 H371 H  N N 119 
A1AM2 H431 H  N N 120 
A1AM2 H461 H  N N 121 
A1AM2 H471 H  N N 122 
A1AM2 H521 H  N N 123 
A1AM2 H541 H  N N 124 
A1AM2 H551 H  N N 125 
A1AM2 H601 H  N N 126 
A1AM2 H612 H  N N 127 
A1AM2 H611 H  N N 128 
A1AM2 H651 H  N N 129 
A1AM2 H671 H  N N 130 
A1AM2 H681 H  N N 131 
A1AM2 H791 H  N N 132 
A1AM2 H831 H  N N 133 
A1AM2 H842 H  N N 134 
A1AM2 H841 H  N N 135 
A1AM2 H851 H  N N 136 
A1AM2 H862 H  N N 137 
A1AM2 H861 H  N N 138 
A1AM2 H863 H  N N 139 
A1AM2 H872 H  N N 140 
A1AM2 H873 H  N N 141 
A1AM2 H871 H  N N 142 
A1AM2 H181 H  N N 143 
A1AM2 H331 H  N N 144 
A1AM2 H511 H  N N 145 
A1AM2 H642 H  N N 146 
A1AM2 H641 H  N N 147 
A1AM2 H661 H  N N 148 
A1AM2 H701 H  N N 149 
A1AM2 H821 H  N N 150 
ALA   N    N  N N 151 
ALA   CA   C  N S 152 
ALA   C    C  N N 153 
ALA   O    O  N N 154 
ALA   CB   C  N N 155 
ALA   OXT  O  N N 156 
ALA   H    H  N N 157 
ALA   H2   H  N N 158 
ALA   HA   H  N N 159 
ALA   HB1  H  N N 160 
ALA   HB2  H  N N 161 
ALA   HB3  H  N N 162 
ALA   HXT  H  N N 163 
ARG   N    N  N N 164 
ARG   CA   C  N S 165 
ARG   C    C  N N 166 
ARG   O    O  N N 167 
ARG   CB   C  N N 168 
ARG   CG   C  N N 169 
ARG   CD   C  N N 170 
ARG   NE   N  N N 171 
ARG   CZ   C  N N 172 
ARG   NH1  N  N N 173 
ARG   NH2  N  N N 174 
ARG   OXT  O  N N 175 
ARG   H    H  N N 176 
ARG   H2   H  N N 177 
ARG   HA   H  N N 178 
ARG   HB2  H  N N 179 
ARG   HB3  H  N N 180 
ARG   HG2  H  N N 181 
ARG   HG3  H  N N 182 
ARG   HD2  H  N N 183 
ARG   HD3  H  N N 184 
ARG   HE   H  N N 185 
ARG   HH11 H  N N 186 
ARG   HH12 H  N N 187 
ARG   HH21 H  N N 188 
ARG   HH22 H  N N 189 
ARG   HXT  H  N N 190 
ASN   N    N  N N 191 
ASN   CA   C  N S 192 
ASN   C    C  N N 193 
ASN   O    O  N N 194 
ASN   CB   C  N N 195 
ASN   CG   C  N N 196 
ASN   OD1  O  N N 197 
ASN   ND2  N  N N 198 
ASN   OXT  O  N N 199 
ASN   H    H  N N 200 
ASN   H2   H  N N 201 
ASN   HA   H  N N 202 
ASN   HB2  H  N N 203 
ASN   HB3  H  N N 204 
ASN   HD21 H  N N 205 
ASN   HD22 H  N N 206 
ASN   HXT  H  N N 207 
ASP   N    N  N N 208 
ASP   CA   C  N S 209 
ASP   C    C  N N 210 
ASP   O    O  N N 211 
ASP   CB   C  N N 212 
ASP   CG   C  N N 213 
ASP   OD1  O  N N 214 
ASP   OD2  O  N N 215 
ASP   OXT  O  N N 216 
ASP   H    H  N N 217 
ASP   H2   H  N N 218 
ASP   HA   H  N N 219 
ASP   HB2  H  N N 220 
ASP   HB3  H  N N 221 
ASP   HD2  H  N N 222 
ASP   HXT  H  N N 223 
CYS   N    N  N N 224 
CYS   CA   C  N R 225 
CYS   C    C  N N 226 
CYS   O    O  N N 227 
CYS   CB   C  N N 228 
CYS   SG   S  N N 229 
CYS   OXT  O  N N 230 
CYS   H    H  N N 231 
CYS   H2   H  N N 232 
CYS   HA   H  N N 233 
CYS   HB2  H  N N 234 
CYS   HB3  H  N N 235 
CYS   HG   H  N N 236 
CYS   HXT  H  N N 237 
GLN   N    N  N N 238 
GLN   CA   C  N S 239 
GLN   C    C  N N 240 
GLN   O    O  N N 241 
GLN   CB   C  N N 242 
GLN   CG   C  N N 243 
GLN   CD   C  N N 244 
GLN   OE1  O  N N 245 
GLN   NE2  N  N N 246 
GLN   OXT  O  N N 247 
GLN   H    H  N N 248 
GLN   H2   H  N N 249 
GLN   HA   H  N N 250 
GLN   HB2  H  N N 251 
GLN   HB3  H  N N 252 
GLN   HG2  H  N N 253 
GLN   HG3  H  N N 254 
GLN   HE21 H  N N 255 
GLN   HE22 H  N N 256 
GLN   HXT  H  N N 257 
GLU   N    N  N N 258 
GLU   CA   C  N S 259 
GLU   C    C  N N 260 
GLU   O    O  N N 261 
GLU   CB   C  N N 262 
GLU   CG   C  N N 263 
GLU   CD   C  N N 264 
GLU   OE1  O  N N 265 
GLU   OE2  O  N N 266 
GLU   OXT  O  N N 267 
GLU   H    H  N N 268 
GLU   H2   H  N N 269 
GLU   HA   H  N N 270 
GLU   HB2  H  N N 271 
GLU   HB3  H  N N 272 
GLU   HG2  H  N N 273 
GLU   HG3  H  N N 274 
GLU   HE2  H  N N 275 
GLU   HXT  H  N N 276 
GLY   N    N  N N 277 
GLY   CA   C  N N 278 
GLY   C    C  N N 279 
GLY   O    O  N N 280 
GLY   OXT  O  N N 281 
GLY   H    H  N N 282 
GLY   H2   H  N N 283 
GLY   HA2  H  N N 284 
GLY   HA3  H  N N 285 
GLY   HXT  H  N N 286 
HIS   N    N  N N 287 
HIS   CA   C  N S 288 
HIS   C    C  N N 289 
HIS   O    O  N N 290 
HIS   CB   C  N N 291 
HIS   CG   C  Y N 292 
HIS   ND1  N  Y N 293 
HIS   CD2  C  Y N 294 
HIS   CE1  C  Y N 295 
HIS   NE2  N  Y N 296 
HIS   OXT  O  N N 297 
HIS   H    H  N N 298 
HIS   H2   H  N N 299 
HIS   HA   H  N N 300 
HIS   HB2  H  N N 301 
HIS   HB3  H  N N 302 
HIS   HD1  H  N N 303 
HIS   HD2  H  N N 304 
HIS   HE1  H  N N 305 
HIS   HE2  H  N N 306 
HIS   HXT  H  N N 307 
HOH   O    O  N N 308 
HOH   H1   H  N N 309 
HOH   H2   H  N N 310 
ILE   N    N  N N 311 
ILE   CA   C  N S 312 
ILE   C    C  N N 313 
ILE   O    O  N N 314 
ILE   CB   C  N S 315 
ILE   CG1  C  N N 316 
ILE   CG2  C  N N 317 
ILE   CD1  C  N N 318 
ILE   OXT  O  N N 319 
ILE   H    H  N N 320 
ILE   H2   H  N N 321 
ILE   HA   H  N N 322 
ILE   HB   H  N N 323 
ILE   HG12 H  N N 324 
ILE   HG13 H  N N 325 
ILE   HG21 H  N N 326 
ILE   HG22 H  N N 327 
ILE   HG23 H  N N 328 
ILE   HD11 H  N N 329 
ILE   HD12 H  N N 330 
ILE   HD13 H  N N 331 
ILE   HXT  H  N N 332 
LEU   N    N  N N 333 
LEU   CA   C  N S 334 
LEU   C    C  N N 335 
LEU   O    O  N N 336 
LEU   CB   C  N N 337 
LEU   CG   C  N N 338 
LEU   CD1  C  N N 339 
LEU   CD2  C  N N 340 
LEU   OXT  O  N N 341 
LEU   H    H  N N 342 
LEU   H2   H  N N 343 
LEU   HA   H  N N 344 
LEU   HB2  H  N N 345 
LEU   HB3  H  N N 346 
LEU   HG   H  N N 347 
LEU   HD11 H  N N 348 
LEU   HD12 H  N N 349 
LEU   HD13 H  N N 350 
LEU   HD21 H  N N 351 
LEU   HD22 H  N N 352 
LEU   HD23 H  N N 353 
LEU   HXT  H  N N 354 
LYS   N    N  N N 355 
LYS   CA   C  N S 356 
LYS   C    C  N N 357 
LYS   O    O  N N 358 
LYS   CB   C  N N 359 
LYS   CG   C  N N 360 
LYS   CD   C  N N 361 
LYS   CE   C  N N 362 
LYS   NZ   N  N N 363 
LYS   OXT  O  N N 364 
LYS   H    H  N N 365 
LYS   H2   H  N N 366 
LYS   HA   H  N N 367 
LYS   HB2  H  N N 368 
LYS   HB3  H  N N 369 
LYS   HG2  H  N N 370 
LYS   HG3  H  N N 371 
LYS   HD2  H  N N 372 
LYS   HD3  H  N N 373 
LYS   HE2  H  N N 374 
LYS   HE3  H  N N 375 
LYS   HZ1  H  N N 376 
LYS   HZ2  H  N N 377 
LYS   HZ3  H  N N 378 
LYS   HXT  H  N N 379 
MET   N    N  N N 380 
MET   CA   C  N S 381 
MET   C    C  N N 382 
MET   O    O  N N 383 
MET   CB   C  N N 384 
MET   CG   C  N N 385 
MET   SD   S  N N 386 
MET   CE   C  N N 387 
MET   OXT  O  N N 388 
MET   H    H  N N 389 
MET   H2   H  N N 390 
MET   HA   H  N N 391 
MET   HB2  H  N N 392 
MET   HB3  H  N N 393 
MET   HG2  H  N N 394 
MET   HG3  H  N N 395 
MET   HE1  H  N N 396 
MET   HE2  H  N N 397 
MET   HE3  H  N N 398 
MET   HXT  H  N N 399 
PHE   N    N  N N 400 
PHE   CA   C  N S 401 
PHE   C    C  N N 402 
PHE   O    O  N N 403 
PHE   CB   C  N N 404 
PHE   CG   C  Y N 405 
PHE   CD1  C  Y N 406 
PHE   CD2  C  Y N 407 
PHE   CE1  C  Y N 408 
PHE   CE2  C  Y N 409 
PHE   CZ   C  Y N 410 
PHE   OXT  O  N N 411 
PHE   H    H  N N 412 
PHE   H2   H  N N 413 
PHE   HA   H  N N 414 
PHE   HB2  H  N N 415 
PHE   HB3  H  N N 416 
PHE   HD1  H  N N 417 
PHE   HD2  H  N N 418 
PHE   HE1  H  N N 419 
PHE   HE2  H  N N 420 
PHE   HZ   H  N N 421 
PHE   HXT  H  N N 422 
PRO   N    N  N N 423 
PRO   CA   C  N S 424 
PRO   C    C  N N 425 
PRO   O    O  N N 426 
PRO   CB   C  N N 427 
PRO   CG   C  N N 428 
PRO   CD   C  N N 429 
PRO   OXT  O  N N 430 
PRO   H    H  N N 431 
PRO   HA   H  N N 432 
PRO   HB2  H  N N 433 
PRO   HB3  H  N N 434 
PRO   HG2  H  N N 435 
PRO   HG3  H  N N 436 
PRO   HD2  H  N N 437 
PRO   HD3  H  N N 438 
PRO   HXT  H  N N 439 
SER   N    N  N N 440 
SER   CA   C  N S 441 
SER   C    C  N N 442 
SER   O    O  N N 443 
SER   CB   C  N N 444 
SER   OG   O  N N 445 
SER   OXT  O  N N 446 
SER   H    H  N N 447 
SER   H2   H  N N 448 
SER   HA   H  N N 449 
SER   HB2  H  N N 450 
SER   HB3  H  N N 451 
SER   HG   H  N N 452 
SER   HXT  H  N N 453 
THR   N    N  N N 454 
THR   CA   C  N S 455 
THR   C    C  N N 456 
THR   O    O  N N 457 
THR   CB   C  N R 458 
THR   OG1  O  N N 459 
THR   CG2  C  N N 460 
THR   OXT  O  N N 461 
THR   H    H  N N 462 
THR   H2   H  N N 463 
THR   HA   H  N N 464 
THR   HB   H  N N 465 
THR   HG1  H  N N 466 
THR   HG21 H  N N 467 
THR   HG22 H  N N 468 
THR   HG23 H  N N 469 
THR   HXT  H  N N 470 
TRP   N    N  N N 471 
TRP   CA   C  N S 472 
TRP   C    C  N N 473 
TRP   O    O  N N 474 
TRP   CB   C  N N 475 
TRP   CG   C  Y N 476 
TRP   CD1  C  Y N 477 
TRP   CD2  C  Y N 478 
TRP   NE1  N  Y N 479 
TRP   CE2  C  Y N 480 
TRP   CE3  C  Y N 481 
TRP   CZ2  C  Y N 482 
TRP   CZ3  C  Y N 483 
TRP   CH2  C  Y N 484 
TRP   OXT  O  N N 485 
TRP   H    H  N N 486 
TRP   H2   H  N N 487 
TRP   HA   H  N N 488 
TRP   HB2  H  N N 489 
TRP   HB3  H  N N 490 
TRP   HD1  H  N N 491 
TRP   HE1  H  N N 492 
TRP   HE3  H  N N 493 
TRP   HZ2  H  N N 494 
TRP   HZ3  H  N N 495 
TRP   HH2  H  N N 496 
TRP   HXT  H  N N 497 
TYR   N    N  N N 498 
TYR   CA   C  N S 499 
TYR   C    C  N N 500 
TYR   O    O  N N 501 
TYR   CB   C  N N 502 
TYR   CG   C  Y N 503 
TYR   CD1  C  Y N 504 
TYR   CD2  C  Y N 505 
TYR   CE1  C  Y N 506 
TYR   CE2  C  Y N 507 
TYR   CZ   C  Y N 508 
TYR   OH   O  N N 509 
TYR   OXT  O  N N 510 
TYR   H    H  N N 511 
TYR   H2   H  N N 512 
TYR   HA   H  N N 513 
TYR   HB2  H  N N 514 
TYR   HB3  H  N N 515 
TYR   HD1  H  N N 516 
TYR   HD2  H  N N 517 
TYR   HE1  H  N N 518 
TYR   HE2  H  N N 519 
TYR   HH   H  N N 520 
TYR   HXT  H  N N 521 
VAL   N    N  N N 522 
VAL   CA   C  N S 523 
VAL   C    C  N N 524 
VAL   O    O  N N 525 
VAL   CB   C  N N 526 
VAL   CG1  C  N N 527 
VAL   CG2  C  N N 528 
VAL   OXT  O  N N 529 
VAL   H    H  N N 530 
VAL   H2   H  N N 531 
VAL   HA   H  N N 532 
VAL   HB   H  N N 533 
VAL   HG11 H  N N 534 
VAL   HG12 H  N N 535 
VAL   HG13 H  N N 536 
VAL   HG21 H  N N 537 
VAL   HG22 H  N N 538 
VAL   HG23 H  N N 539 
VAL   HXT  H  N N 540 
# 
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 
A1AM2 N02  C01  sing N N 1   
A1AM2 C03  N02  sing N N 2   
A1AM2 N05  C04  sing N N 3   
A1AM2 C07  C06  doub Y N 4   
A1AM2 C08  C07  sing Y N 5   
A1AM2 C09  C08  doub Y N 6   
A1AM2 C11  C10  doub Y N 7   
A1AM2 F12  C11  sing N N 8   
A1AM2 C13  C11  sing Y N 9   
A1AM2 C14  C13  doub Y N 10  
A1AM2 C15  C14  sing Y N 11  
A1AM2 O17  C16  doub N N 12  
A1AM2 N18  C16  sing N N 13  
A1AM2 C19  N18  sing N N 14  
A1AM2 C20  C19  sing N N 15  
A1AM2 O21  C20  sing N N 16  
A1AM2 C22  O21  sing N N 17  
A1AM2 C23  C22  sing N N 18  
A1AM2 O24  C23  sing N N 19  
A1AM2 C25  O24  sing N N 20  
A1AM2 C26  C25  sing N N 21  
A1AM2 O27  C26  sing N N 22  
A1AM2 C28  O27  sing N N 23  
A1AM2 C29  C28  sing N N 24  
A1AM2 O30  C29  sing N N 25  
A1AM2 C31  O30  sing N N 26  
A1AM2 C32  C31  sing N N 27  
A1AM2 N33  C32  sing N N 28  
A1AM2 C34  N33  sing N N 29  
A1AM2 O35  C34  doub N N 30  
A1AM2 C36  C34  sing N N 31  
A1AM2 C37  C36  doub N E 32  
A1AM2 C38  C37  sing N N 33  
A1AM2 C39  C38  doub Y N 34  
A1AM2 C41  C40  doub Y N 35  
A1AM2 F42  C41  sing N N 36  
A1AM2 C43  C41  sing Y N 37  
A1AM2 C44  C43  doub Y N 38  
A1AM2 CL45 C44  sing N N 39  
A1AM2 C46  C44  sing Y N 40  
A1AM2 C47  C46  doub Y N 41  
A1AM2 C40  C39  sing N N 42  
A1AM2 C48  C39  sing Y N 43  
A1AM2 O50  C49  doub N N 44  
A1AM2 N51  C49  sing N N 45  
A1AM2 C52  N51  sing N N 46  
A1AM2 C54  C53  doub Y N 47  
A1AM2 C55  C54  sing Y N 48  
A1AM2 C56  C55  doub Y N 49  
A1AM2 F57  C56  sing N N 50  
A1AM2 C58  C56  sing Y N 51  
A1AM2 CL59 C58  sing N N 52  
A1AM2 C60  C58  doub Y N 53  
A1AM2 C53  C52  sing N N 54  
A1AM2 C61  C52  sing N N 55  
A1AM2 C62  C61  sing N N 56  
A1AM2 O63  C62  doub N N 57  
A1AM2 N64  C62  sing N N 58  
A1AM2 C49  C48  sing N N 59  
A1AM2 C65  C48  doub Y N 60  
A1AM2 N66  C65  sing Y N 61  
A1AM2 C16  C15  sing N N 62  
A1AM2 C67  C15  doub Y N 63  
A1AM2 C10  C09  sing N N 64  
A1AM2 C68  C09  sing Y N 65  
A1AM2 C69  C68  doub Y N 66  
A1AM2 N70  C69  sing N N 67  
A1AM2 C71  N70  sing N N 68  
A1AM2 O72  C71  doub N N 69  
A1AM2 C73  C71  sing N N 70  
A1AM2 F76  C75  sing N N 71  
A1AM2 F77  C75  sing N N 72  
A1AM2 F78  C75  sing N N 73  
A1AM2 C75  C74  sing N N 74  
A1AM2 C79  C74  doub N N 75  
A1AM2 C80  C79  sing N N 76  
A1AM2 O81  C80  doub N N 77  
A1AM2 N82  C80  sing N N 78  
A1AM2 C74  C73  sing N N 79  
A1AM2 C83  C73  doub N N 80  
A1AM2 C06  N05  sing N N 81  
A1AM2 C84  N05  sing N N 82  
A1AM2 C85  C84  sing N N 83  
A1AM2 C86  C85  sing N N 84  
A1AM2 C04  C03  sing N N 85  
A1AM2 C87  C03  sing N N 86  
A1AM2 N02  C85  sing N N 87  
A1AM2 C06  C69  sing Y N 88  
A1AM2 C10  C67  sing Y N 89  
A1AM2 C38  N66  sing Y N 90  
A1AM2 C40  C47  sing Y N 91  
A1AM2 C53  C60  sing Y N 92  
A1AM2 N82  C83  sing N N 93  
A1AM2 C01  H013 sing N N 94  
A1AM2 C01  H012 sing N N 95  
A1AM2 C01  H011 sing N N 96  
A1AM2 C03  H031 sing N N 97  
A1AM2 C04  H041 sing N N 98  
A1AM2 C04  H042 sing N N 99  
A1AM2 C07  H071 sing N N 100 
A1AM2 C08  H081 sing N N 101 
A1AM2 C13  H131 sing N N 102 
A1AM2 C14  H141 sing N N 103 
A1AM2 C19  H191 sing N N 104 
A1AM2 C19  H192 sing N N 105 
A1AM2 C20  H202 sing N N 106 
A1AM2 C20  H201 sing N N 107 
A1AM2 C22  H222 sing N N 108 
A1AM2 C22  H221 sing N N 109 
A1AM2 C23  H232 sing N N 110 
A1AM2 C23  H231 sing N N 111 
A1AM2 C25  H252 sing N N 112 
A1AM2 C25  H251 sing N N 113 
A1AM2 C26  H262 sing N N 114 
A1AM2 C26  H261 sing N N 115 
A1AM2 C28  H282 sing N N 116 
A1AM2 C28  H281 sing N N 117 
A1AM2 C29  H291 sing N N 118 
A1AM2 C29  H292 sing N N 119 
A1AM2 C31  H312 sing N N 120 
A1AM2 C31  H311 sing N N 121 
A1AM2 C32  H321 sing N N 122 
A1AM2 C32  H322 sing N N 123 
A1AM2 C36  H361 sing N N 124 
A1AM2 C37  H371 sing N N 125 
A1AM2 C43  H431 sing N N 126 
A1AM2 C46  H461 sing N N 127 
A1AM2 C47  H471 sing N N 128 
A1AM2 C52  H521 sing N N 129 
A1AM2 C54  H541 sing N N 130 
A1AM2 C55  H551 sing N N 131 
A1AM2 C60  H601 sing N N 132 
A1AM2 C61  H612 sing N N 133 
A1AM2 C61  H611 sing N N 134 
A1AM2 C65  H651 sing N N 135 
A1AM2 C67  H671 sing N N 136 
A1AM2 C68  H681 sing N N 137 
A1AM2 C79  H791 sing N N 138 
A1AM2 C83  H831 sing N N 139 
A1AM2 C84  H842 sing N N 140 
A1AM2 C84  H841 sing N N 141 
A1AM2 C85  H851 sing N N 142 
A1AM2 C86  H862 sing N N 143 
A1AM2 C86  H861 sing N N 144 
A1AM2 C86  H863 sing N N 145 
A1AM2 C87  H872 sing N N 146 
A1AM2 C87  H873 sing N N 147 
A1AM2 C87  H871 sing N N 148 
A1AM2 N18  H181 sing N N 149 
A1AM2 N33  H331 sing N N 150 
A1AM2 N51  H511 sing N N 151 
A1AM2 N64  H642 sing N N 152 
A1AM2 N64  H641 sing N N 153 
A1AM2 N66  H661 sing N N 154 
A1AM2 N70  H701 sing N N 155 
A1AM2 N82  H821 sing N N 156 
ALA   N    CA   sing N N 157 
ALA   N    H    sing N N 158 
ALA   N    H2   sing N N 159 
ALA   CA   C    sing N N 160 
ALA   CA   CB   sing N N 161 
ALA   CA   HA   sing N N 162 
ALA   C    O    doub N N 163 
ALA   C    OXT  sing N N 164 
ALA   CB   HB1  sing N N 165 
ALA   CB   HB2  sing N N 166 
ALA   CB   HB3  sing N N 167 
ALA   OXT  HXT  sing N N 168 
ARG   N    CA   sing N N 169 
ARG   N    H    sing N N 170 
ARG   N    H2   sing N N 171 
ARG   CA   C    sing N N 172 
ARG   CA   CB   sing N N 173 
ARG   CA   HA   sing N N 174 
ARG   C    O    doub N N 175 
ARG   C    OXT  sing N N 176 
ARG   CB   CG   sing N N 177 
ARG   CB   HB2  sing N N 178 
ARG   CB   HB3  sing N N 179 
ARG   CG   CD   sing N N 180 
ARG   CG   HG2  sing N N 181 
ARG   CG   HG3  sing N N 182 
ARG   CD   NE   sing N N 183 
ARG   CD   HD2  sing N N 184 
ARG   CD   HD3  sing N N 185 
ARG   NE   CZ   sing N N 186 
ARG   NE   HE   sing N N 187 
ARG   CZ   NH1  sing N N 188 
ARG   CZ   NH2  doub N N 189 
ARG   NH1  HH11 sing N N 190 
ARG   NH1  HH12 sing N N 191 
ARG   NH2  HH21 sing N N 192 
ARG   NH2  HH22 sing N N 193 
ARG   OXT  HXT  sing N N 194 
ASN   N    CA   sing N N 195 
ASN   N    H    sing N N 196 
ASN   N    H2   sing N N 197 
ASN   CA   C    sing N N 198 
ASN   CA   CB   sing N N 199 
ASN   CA   HA   sing N N 200 
ASN   C    O    doub N N 201 
ASN   C    OXT  sing N N 202 
ASN   CB   CG   sing N N 203 
ASN   CB   HB2  sing N N 204 
ASN   CB   HB3  sing N N 205 
ASN   CG   OD1  doub N N 206 
ASN   CG   ND2  sing N N 207 
ASN   ND2  HD21 sing N N 208 
ASN   ND2  HD22 sing N N 209 
ASN   OXT  HXT  sing N N 210 
ASP   N    CA   sing N N 211 
ASP   N    H    sing N N 212 
ASP   N    H2   sing N N 213 
ASP   CA   C    sing N N 214 
ASP   CA   CB   sing N N 215 
ASP   CA   HA   sing N N 216 
ASP   C    O    doub N N 217 
ASP   C    OXT  sing N N 218 
ASP   CB   CG   sing N N 219 
ASP   CB   HB2  sing N N 220 
ASP   CB   HB3  sing N N 221 
ASP   CG   OD1  doub N N 222 
ASP   CG   OD2  sing N N 223 
ASP   OD2  HD2  sing N N 224 
ASP   OXT  HXT  sing N N 225 
CYS   N    CA   sing N N 226 
CYS   N    H    sing N N 227 
CYS   N    H2   sing N N 228 
CYS   CA   C    sing N N 229 
CYS   CA   CB   sing N N 230 
CYS   CA   HA   sing N N 231 
CYS   C    O    doub N N 232 
CYS   C    OXT  sing N N 233 
CYS   CB   SG   sing N N 234 
CYS   CB   HB2  sing N N 235 
CYS   CB   HB3  sing N N 236 
CYS   SG   HG   sing N N 237 
CYS   OXT  HXT  sing N N 238 
GLN   N    CA   sing N N 239 
GLN   N    H    sing N N 240 
GLN   N    H2   sing N N 241 
GLN   CA   C    sing N N 242 
GLN   CA   CB   sing N N 243 
GLN   CA   HA   sing N N 244 
GLN   C    O    doub N N 245 
GLN   C    OXT  sing N N 246 
GLN   CB   CG   sing N N 247 
GLN   CB   HB2  sing N N 248 
GLN   CB   HB3  sing N N 249 
GLN   CG   CD   sing N N 250 
GLN   CG   HG2  sing N N 251 
GLN   CG   HG3  sing N N 252 
GLN   CD   OE1  doub N N 253 
GLN   CD   NE2  sing N N 254 
GLN   NE2  HE21 sing N N 255 
GLN   NE2  HE22 sing N N 256 
GLN   OXT  HXT  sing N N 257 
GLU   N    CA   sing N N 258 
GLU   N    H    sing N N 259 
GLU   N    H2   sing N N 260 
GLU   CA   C    sing N N 261 
GLU   CA   CB   sing N N 262 
GLU   CA   HA   sing N N 263 
GLU   C    O    doub N N 264 
GLU   C    OXT  sing N N 265 
GLU   CB   CG   sing N N 266 
GLU   CB   HB2  sing N N 267 
GLU   CB   HB3  sing N N 268 
GLU   CG   CD   sing N N 269 
GLU   CG   HG2  sing N N 270 
GLU   CG   HG3  sing N N 271 
GLU   CD   OE1  doub N N 272 
GLU   CD   OE2  sing N N 273 
GLU   OE2  HE2  sing N N 274 
GLU   OXT  HXT  sing N N 275 
GLY   N    CA   sing N N 276 
GLY   N    H    sing N N 277 
GLY   N    H2   sing N N 278 
GLY   CA   C    sing N N 279 
GLY   CA   HA2  sing N N 280 
GLY   CA   HA3  sing N N 281 
GLY   C    O    doub N N 282 
GLY   C    OXT  sing N N 283 
GLY   OXT  HXT  sing N N 284 
HIS   N    CA   sing N N 285 
HIS   N    H    sing N N 286 
HIS   N    H2   sing N N 287 
HIS   CA   C    sing N N 288 
HIS   CA   CB   sing N N 289 
HIS   CA   HA   sing N N 290 
HIS   C    O    doub N N 291 
HIS   C    OXT  sing N N 292 
HIS   CB   CG   sing N N 293 
HIS   CB   HB2  sing N N 294 
HIS   CB   HB3  sing N N 295 
HIS   CG   ND1  sing Y N 296 
HIS   CG   CD2  doub Y N 297 
HIS   ND1  CE1  doub Y N 298 
HIS   ND1  HD1  sing N N 299 
HIS   CD2  NE2  sing Y N 300 
HIS   CD2  HD2  sing N N 301 
HIS   CE1  NE2  sing Y N 302 
HIS   CE1  HE1  sing N N 303 
HIS   NE2  HE2  sing N N 304 
HIS   OXT  HXT  sing N N 305 
HOH   O    H1   sing N N 306 
HOH   O    H2   sing N N 307 
ILE   N    CA   sing N N 308 
ILE   N    H    sing N N 309 
ILE   N    H2   sing N N 310 
ILE   CA   C    sing N N 311 
ILE   CA   CB   sing N N 312 
ILE   CA   HA   sing N N 313 
ILE   C    O    doub N N 314 
ILE   C    OXT  sing N N 315 
ILE   CB   CG1  sing N N 316 
ILE   CB   CG2  sing N N 317 
ILE   CB   HB   sing N N 318 
ILE   CG1  CD1  sing N N 319 
ILE   CG1  HG12 sing N N 320 
ILE   CG1  HG13 sing N N 321 
ILE   CG2  HG21 sing N N 322 
ILE   CG2  HG22 sing N N 323 
ILE   CG2  HG23 sing N N 324 
ILE   CD1  HD11 sing N N 325 
ILE   CD1  HD12 sing N N 326 
ILE   CD1  HD13 sing N N 327 
ILE   OXT  HXT  sing N N 328 
LEU   N    CA   sing N N 329 
LEU   N    H    sing N N 330 
LEU   N    H2   sing N N 331 
LEU   CA   C    sing N N 332 
LEU   CA   CB   sing N N 333 
LEU   CA   HA   sing N N 334 
LEU   C    O    doub N N 335 
LEU   C    OXT  sing N N 336 
LEU   CB   CG   sing N N 337 
LEU   CB   HB2  sing N N 338 
LEU   CB   HB3  sing N N 339 
LEU   CG   CD1  sing N N 340 
LEU   CG   CD2  sing N N 341 
LEU   CG   HG   sing N N 342 
LEU   CD1  HD11 sing N N 343 
LEU   CD1  HD12 sing N N 344 
LEU   CD1  HD13 sing N N 345 
LEU   CD2  HD21 sing N N 346 
LEU   CD2  HD22 sing N N 347 
LEU   CD2  HD23 sing N N 348 
LEU   OXT  HXT  sing N N 349 
LYS   N    CA   sing N N 350 
LYS   N    H    sing N N 351 
LYS   N    H2   sing N N 352 
LYS   CA   C    sing N N 353 
LYS   CA   CB   sing N N 354 
LYS   CA   HA   sing N N 355 
LYS   C    O    doub N N 356 
LYS   C    OXT  sing N N 357 
LYS   CB   CG   sing N N 358 
LYS   CB   HB2  sing N N 359 
LYS   CB   HB3  sing N N 360 
LYS   CG   CD   sing N N 361 
LYS   CG   HG2  sing N N 362 
LYS   CG   HG3  sing N N 363 
LYS   CD   CE   sing N N 364 
LYS   CD   HD2  sing N N 365 
LYS   CD   HD3  sing N N 366 
LYS   CE   NZ   sing N N 367 
LYS   CE   HE2  sing N N 368 
LYS   CE   HE3  sing N N 369 
LYS   NZ   HZ1  sing N N 370 
LYS   NZ   HZ2  sing N N 371 
LYS   NZ   HZ3  sing N N 372 
LYS   OXT  HXT  sing N N 373 
MET   N    CA   sing N N 374 
MET   N    H    sing N N 375 
MET   N    H2   sing N N 376 
MET   CA   C    sing N N 377 
MET   CA   CB   sing N N 378 
MET   CA   HA   sing N N 379 
MET   C    O    doub N N 380 
MET   C    OXT  sing N N 381 
MET   CB   CG   sing N N 382 
MET   CB   HB2  sing N N 383 
MET   CB   HB3  sing N N 384 
MET   CG   SD   sing N N 385 
MET   CG   HG2  sing N N 386 
MET   CG   HG3  sing N N 387 
MET   SD   CE   sing N N 388 
MET   CE   HE1  sing N N 389 
MET   CE   HE2  sing N N 390 
MET   CE   HE3  sing N N 391 
MET   OXT  HXT  sing N N 392 
PHE   N    CA   sing N N 393 
PHE   N    H    sing N N 394 
PHE   N    H2   sing N N 395 
PHE   CA   C    sing N N 396 
PHE   CA   CB   sing N N 397 
PHE   CA   HA   sing N N 398 
PHE   C    O    doub N N 399 
PHE   C    OXT  sing N N 400 
PHE   CB   CG   sing N N 401 
PHE   CB   HB2  sing N N 402 
PHE   CB   HB3  sing N N 403 
PHE   CG   CD1  doub Y N 404 
PHE   CG   CD2  sing Y N 405 
PHE   CD1  CE1  sing Y N 406 
PHE   CD1  HD1  sing N N 407 
PHE   CD2  CE2  doub Y N 408 
PHE   CD2  HD2  sing N N 409 
PHE   CE1  CZ   doub Y N 410 
PHE   CE1  HE1  sing N N 411 
PHE   CE2  CZ   sing Y N 412 
PHE   CE2  HE2  sing N N 413 
PHE   CZ   HZ   sing N N 414 
PHE   OXT  HXT  sing N N 415 
PRO   N    CA   sing N N 416 
PRO   N    CD   sing N N 417 
PRO   N    H    sing N N 418 
PRO   CA   C    sing N N 419 
PRO   CA   CB   sing N N 420 
PRO   CA   HA   sing N N 421 
PRO   C    O    doub N N 422 
PRO   C    OXT  sing N N 423 
PRO   CB   CG   sing N N 424 
PRO   CB   HB2  sing N N 425 
PRO   CB   HB3  sing N N 426 
PRO   CG   CD   sing N N 427 
PRO   CG   HG2  sing N N 428 
PRO   CG   HG3  sing N N 429 
PRO   CD   HD2  sing N N 430 
PRO   CD   HD3  sing N N 431 
PRO   OXT  HXT  sing N N 432 
SER   N    CA   sing N N 433 
SER   N    H    sing N N 434 
SER   N    H2   sing N N 435 
SER   CA   C    sing N N 436 
SER   CA   CB   sing N N 437 
SER   CA   HA   sing N N 438 
SER   C    O    doub N N 439 
SER   C    OXT  sing N N 440 
SER   CB   OG   sing N N 441 
SER   CB   HB2  sing N N 442 
SER   CB   HB3  sing N N 443 
SER   OG   HG   sing N N 444 
SER   OXT  HXT  sing N N 445 
THR   N    CA   sing N N 446 
THR   N    H    sing N N 447 
THR   N    H2   sing N N 448 
THR   CA   C    sing N N 449 
THR   CA   CB   sing N N 450 
THR   CA   HA   sing N N 451 
THR   C    O    doub N N 452 
THR   C    OXT  sing N N 453 
THR   CB   OG1  sing N N 454 
THR   CB   CG2  sing N N 455 
THR   CB   HB   sing N N 456 
THR   OG1  HG1  sing N N 457 
THR   CG2  HG21 sing N N 458 
THR   CG2  HG22 sing N N 459 
THR   CG2  HG23 sing N N 460 
THR   OXT  HXT  sing N N 461 
TRP   N    CA   sing N N 462 
TRP   N    H    sing N N 463 
TRP   N    H2   sing N N 464 
TRP   CA   C    sing N N 465 
TRP   CA   CB   sing N N 466 
TRP   CA   HA   sing N N 467 
TRP   C    O    doub N N 468 
TRP   C    OXT  sing N N 469 
TRP   CB   CG   sing N N 470 
TRP   CB   HB2  sing N N 471 
TRP   CB   HB3  sing N N 472 
TRP   CG   CD1  doub Y N 473 
TRP   CG   CD2  sing Y N 474 
TRP   CD1  NE1  sing Y N 475 
TRP   CD1  HD1  sing N N 476 
TRP   CD2  CE2  doub Y N 477 
TRP   CD2  CE3  sing Y N 478 
TRP   NE1  CE2  sing Y N 479 
TRP   NE1  HE1  sing N N 480 
TRP   CE2  CZ2  sing Y N 481 
TRP   CE3  CZ3  doub Y N 482 
TRP   CE3  HE3  sing N N 483 
TRP   CZ2  CH2  doub Y N 484 
TRP   CZ2  HZ2  sing N N 485 
TRP   CZ3  CH2  sing Y N 486 
TRP   CZ3  HZ3  sing N N 487 
TRP   CH2  HH2  sing N N 488 
TRP   OXT  HXT  sing N N 489 
TYR   N    CA   sing N N 490 
TYR   N    H    sing N N 491 
TYR   N    H2   sing N N 492 
TYR   CA   C    sing N N 493 
TYR   CA   CB   sing N N 494 
TYR   CA   HA   sing N N 495 
TYR   C    O    doub N N 496 
TYR   C    OXT  sing N N 497 
TYR   CB   CG   sing N N 498 
TYR   CB   HB2  sing N N 499 
TYR   CB   HB3  sing N N 500 
TYR   CG   CD1  doub Y N 501 
TYR   CG   CD2  sing Y N 502 
TYR   CD1  CE1  sing Y N 503 
TYR   CD1  HD1  sing N N 504 
TYR   CD2  CE2  doub Y N 505 
TYR   CD2  HD2  sing N N 506 
TYR   CE1  CZ   doub Y N 507 
TYR   CE1  HE1  sing N N 508 
TYR   CE2  CZ   sing Y N 509 
TYR   CE2  HE2  sing N N 510 
TYR   CZ   OH   sing N N 511 
TYR   OH   HH   sing N N 512 
TYR   OXT  HXT  sing N N 513 
VAL   N    CA   sing N N 514 
VAL   N    H    sing N N 515 
VAL   N    H2   sing N N 516 
VAL   CA   C    sing N N 517 
VAL   CA   CB   sing N N 518 
VAL   CA   HA   sing N N 519 
VAL   C    O    doub N N 520 
VAL   C    OXT  sing N N 521 
VAL   CB   CG1  sing N N 522 
VAL   CB   CG2  sing N N 523 
VAL   CB   HB   sing N N 524 
VAL   CG1  HG11 sing N N 525 
VAL   CG1  HG12 sing N N 526 
VAL   CG1  HG13 sing N N 527 
VAL   CG2  HG21 sing N N 528 
VAL   CG2  HG22 sing N N 529 
VAL   CG2  HG23 sing N N 530 
VAL   OXT  HXT  sing N N 531 
# 
_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                    9B9H 
_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]   0.011875 
_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]   0.011745 
_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]   0.008957 
_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    . ALA   A 1 27  ? -8.60560  -33.32032 4.59648   1.000 67.51948  ? 1079 ALA   B N    1 
ATOM   2    C  CA   . ALA   A 1 27  ? -10.05259 -33.23314 4.74949   1.000 65.19426  ? 1079 ALA   B CA   1 
ATOM   3    C  C    . ALA   A 1 27  ? -10.50248 -31.78206 4.88193   1.000 59.93114  ? 1079 ALA   B C    1 
ATOM   4    O  O    . ALA   A 1 27  ? -10.30640 -31.14966 5.92267   1.000 62.60793  ? 1079 ALA   B O    1 
ATOM   5    C  CB   . ALA   A 1 27  ? -10.51262 -34.04163 5.95483   1.000 66.63448  ? 1079 ALA   B CB   1 
ATOM   6    N  N    . PHE   A 1 28  ? -11.11047 -31.25643 3.81674   1.000 53.68926  ? 1080 PHE   B N    1 
ATOM   7    C  CA   . PHE   A 1 28  ? -11.66136 -29.90139 3.79822   1.000 52.11313  ? 1080 PHE   B CA   1 
ATOM   8    C  C    . PHE   A 1 28  ? -13.09738 -29.97749 3.27329   1.000 46.60199  ? 1080 PHE   B C    1 
ATOM   9    O  O    . PHE   A 1 28  ? -13.39039 -29.60292 2.13615   1.000 55.66111  ? 1080 PHE   B O    1 
ATOM   10   C  CB   . PHE   A 1 28  ? -10.79031 -28.96079 2.96082   1.000 43.20623  ? 1080 PHE   B CB   1 
ATOM   11   C  CG   . PHE   A 1 28  ? -9.48027  -28.61164 3.60865   1.000 47.96458  ? 1080 PHE   B CG   1 
ATOM   12   C  CD1  . PHE   A 1 28  ? -9.41816  -27.63825 4.59426   1.000 43.77027  ? 1080 PHE   B CD1  1 
ATOM   13   C  CD2  . PHE   A 1 28  ? -8.31033  -29.25788 3.23887   1.000 48.93645  ? 1080 PHE   B CD2  1 
ATOM   14   C  CE1  . PHE   A 1 28  ? -8.21712  -27.31511 5.19710   1.000 49.26183  ? 1080 PHE   B CE1  1 
ATOM   15   C  CE2  . PHE   A 1 28  ? -7.10629  -28.94073 3.83871   1.000 46.26789  ? 1080 PHE   B CE2  1 
ATOM   16   C  CZ   . PHE   A 1 28  ? -7.05818  -27.96635 4.81832   1.000 49.68596  ? 1080 PHE   B CZ   1 
ATOM   17   N  N    . ARG   A 1 29  ? -13.99140 -30.46409 4.12151   1.000 47.07214  ? 1081 ARG   B N    1 
ATOM   18   C  CA   . ARG   A 1 29  ? -15.38042 -30.69213 3.73964   1.000 49.27197  ? 1081 ARG   B CA   1 
ATOM   19   C  C    . ARG   A 1 29  ? -16.10233 -29.36716 3.52614   1.000 43.34346  ? 1081 ARG   B C    1 
ATOM   20   O  O    . ARG   A 1 29  ? -16.13524 -28.54179 4.44481   1.000 38.52310  ? 1081 ARG   B O    1 
ATOM   21   C  CB   . ARG   A 1 29  ? -16.07746 -31.51165 4.82099   1.000 50.06553  ? 1081 ARG   B CB   1 
ATOM   22   C  CG   . ARG   A 1 29  ? -17.48250 -31.96368 4.46821   1.000 53.25591  ? 1081 ARG   B CG   1 
ATOM   23   C  CD   . ARG   A 1 29  ? -18.05054 -32.87821 5.54359   1.000 50.55301  ? 1081 ARG   B CD   1 
ATOM   24   N  NE   . ARG   A 1 29  ? -18.21145 -32.19469 6.82132   1.000 55.21288  ? 1081 ARG   B NE   1 
ATOM   25   C  CZ   . ARG   A 1 29  ? -19.30939 -31.54846 7.19210   1.000 60.05264  ? 1081 ARG   B CZ   1 
ATOM   26   N  NH1  . ARG   A 1 29  ? -20.36641 -31.47069 6.39910   1.000 57.63269  ? 1081 ARG   B NH1  1 
ATOM   27   N  NH2  . ARG   A 1 29  ? -19.34631 -30.96498 8.38787   1.000 59.43492  ? 1081 ARG   B NH2  1 
ATOM   28   N  N    . PRO   A 1 30  ? -16.68634 -29.11858 2.35606   1.000 46.00311  ? 1082 PRO   B N    1 
ATOM   29   C  CA   . PRO   A 1 30  ? -17.44725 -27.87659 2.17259   1.000 41.44884  ? 1082 PRO   B CA   1 
ATOM   30   C  C    . PRO   A 1 30  ? -18.55321 -27.75109 3.21057   1.000 42.46199  ? 1082 PRO   B C    1 
ATOM   31   O  O    . PRO   A 1 30  ? -19.18828 -28.73789 3.58998   1.000 49.21009  ? 1082 PRO   B O    1 
ATOM   32   C  CB   . PRO   A 1 30  ? -18.01430 -28.01410 0.75666   1.000 45.62017  ? 1082 PRO   B CB   1 
ATOM   33   C  CG   . PRO   A 1 30  ? -17.08040 -28.96545 0.07001   1.000 42.48351  ? 1082 PRO   B CG   1 
ATOM   34   C  CD   . PRO   A 1 30  ? -16.63644 -29.92806 1.12938   1.000 43.10644  ? 1082 PRO   B CD   1 
ATOM   35   N  N    . ILE   A 1 31  ? -18.78110 -26.52289 3.67209   1.000 42.01975  ? 1083 ILE   B N    1 
ATOM   36   C  CA   . ILE   A 1 31  ? -19.79405 -26.22442 4.67500   1.000 42.10243  ? 1083 ILE   B CA   1 
ATOM   37   C  C    . ILE   A 1 31  ? -20.79399 -25.19454 4.16263   1.000 45.38596  ? 1083 ILE   B C    1 
ATOM   38   O  O    . ILE   A 1 31  ? -22.00699 -25.35739 4.31473   1.000 47.52758  ? 1083 ILE   B O    1 
ATOM   39   C  CB   . ILE   A 1 31  ? -19.15497 -25.74794 5.99780   1.000 38.72052  ? 1083 ILE   B CB   1 
ATOM   40   C  CG1  . ILE   A 1 31  ? -18.21604 -26.81980 6.55119   1.000 50.19900  ? 1083 ILE   B CG1  1 
ATOM   41   C  CG2  . ILE   A 1 31  ? -20.22692 -25.38546 7.01469   1.000 49.70253  ? 1083 ILE   B CG2  1 
ATOM   42   C  CD1  . ILE   A 1 31  ? -18.88714 -28.15865 6.78574   1.000 51.73899  ? 1083 ILE   B CD1  1 
ATOM   43   N  N    . SER   A 1 32  ? -20.29592 -24.11882 3.55419   1.000 44.67131  ? 1084 SER   B N    1 
ATOM   44   C  CA   . SER   A 1 32  ? -21.16586 -23.10498 2.97481   1.000 41.13138  ? 1084 SER   B CA   1 
ATOM   45   C  C    . SER   A 1 32  ? -20.40083 -22.34447 1.90349   1.000 43.89366  ? 1084 SER   B C    1 
ATOM   46   O  O    . SER   A 1 32  ? -19.16984 -22.39459 1.83347   1.000 40.82186  ? 1084 SER   B O    1 
ATOM   47   C  CB   . SER   A 1 32  ? -21.70175 -22.14152 4.04045   1.000 44.29097  ? 1084 SER   B CB   1 
ATOM   48   O  OG   . SER   A 1 32  ? -20.67067 -21.30540 4.53508   1.000 53.04364  ? 1084 SER   B OG   1 
ATOM   49   N  N    . VAL   A 1 33  ? -21.15780 -21.64974 1.05923   1.000 39.63129  ? 1085 VAL   B N    1 
ATOM   50   C  CA   . VAL   A 1 33  ? -20.60477 -20.80720 0.00788   1.000 43.27606  ? 1085 VAL   B CA   1 
ATOM   51   C  C    . VAL   A 1 33  ? -21.55568 -19.63820 -0.18455  1.000 39.52418  ? 1085 VAL   B C    1 
ATOM   52   O  O    . VAL   A 1 33  ? -22.77169 -19.77704 -0.02546  1.000 43.30337  ? 1085 VAL   B O    1 
ATOM   53   C  CB   . VAL   A 1 33  ? -20.40587 -21.58974 -1.31081  1.000 41.80665  ? 1085 VAL   B CB   1 
ATOM   54   C  CG1  . VAL   A 1 33  ? -21.72193 -22.20281 -1.76353  1.000 41.39727  ? 1085 VAL   B CG1  1 
ATOM   55   C  CG2  . VAL   A 1 33  ? -19.83883 -20.67821 -2.39019  1.000 37.91029  ? 1085 VAL   B CG2  1 
ATOM   56   N  N    . PHE   A 1 34  ? -20.99960 -18.47437 -0.51303  1.000 33.94178  ? 1086 PHE   B N    1 
ATOM   57   C  CA   . PHE   A 1 34  ? -21.85352 -17.31740 -0.73646  1.000 40.76270  ? 1086 PHE   B CA   1 
ATOM   58   C  C    . PHE   A 1 34  ? -21.07946 -16.23675 -1.47691  1.000 44.70541  ? 1086 PHE   B C    1 
ATOM   59   O  O    . PHE   A 1 34  ? -19.85944 -16.11479 -1.34099  1.000 42.32985  ? 1086 PHE   B O    1 
ATOM   60   C  CB   . PHE   A 1 34  ? -22.42544 -16.77083 0.57734   1.000 35.79975  ? 1086 PHE   B CB   1 
ATOM   61   C  CG   . PHE   A 1 34  ? -21.38438 -16.40351 1.59916   1.000 35.82214  ? 1086 PHE   B CG   1 
ATOM   62   C  CD1  . PHE   A 1 34  ? -20.93442 -17.34118 2.51452   1.000 38.43455  ? 1086 PHE   B CD1  1 
ATOM   63   C  CD2  . PHE   A 1 34  ? -20.87228 -15.11652 1.65864   1.000 42.09194  ? 1086 PHE   B CD2  1 
ATOM   64   C  CE1  . PHE   A 1 34  ? -19.98537 -17.00988 3.46536   1.000 34.87035  ? 1086 PHE   B CE1  1 
ATOM   65   C  CE2  . PHE   A 1 34  ? -19.92322 -14.77622 2.60548   1.000 37.55662  ? 1086 PHE   B CE2  1 
ATOM   66   C  CZ   . PHE   A 1 34  ? -19.47727 -15.72790 3.50984   1.000 37.70294  ? 1086 PHE   B CZ   1 
ATOM   67   N  N    . ARG   A 1 35  ? -21.81442 -15.46301 -2.27120  1.000 36.58054  ? 1087 ARG   B N    1 
ATOM   68   C  CA   . ARG   A 1 35  ? -21.29535 -14.32034 -3.00566  1.000 34.61371  ? 1087 ARG   B CA   1 
ATOM   69   C  C    . ARG   A 1 35  ? -21.83123 -13.03505 -2.39016  1.000 42.42492  ? 1087 ARG   B C    1 
ATOM   70   O  O    . ARG   A 1 35  ? -22.69121 -13.04964 -1.50712  1.000 40.54987  ? 1087 ARG   B O    1 
ATOM   71   C  CB   . ARG   A 1 35  ? -21.67440 -14.41190 -4.49062  1.000 38.79222  ? 1087 ARG   B CB   1 
ATOM   72   C  CG   . ARG   A 1 35  ? -23.14743 -14.69788 -4.73046  1.000 42.67957  ? 1087 ARG   B CG   1 
ATOM   73   C  CD   . ARG   A 1 35  ? -23.47649 -14.82644 -6.21340  1.000 39.12662  ? 1087 ARG   B CD   1 
ATOM   74   N  NE   . ARG   A 1 35  ? -23.23241 -13.59175 -6.95189  1.000 43.37051  ? 1087 ARG   B NE   1 
ATOM   75   C  CZ   . ARG   A 1 35  ? -22.33943 -13.46620 -7.92497  1.000 43.27135  ? 1087 ARG   B CZ   1 
ATOM   76   N  NH1  . ARG   A 1 35  ? -21.60952 -14.49142 -8.33159  1.000 41.00629  ? 1087 ARG   B NH1  1 
ATOM   77   N  NH2  . ARG   A 1 35  ? -22.18436 -12.28445 -8.51144  1.000 41.38809  ? 1087 ARG   B NH2  1 
ATOM   78   N  N    . GLU   A 1 36  ? -21.30116 -11.91128 -2.86362  1.000 36.46617  ? 1088 GLU   B N    1 
ATOM   79   C  CA   . GLU   A 1 36  ? -21.72504 -10.61504 -2.35012  1.000 43.78481  ? 1088 GLU   B CA   1 
ATOM   80   C  C    . GLU   A 1 36  ? -23.17503 -10.34409 -2.73818  1.000 41.24614  ? 1088 GLU   B C    1 
ATOM   81   O  O    . GLU   A 1 36  ? -23.55408 -10.48852 -3.90511  1.000 46.02572  ? 1088 GLU   B O    1 
ATOM   82   C  CB   . GLU   A 1 36  ? -20.81497 -9.51033  -2.88358  1.000 32.51211  ? 1088 GLU   B CB   1 
ATOM   83   C  CG   . GLU   A 1 36  ? -21.02485 -8.16205  -2.22111  1.000 35.68440  ? 1088 GLU   B CG   1 
ATOM   84   C  CD   . GLU   A 1 36  ? -20.04578 -7.11632  -2.71155  1.000 44.21521  ? 1088 GLU   B CD   1 
ATOM   85   O  OE1  . GLU   A 1 36  ? -19.27183 -7.41775  -3.64345  1.000 41.85141  ? 1088 GLU   B OE1  1 
ATOM   86   O  OE2  . GLU   A 1 36  ? -20.04768 -5.99110  -2.16800  1.000 43.11689  ? 1088 GLU   B OE2  1 
ATOM   87   N  N    . ALA   A 1 37  ? -23.98298 -9.95164  -1.75831  1.000 40.22338  ? 1089 ALA   B N    1 
ATOM   88   C  CA   . ALA   A 1 37  ? -25.40497 -9.74862  -1.99935  1.000 41.90785  ? 1089 ALA   B CA   1 
ATOM   89   C  C    . ALA   A 1 37  ? -25.64090 -8.54096  -2.89482  1.000 45.36122  ? 1089 ALA   B C    1 
ATOM   90   O  O    . ALA   A 1 37  ? -24.99881 -7.49795  -2.74425  1.000 42.77618  ? 1089 ALA   B O    1 
ATOM   91   C  CB   . ALA   A 1 37  ? -26.14891 -9.56804  -0.67440  1.000 33.75450  ? 1089 ALA   B CB   1 
ATOM   92   N  N    . ASN   A 1 38  ? -26.57394 -8.69226  -3.83573  1.000 53.27359  ? 1090 ASN   B N    1 
ATOM   93   C  CA   . ASN   A 1 38  ? -26.98188 -7.60358  -4.72415  1.000 59.38666  ? 1090 ASN   B CA   1 
ATOM   94   C  C    . ASN   A 1 38  ? -25.78286 -7.00796  -5.46043  1.000 64.54048  ? 1090 ASN   B C    1 
ATOM   95   O  O    . ASN   A 1 38  ? -25.54276 -5.79897  -5.43291  1.000 69.19448  ? 1090 ASN   B O    1 
ATOM   96   C  CB   . ASN   A 1 38  ? -27.74277 -6.52621  -3.95156  1.000 54.07846  ? 1090 ASN   B CB   1 
ATOM   97   C  CG   . ASN   A 1 38  ? -28.77479 -7.10476  -3.00730  1.000 55.04135  ? 1090 ASN   B CG   1 
ATOM   98   O  OD1  . ASN   A 1 38  ? -29.77085 -7.68685  -3.43704  1.000 60.21276  ? 1090 ASN   B OD1  1 
ATOM   99   N  ND2  . ASN   A 1 38  ? -28.54474 -6.93826  -1.70737  1.000 56.07928  ? 1090 ASN   B ND2  1 
ATOM   100  N  N    . GLU   A 1 39  ? -25.02394 -7.87328  -6.12910  1.000 59.15814  ? 1091 GLU   B N    1 
ATOM   101  C  CA   . GLU   A 1 39  ? -23.87093 -7.43468  -6.91031  1.000 49.53365  ? 1091 GLU   B CA   1 
ATOM   102  C  C    . GLU   A 1 39  ? -23.67904 -8.41515  -8.05693  1.000 53.29242  ? 1091 GLU   B C    1 
ATOM   103  O  O    . GLU   A 1 39  ? -23.25412 -9.55310  -7.83449  1.000 52.33235  ? 1091 GLU   B O    1 
ATOM   104  C  CB   . GLU   A 1 39  ? -22.61590 -7.34444  -6.04539  1.000 51.52993  ? 1091 GLU   B CB   1 
ATOM   105  C  CG   . GLU   A 1 39  ? -22.61778 -6.18805  -5.05784  1.000 48.06099  ? 1091 GLU   B CG   1 
ATOM   106  C  CD   . GLU   A 1 39  ? -22.59370 -4.83332  -5.74338  1.000 61.32176  ? 1091 GLU   B CD   1 
ATOM   107  O  OE1  . GLU   A 1 39  ? -22.63073 -4.79481  -6.99239  1.000 54.62143  ? 1091 GLU   B OE1  1 
ATOM   108  O  OE2  . GLU   A 1 39  ? -22.53359 -3.80804  -5.03179  1.000 66.23888  ? 1091 GLU   B OE2  1 
ATOM   109  N  N    . ASP   A 1 40  ? -23.97604 -7.98961  -9.27609  1.000 55.84628  ? 1092 ASP   B N    1 
ATOM   110  C  CA   . ASP   A 1 40  ? -23.76715 -8.86910  -10.45875 1.000 59.71659  ? 1092 ASP   B CA   1 
ATOM   111  C  C    . ASP   A 1 40  ? -22.32119 -9.36921  -10.46959 1.000 55.71530  ? 1092 ASP   B C    1 
ATOM   112  O  O    . ASP   A 1 40  ? -22.08029 -10.49541 -10.93115 1.000 53.27038  ? 1092 ASP   B O    1 
ATOM   113  C  CB   . ASP   A 1 40  ? -24.14313 -8.13557  -11.72803 1.000 64.96561  ? 1092 ASP   B CB   1 
ATOM   114  C  CG   . ASP   A 1 40  ? -25.59915 -8.27962  -12.15493 1.000 83.56307  ? 1092 ASP   B CG   1 
ATOM   115  O  OD1  . ASP   A 1 40  ? -26.23022 -9.28042  -11.75551 1.000 82.97096  ? 1092 ASP   B OD1  1 
ATOM   116  O  OD2  . ASP   A 1 40  ? -26.09110 -7.39387  -12.88326 1.000 81.76881  ? 1092 ASP   B OD2  1 
ATOM   117  N  N    . GLU   A 1 41  ? -21.40311 -8.52310  -10.00495 1.000 51.95487  ? 1093 GLU   B N    1 
ATOM   118  C  CA   . GLU   A 1 41  ? -19.97314 -8.90319  -9.95485  1.000 54.69233  ? 1093 GLU   B CA   1 
ATOM   119  C  C    . GLU   A 1 41  ? -19.55009 -8.88464  -8.48487  1.000 47.61948  ? 1093 GLU   B C    1 
ATOM   120  O  O    . GLU   A 1 41  ? -19.30399 -7.80144  -7.93630  1.000 44.74848  ? 1093 GLU   B O    1 
ATOM   121  C  CB   . GLU   A 1 41  ? -19.13709 -8.02762  -10.88222 1.000 51.19893  ? 1093 GLU   B CB   1 
ATOM   122  C  CG   . GLU   A 1 41  ? -19.46815 -8.24018  -12.35712 1.000 53.37304  ? 1093 GLU   B CG   1 
ATOM   123  C  CD   . GLU   A 1 41  ? -18.93210 -7.18660  -13.30856 1.000 64.51569  ? 1093 GLU   B CD   1 
ATOM   124  O  OE1  . GLU   A 1 41  ? -19.25400 -5.99850  -13.11802 1.000 57.95114  ? 1093 GLU   B OE1  1 
ATOM   125  O  OE2  . GLU   A 1 41  ? -18.19416 -7.55603  -14.24443 1.000 64.30766  ? 1093 GLU   B OE2  1 
ATOM   126  N  N    . SER   A 1 42  ? -19.54216 -10.05840 -7.87440  1.000 38.55267  ? 1094 SER   B N    1 
ATOM   127  C  CA   . SER   A 1 42  ? -19.17013 -10.16387 -6.47037  1.000 33.01247  ? 1094 SER   B CA   1 
ATOM   128  C  C    . SER   A 1 42  ? -17.73309 -9.69591  -6.27360  1.000 35.70597  ? 1094 SER   B C    1 
ATOM   129  O  O    . SER   A 1 42  ? -16.83514 -10.08428 -7.02647  1.000 40.65134  ? 1094 SER   B O    1 
ATOM   130  C  CB   . SER   A 1 42  ? -19.33723 -11.60867 -5.99379  1.000 33.56050  ? 1094 SER   B CB   1 
ATOM   131  O  OG   . SER   A 1 42  ? -19.12620 -11.72214 -4.59776  1.000 34.51753  ? 1094 SER   B OG   1 
ATOM   132  N  N    . GLY   A 1 43  ? -17.51599 -8.86452  -5.25593  1.000 37.22051  ? 1095 GLY   B N    1 
ATOM   133  C  CA   . GLY   A 1 43  ? -16.23494 -8.20156  -5.09923  1.000 33.66679  ? 1095 GLY   B CA   1 
ATOM   134  C  C    . GLY   A 1 43  ? -15.49492 -8.44910  -3.79816  1.000 37.11548  ? 1095 GLY   B C    1 
ATOM   135  O  O    . GLY   A 1 43  ? -14.70084 -7.60399  -3.37252  1.000 38.72593  ? 1095 GLY   B O    1 
ATOM   136  N  N    . PHE   A 1 44  ? -15.72999 -9.59183  -3.15570  1.000 35.35614  ? 1096 PHE   B N    1 
ATOM   137  C  CA   . PHE   A 1 44  ? -14.94898 -9.95642  -1.97958  1.000 34.50051  ? 1096 PHE   B CA   1 
ATOM   138  C  C    . PHE   A 1 44  ? -13.46500 -9.99268  -2.32861  1.000 33.62291  ? 1096 PHE   B C    1 
ATOM   139  O  O    . PHE   A 1 44  ? -13.07307 -10.54612 -3.35840  1.000 35.71625  ? 1096 PHE   B O    1 
ATOM   140  C  CB   . PHE   A 1 44  ? -15.38807 -11.32018 -1.44502  1.000 34.83802  ? 1096 PHE   B CB   1 
ATOM   141  C  CG   . PHE   A 1 44  ? -16.78706 -11.34585 -0.88897  1.000 32.38254  ? 1096 PHE   B CG   1 
ATOM   142  C  CD1  . PHE   A 1 44  ? -17.32095 -10.24056 -0.25139  1.000 37.26756  ? 1096 PHE   B CD1  1 
ATOM   143  C  CD2  . PHE   A 1 44  ? -17.56015 -12.49183 -0.99450  1.000 34.77761  ? 1096 PHE   B CD2  1 
ATOM   144  C  CE1  . PHE   A 1 44  ? -18.60594 -10.27325 0.26866   1.000 43.46721  ? 1096 PHE   B CE1  1 
ATOM   145  C  CE2  . PHE   A 1 44  ? -18.84614 -12.53153 -0.47744  1.000 38.04405  ? 1096 PHE   B CE2  1 
ATOM   146  C  CZ   . PHE   A 1 44  ? -19.36903 -11.42024 0.15313   1.000 34.81863  ? 1096 PHE   B CZ   1 
ATOM   147  N  N    . THR   A 1 45  ? -12.63592 -9.41340  -1.45886  1.000 32.59269  ? 1097 THR   B N    1 
ATOM   148  C  CA   . THR   A 1 45  ? -11.19093 -9.40159  -1.65791  1.000 31.30865  ? 1097 THR   B CA   1 
ATOM   149  C  C    . THR   A 1 45  ? -10.39093 -9.91218  -0.46773  1.000 36.60232  ? 1097 THR   B C    1 
ATOM   150  O  O    . THR   A 1 45  ? -9.26098  -10.36635 -0.66858  1.000 38.14935  ? 1097 THR   B O    1 
ATOM   151  C  CB   . THR   A 1 45  ? -10.70083 -7.98376  -1.99948  1.000 35.18988  ? 1097 THR   B CB   1 
ATOM   152  O  OG1  . THR   A 1 45  ? -11.10673 -7.07332  -0.96983  1.000 32.36002  ? 1097 THR   B OG1  1 
ATOM   153  C  CG2  . THR   A 1 45  ? -11.27383 -7.51924  -3.33165  1.000 28.64442  ? 1097 THR   B CG2  1 
ATOM   154  N  N    . CYS   A 1 46  ? -10.92489 -9.85566  0.75026   1.000 36.95314  ? 1098 CYS   B N    1 
ATOM   155  C  CA   . CYS   A 1 46  ? -10.21690 -10.33424 1.93043   1.000 33.69513  ? 1098 CYS   B CA   1 
ATOM   156  C  C    . CYS   A 1 46  ? -11.24189 -10.61073 3.02057   1.000 38.21039  ? 1098 CYS   B C    1 
ATOM   157  O  O    . CYS   A 1 46  ? -12.38985 -10.17068 2.93843   1.000 37.41232  ? 1098 CYS   B O    1 
ATOM   158  C  CB   . CYS   A 1 46  ? -9.16480  -9.32514  2.40300   1.000 30.59175  ? 1098 CYS   B CB   1 
ATOM   159  S  SG   . CYS   A 1 46  ? -9.80167  -7.65896  2.72336   1.000 38.70797  ? 1098 CYS   B SG   1 
ATOM   160  N  N    . CYS   A 1 47  ? -10.81291 -11.34036 4.04985   1.000 36.42174  ? 1099 CYS   B N    1 
ATOM   161  C  CA   . CYS   A 1 47  ? -11.76192 -11.78089 5.06105   1.000 35.87962  ? 1099 CYS   B CA   1 
ATOM   162  C  C    . CYS   A 1 47  ? -11.04391 -12.12643 6.35617   1.000 44.20917  ? 1099 CYS   B C    1 
ATOM   163  O  O    . CYS   A 1 47  ? -9.84993  -12.44151 6.37326   1.000 40.98533  ? 1099 CYS   B O    1 
ATOM   164  C  CB   . CYS   A 1 47  ? -12.57502 -12.98202 4.56855   1.000 38.87922  ? 1099 CYS   B CB   1 
ATOM   165  S  SG   . CYS   A 1 47  ? -11.56715 -14.40528 4.10608   1.000 41.16884  ? 1099 CYS   B SG   1 
ATOM   166  N  N    . ALA   A 1 48  ? -11.80687 -12.06394 7.44517   1.000 37.78450  ? 1100 ALA   B N    1 
ATOM   167  C  CA   . ALA   A 1 48  ? -11.36986 -12.49945 8.76132   1.000 42.10969  ? 1100 ALA   B CA   1 
ATOM   168  C  C    . ALA   A 1 48  ? -12.60985 -12.69601 9.62344   1.000 43.50398  ? 1100 ALA   B C    1 
ATOM   169  O  O    . ALA   A 1 48  ? -13.57480 -11.93799 9.50517   1.000 44.03800  ? 1100 ALA   B O    1 
ATOM   170  C  CB   . ALA   A 1 48  ? -10.41977 -11.48827 9.41090   1.000 39.26261  ? 1100 ALA   B CB   1 
ATOM   171  N  N    . PHE   A 1 49  ? -12.58591 -13.72068 10.47184  1.000 36.87007  ? 1101 PHE   B N    1 
ATOM   172  C  CA   . PHE   A 1 49  ? -13.69890 -13.94323 11.38196  1.000 42.53342  ? 1101 PHE   B CA   1 
ATOM   173  C  C    . PHE   A 1 49  ? -13.78078 -12.81382 12.40052  1.000 46.53427  ? 1101 PHE   B C    1 
ATOM   174  O  O    . PHE   A 1 49  ? -12.76073 -12.31771 12.88929  1.000 41.10219  ? 1101 PHE   B O    1 
ATOM   175  C  CB   . PHE   A 1 49  ? -13.55298 -15.28896 12.08949  1.000 38.06044  ? 1101 PHE   B CB   1 
ATOM   176  C  CG   . PHE   A 1 49  ? -13.76110 -16.47431 11.18897  1.000 43.15066  ? 1101 PHE   B CG   1 
ATOM   177  C  CD1  . PHE   A 1 49  ? -15.02815 -17.00928 11.00322  1.000 41.38409  ? 1101 PHE   B CD1  1 
ATOM   178  C  CD2  . PHE   A 1 49  ? -12.69117 -17.05265 10.52717  1.000 37.29525  ? 1101 PHE   B CD2  1 
ATOM   179  C  CE1  . PHE   A 1 49  ? -15.22526 -18.10159 10.17266  1.000 40.65760  ? 1101 PHE   B CE1  1 
ATOM   180  C  CE2  . PHE   A 1 49  ? -12.87827 -18.14597 9.69560   1.000 35.44071  ? 1101 PHE   B CE2  1 
ATOM   181  C  CZ   . PHE   A 1 49  ? -14.14932 -18.66994 9.51785   1.000 42.16230  ? 1101 PHE   B CZ   1 
ATOM   182  N  N    . SER   A 1 50  ? -15.00374 -12.39561 12.71239  1.000 48.09201  ? 1102 SER   B N    1 
ATOM   183  C  CA   . SER   A 1 50  ? -15.21063 -11.28523 13.62696  1.000 50.97288  ? 1102 SER   B CA   1 
ATOM   184  C  C    . SER   A 1 50  ? -15.23162 -11.78265 15.07016  1.000 47.15509  ? 1102 SER   B C    1 
ATOM   185  O  O    . SER   A 1 50  ? -15.06671 -12.97456 15.34862  1.000 44.49553  ? 1102 SER   B O    1 
ATOM   186  C  CB   . SER   A 1 50  ? -16.50458 -10.54626 13.28670  1.000 52.01302  ? 1102 SER   B CB   1 
ATOM   187  O  OG   . SER   A 1 50  ? -17.63762 -11.27000 13.73002  1.000 51.84532  ? 1102 SER   B OG   1 
ATOM   188  N  N    . ALA   A 1 51  ? -15.44052 -10.85427 16.00479  1.000 54.27755  ? 1103 ALA   B N    1 
ATOM   189  C  CA   . ALA   A 1 51  ? -15.51851 -11.23070 17.41295  1.000 55.18648  ? 1103 ALA   B CA   1 
ATOM   190  C  C    . ALA   A 1 51  ? -16.80656 -11.98148 17.72128  1.000 55.45495  ? 1103 ALA   B C    1 
ATOM   191  O  O    . ALA   A 1 51  ? -16.83560 -12.81412 18.63461  1.000 59.31165  ? 1103 ALA   B O    1 
ATOM   192  C  CB   . ALA   A 1 51  ? -15.39639 -9.99036  18.29645  1.000 46.80040  ? 1103 ALA   B CB   1 
ATOM   193  N  N    . ARG   A 1 52  ? -17.87456 -11.70869 16.97620  1.000 43.95885  ? 1104 ARG   B N    1 
ATOM   194  C  CA   . ARG   A 1 52  ? -19.15161 -12.37552 17.17251  1.000 53.26195  ? 1104 ARG   B CA   1 
ATOM   195  C  C    . ARG   A 1 52  ? -19.18973 -13.66284 16.36002  1.000 46.95274  ? 1104 ARG   B C    1 
ATOM   196  O  O    . ARG   A 1 52  ? -18.93476 -13.65234 15.15000  1.000 49.54868  ? 1104 ARG   B O    1 
ATOM   197  C  CB   . ARG   A 1 52  ? -20.30755 -11.45358 16.77817  1.000 47.14479  ? 1104 ARG   B CB   1 
ATOM   198  C  CG   . ARG   A 1 52  ? -20.08853 -10.70112 15.47887  1.000 54.11737  ? 1104 ARG   B CG   1 
ATOM   199  C  CD   . ARG   A 1 52  ? -21.20046 -9.69613  15.22751  1.000 57.52002  ? 1104 ARG   B CD   1 
ATOM   200  N  NE   . ARG   A 1 52  ? -22.51650 -10.32000 15.29679  1.000 56.75657  ? 1104 ARG   B NE   1 
ATOM   201  C  CZ   . ARG   A 1 52  ? -23.64347 -9.73606  14.91559  1.000 58.04083  ? 1104 ARG   B CZ   1 
ATOM   202  N  NH1  . ARG   A 1 52  ? -23.65439 -8.51126  14.41611  1.000 56.46974  ? 1104 ARG   B NH1  1 
ATOM   203  N  NH2  . ARG   A 1 52  ? -24.79052 -10.40093 15.03589  1.000 60.58625  ? 1104 ARG   B NH2  1 
ATOM   204  N  N    . GLU   A 1 53  ? -19.50380 -14.76755 17.03046  1.000 43.83771  ? 1105 GLU   B N    1 
ATOM   205  C  CA   . GLU   A 1 53  ? -19.45892 -16.07380 16.38998  1.000 48.11328  ? 1105 GLU   B CA   1 
ATOM   206  C  C    . GLU   A 1 53  ? -20.41996 -16.13620 15.21003  1.000 48.45789  ? 1105 GLU   B C    1 
ATOM   207  O  O    . GLU   A 1 53  ? -21.49791 -15.53311 15.22682  1.000 42.02575  ? 1105 GLU   B O    1 
ATOM   208  C  CB   . GLU   A 1 53  ? -19.80297 -17.16938 17.40342  1.000 45.57149  ? 1105 GLU   B CB   1 
ATOM   209  C  CG   . GLU   A 1 53  ? -19.06692 -17.02891 18.72435  1.000 52.83530  ? 1105 GLU   B CG   1 
ATOM   210  C  CD   . GLU   A 1 53  ? -19.22099 -18.25055 19.60983  1.000 60.51768  ? 1105 GLU   B CD   1 
ATOM   211  O  OE1  . GLU   A 1 53  ? -20.25205 -18.94451 19.49814  1.000 55.50721  ? 1105 GLU   B OE1  1 
ATOM   212  O  OE2  . GLU   A 1 53  ? -18.30499 -18.51330 20.41691  1.000 65.03678  ? 1105 GLU   B OE2  1 
ATOM   213  N  N    . ARG   A 1 54  ? -20.01804 -16.87364 14.17631  1.000 39.88902  ? 1106 ARG   B N    1 
ATOM   214  C  CA   . ARG   A 1 54  ? -20.78110 -17.17306 12.96845  1.000 45.53810  ? 1106 ARG   B CA   1 
ATOM   215  C  C    . ARG   A 1 54  ? -20.70405 -16.05847 11.92801  1.000 45.77049  ? 1106 ARG   B C    1 
ATOM   216  O  O    . ARG   A 1 54  ? -21.28409 -16.21186 10.84009  1.000 43.14492  ? 1106 ARG   B O    1 
ATOM   217  C  CB   . ARG   A 1 54  ? -22.26212 -17.46182 13.26261  1.000 51.17697  ? 1106 ARG   B CB   1 
ATOM   218  C  CG   . ARG   A 1 54  ? -22.48617 -18.50938 14.34103  1.000 54.78023  ? 1106 ARG   B CG   1 
ATOM   219  C  CD   . ARG   A 1 54  ? -23.93520 -18.96725 14.37526  1.000 58.35026  ? 1106 ARG   B CD   1 
ATOM   220  N  NE   . ARG   A 1 54  ? -24.86811 -17.84617 14.40884  1.000 68.36816  ? 1106 ARG   B NE   1 
ATOM   221  C  CZ   . ARG   A 1 54  ? -25.27103 -17.23670 15.51461  1.000 67.50886  ? 1106 ARG   B CZ   1 
ATOM   222  N  NH1  . ARG   A 1 54  ? -24.83103 -17.60526 16.70774  1.000 60.69944  ? 1106 ARG   B NH1  1 
ATOM   223  N  NH2  . ARG   A 1 54  ? -26.13596 -16.23167 15.42324  1.000 60.10285  ? 1106 ARG   B NH2  1 
ATOM   224  N  N    . PHE   A 1 55  ? -20.01595 -14.95742 12.20355  1.000 41.37915  ? 1107 PHE   B N    1 
ATOM   225  C  CA   . PHE   A 1 55  ? -19.97489 -13.82578 11.29110  1.000 41.81949  ? 1107 PHE   B CA   1 
ATOM   226  C  C    . PHE   A 1 55  ? -18.55689 -13.58909 10.79497  1.000 46.26481  ? 1107 PHE   B C    1 
ATOM   227  O  O    . PHE   A 1 55  ? -17.59087 -13.68186 11.56198  1.000 50.13300  ? 1107 PHE   B O    1 
ATOM   228  C  CB   . PHE   A 1 55  ? -20.53377 -12.56747 11.95962  1.000 47.10877  ? 1107 PHE   B CB   1 
ATOM   229  C  CG   . PHE   A 1 55  ? -21.99377 -12.66723 12.29170  1.000 52.02710  ? 1107 PHE   B CG   1 
ATOM   230  C  CD1  . PHE   A 1 55  ? -22.95377 -12.29752 11.36659  1.000 43.16519  ? 1107 PHE   B CD1  1 
ATOM   231  C  CD2  . PHE   A 1 55  ? -22.40577 -13.15871 13.51991  1.000 49.81615  ? 1107 PHE   B CD2  1 
ATOM   232  C  CE1  . PHE   A 1 55  ? -24.29777 -12.40230 11.66867  1.000 55.58769  ? 1107 PHE   B CE1  1 
ATOM   233  C  CE2  . PHE   A 1 55  ? -23.74877 -13.26449 13.82399  1.000 52.65060  ? 1107 PHE   B CE2  1 
ATOM   234  C  CZ   . PHE   A 1 55  ? -24.69377 -12.88478 12.89787  1.000 49.48689  ? 1107 PHE   B CZ   1 
ATOM   235  N  N    . LEU   A 1 56  ? -18.44890 -13.28261 9.50784   1.000 44.16705  ? 1108 LEU   B N    1 
ATOM   236  C  CA   . LEU   A 1 56  ? -17.18191 -13.09098 8.81973   1.000 37.94859  ? 1108 LEU   B CA   1 
ATOM   237  C  C    . LEU   A 1 56  ? -17.10981 -11.66819 8.28716   1.000 41.00353  ? 1108 LEU   B C    1 
ATOM   238  O  O    . LEU   A 1 56  ? -18.09679 -11.13933 7.75498   1.000 40.34208  ? 1108 LEU   B O    1 
ATOM   239  C  CB   . LEU   A 1 56  ? -17.02802 -14.09544 7.66912   1.000 41.77993  ? 1108 LEU   B CB   1 
ATOM   240  C  CG   . LEU   A 1 56  ? -15.67805 -14.20383 6.95313   1.000 35.95939  ? 1108 LEU   B CG   1 
ATOM   241  C  CD1  . LEU   A 1 56  ? -14.63607 -14.86056 7.85336   1.000 37.57903  ? 1108 LEU   B CD1  1 
ATOM   242  C  CD2  . LEU   A 1 56  ? -15.82215 -14.96734 5.64543   1.000 28.11237  ? 1108 LEU   B CD2  1 
ATOM   243  N  N    . MET   A 1 57  ? -15.93676 -11.06422 8.45689   1.000 38.05411  ? 1109 MET   B N    1 
ATOM   244  C  CA   . MET   A 1 57  ? -15.67067 -9.72246  7.90235   1.000 37.70878  ? 1109 MET   B CA   1 
ATOM   245  C  C    . MET   A 1 57  ? -15.03773 -9.91905  6.52541   1.000 37.76279  ? 1109 MET   B C    1 
ATOM   246  O  O    . MET   A 1 57  ? -14.18680 -10.78616 6.42373   1.000 39.09373  ? 1109 MET   B O    1 
ATOM   247  C  CB   . MET   A 1 57  ? -14.65859 -8.98019  8.77103   1.000 42.32079  ? 1109 MET   B CB   1 
ATOM   248  C  CG   . MET   A 1 57  ? -15.26349 -8.05974  9.80168   1.000 57.58466  ? 1109 MET   B CG   1 
ATOM   249  S  SD   . MET   A 1 57  ? -14.07041 -7.55933  11.05645  1.000 60.01582  ? 1109 MET   B SD   1 
ATOM   250  C  CE   . MET   A 1 57  ? -13.34153 -9.17629  11.32007  1.000 48.62109  ? 1109 MET   B CE   1 
ATOM   251  N  N    . LEU   A 1 58  ? -15.46070 -9.16242  5.52212   1.000 35.99539  ? 1110 LEU   B N    1 
ATOM   252  C  CA   . LEU   A 1 58  ? -14.94175 -9.24599  4.16314   1.000 32.38206  ? 1110 LEU   B CA   1 
ATOM   253  C  C    . LEU   A 1 58  ? -14.75765 -7.84123  3.61258   1.000 39.31411  ? 1110 LEU   B C    1 
ATOM   254  O  O    . LEU   A 1 58  ? -15.70359 -7.04916  3.60129   1.000 41.14070  ? 1110 LEU   B O    1 
ATOM   255  C  CB   . LEU   A 1 58  ? -15.87384 -10.05528 3.25649   1.000 33.97563  ? 1110 LEU   B CB   1 
ATOM   256  C  CG   . LEU   A 1 58  ? -16.14594 -11.51011 3.64407   1.000 34.95994  ? 1110 LEU   B CG   1 
ATOM   257  C  CD1  . LEU   A 1 58  ? -17.48593 -11.64072 4.35316   1.000 33.13819  ? 1110 LEU   B CD1  1 
ATOM   258  C  CD2  . LEU   A 1 58  ? -16.09104 -12.41460 2.41643   1.000 34.83882  ? 1110 LEU   B CD2  1 
ATOM   259  N  N    . GLY   A 1 59  ? -13.53864 -7.53149  3.17442   1.000 36.69762  ? 1111 GLY   B N    1 
ATOM   260  C  CA   . GLY   A 1 59  ? -13.32857 -6.34282  2.38195   1.000 33.04507  ? 1111 GLY   B CA   1 
ATOM   261  C  C    . GLY   A 1 59  ? -13.75963 -6.55236  0.94404   1.000 35.87261  ? 1111 GLY   B C    1 
ATOM   262  O  O    . GLY   A 1 59  ? -13.86273 -7.67754  0.46149   1.000 36.48129  ? 1111 GLY   B O    1 
ATOM   263  N  N    . THR   A 1 60  ? -14.02057 -5.44961  0.24961   1.000 38.04667  ? 1112 THR   B N    1 
ATOM   264  C  CA   . THR   A 1 60  ? -14.50961 -5.52312  -1.12034  1.000 36.27120  ? 1112 THR   B CA   1 
ATOM   265  C  C    . THR   A 1 60  ? -13.63657 -4.68755  -2.04270  1.000 38.34560  ? 1112 THR   B C    1 
ATOM   266  O  O    . THR   A 1 60  ? -12.84550 -3.84944  -1.60106  1.000 30.73301  ? 1112 THR   B O    1 
ATOM   267  C  CB   . THR   A 1 60  ? -15.96458 -5.04805  -1.22649  1.000 37.89497  ? 1112 THR   B CB   1 
ATOM   268  O  OG1  . THR   A 1 60  ? -16.02846 -3.63894  -0.97105  1.000 42.74996  ? 1112 THR   B OG1  1 
ATOM   269  C  CG2  . THR   A 1 60  ? -16.83761 -5.78358  -0.22017  1.000 37.50879  ? 1112 THR   B CG2  1 
ATOM   270  N  N    . CYS   A 1 61  ? -13.80363 -4.92505  -3.34460  1.000 37.87599  ? 1113 CYS   B N    1 
ATOM   271  C  CA   . CYS   A 1 61  ? -13.05560 -4.19451  -4.35791  1.000 39.08127  ? 1113 CYS   B CA   1 
ATOM   272  C  C    . CYS   A 1 61  ? -13.48950 -2.73953  -4.48148  1.000 38.83550  ? 1113 CYS   B C    1 
ATOM   273  O  O    . CYS   A 1 61  ? -12.81146 -1.96885  -5.16880  1.000 43.72398  ? 1113 CYS   B O    1 
ATOM   274  C  CB   . CYS   A 1 61  ? -13.19370 -4.89204  -5.71463  1.000 33.83470  ? 1113 CYS   B CB   1 
ATOM   275  S  SG   . CYS   A 1 61  ? -14.87872 -4.94516  -6.36056  1.000 48.03104  ? 1113 CYS   B SG   1 
ATOM   276  N  N    . THR   A 1 62  ? -14.59445 -2.34819  -3.84660  1.000 37.92209  ? 1114 THR   B N    1 
ATOM   277  C  CA   . THR   A 1 62  ? -15.03434 -0.95915  -3.83014  1.000 44.38780  ? 1114 THR   B CA   1 
ATOM   278  C  C    . THR   A 1 62  ? -14.76125 -0.28264  -2.49141  1.000 45.57687  ? 1114 THR   B C    1 
ATOM   279  O  O    . THR   A 1 62  ? -15.32816 0.77751   -2.21181  1.000 40.56329  ? 1114 THR   B O    1 
ATOM   280  C  CB   . THR   A 1 62  ? -16.52334 -0.86317  -4.17713  1.000 37.46229  ? 1114 THR   B CB   1 
ATOM   281  O  OG1  . THR   A 1 62  ? -17.27738 -1.72377  -3.31477  1.000 47.66772  ? 1114 THR   B OG1  1 
ATOM   282  C  CG2  . THR   A 1 62  ? -16.76641 -1.26472  -5.62296  1.000 36.45606  ? 1114 THR   B CG2  1 
ATOM   283  N  N    . GLY   A 1 63  ? -13.90627 -0.87638  -1.66020  1.000 42.17304  ? 1115 GLY   B N    1 
ATOM   284  C  CA   . GLY   A 1 63  ? -13.50418 -0.26292  -0.41146  1.000 39.54222  ? 1115 GLY   B CA   1 
ATOM   285  C  C    . GLY   A 1 63  ? -14.44217 -0.47438  0.75366   1.000 40.75380  ? 1115 GLY   B C    1 
ATOM   286  O  O    . GLY   A 1 63  ? -14.28108 0.19001   1.78339   1.000 40.99122  ? 1115 GLY   B O    1 
ATOM   287  N  N    . GLN   A 1 64  ? -15.40724 -1.37735  0.63704   1.000 41.13940  ? 1116 GLN   B N    1 
ATOM   288  C  CA   . GLN   A 1 64  ? -16.36723 -1.61285  1.70616   1.000 42.41560  ? 1116 GLN   B CA   1 
ATOM   289  C  C    . GLN   A 1 64  ? -15.90329 -2.74153  2.61860   1.000 41.28301  ? 1116 GLN   B C    1 
ATOM   290  O  O    . GLN   A 1 64  ? -15.23537 -3.68475  2.18895   1.000 42.05286  ? 1116 GLN   B O    1 
ATOM   291  C  CB   . GLN   A 1 64  ? -17.74427 -1.95198  1.13034   1.000 38.68318  ? 1116 GLN   B CB   1 
ATOM   292  C  CG   . GLN   A 1 64  ? -18.24022 -0.97135  0.08096   1.000 45.39958  ? 1116 GLN   B CG   1 
ATOM   293  C  CD   . GLN   A 1 64  ? -18.25510 0.45685   0.58540   1.000 56.92522  ? 1116 GLN   B CD   1 
ATOM   294  O  OE1  . GLN   A 1 64  ? -19.03504 0.80326   1.47528   1.000 58.44454  ? 1116 GLN   B OE1  1 
ATOM   295  N  NE2  . GLN   A 1 64  ? -17.38505 1.29556   0.02804   1.000 50.51005  ? 1116 GLN   B NE2  1 
ATOM   296  N  N    . LEU   A 1 65  ? -16.25824 -2.62700  3.89356   1.000 43.79449  ? 1117 LEU   B N    1 
ATOM   297  C  CA   . LEU   A 1 65  ? -16.11630 -3.70463  4.86198   1.000 41.21286  ? 1117 LEU   B CA   1 
ATOM   298  C  C    . LEU   A 1 65  ? -17.50933 -4.22439  5.18323   1.000 42.93734  ? 1117 LEU   B C    1 
ATOM   299  O  O    . LEU   A 1 65  ? -18.36225 -3.46414  5.64695   1.000 41.11907  ? 1117 LEU   B O    1 
ATOM   300  C  CB   . LEU   A 1 65  ? -15.41922 -3.23118  6.13478   1.000 43.90211  ? 1117 LEU   B CB   1 
ATOM   301  C  CG   . LEU   A 1 65  ? -15.42027 -4.26273  7.26818   1.000 40.49678  ? 1117 LEU   B CG   1 
ATOM   302  C  CD1  . LEU   A 1 65  ? -14.38936 -5.35391  7.01259   1.000 39.70694  ? 1117 LEU   B CD1  1 
ATOM   303  C  CD2  . LEU   A 1 65  ? -15.19818 -3.60621  8.62292   1.000 54.65341  ? 1117 LEU   B CD2  1 
ATOM   304  N  N    . LYS   A 1 66  ? -17.74243 -5.50747  4.93874   1.000 41.86110  ? 1118 LYS   B N    1 
ATOM   305  C  CA   . LYS   A 1 66  ? -19.06547 -6.08730  5.10501   1.000 37.32821  ? 1118 LYS   B CA   1 
ATOM   306  C  C    . LYS   A 1 66  ? -19.01853 -7.23491  6.10047   1.000 44.00825  ? 1118 LYS   B C    1 
ATOM   307  O  O    . LYS   A 1 66  ? -18.03259 -7.97696  6.17073   1.000 44.16480  ? 1118 LYS   B O    1 
ATOM   308  C  CB   . LYS   A 1 66  ? -19.62655 -6.55679  3.75922   1.000 42.15925  ? 1118 LYS   B CB   1 
ATOM   309  C  CG   . LYS   A 1 66  ? -19.78449 -5.41517  2.76277   1.000 42.40419  ? 1118 LYS   B CG   1 
ATOM   310  C  CD   . LYS   A 1 66  ? -20.66855 -5.78557  1.58894   1.000 40.41777  ? 1118 LYS   B CD   1 
ATOM   311  C  CE   . LYS   A 1 66  ? -20.96048 -4.56188  0.73247   1.000 39.15761  ? 1118 LYS   B CE   1 
ATOM   312  N  NZ   . LYS   A 1 66  ? -21.93954 -4.84624  -0.35739  1.000 50.41004  ? 1118 LYS   B NZ   1 
ATOM   313  N  N    . LEU   A 1 67  ? -20.08652 -7.35252  6.88054   1.000 45.34655  ? 1119 LEU   B N    1 
ATOM   314  C  CA   . LEU   A 1 67  ? -20.26457 -8.40711  7.86797   1.000 42.26609  ? 1119 LEU   B CA   1 
ATOM   315  C  C    . LEU   A 1 67  ? -21.33966 -9.35323  7.36337   1.000 44.64431  ? 1119 LEU   B C    1 
ATOM   316  O  O    . LEU   A 1 67  ? -22.47263 -8.92024  7.10824   1.000 45.93501  ? 1119 LEU   B O    1 
ATOM   317  C  CB   . LEU   A 1 67  ? -20.66049 -7.82555  9.22575   1.000 43.11654  ? 1119 LEU   B CB   1 
ATOM   318  C  CG   . LEU   A 1 67  ? -19.57045 -7.74921  10.29369  1.000 54.92921  ? 1119 LEU   B CG   1 
ATOM   319  C  CD1  . LEU   A 1 67  ? -19.07655 -9.14211  10.63922  1.000 50.10736  ? 1119 LEU   B CD1  1 
ATOM   320  C  CD2  . LEU   A 1 67  ? -18.42439 -6.86348  9.83030   1.000 56.76213  ? 1119 LEU   B CD2  1 
ATOM   321  N  N    . TYR   A 1 68  ? -20.97776 -10.63531 7.23987   1.000 35.73112  ? 1120 TYR   B N    1 
ATOM   322  C  CA   . TYR   A 1 68  ? -21.83686 -11.67246 6.68531   1.000 40.01035  ? 1120 TYR   B CA   1 
ATOM   323  C  C    . TYR   A 1 68  ? -21.99992 -12.82206 7.66877   1.000 43.44657  ? 1120 TYR   B C    1 
ATOM   324  O  O    . TYR   A 1 68  ? -21.10392 -13.11281 8.46485   1.000 41.07955  ? 1120 TYR   B O    1 
ATOM   325  C  CB   . TYR   A 1 68  ? -21.25994 -12.22902 5.37751   1.000 37.43965  ? 1120 TYR   B CB   1 
ATOM   326  C  CG   . TYR   A 1 68  ? -21.69192 -11.48848 4.14323   1.000 41.96993  ? 1120 TYR   B CG   1 
ATOM   327  C  CD1  . TYR   A 1 68  ? -21.13883 -10.25765 3.82072   1.000 35.25568  ? 1120 TYR   B CD1  1 
ATOM   328  C  CD2  . TYR   A 1 68  ? -22.65199 -12.01974 3.29247   1.000 39.31469  ? 1120 TYR   B CD2  1 
ATOM   329  C  CE1  . TYR   A 1 68  ? -21.53181 -9.57107  2.68946   1.000 41.93035  ? 1120 TYR   B CE1  1 
ATOM   330  C  CE2  . TYR   A 1 68  ? -23.05197 -11.34816 2.16021   1.000 44.87496  ? 1120 TYR   B CE2  1 
ATOM   331  C  CZ   . TYR   A 1 68  ? -22.48988 -10.12232 1.86171   1.000 40.48758  ? 1120 TYR   B CZ   1 
ATOM   332  O  OH   . TYR   A 1 68  ? -22.88786 -9.44573  0.73145   1.000 39.08718  ? 1120 TYR   B OH   1 
ATOM   333  N  N    . ASN   A 1 69  ? -23.14697 -13.49200 7.59306   1.000 41.00926  ? 1121 ASN   B N    1 
ATOM   334  C  CA   . ASN   A 1 69  ? -23.34605 -14.75771 8.29457   1.000 39.81181  ? 1121 ASN   B CA   1 
ATOM   335  C  C    . ASN   A 1 69  ? -22.78616 -15.87010 7.41800   1.000 40.22877  ? 1121 ASN   B C    1 
ATOM   336  O  O    . ASN   A 1 69  ? -23.31022 -16.13749 6.33312   1.000 46.35507  ? 1121 ASN   B O    1 
ATOM   337  C  CB   . ASN   A 1 69  ? -24.82606 -14.97747 8.60170   1.000 38.48963  ? 1121 ASN   B CB   1 
ATOM   338  C  CG   . ASN   A 1 69  ? -25.08414 -16.27615 9.35022   1.000 44.68097  ? 1121 ASN   B CG   1 
ATOM   339  O  OD1  . ASN   A 1 69  ? -24.66424 -17.35136 8.92164   1.000 49.73563  ? 1121 ASN   B OD1  1 
ATOM   340  N  ND2  . ASN   A 1 69  ? -25.77610 -16.17865 10.48021  1.000 51.24775  ? 1121 ASN   B ND2  1 
ATOM   341  N  N    . VAL   A 1 70  ? -21.71420 -16.52000 7.88422   1.000 40.23456  ? 1122 VAL   B N    1 
ATOM   342  C  CA   . VAL   A 1 70  ? -21.00030 -17.47338 7.04258   1.000 43.20142  ? 1122 VAL   B CA   1 
ATOM   343  C  C    . VAL   A 1 70  ? -21.81341 -18.73243 6.77610   1.000 45.55856  ? 1122 VAL   B C    1 
ATOM   344  O  O    . VAL   A 1 70  ? -21.50749 -19.47482 5.83638   1.000 53.33353  ? 1122 VAL   B O    1 
ATOM   345  C  CB   . VAL   A 1 70  ? -19.64431 -17.84924 7.66869   1.000 46.09990  ? 1122 VAL   B CB   1 
ATOM   346  C  CG1  . VAL   A 1 70  ? -18.90820 -16.60512 8.11717   1.000 42.28100  ? 1122 VAL   B CG1  1 
ATOM   347  C  CG2  . VAL   A 1 70  ? -19.84135 -18.81277 8.82807   1.000 42.77095  ? 1122 VAL   B CG2  1 
ATOM   348  N  N    . PHE   A 1 71  ? -22.84540 -18.99903 7.57524   1.000 49.99120  ? 1123 PHE   B N    1 
ATOM   349  C  CA   . PHE   A 1 71  ? -23.64250 -20.20204 7.38173   1.000 50.87931  ? 1123 PHE   B CA   1 
ATOM   350  C  C    . PHE   A 1 71  ? -24.86651 -19.95330 6.50767   1.000 48.22430  ? 1123 PHE   B C    1 
ATOM   351  O  O    . PHE   A 1 71  ? -25.21260 -20.80060 5.67602   1.000 58.79365  ? 1123 PHE   B O    1 
ATOM   352  C  CB   . PHE   A 1 71  ? -24.06651 -20.77448 8.73597   1.000 45.63219  ? 1123 PHE   B CB   1 
ATOM   353  C  CG   . PHE   A 1 71  ? -22.91051 -21.17422 9.61110   1.000 49.21315  ? 1123 PHE   B CG   1 
ATOM   354  C  CD1  . PHE   A 1 71  ? -22.15461 -22.29940 9.31352   1.000 53.06165  ? 1123 PHE   B CD1  1 
ATOM   355  C  CD2  . PHE   A 1 71  ? -22.58042 -20.42980 10.72879  1.000 40.64348  ? 1123 PHE   B CD2  1 
ATOM   356  C  CE1  . PHE   A 1 71  ? -21.08961 -22.66916 10.11464  1.000 40.00148  ? 1123 PHE   B CE1  1 
ATOM   357  C  CE2  . PHE   A 1 71  ? -21.51843 -20.79457 11.53591  1.000 42.44465  ? 1123 PHE   B CE2  1 
ATOM   358  C  CZ   . PHE   A 1 71  ? -20.77152 -21.91575 11.22733  1.000 38.84162  ? 1123 PHE   B CZ   1 
ATOM   359  N  N    . SER   A 1 72  ? -25.52441 -18.80618 6.67224   1.000 53.13712  ? 1124 SER   B N    1 
ATOM   360  C  CA   . SER   A 1 72  ? -26.68741 -18.47841 5.85914   1.000 55.61448  ? 1124 SER   B CA   1 
ATOM   361  C  C    . SER   A 1 72  ? -26.33239 -17.70194 4.59882   1.000 52.74824  ? 1124 SER   B C    1 
ATOM   362  O  O    . SER   A 1 72  ? -27.11042 -17.72026 3.63685   1.000 62.16186  ? 1124 SER   B O    1 
ATOM   363  C  CB   . SER   A 1 72  ? -27.69533 -17.66801 6.67785   1.000 48.93232  ? 1124 SER   B CB   1 
ATOM   364  O  OG   . SER   A 1 72  ? -27.18022 -16.38592 6.99533   1.000 48.96228  ? 1124 SER   B OG   1 
ATOM   365  N  N    . GLY   A 1 73  ? -25.18534 -17.02904 4.57552   1.000 47.65909  ? 1125 GLY   B N    1 
ATOM   366  C  CA   . GLY   A 1 73  ? -24.81931 -16.20151 3.44619   1.000 41.32031  ? 1125 GLY   B CA   1 
ATOM   367  C  C    . GLY   A 1 73  ? -25.46820 -14.83847 3.42067   1.000 47.68152  ? 1125 GLY   B C    1 
ATOM   368  O  O    . GLY   A 1 73  ? -25.37118 -14.14288 2.40239   1.000 42.83979  ? 1125 GLY   B O    1 
ATOM   369  N  N    . GLN   A 1 74  ? -26.12514 -14.43599 4.50653   1.000 45.93570  ? 1126 GLN   B N    1 
ATOM   370  C  CA   . GLN   A 1 74  ? -26.83304 -13.16491 4.57104   1.000 38.43747  ? 1126 GLN   B CA   1 
ATOM   371  C  C    . GLN   A 1 74  ? -25.87794 -12.05182 4.97157   1.000 43.02893  ? 1126 GLN   B C    1 
ATOM   372  O  O    . GLN   A 1 74  ? -25.10592 -12.19851 5.92561   1.000 46.01992  ? 1126 GLN   B O    1 
ATOM   373  C  CB   . GLN   A 1 74  ? -27.99202 -13.24643 5.56511   1.000 44.34931  ? 1126 GLN   B CB   1 
ATOM   374  C  CG   . GLN   A 1 74  ? -29.36004 -13.28958 4.90717   1.000 52.89644  ? 1126 GLN   B CG   1 
ATOM   375  C  CD   . GLN   A 1 74  ? -29.76695 -11.94577 4.33765   1.000 59.02934  ? 1126 GLN   B CD   1 
ATOM   376  O  OE1  . GLN   A 1 74  ? -29.88585 -10.96348 5.06726   1.000 70.31665  ? 1126 GLN   B OE1  1 
ATOM   377  N  NE2  . GLN   A 1 74  ? -29.97399 -11.89328 3.02563   1.000 64.05207  ? 1126 GLN   B NE2  1 
ATOM   378  N  N    . GLU   A 1 75  ? -25.93488 -10.94011 4.24214   1.000 42.85427  ? 1127 GLU   B N    1 
ATOM   379  C  CA   . GLU   A 1 75  ? -25.17077 -9.75702  4.60765   1.000 42.87197  ? 1127 GLU   B CA   1 
ATOM   380  C  C    . GLU   A 1 75  ? -25.81668 -9.08350  5.81240   1.000 45.29637  ? 1127 GLU   B C    1 
ATOM   381  O  O    . GLU   A 1 75  ? -27.00166 -8.73342  5.78229   1.000 48.40888  ? 1127 GLU   B O    1 
ATOM   382  C  CB   . GLU   A 1 75  ? -25.09073 -8.78049  3.43826   1.000 43.03798  ? 1127 GLU   B CB   1 
ATOM   383  C  CG   . GLU   A 1 75  ? -24.37662 -7.47741  3.77472   1.000 42.64076  ? 1127 GLU   B CG   1 
ATOM   384  C  CD   . GLU   A 1 75  ? -24.18259 -6.58891  2.55836   1.000 48.45650  ? 1127 GLU   B CD   1 
ATOM   385  O  OE1  . GLU   A 1 75  ? -23.83066 -7.11936  1.48456   1.000 43.04980  ? 1127 GLU   B OE1  1 
ATOM   386  O  OE2  . GLU   A 1 75  ? -24.39349 -5.36185  2.67488   1.000 43.18508  ? 1127 GLU   B OE2  1 
ATOM   387  N  N    A GLU   A 1 76  ? -25.03264 -8.90014  6.87530   0.479 44.00454  ? 1128 GLU   B N    1 
ATOM   388  N  N    B GLU   A 1 76  ? -25.03964 -8.90913  6.88231   0.521 44.08249  ? 1128 GLU   B N    1 
ATOM   389  C  CA   A GLU   A 1 76  ? -25.51055 -8.26762  8.09707   0.479 44.52260  ? 1128 GLU   B CA   1 
ATOM   390  C  CA   B GLU   A 1 76  ? -25.53055 -8.26462  8.09407   0.521 44.70338  ? 1128 GLU   B CA   1 
ATOM   391  C  C    A GLU   A 1 76  ? -25.21244 -6.77663  8.13147   0.479 47.62652  ? 1128 GLU   B C    1 
ATOM   392  C  C    B GLU   A 1 76  ? -25.20744 -6.77862  8.14747   0.521 47.65950  ? 1128 GLU   B C    1 
ATOM   393  O  O    A GLU   A 1 76  ? -26.05236 -5.98938  8.57518   0.479 46.61086  ? 1128 GLU   B O    1 
ATOM   394  O  O    B GLU   A 1 76  ? -26.03436 -5.99137  8.61118   0.521 46.61702  ? 1128 GLU   B O    1 
ATOM   395  C  CB   A GLU   A 1 76  ? -24.88557 -8.94618  9.31732   0.479 45.93779  ? 1128 GLU   B CB   1 
ATOM   396  C  CB   B GLU   A 1 76  ? -24.95757 -8.95417  9.33532   0.521 45.94563  ? 1128 GLU   B CB   1 
ATOM   397  C  CG   A GLU   A 1 76  ? -25.23668 -10.40910 9.44491   0.479 47.41208  ? 1128 GLU   B CG   1 
ATOM   398  C  CG   B GLU   A 1 76  ? -25.89854 -8.94562  10.53635  0.521 45.69993  ? 1128 GLU   B CG   1 
ATOM   399  C  CD   A GLU   A 1 76  ? -26.72069 -10.63091 9.63804   0.479 43.99311  ? 1128 GLU   B CD   1 
ATOM   400  C  CD   B GLU   A 1 76  ? -25.38544 -8.10520  11.68900  0.521 47.15903  ? 1128 GLU   B CD   1 
ATOM   401  O  OE1  A GLU   A 1 76  ? -27.34761 -9.85157  10.38575  0.479 45.36006  ? 1128 GLU   B OE1  1 
ATOM   402  O  OE1  B GLU   A 1 76  ? -24.35439 -7.41835  11.52070  0.521 52.45641  ? 1128 GLU   B OE1  1 
ATOM   403  O  OE2  A GLU   A 1 76  ? -27.26078 -11.57811 9.02943   0.479 44.79486  ? 1128 GLU   B OE2  1 
ATOM   404  O  OE2  B GLU   A 1 76  ? -26.01541 -8.13473  12.76803  0.521 50.27583  ? 1128 GLU   B OE2  1 
ATOM   405  N  N    . ALA   A 1 77  ? -24.02842 -6.37190  7.67927   1.000 47.22244  ? 1129 ALA   B N    1 
ATOM   406  C  CA   . ALA   A 1 77  ? -23.66631 -4.96090  7.73970   1.000 44.07258  ? 1129 ALA   B CA   1 
ATOM   407  C  C    . ALA   A 1 77  ? -22.69531 -4.59642  6.62553   1.000 48.01431  ? 1129 ALA   B C    1 
ATOM   408  O  O    . ALA   A 1 77  ? -22.06340 -5.46071  6.01785   1.000 42.53712  ? 1129 ALA   B O    1 
ATOM   409  C  CB   . ALA   A 1 77  ? -23.06224 -4.59341  9.09954   1.000 45.19605  ? 1129 ALA   B CB   1 
ATOM   410  N  N    . SER   A 1 78  ? -22.57422 -3.29052  6.38801   1.000 40.87849  ? 1130 SER   B N    1 
ATOM   411  C  CA   . SER   A 1 78  ? -21.65821 -2.74699  5.39077   1.000 38.25359  ? 1130 SER   B CA   1 
ATOM   412  C  C    . SER   A 1 78  ? -21.23008 -1.34985  5.81520   1.000 47.74910  ? 1130 SER   B C    1 
ATOM   413  O  O    . SER   A 1 78  ? -22.06401 -0.54462  6.23891   1.000 42.78178  ? 1130 SER   B O    1 
ATOM   414  C  CB   . SER   A 1 78  ? -22.30724 -2.70848  4.00177   1.000 41.94528  ? 1130 SER   B CB   1 
ATOM   415  O  OG   . SER   A 1 78  ? -21.45422 -2.07392  3.06150   1.000 48.59434  ? 1130 SER   B OG   1 
ATOM   416  N  N    . TYR   A 1 79  ? -19.93307 -1.07300  5.69905   1.000 44.39777  ? 1131 TYR   B N    1 
ATOM   417  C  CA   . TYR   A 1 79  ? -19.36396 0.21910   6.05153   1.000 47.11221  ? 1131 TYR   B CA   1 
ATOM   418  C  C    . TYR   A 1 79  ? -18.39495 0.66259   4.96532   1.000 43.74595  ? 1131 TYR   B C    1 
ATOM   419  O  O    . TYR   A 1 79  ? -17.70003 -0.15570  4.35863   1.000 44.97854  ? 1131 TYR   B O    1 
ATOM   420  C  CB   . TYR   A 1 79  ? -18.62692 0.16257   7.39753   1.000 45.49529  ? 1131 TYR   B CB   1 
ATOM   421  C  CG   . TYR   A 1 79  ? -19.41894 -0.50193  8.49881   1.000 50.77782  ? 1131 TYR   B CG   1 
ATOM   422  C  CD1  . TYR   A 1 79  ? -20.26686 0.23646   9.31555   1.000 49.55028  ? 1131 TYR   B CD1  1 
ATOM   423  C  CD2  . TYR   A 1 79  ? -19.32104 -1.86785  8.71935   1.000 47.72933  ? 1131 TYR   B CD2  1 
ATOM   424  C  CE1  . TYR   A 1 79  ? -20.99688 -0.37008  10.32281  1.000 47.07447  ? 1131 TYR   B CE1  1 
ATOM   425  C  CE2  . TYR   A 1 79  ? -20.04306 -2.48440  9.72162   1.000 53.63552  ? 1131 TYR   B CE2  1 
ATOM   426  C  CZ   . TYR   A 1 79  ? -20.88098 -1.73002  10.51934  1.000 48.63376  ? 1131 TYR   B CZ   1 
ATOM   427  O  OH   . TYR   A 1 79  ? -21.60399 -2.33656  11.51760  1.000 43.05954  ? 1131 TYR   B OH   1 
ATOM   428  N  N    . ASN   A 1 80  ? -18.35486 1.97149   4.72580   1.000 44.16544  ? 1132 ASN   B N    1 
ATOM   429  C  CA   . ASN   A 1 80  ? -17.39884 2.54305   3.78955   1.000 48.20965  ? 1132 ASN   B CA   1 
ATOM   430  C  C    . ASN   A 1 80  ? -16.07680 2.77023   4.51042   1.000 47.49196  ? 1132 ASN   B C    1 
ATOM   431  O  O    . ASN   A 1 80  ? -16.03672 3.45264   5.53915   1.000 45.31423  ? 1132 ASN   B O    1 
ATOM   432  C  CB   . ASN   A 1 80  ? -17.93276 3.85186   3.21305   1.000 49.89920  ? 1132 ASN   B CB   1 
ATOM   433  C  CG   . ASN   A 1 80  ? -16.97574 4.47639   2.21477   1.000 63.22156  ? 1132 ASN   B CG   1 
ATOM   434  O  OD1  . ASN   A 1 80  ? -16.39882 3.79002   1.37303   1.000 63.66709  ? 1132 ASN   B OD1  1 
ATOM   435  N  ND2  . ASN   A 1 80  ? -16.79963 5.78842   2.31125   1.000 67.06520  ? 1132 ASN   B ND2  1 
ATOM   436  N  N    . CYS   A 1 81  ? -15.00186 2.19394   3.98262   1.000 42.83949  ? 1133 CYS   B N    1 
ATOM   437  C  CA   . CYS   A 1 81  ? -13.67883 2.35807   4.57451   1.000 40.25358  ? 1133 CYS   B CA   1 
ATOM   438  C  C    . CYS   A 1 81  ? -12.69381 3.05963   3.65421   1.000 44.60021  ? 1133 CYS   B C    1 
ATOM   439  O  O    . CYS   A 1 81  ? -11.90073 3.87776   4.12386   1.000 46.70593  ? 1133 CYS   B O    1 
ATOM   440  C  CB   . CYS   A 1 81  ? -13.11093 0.99119   4.99304   1.000 44.56858  ? 1133 CYS   B CB   1 
ATOM   441  S  SG   . CYS   A 1 81  ? -13.97694 0.22982   6.40136   1.000 44.97201  ? 1133 CYS   B SG   1 
ATOM   442  N  N    . HIS   A 1 82  ? -12.71987 2.76612   2.35532   1.000 42.15168  ? 1134 HIS   B N    1 
ATOM   443  C  CA   . HIS   A 1 82  ? -11.79185 3.37968   1.41905   1.000 41.43262  ? 1134 HIS   B CA   1 
ATOM   444  C  C    . HIS   A 1 82  ? -12.48487 3.57220   0.08100   1.000 43.40070  ? 1134 HIS   B C    1 
ATOM   445  O  O    . HIS   A 1 82  ? -13.52393 2.96517   -0.19173  1.000 40.52491  ? 1134 HIS   B O    1 
ATOM   446  C  CB   . HIS   A 1 82  ? -10.52592 2.53151   1.24335   1.000 42.16877  ? 1134 HIS   B CB   1 
ATOM   447  C  CG   . HIS   A 1 82  ? -9.85091  2.17697   2.53047   1.000 44.63304  ? 1134 HIS   B CG   1 
ATOM   448  N  ND1  . HIS   A 1 82  ? -8.91583  2.99213   3.13112   1.000 41.48176  ? 1134 HIS   B ND1  1 
ATOM   449  C  CD2  . HIS   A 1 82  ? -9.98097  1.09629   3.33590   1.000 35.72822  ? 1134 HIS   B CD2  1 
ATOM   450  C  CE1  . HIS   A 1 82  ? -8.49484  2.42654   4.25133   1.000 44.74981  ? 1134 HIS   B CE1  1 
ATOM   451  N  NE2  . HIS   A 1 82  ? -9.12492  1.27565   4.39581   1.000 38.69318  ? 1134 HIS   B NE2  1 
ATOM   452  N  N    . ASN   A 1 83  ? -11.90083 4.43282   -0.75536  1.000 43.88123  ? 1135 ASN   B N    1 
ATOM   453  C  CA   . ASN   A 1 83  ? -12.36085 4.61532   -2.12542  1.000 44.15732  ? 1135 ASN   B CA   1 
ATOM   454  C  C    . ASN   A 1 83  ? -11.53795 3.79686   -3.11912  1.000 47.54997  ? 1135 ASN   B C    1 
ATOM   455  O  O    . ASN   A 1 83  ? -11.51996 4.11239   -4.31225  1.000 51.35657  ? 1135 ASN   B O    1 
ATOM   456  C  CB   . ASN   A 1 83  ? -12.35475 6.09617   -2.51001  1.000 40.57246  ? 1135 ASN   B CB   1 
ATOM   457  C  CG   . ASN   A 1 83  ? -10.95571 6.66801   -2.63227  1.000 56.42317  ? 1135 ASN   B CG   1 
ATOM   458  O  OD1  . ASN   A 1 83  ? -10.04572 6.26522   -1.91014  1.000 51.97663  ? 1135 ASN   B OD1  1 
ATOM   459  N  ND2  . ASN   A 1 83  ? -10.77666 7.61363   -3.54865  1.000 52.01992  ? 1135 ASN   B ND2  1 
ATOM   460  N  N    . SER   A 1 84  ? -10.84501 2.76300   -2.63973  1.000 39.73954  ? 1136 SER   B N    1 
ATOM   461  C  CA   . SER   A 1 84  ? -10.21912 1.76461   -3.48936  1.000 37.46798  ? 1136 SER   B CA   1 
ATOM   462  C  C    . SER   A 1 84  ? -10.38820 0.40289   -2.82581  1.000 42.61625  ? 1136 SER   B C    1 
ATOM   463  O  O    . SER   A 1 84  ? -10.83018 0.29738   -1.67976  1.000 36.90978  ? 1136 SER   B O    1 
ATOM   464  C  CB   . SER   A 1 84  ? -8.73810  2.07539   -3.74752  1.000 32.06555  ? 1136 SER   B CB   1 
ATOM   465  O  OG   . SER   A 1 84  ? -7.98107  2.04981   -2.55053  1.000 40.14846  ? 1136 SER   B OG   1 
ATOM   466  N  N    . ALA   A 1 85  ? -10.03131 -0.64543  -3.55941  1.000 36.95386  ? 1137 ALA   B N    1 
ATOM   467  C  CA   . ALA   A 1 85  ? -10.27540 -2.00222  -3.08586  1.000 37.68164  ? 1137 ALA   B CA   1 
ATOM   468  C  C    . ALA   A 1 85  ? -9.45738  -2.30479  -1.83477  1.000 40.56444  ? 1137 ALA   B C    1 
ATOM   469  O  O    . ALA   A 1 85  ? -8.30435  -1.88183  -1.70597  1.000 36.52055  ? 1137 ALA   B O    1 
ATOM   470  C  CB   . ALA   A 1 85  ? -9.94451  -3.00769  -4.18648  1.000 29.89409  ? 1137 ALA   B CB   1 
ATOM   471  N  N    . ILE   A 1 86  ? -10.06241 -3.04538  -0.90946  1.000 37.02778  ? 1138 ILE   B N    1 
ATOM   472  C  CA   . ILE   A 1 86  ? -9.36041  -3.48196  0.29170   1.000 36.08647  ? 1138 ILE   B CA   1 
ATOM   473  C  C    . ILE   A 1 86  ? -8.50052  -4.68816  -0.05485  1.000 36.91177  ? 1138 ILE   B C    1 
ATOM   474  O  O    . ILE   A 1 86  ? -8.97461  -5.66036  -0.64945  1.000 41.38851  ? 1138 ILE   B O    1 
ATOM   475  C  CB   . ILE   A 1 86  ? -10.35240 -3.80744  1.41785   1.000 39.86809  ? 1138 ILE   B CB   1 
ATOM   476  C  CG1  . ILE   A 1 86  ? -11.25330 -2.60525  1.70440   1.000 32.16809  ? 1138 ILE   B CG1  1 
ATOM   477  C  CG2  . ILE   A 1 86  ? -9.60440  -4.21299  2.67999   1.000 26.53896  ? 1138 ILE   B CG2  1 
ATOM   478  C  CD1  . ILE   A 1 86  ? -12.17228 -2.80671  2.89451   1.000 43.62257  ? 1138 ILE   B CD1  1 
ATOM   479  N  N    . THR   A 1 87  ? -7.22350  -4.62412  0.31708   1.000 37.99992  ? 1139 THR   B N    1 
ATOM   480  C  CA   . THR   A 1 87  ? -6.28559  -5.70729  0.05349   1.000 37.89160  ? 1139 THR   B CA   1 
ATOM   481  C  C    . THR   A 1 87  ? -6.14163  -6.66284  1.22586   1.000 36.18397  ? 1139 THR   B C    1 
ATOM   482  O  O    . THR   A 1 87  ? -5.98473  -7.87093  1.02033   1.000 37.29215  ? 1139 THR   B O    1 
ATOM   483  C  CB   . THR   A 1 87  ? -4.90556  -5.14254  -0.30278  1.000 37.09469  ? 1139 THR   B CB   1 
ATOM   484  O  OG1  . THR   A 1 87  ? -4.45546  -4.28516  0.75387   1.000 33.95228  ? 1139 THR   B OG1  1 
ATOM   485  C  CG2  . THR   A 1 87  ? -4.96954  -4.35105  -1.60409  1.000 35.07007  ? 1139 THR   B CG2  1 
ATOM   486  N  N    . HIS   A 1 88  ? -6.20556  -6.15135  2.45266   1.000 37.19074  ? 1140 HIS   B N    1 
ATOM   487  C  CA   . HIS   A 1 88  ? -5.91858  -6.95090  3.63297   1.000 39.94346  ? 1140 HIS   B CA   1 
ATOM   488  C  C    . HIS   A 1 88  ? -6.56250  -6.28338  4.83872   1.000 37.78624  ? 1140 HIS   B C    1 
ATOM   489  O  O    . HIS   A 1 88  ? -6.71340  -5.06035  4.87724   1.000 39.29468  ? 1140 HIS   B O    1 
ATOM   490  C  CB   . HIS   A 1 88  ? -4.40459  -7.09394  3.83198   1.000 33.43674  ? 1140 HIS   B CB   1 
ATOM   491  C  CG   . HIS   A 1 88  ? -4.01563  -8.02153  4.94134   1.000 34.46109  ? 1140 HIS   B CG   1 
ATOM   492  N  ND1  . HIS   A 1 88  ? -3.74756  -7.58305  6.22015   1.000 36.80823  ? 1140 HIS   B ND1  1 
ATOM   493  C  CD2  . HIS   A 1 88  ? -3.83273  -9.36354  4.95886   1.000 34.01558  ? 1140 HIS   B CD2  1 
ATOM   494  C  CE1  . HIS   A 1 88  ? -3.42461  -8.61477  6.97955   1.000 33.55495  ? 1140 HIS   B CE1  1 
ATOM   495  N  NE2  . HIS   A 1 88  ? -3.46772  -9.70806  6.23699   1.000 38.04613  ? 1140 HIS   B NE2  1 
ATOM   496  N  N    . LEU   A 1 89  ? -6.94553  -7.09896  5.81806   1.000 37.30831  ? 1141 LEU   B N    1 
ATOM   497  C  CA   . LEU   A 1 89  ? -7.49645  -6.58442  7.06487   1.000 38.76142  ? 1141 LEU   B CA   1 
ATOM   498  C  C    . LEU   A 1 89  ? -7.12849  -7.52200  8.20323   1.000 36.08563  ? 1141 LEU   B C    1 
ATOM   499  O  O    . LEU   A 1 89  ? -6.76959  -8.68211  7.98768   1.000 41.01656  ? 1141 LEU   B O    1 
ATOM   500  C  CB   . LEU   A 1 89  ? -9.02044  -6.40134  6.98084   1.000 37.70221  ? 1141 LEU   B CB   1 
ATOM   501  C  CG   . LEU   A 1 89  ? -9.92554  -7.58741  6.62334   1.000 41.62070  ? 1141 LEU   B CG   1 
ATOM   502  C  CD1  . LEU   A 1 89  ? -9.93659  -8.64498  7.71576   1.000 47.27363  ? 1141 LEU   B CD1  1 
ATOM   503  C  CD2  . LEU   A 1 89  ? -11.34052 -7.10441  6.34119   1.000 40.08801  ? 1141 LEU   B CD2  1 
ATOM   504  N  N    . GLU   A 1 90  ? -7.21542  -7.00151  9.42403   1.000 39.91142  ? 1142 GLU   B N    1 
ATOM   505  C  CA   . GLU   A 1 90  ? -6.96744  -7.81006  10.61234  1.000 43.68378  ? 1142 GLU   B CA   1 
ATOM   506  C  C    . GLU   A 1 90  ? -7.76637  -7.28553  11.79915  1.000 39.11780  ? 1142 GLU   B C    1 
ATOM   507  O  O    . GLU   A 1 90  ? -7.59527  -6.12838  12.20769  1.000 41.75400  ? 1142 GLU   B O    1 
ATOM   508  C  CB   . GLU   A 1 90  ? -5.48144  -7.83203  10.97330  1.000 39.92193  ? 1142 GLU   B CB   1 
ATOM   509  C  CG   . GLU   A 1 90  ? -5.20546  -8.59155  12.26060  1.000 42.94670  ? 1142 GLU   B CG   1 
ATOM   510  C  CD   . GLU   A 1 90  ? -3.75744  -8.51448  12.70352  1.000 43.64949  ? 1142 GLU   B CD   1 
ATOM   511  O  OE1  . GLU   A 1 90  ? -2.98639  -7.72577  12.11719  1.000 41.75520  ? 1142 GLU   B OE1  1 
ATOM   512  O  OE2  . GLU   A 1 90  ? -3.38947  -9.24614  13.64480  1.000 47.43476  ? 1142 GLU   B OE2  1 
ATOM   513  N  N    . PRO   A 1 91  ? -8.64442  -8.10223  12.37950  1.000 40.31648  ? 1143 PRO   B N    1 
ATOM   514  C  CA   . PRO   A 1 91  ? -9.32635  -7.69869  13.61336  1.000 45.59121  ? 1143 PRO   B CA   1 
ATOM   515  C  C    . PRO   A 1 91  ? -8.50334  -8.04127  14.84448  1.000 45.12944  ? 1143 PRO   B C    1 
ATOM   516  O  O    . PRO   A 1 91  ? -7.92142  -9.12227  14.95989  1.000 47.29044  ? 1143 PRO   B O    1 
ATOM   517  C  CB   . PRO   A 1 91  ? -10.61641 -8.52561  13.57273  1.000 46.61116  ? 1143 PRO   B CB   1 
ATOM   518  C  CG   . PRO   A 1 91  ? -10.20053 -9.78891  12.88422  1.000 45.87809  ? 1143 PRO   B CG   1 
ATOM   519  C  CD   . PRO   A 1 91  ? -9.14353  -9.39439  11.87203  1.000 41.38509  ? 1143 PRO   B CD   1 
ATOM   520  N  N    . SER   A 1 92  ? -8.44824  -7.09090  15.77510  1.000 45.46950  ? 1144 SER   B N    1 
ATOM   521  C  CA   . SER   A 1 92  ? -7.81922  -7.36144  17.05719  1.000 45.29420  ? 1144 SER   B CA   1 
ATOM   522  C  C    . SER   A 1 92  ? -8.55029  -8.50011  17.76366  1.000 42.26616  ? 1144 SER   B C    1 
ATOM   523  O  O    . SER   A 1 92  ? -9.71332  -8.79913  17.48181  1.000 45.48293  ? 1144 SER   B O    1 
ATOM   524  C  CB   . SER   A 1 92  ? -7.81210  -6.11010  17.93169  1.000 44.30571  ? 1144 SER   B CB   1 
ATOM   525  O  OG   . SER   A 1 92  ? -9.13106  -5.69188  18.23556  1.000 47.67543  ? 1144 SER   B OG   1 
ATOM   526  N  N    . ARG   A 1 93  ? -7.84931  -9.14379  18.69989  1.000 47.78860  ? 1145 ARG   B N    1 
ATOM   527  C  CA   . ARG   A 1 93  ? -8.41538  -10.32649 19.34038  1.000 50.28675  ? 1145 ARG   B CA   1 
ATOM   528  C  C    . ARG   A 1 93  ? -9.59333  -9.98304  20.24628  1.000 43.43153  ? 1145 ARG   B C    1 
ATOM   529  O  O    . ARG   A 1 93  ? -10.50139 -10.80691 20.40963  1.000 46.23540  ? 1145 ARG   B O    1 
ATOM   530  C  CB   . ARG   A 1 93  ? -7.33642  -11.07227 20.12364  1.000 45.60030  ? 1145 ARG   B CB   1 
ATOM   531  C  CG   . ARG   A 1 93  ? -6.32050  -11.77670 19.24189  1.000 41.65803  ? 1145 ARG   B CG   1 
ATOM   532  C  CD   . ARG   A 1 93  ? -5.47255  -12.75445 20.04025  1.000 46.32819  ? 1145 ARG   B CD   1 
ATOM   533  N  NE   . ARG   A 1 93  ? -4.65747  -12.08111 21.04796  1.000 52.96088  ? 1145 ARG   B NE   1 
ATOM   534  C  CZ   . ARG   A 1 93  ? -3.43844  -11.60929 20.83174  1.000 58.12688  ? 1145 ARG   B CZ   1 
ATOM   535  N  NH1  . ARG   A 1 93  ? -2.85848  -11.70980 19.64576  1.000 47.82917  ? 1145 ARG   B NH1  1 
ATOM   536  N  NH2  . ARG   A 1 93  ? -2.78436  -11.01895 21.82749  1.000 55.40506  ? 1145 ARG   B NH2  1 
ATOM   537  N  N    . ASP   A 1 94  ? -9.61122  -8.78881  20.83481  1.000 46.25694  ? 1146 ASP   B N    1 
ATOM   538  C  CA   . ASP   A 1 94  ? -10.67016 -8.42236  21.76569  1.000 48.50311  ? 1146 ASP   B CA   1 
ATOM   539  C  C    . ASP   A 1 94  ? -11.89514 -7.82954  21.07849  1.000 52.64818  ? 1146 ASP   B C    1 
ATOM   540  O  O    . ASP   A 1 94  ? -12.85009 -7.45119  21.76537  1.000 63.42817  ? 1146 ASP   B O    1 
ATOM   541  C  CB   . ASP   A 1 94  ? -10.14006 -7.44898  22.82929  1.000 44.15106  ? 1146 ASP   B CB   1 
ATOM   542  C  CG   . ASP   A 1 94  ? -9.75297  -6.09523  22.25974  1.000 50.67251  ? 1146 ASP   B CG   1 
ATOM   543  O  OD1  . ASP   A 1 94  ? -10.15498 -5.76765  21.12363  1.000 55.27317  ? 1146 ASP   B OD1  1 
ATOM   544  O  OD2  . ASP   A 1 94  ? -9.03289  -5.35101  22.95743  1.000 58.07097  ? 1146 ASP   B OD2  1 
ATOM   545  N  N    . GLY   A 1 95  ? -11.88817 -7.72806  19.75045  1.000 57.78841  ? 1147 GLY   B N    1 
ATOM   546  C  CA   . GLY   A 1 95  ? -13.05316 -7.29227  19.00731  1.000 52.34936  ? 1147 GLY   B CA   1 
ATOM   547  C  C    . GLY   A 1 95  ? -13.30804 -5.80225  18.98873  1.000 48.92493  ? 1147 GLY   B C    1 
ATOM   548  O  O    . GLY   A 1 95  ? -14.35602 -5.37937  18.49160  1.000 49.57212  ? 1147 GLY   B O    1 
ATOM   549  N  N    . SER   A 1 96  ? -12.38196 -4.99012  19.49938  1.000 43.54681  ? 1148 SER   B N    1 
ATOM   550  C  CA   . SER   A 1 96  ? -12.59785 -3.55307  19.57782  1.000 53.80430  ? 1148 SER   B CA   1 
ATOM   551  C  C    . SER   A 1 96  ? -11.98982 -2.77558  18.41850  1.000 52.26359  ? 1148 SER   B C    1 
ATOM   552  O  O    . SER   A 1 96  ? -12.38174 -1.62464  18.19805  1.000 49.35174  ? 1148 SER   B O    1 
ATOM   553  C  CB   . SER   A 1 96  ? -12.02877 -3.00060  20.89059  1.000 50.92123  ? 1148 SER   B CB   1 
ATOM   554  O  OG   . SER   A 1 96  ? -10.61578 -3.09970  20.91458  1.000 59.22127  ? 1148 SER   B OG   1 
ATOM   555  N  N    . LEU   A 1 97  ? -11.05389 -3.36695  17.67570  1.000 53.23319  ? 1149 LEU   B N    1 
ATOM   556  C  CA   . LEU   A 1 97  ? -10.31986 -2.63641  16.65439  1.000 49.12421  ? 1149 LEU   B CA   1 
ATOM   557  C  C    . LEU   A 1 97  ? -10.21497 -3.47292  15.38672  1.000 49.33596  ? 1149 LEU   B C    1 
ATOM   558  O  O    . LEU   A 1 97  ? -10.33706 -4.69990  15.41321  1.000 47.73857  ? 1149 LEU   B O    1 
ATOM   559  C  CB   . LEU   A 1 97  ? -8.92282  -2.24632  17.15420  1.000 46.33723  ? 1149 LEU   B CB   1 
ATOM   560  C  CG   . LEU   A 1 97  ? -8.90371  -1.37082  18.40885  1.000 49.75655  ? 1149 LEU   B CG   1 
ATOM   561  C  CD1  . LEU   A 1 97  ? -7.48769  -1.23272  18.94675  1.000 47.34644  ? 1149 LEU   B CD1  1 
ATOM   562  C  CD2  . LEU   A 1 97  ? -9.50062  -0.00189  18.11432  1.000 44.46411  ? 1149 LEU   B CD2  1 
ATOM   563  N  N    . LEU   A 1 98  ? -9.99295  -2.78238  14.27044  1.000 46.86346  ? 1150 LEU   B N    1 
ATOM   564  C  CA   . LEU   A 1 98  ? -9.84103  -3.42490  12.97269  1.000 43.23921  ? 1150 LEU   B CA   1 
ATOM   565  C  C    . LEU   A 1 98  ? -8.80800  -2.67331  12.14636  1.000 41.49361  ? 1150 LEU   B C    1 
ATOM   566  O  O    . LEU   A 1 98  ? -8.86391  -1.44634  12.04888  1.000 43.21087  ? 1150 LEU   B O    1 
ATOM   567  C  CB   . LEU   A 1 98  ? -11.17406 -3.46810  12.21674  1.000 46.50155  ? 1150 LEU   B CB   1 
ATOM   568  C  CG   . LEU   A 1 98  ? -11.09014 -3.96368  10.77194  1.000 51.69333  ? 1150 LEU   B CG   1 
ATOM   569  C  CD1  . LEU   A 1 98  ? -10.74226 -5.44672  10.72651  1.000 43.72789  ? 1150 LEU   B CD1  1 
ATOM   570  C  CD2  . LEU   A 1 98  ? -12.38214 -3.68487  10.02087  1.000 41.44539  ? 1150 LEU   B CD2  1 
ATOM   571  N  N    . LEU   A 1 99  ? -7.87707  -3.40262  11.54662  1.000 44.43392  ? 1151 LEU   B N    1 
ATOM   572  C  CA   . LEU   A 1 99  ? -6.91806  -2.81706  10.62236  1.000 41.66008  ? 1151 LEU   B CA   1 
ATOM   573  C  C    . LEU   A 1 99  ? -7.34212  -3.10959  9.18949   1.000 35.57460  ? 1151 LEU   B C    1 
ATOM   574  O  O    . LEU   A 1 99  ? -7.74322  -4.23169  8.86395   1.000 41.75011  ? 1151 LEU   B O    1 
ATOM   575  C  CB   . LEU   A 1 99  ? -5.50909  -3.35707  10.87053  1.000 40.45983  ? 1151 LEU   B CB   1 
ATOM   576  C  CG   . LEU   A 1 99  ? -4.77501  -2.80364  12.09329  1.000 39.45476  ? 1151 LEU   B CG   1 
ATOM   577  C  CD1  . LEU   A 1 99  ? -3.42006  -3.47968  12.25852  1.000 43.92373  ? 1151 LEU   B CD1  1 
ATOM   578  C  CD2  . LEU   A 1 99  ? -4.61690  -1.29270  11.97969  1.000 36.92348  ? 1151 LEU   B CD2  1 
ATOM   579  N  N    . THR   A 1 100 ? -7.26907  -2.08994  8.33708   1.000 34.21166  ? 1152 THR   B N    1 
ATOM   580  C  CA   . THR   A 1 100 ? -7.53012  -2.25448  6.91616   1.000 35.92475  ? 1152 THR   B CA   1 
ATOM   581  C  C    . THR   A 1 100 ? -6.40110  -1.62588  6.11987   1.000 39.40596  ? 1152 THR   B C    1 
ATOM   582  O  O    . THR   A 1 100 ? -5.73901  -0.69075  6.57948   1.000 42.06702  ? 1152 THR   B O    1 
ATOM   583  C  CB   . THR   A 1 100 ? -8.86309  -1.61755  6.48394   1.000 39.33217  ? 1152 THR   B CB   1 
ATOM   584  O  OG1  . THR   A 1 100 ? -8.77597  -0.19051  6.59838   1.000 38.67095  ? 1152 THR   B OG1  1 
ATOM   585  C  CG2  . THR   A 1 100 ? -10.00710 -2.12112  7.34218   1.000 35.28009  ? 1152 THR   B CG2  1 
ATOM   586  N  N    . SER   A 1 101 ? -6.19217  -2.15437  4.91708   1.000 33.07875  ? 1153 SER   B N    1 
ATOM   587  C  CA   . SER   A 1 101 ? -5.27616  -1.58683  3.94283   1.000 39.02866  ? 1153 SER   B CA   1 
ATOM   588  C  C    . SER   A 1 101 ? -5.97019  -1.55531  2.59083   1.000 38.76879  ? 1153 SER   B C    1 
ATOM   589  O  O    . SER   A 1 101 ? -6.62828  -2.52442  2.20124   1.000 36.50968  ? 1153 SER   B O    1 
ATOM   590  C  CB   . SER   A 1 101 ? -3.97222  -2.39097  3.85311   1.000 38.00993  ? 1153 SER   B CB   1 
ATOM   591  O  OG   . SER   A 1 101 ? -3.26818  -2.36354  5.08307   1.000 44.48631  ? 1153 SER   B OG   1 
ATOM   592  N  N    . ALA   A 1 102 ? -5.82813  -0.44460  1.88239   1.000 40.23029  ? 1154 ALA   B N    1 
ATOM   593  C  CA   . ALA   A 1 102 ? -6.47115  -0.26407  0.58934   1.000 38.85690  ? 1154 ALA   B CA   1 
ATOM   594  C  C    . ALA   A 1 102 ? -5.44020  -0.38659  -0.52865  1.000 40.87327  ? 1154 ALA   B C    1 
ATOM   595  O  O    . ALA   A 1 102 ? -4.25521  -0.63859  -0.29458  1.000 46.73070  ? 1154 ALA   B O    1 
ATOM   596  C  CB   . ALA   A 1 102 ? -7.19505  1.08397   0.53482   1.000 37.40392  ? 1154 ALA   B CB   1 
ATOM   597  N  N    . THR   A 1 103 ? -5.91122  -0.19504  -1.75871  1.000 43.25969  ? 1155 THR   B N    1 
ATOM   598  C  CA   . THR   A 1 103 ? -5.09826  -0.33158  -2.96268  1.000 40.45521  ? 1155 THR   B CA   1 
ATOM   599  C  C    . THR   A 1 103 ? -4.52818  0.99118   -3.45122  1.000 45.00966  ? 1155 THR   B C    1 
ATOM   600  O  O    . THR   A 1 103 ? -3.34518  1.06496   -3.79728  1.000 39.47948  ? 1155 THR   B O    1 
ATOM   601  C  CB   . THR   A 1 103 ? -5.92835  -0.95496  -4.09041  1.000 41.05571  ? 1155 THR   B CB   1 
ATOM   602  O  OG1  . THR   A 1 103 ? -6.50243  -2.19274  -3.65290  1.000 42.15348  ? 1155 THR   B OG1  1 
ATOM   603  C  CG2  . THR   A 1 103 ? -5.06240  -1.20151  -5.31333  1.000 43.90262  ? 1155 THR   B CG2  1 
ATOM   604  N  N    . TRP   A 1 104 ? -5.35010  2.03723   -3.49161  1.000 41.47701  ? 1156 TRP   B N    1 
ATOM   605  C  CA   . TRP   A 1 104 ? -4.95001  3.31698   -4.05913  1.000 43.88148  ? 1156 TRP   B CA   1 
ATOM   606  C  C    . TRP   A 1 104 ? -5.81591  4.42128   -3.47354  1.000 43.34785  ? 1156 TRP   B C    1 
ATOM   607  O  O    . TRP   A 1 104 ? -6.60988  5.04205   -4.18876  1.000 43.73030  ? 1156 TRP   B O    1 
ATOM   608  C  CB   . TRP   A 1 104 ? -5.07106  3.27138   -5.58310  1.000 42.37724  ? 1156 TRP   B CB   1 
ATOM   609  C  CG   . TRP   A 1 104 ? -4.44899  4.43005   -6.29758  1.000 50.68891  ? 1156 TRP   B CG   1 
ATOM   610  C  CD1  . TRP   A 1 104 ? -3.49691  5.28017   -5.81495  1.000 48.05157  ? 1156 TRP   B CD1  1 
ATOM   611  C  CD2  . TRP   A 1 104 ? -4.73600  4.86455   -7.63174  1.000 47.48898  ? 1156 TRP   B CD2  1 
ATOM   612  N  NE1  . TRP   A 1 104 ? -3.17287  6.21777   -6.76833  1.000 44.54533  ? 1156 TRP   B NE1  1 
ATOM   613  C  CE2  . TRP   A 1 104 ? -3.91992  5.98538   -7.89221  1.000 46.11165  ? 1156 TRP   B CE2  1 
ATOM   614  C  CE3  . TRP   A 1 104 ? -5.60606  4.41622   -8.63054  1.000 35.80377  ? 1156 TRP   B CE3  1 
ATOM   615  C  CZ2  . TRP   A 1 104 ? -3.94990  6.66290   -9.11048  1.000 44.98335  ? 1156 TRP   B CZ2  1 
ATOM   616  C  CZ3  . TRP   A 1 104 ? -5.63304  5.08974   -9.83781  1.000 42.01503  ? 1156 TRP   B CZ3  1 
ATOM   617  C  CH2  . TRP   A 1 104 ? -4.81097  6.20159   -10.06727 1.000 45.18249  ? 1156 TRP   B CH2  1 
ATOM   618  N  N    . SER   A 1 105 ? -5.68185  4.66978   -2.17164  1.000 44.61679  ? 1157 SER   B N    1 
ATOM   619  C  CA   . SER   A 1 105 ? -6.49175  5.67411   -1.50101  1.000 47.71928  ? 1157 SER   B CA   1 
ATOM   620  C  C    . SER   A 1 105 ? -5.66267  6.34148   -0.41430  1.000 46.22349  ? 1157 SER   B C    1 
ATOM   621  O  O    . SER   A 1 105 ? -4.56870  5.88853   -0.06915  1.000 49.19193  ? 1157 SER   B O    1 
ATOM   622  C  CB   . SER   A 1 105 ? -7.76378  5.06644   -0.90473  1.000 48.41876  ? 1157 SER   B CB   1 
ATOM   623  O  OG   . SER   A 1 105 ? -7.51679  4.51393   0.37648   1.000 55.81101  ? 1157 SER   B OG   1 
ATOM   624  N  N    . GLN   A 1 106 ? -6.20857  7.42773   0.13028   1.000 56.60158  ? 1158 GLN   B N    1 
ATOM   625  C  CA   . GLN   A 1 106 ? -5.55148  8.20110   1.17696   1.000 53.42608  ? 1158 GLN   B CA   1 
ATOM   626  C  C    . GLN   A 1 106 ? -6.53743  8.35863   2.32493   1.000 53.63470  ? 1158 GLN   B C    1 
ATOM   627  O  O    . GLN   A 1 106 ? -7.61339  8.96064   2.13472   1.000 55.14005  ? 1158 GLN   B O    1 
ATOM   628  C  CB   . GLN   A 1 106 ? -5.08839  9.56285   0.65641   1.000 49.11570  ? 1158 GLN   B CB   1 
ATOM   629  C  CG   . GLN   A 1 106 ? -4.21243  9.48030   -0.58159  1.000 56.13943  ? 1158 GLN   B CG   1 
ATOM   630  C  CD   . GLN   A 1 106 ? -3.53834  10.80011  -0.90913  1.000 71.97977  ? 1158 GLN   B CD   1 
ATOM   631  O  OE1  . GLN   A 1 106 ? -4.15728  11.70994  -1.46347  1.000 56.68945  ? 1158 GLN   B OE1  1 
ATOM   632  N  NE2  . GLN   A 1 106 ? -2.26032  10.91115  -0.56321  1.000 77.78321  ? 1158 GLN   B NE2  1 
ATOM   633  N  N    . PRO   A 1 107 ? -6.23244  7.84108   3.52312   1.000 51.82402  ? 1159 PRO   B N    1 
ATOM   634  C  CA   . PRO   A 1 107 ? -4.99948  7.13413   3.89937   1.000 52.53883  ? 1159 PRO   B CA   1 
ATOM   635  C  C    . PRO   A 1 107 ? -4.91561  5.75587   3.25291   1.000 51.20363  ? 1159 PRO   B C    1 
ATOM   636  O  O    . PRO   A 1 107 ? -5.92866  5.19579   2.84516   1.000 47.26749  ? 1159 PRO   B O    1 
ATOM   637  C  CB   . PRO   A 1 107 ? -5.11544  7.04874   5.42640   1.000 51.38695  ? 1159 PRO   B CB   1 
ATOM   638  C  CG   . PRO   A 1 107 ? -6.59444  6.95896   5.66948   1.000 52.90753  ? 1159 PRO   B CG   1 
ATOM   639  C  CD   . PRO   A 1 107 ? -7.20840  7.86659   4.62914   1.000 44.41377  ? 1159 PRO   B CD   1 
ATOM   640  N  N    . LEU   A 1 108 ? -3.72966  5.17272   3.12210   1.000 53.54755  ? 1160 LEU   B N    1 
ATOM   641  C  CA   . LEU   A 1 108 ? -3.59778  3.82747   2.50163   1.000 50.83104  ? 1160 LEU   B CA   1 
ATOM   642  C  C    . LEU   A 1 108 ? -4.05083  2.74690   3.49707   1.000 41.86025  ? 1160 LEU   B C    1 
ATOM   643  O  O    . LEU   A 1 108 ? -4.69592  1.78877   3.05947   1.000 39.79939  ? 1160 LEU   B O    1 
ATOM   644  C  CB   . LEU   A 1 108 ? -2.18682  3.55516   1.99070   1.000 44.28213  ? 1160 LEU   B CB   1 
ATOM   645  C  CG   . LEU   A 1 108 ? -2.06193  2.53270   0.86110   1.000 53.61463  ? 1160 LEU   B CG   1 
ATOM   646  C  CD1  . LEU   A 1 108 ? -3.13394  2.73737   -0.19095  1.000 42.15966  ? 1160 LEU   B CD1  1 
ATOM   647  C  CD2  . LEU   A 1 108 ? -0.67994  2.65935   0.25201   1.000 55.08315  ? 1160 LEU   B CD2  1 
ATOM   648  N  N    . SER   A 1 109 ? -3.71478  2.90238   4.77200   1.000 40.00699  ? 1161 SER   B N    1 
ATOM   649  C  CA   . SER   A 1 109 ? -4.16483  1.95081   5.78039   1.000 42.46319  ? 1161 SER   B CA   1 
ATOM   650  C  C    . SER   A 1 109 ? -4.85174  2.70431   6.91111   1.000 45.35473  ? 1161 SER   B C    1 
ATOM   651  O  O    . SER   A 1 109 ? -4.66464  3.91037   7.08663   1.000 45.39888  ? 1161 SER   B O    1 
ATOM   652  C  CB   . SER   A 1 109 ? -3.00288  1.10593   6.31969   1.000 44.35141  ? 1161 SER   B CB   1 
ATOM   653  O  OG   . SER   A 1 109 ? -2.44597  0.29948   5.29500   1.000 41.68317  ? 1161 SER   B OG   1 
ATOM   654  N  N    . ALA   A 1 110 ? -5.64877  1.97968   7.69243   1.000 45.03839  ? 1162 ALA   B N    1 
ATOM   655  C  CA   . ALA   A 1 110 ? -6.43869  2.63315   8.72419   1.000 45.90960  ? 1162 ALA   B CA   1 
ATOM   656  C  C    . ALA   A 1 110 ? -6.72973  1.67563   9.86858   1.000 43.75731  ? 1162 ALA   B C    1 
ATOM   657  O  O    . ALA   A 1 110 ? -6.74683  0.45056   9.70306   1.000 37.33898  ? 1162 ALA   B O    1 
ATOM   658  C  CB   . ALA   A 1 110 ? -7.74666  3.19203   8.15401   1.000 43.78184  ? 1162 ALA   B CB   1 
ATOM   659  N  N    . LEU   A 1 111 ? -6.96765  2.26911   11.03935  1.000 46.51810  ? 1163 LEU   B N    1 
ATOM   660  C  CA   . LEU   A 1 111 ? -7.38067  1.57362   12.25064  1.000 50.29926  ? 1163 LEU   B CA   1 
ATOM   661  C  C    . LEU   A 1 111 ? -8.75662  2.09088   12.64747  1.000 52.46737  ? 1163 LEU   B C    1 
ATOM   662  O  O    . LEU   A 1 111 ? -8.92552  3.29399   12.88100  1.000 55.09626  ? 1163 LEU   B O    1 
ATOM   663  C  CB   . LEU   A 1 111 ? -6.38062  1.79499   13.38552  1.000 44.61501  ? 1163 LEU   B CB   1 
ATOM   664  C  CG   . LEU   A 1 111 ? -6.80662  1.24656   14.74875  1.000 43.58354  ? 1163 LEU   B CG   1 
ATOM   665  C  CD1  . LEU   A 1 111 ? -6.76574  -0.27144  14.74635  1.000 40.09830  ? 1163 LEU   B CD1  1 
ATOM   666  C  CD2  . LEU   A 1 111 ? -5.94654  1.81694   15.86550  1.000 44.93903  ? 1163 LEU   B CD2  1 
ATOM   667  N  N    . TRP   A 1 112 ? -9.69869  1.15398   12.69987  1.000 47.55675  ? 1164 TRP   B N    1 
ATOM   668  C  CA   . TRP   A 1 112 ? -11.10965 1.48519   12.95078  1.000 46.93580  ? 1164 TRP   B CA   1 
ATOM   669  C  C    . TRP   A 1 112 ? -11.57765 0.96476   14.29700  1.000 53.34318  ? 1164 TRP   B C    1 
ATOM   670  O  O    . TRP   A 1 112 ? -11.10272 -0.09411  14.72841  1.000 52.72143  ? 1164 TRP   B O    1 
ATOM   671  C  CB   . TRP   A 1 112 ? -11.94574 0.81282   11.85807  1.000 44.57116  ? 1164 TRP   B CB   1 
ATOM   672  C  CG   . TRP   A 1 112 ? -11.46676 1.10023   10.46394  1.000 48.43880  ? 1164 TRP   B CG   1 
ATOM   673  C  CD1  . TRP   A 1 112 ? -10.49883 0.44188   9.76718   1.000 42.94669  ? 1164 TRP   B CD1  1 
ATOM   674  C  CD2  . TRP   A 1 112 ? -11.94770 2.14493   9.59655   1.000 43.96470  ? 1164 TRP   B CD2  1 
ATOM   675  N  NE1  . TRP   A 1 112 ? -10.34282 1.00438   8.53095   1.000 43.86707  ? 1164 TRP   B NE1  1 
ATOM   676  C  CE2  . TRP   A 1 112 ? -11.21774 2.04639   8.39556   1.000 47.80277  ? 1164 TRP   B CE2  1 
ATOM   677  C  CE3  . TRP   A 1 112 ? -12.91862 3.14105   9.71718   1.000 50.78913  ? 1164 TRP   B CE3  1 
ATOM   678  C  CZ2  . TRP   A 1 112 ? -11.42571 2.91399   7.32923   1.000 46.36255  ? 1164 TRP   B CZ2  1 
ATOM   679  C  CZ3  . TRP   A 1 112 ? -13.12558 3.99665   8.66185   1.000 47.82293  ? 1164 TRP   B CZ3  1 
ATOM   680  C  CH2  . TRP   A 1 112 ? -12.39063 3.88112   7.48487   1.000 42.22567  ? 1164 TRP   B CH2  1 
ATOM   681  N  N    . GLY   A 1 113 ? -12.51458 1.68207   14.90975  1.000 52.13957  ? 1165 GLY   B N    1 
ATOM   682  C  CA   . GLY   A 1 113 ? -13.11458 1.21061   16.15995  1.000 52.70686  ? 1165 GLY   B CA   1 
ATOM   683  C  C    . GLY   A 1 113 ? -14.33665 0.40557   15.81130  1.000 59.64144  ? 1165 GLY   B C    1 
ATOM   684  O  O    . GLY   A 1 113 ? -15.07765 0.81927   14.90816  1.000 56.18593  ? 1165 GLY   B O    1 
ATOM   685  N  N    . MET   A 1 114 ? -14.51472 -0.72415  16.47676  1.000 55.48446  ? 1166 MET   B N    1 
ATOM   686  C  CA   . MET   A 1 114 ? -15.65780 -1.60818  16.17214  1.000 61.13299  ? 1166 MET   B CA   1 
ATOM   687  C  C    . MET   A 1 114 ? -16.59377 -1.68263  17.39020  1.000 73.69763  ? 1166 MET   B C    1 
ATOM   688  O  O    . MET   A 1 114 ? -17.68882 -2.24361  17.23745  1.000 74.42010  ? 1166 MET   B O    1 
ATOM   689  C  CB   . MET   A 1 114 ? -15.13292 -2.99937  15.81668  1.000 56.90143  ? 1166 MET   B CB   1 
ATOM   690  C  CG   . MET   A 1 114 ? -14.16095 -2.99890  14.66165  1.000 56.04982  ? 1166 MET   B CG   1 
ATOM   691  S  SD   . MET   A 1 114 ? -14.63308 -4.22535  13.43015  1.000 72.34464  ? 1166 MET   B SD   1 
ATOM   692  C  CE   . MET   A 1 114 ? -13.81417 -5.65113  14.15169  1.000 51.70830  ? 1166 MET   B CE   1 
ATOM   693  N  N    . LYS   A 1 115 ? -16.16569 -1.16720  18.55298  1.000 80.19853  ? 1167 LYS   B N    1 
ATOM   694  C  CA   . LYS   A 1 115 ? -16.98567 -1.27665  19.78205  1.000 81.05811  ? 1167 LYS   B CA   1 
ATOM   695  C  C    . LYS   A 1 115 ? -18.13759 -0.28461  19.65669  1.000 84.99231  ? 1167 LYS   B C    1 
ATOM   696  O  O    . LYS   A 1 115 ? -17.86451 0.91328   19.45021  1.000 83.11137  ? 1167 LYS   B O    1 
ATOM   697  C  CB   . LYS   A 1 115 ? -16.15361 -1.02622  21.03993  1.000 79.31446  ? 1167 LYS   B CB   1 
ATOM   698  C  CG   . LYS   A 1 115 ? -15.90468 -2.27090  21.88341  1.000 80.09446  ? 1167 LYS   B CG   1 
ATOM   699  C  CD   . LYS   A 1 115 ? -16.36280 -3.57113  21.23194  1.000 66.60350  ? 1167 LYS   B CD   1 
ATOM   700  C  CE   . LYS   A 1 115 ? -15.73688 -4.76592  21.87539  1.000 62.68621  ? 1167 LYS   B CE   1 
ATOM   701  N  NZ   . LYS   A 1 115 ? -16.02699 -6.00119  21.14289  1.000 69.33645  ? 1167 LYS   B NZ   1 
ATOM   702  N  N    . SER   A 1 116 ? -19.36563 -0.78647  19.77593  1.000 91.67228  ? 1168 SER   B N    1 
ATOM   703  C  CA   . SER   A 1 116 ? -20.56457 0.07056   19.61862  1.000 87.59271  ? 1168 SER   B CA   1 
ATOM   704  C  C    . SER   A 1 116 ? -20.59157 0.63100   18.19140  1.000 85.17351  ? 1168 SER   B C    1 
ATOM   705  O  O    . SER   A 1 116 ? -20.98265 -0.12133  17.28071  1.000 92.86903  ? 1168 SER   B O    1 
ATOM   706  C  CB   . SER   A 1 116 ? -20.61145 1.14698   20.67120  1.000 84.70513  ? 1168 SER   B CB   1 
ATOM   707  O  OG   . SER   A 1 116 ? -20.07245 0.68643   21.90136  1.000 78.66671  ? 1168 SER   B OG   1 
ATOM   708  N  N    . VAL   A 1 117 ? -20.16247 1.87389   17.99590  1.000 83.89718  ? 1169 VAL   B N    1 
ATOM   709  C  CA   . VAL   A 1 117 ? -20.27747 2.50236   16.64365  1.000 82.08463  ? 1169 VAL   B CA   1 
ATOM   710  C  C    . VAL   A 1 117 ? -19.01551 2.19694   15.82673  1.000 79.42702  ? 1169 VAL   B C    1 
ATOM   711  O  O    . VAL   A 1 117 ? -17.94051 2.00110   16.43178  1.000 76.24465  ? 1169 VAL   B O    1 
ATOM   712  C  CB   . VAL   A 1 117 ? -20.50635 4.02141   16.72606  1.000 78.34991  ? 1169 VAL   B CB   1 
ATOM   713  C  CG1  . VAL   A 1 117 ? -21.96331 4.35664   17.01397  1.000 75.16449  ? 1169 VAL   B CG1  1 
ATOM   714  C  CG2  . VAL   A 1 117 ? -19.58026 4.67474   17.74377  1.000 70.68301  ? 1169 VAL   B CG2  1 
ATOM   715  N  N    . PHE   A 1 118 ? -19.15255 2.18343   14.50474  1.000 71.98169  ? 1170 PHE   B N    1 
ATOM   716  C  CA   . PHE   A 1 118 ? -17.98760 1.91901   13.67081  1.000 62.80085  ? 1170 PHE   B CA   1 
ATOM   717  C  C    . PHE   A 1 118 ? -17.42351 3.24477   13.17127  1.000 64.52881  ? 1170 PHE   B C    1 
ATOM   718  O  O    . PHE   A 1 118 ? -18.10348 3.97653   12.44100  1.000 65.69141  ? 1170 PHE   B O    1 
ATOM   719  C  CB   . PHE   A 1 118 ? -18.35570 1.01057   12.49718  1.000 55.45664  ? 1170 PHE   B CB   1 
ATOM   720  C  CG   . PHE   A 1 118 ? -17.18376 0.60714   11.64531  1.000 60.36621  ? 1170 PHE   B CG   1 
ATOM   721  C  CD1  . PHE   A 1 118 ? -16.75673 1.41570   10.60498  1.000 53.77473  ? 1170 PHE   B CD1  1 
ATOM   722  C  CD2  . PHE   A 1 118 ? -16.51585 -0.58282  11.88276  1.000 61.53299  ? 1170 PHE   B CD2  1 
ATOM   723  C  CE1  . PHE   A 1 118 ? -15.67878 1.04830   9.81809   1.000 56.64849  ? 1170 PHE   B CE1  1 
ATOM   724  C  CE2  . PHE   A 1 118 ? -15.43790 -0.95721  11.10088  1.000 60.56690  ? 1170 PHE   B CE2  1 
ATOM   725  C  CZ   . PHE   A 1 118 ? -15.01886 -0.13865  10.06654  1.000 56.16975  ? 1170 PHE   B CZ   1 
ATOM   726  N  N    . ASP   A 1 119 ? -16.18448 3.54582   13.55712  1.000 54.95984  ? 1171 ASP   B N    1 
ATOM   727  C  CA   . ASP   A 1 119 ? -15.53139 4.79062   13.17760  1.000 58.01998  ? 1171 ASP   B CA   1 
ATOM   728  C  C    . ASP   A 1 119 ? -14.04742 4.52942   12.96766  1.000 58.61699  ? 1171 ASP   B C    1 
ATOM   729  O  O    . ASP   A 1 119 ? -13.52749 3.45751   13.29407  1.000 56.22959  ? 1171 ASP   B O    1 
ATOM   730  C  CB   . ASP   A 1 119 ? -15.73427 5.87806   14.24218  1.000 61.14657  ? 1171 ASP   B CB   1 
ATOM   731  C  CG   . ASP   A 1 119 ? -15.18827 5.47355   15.60132  1.000 63.15380  ? 1171 ASP   B CG   1 
ATOM   732  O  OD1  . ASP   A 1 119 ? -15.36835 4.29972   15.99079  1.000 66.30400  ? 1171 ASP   B OD1  1 
ATOM   733  O  OD2  . ASP   A 1 119 ? -14.57118 6.32577   16.27697  1.000 65.76929  ? 1171 ASP   B OD2  1 
ATOM   734  N  N    . MET   A 1 120 ? -13.36136 5.52615   12.41225  1.000 50.02249  ? 1172 MET   B N    1 
ATOM   735  C  CA   . MET   A 1 120 ? -11.92137 5.45096   12.20824  1.000 50.09123  ? 1172 MET   B CA   1 
ATOM   736  C  C    . MET   A 1 120 ? -11.21529 6.03738   13.42298  1.000 54.28714  ? 1172 MET   B C    1 
ATOM   737  O  O    . MET   A 1 120 ? -11.40919 7.21253   13.75252  1.000 60.24870  ? 1172 MET   B O    1 
ATOM   738  C  CB   . MET   A 1 120 ? -11.49735 6.19242   10.94093  1.000 48.94614  ? 1172 MET   B CB   1 
ATOM   739  C  CG   . MET   A 1 120 ? -9.99036  6.13621   10.68991  1.000 53.02955  ? 1172 MET   B CG   1 
ATOM   740  S  SD   . MET   A 1 120 ? -9.38330  7.30967   9.45943   1.000 61.65590  ? 1172 MET   B SD   1 
ATOM   741  C  CE   . MET   A 1 120 ? -10.07940 6.62813   7.95572   1.000 59.10121  ? 1172 MET   B CE   1 
ATOM   742  N  N    . LYS   A 1 121 ? -10.39933 5.21858   14.09028  1.000 56.70286  ? 1173 LYS   B N    1 
ATOM   743  C  CA   . LYS   A 1 121 ? -9.58926  5.72696   15.19006  1.000 54.22768  ? 1173 LYS   B CA   1 
ATOM   744  C  C    . LYS   A 1 121 ? -8.35722  6.45165   14.66874  1.000 58.77462  ? 1173 LYS   B C    1 
ATOM   745  O  O    . LYS   A 1 121 ? -8.07112  7.58080   15.08428  1.000 59.96196  ? 1173 LYS   B O    1 
ATOM   746  C  CB   . LYS   A 1 121 ? -9.17932  4.58529   16.12350  1.000 56.27866  ? 1173 LYS   B CB   1 
ATOM   747  C  CG   . LYS   A 1 121 ? -10.34235 3.90866   16.82680  1.000 65.91225  ? 1173 LYS   B CG   1 
ATOM   748  C  CD   . LYS   A 1 121 ? -11.28325 4.92598   17.45043  1.000 64.92685  ? 1173 LYS   B CD   1 
ATOM   749  C  CE   . LYS   A 1 121 ? -12.40729 4.23537   18.20273  1.000 67.81862  ? 1173 LYS   B CE   1 
ATOM   750  N  NZ   . LYS   A 1 121 ? -13.61321 5.09351   18.32743  1.000 74.35903  ? 1173 LYS   B NZ   1 
ATOM   751  N  N    . HIS   A 1 122 ? -7.62429  5.82723   13.75296  1.000 54.25365  ? 1174 HIS   B N    1 
ATOM   752  C  CA   . HIS   A 1 122 ? -6.38926  6.42695   13.26469  1.000 57.27092  ? 1174 HIS   B CA   1 
ATOM   753  C  C    . HIS   A 1 122 ? -6.16933  6.03735   11.81083  1.000 53.28787  ? 1174 HIS   B C    1 
ATOM   754  O  O    . HIS   A 1 122 ? -6.78442  5.10520   11.29722  1.000 54.53709  ? 1174 HIS   B O    1 
ATOM   755  C  CB   . HIS   A 1 122 ? -5.18727  6.01219   14.12182  1.000 53.00878  ? 1174 HIS   B CB   1 
ATOM   756  C  CG   . HIS   A 1 122 ? -5.19818  6.59874   15.49958  1.000 59.75658  ? 1174 HIS   B CG   1 
ATOM   757  N  ND1  . HIS   A 1 122 ? -5.17621  5.82519   16.63889  1.000 61.99219  ? 1174 HIS   B ND1  1 
ATOM   758  C  CD2  . HIS   A 1 122 ? -5.23507  7.88591   15.92008  1.000 61.05259  ? 1174 HIS   B CD2  1 
ATOM   759  C  CE1  . HIS   A 1 122 ? -5.19912  6.60961   17.70158  1.000 56.99295  ? 1174 HIS   B CE1  1 
ATOM   760  N  NE2  . HIS   A 1 122 ? -5.23403  7.86445   17.29308  1.000 69.25773  ? 1174 HIS   B NE2  1 
ATOM   761  N  N    . SER   A 1 123 ? -5.27930  6.77102   11.14952  1.000 54.25452  ? 1175 SER   B N    1 
ATOM   762  C  CA   . SER   A 1 123 ? -4.90436  6.47945   9.77662   1.000 55.42575  ? 1175 SER   B CA   1 
ATOM   763  C  C    . SER   A 1 123 ? -3.39337  6.34130   9.68363   1.000 53.34617  ? 1175 SER   B C    1 
ATOM   764  O  O    . SER   A 1 123 ? -2.64530  6.97553   10.43436  1.000 50.00572  ? 1175 SER   B O    1 
ATOM   765  C  CB   . SER   A 1 123 ? -5.38430  7.56710   8.80721   1.000 52.92626  ? 1175 SER   B CB   1 
ATOM   766  O  OG   . SER   A 1 123 ? -4.36524  8.52293   8.57280   1.000 57.81473  ? 1175 SER   B OG   1 
ATOM   767  N  N    . PHE   A 1 124 ? -2.95247  5.49889   8.75695   1.000 54.31925  ? 1176 PHE   B N    1 
ATOM   768  C  CA   . PHE   A 1 124 ? -1.54249  5.30966   8.43899   1.000 44.96842  ? 1176 PHE   B CA   1 
ATOM   769  C  C    . PHE   A 1 124 ? -1.43751  5.61606   6.94886   1.000 62.04226  ? 1176 PHE   B C    1 
ATOM   770  O  O    . PHE   A 1 124 ? -1.85060  4.81276   6.10019   1.000 62.87476  ? 1176 PHE   B O    1 
ATOM   771  C  CB   . PHE   A 1 124 ? -1.09359  3.90377   8.81153   1.000 44.06428  ? 1176 PHE   B CB   1 
ATOM   772  C  CG   . PHE   A 1 124 ? -1.64558  3.44234   10.13373  1.000 47.77470  ? 1176 PHE   B CG   1 
ATOM   773  C  CD1  . PHE   A 1 124 ? -1.09052  3.88377   11.32454  1.000 43.09013  ? 1176 PHE   B CD1  1 
ATOM   774  C  CD2  . PHE   A 1 124 ? -2.74065  2.59744   10.18710  1.000 43.38976  ? 1176 PHE   B CD2  1 
ATOM   775  C  CE1  . PHE   A 1 124 ? -1.60351  3.47329   12.54272  1.000 44.12252  ? 1176 PHE   B CE1  1 
ATOM   776  C  CE2  . PHE   A 1 124 ? -3.25865  2.18097   11.40328  1.000 45.36629  ? 1176 PHE   B CE2  1 
ATOM   777  C  CZ   . PHE   A 1 124 ? -2.68858  2.61739   12.58109  1.000 50.32193  ? 1176 PHE   B CZ   1 
ATOM   778  N  N    . THR   A 1 125 ? -0.90043  6.80190   6.65238   1.000 45.58459  ? 1177 THR   B N    1 
ATOM   779  C  CA   . THR   A 1 125 ? -1.17341  7.46242   5.38012   1.000 52.95781  ? 1177 THR   B CA   1 
ATOM   780  C  C    . THR   A 1 125 ? -0.67451  6.64291   4.19743   1.000 50.94570  ? 1177 THR   B C    1 
ATOM   781  O  O    . THR   A 1 125 ? -1.43956  6.33561   3.27558   1.000 58.38521  ? 1177 THR   B O    1 
ATOM   782  C  CB   . THR   A 1 125 ? -0.54930  8.86137   5.37955   1.000 62.49333  ? 1177 THR   B CB   1 
ATOM   783  O  OG1  . THR   A 1 125 ? -0.68330  9.44987   4.08032   1.000 66.67990  ? 1177 THR   B OG1  1 
ATOM   784  C  CG2  . THR   A 1 125 ? 0.92570   8.80041   5.76753   1.000 55.15893  ? 1177 THR   B CG2  1 
ATOM   785  N  N    . GLU   A 1 126 ? 0.60746   6.28481   4.19654   1.000 47.67668  ? 1178 GLU   B N    1 
ATOM   786  C  CA   . GLU   A 1 126 ? 1.21538   5.63531   3.04278   1.000 53.76181  ? 1178 GLU   B CA   1 
ATOM   787  C  C    . GLU   A 1 126 ? 1.70328   4.22239   3.33932   1.000 48.40789  ? 1178 GLU   B C    1 
ATOM   788  O  O    . GLU   A 1 126 ? 2.40421   3.63400   2.50653   1.000 46.78290  ? 1178 GLU   B O    1 
ATOM   789  C  CB   . GLU   A 1 126 ? 2.35843   6.49701   2.49940   1.000 57.72735  ? 1178 GLU   B CB   1 
ATOM   790  C  CG   . GLU   A 1 126 ? 1.85950   7.69073   1.69794   1.000 56.50557  ? 1178 GLU   B CG   1 
ATOM   791  C  CD   . GLU   A 1 126 ? 2.80759   8.87267   1.73245   1.000 74.09372  ? 1178 GLU   B CD   1 
ATOM   792  O  OE1  . GLU   A 1 126 ? 4.01158   8.67168   1.99449   1.000 69.92963  ? 1178 GLU   B OE1  1 
ATOM   793  O  OE2  . GLU   A 1 126 ? 2.34067   10.00961  1.50301   1.000 89.92588  ? 1178 GLU   B OE2  1 
ATOM   794  N  N    . ASP   A 1 127 ? 1.35127   3.66187   4.49255   1.000 49.97810  ? 1179 ASP   B N    1 
ATOM   795  C  CA   . ASP   A 1 127 ? 1.63316   2.25695   4.75710   1.000 45.89719  ? 1179 ASP   B CA   1 
ATOM   796  C  C    . ASP   A 1 127 ? 0.67107   1.38971   3.95347   1.000 45.31568  ? 1179 ASP   B C    1 
ATOM   797  O  O    . ASP   A 1 127 ? -0.54492  1.43589   4.16649   1.000 44.71467  ? 1179 ASP   B O    1 
ATOM   798  C  CB   . ASP   A 1 127 ? 1.50819   1.95856   6.25022   1.000 39.90763  ? 1179 ASP   B CB   1 
ATOM   799  C  CG   . ASP   A 1 127 ? 2.58926   2.63380   7.07192   1.000 46.37043  ? 1179 ASP   B CG   1 
ATOM   800  O  OD1  . ASP   A 1 127 ? 3.49929   3.24449   6.46965   1.000 47.38918  ? 1179 ASP   B OD1  1 
ATOM   801  O  OD2  . ASP   A 1 127 ? 2.52629   2.55729   8.31696   1.000 48.37138  ? 1179 ASP   B OD2  1 
ATOM   802  N  N    . HIS   A 1 128 ? 1.21599   0.60930   3.02076   1.000 46.91255  ? 1180 HIS   B N    1 
ATOM   803  C  CA   . HIS   A 1 128 ? 0.40489   -0.27996  2.19814   1.000 44.99437  ? 1180 HIS   B CA   1 
ATOM   804  C  C    . HIS   A 1 128 ? -0.02518  -1.54264  2.92965   1.000 37.81061  ? 1180 HIS   B C    1 
ATOM   805  O  O    . HIS   A 1 128 ? -0.85826  -2.28978  2.40397   1.000 37.29130  ? 1180 HIS   B O    1 
ATOM   806  C  CB   . HIS   A 1 128 ? 1.17483   -0.66552  0.93227   1.000 40.20971  ? 1180 HIS   B CB   1 
ATOM   807  C  CG   . HIS   A 1 128 ? 2.50078   -1.30352  1.20648   1.000 48.55556  ? 1180 HIS   B CG   1 
ATOM   808  N  ND1  . HIS   A 1 128 ? 3.69783   -0.65370  0.99419   1.000 51.11016  ? 1180 HIS   B ND1  1 
ATOM   809  C  CD2  . HIS   A 1 128 ? 2.81770   -2.52935  1.68496   1.000 50.30564  ? 1180 HIS   B CD2  1 
ATOM   810  C  CE1  . HIS   A 1 128 ? 4.69578   -1.45164  1.32448   1.000 43.91926  ? 1180 HIS   B CE1  1 
ATOM   811  N  NE2  . HIS   A 1 128 ? 4.18870   -2.59443  1.74994   1.000 49.80176  ? 1180 HIS   B NE2  1 
ATOM   812  N  N    . TYR   A 1 129 ? 0.51483   -1.79821  4.11874   1.000 39.92276  ? 1181 TYR   B N    1 
ATOM   813  C  CA   . TYR   A 1 129 ? 0.23476   -3.01789  4.86323   1.000 40.87104  ? 1181 TYR   B CA   1 
ATOM   814  C  C    . TYR   A 1 129 ? 0.43982   -2.73033  6.34211   1.000 39.85884  ? 1181 TYR   B C    1 
ATOM   815  O  O    . TYR   A 1 129 ? 1.36789   -2.01125  6.71480   1.000 44.29805  ? 1181 TYR   B O    1 
ATOM   816  C  CB   . TYR   A 1 129 ? 1.14666   -4.15915  4.39665   1.000 39.47181  ? 1181 TYR   B CB   1 
ATOM   817  C  CG   . TYR   A 1 129 ? 0.98258   -5.45884  5.15017   1.000 39.03624  ? 1181 TYR   B CG   1 
ATOM   818  C  CD1  . TYR   A 1 129 ? 0.03149   -6.39492  4.76157   1.000 38.54732  ? 1181 TYR   B CD1  1 
ATOM   819  C  CD2  . TYR   A 1 129 ? 1.79459   -5.76147  6.23427   1.000 46.27850  ? 1181 TYR   B CD2  1 
ATOM   820  C  CE1  . TYR   A 1 129 ? -0.11758  -7.59164  5.44205   1.000 39.14527  ? 1181 TYR   B CE1  1 
ATOM   821  C  CE2  . TYR   A 1 129 ? 1.65451   -6.95519  6.92075   1.000 44.98385  ? 1181 TYR   B CE2  1 
ATOM   822  C  CZ   . TYR   A 1 129 ? 0.69843   -7.86628  6.52013   1.000 40.48717  ? 1181 TYR   B CZ   1 
ATOM   823  O  OH   . TYR   A 1 129 ? 0.55736   -9.05199  7.20261   1.000 41.87549  ? 1181 TYR   B OH   1 
ATOM   824  N  N    . VAL   A 1 130 ? -0.43819  -3.27992  7.18235   1.000 39.83373  ? 1182 VAL   B N    1 
ATOM   825  C  CA   . VAL   A 1 130 ? -0.38613  -3.03536  8.61825   1.000 45.08486  ? 1182 VAL   B CA   1 
ATOM   826  C  C    . VAL   A 1 130 ? -0.76821  -4.30303  9.36877   1.000 43.65495  ? 1182 VAL   B C    1 
ATOM   827  O  O    . VAL   A 1 130 ? -1.61128  -5.08714  8.92410   1.000 41.58158  ? 1182 VAL   B O    1 
ATOM   828  C  CB   . VAL   A 1 130 ? -1.30603  -1.86812  9.04182   1.000 36.98463  ? 1182 VAL   B CB   1 
ATOM   829  C  CG1  . VAL   A 1 130 ? -0.73094  -0.54235  8.57728   1.000 37.36350  ? 1182 VAL   B CG1  1 
ATOM   830  C  CG2  . VAL   A 1 130 ? -2.71206  -2.07023  8.49294   1.000 37.98742  ? 1182 VAL   B CG2  1 
ATOM   831  N  N    . GLU   A 1 131 ? -0.13119  -4.49463  10.52183  1.000 42.27387  ? 1183 GLU   B N    1 
ATOM   832  C  CA   . GLU   A 1 131 ? -0.41825  -5.59425  11.43027  1.000 41.22413  ? 1183 GLU   B CA   1 
ATOM   833  C  C    . GLU   A 1 131 ? -0.51016  -5.05468  12.85006  1.000 40.09547  ? 1183 GLU   B C    1 
ATOM   834  O  O    . GLU   A 1 131 ? 0.04593   -4.00159  13.17362  1.000 45.01228  ? 1183 GLU   B O    1 
ATOM   835  C  CB   . GLU   A 1 131 ? 0.65967   -6.68935  11.38167  1.000 44.35349  ? 1183 GLU   B CB   1 
ATOM   836  C  CG   . GLU   A 1 131 ? 0.75257   -7.46787  10.08598  1.000 45.23090  ? 1183 GLU   B CG   1 
ATOM   837  C  CD   . GLU   A 1 131 ? 1.77848   -8.58191  10.17339  1.000 46.54763  ? 1183 GLU   B CD   1 
ATOM   838  O  OE1  . GLU   A 1 131 ? 2.40450   -8.72654  11.24343  1.000 42.45187  ? 1183 GLU   B OE1  1 
ATOM   839  O  OE2  . GLU   A 1 131 ? 1.96340   -9.31532  9.17967   1.000 47.30938  ? 1183 GLU   B OE2  1 
ATOM   840  N  N    . PHE   A 1 132 ? -1.22620  -5.78429  13.69737  1.000 38.50897  ? 1184 PHE   B N    1 
ATOM   841  C  CA   . PHE   A 1 132 ? -1.17613  -5.52672  15.12526  1.000 47.96538  ? 1184 PHE   B CA   1 
ATOM   842  C  C    . PHE   A 1 132 ? 0.08484   -6.14159  15.71647  1.000 49.05181  ? 1184 PHE   B C    1 
ATOM   843  O  O    . PHE   A 1 132 ? 0.62374   -7.11984  15.19584  1.000 45.47346  ? 1184 PHE   B O    1 
ATOM   844  C  CB   . PHE   A 1 132 ? -2.39416  -6.11835  15.84153  1.000 46.95024  ? 1184 PHE   B CB   1 
ATOM   845  C  CG   . PHE   A 1 132 ? -3.67111  -5.35834  15.61627  1.000 42.92604  ? 1184 PHE   B CG   1 
ATOM   846  C  CD1  . PHE   A 1 132 ? -3.79099  -4.04116  16.03075  1.000 43.05194  ? 1184 PHE   B CD1  1 
ATOM   847  C  CD2  . PHE   A 1 132 ? -4.76017  -5.97449  15.02255  1.000 39.92777  ? 1184 PHE   B CD2  1 
ATOM   848  C  CE1  . PHE   A 1 132 ? -4.97094  -3.34415  15.83451  1.000 42.34664  ? 1184 PHE   B CE1  1 
ATOM   849  C  CE2  . PHE   A 1 132 ? -5.94112  -5.28447  14.82331  1.000 39.70101  ? 1184 PHE   B CE2  1 
ATOM   850  C  CZ   . PHE   A 1 132 ? -6.04701  -3.96730  15.22979  1.000 45.75205  ? 1184 PHE   B CZ   1 
ATOM   851  N  N    . SER   A 1 133 ? 0.55191   -5.56119  16.82023  1.000 52.18125  ? 1185 SER   B N    1 
ATOM   852  C  CA   . SER   A 1 133 ? 1.46388   -6.30692  17.66850  1.000 47.93068  ? 1185 SER   B CA   1 
ATOM   853  C  C    . SER   A 1 133 ? 0.76280   -7.57768  18.14202  1.000 49.98461  ? 1185 SER   B C    1 
ATOM   854  O  O    . SER   A 1 133 ? -0.46522  -7.69360  18.09910  1.000 52.58516  ? 1185 SER   B O    1 
ATOM   855  C  CB   . SER   A 1 133 ? 1.93098   -5.45649  18.85015  1.000 53.55555  ? 1185 SER   B CB   1 
ATOM   856  O  OG   . SER   A 1 133 ? 0.83505   -4.85714  19.51694  1.000 52.06087  ? 1185 SER   B OG   1 
ATOM   857  N  N    . LYS   A 1 134 ? 1.55473   -8.54856  18.59238  1.000 47.04766  ? 1186 LYS   B N    1 
ATOM   858  C  CA   . LYS   A 1 134 ? 1.05163   -9.90446  18.76693  1.000 51.05648  ? 1186 LYS   B CA   1 
ATOM   859  C  C    . LYS   A 1 134 ? 0.78565   -10.28686 20.21609  1.000 56.55281  ? 1186 LYS   B C    1 
ATOM   860  O  O    . LYS   A 1 134 ? -0.28939  -10.80966 20.52133  1.000 60.94255  ? 1186 LYS   B O    1 
ATOM   861  C  CB   . LYS   A 1 134 ? 2.02554   -10.89179 18.11029  1.000 43.88730  ? 1186 LYS   B CB   1 
ATOM   862  C  CG   . LYS   A 1 134 ? 2.33553   -10.49638 16.67613  1.000 45.10493  ? 1186 LYS   B CG   1 
ATOM   863  C  CD   . LYS   A 1 134 ? 2.79941   -11.65376 15.82057  1.000 47.64147  ? 1186 LYS   B CD   1 
ATOM   864  C  CE   . LYS   A 1 134 ? 2.80340   -11.24234 14.35341  1.000 50.15927  ? 1186 LYS   B CE   1 
ATOM   865  N  NZ   . LYS   A 1 134 ? 3.72731   -12.07373 13.53571  1.000 59.85455  ? 1186 LYS   B NZ   1 
ATOM   866  N  N    . HIS   A 1 135 ? 1.72469   -10.04657 21.12997  1.000 59.51816  ? 1187 HIS   B N    1 
ATOM   867  C  CA   . HIS   A 1 135 ? 1.46471   -10.37900 22.52511  1.000 64.57752  ? 1187 HIS   B CA   1 
ATOM   868  C  C    . HIS   A 1 135 ? 0.42980   -9.42469  23.10776  1.000 61.48725  ? 1187 HIS   B C    1 
ATOM   869  O  O    . HIS   A 1 135 ? -0.72122  -9.80851  23.33995  1.000 63.64806  ? 1187 HIS   B O    1 
ATOM   870  C  CB   . HIS   A 1 135 ? 2.74973   -10.34277 23.35506  1.000 62.49478  ? 1187 HIS   B CB   1 
ATOM   871  C  CG   . HIS   A 1 135 ? 2.55374   -10.75319 24.78022  1.000 73.14748  ? 1187 HIS   B CG   1 
ATOM   872  N  ND1  . HIS   A 1 135 ? 2.53784   -9.84978  25.82287  1.000 65.32284  ? 1187 HIS   B ND1  1 
ATOM   873  C  CD2  . HIS   A 1 135 ? 2.34367   -11.96996 25.33671  1.000 68.59964  ? 1187 HIS   B CD2  1 
ATOM   874  C  CE1  . HIS   A 1 135 ? 2.33683   -10.49231 26.95713  1.000 75.47030  ? 1187 HIS   B CE1  1 
ATOM   875  N  NE2  . HIS   A 1 135 ? 2.21572   -11.78041 26.69064  1.000 73.62317  ? 1187 HIS   B NE2  1 
ATOM   876  N  N    . SER   A 1 136 ? 0.83490   -8.18262  23.35626  1.000 56.14726  ? 1188 SER   B N    1 
ATOM   877  C  CA   . SER   A 1 136 ? -0.08200  -7.12040  23.74486  1.000 61.63794  ? 1188 SER   B CA   1 
ATOM   878  C  C    . SER   A 1 136 ? -0.36097  -6.26586  22.51853  1.000 62.77752  ? 1188 SER   B C    1 
ATOM   879  O  O    . SER   A 1 136 ? 0.57005   -5.73518  21.90330  1.000 59.28131  ? 1188 SER   B O    1 
ATOM   880  C  CB   . SER   A 1 136 ? 0.50109   -6.27299  24.87651  1.000 49.02279  ? 1188 SER   B CB   1 
ATOM   881  O  OG   . SER   A 1 136 ? -0.40881  -5.26377  25.27414  1.000 63.67612  ? 1188 SER   B OG   1 
ATOM   882  N  N    . GLN   A 1 137 ? -1.63697  -6.13690  22.16252  1.000 54.94445  ? 1189 GLN   B N    1 
ATOM   883  C  CA   . GLN   A 1 137 ? -2.02896  -5.44236  20.93726  1.000 53.20961  ? 1189 GLN   B CA   1 
ATOM   884  C  C    . GLN   A 1 137 ? -2.32283  -3.96622  21.21668  1.000 54.02186  ? 1189 GLN   B C    1 
ATOM   885  O  O    . GLN   A 1 137 ? -3.43780  -3.47220  21.05652  1.000 56.22475  ? 1189 GLN   B O    1 
ATOM   886  C  CB   . GLN   A 1 137 ? -3.22203  -6.14452  20.29957  1.000 46.73780  ? 1189 GLN   B CB   1 
ATOM   887  C  CG   . GLN   A 1 137 ? -2.91515  -7.56571  19.86112  1.000 51.35538  ? 1189 GLN   B CG   1 
ATOM   888  C  CD   . GLN   A 1 137 ? -4.05023  -8.20193  19.08541  1.000 53.37832  ? 1189 GLN   B CD   1 
ATOM   889  O  OE1  . GLN   A 1 137 ? -5.21920  -8.06070  19.44539  1.000 50.00586  ? 1189 GLN   B OE1  1 
ATOM   890  N  NE2  . GLN   A 1 137 ? -3.71231  -8.90039  18.00768  1.000 56.64409  ? 1189 GLN   B NE2  1 
ATOM   891  N  N    . ASP   A 1 138 ? -1.23677  -3.25618  21.53337  1.000 51.97974  ? 1190 ASP   B N    1 
ATOM   892  C  CA   . ASP   A 1 138 ? -1.31565  -1.81604  21.87380  1.000 53.08157  ? 1190 ASP   B CA   1 
ATOM   893  C  C    . ASP   A 1 138 ? -0.55762  -1.00852  20.82646  1.000 54.26389  ? 1190 ASP   B C    1 
ATOM   894  O  O    . ASP   A 1 138 ? -0.48352  0.22353   20.96197  1.000 53.49421  ? 1190 ASP   B O    1 
ATOM   895  C  CB   . ASP   A 1 138 ? -0.66959  -1.57356  23.22269  1.000 55.86574  ? 1190 ASP   B CB   1 
ATOM   896  C  CG   . ASP   A 1 138 ? 0.81339   -1.90664  23.30377  1.000 66.01992  ? 1190 ASP   B CG   1 
ATOM   897  O  OD1  . ASP   A 1 138 ? 1.21529   -2.94889  22.75117  1.000 59.83229  ? 1190 ASP   B OD1  1 
ATOM   898  O  OD2  . ASP   A 1 138 ? 1.55547   -1.11545  23.92144  1.000 75.11618  ? 1190 ASP   B OD2  1 
ATOM   899  N  N    . ARG   A 1 139 ? -0.00670  -1.68595  19.82371  1.000 51.29694  ? 1191 ARG   B N    1 
ATOM   900  C  CA   . ARG   A 1 139 ? 0.74533   -0.99742  18.79042  1.000 58.25499  ? 1191 ARG   B CA   1 
ATOM   901  C  C    . ARG   A 1 139 ? 0.41224   -1.58594  17.42666  1.000 49.49270  ? 1191 ARG   B C    1 
ATOM   902  O  O    . ARG   A 1 139 ? -0.07885  -2.71094  17.31012  1.000 46.44254  ? 1191 ARG   B O    1 
ATOM   903  C  CB   . ARG   A 1 139 ? 2.25933   -1.07744  19.03740  1.000 54.42603  ? 1191 ARG   B CB   1 
ATOM   904  C  CG   . ARG   A 1 139 ? 2.75543   -0.16004  20.14203  1.000 61.84151  ? 1191 ARG   B CG   1 
ATOM   905  C  CD   . ARG   A 1 139 ? 4.22042   -0.41804  20.44908  1.000 57.85855  ? 1191 ARG   B CD   1 
ATOM   906  N  NE   . ARG   A 1 139 ? 4.43733   -1.77586  20.93262  1.000 63.02825  ? 1191 ARG   B NE   1 
ATOM   907  C  CZ   . ARG   A 1 139 ? 5.62630   -2.29384  21.20779  1.000 63.35769  ? 1191 ARG   B CZ   1 
ATOM   908  N  NH1  . ARG   A 1 139 ? 6.73835   -1.59499  21.05048  1.000 59.30556  ? 1191 ARG   B NH1  1 
ATOM   909  N  NH2  . ARG   A 1 139 ? 5.70321   -3.54768  21.64828  1.000 52.30541  ? 1191 ARG   B NH2  1 
ATOM   910  N  N    . VAL   A 1 140 ? 0.68927   -0.79737  16.39634  1.000 49.27637  ? 1192 VAL   B N    1 
ATOM   911  C  CA   . VAL   A 1 140 ? 0.50420   -1.20490  15.00850  1.000 53.25631  ? 1192 VAL   B CA   1 
ATOM   912  C  C    . VAL   A 1 140 ? 1.83519   -1.06729  14.28741  1.000 47.32485  ? 1192 VAL   B C    1 
ATOM   913  O  O    . VAL   A 1 140 ? 2.57127   -0.10226  14.51001  1.000 46.70631  ? 1192 VAL   B O    1 
ATOM   914  C  CB   . VAL   A 1 140 ? -0.58576  -0.36709  14.30721  1.000 49.53147  ? 1192 VAL   B CB   1 
ATOM   915  C  CG1  . VAL   A 1 140 ? -0.56482  -0.61369  12.80430  1.000 47.10103  ? 1192 VAL   B CG1  1 
ATOM   916  C  CG2  . VAL   A 1 140 ? -1.95577  -0.68576  14.88637  1.000 48.63264  ? 1192 VAL   B CG2  1 
ATOM   917  N  N    . ILE   A 1 141 ? 2.15009   -2.03265  13.43178  1.000 45.95518  ? 1193 ILE   B N    1 
ATOM   918  C  CA   . ILE   A 1 141 ? 3.34807   -1.96507  12.60172  1.000 42.62620  ? 1193 ILE   B CA   1 
ATOM   919  C  C    . ILE   A 1 141 ? 2.91103   -1.95262  11.14573  1.000 42.29372  ? 1193 ILE   B C    1 
ATOM   920  O  O    . ILE   A 1 141 ? 2.29794   -2.91276  10.66413  1.000 39.20885  ? 1193 ILE   B O    1 
ATOM   921  C  CB   . ILE   A 1 141 ? 4.31999   -3.12104  12.88215  1.000 46.89486  ? 1193 ILE   B CB   1 
ATOM   922  C  CG1  . ILE   A 1 141 ? 5.60398   -2.92846  12.07404  1.000 43.01490  ? 1193 ILE   B CG1  1 
ATOM   923  C  CG2  . ILE   A 1 141 ? 3.67387   -4.46311  12.56370  1.000 43.43850  ? 1193 ILE   B CG2  1 
ATOM   924  C  CD1  . ILE   A 1 141 ? 6.73692   -3.85139  12.48037  1.000 41.59294  ? 1193 ILE   B CD1  1 
ATOM   925  N  N    . GLY   A 1 142 ? 3.21509   -0.85991  10.45729  1.000 44.12160  ? 1194 GLY   B N    1 
ATOM   926  C  CA   . GLY   A 1 142 ? 2.92406   -0.72045  9.04824   1.000 40.10932  ? 1194 GLY   B CA   1 
ATOM   927  C  C    . GLY   A 1 142 ? 4.18604   -0.71088  8.21120   1.000 45.02665  ? 1194 GLY   B C    1 
ATOM   928  O  O    . GLY   A 1 142 ? 5.28807   -0.51476  8.73309   1.000 43.76532  ? 1194 GLY   B O    1 
ATOM   929  N  N    . THR   A 1 143 ? 4.03198   -0.92238  6.91229   1.000 43.85849  ? 1195 THR   B N    1 
ATOM   930  C  CA   . THR   A 1 143 ? 5.15795   -1.02283  5.99529   1.000 41.74687  ? 1195 THR   B CA   1 
ATOM   931  C  C    . THR   A 1 143 ? 4.97299   -0.05527  4.84092   1.000 46.15435  ? 1195 THR   B C    1 
ATOM   932  O  O    . THR   A 1 143 ? 3.88198   0.04459   4.27191   1.000 42.28627  ? 1195 THR   B O    1 
ATOM   933  C  CB   . THR   A 1 143 ? 5.31182   -2.44806  5.45385   1.000 44.16191  ? 1195 THR   B CB   1 
ATOM   934  O  OG1  . THR   A 1 143 ? 5.44278   -3.36663  6.54621   1.000 40.83655  ? 1195 THR   B OG1  1 
ATOM   935  C  CG2  . THR   A 1 143 ? 6.54079   -2.54650  4.56386   1.000 41.86736  ? 1195 THR   B CG2  1 
ATOM   936  N  N    . LYS   A 1 144 ? 6.04503   0.65751   4.50160   1.000 42.10831  ? 1196 LYS   B N    1 
ATOM   937  C  CA   . LYS   A 1 144 ? 6.08807   1.52204   3.32326   1.000 48.78588  ? 1196 LYS   B CA   1 
ATOM   938  C  C    . LYS   A 1 144 ? 7.40102   1.24865   2.60433   1.000 46.37766  ? 1196 LYS   B C    1 
ATOM   939  O  O    . LYS   A 1 144 ? 8.46707   1.65476   3.07814   1.000 46.13019  ? 1196 LYS   B O    1 
ATOM   940  C  CB   . LYS   A 1 144 ? 5.95919   2.99720   3.70868   1.000 49.36893  ? 1196 LYS   B CB   1 
ATOM   941  C  CG   . LYS   A 1 144 ? 6.16323   3.95973   2.55129   1.000 48.22612  ? 1196 LYS   B CG   1 
ATOM   942  C  CD   . LYS   A 1 144 ? 5.81335   5.38092   2.96074   1.000 58.15291  ? 1196 LYS   B CD   1 
ATOM   943  C  CE   . LYS   A 1 144 ? 6.68141   6.39857   2.23831   1.000 57.51896  ? 1196 LYS   B CE   1 
ATOM   944  N  NZ   . LYS   A 1 144 ? 6.27253   7.79572   2.55077   1.000 64.18226  ? 1196 LYS   B NZ   1 
ATOM   945  N  N    . GLY   A 1 145 ? 7.32494   0.54522   1.47961   1.000 47.43502  ? 1197 GLY   B N    1 
ATOM   946  C  CA   . GLY   A 1 145 ? 8.54389   0.15685   0.79073   1.000 43.53033  ? 1197 GLY   B CA   1 
ATOM   947  C  C    . GLY   A 1 145 ? 9.42985   -0.66586  1.70503   1.000 51.19384  ? 1197 GLY   B C    1 
ATOM   948  O  O    . GLY   A 1 145 ? 9.00379   -1.67560  2.27944   1.000 51.23271  ? 1197 GLY   B O    1 
ATOM   949  N  N    . ASP   A 1 146 ? 10.67789  -0.22590  1.85582   1.000 45.73117  ? 1198 ASP   B N    1 
ATOM   950  C  CA   . ASP   A 1 146 ? 11.65786  -0.90164  2.69405   1.000 46.16503  ? 1198 ASP   B CA   1 
ATOM   951  C  C    . ASP   A 1 146 ? 11.59294  -0.47306  4.15389   1.000 41.72789  ? 1198 ASP   B C    1 
ATOM   952  O  O    . ASP   A 1 146 ? 12.37192  -0.98180  4.96707   1.000 46.22416  ? 1198 ASP   B O    1 
ATOM   953  C  CB   . ASP   A 1 146 ? 13.07486  -0.64496  2.16291   1.000 51.76801  ? 1198 ASP   B CB   1 
ATOM   954  C  CG   . ASP   A 1 146 ? 13.21479  -0.97056  0.68804   1.000 54.12297  ? 1198 ASP   B CG   1 
ATOM   955  O  OD1  . ASP   A 1 146 ? 12.52271  -1.89069  0.20942   1.000 53.10435  ? 1198 ASP   B OD1  1 
ATOM   956  O  OD2  . ASP   A 1 146 ? 14.01983  -0.30189  0.00775   1.000 56.85972  ? 1198 ASP   B OD2  1 
ATOM   957  N  N    . ILE   A 1 147 ? 10.69302  0.43915   4.50555   1.000 41.46015  ? 1199 ILE   B N    1 
ATOM   958  C  CA   . ILE   A 1 147 ? 10.67110  1.06667   5.82231   1.000 43.88285  ? 1199 ILE   B CA   1 
ATOM   959  C  C    . ILE   A 1 147 ? 9.52708   0.49109   6.64257   1.000 43.23662  ? 1199 ILE   B C    1 
ATOM   960  O  O    . ILE   A 1 147 ? 8.44105   0.21696   6.11371   1.000 45.66707  ? 1199 ILE   B O    1 
ATOM   961  C  CB   . ILE   A 1 147 ? 10.53822  2.59664   5.70370   1.000 48.85156  ? 1199 ILE   B CB   1 
ATOM   962  C  CG1  . ILE   A 1 147 ? 11.70924  3.16923   4.89844   1.000 45.48980  ? 1199 ILE   B CG1  1 
ATOM   963  C  CG2  . ILE   A 1 147 ? 10.46531  3.23419   7.08445   1.000 45.78308  ? 1199 ILE   B CG2  1 
ATOM   964  C  CD1  . ILE   A 1 147 ? 11.32831  4.34191   4.02299   1.000 45.59183  ? 1199 ILE   B CD1  1 
ATOM   965  N  N    . ALA   A 1 148 ? 9.76711   0.32158   7.93963   1.000 41.79648  ? 1200 ALA   B N    1 
ATOM   966  C  CA   . ALA   A 1 148 ? 8.73610   -0.08796  8.88382   1.000 48.73042  ? 1200 ALA   B CA   1 
ATOM   967  C  C    . ALA   A 1 148 ? 8.39522   1.07543   9.80337   1.000 56.26762  ? 1200 ALA   B C    1 
ATOM   968  O  O    . ALA   A 1 148 ? 9.27529   1.85051   10.18604  1.000 53.23605  ? 1200 ALA   B O    1 
ATOM   969  C  CB   . ALA   A 1 148 ? 9.19204   -1.29367  9.70928   1.000 40.62277  ? 1200 ALA   B CB   1 
ATOM   970  N  N    . HIS   A 1 149 ? 7.11624   1.19567   10.15536  1.000 50.37103  ? 1201 HIS   B N    1 
ATOM   971  C  CA   . HIS   A 1 149 ? 6.63635   2.21907   11.07497  1.000 47.45704  ? 1201 HIS   B CA   1 
ATOM   972  C  C    . HIS   A 1 149 ? 5.91633   1.53558   12.22626  1.000 48.46504  ? 1201 HIS   B C    1 
ATOM   973  O  O    . HIS   A 1 149 ? 5.07325   0.66455   12.00063  1.000 48.33981  ? 1201 HIS   B O    1 
ATOM   974  C  CB   . HIS   A 1 149 ? 5.68940   3.20186   10.37561  1.000 47.86095  ? 1201 HIS   B CB   1 
ATOM   975  C  CG   . HIS   A 1 149 ? 6.30343   3.91836   9.21431   1.000 48.07096  ? 1201 HIS   B CG   1 
ATOM   976  N  ND1  . HIS   A 1 149 ? 5.65740   4.05893   8.00527   1.000 44.83285  ? 1201 HIS   B ND1  1 
ATOM   977  C  CD2  . HIS   A 1 149 ? 7.49347   4.54921   9.08102   1.000 53.23321  ? 1201 HIS   B CD2  1 
ATOM   978  C  CE1  . HIS   A 1 149 ? 6.42643   4.73754   7.17298   1.000 47.58117  ? 1201 HIS   B CE1  1 
ATOM   979  N  NE2  . HIS   A 1 149 ? 7.54547   5.04770   7.80082   1.000 51.17155  ? 1201 HIS   B NE2  1 
ATOM   980  N  N    . ILE   A 1 150 ? 6.24840   1.92204   13.45510  1.000 48.22736  ? 1202 ILE   B N    1 
ATOM   981  C  CA   . ILE   A 1 150 ? 5.59639   1.39456   14.64733  1.000 46.59501  ? 1202 ILE   B CA   1 
ATOM   982  C  C    . ILE   A 1 150 ? 4.86850   2.54389   15.32889  1.000 53.58264  ? 1202 ILE   B C    1 
ATOM   983  O  O    . ILE   A 1 150 ? 5.49659   3.54599   15.69948  1.000 57.97141  ? 1202 ILE   B O    1 
ATOM   984  C  CB   . ILE   A 1 150 ? 6.59437   0.72386   15.60256  1.000 47.57066  ? 1202 ILE   B CB   1 
ATOM   985  C  CG1  . ILE   A 1 150 ? 7.22025   -0.50245  14.93403  1.000 54.58907  ? 1202 ILE   B CG1  1 
ATOM   986  C  CG2  . ILE   A 1 150 ? 5.90637   0.32143   16.89874  1.000 46.24650  ? 1202 ILE   B CG2  1 
ATOM   987  C  CD1  . ILE   A 1 150 ? 7.92621   -1.43012  15.89938  1.000 54.92076  ? 1202 ILE   B CD1  1 
ATOM   988  N  N    . TYR   A 1 151 ? 3.55049   2.38605   15.48699  1.000 54.78662  ? 1203 TYR   B N    1 
ATOM   989  C  CA   . TYR   A 1 151 ? 2.64358   3.38534   16.02962  1.000 52.90475  ? 1203 TYR   B CA   1 
ATOM   990  C  C    . TYR   A 1 151 ? 2.02558   2.88790   17.32984  1.000 53.18414  ? 1203 TYR   B C    1 
ATOM   991  O  O    . TYR   A 1 151 ? 1.79250   1.68799   17.50532  1.000 51.28223  ? 1203 TYR   B O    1 
ATOM   992  C  CB   . TYR   A 1 151 ? 1.48958   3.69405   15.06454  1.000 48.11817  ? 1203 TYR   B CB   1 
ATOM   993  C  CG   . TYR   A 1 151 ? 1.88056   3.96745   13.63242  1.000 55.84665  ? 1203 TYR   B CG   1 
ATOM   994  C  CD1  . TYR   A 1 151 ? 2.04445   2.92908   12.72482  1.000 49.38524  ? 1203 TYR   B CD1  1 
ATOM   995  C  CD2  . TYR   A 1 151 ? 2.05565   5.26826   13.17990  1.000 44.63780  ? 1203 TYR   B CD2  1 
ATOM   996  C  CE1  . TYR   A 1 151 ? 2.39043   3.17753   11.40871  1.000 46.39873  ? 1203 TYR   B CE1  1 
ATOM   997  C  CE2  . TYR   A 1 151 ? 2.39963   5.52671   11.86778  1.000 48.72772  ? 1203 TYR   B CE2  1 
ATOM   998  C  CZ   . TYR   A 1 151 ? 2.56652   4.48035   10.98919  1.000 49.47612  ? 1203 TYR   B CZ   1 
ATOM   999  O  OH   . TYR   A 1 151 ? 2.90850   4.73981   9.68208   1.000 46.05792  ? 1203 TYR   B OH   1 
ATOM   1000 N  N    . ASP   A 1 152 ? 1.72668   3.83228   18.21948  1.000 56.12405  ? 1204 ASP   B N    1 
ATOM   1001 C  CA   . ASP   A 1 152 ? 0.94570   3.54181   19.41361  1.000 59.35828  ? 1204 ASP   B CA   1 
ATOM   1002 C  C    . ASP   A 1 152 ? -0.54131  3.58779   19.07464  1.000 53.40138  ? 1204 ASP   B C    1 
ATOM   1003 O  O    . ASP   A 1 152 ? -1.00926  4.52557   18.42328  1.000 50.56314  ? 1204 ASP   B O    1 
ATOM   1004 C  CB   . ASP   A 1 152 ? 1.27481   4.54422   20.51921  1.000 60.24722  ? 1204 ASP   B CB   1 
ATOM   1005 C  CG   . ASP   A 1 152 ? 0.37683   4.38977   21.72829  1.000 61.16062  ? 1204 ASP   B CG   1 
ATOM   1006 O  OD1  . ASP   A 1 152 ? 0.53077   3.38605   22.45569  1.000 60.81147  ? 1204 ASP   B OD1  1 
ATOM   1007 O  OD2  . ASP   A 1 152 ? -0.48409  5.26692   21.94897  1.000 61.48741  ? 1204 ASP   B OD2  1 
ATOM   1008 N  N    . ILE   A 1 153 ? -1.28038  2.56702   19.51606  1.000 53.75928  ? 1205 ILE   B N    1 
ATOM   1009 C  CA   . ILE   A 1 153 ? -2.69439  2.47000   19.16914  1.000 53.11631  ? 1205 ILE   B CA   1 
ATOM   1010 C  C    . ILE   A 1 153 ? -3.48129  3.62830   19.77371  1.000 58.10003  ? 1205 ILE   B C    1 
ATOM   1011 O  O    . ILE   A 1 153 ? -4.36226  4.20111   19.12451  1.000 59.14151  ? 1205 ILE   B O    1 
ATOM   1012 C  CB   . ILE   A 1 153 ? -3.26549  1.11122   19.61370  1.000 47.97438  ? 1205 ILE   B CB   1 
ATOM   1013 C  CG1  . ILE   A 1 153 ? -2.77060  -0.00419  18.69113  1.000 48.80417  ? 1205 ILE   B CG1  1 
ATOM   1014 C  CG2  . ILE   A 1 153 ? -4.78448  1.15434   19.64273  1.000 48.78638  ? 1205 ILE   B CG2  1 
ATOM   1015 C  CD1  . ILE   A 1 153 ? -3.31170  -1.37101  19.04768  1.000 49.79194  ? 1205 ILE   B CD1  1 
ATOM   1016 N  N    . GLN   A 1 154 ? -3.18122  3.98577   21.02256  1.000 62.00113  ? 1206 GLN   B N    1 
ATOM   1017 C  CA   . GLN   A 1 154 ? -3.95912  5.01810   21.69917  1.000 61.14745  ? 1206 GLN   B CA   1 
ATOM   1018 C  C    . GLN   A 1 154 ? -3.70303  6.39083   21.08662  1.000 62.11936  ? 1206 GLN   B C    1 
ATOM   1019 O  O    . GLN   A 1 154 ? -4.61400  7.02369   20.54340  1.000 62.00045  ? 1206 GLN   B O    1 
ATOM   1020 C  CB   . GLN   A 1 154 ? -3.63908  5.02266   23.19416  1.000 62.16811  ? 1206 GLN   B CB   1 
ATOM   1021 C  CG   . GLN   A 1 154 ? -4.87706  4.97311   24.07122  1.000 71.14194  ? 1206 GLN   B CG   1 
ATOM   1022 C  CD   . GLN   A 1 154 ? -5.74316  3.76505   23.76972  1.000 75.32796  ? 1206 GLN   B CD   1 
ATOM   1023 O  OE1  . GLN   A 1 154 ? -5.29824  2.62407   23.88916  1.000 78.11370  ? 1206 GLN   B OE1  1 
ATOM   1024 N  NE2  . GLN   A 1 154 ? -6.98315  4.01299   23.36266  1.000 73.94147  ? 1206 GLN   B NE2  1 
ATOM   1025 N  N    . THR   A 1 155 ? -2.45999  6.86777   21.16940  1.000 64.36364  ? 1207 THR   B N    1 
ATOM   1026 C  CA   . THR   A 1 155 ? -2.13191  8.17953   20.62687  1.000 64.87641  ? 1207 THR   B CA   1 
ATOM   1027 C  C    . THR   A 1 155 ? -2.13695  8.19493   19.10486  1.000 69.77454  ? 1207 THR   B C    1 
ATOM   1028 O  O    . THR   A 1 155 ? -2.32589  9.26171   18.50945  1.000 64.28138  ? 1207 THR   B O    1 
ATOM   1029 C  CB   . THR   A 1 155 ? -0.76186  8.63262   21.13065  1.000 70.27438  ? 1207 THR   B CB   1 
ATOM   1030 O  OG1  . THR   A 1 155 ? 0.25508   8.15319   20.24081  1.000 71.48886  ? 1207 THR   B OG1  1 
ATOM   1031 C  CG2  . THR   A 1 155 ? -0.49986  8.07715   22.52286  1.000 71.87342  ? 1207 THR   B CG2  1 
ATOM   1032 N  N    . GLY   A 1 156 ? -1.94206  7.04466   18.46631  1.000 66.56599  ? 1208 GLY   B N    1 
ATOM   1033 C  CA   . GLY   A 1 156 ? -1.73310  7.02508   17.03431  1.000 55.40013  ? 1208 GLY   B CA   1 
ATOM   1034 C  C    . GLY   A 1 156 ? -0.41007  7.59780   16.59105  1.000 62.49770  ? 1208 GLY   B C    1 
ATOM   1035 O  O    . GLY   A 1 156 ? -0.20009  7.78731   15.38797  1.000 66.41675  ? 1208 GLY   B O    1 
ATOM   1036 N  N    . ASN   A 1 157 ? 0.49298   7.88310   17.52591  1.000 60.12476  ? 1209 ASN   B N    1 
ATOM   1037 C  CA   . ASN   A 1 157 ? 1.78201   8.47387   17.20064  1.000 62.17205  ? 1209 ASN   B CA   1 
ATOM   1038 C  C    . ASN   A 1 157 ? 2.73692   7.41658   16.66103  1.000 58.68780  ? 1209 ASN   B C    1 
ATOM   1039 O  O    . ASN   A 1 157 ? 2.72884   6.26075   17.08848  1.000 51.76251  ? 1209 ASN   B O    1 
ATOM   1040 C  CB   . ASN   A 1 157 ? 2.39510   9.13931   18.43336  1.000 64.55500  ? 1209 ASN   B CB   1 
ATOM   1041 C  CG   . ASN   A 1 157 ? 1.51620   10.23460  19.00495  1.000 66.20390  ? 1209 ASN   B CG   1 
ATOM   1042 O  OD1  . ASN   A 1 157 ? 0.69523   10.82239  18.29974  1.000 72.63228  ? 1209 ASN   B OD1  1 
ATOM   1043 N  ND2  . ASN   A 1 157 ? 1.68326   10.51410  20.29283  1.000 65.94927  ? 1209 ASN   B ND2  1 
ATOM   1044 N  N    . LYS   A 1 158 ? 3.57292   7.84814   15.72283  1.000 57.14505  ? 1210 LYS   B N    1 
ATOM   1045 C  CA   . LYS   A 1 158 ? 4.60584   6.94285   15.17916  1.000 49.92151  ? 1210 LYS   B CA   1 
ATOM   1046 C  C    . LYS   A 1 158 ? 5.72586   6.87117   16.20915  1.000 57.48836  ? 1210 LYS   B C    1 
ATOM   1047 O  O    . LYS   A 1 158 ? 6.42894   7.87420   16.41274  1.000 55.54828  ? 1210 LYS   B O    1 
ATOM   1048 C  CB   . LYS   A 1 158 ? 5.14784   7.45428   13.84994  1.000 50.35956  ? 1210 LYS   B CB   1 
ATOM   1049 C  CG   . LYS   A 1 158 ? 6.24975   6.59796   13.25525  1.000 58.68878  ? 1210 LYS   B CG   1 
ATOM   1050 C  CD   . LYS   A 1 158 ? 6.05769   6.40238   11.76033  1.000 52.87161  ? 1210 LYS   B CD   1 
ATOM   1051 C  CE   . LYS   A 1 158 ? 6.40976   7.61504   10.97284  1.000 55.37394  ? 1210 LYS   B CE   1 
ATOM   1052 N  NZ   . LYS   A 1 158 ? 5.50774   7.77766   9.83180   1.000 63.28447  ? 1210 LYS   B NZ   1 
ATOM   1053 N  N    . LEU   A 1 159 ? 5.85479   5.71841   16.84161  1.000 58.79071  ? 1211 LEU   B N    1 
ATOM   1054 C  CA   . LEU   A 1 159 ? 6.86981   5.55474   17.87464  1.000 58.64852  ? 1211 LEU   B CA   1 
ATOM   1055 C  C    . LEU   A 1 159 ? 8.23977   5.26640   17.27572  1.000 64.45681  ? 1211 LEU   B C    1 
ATOM   1056 O  O    . LEU   A 1 159 ? 9.25282   5.77651   17.76548  1.000 59.96886  ? 1211 LEU   B O    1 
ATOM   1057 C  CB   . LEU   A 1 159 ? 6.46575   4.43715   18.83610  1.000 51.59621  ? 1211 LEU   B CB   1 
ATOM   1058 C  CG   . LEU   A 1 159 ? 5.20679   4.70358   19.66303  1.000 61.20001  ? 1211 LEU   B CG   1 
ATOM   1059 C  CD1  . LEU   A 1 159 ? 4.82172   3.47293   20.46853  1.000 55.12096  ? 1211 LEU   B CD1  1 
ATOM   1060 C  CD2  . LEU   A 1 159 ? 5.40591   5.90992   20.56654  1.000 61.68152  ? 1211 LEU   B CD2  1 
ATOM   1061 N  N    . LEU   A 1 160 ? 8.29367   4.45897   16.21803  1.000 64.73893  ? 1212 LEU   B N    1 
ATOM   1062 C  CA   . LEU   A 1 160 ? 9.57563   4.07864   15.63715  1.000 52.64142  ? 1212 LEU   B CA   1 
ATOM   1063 C  C    . LEU   A 1 160 ? 9.49658   4.07805   14.11715  1.000 53.87740  ? 1212 LEU   B C    1 
ATOM   1064 O  O    . LEU   A 1 160 ? 8.45254   3.77790   13.53430  1.000 61.49449  ? 1212 LEU   B O    1 
ATOM   1065 C  CB   . LEU   A 1 160 ? 10.03253  2.69180   16.11568  1.000 60.21539  ? 1212 LEU   B CB   1 
ATOM   1066 C  CG   . LEU   A 1 160 ? 10.28756  2.46337   17.60676  1.000 63.52715  ? 1212 LEU   B CG   1 
ATOM   1067 C  CD1  . LEU   A 1 160 ? 10.77146  1.04142   17.84031  1.000 50.29352  ? 1212 LEU   B CD1  1 
ATOM   1068 C  CD2  . LEU   A 1 160 ? 11.29065  3.46851   18.15534  1.000 69.31886  ? 1212 LEU   B CD2  1 
ATOM   1069 N  N    . THR   A 1 161 ? 10.62159  4.40871   13.48698  1.000 52.15587  ? 1213 THR   B N    1 
ATOM   1070 C  CA   . THR   A 1 161 ? 10.82453  4.22113   12.05305  1.000 52.41255  ? 1213 THR   B CA   1 
ATOM   1071 C  C    . THR   A 1 161 ? 12.06346  3.34997   11.88436  1.000 56.96280  ? 1213 THR   B C    1 
ATOM   1072 O  O    . THR   A 1 161 ? 13.17950  3.78300   12.19016  1.000 58.99509  ? 1213 THR   B O    1 
ATOM   1073 C  CB   . THR   A 1 161 ? 10.98861  5.55183   11.32352  1.000 57.36211  ? 1213 THR   B CB   1 
ATOM   1074 O  OG1  . THR   A 1 161 ? 9.79168   6.32898   11.46525  1.000 62.80704  ? 1213 THR   B OG1  1 
ATOM   1075 C  CG2  . THR   A 1 161 ? 11.25455  5.31222   9.84061   1.000 50.76343  ? 1213 THR   B CG2  1 
ATOM   1076 N  N    . LEU   A 1 162 ? 11.86535  2.12479   11.41085  1.000 61.10730  ? 1214 LEU   B N    1 
ATOM   1077 C  CA   . LEU   A 1 162 ? 12.94027  1.15365   11.26220  1.000 45.94015  ? 1214 LEU   B CA   1 
ATOM   1078 C  C    . LEU   A 1 162 ? 13.35322  1.07404   9.79622   1.000 53.10658  ? 1214 LEU   B C    1 
ATOM   1079 O  O    . LEU   A 1 162 ? 12.52017  0.79376   8.92236   1.000 49.42022  ? 1214 LEU   B O    1 
ATOM   1080 C  CB   . LEU   A 1 162 ? 12.51518  -0.21711  11.78276  1.000 50.85902  ? 1214 LEU   B CB   1 
ATOM   1081 C  CG   . LEU   A 1 162 ? 12.09922  -0.25449  13.25779  1.000 49.20637  ? 1214 LEU   B CG   1 
ATOM   1082 C  CD1  . LEU   A 1 162 ? 11.87712  -1.68129  13.73336  1.000 39.73788  ? 1214 LEU   B CD1  1 
ATOM   1083 C  CD2  . LEU   A 1 162 ? 13.12630  0.45177   14.12948  1.000 54.71750  ? 1214 LEU   B CD2  1 
ATOM   1084 N  N    . PHE   A 1 163 ? 14.63423  1.33684   9.53708   1.000 52.00923  ? 1215 PHE   B N    1 
ATOM   1085 C  CA   . PHE   A 1 163 ? 15.24219  1.21527   8.22111   1.000 55.56435  ? 1215 PHE   B CA   1 
ATOM   1086 C  C    . PHE   A 1 163 ? 16.74221  1.43020   8.35198   1.000 59.30779  ? 1215 PHE   B C    1 
ATOM   1087 O  O    . PHE   A 1 163 ? 17.18230  2.31546   9.09362   1.000 56.06185  ? 1215 PHE   B O    1 
ATOM   1088 C  CB   . PHE   A 1 163 ? 14.65323  2.21892   7.22573   1.000 49.34457  ? 1215 PHE   B CB   1 
ATOM   1089 C  CG   . PHE   A 1 163 ? 15.41220  2.29435   5.92968   1.000 48.79512  ? 1215 PHE   B CG   1 
ATOM   1090 C  CD1  . PHE   A 1 163 ? 15.17210  1.37997   4.91605   1.000 52.39251  ? 1215 PHE   B CD1  1 
ATOM   1091 C  CD2  . PHE   A 1 163 ? 16.37427  3.27020   5.73126   1.000 56.30517  ? 1215 PHE   B CD2  1 
ATOM   1092 C  CE1  . PHE   A 1 163 ? 15.87507  1.44144   3.72500   1.000 50.78932  ? 1215 PHE   B CE1  1 
ATOM   1093 C  CE2  . PHE   A 1 163 ? 17.08124  3.33567   4.54322   1.000 62.57173  ? 1215 PHE   B CE2  1 
ATOM   1094 C  CZ   . PHE   A 1 163 ? 16.83014  2.41929   3.53959   1.000 60.03532  ? 1215 PHE   B CZ   1 
ATOM   1095 N  N    . ASN   A 1 164 ? 17.51612  0.62386   7.62828   1.000 57.64695  ? 1216 ASN   B N    1 
ATOM   1096 C  CA   . ASN   A 1 164 ? 18.97013  0.73173   7.59219   1.000 50.04429  ? 1216 ASN   B CA   1 
ATOM   1097 C  C    . ASN   A 1 164 ? 19.44307  0.50513   6.16227   1.000 53.74202  ? 1216 ASN   B C    1 
ATOM   1098 O  O    . ASN   A 1 164 ? 19.36097  -0.62007  5.65272   1.000 58.24352  ? 1216 ASN   B O    1 
ATOM   1099 C  CB   . ASN   A 1 164 ? 19.60808  -0.28294  8.54658   1.000 59.28422  ? 1216 ASN   B CB   1 
ATOM   1100 C  CG   . ASN   A 1 164 ? 21.13109  -0.20405  8.57150   1.000 57.97852  ? 1216 ASN   B CG   1 
ATOM   1101 O  OD1  . ASN   A 1 164 ? 21.78504  -0.99383  9.25079   1.000 58.66632  ? 1216 ASN   B OD1  1 
ATOM   1102 N  ND2  . ASN   A 1 164 ? 21.69814  0.75362   7.84410   1.000 65.51744  ? 1216 ASN   B ND2  1 
ATOM   1103 N  N    . PRO   A 1 165 ? 19.94913  1.53882   5.48484   1.000 56.42449  ? 1217 PRO   B N    1 
ATOM   1104 C  CA   . PRO   A 1 165 ? 20.38108  1.35423   4.09090   1.000 53.31865  ? 1217 PRO   B CA   1 
ATOM   1105 C  C    . PRO   A 1 165 ? 21.55900  0.40909   3.94524   1.000 54.68316  ? 1217 PRO   B C    1 
ATOM   1106 O  O    . PRO   A 1 165 ? 21.72792  -0.18635  2.87247   1.000 53.92964  ? 1217 PRO   B O    1 
ATOM   1107 C  CB   . PRO   A 1 165 ? 20.74317  2.77603   3.64333   1.000 56.91351  ? 1217 PRO   B CB   1 
ATOM   1108 C  CG   . PRO   A 1 165 ? 21.12426  3.47150   4.90705   1.000 53.23940  ? 1217 PRO   B CG   1 
ATOM   1109 C  CD   . PRO   A 1 165 ? 20.23225  2.89799   5.97830   1.000 54.90630  ? 1217 PRO   B CD   1 
ATOM   1110 N  N    . ASP   A 1 166 ? 22.37902  0.24543   4.98528   1.000 57.27952  ? 1218 ASP   B N    1 
ATOM   1111 C  CA   . ASP   A 1 166 ? 23.46394  -0.72767  4.92664   1.000 58.11263  ? 1218 ASP   B CA   1 
ATOM   1112 C  C    . ASP   A 1 166 ? 22.92083  -2.14867  4.83822   1.000 59.51012  ? 1218 ASP   B C    1 
ATOM   1113 O  O    . ASP   A 1 166 ? 23.38674  -2.95802  4.02752   1.000 61.23611  ? 1218 ASP   B O    1 
ATOM   1114 C  CB   . ASP   A 1 166 ? 24.37299  -0.57526  6.14755   1.000 64.40936  ? 1218 ASP   B CB   1 
ATOM   1115 C  CG   . ASP   A 1 166 ? 25.27908  0.63963   6.05704   1.000 62.73113  ? 1218 ASP   B CG   1 
ATOM   1116 O  OD1  . ASP   A 1 166 ? 25.99006  0.78117   5.03897   1.000 64.31236  ? 1218 ASP   B OD1  1 
ATOM   1117 O  OD2  . ASP   A 1 166 ? 25.27917  1.45601   7.00172   1.000 64.29705  ? 1218 ASP   B OD2  1 
ATOM   1118 N  N    . LEU   A 1 167 ? 21.92182  -2.46726  5.66237   1.000 56.08209  ? 1219 LEU   B N    1 
ATOM   1119 C  CA   . LEU   A 1 167 ? 21.40472  -3.82317  5.78792   1.000 52.50943  ? 1219 LEU   B CA   1 
ATOM   1120 C  C    . LEU   A 1 167 ? 20.17368  -4.09042  4.93007   1.000 51.71914  ? 1219 LEU   B C    1 
ATOM   1121 O  O    . LEU   A 1 167 ? 19.66659  -5.21537  4.94053   1.000 53.63138  ? 1219 LEU   B O    1 
ATOM   1122 C  CB   . LEU   A 1 167 ? 21.07174  -4.12257  7.25405   1.000 55.84458  ? 1219 LEU   B CB   1 
ATOM   1123 C  CG   . LEU   A 1 167 ? 22.19478  -4.00325  8.28797   1.000 52.03473  ? 1219 LEU   B CG   1 
ATOM   1124 C  CD1  . LEU   A 1 167 ? 21.65480  -4.25665  9.68609   1.000 41.27640  ? 1219 LEU   B CD1  1 
ATOM   1125 C  CD2  . LEU   A 1 167 ? 23.32670  -4.96846  7.96732   1.000 49.91926  ? 1219 LEU   B CD2  1 
ATOM   1126 N  N    . ALA   A 1 168 ? 19.68373  -3.09767  4.19169   1.000 51.52725  ? 1220 ALA   B N    1 
ATOM   1127 C  CA   . ALA   A 1 168 ? 18.43670  -3.26286  3.45879   1.000 50.76043  ? 1220 ALA   B CA   1 
ATOM   1128 C  C    . ALA   A 1 168 ? 18.54858  -4.37329  2.41623   1.000 52.76126  ? 1220 ALA   B C    1 
ATOM   1129 O  O    . ALA   A 1 168 ? 19.60655  -4.60360  1.82429   1.000 49.72151  ? 1220 ALA   B O    1 
ATOM   1130 C  CB   . ALA   A 1 168 ? 18.04478  -1.94910  2.78028   1.000 50.14953  ? 1220 ALA   B CB   1 
ATOM   1131 N  N    . ASN   A 1 169 ? 17.42752  -5.06929  2.19753   1.000 48.23665  ? 1221 ASN   B N    1 
ATOM   1132 C  CA   . ASN   A 1 169 ? 17.32541  -6.09668  1.17094   1.000 40.99227  ? 1221 ASN   B CA   1 
ATOM   1133 C  C    . ASN   A 1 169 ? 16.47941  -5.68309  -0.02520  1.000 42.40514  ? 1221 ASN   B C    1 
ATOM   1134 O  O    . ASN   A 1 169 ? 16.65133  -6.25453  -1.10697  1.000 46.07648  ? 1221 ASN   B O    1 
ATOM   1135 C  CB   . ASN   A 1 169 ? 16.74033  -7.38940  1.76647   1.000 42.90242  ? 1221 ASN   B CB   1 
ATOM   1136 C  CG   . ASN   A 1 169 ? 17.78428  -8.22520  2.48177   1.000 43.97356  ? 1221 ASN   B CG   1 
ATOM   1137 O  OD1  . ASN   A 1 169 ? 18.83524  -8.53550  1.92286   1.000 42.50027  ? 1221 ASN   B OD1  1 
ATOM   1138 N  ND2  . ASN   A 1 169 ? 17.49729  -8.59069  3.72593   1.000 38.73314  ? 1221 ASN   B ND2  1 
ATOM   1139 N  N    . ASN   A 1 170 ? 15.57149  -4.71895  0.14345   1.000 35.95310  ? 1222 ASN   B N    1 
ATOM   1140 C  CA   . ASN   A 1 170 ? 14.75249  -4.20433  -0.95573  1.000 37.95725  ? 1222 ASN   B CA   1 
ATOM   1141 C  C    . ASN   A 1 170 ? 13.76340  -5.25345  -1.46829  1.000 41.47102  ? 1222 ASN   B C    1 
ATOM   1142 O  O    . ASN   A 1 170 ? 13.49536  -5.33191  -2.66725  1.000 38.01306  ? 1222 ASN   B O    1 
ATOM   1143 C  CB   . ASN   A 1 170 ? 15.62450  -3.68885  -2.10296  1.000 37.39016  ? 1222 ASN   B CB   1 
ATOM   1144 C  CG   . ASN   A 1 170 ? 16.68159  -2.69875  -1.63938  1.000 55.79356  ? 1222 ASN   B CG   1 
ATOM   1145 O  OD1  . ASN   A 1 170 ? 17.87257  -2.89193  -1.87534  1.000 50.85183  ? 1222 ASN   B OD1  1 
ATOM   1146 N  ND2  . ASN   A 1 170 ? 16.24669  -1.63245  -0.97779  1.000 55.23138  ? 1222 ASN   B ND2  1 
ATOM   1147 N  N    . TYR   A 1 171 ? 13.22136  -6.06705  -0.56295  1.000 39.60981  ? 1223 TYR   B N    1 
ATOM   1148 C  CA   . TYR   A 1 171 ? 12.22127  -7.04713  -0.96953  1.000 41.09337  ? 1223 TYR   B CA   1 
ATOM   1149 C  C    . TYR   A 1 171 ? 11.01431  -6.34228  -1.57477  1.000 32.87858  ? 1223 TYR   B C    1 
ATOM   1150 O  O    . TYR   A 1 171 ? 10.45040  -5.42300  -0.97712  1.000 34.30359  ? 1223 TYR   B O    1 
ATOM   1151 C  CB   . TYR   A 1 171 ? 11.79824  -7.90663  0.22082   1.000 33.54316  ? 1223 TYR   B CB   1 
ATOM   1152 C  CG   . TYR   A 1 171 ? 12.80817  -8.97056  0.59521   1.000 34.49426  ? 1223 TYR   B CG   1 
ATOM   1153 C  CD1  . TYR   A 1 171 ? 13.15207  -9.97394  -0.29940  1.000 37.05532  ? 1223 TYR   B CD1  1 
ATOM   1154 C  CD2  . TYR   A 1 171 ? 13.40321  -8.97811  1.84720   1.000 35.04409  ? 1223 TYR   B CD2  1 
ATOM   1155 C  CE1  . TYR   A 1 171 ? 14.07000  -10.95388 0.04196   1.000 39.49302  ? 1223 TYR   B CE1  1 
ATOM   1156 C  CE2  . TYR   A 1 171 ? 14.31914  -9.95304  2.19956   1.000 36.82980  ? 1223 TYR   B CE2  1 
ATOM   1157 C  CZ   . TYR   A 1 171 ? 14.64904  -10.93743 1.29094   1.000 38.07928  ? 1223 TYR   B CZ   1 
ATOM   1158 O  OH   . TYR   A 1 171 ? 15.56197  -11.90736 1.63330   1.000 38.34056  ? 1223 TYR   B OH   1 
ATOM   1159 N  N    . LYS   A 1 172 ? 10.61224  -6.75172  -2.76860  1.000 34.07992  ? 1224 LYS   B N    1 
ATOM   1160 C  CA   . LYS   A 1 172 ? 9.52828   -6.04092  -3.49185  1.000 38.71567  ? 1224 LYS   B CA   1 
ATOM   1161 C  C    . LYS   A 1 172 ? 8.18329   -6.18153  -2.76875  1.000 42.62576  ? 1224 LYS   B C    1 
ATOM   1162 O  O    . LYS   A 1 172 ? 7.35835   -5.28252  -2.90308  1.000 38.74805  ? 1224 LYS   B O    1 
ATOM   1163 C  CB   . LYS   A 1 172 ? 9.47319   -6.58448  -4.91963  1.000 37.81641  ? 1224 LYS   B CB   1 
ATOM   1164 C  CG   . LYS   A 1 172 ? 10.74618  -6.39090  -5.72075  1.000 50.35083  ? 1224 LYS   B CG   1 
ATOM   1165 C  CD   . LYS   A 1 172 ? 10.52713  -6.56948  -7.21567  1.000 52.88395  ? 1224 LYS   B CD   1 
ATOM   1166 C  CE   . LYS   A 1 172 ? 11.68614  -6.08388  -8.02290  1.000 58.09798  ? 1224 LYS   B CE   1 
ATOM   1167 N  NZ   . LYS   A 1 172 ? 11.42709  -6.22743  -9.45683  1.000 70.12459  ? 1224 LYS   B NZ   1 
ATOM   1168 N  N    . ARG   A 1 173 ? 7.97422   -7.28724  -2.06531  1.000 40.10033  ? 1225 ARG   B N    1 
ATOM   1169 C  CA   . ARG   A 1 173 ? 6.73623   -7.48585  -1.31519  1.000 41.38834  ? 1225 ARG   B CA   1 
ATOM   1170 C  C    . ARG   A 1 173 ? 6.99228   -7.44127  0.19078   1.000 43.07288  ? 1225 ARG   B C    1 
ATOM   1171 O  O    . ARG   A 1 173 ? 6.39724   -8.19792  0.96210   1.000 32.03568  ? 1225 ARG   B O    1 
ATOM   1172 C  CB   . ARG   A 1 173 ? 6.06912   -8.80395  -1.70065  1.000 33.43848  ? 1225 ARG   B CB   1 
ATOM   1173 C  CG   . ARG   A 1 173 ? 5.92105   -9.04353  -3.19955  1.000 38.49207  ? 1225 ARG   B CG   1 
ATOM   1174 C  CD   . ARG   A 1 173 ? 5.02011   -8.01372  -3.86594  1.000 42.51409  ? 1225 ARG   B CD   1 
ATOM   1175 N  NE   . ARG   A 1 173 ? 3.67813   -7.98939  -3.29491  1.000 40.12971  ? 1225 ARG   B NE   1 
ATOM   1176 C  CZ   . ARG   A 1 173 ? 2.64306   -8.67050  -3.77161  1.000 42.35647  ? 1225 ARG   B CZ   1 
ATOM   1177 N  NH1  . ARG   A 1 173 ? 2.75897   -9.44993  -4.83530  1.000 39.48797  ? 1225 ARG   B NH1  1 
ATOM   1178 N  NH2  . ARG   A 1 173 ? 1.46409   -8.56217  -3.16761  1.000 37.39191  ? 1225 ARG   B NH2  1 
ATOM   1179 N  N    . ASN   A 1 174 ? 7.87636   -6.54417  0.62140   1.000 35.84908  ? 1226 ASN   B N    1 
ATOM   1180 C  CA   . ASN   A 1 174 ? 8.25341   -6.47664  2.02836   1.000 40.95585  ? 1226 ASN   B CA   1 
ATOM   1181 C  C    . ASN   A 1 174 ? 7.04145   -6.19120  2.91028   1.000 39.84590  ? 1226 ASN   B C    1 
ATOM   1182 O  O    . ASN   A 1 174 ? 6.17651   -5.38327  2.56299   1.000 40.72126  ? 1226 ASN   B O    1 
ATOM   1183 C  CB   . ASN   A 1 174 ? 9.31550   -5.39464  2.23890   1.000 42.47685  ? 1226 ASN   B CB   1 
ATOM   1184 C  CG   . ASN   A 1 174 ? 9.64956   -5.18408  3.70681   1.000 39.02048  ? 1226 ASN   B CG   1 
ATOM   1185 O  OD1  . ASN   A 1 174 ? 9.84050   -6.14080  4.45818   1.000 41.68876  ? 1226 ASN   B OD1  1 
ATOM   1186 N  ND2  . ASN   A 1 174 ? 9.70567   -3.92492  4.12331   1.000 46.34408  ? 1226 ASN   B ND2  1 
ATOM   1187 N  N    . CYS   A 1 175 ? 6.99144   -6.85974  4.06155   1.000 38.19555  ? 1227 CYS   B N    1 
ATOM   1188 C  CA   . CYS   A 1 175 ? 5.96248   -6.62826  5.07049   1.000 40.95669  ? 1227 CYS   B CA   1 
ATOM   1189 C  C    . CYS   A 1 175 ? 6.60251   -6.76977  6.44153   1.000 41.36958  ? 1227 CYS   B C    1 
ATOM   1190 O  O    . CYS   A 1 175 ? 7.07244   -7.85466  6.79794   1.000 42.85001  ? 1227 CYS   B O    1 
ATOM   1191 C  CB   . CYS   A 1 175 ? 4.79040   -7.60623  4.92191   1.000 41.44245  ? 1227 CYS   B CB   1 
ATOM   1192 S  SG   . CYS   A 1 175 ? 3.70239   -7.27470  3.51481   1.000 49.47999  ? 1227 CYS   B SG   1 
ATOM   1193 N  N    . ALA   A 1 176 ? 6.62762   -5.67947  7.20209   1.000 39.88761  ? 1228 ALA   B N    1 
ATOM   1194 C  CA   . ALA   A 1 176 ? 7.20666   -5.70298  8.53709   1.000 40.42154  ? 1228 ALA   B CA   1 
ATOM   1195 C  C    . ALA   A 1 176 ? 6.25064   -6.36352  9.52238   1.000 45.59645  ? 1228 ALA   B C    1 
ATOM   1196 O  O    . ALA   A 1 176 ? 5.02664   -6.26448  9.39137   1.000 43.64738  ? 1228 ALA   B O    1 
ATOM   1197 C  CB   . ALA   A 1 176 ? 7.54378   -4.28682  9.00152   1.000 41.89794  ? 1228 ALA   B CB   1 
ATOM   1198 N  N    . THR   A 1 177 ? 6.81961   -7.03917  10.51963  1.000 41.74811  ? 1229 THR   B N    1 
ATOM   1199 C  CA   . THR   A 1 177 ? 6.01258   -7.83674  11.43197  1.000 44.21603  ? 1229 THR   B CA   1 
ATOM   1200 C  C    . THR   A 1 177 ? 6.72960   -7.99627  12.76701  1.000 45.27657  ? 1229 THR   B C    1 
ATOM   1201 O  O    . THR   A 1 177 ? 7.95760   -8.10835  12.80702  1.000 44.46139  ? 1229 THR   B O    1 
ATOM   1202 C  CB   . THR   A 1 177 ? 5.70645   -9.21396  10.82752  1.000 42.88828  ? 1229 THR   B CB   1 
ATOM   1203 O  OG1  . THR   A 1 177 ? 4.91742   -9.97854  11.74485  1.000 42.31905  ? 1229 THR   B OG1  1 
ATOM   1204 C  CG2  . THR   A 1 177 ? 6.99939   -9.96418  10.52578  1.000 37.87316  ? 1229 THR   B CG2  1 
ATOM   1205 N  N    . PHE   A 1 178 ? 5.95264   -8.00778  13.84704  1.000 46.69119  ? 1230 PHE   B N    1 
ATOM   1206 C  CA   . PHE   A 1 178 ? 6.45265   -8.31730  15.17814  1.000 42.74733  ? 1230 PHE   B CA   1 
ATOM   1207 C  C    . PHE   A 1 178 ? 6.65054   -9.82225  15.33973  1.000 48.61029  ? 1230 PHE   B C    1 
ATOM   1208 O  O    . PHE   A 1 178 ? 6.05145   -10.63248 14.62907  1.000 45.07636  ? 1230 PHE   B O    1 
ATOM   1209 C  CB   . PHE   A 1 178 ? 5.47772   -7.83979  16.25898  1.000 45.12972  ? 1230 PHE   B CB   1 
ATOM   1210 C  CG   . PHE   A 1 178 ? 5.49184   -6.35670  16.50140  1.000 49.86986  ? 1230 PHE   B CG   1 
ATOM   1211 C  CD1  . PHE   A 1 178 ? 6.46291   -5.78046  17.30314  1.000 56.34024  ? 1230 PHE   B CD1  1 
ATOM   1212 C  CD2  . PHE   A 1 178 ? 4.50589   -5.54383  15.96210  1.000 44.80044  ? 1230 PHE   B CD2  1 
ATOM   1213 C  CE1  . PHE   A 1 178 ? 6.46802   -4.41636  17.54160  1.000 56.45368  ? 1230 PHE   B CE1  1 
ATOM   1214 C  CE2  . PHE   A 1 178 ? 4.50200   -4.17874  16.19856  1.000 45.32825  ? 1230 PHE   B CE2  1 
ATOM   1215 C  CZ   . PHE   A 1 178 ? 5.48207   -3.61550  16.98931  1.000 49.49556  ? 1230 PHE   B CZ   1 
ATOM   1216 N  N    . ASN   A 1 179 ? 7.48254   -10.19093 16.30486  1.000 44.24873  ? 1231 ASN   B N    1 
ATOM   1217 C  CA   . ASN   A 1 179 ? 7.55444   -11.57176 16.75240  1.000 45.87838  ? 1231 ASN   B CA   1 
ATOM   1218 C  C    . ASN   A 1 179 ? 6.55146   -11.79524 17.87252  1.000 50.31671  ? 1231 ASN   B C    1 
ATOM   1219 O  O    . ASN   A 1 179 ? 5.95755   -10.84898 18.39516  1.000 43.33819  ? 1231 ASN   B O    1 
ATOM   1220 C  CB   . ASN   A 1 179 ? 8.97843   -11.90869 17.19449  1.000 50.47488  ? 1231 ASN   B CB   1 
ATOM   1221 C  CG   . ASN   A 1 179 ? 9.31751   -11.35718 18.56526  1.000 52.19866  ? 1231 ASN   B CG   1 
ATOM   1222 O  OD1  . ASN   A 1 179 ? 9.02961   -10.20103 18.87181  1.000 46.45976  ? 1231 ASN   B OD1  1 
ATOM   1223 N  ND2  . ASN   A 1 179 ? 9.93347   -12.18790 19.39657  1.000 52.63448  ? 1231 ASN   B ND2  1 
ATOM   1224 N  N    . PRO   A 1 180 ? 6.32537   -13.05306 18.26402  1.000 41.57423  ? 1232 PRO   B N    1 
ATOM   1225 C  CA   . PRO   A 1 180 ? 5.22338   -13.34361 19.19917  1.000 49.56741  ? 1232 PRO   B CA   1 
ATOM   1226 C  C    . PRO   A 1 180 ? 5.28148   -12.57210 20.50686  1.000 47.96075  ? 1232 PRO   B C    1 
ATOM   1227 O  O    . PRO   A 1 180 ? 4.22352   -12.23680 21.05076  1.000 62.48755  ? 1232 PRO   B O    1 
ATOM   1228 C  CB   . PRO   A 1 180 ? 5.35527   -14.85553 19.42376  1.000 37.81966  ? 1232 PRO   B CB   1 
ATOM   1229 C  CG   . PRO   A 1 180 ? 5.99519   -15.35508 18.17094  1.000 44.64941  ? 1232 PRO   B CG   1 
ATOM   1230 C  CD   . PRO   A 1 180 ? 6.96226   -14.28231 17.76249  1.000 42.74104  ? 1232 PRO   B CD   1 
ATOM   1231 N  N    . THR   A 1 181 ? 6.46752   -12.28298 21.04171  1.000 55.71948  ? 1233 THR   B N    1 
ATOM   1232 C  CA   . THR   A 1 181 ? 6.57861   -11.54649 22.29342  1.000 54.90837  ? 1233 THR   B CA   1 
ATOM   1233 C  C    . THR   A 1 181 ? 6.78772   -10.05059 22.08482  1.000 55.46247  ? 1233 THR   B C    1 
ATOM   1234 O  O    . THR   A 1 181 ? 7.10780   -9.34123  23.04453  1.000 57.97053  ? 1233 THR   B O    1 
ATOM   1235 C  CB   . THR   A 1 181 ? 7.70859   -12.12123 23.15961  1.000 54.92043  ? 1233 THR   B CB   1 
ATOM   1236 O  OG1  . THR   A 1 181 ? 8.89856   -12.26964 22.37364  1.000 57.13334  ? 1233 THR   B OG1  1 
ATOM   1237 C  CG2  . THR   A 1 181 ? 7.30850   -13.47098 23.73516  1.000 50.01745  ? 1233 THR   B CG2  1 
ATOM   1238 N  N    . ASP   A 1 182 ? 6.63872   -9.56406  20.85463  1.000 54.59413  ? 1234 ASP   B N    1 
ATOM   1239 C  CA   . ASP   A 1 182 ? 6.68182   -8.15422  20.47207  1.000 54.84320  ? 1234 ASP   B CA   1 
ATOM   1240 C  C    . ASP   A 1 182 ? 8.01588   -7.47021  20.76276  1.000 56.82123  ? 1234 ASP   B C    1 
ATOM   1241 O  O    . ASP   A 1 182 ? 8.11397   -6.24228  20.60627  1.000 59.66863  ? 1234 ASP   B O    1 
ATOM   1242 C  CB   . ASP   A 1 182 ? 5.56090   -7.34687  21.14079  1.000 56.18248  ? 1234 ASP   B CB   1 
ATOM   1243 C  CG   . ASP   A 1 182 ? 4.18285   -7.89288  20.82404  1.000 58.13466  ? 1234 ASP   B CG   1 
ATOM   1244 O  OD1  . ASP   A 1 182 ? 4.01577   -8.50230  19.74529  1.000 60.69867  ? 1234 ASP   B OD1  1 
ATOM   1245 O  OD2  . ASP   A 1 182 ? 3.26589   -7.70449  21.65000  1.000 61.38563  ? 1234 ASP   B OD2  1 
ATOM   1246 N  N    . ASP   A 1 183 ? 9.04284   -8.20912  21.18503  1.000 55.57236  ? 1235 ASP   B N    1 
ATOM   1247 C  CA   . ASP   A 1 183 ? 10.34689  -7.61711  21.46475  1.000 58.52363  ? 1235 ASP   B CA   1 
ATOM   1248 C  C    . ASP   A 1 183 ? 11.26386  -7.58566  20.25071  1.000 60.31120  ? 1235 ASP   B C    1 
ATOM   1249 O  O    . ASP   A 1 183 ? 12.29591  -6.90772  20.29441  1.000 57.37551  ? 1235 ASP   B O    1 
ATOM   1250 C  CB   . ASP   A 1 183 ? 11.04386  -8.37871  22.60103  1.000 57.67969  ? 1235 ASP   B CB   1 
ATOM   1251 C  CG   . ASP   A 1 183 ? 11.24074  -9.84485  22.28561  1.000 61.63193  ? 1235 ASP   B CG   1 
ATOM   1252 O  OD1  . ASP   A 1 183 ? 10.30168  -10.46999 21.74888  1.000 62.87077  ? 1235 ASP   B OD1  1 
ATOM   1253 O  OD2  . ASP   A 1 183 ? 12.33471  -10.37682 22.57879  1.000 69.96765  ? 1235 ASP   B OD2  1 
ATOM   1254 N  N    . LEU   A 1 184 ? 10.91977  -8.29406  19.17700  1.000 49.23716  ? 1236 LEU   B N    1 
ATOM   1255 C  CA   . LEU   A 1 184 ? 11.70373  -8.29461  17.95298  1.000 49.95074  ? 1236 LEU   B CA   1 
ATOM   1256 C  C    . LEU   A 1 184 ? 10.81173  -7.93400  16.77486  1.000 51.33105  ? 1236 LEU   B C    1 
ATOM   1257 O  O    . LEU   A 1 184 ? 9.60271   -8.17790  16.79100  1.000 51.34246  ? 1236 LEU   B O    1 
ATOM   1258 C  CB   . LEU   A 1 184 ? 12.36362  -9.65776  17.70150  1.000 49.59013  ? 1236 LEU   B CB   1 
ATOM   1259 C  CG   . LEU   A 1 184 ? 13.46962  -10.07946 18.67064  1.000 52.56406  ? 1236 LEU   B CG   1 
ATOM   1260 C  CD1  . LEU   A 1 184 ? 13.95250  -11.48563 18.34418  1.000 43.21425  ? 1236 LEU   B CD1  1 
ATOM   1261 C  CD2  . LEU   A 1 184 ? 14.62369  -9.08856  18.62821  1.000 53.90084  ? 1236 LEU   B CD2  1 
ATOM   1262 N  N    . VAL   A 1 185 ? 11.42174  -7.34746  15.74861  1.000 43.96197  ? 1237 VAL   B N    1 
ATOM   1263 C  CA   . VAL   A 1 185 ? 10.71973  -7.00489  14.52050  1.000 43.07772  ? 1237 VAL   B CA   1 
ATOM   1264 C  C    . VAL   A 1 185 ? 11.51366  -7.53842  13.33869  1.000 45.55746  ? 1237 VAL   B C    1 
ATOM   1265 O  O    . VAL   A 1 185 ? 12.74065  -7.65249  13.39070  1.000 49.69943  ? 1237 VAL   B O    1 
ATOM   1266 C  CB   . VAL   A 1 185 ? 10.49785  -5.48092  14.39390  1.000 41.74347  ? 1237 VAL   B CB   1 
ATOM   1267 C  CG1  . VAL   A 1 185 ? 10.20384  -5.09347  12.95276  1.000 39.27956  ? 1237 VAL   B CG1  1 
ATOM   1268 C  CG2  . VAL   A 1 185 ? 9.36291   -5.03647  15.30176  1.000 39.45837  ? 1237 VAL   B CG2  1 
ATOM   1269 N  N    . LEU   A 1 186 ? 10.80460  -7.88178  12.26984  1.000 39.66196  ? 1238 LEU   B N    1 
ATOM   1270 C  CA   . LEU   A 1 186 ? 11.41953  -8.34232  11.03301  1.000 41.30956  ? 1238 LEU   B CA   1 
ATOM   1271 C  C    . LEU   A 1 186 ? 10.97657  -7.41373  9.91565   1.000 41.31619  ? 1238 LEU   B C    1 
ATOM   1272 O  O    . LEU   A 1 186 ? 9.77557   -7.27574  9.66263   1.000 44.08390  ? 1238 LEU   B O    1 
ATOM   1273 C  CB   . LEU   A 1 186 ? 11.03340  -9.79441  10.73359  1.000 43.79257  ? 1238 LEU   B CB   1 
ATOM   1274 C  CG   . LEU   A 1 186 ? 12.00432  -10.62682 9.89389   1.000 51.52216  ? 1238 LEU   B CG   1 
ATOM   1275 C  CD1  . LEU   A 1 186 ? 13.43635  -10.42574 10.37277  1.000 53.93977  ? 1238 LEU   B CD1  1 
ATOM   1276 C  CD2  . LEU   A 1 186 ? 11.62720  -12.09676 9.96049   1.000 50.53206  ? 1238 LEU   B CD2  1 
ATOM   1277 N  N    . ASN   A 1 187 ? 11.93760  -6.76006  9.26437   1.000 42.43199  ? 1239 ASN   B N    1 
ATOM   1278 C  CA   . ASN   A 1 187 ? 11.62364  -5.81146  8.19900   1.000 40.00731  ? 1239 ASN   B CA   1 
ATOM   1279 C  C    . ASN   A 1 187 ? 12.65160  -5.94798  7.09002   1.000 43.77687  ? 1239 ASN   B C    1 
ATOM   1280 O  O    . ASN   A 1 187 ? 13.84762  -5.76498  7.32892   1.000 45.78854  ? 1239 ASN   B O    1 
ATOM   1281 C  CB   . ASN   A 1 187 ? 11.59577  -4.37125  8.71843   1.000 41.75187  ? 1239 ASN   B CB   1 
ATOM   1282 C  CG   . ASN   A 1 187 ? 11.23381  -3.37065  7.63504   1.000 44.51026  ? 1239 ASN   B CG   1 
ATOM   1283 O  OD1  . ASN   A 1 187 ? 10.29777  -3.58689  6.86316   1.000 46.41911  ? 1239 ASN   B OD1  1 
ATOM   1284 N  ND2  . ASN   A 1 187 ? 11.98490  -2.27674  7.56159   1.000 40.77370  ? 1239 ASN   B ND2  1 
ATOM   1285 N  N    . ASP   A 1 188 ? 12.18454  -6.25142  5.87916   1.000 38.21339  ? 1240 ASP   B N    1 
ATOM   1286 C  CA   . ASP   A 1 188 ? 13.06449  -6.37795  4.72218   1.000 41.84971  ? 1240 ASP   B CA   1 
ATOM   1287 C  C    . ASP   A 1 188 ? 14.11842  -7.45894  4.93958   1.000 47.11784  ? 1240 ASP   B C    1 
ATOM   1288 O  O    . ASP   A 1 188 ? 15.22141  -7.38624  4.39452   1.000 42.51558  ? 1240 ASP   B O    1 
ATOM   1289 C  CB   . ASP   A 1 188 ? 13.73559  -5.03913  4.39463   1.000 43.38703  ? 1240 ASP   B CB   1 
ATOM   1290 C  CG   . ASP   A 1 188 ? 14.05756  -4.89474  2.92156   1.000 42.90453  ? 1240 ASP   B CG   1 
ATOM   1291 O  OD1  . ASP   A 1 188 ? 13.49647  -5.65602  2.10588   1.000 42.63384  ? 1240 ASP   B OD1  1 
ATOM   1292 O  OD2  . ASP   A 1 188 ? 14.87761  -4.02094  2.57919   1.000 46.70383  ? 1240 ASP   B OD2  1 
ATOM   1293 N  N    . GLY   A 1 189 ? 13.78736  -8.46960  5.74099   1.000 42.18134  ? 1241 GLY   B N    1 
ATOM   1294 C  CA   . GLY   A 1 189 ? 14.74329  -9.50855  6.06337   1.000 42.79453  ? 1241 GLY   B CA   1 
ATOM   1295 C  C    . GLY   A 1 189 ? 15.77035  -9.12822  7.10119   1.000 42.95434  ? 1241 GLY   B C    1 
ATOM   1296 O  O    . GLY   A 1 189 ? 16.77830  -9.82524  7.24444   1.000 44.61008  ? 1241 GLY   B O    1 
ATOM   1297 N  N    . VAL   A 1 190 ? 15.55146  -8.03691  7.82776   1.000 45.87082  ? 1242 VAL   B N    1 
ATOM   1298 C  CA   . VAL   A 1 190 ? 16.46252  -7.56857  8.86355   1.000 42.49519  ? 1242 VAL   B CA   1 
ATOM   1299 C  C    . VAL   A 1 190 ? 15.78155  -7.72899  10.21364  1.000 48.64370  ? 1242 VAL   B C    1 
ATOM   1300 O  O    . VAL   A 1 190 ? 14.60858  -7.36483  10.37453  1.000 43.49752  ? 1242 VAL   B O    1 
ATOM   1301 C  CB   . VAL   A 1 190 ? 16.88263  -6.10770  8.62996   1.000 46.89809  ? 1242 VAL   B CB   1 
ATOM   1302 C  CG1  . VAL   A 1 190 ? 17.80870  -5.64333  9.74175   1.000 41.12189  ? 1242 VAL   B CG1  1 
ATOM   1303 C  CG2  . VAL   A 1 190 ? 17.54960  -5.95729  7.27188   1.000 46.47516  ? 1242 VAL   B CG2  1 
ATOM   1304 N  N    . LEU   A 1 191 ? 16.51654  -8.28366  11.17683  1.000 48.34202  ? 1243 LEU   B N    1 
ATOM   1305 C  CA   . LEU   A 1 191 ? 16.02756  -8.51409  12.52694  1.000 47.53454  ? 1243 LEU   B CA   1 
ATOM   1306 C  C    . LEU   A 1 191 ? 16.37468  -7.30477  13.38845  1.000 52.52279  ? 1243 LEU   B C    1 
ATOM   1307 O  O    . LEU   A 1 191 ? 17.55071  -6.94981  13.52528  1.000 53.34001  ? 1243 LEU   B O    1 
ATOM   1308 C  CB   . LEU   A 1 191 ? 16.65047  -9.78991  13.09843  1.000 45.04245  ? 1243 LEU   B CB   1 
ATOM   1309 C  CG   . LEU   A 1 191 ? 16.14047  -10.35435 14.42266  1.000 52.59129  ? 1243 LEU   B CG   1 
ATOM   1310 C  CD1  . LEU   A 1 191 ? 14.66944  -10.71828 14.31485  1.000 47.45739  ? 1243 LEU   B CD1  1 
ATOM   1311 C  CD2  . LEU   A 1 191 ? 16.97039  -11.56425 14.83712  1.000 45.66239  ? 1243 LEU   B CD2  1 
ATOM   1312 N  N    . TRP   A 1 192 ? 15.35274  -6.67447  13.95623  1.000 50.84303  ? 1244 TRP   B N    1 
ATOM   1313 C  CA   . TRP   A 1 192 ? 15.49686  -5.47816  14.76975  1.000 53.51773  ? 1244 TRP   B CA   1 
ATOM   1314 C  C    . TRP   A 1 192 ? 15.12188  -5.77756  16.21388  1.000 56.07064  ? 1244 TRP   B C    1 
ATOM   1315 O  O    . TRP   A 1 192 ? 14.12883  -6.46438  16.47818  1.000 53.24664  ? 1244 TRP   B O    1 
ATOM   1316 C  CB   . TRP   A 1 192 ? 14.60893  -4.34730  14.24633  1.000 47.89240  ? 1244 TRP   B CB   1 
ATOM   1317 C  CG   . TRP   A 1 192 ? 14.99093  -3.82786  12.90212  1.000 48.26290  ? 1244 TRP   B CG   1 
ATOM   1318 C  CD1  . TRP   A 1 192 ? 14.70485  -4.39432  11.69135  1.000 43.00759  ? 1244 TRP   B CD1  1 
ATOM   1319 C  CD2  . TRP   A 1 192 ? 15.70902  -2.62003  12.62162  1.000 53.69233  ? 1244 TRP   B CD2  1 
ATOM   1320 N  NE1  . TRP   A 1 192 ? 15.21288  -3.61576  10.67702  1.000 51.68187  ? 1244 TRP   B NE1  1 
ATOM   1321 C  CE2  . TRP   A 1 192 ? 15.83198  -2.52159  11.22057  1.000 47.00839  ? 1244 TRP   B CE2  1 
ATOM   1322 C  CE3  . TRP   A 1 192 ? 16.26212  -1.61475  13.42220  1.000 54.53700  ? 1244 TRP   B CE3  1 
ATOM   1323 C  CZ2  . TRP   A 1 192 ? 16.48905  -1.45389  10.60313  1.000 55.60138  ? 1244 TRP   B CZ2  1 
ATOM   1324 C  CZ3  . TRP   A 1 192 ? 16.91318  -0.55905  12.80577  1.000 52.26436  ? 1244 TRP   B CZ3  1 
ATOM   1325 C  CH2  . TRP   A 1 192 ? 17.02015  -0.48761  11.41073  1.000 49.81426  ? 1244 TRP   B CH2  1 
ATOM   1326 N  N    . ASP   A 1 193 ? 15.91595  -5.24825  17.13765  1.000 55.60697  ? 1245 ASP   B N    1 
ATOM   1327 C  CA   . ASP   A 1 193 ? 15.57799  -5.24367  18.55466  1.000 57.89484  ? 1245 ASP   B CA   1 
ATOM   1328 C  C    . ASP   A 1 193 ? 14.76109  -3.99149  18.85019  1.000 49.35041  ? 1245 ASP   B C    1 
ATOM   1329 O  O    . ASP   A 1 193 ? 15.26318  -2.86958  18.71373  1.000 56.03035  ? 1245 ASP   B O    1 
ATOM   1330 C  CB   . ASP   A 1 193 ? 16.83901  -5.28843  19.41464  1.000 51.79875  ? 1245 ASP   B CB   1 
ATOM   1331 C  CG   . ASP   A 1 193 ? 16.55707  -5.02382  20.87854  1.000 54.65812  ? 1245 ASP   B CG   1 
ATOM   1332 O  OD1  . ASP   A 1 193 ? 16.02102  -5.92651  21.55692  1.000 50.19269  ? 1245 ASP   B OD1  1 
ATOM   1333 O  OD2  . ASP   A 1 193 ? 16.86717  -3.90666  21.34709  1.000 57.73647  ? 1245 ASP   B OD2  1 
ATOM   1334 N  N    . VAL   A 1 194 ? 13.50209  -4.18123  19.24730  1.000 53.09775  ? 1246 VAL   B N    1 
ATOM   1335 C  CA   . VAL   A 1 194 ? 12.59418  -3.04710  19.40588  1.000 59.00332  ? 1246 VAL   B CA   1 
ATOM   1336 C  C    . VAL   A 1 194 ? 13.08129  -2.11770  20.50950  1.000 55.27965  ? 1246 VAL   B C    1 
ATOM   1337 O  O    . VAL   A 1 194 ? 13.06138  -0.89076  20.35801  1.000 63.14576  ? 1246 VAL   B O    1 
ATOM   1338 C  CB   . VAL   A 1 194 ? 11.16215  -3.54488  19.68012  1.000 59.37551  ? 1246 VAL   B CB   1 
ATOM   1339 C  CG1  . VAL   A 1 194 ? 10.23925  -2.37269  19.96868  1.000 59.46298  ? 1246 VAL   B CG1  1 
ATOM   1340 C  CG2  . VAL   A 1 194 ? 10.65206  -4.36330  18.51046  1.000 58.00610  ? 1246 VAL   B CG2  1 
ATOM   1341 N  N    . ARG   A 1 195 ? 13.52228  -2.68629  21.63471  1.000 64.67454  ? 1247 ARG   B N    1 
ATOM   1342 C  CA   . ARG   A 1 195 ? 13.90038  -1.87086  22.78737  1.000 60.93209  ? 1247 ARG   B CA   1 
ATOM   1343 C  C    . ARG   A 1 195 ? 14.94745  -0.82909  22.40793  1.000 59.32778  ? 1247 ARG   B C    1 
ATOM   1344 O  O    . ARG   A 1 195 ? 14.79155  0.36203   22.69546  1.000 65.07675  ? 1247 ARG   B O    1 
ATOM   1345 C  CB   . ARG   A 1 195 ? 14.41134  -2.76746  23.91471  1.000 56.53444  ? 1247 ARG   B CB   1 
ATOM   1346 C  CG   . ARG   A 1 195 ? 14.80843  -2.00999  25.17040  1.000 72.27503  ? 1247 ARG   B CG   1 
ATOM   1347 C  CD   . ARG   A 1 195 ? 15.23839  -2.95158  26.28176  1.000 77.55650  ? 1247 ARG   B CD   1 
ATOM   1348 N  NE   . ARG   A 1 195 ? 15.59749  -2.22513  27.49446  1.000 98.59192  ? 1247 ARG   B NE   1 
ATOM   1349 C  CZ   . ARG   A 1 195 ? 15.82448  -2.79468  28.67268  1.000 104.26541 ? 1247 ARG   B CZ   1 
ATOM   1350 N  NH1  . ARG   A 1 195 ? 15.73638  -4.10261  28.83820  1.000 94.62396  ? 1247 ARG   B NH1  1 
ATOM   1351 N  NH2  . ARG   A 1 195 ? 16.14657  -2.02830  29.71037  1.000 106.46842 ? 1247 ARG   B NH2  1 
ATOM   1352 N  N    . SER   A 1 196 ? 16.02239  -1.26244  21.75207  1.000 62.55500  ? 1248 SER   B N    1 
ATOM   1353 C  CA   . SER   A 1 196 ? 17.09345  -0.35868  21.35468  1.000 62.18075  ? 1248 SER   B CA   1 
ATOM   1354 C  C    . SER   A 1 196 ? 16.91445  0.20378   19.95146  1.000 65.30493  ? 1248 SER   B C    1 
ATOM   1355 O  O    . SER   A 1 196 ? 17.67751  1.09257   19.55809  1.000 59.32248  ? 1248 SER   B O    1 
ATOM   1356 C  CB   . SER   A 1 196 ? 18.44640  -1.07075  21.43892  1.000 63.31904  ? 1248 SER   B CB   1 
ATOM   1357 O  OG   . SER   A 1 196 ? 18.58029  -2.03017  20.40630  1.000 64.81247  ? 1248 SER   B OG   1 
ATOM   1358 N  N    . ALA   A 1 197 ? 15.93239  -0.28444  19.19169  1.000 64.42115  ? 1249 ALA   B N    1 
ATOM   1359 C  CA   . ALA   A 1 197 ? 15.72739  0.15303   17.81252  1.000 60.69624  ? 1249 ALA   B CA   1 
ATOM   1360 C  C    . ALA   A 1 197 ? 16.98034  -0.08840  16.97658  1.000 60.28280  ? 1249 ALA   B C    1 
ATOM   1361 O  O    . ALA   A 1 197 ? 17.36438  0.73524   16.14524  1.000 59.52676  ? 1249 ALA   B O    1 
ATOM   1362 C  CB   . ALA   A 1 197 ? 15.30950  1.62304   17.75295  1.000 63.01503  ? 1249 ALA   B CB   1 
ATOM   1363 N  N    . GLN   A 1 198 ? 17.62426  -1.23336  17.19901  1.000 63.82591  ? 1250 GLN   B N    1 
ATOM   1364 C  CA   . GLN   A 1 198 ? 18.90122  -1.55271  16.57510  1.000 65.72850  ? 1250 GLN   B CA   1 
ATOM   1365 C  C    . GLN   A 1 198 ? 18.78509  -2.88099  15.84363  1.000 60.82453  ? 1250 GLN   B C    1 
ATOM   1366 O  O    . GLN   A 1 198 ? 18.40403  -3.89172  16.44404  1.000 58.57161  ? 1250 GLN   B O    1 
ATOM   1367 C  CB   . GLN   A 1 198 ? 20.01824  -1.61438  17.61909  1.000 66.83267  ? 1250 GLN   B CB   1 
ATOM   1368 C  CG   . GLN   A 1 198 ? 20.25837  -0.30111  18.34256  1.000 68.58294  ? 1250 GLN   B CG   1 
ATOM   1369 C  CD   . GLN   A 1 198 ? 20.89142  0.74648   17.44813  1.000 68.55651  ? 1250 GLN   B CD   1 
ATOM   1370 O  OE1  . GLN   A 1 198 ? 20.31250  1.80543   17.20373  1.000 76.71170  ? 1250 GLN   B OE1  1 
ATOM   1371 N  NE2  . GLN   A 1 198 ? 22.09338  0.45620   16.96021  1.000 71.82319  ? 1250 GLN   B NE2  1 
ATOM   1372 N  N    . ALA   A 1 199 ? 19.11305  -2.87853  14.55362  1.000 57.11259  ? 1251 ALA   B N    1 
ATOM   1373 C  CA   . ALA   A 1 199 ? 19.16194  -4.11883  13.79411  1.000 59.37594  ? 1251 ALA   B CA   1 
ATOM   1374 C  C    . ALA   A 1 199 ? 20.24388  -5.02969  14.35644  1.000 59.60124  ? 1251 ALA   B C    1 
ATOM   1375 O  O    . ALA   A 1 199 ? 21.38492  -4.60370  14.55823  1.000 64.68106  ? 1251 ALA   B O    1 
ATOM   1376 C  CB   . ALA   A 1 199 ? 19.42091  -3.82944  12.31699  1.000 49.66720  ? 1251 ALA   B CB   1 
ATOM   1377 N  N    . ILE   A 1 200 ? 19.88379  -6.28556  14.61694  1.000 52.52432  ? 1252 ILE   B N    1 
ATOM   1378 C  CA   . ILE   A 1 200 ? 20.81874  -7.23240  15.21329  1.000 53.89494  ? 1252 ILE   B CA   1 
ATOM   1379 C  C    . ILE   A 1 200 ? 21.37863  -8.23684  14.20867  1.000 58.16494  ? 1252 ILE   B C    1 
ATOM   1380 O  O    . ILE   A 1 200 ? 22.41459  -8.86081  14.49189  1.000 57.79165  ? 1252 ILE   B O    1 
ATOM   1381 C  CB   . ILE   A 1 200 ? 20.17271  -7.97588  16.40060  1.000 58.89363  ? 1252 ILE   B CB   1 
ATOM   1382 C  CG1  . ILE   A 1 200 ? 18.71668  -8.32389  16.08779  1.000 57.81093  ? 1252 ILE   B CG1  1 
ATOM   1383 C  CG2  . ILE   A 1 200 ? 20.28181  -7.14838  17.67427  1.000 60.34611  ? 1252 ILE   B CG2  1 
ATOM   1384 C  CD1  . ILE   A 1 200 ? 17.98066  -8.96737  17.24706  1.000 56.30884  ? 1252 ILE   B CD1  1 
ATOM   1385 N  N    . HIS   A 1 201 ? 20.74458  -8.40625  13.04976  1.000 54.08559  ? 1253 HIS   B N    1 
ATOM   1386 C  CA   . HIS   A 1 201 ? 21.22548  -9.38567  12.08813  1.000 48.03282  ? 1253 HIS   B CA   1 
ATOM   1387 C  C    . HIS   A 1 201 ? 20.48445  -9.21513  10.77009  1.000 46.09942  ? 1253 HIS   B C    1 
ATOM   1388 O  O    . HIS   A 1 201 ? 19.26647  -9.02804  10.75505  1.000 49.11550  ? 1253 HIS   B O    1 
ATOM   1389 C  CB   . HIS   A 1 201 ? 21.03938  -10.81344 12.62070  1.000 53.81791  ? 1253 HIS   B CB   1 
ATOM   1390 C  CG   . HIS   A 1 201 ? 21.44527  -11.88086 11.65111  1.000 54.88664  ? 1253 HIS   B CG   1 
ATOM   1391 N  ND1  . HIS   A 1 201 ? 20.56718  -12.83298 11.17952  1.000 56.53751  ? 1253 HIS   B ND1  1 
ATOM   1392 C  CD2  . HIS   A 1 201 ? 22.63523  -12.14518 11.06318  1.000 56.50118  ? 1253 HIS   B CD2  1 
ATOM   1393 C  CE1  . HIS   A 1 201 ? 21.19809  -13.63835 10.34382  1.000 48.34528  ? 1253 HIS   B CE1  1 
ATOM   1394 N  NE2  . HIS   A 1 201 ? 22.45312  -13.24249 10.25462  1.000 54.43654  ? 1253 HIS   B NE2  1 
ATOM   1395 N  N    . LYS   A 1 202 ? 21.22141  -9.29562  9.66910   1.000 48.26157  ? 1254 LYS   B N    1 
ATOM   1396 C  CA   . LYS   A 1 202 ? 20.63637  -9.27411  8.33410   1.000 42.60795  ? 1254 LYS   B CA   1 
ATOM   1397 C  C    . LYS   A 1 202 ? 20.65825  -10.68234 7.75966   1.000 50.86844  ? 1254 LYS   B C    1 
ATOM   1398 O  O    . LYS   A 1 202 ? 21.72820  -11.28947 7.63187   1.000 46.23674  ? 1254 LYS   B O    1 
ATOM   1399 C  CB   . LYS   A 1 202 ? 21.38742  -8.31753  7.40770   1.000 42.80665  ? 1254 LYS   B CB   1 
ATOM   1400 C  CG   . LYS   A 1 202 ? 21.09536  -8.58209  5.93982   1.000 43.19514  ? 1254 LYS   B CG   1 
ATOM   1401 C  CD   . LYS   A 1 202 ? 21.74441  -7.56650  5.02140   1.000 54.47865  ? 1254 LYS   B CD   1 
ATOM   1402 C  CE   . LYS   A 1 202 ? 21.55534  -7.97306  3.56656   1.000 46.30145  ? 1254 LYS   B CE   1 
ATOM   1403 N  NZ   . LYS   A 1 202 ? 21.87739  -6.86546  2.62511   1.000 65.56187  ? 1254 LYS   B NZ   1 
ATOM   1404 N  N    . PHE   A 1 203 ? 19.48220  -11.19838 7.41690   1.000 49.20205  ? 1255 PHE   B N    1 
ATOM   1405 C  CA   . PHE   A 1 203 ? 19.39208  -12.46965 6.71141   1.000 33.68551  ? 1255 PHE   B CA   1 
ATOM   1406 C  C    . PHE   A 1 203 ? 19.63205  -12.23726 5.22531   1.000 44.10340  ? 1255 PHE   B C    1 
ATOM   1407 O  O    . PHE   A 1 203 ? 19.06911  -11.30945 4.63496   1.000 43.33529  ? 1255 PHE   B O    1 
ATOM   1408 C  CB   . PHE   A 1 203 ? 18.02804  -13.11745 6.94270   1.000 43.49557  ? 1255 PHE   B CB   1 
ATOM   1409 C  CG   . PHE   A 1 203 ? 17.79404  -13.54687 8.36388   1.000 35.21726  ? 1255 PHE   B CG   1 
ATOM   1410 C  CD1  . PHE   A 1 203 ? 18.26896  -14.76573 8.82135   1.000 39.16575  ? 1255 PHE   B CD1  1 
ATOM   1411 C  CD2  . PHE   A 1 203 ? 17.09813  -12.73447 9.24358   1.000 45.62073  ? 1255 PHE   B CD2  1 
ATOM   1412 C  CE1  . PHE   A 1 203 ? 18.05397  -15.16420 10.12851  1.000 39.66179  ? 1255 PHE   B CE1  1 
ATOM   1413 C  CE2  . PHE   A 1 203 ? 16.88014  -13.12694 10.55174  1.000 43.43722  ? 1255 PHE   B CE2  1 
ATOM   1414 C  CZ   . PHE   A 1 203 ? 17.35906  -14.34480 10.99421  1.000 42.53553  ? 1255 PHE   B CZ   1 
ATOM   1415 N  N    . ASP   A 1 204 ? 20.47097  -13.07556 4.62361   1.000 39.62511  ? 1256 ASP   B N    1 
ATOM   1416 C  CA   . ASP   A 1 204 ? 20.85294  -12.87914 3.23452   1.000 42.59332  ? 1256 ASP   B CA   1 
ATOM   1417 C  C    . ASP   A 1 204 ? 19.64091  -12.99041 2.31360   1.000 42.38847  ? 1256 ASP   B C    1 
ATOM   1418 O  O    . ASP   A 1 204 ? 18.64187  -13.63821 2.63289   1.000 43.86948  ? 1256 ASP   B O    1 
ATOM   1419 C  CB   . ASP   A 1 204 ? 21.92585  -13.89238 2.83089   1.000 40.32756  ? 1256 ASP   B CB   1 
ATOM   1420 C  CG   . ASP   A 1 204 ? 23.26189  -13.62022 3.49975   1.000 47.63908  ? 1256 ASP   B CG   1 
ATOM   1421 O  OD1  . ASP   A 1 204 ? 23.42500  -12.52301 4.07431   1.000 48.67241  ? 1256 ASP   B OD1  1 
ATOM   1422 O  OD2  . ASP   A 1 204 ? 24.14482  -14.50331 3.45907   1.000 51.39849  ? 1256 ASP   B OD2  1 
ATOM   1423 N  N    . LYS   A 1 205 ? 19.74592  -12.34388 1.15634   1.000 41.15343  ? 1257 LYS   B N    1 
ATOM   1424 C  CA   . LYS   A 1 205 ? 18.63791  -12.23617 0.21333   1.000 39.93820  ? 1257 LYS   B CA   1 
ATOM   1425 C  C    . LYS   A 1 205 ? 18.72279  -13.38057 -0.79321  1.000 44.61408  ? 1257 LYS   B C    1 
ATOM   1426 O  O    . LYS   A 1 205 ? 19.66176  -13.44596 -1.59222  1.000 42.69376  ? 1257 LYS   B O    1 
ATOM   1427 C  CB   . LYS   A 1 205 ? 18.67199  -10.88045 -0.48920  1.000 39.77033  ? 1257 LYS   B CB   1 
ATOM   1428 C  CG   . LYS   A 1 205 ? 17.54098  -10.65375 -1.47826  1.000 44.57147  ? 1257 LYS   B CG   1 
ATOM   1429 C  CD   . LYS   A 1 205 ? 17.57607  -9.23497  -2.02882  1.000 44.57369  ? 1257 LYS   B CD   1 
ATOM   1430 C  CE   . LYS   A 1 205 ? 16.45406  -9.00128  -3.02188  1.000 40.84553  ? 1257 LYS   B CE   1 
ATOM   1431 N  NZ   . LYS   A 1 205 ? 16.49515  -7.62951  -3.59843  1.000 44.62203  ? 1257 LYS   B NZ   1 
ATOM   1432 N  N    . PHE   A 1 206 ? 17.73172  -14.27348 -0.76183  1.000 41.06479  ? 1258 PHE   B N    1 
ATOM   1433 C  CA   . PHE   A 1 206 ? 17.68260  -15.41484 -1.66838  1.000 38.52240  ? 1258 PHE   B CA   1 
ATOM   1434 C  C    . PHE   A 1 206 ? 16.42658  -15.42208 -2.53034  1.000 43.66106  ? 1258 PHE   B C    1 
ATOM   1435 O  O    . PHE   A 1 206 ? 16.12448  -16.44331 -3.16393  1.000 44.80540  ? 1258 PHE   B O    1 
ATOM   1436 C  CB   . PHE   A 1 206 ? 17.79352  -16.72653 -0.88386  1.000 39.83303  ? 1258 PHE   B CB   1 
ATOM   1437 C  CG   . PHE   A 1 206 ? 19.06654  -16.84732 -0.09585  1.000 38.25681  ? 1258 PHE   B CG   1 
ATOM   1438 C  CD1  . PHE   A 1 206 ? 20.27850  -17.04667 -0.73781  1.000 49.74313  ? 1258 PHE   B CD1  1 
ATOM   1439 C  CD2  . PHE   A 1 206 ? 19.05359  -16.76177 1.28611   1.000 34.74614  ? 1258 PHE   B CD2  1 
ATOM   1440 C  CE1  . PHE   A 1 206 ? 21.45352  -17.15548 -0.02080  1.000 44.04624  ? 1258 PHE   B CE1  1 
ATOM   1441 C  CE2  . PHE   A 1 206 ? 20.22360  -16.87258 2.01312   1.000 39.83997  ? 1258 PHE   B CE2  1 
ATOM   1442 C  CZ   . PHE   A 1 206 ? 21.42656  -17.06893 1.35817   1.000 40.46912  ? 1258 PHE   B CZ   1 
ATOM   1443 N  N    . ASN   A 1 207 ? 15.68066  -14.32103 -2.56275  1.000 41.52297  ? 1259 ASN   B N    1 
ATOM   1444 C  CA   . ASN   A 1 207 ? 14.56065  -14.16731 -3.47978  1.000 32.76671  ? 1259 ASN   B CA   1 
ATOM   1445 C  C    . ASN   A 1 207 ? 14.24776  -12.68132 -3.56836  1.000 33.05063  ? 1259 ASN   B C    1 
ATOM   1446 O  O    . ASN   A 1 207 ? 14.76085  -11.87305 -2.79069  1.000 36.60149  ? 1259 ASN   B O    1 
ATOM   1447 C  CB   . ASN   A 1 207 ? 13.34460  -14.98504 -3.03242  1.000 31.99946  ? 1259 ASN   B CB   1 
ATOM   1448 C  CG   . ASN   A 1 207 ? 12.45168  -14.23459 -2.07069  1.000 37.35927  ? 1259 ASN   B CG   1 
ATOM   1449 O  OD1  . ASN   A 1 207 ? 12.78873  -14.05315 -0.90077  1.000 38.84791  ? 1259 ASN   B OD1  1 
ATOM   1450 N  ND2  . ASN   A 1 207 ? 11.29570  -13.80369 -2.55583  1.000 31.85298  ? 1259 ASN   B ND2  1 
ATOM   1451 N  N    . MET   A 1 208 ? 13.39776  -12.32564 -4.52848  1.000 36.76921  ? 1260 MET   B N    1 
ATOM   1452 C  CA   . MET   A 1 208 ? 13.16586  -10.92174 -4.84302  1.000 38.15943  ? 1260 MET   B CA   1 
ATOM   1453 C  C    . MET   A 1 208 ? 12.00193  -10.29735 -4.08724  1.000 41.83349  ? 1260 MET   B C    1 
ATOM   1454 O  O    . MET   A 1 208 ? 11.93003  -9.06631  -4.00572  1.000 36.59134  ? 1260 MET   B O    1 
ATOM   1455 C  CB   . MET   A 1 208 ? 12.92183  -10.75432 -6.34708  1.000 41.66735  ? 1260 MET   B CB   1 
ATOM   1456 C  CG   . MET   A 1 208 ? 14.11677  -11.10876 -7.22398  1.000 43.30396  ? 1260 MET   B CG   1 
ATOM   1457 S  SD   . MET   A 1 208 ? 15.55286  -10.06574 -6.90543  1.000 56.72791  ? 1260 MET   B SD   1 
ATOM   1458 C  CE   . MET   A 1 208 ? 14.91198  -8.44886  -7.33605  1.000 49.11492  ? 1260 MET   B CE   1 
ATOM   1459 N  N    . ASN   A 1 209 ? 11.09388  -11.09606 -3.52989  1.000 35.86943  ? 1261 ASN   B N    1 
ATOM   1460 C  CA   . ASN   A 1 209 ? 9.80094   -10.57579 -3.10106  1.000 36.10721  ? 1261 ASN   B CA   1 
ATOM   1461 C  C    . ASN   A 1 209 ? 9.50996   -10.78818 -1.62397  1.000 36.55724  ? 1261 ASN   B C    1 
ATOM   1462 O  O    . ASN   A 1 209 ? 9.14006   -9.83288  -0.93034  1.000 33.03799  ? 1261 ASN   B O    1 
ATOM   1463 C  CB   . ASN   A 1 209 ? 8.69186   -11.21104 -3.95478  1.000 37.10525  ? 1261 ASN   B CB   1 
ATOM   1464 C  CG   . ASN   A 1 209 ? 8.88484   -10.95965 -5.44088  1.000 41.66954  ? 1261 ASN   B CG   1 
ATOM   1465 O  OD1  . ASN   A 1 209 ? 9.08191   -9.82283  -5.86734  1.000 50.74170  ? 1261 ASN   B OD1  1 
ATOM   1466 N  ND2  . ASN   A 1 209 ? 8.84273   -12.02696 -6.23146  1.000 38.15913  ? 1261 ASN   B ND2  1 
ATOM   1467 N  N    . ILE   A 1 210 ? 9.65188   -12.01499 -1.11849  1.000 33.54688  ? 1262 ILE   B N    1 
ATOM   1468 C  CA   . ILE   A 1 210 ? 9.17990   -12.37043 0.21867   1.000 33.78347  ? 1262 ILE   B CA   1 
ATOM   1469 C  C    . ILE   A 1 210 ? 10.23895  -12.00510 1.25249   1.000 38.04668  ? 1262 ILE   B C    1 
ATOM   1470 O  O    . ILE   A 1 210 ? 11.41792  -12.35125 1.10159   1.000 35.84076  ? 1262 ILE   B O    1 
ATOM   1471 C  CB   . ILE   A 1 210 ? 8.82778   -13.86537 0.29127   1.000 36.74729  ? 1262 ILE   B CB   1 
ATOM   1472 C  CG1  . ILE   A 1 210 ? 7.62373   -14.17163 -0.60457  1.000 38.09466  ? 1262 ILE   B CG1  1 
ATOM   1473 C  CG2  . ILE   A 1 210 ? 8.55279   -14.28478 1.72544   1.000 32.14653  ? 1262 ILE   B CG2  1 
ATOM   1474 C  CD1  . ILE   A 1 210 ? 6.38680   -13.36440 -0.25986  1.000 30.08439  ? 1262 ILE   B CD1  1 
ATOM   1475 N  N    . SER   A 1 211 ? 9.81304   -11.31965 2.31523   1.000 37.85587  ? 1263 SER   B N    1 
ATOM   1476 C  CA   . SER   A 1 211 ? 10.71911  -10.84831 3.35302   1.000 42.83663  ? 1263 SER   B CA   1 
ATOM   1477 C  C    . SER   A 1 211 ? 10.69408  -11.69580 4.62036   1.000 34.82783  ? 1263 SER   B C    1 
ATOM   1478 O  O    . SER   A 1 211 ? 11.56812  -11.51953 5.47626   1.000 40.02584  ? 1263 SER   B O    1 
ATOM   1479 C  CB   . SER   A 1 211 ? 10.40123  -9.38914  3.70545   1.000 35.77409  ? 1263 SER   B CB   1 
ATOM   1480 O  OG   . SER   A 1 211 ? 9.08325   -9.25284  4.21044   1.000 43.31720  ? 1263 SER   B OG   1 
ATOM   1481 N  N    . GLY   A 1 212 ? 9.72301   -12.58967 4.77574   1.000 35.81398  ? 1264 GLY   B N    1 
ATOM   1482 C  CA   . GLY   A 1 212 ? 9.73097   -13.55024 5.86012   1.000 32.17053  ? 1264 GLY   B CA   1 
ATOM   1483 C  C    . GLY   A 1 212 ? 8.83904   -13.14171 7.02298   1.000 40.44870  ? 1264 GLY   B C    1 
ATOM   1484 O  O    . GLY   A 1 212 ? 8.39613   -11.99862 7.15254   1.000 41.17426  ? 1264 GLY   B O    1 
ATOM   1485 N  N    . VAL   A 1 213 ? 8.58598   -14.12334 7.89438   1.000 39.30036  ? 1265 VAL   B N    1 
ATOM   1486 C  CA   . VAL   A 1 213 ? 7.72903   -13.95582 9.06134   1.000 37.35969  ? 1265 VAL   B CA   1 
ATOM   1487 C  C    . VAL   A 1 213 ? 8.31400   -14.75140 10.22164  1.000 39.56276  ? 1265 VAL   B C    1 
ATOM   1488 O  O    . VAL   A 1 213 ? 9.24394   -15.54354 10.05992  1.000 39.30305  ? 1265 VAL   B O    1 
ATOM   1489 C  CB   . VAL   A 1 213 ? 6.27899   -14.40681 8.78756   1.000 31.98575  ? 1265 VAL   B CB   1 
ATOM   1490 C  CG1  . VAL   A 1 213 ? 5.68402   -13.62522 7.63327   1.000 40.30508  ? 1265 VAL   B CG1  1 
ATOM   1491 C  CG2  . VAL   A 1 213 ? 6.23186   -15.90292 8.50815   1.000 36.72401  ? 1265 VAL   B CG2  1 
ATOM   1492 N  N    . PHE   A 1 214 ? 7.74706   -14.53189 11.40657  1.000 41.54405  ? 1266 PHE   B N    1 
ATOM   1493 C  CA   . PHE   A 1 214 ? 8.12403   -15.27545 12.60185  1.000 42.32952  ? 1266 PHE   B CA   1 
ATOM   1494 C  C    . PHE   A 1 214 ? 7.23994   -16.50732 12.75036  1.000 41.67667  ? 1266 PHE   B C    1 
ATOM   1495 O  O    . PHE   A 1 214 ? 6.01694   -16.42428 12.60437  1.000 44.25364  ? 1266 PHE   B O    1 
ATOM   1496 C  CB   . PHE   A 1 214 ? 8.00114   -14.40794 13.85551  1.000 44.96627  ? 1266 PHE   B CB   1 
ATOM   1497 C  CG   . PHE   A 1 214 ? 9.04423   -13.33598 13.96805  1.000 40.69971  ? 1266 PHE   B CG   1 
ATOM   1498 C  CD1  . PHE   A 1 214 ? 10.34121  -13.64893 14.33514  1.000 42.38888  ? 1266 PHE   B CD1  1 
ATOM   1499 C  CD2  . PHE   A 1 214 ? 8.72332   -12.01105 13.72754  1.000 42.66750  ? 1266 PHE   B CD2  1 
ATOM   1500 C  CE1  . PHE   A 1 214 ? 11.30429  -12.66296 14.44472  1.000 43.00035  ? 1266 PHE   B CE1  1 
ATOM   1501 C  CE2  . PHE   A 1 214 ? 9.68140   -11.01808 13.83812  1.000 45.27475  ? 1266 PHE   B CE2  1 
ATOM   1502 C  CZ   . PHE   A 1 214 ? 10.97339  -11.34604 14.19721  1.000 41.46869  ? 1266 PHE   B CZ   1 
ATOM   1503 N  N    . HIS   A 1 215 ? 7.86186   -17.64325 13.03879  1.000 36.89878  ? 1267 HIS   B N    1 
ATOM   1504 C  CA   . HIS   A 1 215 ? 7.10278   -18.81603 13.44328  1.000 43.40879  ? 1267 HIS   B CA   1 
ATOM   1505 C  C    . HIS   A 1 215 ? 6.45784   -18.55744 14.80420  1.000 49.07404  ? 1267 HIS   B C    1 
ATOM   1506 O  O    . HIS   A 1 215 ? 7.08992   -17.96815 15.68595  1.000 42.97674  ? 1267 HIS   B O    1 
ATOM   1507 C  CB   . HIS   A 1 215 ? 8.01369   -20.04208 13.51274  1.000 41.97395  ? 1267 HIS   B CB   1 
ATOM   1508 C  CG   . HIS   A 1 215 ? 7.28660   -21.33394 13.72427  1.000 43.43714  ? 1267 HIS   B CG   1 
ATOM   1509 N  ND1  . HIS   A 1 215 ? 6.53561   -21.59043 14.85140  1.000 42.32223  ? 1267 HIS   B ND1  1 
ATOM   1510 C  CD2  . HIS   A 1 215 ? 7.21349   -22.45023 12.96272  1.000 38.80800  ? 1267 HIS   B CD2  1 
ATOM   1511 C  CE1  . HIS   A 1 215 ? 6.02351   -22.80542 14.77089  1.000 42.01938  ? 1267 HIS   B CE1  1 
ATOM   1512 N  NE2  . HIS   A 1 215 ? 6.42044   -23.34991 13.63409  1.000 42.95227  ? 1267 HIS   B NE2  1 
ATOM   1513 N  N    . PRO   A 1 216 ? 5.20582   -18.97127 15.00240  1.000 48.10534  ? 1268 PRO   B N    1 
ATOM   1514 C  CA   . PRO   A 1 216 ? 4.55088   -18.71771 16.29632  1.000 48.45826  ? 1268 PRO   B CA   1 
ATOM   1515 C  C    . PRO   A 1 216 ? 5.31287   -19.27930 17.48452  1.000 43.45754  ? 1268 PRO   B C    1 
ATOM   1516 O  O    . PRO   A 1 216 ? 5.10194   -18.80683 18.60734  1.000 51.56380  ? 1268 PRO   B O    1 
ATOM   1517 C  CB   . PRO   A 1 216 ? 3.17682   -19.38766 16.13962  1.000 45.18813  ? 1268 PRO   B CB   1 
ATOM   1518 C  CG   . PRO   A 1 216 ? 3.32971   -20.33913 14.98399  1.000 51.73074  ? 1268 PRO   B CG   1 
ATOM   1519 C  CD   . PRO   A 1 216 ? 4.32373   -19.69057 14.06671  1.000 46.35757  ? 1268 PRO   B CD   1 
ATOM   1520 N  N    . ASN   A 1 217 ? 6.19478   -20.26144 17.28088  1.000 51.59824  ? 1269 ASN   B N    1 
ATOM   1521 C  CA   . ASN   A 1 217 ? 6.96077   -20.80906 18.39207  1.000 44.13176  ? 1269 ASN   B CA   1 
ATOM   1522 C  C    . ASN   A 1 217 ? 8.04286   -19.85795 18.88467  1.000 45.80638  ? 1269 ASN   B C    1 
ATOM   1523 O  O    . ASN   A 1 217 ? 8.67887   -20.14560 19.90376  1.000 52.61041  ? 1269 ASN   B O    1 
ATOM   1524 C  CB   . ASN   A 1 217 ? 7.58766   -22.15427 17.99659  1.000 50.68907  ? 1269 ASN   B CB   1 
ATOM   1525 C  CG   . ASN   A 1 217 ? 8.62164   -22.02779 16.88351  1.000 48.41435  ? 1269 ASN   B CG   1 
ATOM   1526 O  OD1  . ASN   A 1 217 ? 9.14571   -20.94694 16.61606  1.000 45.25834  ? 1269 ASN   B OD1  1 
ATOM   1527 N  ND2  . ASN   A 1 217 ? 8.91953   -23.14607 16.22994  1.000 45.83796  ? 1269 ASN   B ND2  1 
ATOM   1528 N  N    . GLY   A 1 218 ? 8.26293   -18.74024 18.19522  1.000 46.93451  ? 1270 GLY   B N    1 
ATOM   1529 C  CA   . GLY   A 1 218 ? 9.28501   -17.79017 18.57081  1.000 47.25934  ? 1270 GLY   B CA   1 
ATOM   1530 C  C    . GLY   A 1 218 ? 10.70597  -18.29333 18.46597  1.000 50.55157  ? 1270 GLY   B C    1 
ATOM   1531 O  O    . GLY   A 1 218 ? 11.62804  -17.57923 18.88066  1.000 48.51961  ? 1270 GLY   B O    1 
ATOM   1532 N  N    . LEU   A 1 219 ? 10.92086  -19.49156 17.92144  1.000 45.54126  ? 1271 LEU   B N    1 
ATOM   1533 C  CA   . LEU   A 1 219 ? 12.24982  -20.07669 17.84463  1.000 48.91056  ? 1271 LEU   B CA   1 
ATOM   1534 C  C    . LEU   A 1 219 ? 12.91379  -19.90828 16.48554  1.000 49.22830  ? 1271 LEU   B C    1 
ATOM   1535 O  O    . LEU   A 1 219 ? 14.13978  -20.03141 16.39655  1.000 55.33608  ? 1271 LEU   B O    1 
ATOM   1536 C  CB   . LEU   A 1 219 ? 12.18871  -21.57055 18.18422  1.000 52.61150  ? 1271 LEU   B CB   1 
ATOM   1537 C  CG   . LEU   A 1 219 ? 11.65372  -21.92596 19.57338  1.000 47.08621  ? 1271 LEU   B CG   1 
ATOM   1538 C  CD1  . LEU   A 1 219 ? 11.33561  -23.40990 19.66997  1.000 50.54680  ? 1271 LEU   B CD1  1 
ATOM   1539 C  CD2  . LEU   A 1 219 ? 12.65079  -21.51961 20.64819  1.000 55.28775  ? 1271 LEU   B CD2  1 
ATOM   1540 N  N    . GLU   A 1 220 ? 12.14778  -19.63164 15.43345  1.000 40.44555  ? 1272 GLU   B N    1 
ATOM   1541 C  CA   . GLU   A 1 220 ? 12.71974  -19.58721 14.09542  1.000 45.84987  ? 1272 GLU   B CA   1 
ATOM   1542 C  C    . GLU   A 1 220 ? 11.97880  -18.56449 13.24604  1.000 46.50747  ? 1272 GLU   B C    1 
ATOM   1543 O  O    . GLU   A 1 220 ? 10.89585  -18.08627 13.60088  1.000 42.11008  ? 1272 GLU   B O    1 
ATOM   1544 C  CB   . GLU   A 1 220 ? 12.69162  -20.97147 13.43897  1.000 44.09400  ? 1272 GLU   B CB   1 
ATOM   1545 C  CG   . GLU   A 1 220 ? 11.33456  -21.64836 13.45628  1.000 48.54613  ? 1272 GLU   B CG   1 
ATOM   1546 C  CD   . GLU   A 1 220 ? 11.44445  -23.15937 13.44487  1.000 50.01972  ? 1272 GLU   B CD   1 
ATOM   1547 O  OE1  . GLU   A 1 220 ? 12.26543  -23.69513 14.21806  1.000 63.80426  ? 1272 GLU   B OE1  1 
ATOM   1548 O  OE2  . GLU   A 1 220 ? 10.71837  -23.81062 12.66215  1.000 44.84177  ? 1272 GLU   B OE2  1 
ATOM   1549 N  N    . VAL   A 1 221 ? 12.63279  -18.23399 12.12489  1.000 38.92550  ? 1273 VAL   B N    1 
ATOM   1550 C  CA   . VAL   A 1 221 ? 12.05484  -17.27633 11.14352  1.000 39.62782  ? 1273 VAL   B CA   1 
ATOM   1551 C  C    . VAL   A 1 221 ? 11.88774  -17.99685 9.79981   1.000 48.92262  ? 1273 VAL   B C    1 
ATOM   1552 O  O    . VAL   A 1 221 ? 12.77367  -18.78406 9.42510   1.000 46.34039  ? 1273 VAL   B O    1 
ATOM   1553 C  CB   . VAL   A 1 221 ? 12.87593  -15.98746 10.97599  1.000 47.35870  ? 1273 VAL   B CB   1 
ATOM   1554 C  CG1  . VAL   A 1 221 ? 12.30997  -15.10085 9.87766   1.000 53.64177  ? 1273 VAL   B CG1  1 
ATOM   1555 C  CG2  . VAL   A 1 221 ? 13.00003  -15.20495 12.27268  1.000 48.71760  ? 1273 VAL   B CG2  1 
ATOM   1556 N  N    . ILE   A 1 222 ? 10.77474  -17.74503 9.12675   1.000 39.31317  ? 1274 ILE   B N    1 
ATOM   1557 C  CA   . ILE   A 1 222 ? 10.43465  -18.36651 7.85200   1.000 41.15998  ? 1274 ILE   B CA   1 
ATOM   1558 C  C    . ILE   A 1 222 ? 10.54371  -17.28694 6.78357   1.000 38.01123  ? 1274 ILE   B C    1 
ATOM   1559 O  O    . ILE   A 1 222 ? 9.67977   -16.40490 6.69425   1.000 37.92933  ? 1274 ILE   B O    1 
ATOM   1560 C  CB   . ILE   A 1 222 ? 9.03061   -18.98238 7.88129   1.000 40.30642  ? 1274 ILE   B CB   1 
ATOM   1561 C  CG1  . ILE   A 1 222 ? 8.90957   -19.95591 9.05668   1.000 43.53850  ? 1274 ILE   B CG1  1 
ATOM   1562 C  CG2  . ILE   A 1 222 ? 8.71351   -19.66988 6.56057   1.000 34.81260  ? 1274 ILE   B CG2  1 
ATOM   1563 C  CD1  . ILE   A 1 222 ? 7.55759   -19.92854 9.73971   1.000 41.11935  ? 1274 ILE   B CD1  1 
ATOM   1564 N  N    . ILE   A 1 223 ? 11.60268  -17.34034 5.98056   1.000 30.89991  ? 1275 ILE   B N    1 
ATOM   1565 C  CA   . ILE   A 1 223 ? 11.87673  -16.33376 4.96116   1.000 35.37743  ? 1275 ILE   B CA   1 
ATOM   1566 C  C    . ILE   A 1 223 ? 11.86763  -17.05829 3.62144   1.000 38.01805  ? 1275 ILE   B C    1 
ATOM   1567 O  O    . ILE   A 1 223 ? 12.85857  -17.69152 3.23466   1.000 38.82833  ? 1275 ILE   B O    1 
ATOM   1568 C  CB   . ILE   A 1 223 ? 13.20379  -15.61077 5.20283   1.000 33.17261  ? 1275 ILE   B CB   1 
ATOM   1569 C  CG1  . ILE   A 1 223 ? 13.24787  -15.06621 6.63361   1.000 34.23788  ? 1275 ILE   B CG1  1 
ATOM   1570 C  CG2  . ILE   A 1 223 ? 13.39185  -14.48518 4.19538   1.000 33.67446  ? 1275 ILE   B CG2  1 
ATOM   1571 C  CD1  . ILE   A 1 223 ? 14.48595  -14.25418 6.94026   1.000 35.26678  ? 1275 ILE   B CD1  1 
ATOM   1572 N  N    . ASN   A 1 224 ? 10.74762  -16.96249 2.90744   1.000 33.99812  ? 1276 ASN   B N    1 
ATOM   1573 C  CA   . ASN   A 1 224 ? 10.56952  -17.70696 1.66874   1.000 33.48614  ? 1276 ASN   B CA   1 
ATOM   1574 C  C    . ASN   A 1 224 ? 10.83842  -19.18889 1.91332   1.000 30.49507  ? 1276 ASN   B C    1 
ATOM   1575 O  O    . ASN   A 1 224 ? 10.16839  -19.81151 2.74258   1.000 35.32817  ? 1276 ASN   B O    1 
ATOM   1576 C  CB   . ASN   A 1 224 ? 11.48453  -17.16847 0.56750   1.000 30.26080  ? 1276 ASN   B CB   1 
ATOM   1577 C  CG   . ASN   A 1 224 ? 10.92347  -17.41198 -0.82239  1.000 39.03289  ? 1276 ASN   B CG   1 
ATOM   1578 O  OD1  . ASN   A 1 224 ? 9.71247   -17.33797 -1.03338  1.000 32.98634  ? 1276 ASN   B OD1  1 
ATOM   1579 N  ND2  . ASN   A 1 224 ? 11.80042  -17.71042 -1.77330  1.000 36.36527  ? 1276 ASN   B ND2  1 
ATOM   1580 N  N    . THR   A 1 225 ? 11.82435  -19.75224 1.22051   1.000 36.57323  ? 1277 THR   B N    1 
ATOM   1581 C  CA   . THR   A 1 225 ? 12.13224  -21.17222 1.33206   1.000 38.30131  ? 1277 THR   B CA   1 
ATOM   1582 C  C    . THR   A 1 225 ? 13.13725  -21.49086 2.43316   1.000 38.15935  ? 1277 THR   B C    1 
ATOM   1583 O  O    . THR   A 1 225 ? 13.43517  -22.66880 2.65662   1.000 37.54331  ? 1277 THR   B O    1 
ATOM   1584 C  CB   . THR   A 1 225 ? 12.65816  -21.70479 -0.00774  1.000 39.48281  ? 1277 THR   B CB   1 
ATOM   1585 O  OG1  . THR   A 1 225 ? 13.80121  -20.94004 -0.41708  1.000 37.35891  ? 1277 THR   B OG1  1 
ATOM   1586 C  CG2  . THR   A 1 225 ? 11.58514  -21.60913 -1.08275  1.000 33.38339  ? 1277 THR   B CG2  1 
ATOM   1587 N  N    . GLU   A 1 226 ? 13.66535  -20.48663 3.12675   1.000 35.31148  ? 1278 GLU   B N    1 
ATOM   1588 C  CA   . GLU   A 1 226 ? 14.67136  -20.69930 4.15680   1.000 36.99535  ? 1278 GLU   B CA   1 
ATOM   1589 C  C    . GLU   A 1 226 ? 14.03941  -20.61470 5.54079   1.000 39.99352  ? 1278 GLU   B C    1 
ATOM   1590 O  O    . GLU   A 1 226 ? 13.38350  -19.61952 5.87241   1.000 36.90210  ? 1278 GLU   B O    1 
ATOM   1591 C  CB   . GLU   A 1 226 ? 15.80644  -19.67743 4.03436   1.000 43.72631  ? 1278 GLU   B CB   1 
ATOM   1592 C  CG   . GLU   A 1 226 ? 16.78638  -19.96896 2.90445   1.000 30.13027  ? 1278 GLU   B CG   1 
ATOM   1593 C  CD   . GLU   A 1 226 ? 16.12634  -19.95445 1.53946   1.000 38.07711  ? 1278 GLU   B CD   1 
ATOM   1594 O  OE1  . GLU   A 1 226 ? 15.70842  -18.86559 1.09205   1.000 36.56767  ? 1278 GLU   B OE1  1 
ATOM   1595 O  OE2  . GLU   A 1 226 ? 16.01224  -21.03268 0.92289   1.000 40.96447  ? 1278 GLU   B OE2  1 
ATOM   1596 N  N    . ILE   A 1 227 ? 14.24135  -21.65140 6.34819   1.000 38.07434  ? 1279 ILE   B N    1 
ATOM   1597 C  CA   . ILE   A 1 227 ? 13.80239  -21.66681 7.73421   1.000 42.35764  ? 1279 ILE   B CA   1 
ATOM   1598 C  C    . ILE   A 1 227 ? 15.05143  -21.53957 8.59312   1.000 40.06820  ? 1279 ILE   B C    1 
ATOM   1599 O  O    . ILE   A 1 227 ? 15.83936  -22.49360 8.68348   1.000 41.40811  ? 1279 ILE   B O    1 
ATOM   1600 C  CB   . ILE   A 1 227 ? 13.01631  -22.93862 8.07874   1.000 34.80460  ? 1279 ILE   B CB   1 
ATOM   1601 C  CG1  . ILE   A 1 227 ? 11.83926  -23.11291 7.11484   1.000 35.87276  ? 1279 ILE   B CG1  1 
ATOM   1602 C  CG2  . ILE   A 1 227 ? 12.53135  -22.88901 9.51873   1.000 41.90998  ? 1279 ILE   B CG2  1 
ATOM   1603 C  CD1  . ILE   A 1 227 ? 10.87335  -21.95883 7.12741   1.000 45.88662  ? 1279 ILE   B CD1  1 
ATOM   1604 N  N    . TRP   A 1 228 ? 15.22254  -20.36334 9.20465   1.000 39.96681  ? 1280 TRP   B N    1 
ATOM   1605 C  CA   . TRP   A 1 228 ? 16.38759  -20.02411 10.01448  1.000 42.34850  ? 1280 TRP   B CA   1 
ATOM   1606 C  C    . TRP   A 1 228 ? 16.08462  -20.19250 11.49756  1.000 42.84390  ? 1280 TRP   B C    1 
ATOM   1607 O  O    . TRP   A 1 228 ? 14.97566  -19.90123 11.95548  1.000 42.54952  ? 1280 TRP   B O    1 
ATOM   1608 C  CB   . TRP   A 1 228 ? 16.83269  -18.57624 9.78290   1.000 34.27638  ? 1280 TRP   B CB   1 
ATOM   1609 C  CG   . TRP   A 1 228 ? 17.14268  -18.19582 8.37574   1.000 40.07914  ? 1280 TRP   B CG   1 
ATOM   1610 C  CD1  . TRP   A 1 228 ? 16.35671  -17.46809 7.53347   1.000 40.91319  ? 1280 TRP   B CD1  1 
ATOM   1611 C  CD2  . TRP   A 1 228 ? 18.34564  -18.48220 7.65182   1.000 37.30819  ? 1280 TRP   B CD2  1 
ATOM   1612 N  NE1  . TRP   A 1 228 ? 16.98569  -17.29862 6.32439   1.000 43.77817  ? 1280 TRP   B NE1  1 
ATOM   1613 C  CE2  . TRP   A 1 228 ? 18.20765  -17.91470 6.37060   1.000 40.74834  ? 1280 TRP   B CE2  1 
ATOM   1614 C  CE3  . TRP   A 1 228 ? 19.51859  -19.17917 7.95906   1.000 36.71239  ? 1280 TRP   B CE3  1 
ATOM   1615 C  CZ2  . TRP   A 1 228 ? 19.20061  -18.01816 5.39961   1.000 43.78594  ? 1280 TRP   B CZ2  1 
ATOM   1616 C  CZ3  . TRP   A 1 228 ? 20.50156  -19.28063 6.99407   1.000 43.24608  ? 1280 TRP   B CZ3  1 
ATOM   1617 C  CH2  . TRP   A 1 228 ? 20.33957  -18.70212 5.72884   1.000 38.47294  ? 1280 TRP   B CH2  1 
ATOM   1618 N  N    . ASP   A 1 229 ? 17.09161  -20.62728 12.25070  1.000 45.53973  ? 1281 ASP   B N    1 
ATOM   1619 C  CA   . ASP   A 1 229 ? 16.99765  -20.65470 13.70372  1.000 45.15915  ? 1281 ASP   B CA   1 
ATOM   1620 C  C    . ASP   A 1 229 ? 17.30377  -19.27050 14.26116  1.000 44.32809  ? 1281 ASP   B C    1 
ATOM   1621 O  O    . ASP   A 1 229 ? 18.28181  -18.63274 13.85888  1.000 41.94090  ? 1281 ASP   B O    1 
ATOM   1622 C  CB   . ASP   A 1 229 ? 17.96559  -21.68855 14.28210  1.000 49.89424  ? 1281 ASP   B CB   1 
ATOM   1623 C  CG   . ASP   A 1 229 ? 17.93763  -21.73194 15.80012  1.000 49.64725  ? 1281 ASP   B CG   1 
ATOM   1624 O  OD1  . ASP   A 1 229 ? 16.95160  -22.24464 16.36535  1.000 60.04853  ? 1281 ASP   B OD1  1 
ATOM   1625 O  OD2  . ASP   A 1 229 ? 18.90468  -21.25177 16.42590  1.000 56.31714  ? 1281 ASP   B OD2  1 
ATOM   1626 N  N    . LEU   A 1 230 ? 16.46184  -18.80207 15.18700  1.000 45.02547  ? 1282 LEU   B N    1 
ATOM   1627 C  CA   . LEU   A 1 230 ? 16.66096  -17.47586 15.76147  1.000 47.93660  ? 1282 LEU   B CA   1 
ATOM   1628 C  C    . LEU   A 1 230 ? 17.90799  -17.42361 16.63741  1.000 47.25014  ? 1282 LEU   B C    1 
ATOM   1629 O  O    . LEU   A 1 230 ? 18.66406  -16.44668 16.59500  1.000 46.75880  ? 1282 LEU   B O    1 
ATOM   1630 C  CB   . LEU   A 1 230 ? 15.42701  -17.05345 16.56234  1.000 46.34537  ? 1282 LEU   B CB   1 
ATOM   1631 C  CG   . LEU   A 1 230 ? 14.44707  -16.10564 15.86699  1.000 55.23847  ? 1282 LEU   B CG   1 
ATOM   1632 C  CD1  . LEU   A 1 230 ? 13.23611  -15.85120 16.75093  1.000 53.13787  ? 1282 LEU   B CD1  1 
ATOM   1633 C  CD2  . LEU   A 1 230 ? 15.13216  -14.79884 15.50545  1.000 46.47039  ? 1282 LEU   B CD2  1 
ATOM   1634 N  N    . ARG   A 1 231 ? 18.14293  -18.46731 17.43282  1.000 50.54461  ? 1283 ARG   B N    1 
ATOM   1635 C  CA   . ARG   A 1 231 ? 19.26896  -18.44803 18.36078  1.000 55.52397  ? 1283 ARG   B CA   1 
ATOM   1636 C  C    . ARG   A 1 231 ? 20.59694  -18.40143 17.61572  1.000 52.34067  ? 1283 ARG   B C    1 
ATOM   1637 O  O    . ARG   A 1 231 ? 21.43201  -17.52340 17.86035  1.000 54.42413  ? 1283 ARG   B O    1 
ATOM   1638 C  CB   . ARG   A 1 231 ? 19.21489  -19.67166 19.28126  1.000 60.87261  ? 1283 ARG   B CB   1 
ATOM   1639 C  CG   . ARG   A 1 231 ? 19.73895  -19.40915 20.68414  1.000 61.28843  ? 1283 ARG   B CG   1 
ATOM   1640 C  CD   . ARG   A 1 231 ? 19.97087  -20.69486 21.47365  1.000 59.47866  ? 1283 ARG   B CD   1 
ATOM   1641 N  NE   . ARG   A 1 231 ? 21.32983  -21.20002 21.31581  1.000 74.27787  ? 1283 ARG   B NE   1 
ATOM   1642 C  CZ   . ARG   A 1 231 ? 21.64272  -22.36626 20.76626  1.000 59.99762  ? 1283 ARG   B CZ   1 
ATOM   1643 N  NH1  . ARG   A 1 231 ? 20.71165  -23.20336 20.34062  1.000 70.11155  ? 1283 ARG   B NH1  1 
ATOM   1644 N  NH2  . ARG   A 1 231 ? 22.92469  -22.70641 20.65135  1.000 62.76524  ? 1283 ARG   B NH2  1 
ATOM   1645 N  N    . THR   A 1 232 ? 20.80584  -19.33281 16.68708  1.000 47.48873  ? 1284 THR   B N    1 
ATOM   1646 C  CA   . THR   A 1 232 ? 22.10480  -19.54716 16.06813  1.000 48.27620  ? 1284 THR   B CA   1 
ATOM   1647 C  C    . THR   A 1 232 ? 22.18580  -19.05874 14.62793  1.000 51.01820  ? 1284 THR   B C    1 
ATOM   1648 O  O    . THR   A 1 232 ? 23.26678  -19.11406 14.03092  1.000 50.01734  ? 1284 THR   B O    1 
ATOM   1649 C  CB   . THR   A 1 232 ? 22.46369  -21.03617 16.11971  1.000 51.81648  ? 1284 THR   B CB   1 
ATOM   1650 O  OG1  . THR   A 1 232 ? 21.63661  -21.75747 15.19802  1.000 52.97394  ? 1284 THR   B OG1  1 
ATOM   1651 C  CG2  . THR   A 1 232 ? 22.23569  -21.58160 17.52093  1.000 47.87953  ? 1284 THR   B CG2  1 
ATOM   1652 N  N    . PHE   A 1 233 ? 21.08382  -18.58788 14.04978  1.000 47.07151  ? 1285 PHE   B N    1 
ATOM   1653 C  CA   . PHE   A 1 233 ? 21.02481  -18.15343 12.65761  1.000 41.03439  ? 1285 PHE   B CA   1 
ATOM   1654 C  C    . PHE   A 1 233 ? 21.38770  -19.26584 11.68204  1.000 44.54547  ? 1285 PHE   B C    1 
ATOM   1655 O  O    . PHE   A 1 233 ? 21.65968  -18.98533 10.50692  1.000 42.51313  ? 1285 PHE   B O    1 
ATOM   1656 C  CB   . PHE   A 1 233 ? 21.92490  -16.93659 12.41310  1.000 51.89509  ? 1285 PHE   B CB   1 
ATOM   1657 C  CG   . PHE   A 1 233 ? 21.62802  -15.77021 13.30965  1.000 48.30645  ? 1285 PHE   B CG   1 
ATOM   1658 C  CD1  . PHE   A 1 233 ? 20.39606  -15.14214 13.26443  1.000 51.44770  ? 1285 PHE   B CD1  1 
ATOM   1659 C  CD2  . PHE   A 1 233 ? 22.58408  -15.29694 14.19243  1.000 55.18019  ? 1285 PHE   B CD2  1 
ATOM   1660 C  CE1  . PHE   A 1 233 ? 20.11917  -14.06379 14.08802  1.000 54.16970  ? 1285 PHE   B CE1  1 
ATOM   1661 C  CE2  . PHE   A 1 233 ? 22.31419  -14.22159 15.01601  1.000 59.69154  ? 1285 PHE   B CE2  1 
ATOM   1662 C  CZ   . PHE   A 1 233 ? 21.08123  -13.60452 14.96281  1.000 51.26123  ? 1285 PHE   B CZ   1 
ATOM   1663 N  N    . HIS   A 1 234 ? 21.41461  -20.51766 12.13553  1.000 45.19521  ? 1286 HIS   B N    1 
ATOM   1664 C  CA   . HIS   A 1 234 ? 21.64850  -21.63604 11.23297  1.000 44.29392  ? 1286 HIS   B CA   1 
ATOM   1665 C  C    . HIS   A 1 234 ? 20.44146  -21.85130 10.32909  1.000 46.03243  ? 1286 HIS   B C    1 
ATOM   1666 O  O    . HIS   A 1 234 ? 19.31249  -21.48708 10.66098  1.000 46.70764  ? 1286 HIS   B O    1 
ATOM   1667 C  CB   . HIS   A 1 234 ? 21.93042  -22.91675 12.01847  1.000 43.81410  ? 1286 HIS   B CB   1 
ATOM   1668 C  CG   . HIS   A 1 234 ? 23.24544  -22.91957 12.73443  1.000 48.80388  ? 1286 HIS   B CG   1 
ATOM   1669 N  ND1  . HIS   A 1 234 ? 23.62339  -23.93526 13.58782  1.000 48.30102  ? 1286 HIS   B ND1  1 
ATOM   1670 C  CD2  . HIS   A 1 234 ? 24.27451  -22.03765 12.72205  1.000 49.63598  ? 1286 HIS   B CD2  1 
ATOM   1671 C  CE1  . HIS   A 1 234 ? 24.82342  -23.67716 14.07368  1.000 51.21270  ? 1286 HIS   B CE1  1 
ATOM   1672 N  NE2  . HIS   A 1 234 ? 25.23950  -22.53239 13.56422  1.000 58.21231  ? 1286 HIS   B NE2  1 
ATOM   1673 N  N    . LEU   A 1 235 ? 20.69138  -22.45078 9.16632   1.000 39.72376  ? 1287 LEU   B N    1 
ATOM   1674 C  CA   . LEU   A 1 235 ? 19.61532  -22.81806 8.25549   1.000 42.37966  ? 1287 LEU   B CA   1 
ATOM   1675 C  C    . LEU   A 1 235 ? 19.00523  -24.12482 8.73703   1.000 45.59158  ? 1287 LEU   B C    1 
ATOM   1676 O  O    . LEU   A 1 235 ? 19.62515  -25.18792 8.61543   1.000 44.78233  ? 1287 LEU   B O    1 
ATOM   1677 C  CB   . LEU   A 1 235 ? 20.12727  -22.94766 6.82553   1.000 41.34030  ? 1287 LEU   B CB   1 
ATOM   1678 C  CG   . LEU   A 1 235 ? 19.08820  -23.39699 5.79374   1.000 37.24469  ? 1287 LEU   B CG   1 
ATOM   1679 C  CD1  . LEU   A 1 235 ? 18.07728  -22.28202 5.51833   1.000 36.21537  ? 1287 LEU   B CD1  1 
ATOM   1680 C  CD2  . LEU   A 1 235 ? 19.75613  -23.85555 4.50690   1.000 34.66928  ? 1287 LEU   B CD2  1 
ATOM   1681 N  N    . LEU   A 1 236 ? 17.79525  -24.05351 9.29304   1.000 43.08703  ? 1288 LEU   B N    1 
ATOM   1682 C  CA   . LEU   A 1 236 ? 17.15818  -25.25225 9.82353   1.000 44.84290  ? 1288 LEU   B CA   1 
ATOM   1683 C  C    . LEU   A 1 236 ? 16.46908  -26.05163 8.72587   1.000 39.99658  ? 1288 LEU   B C    1 
ATOM   1684 O  O    . LEU   A 1 236 ? 16.48499  -27.28862 8.75536   1.000 40.54624  ? 1288 LEU   B O    1 
ATOM   1685 C  CB   . LEU   A 1 236 ? 16.15424  -24.88174 10.91441  1.000 45.15360  ? 1288 LEU   B CB   1 
ATOM   1686 C  CG   . LEU   A 1 236 ? 16.71632  -24.30127 12.21617  1.000 50.03499  ? 1288 LEU   B CG   1 
ATOM   1687 C  CD1  . LEU   A 1 236 ? 15.58438  -23.97680 13.17507  1.000 43.65586  ? 1288 LEU   B CD1  1 
ATOM   1688 C  CD2  . LEU   A 1 236 ? 17.70327  -25.26409 12.85752  1.000 41.76554  ? 1288 LEU   B CD2  1 
ATOM   1689 N  N    . HIS   A 1 237 ? 15.85611  -25.37496 7.75662   1.000 38.43041  ? 1289 HIS   B N    1 
ATOM   1690 C  CA   . HIS   A 1 237 ? 15.14002  -26.11032 6.72293   1.000 39.31492  ? 1289 HIS   B CA   1 
ATOM   1691 C  C    . HIS   A 1 237 ? 15.23403  -25.41986 5.37065   1.000 34.69666  ? 1289 HIS   B C    1 
ATOM   1692 O  O    . HIS   A 1 237 ? 15.21613  -24.18789 5.28117   1.000 39.84615  ? 1289 HIS   B O    1 
ATOM   1693 C  CB   . HIS   A 1 237 ? 13.65902  -26.29206 7.08705   1.000 37.72661  ? 1289 HIS   B CB   1 
ATOM   1694 C  CG   . HIS   A 1 237 ? 13.42698  -27.19658 8.25541   1.000 36.14195  ? 1289 HIS   B CG   1 
ATOM   1695 N  ND1  . HIS   A 1 237 ? 13.24505  -26.72406 9.53823   1.000 43.27787  ? 1289 HIS   B ND1  1 
ATOM   1696 C  CD2  . HIS   A 1 237 ? 13.34788  -28.54554 8.33595   1.000 31.86110  ? 1289 HIS   B CD2  1 
ATOM   1697 C  CE1  . HIS   A 1 237 ? 13.06300  -27.74372 10.35764  1.000 38.92665  ? 1289 HIS   B CE1  1 
ATOM   1698 N  NE2  . HIS   A 1 237 ? 13.12289  -28.86000 9.65508   1.000 34.35244  ? 1289 HIS   B NE2  1 
ATOM   1699 N  N    . THR   A 1 238 ? 15.31894  -26.23928 4.32298   1.000 35.89666  ? 1290 THR   B N    1 
ATOM   1700 C  CA   . THR   A 1 238 ? 15.08393  -25.81481 2.94881   1.000 34.35523  ? 1290 THR   B CA   1 
ATOM   1701 C  C    . THR   A 1 238 ? 13.71288  -26.32887 2.52606   1.000 36.70123  ? 1290 THR   B C    1 
ATOM   1702 O  O    . THR   A 1 238 ? 13.49778  -27.54388 2.44355   1.000 35.35942  ? 1290 THR   B O    1 
ATOM   1703 C  CB   . THR   A 1 238 ? 16.16286  -26.34926 2.00599   1.000 36.79111  ? 1290 THR   B CB   1 
ATOM   1704 O  OG1  . THR   A 1 238 ? 17.44691  -25.83721 2.38975   1.000 36.06292  ? 1290 THR   B OG1  1 
ATOM   1705 C  CG2  . THR   A 1 238 ? 15.86085  -25.93381 0.57584   1.000 34.47439  ? 1290 THR   B CG2  1 
ATOM   1706 N  N    . VAL   A 1 239 ? 12.78894  -25.40890 2.26272   1.000 36.43013  ? 1291 VAL   B N    1 
ATOM   1707 C  CA   . VAL   A 1 239 ? 11.41690  -25.77693 1.92291   1.000 37.08267  ? 1291 VAL   B CA   1 
ATOM   1708 C  C    . VAL   A 1 239 ? 11.05491  -25.16944 0.57068   1.000 37.40924  ? 1291 VAL   B C    1 
ATOM   1709 O  O    . VAL   A 1 239 ? 10.43099  -24.09941 0.51927   1.000 38.52024  ? 1291 VAL   B O    1 
ATOM   1710 C  CB   . VAL   A 1 239 ? 10.43597  -25.32242 3.01576   1.000 34.79745  ? 1291 VAL   B CB   1 
ATOM   1711 C  CG1  . VAL   A 1 239 ? 9.04292   -25.86742 2.74101   1.000 32.99824  ? 1291 VAL   B CG1  1 
ATOM   1712 C  CG2  . VAL   A 1 239 ? 10.93498  -25.76592 4.38592   1.000 33.18046  ? 1291 VAL   B CG2  1 
ATOM   1713 N  N    . PRO   A 1 240 ? 11.41283  -25.81590 -0.54108  1.000 37.15331  ? 1292 PRO   B N    1 
ATOM   1714 C  CA   . PRO   A 1 240 ? 11.14584  -25.20540 -1.85531  1.000 34.43191  ? 1292 PRO   B CA   1 
ATOM   1715 C  C    . PRO   A 1 240 ? 9.67985   -24.89738 -2.09639  1.000 43.64444  ? 1292 PRO   B C    1 
ATOM   1716 O  O    . PRO   A 1 240 ? 9.37190   -23.97466 -2.85975  1.000 37.48593  ? 1292 PRO   B O    1 
ATOM   1717 C  CB   . PRO   A 1 240 ? 11.66673  -26.26083 -2.84291  1.000 38.33568  ? 1292 PRO   B CB   1 
ATOM   1718 C  CG   . PRO   A 1 240 ? 12.64069  -27.08260 -2.05261  1.000 37.05150  ? 1292 PRO   B CG   1 
ATOM   1719 C  CD   . PRO   A 1 240 ? 12.10172  -27.11200 -0.65558  1.000 35.56455  ? 1292 PRO   B CD   1 
ATOM   1720 N  N    . ALA   A 1 241 ? 8.76481   -25.64107 -1.46807  1.000 35.67569  ? 1293 ALA   B N    1 
ATOM   1721 C  CA   . ALA   A 1 241 ? 7.34182   -25.43805 -1.71211  1.000 40.42771  ? 1293 ALA   B CA   1 
ATOM   1722 C  C    . ALA   A 1 241 ? 6.83894   -24.10880 -1.16962  1.000 37.54843  ? 1293 ALA   B C    1 
ATOM   1723 O  O    . ALA   A 1 241 ? 5.76497   -23.65688 -1.57777  1.000 38.39972  ? 1293 ALA   B O    1 
ATOM   1724 C  CB   . ALA   A 1 241 ? 6.53275   -26.58875 -1.10963  1.000 39.56014  ? 1293 ALA   B CB   1 
ATOM   1725 N  N    . LEU   A 1 242 ? 7.57902   -23.47350 -0.26689  1.000 40.87005  ? 1294 LEU   B N    1 
ATOM   1726 C  CA   . LEU   A 1 242 ? 7.17613   -22.19024 0.29461   1.000 36.55197  ? 1294 LEU   B CA   1 
ATOM   1727 C  C    . LEU   A 1 242 ? 7.59320   -21.00462 -0.56687  1.000 36.79924  ? 1294 LEU   B C    1 
ATOM   1728 O  O    . LEU   A 1 242 ? 7.40330   -19.85844 -0.14932  1.000 39.16842  ? 1294 LEU   B O    1 
ATOM   1729 C  CB   . LEU   A 1 242 ? 7.74719   -22.02673 1.70353   1.000 29.94340  ? 1294 LEU   B CB   1 
ATOM   1730 C  CG   . LEU   A 1 242 ? 7.14615   -22.94026 2.76991   1.000 41.05636  ? 1294 LEU   B CG   1 
ATOM   1731 C  CD1  . LEU   A 1 242 ? 7.82021   -22.71778 4.11380   1.000 33.96753  ? 1294 LEU   B CD1  1 
ATOM   1732 C  CD2  . LEU   A 1 242 ? 5.64617   -22.71011 2.87086   1.000 36.33946  ? 1294 LEU   B CD2  1 
ATOM   1733 N  N    . ASP   A 1 243 ? 8.15015   -21.24813 -1.75179  1.000 33.84345  ? 1295 ASP   B N    1 
ATOM   1734 C  CA   . ASP   A 1 243 ? 8.65521   -20.16050 -2.57723  1.000 38.35839  ? 1295 ASP   B CA   1 
ATOM   1735 C  C    . ASP   A 1 243 ? 7.52327   -19.22857 -2.99157  1.000 41.44277  ? 1295 ASP   B C    1 
ATOM   1736 O  O    . ASP   A 1 243 ? 6.53422   -19.66473 -3.59137  1.000 38.20363  ? 1295 ASP   B O    1 
ATOM   1737 C  CB   . ASP   A 1 243 ? 9.36813   -20.72104 -3.80903  1.000 34.93112  ? 1295 ASP   B CB   1 
ATOM   1738 C  CG   . ASP   A 1 243 ? 9.92319   -19.63244 -4.70348  1.000 41.29380  ? 1295 ASP   B CG   1 
ATOM   1739 O  OD1  . ASP   A 1 243 ? 10.47928  -18.64727 -4.16689  1.000 40.43722  ? 1295 ASP   B OD1  1 
ATOM   1740 O  OD2  . ASP   A 1 243 ? 9.80714   -19.76292 -5.94043  1.000 37.64716  ? 1295 ASP   B OD2  1 
ATOM   1741 N  N    . GLN   A 1 244 ? 7.67438   -17.94145 -2.66708  1.000 32.98887  ? 1296 GLN   B N    1 
ATOM   1742 C  CA   . GLN   A 1 244 ? 6.70945   -16.89851 -3.00047  1.000 39.17177  ? 1296 GLN   B CA   1 
ATOM   1743 C  C    . GLN   A 1 244 ? 5.39646   -17.05311 -2.24637  1.000 37.47687  ? 1296 GLN   B C    1 
ATOM   1744 O  O    . GLN   A 1 244 ? 4.35848   -16.56221 -2.70153  1.000 38.56861  ? 1296 GLN   B O    1 
ATOM   1745 C  CB   . GLN   A 1 244 ? 6.43541   -16.85009 -4.50748  1.000 38.47544  ? 1296 GLN   B CB   1 
ATOM   1746 C  CG   . GLN   A 1 244 ? 7.67640   -16.63052 -5.34660  1.000 36.37471  ? 1296 GLN   B CG   1 
ATOM   1747 C  CD   . GLN   A 1 244 ? 8.54250   -15.51037 -4.81007  1.000 41.86822  ? 1296 GLN   B CD   1 
ATOM   1748 O  OE1  . GLN   A 1 244 ? 8.16659   -14.33736 -4.85753  1.000 40.39586  ? 1296 GLN   B OE1  1 
ATOM   1749 N  NE2  . GLN   A 1 244 ? 9.70349   -15.86825 -4.28196  1.000 35.92629  ? 1296 GLN   B NE2  1 
ATOM   1750 N  N    . CYS   A 1 245 ? 5.41644   -17.72166 -1.09710  1.000 33.86528  ? 1297 CYS   B N    1 
ATOM   1751 C  CA   . CYS   A 1 245 ? 4.19844   -18.03927 -0.36794  1.000 33.74437  ? 1297 CYS   B CA   1 
ATOM   1752 C  C    . CYS   A 1 245 ? 3.96955   -17.07280 0.78668   1.000 37.95789  ? 1297 CYS   B C    1 
ATOM   1753 O  O    . CYS   A 1 245 ? 4.91260   -16.64061 1.45548   1.000 39.40860  ? 1297 CYS   B O    1 
ATOM   1754 C  CB   . CYS   A 1 245 ? 4.24334   -19.47006 0.17162   1.000 32.88096  ? 1297 CYS   B CB   1 
ATOM   1755 S  SG   . CYS   A 1 245 ? 3.83921   -20.73451 -1.03787  1.000 38.26260  ? 1297 CYS   B SG   1 
ATOM   1756 N  N    . ARG   A 1 246 ? 2.70558   -16.72862 0.99458   1.000 37.13537  ? 1298 ARG   B N    1 
ATOM   1757 C  CA   . ARG   A 1 246 ? 2.25466   -16.15309 2.25337   1.000 31.81224  ? 1298 ARG   B CA   1 
ATOM   1758 C  C    . ARG   A 1 246 ? 1.71760   -17.27670 3.12783   1.000 33.77496  ? 1298 ARG   B C    1 
ATOM   1759 O  O    . ARG   A 1 246 ? 1.12451   -18.23885 2.62423   1.000 32.55297  ? 1298 ARG   B O    1 
ATOM   1760 C  CB   . ARG   A 1 246 ? 1.17874   -15.09209 2.01998   1.000 32.14875  ? 1298 ARG   B CB   1 
ATOM   1761 C  CG   . ARG   A 1 246 ? 1.68181   -13.83541 1.31547   1.000 31.57525  ? 1298 ARG   B CG   1 
ATOM   1762 C  CD   . ARG   A 1 246 ? 2.32292   -12.86507 2.29907   1.000 32.40585  ? 1298 ARG   B CD   1 
ATOM   1763 N  NE   . ARG   A 1 246 ? 1.35098   -12.36762 3.26490   1.000 30.83239  ? 1298 ARG   B NE   1 
ATOM   1764 C  CZ   . ARG   A 1 246 ? 1.64008   -11.59023 4.29658   1.000 40.40680  ? 1298 ARG   B CZ   1 
ATOM   1765 N  NH1  . ARG   A 1 246 ? 2.87911   -11.19023 4.53539   1.000 39.48125  ? 1298 ARG   B NH1  1 
ATOM   1766 N  NH2  . ARG   A 1 246 ? 0.66313   -11.20583 5.11546   1.000 36.06953  ? 1298 ARG   B NH2  1 
ATOM   1767 N  N    . VAL   A 1 247 ? 1.93965   -17.16020 4.43878   1.000 36.88107  ? 1299 VAL   B N    1 
ATOM   1768 C  CA   . VAL   A 1 247 ? 1.66059   -18.24781 5.36622   1.000 42.08471  ? 1299 VAL   B CA   1 
ATOM   1769 C  C    . VAL   A 1 247 ? 0.82466   -17.74828 6.53504   1.000 38.26400  ? 1299 VAL   B C    1 
ATOM   1770 O  O    . VAL   A 1 247 ? 0.88777   -16.57713 6.92158   1.000 39.62992  ? 1299 VAL   B O    1 
ATOM   1771 C  CB   . VAL   A 1 247 ? 2.95655   -18.90370 5.89044   1.000 38.11913  ? 1299 VAL   B CB   1 
ATOM   1772 C  CG1  . VAL   A 1 247 ? 3.83949   -19.33923 4.72958   1.000 42.73710  ? 1299 VAL   B CG1  1 
ATOM   1773 C  CG2  . VAL   A 1 247 ? 3.69666   -17.95039 6.81604   1.000 35.14441  ? 1299 VAL   B CG2  1 
ATOM   1774 N  N    . VAL   A 1 248 ? 0.03561   -18.66100 7.09543   1.000 39.14496  ? 1300 VAL   B N    1 
ATOM   1775 C  CA   . VAL   A 1 248 ? -0.74534  -18.40746 8.30335   1.000 42.62265  ? 1300 VAL   B CA   1 
ATOM   1776 C  C    . VAL   A 1 248 ? -0.87542  -19.71715 9.06387   1.000 44.31624  ? 1300 VAL   B C    1 
ATOM   1777 O  O    . VAL   A 1 248 ? -1.06852  -20.77837 8.46630   1.000 43.19177  ? 1300 VAL   B O    1 
ATOM   1778 C  CB   . VAL   A 1 248 ? -2.13630  -17.81648 7.97816   1.000 42.60013  ? 1300 VAL   B CB   1 
ATOM   1779 C  CG1  . VAL   A 1 248 ? -2.94240  -18.79075 7.13857   1.000 39.76987  ? 1300 VAL   B CG1  1 
ATOM   1780 C  CG2  . VAL   A 1 248 ? -2.87724  -17.47491 9.26304   1.000 43.38337  ? 1300 VAL   B CG2  1 
ATOM   1781 N  N    . PHE   A 1 249 ? -0.78337  -19.64763 10.38584  1.000 41.74387  ? 1301 PHE   B N    1 
ATOM   1782 C  CA   . PHE   A 1 249 ? -0.80444  -20.84730 11.20832  1.000 51.22607  ? 1301 PHE   B CA   1 
ATOM   1783 C  C    . PHE   A 1 249 ? -2.16243  -21.02494 11.87243  1.000 42.44516  ? 1301 PHE   B C    1 
ATOM   1784 O  O    . PHE   A 1 249 ? -2.88135  -20.05578 12.12607  1.000 44.49870  ? 1301 PHE   B O    1 
ATOM   1785 C  CB   . PHE   A 1 249 ? 0.28660   -20.78296 12.28026  1.000 42.20433  ? 1301 PHE   B CB   1 
ATOM   1786 C  CG   . PHE   A 1 249 ? 1.68058   -20.78229 11.72222  1.000 42.10396  ? 1301 PHE   B CG   1 
ATOM   1787 C  CD1  . PHE   A 1 249 ? 2.22865   -19.62555 11.19274  1.000 38.56716  ? 1301 PHE   B CD1  1 
ATOM   1788 C  CD2  . PHE   A 1 249 ? 2.44249   -21.93835 11.72765  1.000 40.54126  ? 1301 PHE   B CD2  1 
ATOM   1789 C  CE1  . PHE   A 1 249 ? 3.50964   -19.62385 10.67871  1.000 43.85258  ? 1301 PHE   B CE1  1 
ATOM   1790 C  CE2  . PHE   A 1 249 ? 3.72448   -21.94265 11.21662  1.000 41.27644  ? 1301 PHE   B CE2  1 
ATOM   1791 C  CZ   . PHE   A 1 249 ? 4.25955   -20.78390 10.69014  1.000 36.28621  ? 1301 PHE   B CZ   1 
ATOM   1792 N  N    . ASN   A 1 250 ? -2.51252  -22.27980 12.15293  1.000 44.05319  ? 1302 ASN   B N    1 
ATOM   1793 C  CA   . ASN   A 1 250 ? -3.61451  -22.51435 13.06706  1.000 50.99357  ? 1302 ASN   B CA   1 
ATOM   1794 C  C    . ASN   A 1 250 ? -3.23743  -21.97083 14.44483  1.000 56.24921  ? 1302 ASN   B C    1 
ATOM   1795 O  O    . ASN   A 1 250 ? -2.08340  -21.62982 14.71166  1.000 48.89800  ? 1302 ASN   B O    1 
ATOM   1796 C  CB   . ASN   A 1 250 ? -3.97763  -24.00130 13.12566  1.000 48.99166  ? 1302 ASN   B CB   1 
ATOM   1797 C  CG   . ASN   A 1 250 ? -2.84668  -24.86718 13.63997  1.000 48.24271  ? 1302 ASN   B CG   1 
ATOM   1798 O  OD1  . ASN   A 1 250 ? -1.82663  -24.37107 14.11474  1.000 53.25170  ? 1302 ASN   B OD1  1 
ATOM   1799 N  ND2  . ASN   A 1 250 ? -3.03078  -26.18020 13.55849  1.000 47.83369  ? 1302 ASN   B ND2  1 
ATOM   1800 N  N    . HIS   A 1 251 ? -4.22840  -21.87041 15.32182  1.000 53.76147  ? 1303 HIS   B N    1 
ATOM   1801 C  CA   . HIS   A 1 251 ? -3.99531  -21.16493 16.57454  1.000 52.25666  ? 1303 HIS   B CA   1 
ATOM   1802 C  C    . HIS   A 1 251 ? -3.23134  -21.99359 17.60284  1.000 53.98504  ? 1303 HIS   B C    1 
ATOM   1803 O  O    . HIS   A 1 251 ? -2.78727  -21.43222 18.60761  1.000 55.81303  ? 1303 HIS   B O    1 
ATOM   1804 C  CB   . HIS   A 1 251 ? -5.32525  -20.67760 17.14638  1.000 55.84101  ? 1303 HIS   B CB   1 
ATOM   1805 C  CG   . HIS   A 1 251 ? -5.94919  -19.58188 16.33597  1.000 47.99364  ? 1303 HIS   B CG   1 
ATOM   1806 N  ND1  . HIS   A 1 251 ? -6.59524  -19.81830 15.14208  1.000 56.21107  ? 1303 HIS   B ND1  1 
ATOM   1807 C  CD2  . HIS   A 1 251 ? -5.99208  -18.24480 16.52944  1.000 50.37589  ? 1303 HIS   B CD2  1 
ATOM   1808 C  CE1  . HIS   A 1 251 ? -7.02517  -18.67246 14.64264  1.000 52.61582  ? 1303 HIS   B CE1  1 
ATOM   1809 N  NE2  . HIS   A 1 251 ? -6.67307  -17.70216 15.46525  1.000 44.50048  ? 1303 HIS   B NE2  1 
ATOM   1810 N  N    . THR   A 1 252 ? -3.04945  -23.29269 17.37235  1.000 52.66166  ? 1304 THR   B N    1 
ATOM   1811 C  CA   . THR   A 1 252 ? -2.18549  -24.10442 18.21765  1.000 59.56923  ? 1304 THR   B CA   1 
ATOM   1812 C  C    . THR   A 1 252 ? -0.75551  -24.17574 17.69663  1.000 61.77358  ? 1304 THR   B C    1 
ATOM   1813 O  O    . THR   A 1 252 ? 0.07346   -24.87157 18.28988  1.000 64.07774  ? 1304 THR   B O    1 
ATOM   1814 C  CB   . THR   A 1 252 ? -2.75059  -25.52332 18.35723  1.000 55.03301  ? 1304 THR   B CB   1 
ATOM   1815 O  OG1  . THR   A 1 252 ? -2.75868  -26.16983 17.07748  1.000 50.19000  ? 1304 THR   B OG1  1 
ATOM   1816 C  CG2  . THR   A 1 252 ? -4.16857  -25.48000 18.90925  1.000 57.11983  ? 1304 THR   B CG2  1 
ATOM   1817 N  N    . GLY   A 1 253 ? -0.45049  -23.47820 16.60435  1.000 58.06772  ? 1305 GLY   B N    1 
ATOM   1818 C  CA   . GLY   A 1 253 ? 0.89850   -23.45651 16.06930  1.000 57.66180  ? 1305 GLY   B CA   1 
ATOM   1819 C  C    . GLY   A 1 253 ? 1.40038   -24.78476 15.55481  1.000 51.27495  ? 1305 GLY   B C    1 
ATOM   1820 O  O    . GLY   A 1 253 ? 2.60736   -25.04283 15.59788  1.000 59.35022  ? 1305 GLY   B O    1 
ATOM   1821 N  N    . THR   A 1 254 ? 0.50630   -25.63589 15.04917  1.000 44.86727  ? 1306 THR   B N    1 
ATOM   1822 C  CA   . THR   A 1 254 ? 0.87418   -26.97708 14.62169  1.000 44.77675  ? 1306 THR   B CA   1 
ATOM   1823 C  C    . THR   A 1 254 ? 0.71212   -27.22566 13.12880  1.000 47.04481  ? 1306 THR   B C    1 
ATOM   1824 O  O    . THR   A 1 254 ? 1.31703   -28.17191 12.61515  1.000 47.21672  ? 1306 THR   B O    1 
ATOM   1825 C  CB   . THR   A 1 254 ? 0.05013   -28.02872 15.38113  1.000 51.24521  ? 1306 THR   B CB   1 
ATOM   1826 O  OG1  . THR   A 1 254 ? -1.30189  -28.02180 14.90517  1.000 51.38984  ? 1306 THR   B OG1  1 
ATOM   1827 C  CG2  . THR   A 1 254 ? 0.05419   -27.72913 16.87402  1.000 52.81833  ? 1306 THR   B CG2  1 
ATOM   1828 N  N    . VAL   A 1 255 ? -0.08384  -26.42488 12.42350  1.000 48.30664  ? 1307 VAL   B N    1 
ATOM   1829 C  CA   . VAL   A 1 255 ? -0.24489  -26.54044 10.97855  1.000 50.10052  ? 1307 VAL   B CA   1 
ATOM   1830 C  C    . VAL   A 1 255 ? -0.06680  -25.16070 10.36200  1.000 44.22968  ? 1307 VAL   B C    1 
ATOM   1831 O  O    . VAL   A 1 255 ? -0.49270  -24.15244 10.93862  1.000 46.10146  ? 1307 VAL   B O    1 
ATOM   1832 C  CB   . VAL   A 1 255 ? -1.61495  -27.13649 10.59183  1.000 40.55984  ? 1307 VAL   B CB   1 
ATOM   1833 C  CG1  . VAL   A 1 255 ? -1.81499  -27.06807 9.08381   1.000 48.98108  ? 1307 VAL   B CG1  1 
ATOM   1834 C  CG2  . VAL   A 1 255 ? -1.72304  -28.57228 11.08140  1.000 44.56178  ? 1307 VAL   B CG2  1 
ATOM   1835 N  N    . MET   A 1 256 ? 0.56217   -25.11521 9.18797   1.000 44.31444  ? 1308 MET   B N    1 
ATOM   1836 C  CA   . MET   A 1 256 ? 0.83525   -23.86451 8.49246   1.000 45.33551  ? 1308 MET   B CA   1 
ATOM   1837 C  C    . MET   A 1 256 ? 0.24620   -23.93702 7.09151   1.000 40.92739  ? 1308 MET   B C    1 
ATOM   1838 O  O    . MET   A 1 256 ? 0.59611   -24.83235 6.31685   1.000 40.33028  ? 1308 MET   B O    1 
ATOM   1839 C  CB   . MET   A 1 256 ? 2.34127   -23.58765 8.42631   1.000 40.13778  ? 1308 MET   B CB   1 
ATOM   1840 C  CG   . MET   A 1 256 ? 2.70535   -22.29296 7.71579   1.000 44.70010  ? 1308 MET   B CG   1 
ATOM   1841 S  SD   . MET   A 1 256 ? 4.48836   -22.03515 7.58263   1.000 41.14817  ? 1308 MET   B SD   1 
ATOM   1842 C  CE   . MET   A 1 256 ? 4.95422   -23.39461 6.51616   1.000 36.86915  ? 1308 MET   B CE   1 
ATOM   1843 N  N    . TYR   A 1 257 ? -0.64774  -23.00907 6.77117   1.000 42.86248  ? 1309 TYR   B N    1 
ATOM   1844 C  CA   . TYR   A 1 257 ? -1.16477  -22.86257 5.42013   1.000 43.81670  ? 1309 TYR   B CA   1 
ATOM   1845 C  C    . TYR   A 1 257 ? -0.26872  -21.90394 4.64972   1.000 39.00132  ? 1309 TYR   B C    1 
ATOM   1846 O  O    . TYR   A 1 257 ? 0.07138   -20.82677 5.14928   1.000 45.44658  ? 1309 TYR   B O    1 
ATOM   1847 C  CB   . TYR   A 1 257 ? -2.59873  -22.33245 5.43296   1.000 38.56277  ? 1309 TYR   B CB   1 
ATOM   1848 C  CG   . TYR   A 1 257 ? -3.57477  -23.17206 6.21832   1.000 47.87528  ? 1309 TYR   B CG   1 
ATOM   1849 C  CD1  . TYR   A 1 257 ? -3.70172  -23.01851 7.59126   1.000 44.18349  ? 1309 TYR   B CD1  1 
ATOM   1850 C  CD2  . TYR   A 1 257 ? -4.38586  -24.10325 5.58571   1.000 44.45564  ? 1309 TYR   B CD2  1 
ATOM   1851 C  CE1  . TYR   A 1 257 ? -4.60075  -23.77415 8.31659   1.000 41.23648  ? 1309 TYR   B CE1  1 
ATOM   1852 C  CE2  . TYR   A 1 257 ? -5.28990  -24.86790 6.30104   1.000 47.41388  ? 1309 TYR   B CE2  1 
ATOM   1853 C  CZ   . TYR   A 1 257 ? -5.39184  -24.69835 7.66598   1.000 50.87426  ? 1309 TYR   B CZ   1 
ATOM   1854 O  OH   . TYR   A 1 257 ? -6.28588  -25.45700 8.38430   1.000 50.50755  ? 1309 TYR   B OH   1 
ATOM   1855 N  N    . GLY   A 1 258 ? 0.10922   -22.30045 3.44886   1.000 36.67375  ? 1310 GLY   B N    1 
ATOM   1856 C  CA   . GLY   A 1 258 ? 0.88726   -21.44085 2.57250   1.000 33.33351  ? 1310 GLY   B CA   1 
ATOM   1857 C  C    . GLY   A 1 258 ? 0.28422   -21.40136 1.18650   1.000 38.55879  ? 1310 GLY   B C    1 
ATOM   1858 O  O    . GLY   A 1 258 ? -0.14787  -22.42453 0.65692   1.000 42.35682  ? 1310 GLY   B O    1 
ATOM   1859 N  N    . ALA   A 1 259 ? 0.25130   -20.20358 0.60703   1.000 35.54554  ? 1311 ALA   B N    1 
ATOM   1860 C  CA   . ALA   A 1 259 ? -0.25973  -20.01908 -0.74603  1.000 35.87903  ? 1311 ALA   B CA   1 
ATOM   1861 C  C    . ALA   A 1 259 ? 0.72131   -19.19147 -1.55638  1.000 36.93987  ? 1311 ALA   B C    1 
ATOM   1862 O  O    . ALA   A 1 259 ? 1.27840   -18.20832 -1.05979  1.000 28.17812  ? 1311 ALA   B O    1 
ATOM   1863 C  CB   . ALA   A 1 259 ? -1.63868  -19.34797 -0.74525  1.000 33.65828  ? 1311 ALA   B CB   1 
ATOM   1864 N  N    . MET   A 1 260 ? 0.92024   -19.58999 -2.81123  1.000 36.93421  ? 1312 MET   B N    1 
ATOM   1865 C  CA   . MET   A 1 260 ? 1.89227   -18.93640 -3.67452  1.000 41.33956  ? 1312 MET   B CA   1 
ATOM   1866 C  C    . MET   A 1 260 ? 1.28435   -17.69461 -4.31499  1.000 35.71343  ? 1312 MET   B C    1 
ATOM   1867 O  O    . MET   A 1 260 ? 0.19833   -17.75076 -4.89894  1.000 37.59524  ? 1312 MET   B O    1 
ATOM   1868 C  CB   . MET   A 1 260 ? 2.37516   -19.90187 -4.75615  1.000 40.16439  ? 1312 MET   B CB   1 
ATOM   1869 C  CG   . MET   A 1 260 ? 3.63818   -19.46025 -5.47536  1.000 39.33978  ? 1312 MET   B CG   1 
ATOM   1870 S  SD   . MET   A 1 260 ? 3.96006   -20.43886 -6.95699  1.000 42.40928  ? 1312 MET   B SD   1 
ATOM   1871 C  CE   . MET   A 1 260 ? 5.74506   -20.33804 -7.04708  1.000 44.30120  ? 1312 MET   B CE   1 
ATOM   1872 N  N    . LEU   A 1 261 ? 1.99544   -16.57362 -4.21046  1.000 35.91808  ? 1313 LEU   B N    1 
ATOM   1873 C  CA   . LEU   A 1 261 ? 1.54552   -15.34284 -4.83993  1.000 35.54080  ? 1313 LEU   B CA   1 
ATOM   1874 C  C    . LEU   A 1 261 ? 1.44946   -15.51243 -6.35086  1.000 41.37582  ? 1313 LEU   B C    1 
ATOM   1875 O  O    . LEU   A 1 261 ? 2.11937   -16.35672 -6.95255  1.000 38.06272  ? 1313 LEU   B O    1 
ATOM   1876 C  CB   . LEU   A 1 261 ? 2.49261   -14.19278 -4.50141  1.000 39.77861  ? 1313 LEU   B CB   1 
ATOM   1877 C  CG   . LEU   A 1 261 ? 2.48570   -13.69221 -3.05761  1.000 36.13913  ? 1313 LEU   B CG   1 
ATOM   1878 C  CD1  . LEU   A 1 261 ? 3.69977   -12.81920 -2.79299  1.000 36.22413  ? 1313 LEU   B CD1  1 
ATOM   1879 C  CD2  . LEU   A 1 261 ? 1.20376   -12.92400 -2.77988  1.000 32.74355  ? 1313 LEU   B CD2  1 
ATOM   1880 N  N    . GLN   A 1 262 ? 0.59150   -14.70360 -6.95916  1.000 37.70948  ? 1314 GLN   B N    1 
ATOM   1881 C  CA   . GLN   A 1 262 ? 0.45246   -14.72517 -8.43014  1.000 40.98923  ? 1314 GLN   B CA   1 
ATOM   1882 C  C    . GLN   A 1 262 ? 1.68649   -14.07251 -9.04844  1.000 49.58508  ? 1314 GLN   B C    1 
ATOM   1883 O  O    . GLN   A 1 262 ? 2.02559   -12.94438 -8.65190  1.000 49.28428  ? 1314 GLN   B O    1 
ATOM   1884 C  CB   . GLN   A 1 262 ? -0.79649  -13.95324 -8.83941  1.000 47.87060  ? 1314 GLN   B CB   1 
ATOM   1885 C  CG   . GLN   A 1 262 ? -1.10654  -13.99880 -10.32939 1.000 54.18130  ? 1314 GLN   B CG   1 
ATOM   1886 C  CD   . GLN   A 1 262 ? -1.77465  -15.28492 -10.75986 1.000 58.79537  ? 1314 GLN   B CD   1 
ATOM   1887 O  OE1  . GLN   A 1 262 ? -1.82972  -15.61439 -11.94773 1.000 67.59855  ? 1314 GLN   B OE1  1 
ATOM   1888 N  NE2  . GLN   A 1 262 ? -2.29168  -16.02850 -9.79355  1.000 63.96481  ? 1314 GLN   B NE2  1 
ATOM   1889 N  N    . ALA   A 1 263 ? 2.32241   -14.76693 -9.98018  1.000 48.05656  ? 1315 ALA   B N    1 
ATOM   1890 C  CA   . ALA   A 1 263 ? 3.49343   -14.22629 -10.66043 1.000 60.03670  ? 1315 ALA   B CA   1 
ATOM   1891 C  C    . ALA   A 1 263 ? 3.10950   -12.99959 -11.47791 1.000 65.42682  ? 1315 ALA   B C    1 
ATOM   1892 O  O    . ALA   A 1 263 ? 2.04549   -12.95575 -12.10289 1.000 63.96501  ? 1315 ALA   B O    1 
ATOM   1893 C  CB   . ALA   A 1 263 ? 4.12332   -15.28670 -11.56203 1.000 70.76283  ? 1315 ALA   B CB   1 
ATOM   1894 N  N    . ASP   A 1 264 ? 3.99058   -11.99665 -11.47533 1.000 73.69909  ? 1316 ASP   B N    1 
ATOM   1895 C  CA   . ASP   A 1 264 ? 3.71566   -10.73190 -12.14382 1.000 80.37614  ? 1316 ASP   B CA   1 
ATOM   1896 C  C    . ASP   A 1 264 ? 4.18962   -10.68951 -13.58985 1.000 84.24059  ? 1316 ASP   B C    1 
ATOM   1897 O  O    . ASP   A 1 264 ? 3.77567   -9.78977  -14.32820 1.000 91.58391  ? 1316 ASP   B O    1 
ATOM   1898 C  CB   . ASP   A 1 264 ? 4.34277   -9.56864  -11.36730 1.000 81.41510  ? 1316 ASP   B CB   1 
ATOM   1899 C  CG   . ASP   A 1 264 ? 3.32685   -8.82622  -10.51956 1.000 93.02384  ? 1316 ASP   B CG   1 
ATOM   1900 O  OD1  . ASP   A 1 264 ? 2.26082   -9.40902  -10.22430 1.000 97.18351  ? 1316 ASP   B OD1  1 
ATOM   1901 O  OD2  . ASP   A 1 264 ? 3.58396   -7.65710  -10.16703 1.000 92.39788  ? 1316 ASP   B OD2  1 
ATOM   1902 N  N    . ASP   A 1 265 ? 5.01253   -11.66872 -13.97849 1.000 80.09749  ? 1317 ASP   B N    1 
ATOM   1903 C  CA   . ASP   A 1 265 ? 5.46548   -11.78532 -15.39246 1.000 91.01350  ? 1317 ASP   B CA   1 
ATOM   1904 C  C    . ASP   A 1 265 ? 6.11157   -10.48255 -15.85199 1.000 96.83337  ? 1317 ASP   B C    1 
ATOM   1905 O  O    . ASP   A 1 265 ? 6.95563   -9.94832  -15.10423 1.000 102.35359 ? 1317 ASP   B O    1 
ATOM   1906 C  CB   . ASP   A 1 265 ? 4.32542   -12.17160 -16.31927 1.000 88.34725  ? 1317 ASP   B CB   1 
ATOM   1907 C  CG   . ASP   A 1 265 ? 4.31030   -13.61778 -16.78370 1.000 93.13335  ? 1317 ASP   B CG   1 
ATOM   1908 O  OD1  . ASP   A 1 265 ? 4.34325   -14.51444 -15.91534 1.000 88.42433  ? 1317 ASP   B OD1  1 
ATOM   1909 O  OD2  . ASP   A 1 265 ? 4.26124   -13.83326 -18.01061 1.000 99.26204  ? 1317 ASP   B OD2  1 
ATOM   1910 N  N    . GLU   A 1 266 ? 5.74057   -10.00599 -17.03817 1.000 91.36758  ? 1318 GLU   B N    1 
ATOM   1911 C  CA   . GLU   A 1 266 ? 6.26266   -8.70823  -17.53170 1.000 97.84437  ? 1318 GLU   B CA   1 
ATOM   1912 C  C    . GLU   A 1 266 ? 5.24067   -8.13654  -18.51289 1.000 98.18010  ? 1318 GLU   B C    1 
ATOM   1913 O  O    . GLU   A 1 266 ? 4.24573   -7.54328  -18.05410 1.000 96.19041  ? 1318 GLU   B O    1 
ATOM   1914 C  CB   . GLU   A 1 266 ? 7.61463   -8.83761  -18.23069 1.000 98.27580  ? 1318 GLU   B CB   1 
ATOM   1915 C  CG   . GLU   A 1 266 ? 8.76769   -8.26937  -17.41095 1.000 101.29299 ? 1318 GLU   B CG   1 
ATOM   1916 C  CD   . GLU   A 1 266 ? 9.91462   -9.24238  -17.20059 1.000 102.08947 ? 1318 GLU   B CD   1 
ATOM   1917 O  OE1  . GLU   A 1 266 ? 9.87459   -10.00999 -16.21729 1.000 92.77015  ? 1318 GLU   B OE1  1 
ATOM   1918 O  OE2  . GLU   A 1 266 ? 10.85060  -9.22878  -18.02563 1.000 97.74565  ? 1318 GLU   B OE2  1 
ATOM   1919 N  N    . ASP   A 1 267 ? 5.46762   -8.33907  -19.80882 1.000 102.91560 ? 1319 ASP   B N    1 
ATOM   1920 C  CA   . ASP   A 1 267 ? 4.47262   -7.89639  -20.82297 1.000 103.65454 ? 1319 ASP   B CA   1 
ATOM   1921 C  C    . ASP   A 1 267 ? 3.47353   -9.03338  -20.99549 1.000 95.66887  ? 1319 ASP   B C    1 
ATOM   1922 O  O    . ASP   A 1 267 ? 3.12347   -9.35381  -22.15035 1.000 93.22395  ? 1319 ASP   B O    1 
ATOM   1923 C  CB   . ASP   A 1 267 ? 5.12562   -7.48996  -22.13315 1.000 101.99259 ? 1319 ASP   B CB   1 
ATOM   1924 C  CG   . ASP   A 1 267 ? 6.15771   -6.37900  -22.02462 1.000 105.47687 ? 1319 ASP   B CG   1 
ATOM   1925 O  OD1  . ASP   A 1 267 ? 7.26970   -6.66289  -21.52954 1.000 107.89153 ? 1319 ASP   B OD1  1 
ATOM   1926 O  OD2  . ASP   A 1 267 ? 5.83878   -5.24313  -22.43406 1.000 95.43996  ? 1319 ASP   B OD2  1 
ATOM   1927 N  N    . ASP   A 1 268 ? 3.05652   -9.62791  -19.88024 1.000 92.30933  ? 1320 ASP   B N    1 
ATOM   1928 C  CA   . ASP   A 1 268 ? 2.03743   -10.70285 -19.93878 1.000 87.15953  ? 1320 ASP   B CA   1 
ATOM   1929 C  C    . ASP   A 1 268 ? 0.74646   -10.12698 -20.50397 1.000 77.05467  ? 1320 ASP   B C    1 
ATOM   1930 O  O    . ASP   A 1 268 ? 0.54156   -8.89994  -20.46045 1.000 81.41577  ? 1320 ASP   B O    1 
ATOM   1931 C  CB   . ASP   A 1 268 ? 1.75742   -11.32629 -18.58253 1.000 83.59069  ? 1320 ASP   B CB   1 
ATOM   1932 C  CG   . ASP   A 1 268 ? 1.08832   -12.69225 -18.59697 1.000 79.89146  ? 1320 ASP   B CG   1 
ATOM   1933 O  OD1  . ASP   A 1 268 ? 0.64525   -13.11664 -19.68079 1.000 79.15680  ? 1320 ASP   B OD1  1 
ATOM   1934 O  OD2  . ASP   A 1 268 ? 1.01530   -13.31682 -17.52072 1.000 75.00928  ? 1320 ASP   B OD2  1 
ATOM   1935 N  N    . LEU   A 1 269 ? -0.09262  -11.00711 -21.01060 1.000 69.37899  ? 1321 LEU   B N    1 
ATOM   1936 C  CA   . LEU   A 1 269 ? -1.37961  -10.59522 -21.54973 1.000 69.63211  ? 1321 LEU   B CA   1 
ATOM   1937 C  C    . LEU   A 1 269 ? -2.12351  -9.72277  -20.55405 1.000 69.92675  ? 1321 LEU   B C    1 
ATOM   1938 O  O    . LEU   A 1 269 ? -2.08349  -9.95630  -19.34396 1.000 66.29824  ? 1321 LEU   B O    1 
ATOM   1939 C  CB   . LEU   A 1 269 ? -2.23771  -11.81929 -21.87922 1.000 57.41974  ? 1321 LEU   B CB   1 
ATOM   1940 C  CG   . LEU   A 1 269 ? -1.82282  -12.73877 -23.02386 1.000 59.20941  ? 1321 LEU   B CG   1 
ATOM   1941 C  CD1  . LEU   A 1 269 ? -2.59092  -14.05069 -22.95432 1.000 55.63937  ? 1321 LEU   B CD1  1 
ATOM   1942 C  CD2  . LEU   A 1 269 ? -2.05380  -12.06029 -24.36213 1.000 48.71096  ? 1321 LEU   B CD2  1 
ATOM   1943 N  N    . MET   A 1 270 ? -2.88546  -8.79694  -21.11739 1.000 59.70180  ? 1322 MET   B N    1 
ATOM   1944 C  CA   . MET   A 1 270 ? -3.79837  -8.07651  -20.22165 1.000 66.82285  ? 1322 MET   B CA   1 
ATOM   1945 C  C    . MET   A 1 270 ? -4.74545  -9.18025  -19.74519 1.000 75.21854  ? 1322 MET   B C    1 
ATOM   1946 O  O    . MET   A 1 270 ? -4.61955  -10.34043 -20.18973 1.000 80.15533  ? 1322 MET   B O    1 
ATOM   1947 C  CB   . MET   A 1 270 ? -4.54231  -6.97575  -20.97607 1.000 60.22557  ? 1322 MET   B CB   1 
ATOM   1948 C  CG   . MET   A 1 270 ? -4.77719  -5.71542  -20.17356 1.000 68.16988  ? 1322 MET   B CG   1 
ATOM   1949 S  SD   . MET   A 1 270 ? -3.56709  -4.39960  -20.40911 1.000 66.63956  ? 1322 MET   B SD   1 
ATOM   1950 C  CE   . MET   A 1 270 ? -2.63918  -4.96124  -21.84192 1.000 54.80297  ? 1322 MET   B CE   1 
ATOM   1951 N  N    . GLU   A 1 271 ? -5.68039  -8.85284  -18.89029 1.000 67.95613  ? 1323 GLU   B N    1 
ATOM   1952 C  CA   . GLU   A 1 271 ? -6.59346  -9.84455  -18.33187 1.000 72.12579  ? 1323 GLU   B CA   1 
ATOM   1953 C  C    . GLU   A 1 271 ? -5.83750  -10.77723 -17.38952 1.000 67.01434  ? 1323 GLU   B C    1 
ATOM   1954 O  O    . GLU   A 1 271 ? -6.41952  -11.33482 -16.45528 1.000 73.50459  ? 1323 GLU   B O    1 
ATOM   1955 C  CB   . GLU   A 1 271 ? -7.28455  -10.64293 -19.44753 1.000 73.59631  ? 1323 GLU   B CB   1 
ATOM   1956 C  CG   . GLU   A 1 271 ? -7.87552  -9.77933  -20.55986 1.000 77.92543  ? 1323 GLU   B CG   1 
ATOM   1957 C  CD   . GLU   A 1 271 ? -7.53360  -10.28591 -21.95467 1.000 68.66867  ? 1323 GLU   B CD   1 
ATOM   1958 O  OE1  . GLU   A 1 271 ? -6.34262  -10.53911 -22.22860 1.000 50.83581  ? 1323 GLU   B OE1  1 
ATOM   1959 O  OE2  . GLU   A 1 271 ? -8.45863  -10.43616 -22.77758 1.000 61.48190  ? 1323 GLU   B OE2  1 
ATOM   1960 N  N    . GLU   A 1 272 ? -4.53452  -10.95043 -17.63549 1.000 64.38128  ? 1324 GLU   B N    1 
ATOM   1961 C  CA   . GLU   A 1 272 ? -3.66155  -11.72215 -16.76621 1.000 65.63551  ? 1324 GLU   B CA   1 
ATOM   1962 C  C    . GLU   A 1 272 ? -2.87946  -10.85583 -15.78958 1.000 64.61904  ? 1324 GLU   B C    1 
ATOM   1963 O  O    . GLU   A 1 272 ? -2.38447  -11.37647 -14.78639 1.000 74.08495  ? 1324 GLU   B O    1 
ATOM   1964 C  CB   . GLU   A 1 272 ? -2.66764  -12.54456 -17.59692 1.000 64.52380  ? 1324 GLU   B CB   1 
ATOM   1965 C  CG   . GLU   A 1 272 ? -3.31275  -13.54288 -18.53950 1.000 65.46268  ? 1324 GLU   B CG   1 
ATOM   1966 C  CD   . GLU   A 1 272 ? -3.90682  -14.73355 -17.81301 1.000 70.89242  ? 1324 GLU   B CD   1 
ATOM   1967 O  OE1  . GLU   A 1 272 ? -3.21384  -15.30626 -16.94381 1.000 62.45687  ? 1324 GLU   B OE1  1 
ATOM   1968 O  OE2  . GLU   A 1 272 ? -5.06886  -15.08957 -18.10484 1.000 65.09224  ? 1324 GLU   B OE2  1 
ATOM   1969 N  N    . ARG   A 1 273 ? -2.76737  -9.55594  -16.05210 1.000 62.34820  ? 1325 ARG   B N    1 
ATOM   1970 C  CA   . ARG   A 1 273 ? -2.02127  -8.64466  -15.18948 1.000 67.30798  ? 1325 ARG   B CA   1 
ATOM   1971 C  C    . ARG   A 1 273 ? -2.74722  -8.46707  -13.85653 1.000 68.30240  ? 1325 ARG   B C    1 
ATOM   1972 O  O    . ARG   A 1 273 ? -3.83917  -7.88597  -13.80573 1.000 61.69903  ? 1325 ARG   B O    1 
ATOM   1973 C  CB   . ARG   A 1 273 ? -1.82819  -7.30195  -15.88502 1.000 66.54180  ? 1325 ARG   B CB   1 
ATOM   1974 C  CG   . ARG   A 1 273 ? -1.14123  -7.38754  -17.24200 1.000 70.29044  ? 1325 ARG   B CG   1 
ATOM   1975 C  CD   . ARG   A 1 273 ? -0.91214  -6.00379  -17.84556 1.000 57.36596  ? 1325 ARG   B CD   1 
ATOM   1976 N  NE   . ARG   A 1 273 ? -0.05718  -6.05633  -19.02656 1.000 62.19395  ? 1325 ARG   B NE   1 
ATOM   1977 C  CZ   . ARG   A 1 273 ? 0.41088   -4.99162  -19.66300 1.000 61.23141  ? 1325 ARG   B CZ   1 
ATOM   1978 N  NH1  . ARG   A 1 273 ? 0.11699   -3.76344  -19.26647 1.000 59.52342  ? 1325 ARG   B NH1  1 
ATOM   1979 N  NH2  . ARG   A 1 273 ? 1.19484   -5.16310  -20.72395 1.000 68.78890  ? 1325 ARG   B NH2  1 
ATOM   1980 N  N    . MET   A 1 274 ? -2.12222  -8.94369  -12.77536 1.000 75.47826  ? 1326 MET   B N    1 
ATOM   1981 C  CA   . MET   A 1 274 ? -2.68218  -8.91711  -11.42335 1.000 79.00634  ? 1326 MET   B CA   1 
ATOM   1982 C  C    . MET   A 1 274 ? -3.96224  -9.74102  -11.42699 1.000 69.15155  ? 1326 MET   B C    1 
ATOM   1983 O  O    . MET   A 1 274 ? -3.88635  -10.96810 -11.62850 1.000 73.56858  ? 1326 MET   B O    1 
ATOM   1984 C  CB   . MET   A 1 274 ? -2.82005  -7.45193  -10.99493 1.000 86.11392  ? 1326 MET   B CB   1 
ATOM   1985 C  CG   . MET   A 1 274 ? -1.48999  -6.75098  -10.84024 1.000 91.28261  ? 1326 MET   B CG   1 
ATOM   1986 S  SD   . MET   A 1 274 ? -0.40302  -7.50257  -9.60498  1.000 123.36677 ? 1326 MET   B SD   1 
ATOM   1987 C  CE   . MET   A 1 274 ? -1.31895  -7.16091  -8.10009  1.000 89.02585  ? 1326 MET   B CE   1 
ATOM   1988 N  N    . LYS   A 1 275 ? -5.11619  -9.11485  -11.23720 1.000 63.52659  ? 1327 LYS   B N    1 
ATOM   1989 C  CA   . LYS   A 1 275 ? -6.41525  -9.84277  -11.29187 1.000 58.87520  ? 1327 LYS   B CA   1 
ATOM   1990 C  C    . LYS   A 1 275 ? -6.61228  -10.73826 -10.04651 1.000 53.58082  ? 1327 LYS   B C    1 
ATOM   1991 O  O    . LYS   A 1 275 ? -7.78529  -10.96604 -9.70039  1.000 54.88315  ? 1327 LYS   B O    1 
ATOM   1992 C  CB   . LYS   A 1 275 ? -6.60135  -10.59328 -12.61657 1.000 57.35648  ? 1327 LYS   B CB   1 
ATOM   1993 C  CG   . LYS   A 1 275 ? -6.49231  -9.72478  -13.85992 1.000 70.28962  ? 1327 LYS   B CG   1 
ATOM   1994 C  CD   . LYS   A 1 275 ? -7.18521  -8.36871  -13.81344 1.000 65.26261  ? 1327 LYS   B CD   1 
ATOM   1995 C  CE   . LYS   A 1 275 ? -6.89718  -7.56122  -15.04076 1.000 69.03799  ? 1327 LYS   B CE   1 
ATOM   1996 N  NZ   . LYS   A 1 275 ? -7.16206  -6.13412  -14.84932 1.000 49.02182  ? 1327 LYS   B NZ   1 
ATOM   1997 N  N    . SER   A 1 276 ? -5.54830  -11.23009 -9.40435  1.000 43.21670  ? 1328 SER   B N    1 
ATOM   1998 C  CA   . SER   A 1 276 ? -5.69432  -11.97559 -8.16005  1.000 38.65606  ? 1328 SER   B CA   1 
ATOM   1999 C  C    . SER   A 1 276 ? -4.36830  -11.97940 -7.42309  1.000 45.13524  ? 1328 SER   B C    1 
ATOM   2000 O  O    . SER   A 1 276 ? -3.31532  -12.05474 -8.07209  1.000 42.24972  ? 1328 SER   B O    1 
ATOM   2001 C  CB   . SER   A 1 276 ? -6.15644  -13.41066 -8.42347  1.000 38.70060  ? 1328 SER   B CB   1 
ATOM   2002 O  OG   . SER   A 1 276 ? -5.08152  -14.20292 -8.88619  1.000 51.05153  ? 1328 SER   B OG   1 
ATOM   2003 N  N    . PRO   A 1 277 ? -4.37125  -11.90487 -6.08912  1.000 37.23192  ? 1329 PRO   B N    1 
ATOM   2004 C  CA   . PRO   A 1 277 ? -3.09323  -11.90268 -5.36216  1.000 37.25351  ? 1329 PRO   B CA   1 
ATOM   2005 C  C    . PRO   A 1 277 ? -2.41034  -13.25873 -5.33864  1.000 37.02120  ? 1329 PRO   B C    1 
ATOM   2006 O  O    . PRO   A 1 277 ? -1.17534  -13.31482 -5.33565  1.000 32.75036  ? 1329 PRO   B O    1 
ATOM   2007 C  CB   . PRO   A 1 277 ? -3.49116  -11.44809 -3.95032  1.000 39.25042  ? 1329 PRO   B CB   1 
ATOM   2008 C  CG   . PRO   A 1 277 ? -4.93318  -11.82493 -3.82813  1.000 35.04640  ? 1329 PRO   B CG   1 
ATOM   2009 C  CD   . PRO   A 1 277 ? -5.52221  -11.66843 -5.20018  1.000 35.67732  ? 1329 PRO   B CD   1 
ATOM   2010 N  N    . PHE   A 1 278 ? -3.16542  -14.35166 -5.32119  1.000 34.59982  ? 1330 PHE   B N    1 
ATOM   2011 C  CA   . PHE   A 1 278 ? -2.58752  -15.68167 -5.21568  1.000 33.42636  ? 1330 PHE   B CA   1 
ATOM   2012 C  C    . PHE   A 1 278 ? -2.99062  -16.52311 -6.41633  1.000 36.58200  ? 1330 PHE   B C    1 
ATOM   2013 O  O    . PHE   A 1 278 ? -3.86762  -16.15435 -7.20145  1.000 39.20297  ? 1330 PHE   B O    1 
ATOM   2014 C  CB   . PHE   A 1 278 ? -3.02854  -16.38812 -3.92538  1.000 29.46606  ? 1330 PHE   B CB   1 
ATOM   2015 C  CG   . PHE   A 1 278 ? -2.64545  -15.65565 -2.67168  1.000 33.39349  ? 1330 PHE   B CG   1 
ATOM   2016 C  CD1  . PHE   A 1 278 ? -1.41444  -15.87251 -2.07563  1.000 38.23234  ? 1330 PHE   B CD1  1 
ATOM   2017 C  CD2  . PHE   A 1 278 ? -3.51636  -14.74736 -2.09102  1.000 39.45892  ? 1330 PHE   B CD2  1 
ATOM   2018 C  CE1  . PHE   A 1 278 ? -1.05436  -15.19308 -0.91791  1.000 35.72851  ? 1330 PHE   B CE1  1 
ATOM   2019 C  CE2  . PHE   A 1 278 ? -3.16327  -14.06393 -0.93530  1.000 35.57000  ? 1330 PHE   B CE2  1 
ATOM   2020 C  CZ   . PHE   A 1 278 ? -1.92927  -14.28779 -0.34925  1.000 32.54613  ? 1330 PHE   B CZ   1 
ATOM   2021 N  N    . GLY   A 1 279 ? -2.33472  -17.67121 -6.53990  1.000 37.29249  ? 1331 GLY   B N    1 
ATOM   2022 C  CA   . GLY   A 1 279 ? -2.74582  -18.68055 -7.48948  1.000 34.76913  ? 1331 GLY   B CA   1 
ATOM   2023 C  C    . GLY   A 1 279 ? -3.99486  -19.39026 -7.00317  1.000 39.63582  ? 1331 GLY   B C    1 
ATOM   2024 O  O    . GLY   A 1 279 ? -4.72980  -18.89787 -6.14334  1.000 40.12217  ? 1331 GLY   B O    1 
ATOM   2025 N  N    . SER   A 1 280 ? -4.23097  -20.57647 -7.56069  1.000 35.30795  ? 1332 SER   B N    1 
ATOM   2026 C  CA   . SER   A 1 280 ? -5.44702  -21.33427 -7.30135  1.000 38.55327  ? 1332 SER   B CA   1 
ATOM   2027 C  C    . SER   A 1 280 ? -5.25208  -22.43988 -6.26692  1.000 45.58821  ? 1332 SER   B C    1 
ATOM   2028 O  O    . SER   A 1 280 ? -6.16413  -23.24772 -6.05658  1.000 38.21160  ? 1332 SER   B O    1 
ATOM   2029 C  CB   . SER   A 1 280 ? -5.98011  -21.92575 -8.60910  1.000 38.89589  ? 1332 SER   B CB   1 
ATOM   2030 O  OG   . SER   A 1 280 ? -5.17120  -22.99998 -9.04170  1.000 43.14819  ? 1332 SER   B OG   1 
ATOM   2031 N  N    . SER   A 1 281 ? -4.09706  -22.49470 -5.60693  1.000 40.56158  ? 1333 SER   B N    1 
ATOM   2032 C  CA   . SER   A 1 281 ? -3.81212  -23.59137 -4.69551  1.000 47.22670  ? 1333 SER   B CA   1 
ATOM   2033 C  C    . SER   A 1 281 ? -3.22104  -23.07990 -3.39073  1.000 44.76060  ? 1333 SER   B C    1 
ATOM   2034 O  O    . SER   A 1 281 ? -2.59096  -22.01992 -3.33717  1.000 42.04926  ? 1333 SER   B O    1 
ATOM   2035 C  CB   . SER   A 1 281 ? -2.85022  -24.60969 -5.32713  1.000 38.65781  ? 1333 SER   B CB   1 
ATOM   2036 O  OG   . SER   A 1 281 ? -1.59718  -24.01890 -5.61041  1.000 59.37957  ? 1333 SER   B OG   1 
ATOM   2037 N  N    . PHE   A 1 282 ? -3.44707  -23.85146 -2.33242  1.000 42.08221  ? 1334 PHE   B N    1 
ATOM   2038 C  CA   . PHE   A 1 282 ? -2.75802  -23.65001 -1.06552  1.000 47.74857  ? 1334 PHE   B CA   1 
ATOM   2039 C  C    . PHE   A 1 282 ? -2.42311  -25.00280 -0.45899  1.000 46.60553  ? 1334 PHE   B C    1 
ATOM   2040 O  O    . PHE   A 1 282 ? -3.09819  -26.00385 -0.71358  1.000 45.92946  ? 1334 PHE   B O    1 
ATOM   2041 C  CB   . PHE   A 1 282 ? -3.57892  -22.80556 -0.07683  1.000 39.70898  ? 1334 PHE   B CB   1 
ATOM   2042 C  CG   . PHE   A 1 282 ? -4.83296  -23.47227 0.40547   1.000 47.44350  ? 1334 PHE   B CG   1 
ATOM   2043 C  CD1  . PHE   A 1 282 ? -5.98798  -23.43348 -0.35451  1.000 47.01221  ? 1334 PHE   B CD1  1 
ATOM   2044 C  CD2  . PHE   A 1 282 ? -4.86398  -24.12378 1.62973   1.000 51.04756  ? 1334 PHE   B CD2  1 
ATOM   2045 C  CE1  . PHE   A 1 282 ? -7.14802  -24.04021 0.08777   1.000 46.40862  ? 1334 PHE   B CE1  1 
ATOM   2046 C  CE2  . PHE   A 1 282 ? -6.02401  -24.73151 2.07901   1.000 48.74844  ? 1334 PHE   B CE2  1 
ATOM   2047 C  CZ   . PHE   A 1 282 ? -7.16703  -24.69073 1.30503   1.000 49.15108  ? 1334 PHE   B CZ   1 
ATOM   2048 N  N    . ARG   A 1 283 ? -1.36808  -25.02856 0.34499   1.000 40.79327  ? 1335 ARG   B N    1 
ATOM   2049 C  CA   . ARG   A 1 283 ? -0.87016  -26.26437 0.92046   1.000 45.51562  ? 1335 ARG   B CA   1 
ATOM   2050 C  C    . ARG   A 1 283 ? -0.78711  -26.12978 2.43241   1.000 43.39547  ? 1335 ARG   B C    1 
ATOM   2051 O  O    . ARG   A 1 283 ? -0.70801  -25.02757 2.97797   1.000 45.79317  ? 1335 ARG   B O    1 
ATOM   2052 C  CB   . ARG   A 1 283 ? 0.49879   -26.63971 0.34057   1.000 45.37273  ? 1335 ARG   B CB   1 
ATOM   2053 C  CG   . ARG   A 1 283 ? 0.50074   -26.74231 -1.17539  1.000 48.13437  ? 1335 ARG   B CG   1 
ATOM   2054 C  CD   . ARG   A 1 283 ? 1.85975   -26.38764 -1.74357  1.000 59.46443  ? 1335 ARG   B CD   1 
ATOM   2055 N  NE   . ARG   A 1 283 ? 2.80767   -27.49067 -1.64416  1.000 60.86773  ? 1335 ARG   B NE   1 
ATOM   2056 C  CZ   . ARG   A 1 283 ? 3.35559   -28.10013 -2.68694  1.000 69.43387  ? 1335 ARG   B CZ   1 
ATOM   2057 N  NH1  . ARG   A 1 283 ? 3.08958   -27.72260 -3.92608  1.000 64.83517  ? 1335 ARG   B NH1  1 
ATOM   2058 N  NH2  . ARG   A 1 283 ? 4.19752   -29.10911 -2.48256  1.000 71.78564  ? 1335 ARG   B NH2  1 
ATOM   2059 N  N    . THR   A 1 284 ? -0.82718  -27.27451 3.10386   1.000 43.58638  ? 1336 THR   B N    1 
ATOM   2060 C  CA   . THR   A 1 284 ? -0.66314  -27.34395 4.54588   1.000 44.32295  ? 1336 THR   B CA   1 
ATOM   2061 C  C    . THR   A 1 284 ? 0.64181   -28.05592 4.87513   1.000 44.09785  ? 1336 THR   B C    1 
ATOM   2062 O  O    . THR   A 1 284 ? 1.01972   -29.02622 4.21250   1.000 40.43790  ? 1336 THR   B O    1 
ATOM   2063 C  CB   . THR   A 1 284 ? -1.83918  -28.06560 5.20920   1.000 41.03033  ? 1336 THR   B CB   1 
ATOM   2064 O  OG1  . THR   A 1 284 ? -2.09129  -29.30485 4.53470   1.000 50.62306  ? 1336 THR   B OG1  1 
ATOM   2065 C  CG2  . THR   A 1 284 ? -3.08711  -27.19652 5.15590   1.000 46.46869  ? 1336 THR   B CG2  1 
ATOM   2066 N  N    . PHE   A 1 285 ? 1.32888   -27.54858 5.89091   1.000 44.64828  ? 1337 PHE   B N    1 
ATOM   2067 C  CA   . PHE   A 1 285 ? 2.61186   -28.06550 6.33207   1.000 44.14346  ? 1337 PHE   B CA   1 
ATOM   2068 C  C    . PHE   A 1 285 ? 2.54488   -28.36891 7.81720   1.000 46.01228  ? 1337 PHE   B C    1 
ATOM   2069 O  O    . PHE   A 1 285 ? 1.89095   -27.64556 8.57793   1.000 46.22007  ? 1337 PHE   B O    1 
ATOM   2070 C  CB   . PHE   A 1 285 ? 3.74693   -27.06369 6.08064   1.000 42.95964  ? 1337 PHE   B CB   1 
ATOM   2071 C  CG   . PHE   A 1 285 ? 3.95891   -26.72328 4.63750   1.000 38.98758  ? 1337 PHE   B CG   1 
ATOM   2072 C  CD1  . PHE   A 1 285 ? 3.16697   -25.77746 4.00915   1.000 34.50086  ? 1337 PHE   B CD1  1 
ATOM   2073 C  CD2  . PHE   A 1 285 ? 4.96584   -27.33464 3.91271   1.000 38.55910  ? 1337 PHE   B CD2  1 
ATOM   2074 C  CE1  . PHE   A 1 285 ? 3.36495   -25.45800 2.67802   1.000 35.78052  ? 1337 PHE   B CE1  1 
ATOM   2075 C  CE2  . PHE   A 1 285 ? 5.17083   -27.02118 2.58458   1.000 43.88970  ? 1337 PHE   B CE2  1 
ATOM   2076 C  CZ   . PHE   A 1 285 ? 4.36988   -26.08036 1.96624   1.000 46.71651  ? 1337 PHE   B CZ   1 
ATOM   2077 N  N    . ASN   A 1 286 ? 3.21680   -29.43880 8.22160   1.000 49.14286  ? 1338 ASN   B N    1 
ATOM   2078 C  CA   . ASN   A 1 286 ? 3.46983   -29.66626 9.63568   1.000 49.40781  ? 1338 ASN   B CA   1 
ATOM   2079 C  C    . ASN   A 1 286 ? 4.32893   -28.52911 10.17121  1.000 46.71054  ? 1338 ASN   B C    1 
ATOM   2080 O  O    . ASN   A 1 286 ? 5.42394   -28.27740 9.66107   1.000 42.62261  ? 1338 ASN   B O    1 
ATOM   2081 C  CB   . ASN   A 1 286 ? 4.16273   -31.01623 9.83420   1.000 40.99795  ? 1338 ASN   B CB   1 
ATOM   2082 C  CG   . ASN   A 1 286 ? 4.37575   -31.35467 11.29632  1.000 46.72668  ? 1338 ASN   B CG   1 
ATOM   2083 O  OD1  . ASN   A 1 286 ? 4.99883   -30.59943 12.03901  1.000 52.97496  ? 1338 ASN   B OD1  1 
ATOM   2084 N  ND2  . ASN   A 1 286 ? 3.84867   -32.49946 11.71879  1.000 45.44185  ? 1338 ASN   B ND2  1 
ATOM   2085 N  N    . ALA   A 1 287 ? 3.82402   -27.82867 11.18594  1.000 42.29366  ? 1339 ALA   B N    1 
ATOM   2086 C  CA   . ALA   A 1 287 ? 4.48713   -26.62153 11.67445  1.000 47.82985  ? 1339 ALA   B CA   1 
ATOM   2087 C  C    . ALA   A 1 287 ? 5.78713   -26.90234 12.41552  1.000 45.81499  ? 1339 ALA   B C    1 
ATOM   2088 O  O    . ALA   A 1 287 ? 6.46621   -25.94424 12.80612  1.000 41.17098  ? 1339 ALA   B O    1 
ATOM   2089 C  CB   . ALA   A 1 287 ? 3.53521   -25.83410 12.57816  1.000 39.57108  ? 1339 ALA   B CB   1 
ATOM   2090 N  N    . THR   A 1 288 ? 6.15603   -28.16429 12.62001  1.000 43.62566  ? 1340 THR   B N    1 
ATOM   2091 C  CA   . THR   A 1 288 ? 7.38403   -28.51110 13.32211  1.000 48.49049  ? 1340 THR   B CA   1 
ATOM   2092 C  C    . THR   A 1 288 ? 8.48596   -29.01855 12.40528  1.000 48.09799  ? 1340 THR   B C    1 
ATOM   2093 O  O    . THR   A 1 288 ? 9.63800   -28.60159 12.54808  1.000 51.23470  ? 1340 THR   B O    1 
ATOM   2094 C  CB   . THR   A 1 288 ? 7.10198   -29.56666 14.39954  1.000 51.01891  ? 1340 THR   B CB   1 
ATOM   2095 O  OG1  . THR   A 1 288 ? 6.67986   -30.78687 13.77903  1.000 59.33237  ? 1340 THR   B OG1  1 
ATOM   2096 C  CG2  . THR   A 1 288 ? 6.01204   -29.08520 15.34338  1.000 42.30119  ? 1340 THR   B CG2  1 
ATOM   2097 N  N    . ASP   A 1 289 ? 8.17086   -29.91090 11.46664  1.000 48.27008  ? 1341 ASP   B N    1 
ATOM   2098 C  CA   . ASP   A 1 289 ? 9.15580   -30.42235 10.52581  1.000 48.56798  ? 1341 ASP   B CA   1 
ATOM   2099 C  C    . ASP   A 1 289 ? 8.94980   -29.89989 9.10961   1.000 47.68711  ? 1341 ASP   B C    1 
ATOM   2100 O  O    . ASP   A 1 289 ? 9.69774   -30.29131 8.20475   1.000 53.31157  ? 1341 ASP   B O    1 
ATOM   2101 C  CB   . ASP   A 1 289 ? 9.14468   -31.95735 10.52342  1.000 41.64613  ? 1341 ASP   B CB   1 
ATOM   2102 C  CG   . ASP   A 1 289 ? 7.82962   -32.53944 10.03469  1.000 51.10184  ? 1341 ASP   B CG   1 
ATOM   2103 O  OD1  . ASP   A 1 289 ? 6.96866   -31.77556 9.55141   1.000 50.10465  ? 1341 ASP   B OD1  1 
ATOM   2104 O  OD2  . ASP   A 1 289 ? 7.65852   -33.77339 10.13118  1.000 59.35937  ? 1341 ASP   B OD2  1 
ATOM   2105 N  N    . TYR   A 1 290 ? 7.95686   -29.04090 8.89030   1.000 40.15140  ? 1342 TYR   B N    1 
ATOM   2106 C  CA   . TYR   A 1 290 ? 7.68587   -28.39639 7.60905   1.000 38.75029  ? 1342 TYR   B CA   1 
ATOM   2107 C  C    . TYR   A 1 290 ? 7.41876   -29.38381 6.48045   1.000 40.89518  ? 1342 TYR   B C    1 
ATOM   2108 O  O    . TYR   A 1 290 ? 7.45675   -28.99728 5.30430   1.000 41.64446  ? 1342 TYR   B O    1 
ATOM   2109 C  CB   . TYR   A 1 290 ? 8.82593   -27.44863 7.21165   1.000 42.17562  ? 1342 TYR   B CB   1 
ATOM   2110 C  CG   . TYR   A 1 290 ? 8.95605   -26.26628 8.13517   1.000 36.31329  ? 1342 TYR   B CG   1 
ATOM   2111 C  CD1  . TYR   A 1 290 ? 9.74908   -26.33489 9.27118   1.000 39.03101  ? 1342 TYR   B CD1  1 
ATOM   2112 C  CD2  . TYR   A 1 290 ? 8.27613   -25.08333 7.87873   1.000 31.31009  ? 1342 TYR   B CD2  1 
ATOM   2113 C  CE1  . TYR   A 1 290 ? 9.86719   -25.26056 10.12075  1.000 36.01235  ? 1342 TYR   B CE1  1 
ATOM   2114 C  CE2  . TYR   A 1 290 ? 8.38924   -24.00100 8.72129   1.000 44.22489  ? 1342 TYR   B CE2  1 
ATOM   2115 C  CZ   . TYR   A 1 290 ? 9.18527   -24.09462 9.84331   1.000 41.60821  ? 1342 TYR   B CZ   1 
ATOM   2116 O  OH   . TYR   A 1 290 ? 9.30038   -23.01430 10.68688  1.000 41.45255  ? 1342 TYR   B OH   1 
ATOM   2117 N  N    . LYS   A 1 291 ? 7.15467   -30.64867 6.80196   1.000 44.43370  ? 1343 LYS   B N    1 
ATOM   2118 C  CA   . LYS   A 1 291 ? 6.82956   -31.59406 5.74835   1.000 45.54873  ? 1343 LYS   B CA   1 
ATOM   2119 C  C    . LYS   A 1 291 ? 5.40957   -31.35615 5.23729   1.000 48.72148  ? 1343 LYS   B C    1 
ATOM   2120 O  O    . LYS   A 1 291 ? 4.53963   -30.90579 5.98714   1.000 43.95004  ? 1343 LYS   B O    1 
ATOM   2121 C  CB   . LYS   A 1 291 ? 6.96347   -33.02987 6.24991   1.000 50.09395  ? 1343 LYS   B CB   1 
ATOM   2122 C  CG   . LYS   A 1 291 ? 8.39544   -33.46388 6.50704   1.000 53.33243  ? 1343 LYS   B CG   1 
ATOM   2123 C  CD   . LYS   A 1 291 ? 8.50433   -34.97483 6.64563   1.000 59.48167  ? 1343 LYS   B CD   1 
ATOM   2124 C  CE   . LYS   A 1 291 ? 9.94730   -35.39885 6.89676   1.000 59.82576  ? 1343 LYS   B CE   1 
ATOM   2125 N  NZ   . LYS   A 1 291 ? 10.85730  -34.96935 5.79456   1.000 73.07663  ? 1343 LYS   B NZ   1 
ATOM   2126 N  N    . PRO   A 1 292 ? 5.15551   -31.64464 3.96341   1.000 50.71523  ? 1344 PRO   B N    1 
ATOM   2127 C  CA   . PRO   A 1 292 ? 3.82551   -31.39375 3.40335   1.000 51.95909  ? 1344 PRO   B CA   1 
ATOM   2128 C  C    . PRO   A 1 292 ? 2.76946   -32.28342 4.03974   1.000 51.53098  ? 1344 PRO   B C    1 
ATOM   2129 O  O    . PRO   A 1 292 ? 3.03038   -33.42329 4.43018   1.000 51.59484  ? 1344 PRO   B O    1 
ATOM   2130 C  CB   . PRO   A 1 292 ? 3.99444   -31.72036 1.91348   1.000 54.17852  ? 1344 PRO   B CB   1 
ATOM   2131 C  CG   . PRO   A 1 292 ? 5.47344   -31.69557 1.67143   1.000 47.17434  ? 1344 PRO   B CG   1 
ATOM   2132 C  CD   . PRO   A 1 292 ? 6.09844   -32.14711 2.95159   1.000 50.15880  ? 1344 PRO   B CD   1 
ATOM   2133 N  N    . ILE   A 1 293 ? 1.55651   -31.73929 4.13956   1.000 46.25069  ? 1345 ILE   B N    1 
ATOM   2134 C  CA   . ILE   A 1 293 ? 0.39046   -32.47901 4.61189   1.000 47.63855  ? 1345 ILE   B CA   1 
ATOM   2135 C  C    . ILE   A 1 293 ? -0.62159  -32.67637 3.48999   1.000 50.39703  ? 1345 ILE   B C    1 
ATOM   2136 O  O    . ILE   A 1 293 ? -1.00668  -33.80547 3.17945   1.000 57.97329  ? 1345 ILE   B O    1 
ATOM   2137 C  CB   . ILE   A 1 293 ? -0.25645  -31.78848 5.83363   1.000 47.24385  ? 1345 ILE   B CB   1 
ATOM   2138 C  CG1  . ILE   A 1 293 ? 0.70859   -31.77808 7.01860   1.000 44.86601  ? 1345 ILE   B CG1  1 
ATOM   2139 C  CG2  . ILE   A 1 293 ? -1.55849  -32.48323 6.20894   1.000 45.63359  ? 1345 ILE   B CG2  1 
ATOM   2140 C  CD1  . ILE   A 1 293 ? 0.13567   -31.12954 8.26236   1.000 37.71098  ? 1345 ILE   B CD1  1 
ATOM   2141 N  N    . ALA   A 1 294 ? -1.06252  -31.58559 2.86457   1.000 56.84631  ? 1346 ALA   B N    1 
ATOM   2142 C  CA   . ALA   A 1 294 ? -2.04156  -31.66094 1.79263   1.000 53.76414  ? 1346 ALA   B CA   1 
ATOM   2143 C  C    . ALA   A 1 294 ? -1.84549  -30.48632 0.84816   1.000 53.69540  ? 1346 ALA   B C    1 
ATOM   2144 O  O    . ALA   A 1 294 ? -1.36240  -29.42321 1.24473   1.000 48.04656  ? 1346 ALA   B O    1 
ATOM   2145 C  CB   . ALA   A 1 294 ? -3.47454  -31.67061 2.33768   1.000 56.34449  ? 1346 ALA   B CB   1 
ATOM   2146 N  N    . THR   A 1 295 ? -2.22255  -30.69379 -0.41074  1.000 58.40984  ? 1347 THR   B N    1 
ATOM   2147 C  CA   . THR   A 1 295 ? -2.21650  -29.65520 -1.43316  1.000 52.71365  ? 1347 THR   B CA   1 
ATOM   2148 C  C    . THR   A 1 295 ? -3.61951  -29.56132 -2.01315  1.000 52.57091  ? 1347 THR   B C    1 
ATOM   2149 O  O    . THR   A 1 295 ? -4.15660  -30.55747 -2.50574  1.000 54.24029  ? 1347 THR   B O    1 
ATOM   2150 C  CB   . THR   A 1 295 ? -1.19855  -29.96571 -2.53306  1.000 55.06250  ? 1347 THR   B CB   1 
ATOM   2151 O  OG1  . THR   A 1 295 ? 0.12446   -29.95560 -1.97811  1.000 61.66402  ? 1347 THR   B OG1  1 
ATOM   2152 C  CG2  . THR   A 1 295 ? -1.28751  -28.93715 -3.64847  1.000 47.86306  ? 1347 THR   B CG2  1 
ATOM   2153 N  N    . ILE   A 1 296 ? -4.21741  -28.37325 -1.95160  1.000 49.09540  ? 1348 ILE   B N    1 
ATOM   2154 C  CA   . ILE   A 1 296 ? -5.58341  -28.15532 -2.40365  1.000 50.63860  ? 1348 ILE   B CA   1 
ATOM   2155 C  C    . ILE   A 1 296 ? -5.54737  -27.16278 -3.55104  1.000 47.50033  ? 1348 ILE   B C    1 
ATOM   2156 O  O    . ILE   A 1 296 ? -5.15827  -26.00073 -3.36152  1.000 47.29411  ? 1348 ILE   B O    1 
ATOM   2157 C  CB   . ILE   A 1 296 ? -6.48934  -27.64280 -1.27283  1.000 51.86160  ? 1348 ILE   B CB   1 
ATOM   2158 C  CG1  . ILE   A 1 296 ? -6.48038  -28.61534 -0.09344  1.000 60.32329  ? 1348 ILE   B CG1  1 
ATOM   2159 C  CG2  . ILE   A 1 296 ? -7.90233  -27.43189 -1.77987  1.000 47.59242  ? 1348 ILE   B CG2  1 
ATOM   2160 C  CD1  . ILE   A 1 296 ? -6.94750  -30.01444 -0.44887  1.000 62.13559  ? 1348 ILE   B CD1  1 
ATOM   2161 N  N    . ASP   A 1 297 ? -5.94144  -27.61622 -4.73685  1.000 44.82575  ? 1349 ASP   B N    1 
ATOM   2162 C  CA   . ASP   A 1 297 ? -6.10640  -26.75467 -5.90419  1.000 46.30684  ? 1349 ASP   B CA   1 
ATOM   2163 C  C    . ASP   A 1 297 ? -7.60539  -26.56663 -6.10222  1.000 53.80172  ? 1349 ASP   B C    1 
ATOM   2164 O  O    . ASP   A 1 297 ? -8.29048  -27.46477 -6.59384  1.000 44.64898  ? 1349 ASP   B O    1 
ATOM   2165 C  CB   . ASP   A 1 297 ? -5.44849  -27.36321 -7.13797  1.000 47.25574  ? 1349 ASP   B CB   1 
ATOM   2166 C  CG   . ASP   A 1 297 ? -5.33444  -26.37367 -8.28836  1.000 50.18286  ? 1349 ASP   B CG   1 
ATOM   2167 O  OD1  . ASP   A 1 297 ? -6.09137  -25.38162 -8.30073  1.000 47.77339  ? 1349 ASP   B OD1  1 
ATOM   2168 O  OD2  . ASP   A 1 297 ? -4.48549  -26.58509 -9.18030  1.000 61.08112  ? 1349 ASP   B OD2  1 
ATOM   2169 N  N    . VAL   A 1 298 ? -8.11329  -25.39443 -5.70667  1.000 43.36092  ? 1350 VAL   B N    1 
ATOM   2170 C  CA   . VAL   A 1 298 ? -9.54227  -25.10737 -5.82474  1.000 41.34033  ? 1350 VAL   B CA   1 
ATOM   2171 C  C    . VAL   A 1 298 ? -9.94928  -24.72289 -7.23588  1.000 44.46963  ? 1350 VAL   B C    1 
ATOM   2172 O  O    . VAL   A 1 298 ? -11.14027 -24.49090 -7.48394  1.000 47.88202  ? 1350 VAL   B O    1 
ATOM   2173 C  CB   . VAL   A 1 298 ? -9.96716  -23.98595 -4.85317  1.000 45.17791  ? 1350 VAL   B CB   1 
ATOM   2174 C  CG1  . VAL   A 1 298 ? -9.81615  -24.45239 -3.41299  1.000 41.01823  ? 1350 VAL   B CG1  1 
ATOM   2175 C  CG2  . VAL   A 1 298 ? -9.14607  -22.73111 -5.09969  1.000 41.80388  ? 1350 VAL   B CG2  1 
ATOM   2176 N  N    . LYS   A 1 299 ? -9.00331  -24.65134 -8.16994  1.000 44.72668  ? 1351 LYS   B N    1 
ATOM   2177 C  CA   . LYS   A 1 299 ? -9.25232  -24.32787 -9.57006  1.000 45.56325  ? 1351 LYS   B CA   1 
ATOM   2178 C  C    . LYS   A 1 299 ? -9.75522  -22.90491 -9.76461  1.000 43.40022  ? 1351 LYS   B C    1 
ATOM   2179 O  O    . LYS   A 1 299 ? -10.23922 -22.56830 -10.85173 1.000 51.24572  ? 1351 LYS   B O    1 
ATOM   2180 C  CB   . LYS   A 1 299 ? -10.23942 -25.31105 -10.20564 1.000 43.72276  ? 1351 LYS   B CB   1 
ATOM   2181 C  CG   . LYS   A 1 299 ? -9.82353  -26.76803 -10.07808 1.000 44.96646  ? 1351 LYS   B CG   1 
ATOM   2182 C  CD   . LYS   A 1 299 ? -8.45656  -27.01038 -10.69702 1.000 48.53555  ? 1351 LYS   B CD   1 
ATOM   2183 C  CE   . LYS   A 1 299 ? -8.06368  -28.47938 -10.61445 1.000 60.36370  ? 1351 LYS   B CE   1 
ATOM   2184 N  NZ   . LYS   A 1 299 ? -6.71171  -28.72571 -11.19239 1.000 61.96260  ? 1351 LYS   B NZ   1 
ATOM   2185 N  N    . ARG   A 1 300 ? -9.66312  -22.06451 -8.73894  1.000 42.81946  ? 1352 ARG   B N    1 
ATOM   2186 C  CA   . ARG   A 1 300 ? -10.02402 -20.65752 -8.82849  1.000 36.75780  ? 1352 ARG   B CA   1 
ATOM   2187 C  C    . ARG   A 1 300 ? -8.96693  -19.84531 -8.09984  1.000 39.44377  ? 1352 ARG   B C    1 
ATOM   2188 O  O    . ARG   A 1 300 ? -8.52593  -20.22992 -7.01470  1.000 39.00254  ? 1352 ARG   B O    1 
ATOM   2189 C  CB   . ARG   A 1 300 ? -11.40598 -20.38617 -8.21755  1.000 34.59598  ? 1352 ARG   B CB   1 
ATOM   2190 C  CG   . ARG   A 1 300 ? -12.54905 -21.11035 -8.91023  1.000 38.06023  ? 1352 ARG   B CG   1 
ATOM   2191 C  CD   . ARG   A 1 300 ? -13.83102 -21.03293 -8.09823  1.000 43.18229  ? 1352 ARG   B CD   1 
ATOM   2192 N  NE   . ARG   A 1 300 ? -13.78906 -21.89847 -6.92589  1.000 40.66551  ? 1352 ARG   B NE   1 
ATOM   2193 C  CZ   . ARG   A 1 300 ? -14.12416 -23.18145 -6.93537  1.000 47.27286  ? 1352 ARG   B CZ   1 
ATOM   2194 N  NH1  . ARG   A 1 300 ? -14.51724 -23.78486 -8.04512  1.000 41.31386  ? 1352 ARG   B NH1  1 
ATOM   2195 N  NH2  . ARG   A 1 300 ? -14.06118 -23.87501 -5.80209  1.000 35.04813  ? 1352 ARG   B NH2  1 
ATOM   2196 N  N    . ASN   A 1 301 ? -8.56286  -18.72658 -8.69529  1.000 36.59836  ? 1353 ASN   B N    1 
ATOM   2197 C  CA   . ASN   A 1 301 ? -7.55878  -17.88541 -8.06266  1.000 36.46651  ? 1353 ASN   B CA   1 
ATOM   2198 C  C    . ASN   A 1 301 ? -8.02170  -17.46882 -6.67281  1.000 37.90079  ? 1353 ASN   B C    1 
ATOM   2199 O  O    . ASN   A 1 301 ? -9.17467  -17.07565 -6.47393  1.000 40.76245  ? 1353 ASN   B O    1 
ATOM   2200 C  CB   . ASN   A 1 301 ? -7.27271  -16.65577 -8.92115  1.000 31.31053  ? 1353 ASN   B CB   1 
ATOM   2201 C  CG   . ASN   A 1 301 ? -6.49577  -16.99232 -10.17204 1.000 39.32684  ? 1353 ASN   B CG   1 
ATOM   2202 O  OD1  . ASN   A 1 301 ? -5.80285  -18.00840 -10.22666 1.000 43.66473  ? 1353 ASN   B OD1  1 
ATOM   2203 N  ND2  . ASN   A 1 301 ? -6.59973  -16.13672 -11.18538 1.000 47.06457  ? 1353 ASN   B ND2  1 
ATOM   2204 N  N    . ILE   A 1 302 ? -7.11868  -17.56851 -5.71180  1.000 31.54993  ? 1354 ILE   B N    1 
ATOM   2205 C  CA   . ILE   A 1 302 ? -7.41662  -17.27694 -4.31890  1.000 34.06196  ? 1354 ILE   B CA   1 
ATOM   2206 C  C    . ILE   A 1 302 ? -7.09150  -15.81885 -4.02949  1.000 40.48758  ? 1354 ILE   B C    1 
ATOM   2207 O  O    . ILE   A 1 302 ? -6.09347  -15.27912 -4.52173  1.000 35.60889  ? 1354 ILE   B O    1 
ATOM   2208 C  CB   . ILE   A 1 302 ? -6.63667  -18.21963 -3.38555  1.000 33.26868  ? 1354 ILE   B CB   1 
ATOM   2209 C  CG1  . ILE   A 1 302 ? -7.05979  -19.67269 -3.62896  1.000 40.06521  ? 1354 ILE   B CG1  1 
ATOM   2210 C  CG2  . ILE   A 1 302 ? -6.83159  -17.82704 -1.93470  1.000 32.85101  ? 1354 ILE   B CG2  1 
ATOM   2211 C  CD1  . ILE   A 1 302 ? -6.28284  -20.68243 -2.81259  1.000 37.41133  ? 1354 ILE   B CD1  1 
ATOM   2212 N  N    . PHE   A 1 303 ? -7.94442  -15.17447 -3.23672  1.000 31.30524  ? 1355 PHE   B N    1 
ATOM   2213 C  CA   . PHE   A 1 303 ? -7.71031  -13.80931 -2.78927  1.000 35.54502  ? 1355 PHE   B CA   1 
ATOM   2214 C  C    . PHE   A 1 303 ? -7.25926  -13.72577 -1.33931  1.000 32.67319  ? 1355 PHE   B C    1 
ATOM   2215 O  O    . PHE   A 1 303 ? -6.50418  -12.81369 -0.98870  1.000 35.31613  ? 1355 PHE   B O    1 
ATOM   2216 C  CB   . PHE   A 1 303 ? -8.97724  -12.96528 -2.96256  1.000 32.96739  ? 1355 PHE   B CB   1 
ATOM   2217 C  CG   . PHE   A 1 303 ? -9.05323  -12.24979 -4.27884  1.000 37.35107  ? 1355 PHE   B CG   1 
ATOM   2218 C  CD1  . PHE   A 1 303 ? -9.25732  -12.94924 -5.45556  1.000 38.15151  ? 1355 PHE   B CD1  1 
ATOM   2219 C  CD2  . PHE   A 1 303 ? -8.92812  -10.87183 -4.33839  1.000 31.44921  ? 1355 PHE   B CD2  1 
ATOM   2220 C  CE1  . PHE   A 1 303 ? -9.33230  -12.28772 -6.66982  1.000 39.37280  ? 1355 PHE   B CE1  1 
ATOM   2221 C  CE2  . PHE   A 1 303 ? -8.99911  -10.20430 -5.54565  1.000 38.28199  ? 1355 PHE   B CE2  1 
ATOM   2222 C  CZ   . PHE   A 1 303 ? -9.20220  -10.91374 -6.71337  1.000 37.22141  ? 1355 PHE   B CZ   1 
ATOM   2223 N  N    . ASP   A 1 304 ? -7.69230  -14.65940 -0.49593  1.000 33.33931  ? 1356 ASP   B N    1 
ATOM   2224 C  CA   . ASP   A 1 304 ? -7.40326  -14.59886 0.93104   1.000 33.81900  ? 1356 ASP   B CA   1 
ATOM   2225 C  C    . ASP   A 1 304 ? -7.96334  -15.85756 1.57655   1.000 34.43898  ? 1356 ASP   B C    1 
ATOM   2226 O  O    . ASP   A 1 304 ? -8.81241  -16.54272 0.99985   1.000 34.76044  ? 1356 ASP   B O    1 
ATOM   2227 C  CB   . ASP   A 1 304 ? -8.01314  -13.34856 1.57456   1.000 30.18123  ? 1356 ASP   B CB   1 
ATOM   2228 C  CG   . ASP   A 1 304 ? -7.38608  -13.01308 2.91241   1.000 34.01098  ? 1356 ASP   B CG   1 
ATOM   2229 O  OD1  . ASP   A 1 304 ? -6.33911  -13.60703 3.24261   1.000 38.92792  ? 1356 ASP   B OD1  1 
ATOM   2230 O  OD2  . ASP   A 1 304 ? -7.94099  -12.15375 3.63109   1.000 33.77796  ? 1356 ASP   B OD2  1 
ATOM   2231 N  N    . LEU   A 1 305 ? -7.47632  -16.15712 2.77666   1.000 38.72875  ? 1357 LEU   B N    1 
ATOM   2232 C  CA   . LEU   A 1 305 ? -8.06438  -17.22976 3.56910   1.000 38.80952  ? 1357 LEU   B CA   1 
ATOM   2233 C  C    . LEU   A 1 305 ? -7.69832  -17.02321 5.03101   1.000 42.50903  ? 1357 LEU   B C    1 
ATOM   2234 O  O    . LEU   A 1 305 ? -6.71026  -16.36516 5.36172   1.000 31.92965  ? 1357 LEU   B O    1 
ATOM   2235 C  CB   . LEU   A 1 305 ? -7.62851  -18.61799 3.07564   1.000 36.85677  ? 1357 LEU   B CB   1 
ATOM   2236 C  CG   . LEU   A 1 305 ? -6.22854  -19.18501 3.30682   1.000 41.39005  ? 1357 LEU   B CG   1 
ATOM   2237 C  CD1  . LEU   A 1 305 ? -6.02553  -19.61445 4.75498   1.000 39.53673  ? 1357 LEU   B CD1  1 
ATOM   2238 C  CD2  . LEU   A 1 305 ? -5.99166  -20.36240 2.36828   1.000 39.79963  ? 1357 LEU   B CD2  1 
ATOM   2239 N  N    . CYS   A 1 306 ? -8.52934  -17.59281 5.89826   1.000 41.05361  ? 1358 CYS   B N    1 
ATOM   2240 C  CA   . CYS   A 1 306 ? -8.37829  -17.41625 7.33518   1.000 36.97891  ? 1358 CYS   B CA   1 
ATOM   2241 C  C    . CYS   A 1 306 ? -9.05336  -18.58292 8.04466   1.000 42.40097  ? 1358 CYS   B C    1 
ATOM   2242 O  O    . CYS   A 1 306 ? -9.77644  -19.36910 7.43400   1.000 43.46991  ? 1358 CYS   B O    1 
ATOM   2243 C  CB   . CYS   A 1 306 ? -8.97317  -16.07802 7.79767   1.000 41.50614  ? 1358 CYS   B CB   1 
ATOM   2244 S  SG   . CYS   A 1 306 ? -10.76417 -15.92099 7.51566   1.000 38.71495  ? 1358 CYS   B SG   1 
ATOM   2245 N  N    . THR   A 1 307 ? -8.79233  -18.68442 9.34670   1.000 38.25159  ? 1359 THR   B N    1 
ATOM   2246 C  CA   . THR   A 1 307 ? -9.45838  -19.65303 10.20310  1.000 42.04650  ? 1359 THR   B CA   1 
ATOM   2247 C  C    . THR   A 1 307 ? -9.99729  -18.94250 11.43883  1.000 45.04513  ? 1359 THR   B C    1 
ATOM   2248 O  O    . THR   A 1 307 ? -9.59019  -17.82440 11.76538  1.000 46.63013  ? 1359 THR   B O    1 
ATOM   2249 C  CB   . THR   A 1 307 ? -8.52345  -20.79594 10.62552  1.000 41.14404  ? 1359 THR   B CB   1 
ATOM   2250 O  OG1  . THR   A 1 307 ? -7.43939  -20.26871 11.39928  1.000 50.31673  ? 1359 THR   B OG1  1 
ATOM   2251 C  CG2  . THR   A 1 307 ? -7.97055  -21.51846 9.40479   1.000 44.25489  ? 1359 THR   B CG2  1 
ATOM   2252 N  N    . ASP   A 1 308 ? -10.93132 -19.60216 12.11512  1.000 44.64177  ? 1360 ASP   B N    1 
ATOM   2253 C  CA   . ASP   A 1 308 ? -11.49424 -19.06463 13.34193  1.000 44.96907  ? 1360 ASP   B CA   1 
ATOM   2254 C  C    . ASP   A 1 308 ? -10.57423 -19.36523 14.52402  1.000 46.64002  ? 1360 ASP   B C    1 
ATOM   2255 O  O    . ASP   A 1 308 ? -9.62129  -20.14235 14.42730  1.000 41.86801  ? 1360 ASP   B O    1 
ATOM   2256 C  CB   . ASP   A 1 308 ? -12.88428 -19.64342 13.59720  1.000 51.85153  ? 1360 ASP   B CB   1 
ATOM   2257 C  CG   . ASP   A 1 308 ? -12.85338 -21.13732 13.84879  1.000 42.90939  ? 1360 ASP   B CG   1 
ATOM   2258 O  OD1  . ASP   A 1 308 ? -12.23546 -21.86369 13.04306  1.000 47.79749  ? 1360 ASP   B OD1  1 
ATOM   2259 O  OD2  . ASP   A 1 308 ? -13.43939 -21.58188 14.85898  1.000 53.10291  ? 1360 ASP   B OD2  1 
ATOM   2260 N  N    . THR   A 1 309 ? -10.86514 -18.73576 15.65778  1.000 43.91556  ? 1361 THR   B N    1 
ATOM   2261 C  CA   . THR   A 1 309 ? -10.02712 -18.91435 16.85882  1.000 46.77604  ? 1361 THR   B CA   1 
ATOM   2262 C  C    . THR   A 1 309 ? -9.93423  -20.37421 17.23740  1.000 49.31269  ? 1361 THR   B C    1 
ATOM   2263 O  O    . THR   A 1 309 ? -8.85524  -20.78212 17.67753  1.000 55.40323  ? 1361 THR   B O    1 
ATOM   2264 C  CB   . THR   A 1 309 ? -10.61503 -18.08586 17.99651  1.000 48.27298  ? 1361 THR   B CB   1 
ATOM   2265 O  OG1  . THR   A 1 309 ? -11.98305 -18.47072 18.06971  1.000 58.96858  ? 1361 THR   B OG1  1 
ATOM   2266 C  CG2  . THR   A 1 309 ? -10.49292 -16.59496 17.74892  1.000 45.38320  ? 1361 THR   B CG2  1 
ATOM   2267 N  N    . LYS   A 1 310 ? -11.00529 -21.14420 17.05974  1.000 49.86468  ? 1362 LYS   B N    1 
ATOM   2268 C  CA   . LYS   A 1 310 ? -11.00039 -22.55401 17.53829  1.000 52.57657  ? 1362 LYS   B CA   1 
ATOM   2269 C  C    . LYS   A 1 310 ? -10.52649 -23.50148 16.43665  1.000 53.68452  ? 1362 LYS   B C    1 
ATOM   2270 O  O    . LYS   A 1 310 ? -10.61258 -24.72339 16.65414  1.000 49.64224  ? 1362 LYS   B O    1 
ATOM   2271 C  CB   . LYS   A 1 310 ? -12.37540 -22.97969 18.05750  1.000 54.74077  ? 1362 LYS   B CB   1 
ATOM   2272 C  CG   . LYS   A 1 310 ? -12.83431 -22.27516 19.32524  1.000 66.38926  ? 1362 LYS   B CG   1 
ATOM   2273 C  CD   . LYS   A 1 310 ? -14.21533 -22.70786 19.79645  1.000 75.60041  ? 1362 LYS   B CD   1 
ATOM   2274 C  CE   . LYS   A 1 310 ? -14.64024 -22.02233 21.05719  1.000 83.81124  ? 1362 LYS   B CE   1 
ATOM   2275 N  NZ   . LYS   A 1 310 ? -15.98126 -22.44506 21.46840  1.000 83.65067  ? 1362 LYS   B NZ   1 
ATOM   2276 N  N    . ASP   A 1 311 ? -10.08648 -22.95896 15.30543  1.000 53.18576  ? 1363 ASP   B N    1 
ATOM   2277 C  CA   . ASP   A 1 311 ? -9.50458  -23.78643 14.24874  1.000 49.21746  ? 1363 ASP   B CA   1 
ATOM   2278 C  C    . ASP   A 1 311 ? -10.49367 -24.83655 13.75118  1.000 47.29814  ? 1363 ASP   B C    1 
ATOM   2279 O  O    . ASP   A 1 311 ? -10.12477 -25.97669 13.46362  1.000 52.23942  ? 1363 ASP   B O    1 
ATOM   2280 C  CB   . ASP   A 1 311 ? -8.20762  -24.45134 14.71896  1.000 48.15790  ? 1363 ASP   B CB   1 
ATOM   2281 C  CG   . ASP   A 1 311 ? -7.11953  -23.44630 15.03853  1.000 55.02222  ? 1363 ASP   B CG   1 
ATOM   2282 O  OD1  . ASP   A 1 311 ? -6.98547  -22.45561 14.28714  1.000 49.38878  ? 1363 ASP   B OD1  1 
ATOM   2283 O  OD2  . ASP   A 1 311 ? -6.40151  -23.64296 16.04359  1.000 62.63306  ? 1363 ASP   B OD2  1 
ATOM   2284 N  N    . CYS   A 1 312 ? -11.76365 -24.45349 13.64807  1.000 47.64534  ? 1364 CYS   B N    1 
ATOM   2285 C  CA   . CYS   A 1 312 ? -12.77573 -25.36062 13.11946  1.000 46.06722  ? 1364 CYS   B CA   1 
ATOM   2286 C  C    . CYS   A 1 312 ? -12.99176 -25.17619 11.62339  1.000 45.12498  ? 1364 CYS   B C    1 
ATOM   2287 O  O    . CYS   A 1 312 ? -13.22886 -26.15646 10.90978  1.000 47.57420  ? 1364 CYS   B O    1 
ATOM   2288 C  CB   . CYS   A 1 312 ? -14.10070 -25.16822 13.85842  1.000 54.72626  ? 1364 CYS   B CB   1 
ATOM   2289 S  SG   . CYS   A 1 312 ? -14.11069 -25.74755 15.56665  1.000 67.39088  ? 1364 CYS   B SG   1 
ATOM   2290 N  N    . TYR   A 1 313 ? -12.89468 -23.94340 11.13090  1.000 44.87692  ? 1365 TYR   B N    1 
ATOM   2291 C  CA   . TYR   A 1 313 ? -13.26170 -23.63391 9.75779   1.000 44.31006  ? 1365 TYR   B CA   1 
ATOM   2292 C  C    . TYR   A 1 313 ? -12.13366 -22.89928 9.04346   1.000 47.13658  ? 1365 TYR   B C    1 
ATOM   2293 O  O    . TYR   A 1 313 ? -11.29559 -22.23710 9.65818   1.000 44.93251  ? 1365 TYR   B O    1 
ATOM   2294 C  CB   . TYR   A 1 313 ? -14.53564 -22.78584 9.69249   1.000 42.49936  ? 1365 TYR   B CB   1 
ATOM   2295 C  CG   . TYR   A 1 313 ? -15.72966 -23.42248 10.36078  1.000 50.10375  ? 1365 TYR   B CG   1 
ATOM   2296 C  CD1  . TYR   A 1 313 ? -16.39876 -24.48366 9.76722   1.000 43.89625  ? 1365 TYR   B CD1  1 
ATOM   2297 C  CD2  . TYR   A 1 313 ? -16.19559 -22.95396 11.58160  1.000 49.44385  ? 1365 TYR   B CD2  1 
ATOM   2298 C  CE1  . TYR   A 1 313 ? -17.49279 -25.06634 10.37448  1.000 49.85772  ? 1365 TYR   B CE1  1 
ATOM   2299 C  CE2  . TYR   A 1 313 ? -17.28762 -23.53163 12.19787  1.000 47.43743  ? 1365 TYR   B CE2  1 
ATOM   2300 C  CZ   . TYR   A 1 313 ? -17.93372 -24.58682 11.58930  1.000 45.76114  ? 1365 TYR   B CZ   1 
ATOM   2301 O  OH   . TYR   A 1 313 ? -19.02475 -25.16150 12.19856  1.000 58.59624  ? 1365 TYR   B OH   1 
ATOM   2302 N  N    . LEU   A 1 314 ? -12.14871 -23.02780 7.71951   1.000 43.21343  ? 1366 LEU   B N    1 
ATOM   2303 C  CA   . LEU   A 1 314 ? -11.24768 -22.31723 6.82021   1.000 40.74324  ? 1366 LEU   B CA   1 
ATOM   2304 C  C    . LEU   A 1 314 ? -12.10365 -21.54756 5.82293   1.000 43.94692  ? 1366 LEU   B C    1 
ATOM   2305 O  O    . LEU   A 1 314 ? -12.82072 -22.15182 5.01819   1.000 39.76870  ? 1366 LEU   B O    1 
ATOM   2306 C  CB   . LEU   A 1 314 ? -10.30778 -23.28959 6.10656   1.000 40.40926  ? 1366 LEU   B CB   1 
ATOM   2307 C  CG   . LEU   A 1 314 ? -9.29376  -22.69305 5.13130   1.000 45.43008  ? 1366 LEU   B CG   1 
ATOM   2308 C  CD1  . LEU   A 1 314 ? -8.24268  -21.88484 5.87895   1.000 46.78359  ? 1366 LEU   B CD1  1 
ATOM   2309 C  CD2  . LEU   A 1 314 ? -8.64087  -23.78643 4.28871   1.000 43.71716  ? 1366 LEU   B CD2  1 
ATOM   2310 N  N    . ALA   A 1 315 ? -12.05155 -20.22254 5.88540   1.000 40.30983  ? 1367 ALA   B N    1 
ATOM   2311 C  CA   . ALA   A 1 315 ? -12.74351 -19.36986 4.92808   1.000 37.75471  ? 1367 ALA   B CA   1 
ATOM   2312 C  C    . ALA   A 1 315 ? -11.76651 -18.95937 3.83789   1.000 41.36883  ? 1367 ALA   B C    1 
ATOM   2313 O  O    . ALA   A 1 315 ? -10.64947 -18.52434 4.13569   1.000 35.16495  ? 1367 ALA   B O    1 
ATOM   2314 C  CB   . ALA   A 1 315 ? -13.33339 -18.13855 5.61361   1.000 35.56741  ? 1367 ALA   B CB   1 
ATOM   2315 N  N    . VAL   A 1 316 ? -12.18556 -19.09684 2.57896   1.000 36.45482  ? 1368 VAL   B N    1 
ATOM   2316 C  CA   . VAL   A 1 316 ? -11.33157 -18.85236 1.42584   1.000 34.36373  ? 1368 VAL   B CA   1 
ATOM   2317 C  C    . VAL   A 1 316 ? -12.10454 -18.01570 0.41653   1.000 39.02233  ? 1368 VAL   B C    1 
ATOM   2318 O  O    . VAL   A 1 316 ? -13.24857 -18.34174 0.08469   1.000 35.43254  ? 1368 VAL   B O    1 
ATOM   2319 C  CB   . VAL   A 1 316 ? -10.85769 -20.16565 0.77434   1.000 38.12534  ? 1368 VAL   B CB   1 
ATOM   2320 C  CG1  . VAL   A 1 316 ? -9.82270  -19.88216 -0.30680  1.000 37.86203  ? 1368 VAL   B CG1  1 
ATOM   2321 C  CG2  . VAL   A 1 316 ? -10.30874 -21.11828 1.82170   1.000 38.22158  ? 1368 VAL   B CG2  1 
ATOM   2322 N  N    . ILE   A 1 317 ? -11.48947 -16.94094 -0.06391  1.000 37.87491  ? 1369 ILE   B N    1 
ATOM   2323 C  CA   . ILE   A 1 317 ? -12.06644 -16.12731 -1.12822  1.000 32.22713  ? 1369 ILE   B CA   1 
ATOM   2324 C  C    . ILE   A 1 317 ? -11.52152 -16.63888 -2.45803  1.000 33.05180  ? 1369 ILE   B C    1 
ATOM   2325 O  O    . ILE   A 1 317 ? -10.30852 -16.61807 -2.69108  1.000 32.50932  ? 1369 ILE   B O    1 
ATOM   2326 C  CB   . ILE   A 1 317 ? -11.74732 -14.63926 -0.93482  1.000 37.25850  ? 1369 ILE   B CB   1 
ATOM   2327 C  CG1  . ILE   A 1 317 ? -12.19524 -14.16868 0.44901   1.000 37.96148  ? 1369 ILE   B CG1  1 
ATOM   2328 C  CG2  . ILE   A 1 317 ? -12.42028 -13.81064 -2.02013  1.000 36.00539  ? 1369 ILE   B CG2  1 
ATOM   2329 C  CD1  . ILE   A 1 317 ? -13.67324 -14.33946 0.70412   1.000 41.53277  ? 1369 ILE   B CD1  1 
ATOM   2330 N  N    . GLU   A 1 318 ? -12.41858 -17.09616 -3.32883  1.000 29.50440  ? 1370 GLU   B N    1 
ATOM   2331 C  CA   . GLU   A 1 318 ? -12.04766 -17.71768 -4.59059  1.000 31.56251  ? 1370 GLU   B CA   1 
ATOM   2332 C  C    . GLU   A 1 318 ? -12.75764 -17.00408 -5.73085  1.000 37.56504  ? 1370 GLU   B C    1 
ATOM   2333 O  O    . GLU   A 1 318 ? -13.96862 -16.78096 -5.66391  1.000 43.13153  ? 1370 GLU   B O    1 
ATOM   2334 C  CB   . GLU   A 1 318 ? -12.40878 -19.20566 -4.58899  1.000 29.51429  ? 1370 GLU   B CB   1 
ATOM   2335 C  CG   . GLU   A 1 318 ? -12.03080 -19.92918 -3.30372  1.000 34.61408  ? 1370 GLU   B CG   1 
ATOM   2336 C  CD   . GLU   A 1 318 ? -12.52491 -21.36313 -3.27613  1.000 39.52468  ? 1370 GLU   B CD   1 
ATOM   2337 O  OE1  . GLU   A 1 318 ? -13.14097 -21.79947 -4.27294  1.000 41.61548  ? 1370 GLU   B OE1  1 
ATOM   2338 O  OE2  . GLU   A 1 318 ? -12.29793 -22.04674 -2.25587  1.000 40.86794  ? 1370 GLU   B OE2  1 
ATOM   2339 N  N    . ASN   A 1 319 ? -12.01164 -16.65355 -6.77501  1.000 33.33018  ? 1371 ASN   B N    1 
ATOM   2340 C  CA   . ASN   A 1 319 ? -12.57562 -15.93296 -7.90728  1.000 37.26083  ? 1371 ASN   B CA   1 
ATOM   2341 C  C    . ASN   A 1 319 ? -13.01773 -16.91735 -8.98088  1.000 36.38427  ? 1371 ASN   B C    1 
ATOM   2342 O  O    . ASN   A 1 319 ? -12.19580 -17.67262 -9.51460  1.000 39.26632  ? 1371 ASN   B O    1 
ATOM   2343 C  CB   . ASN   A 1 319 ? -11.56456 -14.94426 -8.48170  1.000 36.76148  ? 1371 ASN   B CB   1 
ATOM   2344 C  CG   . ASN   A 1 319 ? -12.10554 -14.19470 -9.68498  1.000 42.17192  ? 1371 ASN   B CG   1 
ATOM   2345 O  OD1  . ASN   A 1 319 ? -13.28451 -13.84862 -9.73309  1.000 41.82065  ? 1371 ASN   B OD1  1 
ATOM   2346 N  ND2  . ASN   A 1 319 ? -11.24855 -13.95515 -10.67310 1.000 42.03496  ? 1371 ASN   B ND2  1 
ATOM   2347 N  N    . GLN   A 1 320 ? -14.30874 -16.91237 -9.29284  1.000 33.82050  ? 1372 GLN   B N    1 
ATOM   2348 C  CA   . GLN   A 1 320 ? -14.83483 -17.59079 -10.46456 1.000 45.43694  ? 1372 GLN   B CA   1 
ATOM   2349 C  C    . GLN   A 1 320 ? -14.94278 -16.60224 -11.61795 1.000 43.59309  ? 1372 GLN   B C    1 
ATOM   2350 O  O    . GLN   A 1 320 ? -14.91268 -15.38317 -11.42943 1.000 54.02450  ? 1372 GLN   B O    1 
ATOM   2351 C  CB   . GLN   A 1 320 ? -16.20186 -18.21057 -10.15927 1.000 45.21436  ? 1372 GLN   B CB   1 
ATOM   2352 C  CG   . GLN   A 1 320 ? -17.17777 -17.24523 -9.50163  1.000 47.29304  ? 1372 GLN   B CG   1 
ATOM   2353 C  CD   . GLN   A 1 320 ? -18.53881 -17.87102 -9.24534  1.000 43.84885  ? 1372 GLN   B CD   1 
ATOM   2354 O  OE1  . GLN   A 1 320 ? -18.64189 -19.05088 -8.91087  1.000 43.97412  ? 1372 GLN   B OE1  1 
ATOM   2355 N  NE2  . GLN   A 1 320 ? -19.59075 -17.07901 -9.41062  1.000 37.30047  ? 1372 GLN   B NE2  1 
ATOM   2356 N  N    . GLY   A 1 321 ? -15.06386 -17.13871 -12.82773 1.000 60.19834  ? 1373 GLY   B N    1 
ATOM   2357 C  CA   . GLY   A 1 321 ? -15.21483 -16.28916 -13.99306 1.000 79.42148  ? 1373 GLY   B CA   1 
ATOM   2358 C  C    . GLY   A 1 321 ? -14.28389 -16.63368 -15.13696 1.000 78.58276  ? 1373 GLY   B C    1 
ATOM   2359 O  O    . GLY   A 1 321 ? -14.00799 -17.81081 -15.38850 1.000 81.85390  ? 1373 GLY   B O    1 
ATOM   2360 N  N    . SER   A 1 322 ? -13.78883 -15.61600 -15.83637 1.000 85.00282  ? 1374 SER   B N    1 
ATOM   2361 C  CA   . SER   A 1 322 ? -12.94388 -15.82853 -17.00231 1.000 90.75854  ? 1374 SER   B CA   1 
ATOM   2362 C  C    . SER   A 1 322 ? -12.26679 -14.51672 -17.36085 1.000 92.54506  ? 1374 SER   B C    1 
ATOM   2363 O  O    . SER   A 1 322 ? -12.72169 -13.43653 -16.96927 1.000 90.19834  ? 1374 SER   B O    1 
ATOM   2364 C  CB   . SER   A 1 322 ? -13.75496 -16.35493 -18.19108 1.000 92.76043  ? 1374 SER   B CB   1 
ATOM   2365 O  OG   . SER   A 1 322 ? -14.28005 -17.64379 -17.91856 1.000 105.50212 ? 1374 SER   B OG   1 
ATOM   2366 N  N    . MET   A 1 323 ? -11.16682 -14.62510 -18.11384 1.000 94.70660  ? 1375 MET   B N    1 
ATOM   2367 C  CA   . MET   A 1 323 ? -10.53574 -13.43437 -18.67333 1.000 89.30259  ? 1375 MET   B CA   1 
ATOM   2368 C  C    . MET   A 1 323 ? -11.55270 -12.56458 -19.39765 1.000 89.34583  ? 1375 MET   B C    1 
ATOM   2369 O  O    . MET   A 1 323 ? -11.41260 -11.33661 -19.42914 1.000 83.61011  ? 1375 MET   B O    1 
ATOM   2370 C  CB   . MET   A 1 323 ? -9.41080  -13.83484 -19.62821 1.000 92.02779  ? 1375 MET   B CB   1 
ATOM   2371 C  CG   . MET   A 1 323 ? -9.75892  -15.01617 -20.52073 1.000 96.67355  ? 1375 MET   B CG   1 
ATOM   2372 S  SD   . MET   A 1 323 ? -8.91696  -14.97286 -22.11277 1.000 105.21359 ? 1375 MET   B SD   1 
ATOM   2373 C  CE   . MET   A 1 323 ? -10.26496 -14.48418 -23.18792 1.000 86.25061  ? 1375 MET   B CE   1 
ATOM   2374 N  N    . ASP   A 1 324 ? -12.58176 -13.19672 -19.95537 1.000 91.11222  ? 1376 ASP   B N    1 
ATOM   2375 C  CA   . ASP   A 1 324 ? -13.67572 -12.41288 -20.57564 1.000 86.42848  ? 1376 ASP   B CA   1 
ATOM   2376 C  C    . ASP   A 1 324 ? -14.08961 -11.31746 -19.59707 1.000 84.89379  ? 1376 ASP   B C    1 
ATOM   2377 O  O    . ASP   A 1 324 ? -14.32353 -10.17762 -20.04051 1.000 78.67134  ? 1376 ASP   B O    1 
ATOM   2378 C  CB   . ASP   A 1 324 ? -14.86780 -13.29991 -20.87326 1.000 80.99451  ? 1376 ASP   B CB   1 
ATOM   2379 C  CG   . ASP   A 1 324 ? -14.53292 -14.59222 -21.59776 1.000 99.86738  ? 1376 ASP   B CG   1 
ATOM   2380 O  OD1  . ASP   A 1 324 ? -13.94895 -14.51070 -22.69681 1.000 103.75646 ? 1376 ASP   B OD1  1 
ATOM   2381 O  OD2  . ASP   A 1 324 ? -14.85699 -15.66898 -21.05532 1.000 98.54219  ? 1376 ASP   B OD2  1 
ATOM   2382 N  N    . ALA   A 1 325 ? -14.12959 -11.64595 -18.30893 1.000 77.55553  ? 1377 ALA   B N    1 
ATOM   2383 C  CA   . ALA   A 1 325 ? -14.63349 -10.67052 -17.32331 1.000 71.39448  ? 1377 ALA   B CA   1 
ATOM   2384 C  C    . ALA   A 1 325 ? -13.66739 -9.50753  -17.15879 1.000 69.64586  ? 1377 ALA   B C    1 
ATOM   2385 O  O    . ALA   A 1 325 ? -12.44741 -9.72459  -17.06974 1.000 71.36909  ? 1377 ALA   B O    1 
ATOM   2386 C  CB   . ALA   A 1 325 ? -14.87050 -11.34198 -16.00403 1.000 64.55093  ? 1377 ALA   B CB   1 
ATOM   2387 N  N    . LEU   A 1 326 ? -14.22530 -8.30746  -17.09825 1.000 59.17896  ? 1378 LEU   B N    1 
ATOM   2388 C  CA   . LEU   A 1 326 ? -13.38920 -7.11743  -16.84375 1.000 64.53573  ? 1378 LEU   B CA   1 
ATOM   2389 C  C    . LEU   A 1 326 ? -13.27314 -6.95184  -15.32682 1.000 57.11068  ? 1378 LEU   B C    1 
ATOM   2390 O  O    . LEU   A 1 326 ? -12.51106 -6.08072  -14.89018 1.000 53.33342  ? 1378 LEU   B O    1 
ATOM   2391 C  CB   . LEU   A 1 326 ? -14.08413 -5.93564  -17.51020 1.000 51.88870  ? 1378 LEU   B CB   1 
ATOM   2392 C  CG   . LEU   A 1 326 ? -14.54519 -6.16617  -18.94809 1.000 48.43308  ? 1378 LEU   B CG   1 
ATOM   2393 C  CD1  . LEU   A 1 326 ? -15.54512 -5.10025  -19.33848 1.000 54.53049  ? 1378 LEU   B CD1  1 
ATOM   2394 C  CD2  . LEU   A 1 326 ? -13.34221 -6.14863  -19.86513 1.000 49.34936  ? 1378 LEU   B CD2  1 
ATOM   2395 N  N    . ASN   A 1 327 ? -13.99118 -7.78148  -14.56647 1.000 55.06542  ? 1379 ASN   B N    1 
ATOM   2396 C  CA   . ASN   A 1 327 ? -13.96713 -7.64091  -13.12052 1.000 58.34472  ? 1379 ASN   B CA   1 
ATOM   2397 C  C    . ASN   A 1 327 ? -13.91922 -9.01966  -12.48098 1.000 56.49346  ? 1379 ASN   B C    1 
ATOM   2398 O  O    . ASN   A 1 327 ? -14.22432 -10.03589 -13.10957 1.000 50.34112  ? 1379 ASN   B O    1 
ATOM   2399 C  CB   . ASN   A 1 327 ? -15.19306 -6.87661  -12.60379 1.000 52.25092  ? 1379 ASN   B CB   1 
ATOM   2400 C  CG   . ASN   A 1 327 ? -15.19996 -5.43078  -13.04036 1.000 59.40415  ? 1379 ASN   B CG   1 
ATOM   2401 O  OD1  . ASN   A 1 327 ? -14.24089 -4.69677  -12.81068 1.000 56.32769  ? 1379 ASN   B OD1  1 
ATOM   2402 N  ND2  . ASN   A 1 327 ? -16.28294 -5.01295  -13.68350 1.000 58.92430  ? 1379 ASN   B ND2  1 
ATOM   2403 N  N    . MET   A 1 328 ? -13.52618 -9.03919  -11.21198 1.000 48.88395  ? 1380 MET   B N    1 
ATOM   2404 C  CA   . MET   A 1 328 ? -13.58826 -10.26288 -10.43650 1.000 42.92620  ? 1380 MET   B CA   1 
ATOM   2405 C  C    . MET   A 1 328 ? -15.04128 -10.65767 -10.18930 1.000 50.68953  ? 1380 MET   B C    1 
ATOM   2406 O  O    . MET   A 1 328 ? -15.96522 -9.84463  -10.28759 1.000 42.56201  ? 1380 MET   B O    1 
ATOM   2407 C  CB   . MET   A 1 328 ? -12.86620 -10.08541 -9.10159  1.000 35.48973  ? 1380 MET   B CB   1 
ATOM   2408 C  CG   . MET   A 1 328 ? -13.58410 -9.12498  -8.16195  1.000 37.57361  ? 1380 MET   B CG   1 
ATOM   2409 S  SD   . MET   A 1 328 ? -12.80504 -8.94640  -6.54504  1.000 45.06492  ? 1380 MET   B SD   1 
ATOM   2410 C  CE   . MET   A 1 328 ? -11.38697 -7.93067  -6.95048  1.000 51.46500  ? 1380 MET   B CE   1 
ATOM   2411 N  N    . ASP   A 1 329 ? -15.23637 -11.93753 -9.87079  1.000 35.05280  ? 1381 ASP   B N    1 
ATOM   2412 C  CA   . ASP   A 1 329 ? -16.51239 -12.44523 -9.36755  1.000 38.99488  ? 1381 ASP   B CA   1 
ATOM   2413 C  C    . ASP   A 1 329 ? -16.14244 -13.47884 -8.30715  1.000 39.43240  ? 1381 ASP   B C    1 
ATOM   2414 O  O    . ASP   A 1 329 ? -16.04054 -14.67895 -8.57668  1.000 40.11952  ? 1381 ASP   B O    1 
ATOM   2415 C  CB   . ASP   A 1 329 ? -17.38347 -13.03260 -10.47929 1.000 40.95487  ? 1381 ASP   B CB   1 
ATOM   2416 C  CG   . ASP   A 1 329 ? -18.77848 -13.38330 -10.00011 1.000 35.69710  ? 1381 ASP   B CG   1 
ATOM   2417 O  OD1  . ASP   A 1 329 ? -19.42240 -12.53399 -9.34743  1.000 43.55638  ? 1381 ASP   B OD1  1 
ATOM   2418 O  OD2  . ASP   A 1 329 ? -19.23758 -14.50738 -10.28265 1.000 40.53537  ? 1381 ASP   B OD2  1 
ATOM   2419 N  N    . THR   A 1 330 ? -15.90337 -13.00038 -7.09534  1.000 33.52564  ? 1382 THR   B N    1 
ATOM   2420 C  CA   . THR   A 1 330 ? -15.41840 -13.85199 -6.02402  1.000 37.87229  ? 1382 THR   B CA   1 
ATOM   2421 C  C    . THR   A 1 330 ? -16.57142 -14.40457 -5.19977  1.000 39.70551  ? 1382 THR   B C    1 
ATOM   2422 O  O    . THR   A 1 330 ? -17.65938 -13.82646 -5.13197  1.000 37.92237  ? 1382 THR   B O    1 
ATOM   2423 C  CB   . THR   A 1 330 ? -14.45132 -13.09170 -5.11535  1.000 39.52654  ? 1382 THR   B CB   1 
ATOM   2424 O  OG1  . THR   A 1 330 ? -15.05021 -11.85749 -4.70282  1.000 38.38040  ? 1382 THR   B OG1  1 
ATOM   2425 C  CG2  . THR   A 1 330 ? -13.14432 -12.79910 -5.84651  1.000 34.85782  ? 1382 THR   B CG2  1 
ATOM   2426 N  N    . VAL   A 1 331 ? -16.31849 -15.55435 -4.59232  1.000 40.64181  ? 1383 VAL   B N    1 
ATOM   2427 C  CA   . VAL   A 1 331 ? -17.21251 -16.17590 -3.63205  1.000 36.56235  ? 1383 VAL   B CA   1 
ATOM   2428 C  C    . VAL   A 1 331 ? -16.38850 -16.51748 -2.39894  1.000 41.68447  ? 1383 VAL   B C    1 
ATOM   2429 O  O    . VAL   A 1 331 ? -15.17152 -16.71560 -2.47590  1.000 35.07462  ? 1383 VAL   B O    1 
ATOM   2430 C  CB   . VAL   A 1 331 ? -17.89463 -17.44307 -4.19853  1.000 39.66608  ? 1383 VAL   B CB   1 
ATOM   2431 C  CG1  . VAL   A 1 331 ? -18.72264 -17.10850 -5.42664  1.000 40.62122  ? 1383 VAL   B CG1  1 
ATOM   2432 C  CG2  . VAL   A 1 331 ? -16.85272 -18.50328 -4.52414  1.000 37.66559  ? 1383 VAL   B CG2  1 
ATOM   2433 N  N    . CYS   A 1 332 ? -17.05847 -16.56697 -1.25390  1.000 33.78961  ? 1384 CYS   B N    1 
ATOM   2434 C  CA   . CYS   A 1 332 ? -16.44647 -17.04053 -0.02273  1.000 34.84040  ? 1384 CYS   B CA   1 
ATOM   2435 C  C    . CYS   A 1 332 ? -16.90158 -18.47040 0.22185   1.000 35.30748  ? 1384 CYS   B C    1 
ATOM   2436 O  O    . CYS   A 1 332 ? -18.10460 -18.75131 0.22800   1.000 37.80078  ? 1384 CYS   B O    1 
ATOM   2437 C  CB   . CYS   A 1 332 ? -16.81737 -16.15304 1.16493   1.000 32.00512  ? 1384 CYS   B CB   1 
ATOM   2438 S  SG   . CYS   A 1 332 ? -16.10837 -16.70647 2.72713   1.000 39.56899  ? 1384 CYS   B SG   1 
ATOM   2439 N  N    . ARG   A 1 333 ? -15.94164 -19.37041 0.40018   1.000 35.20491  ? 1385 ARG   B N    1 
ATOM   2440 C  CA   . ARG   A 1 333 ? -16.21974 -20.76426 0.71474   1.000 38.52044  ? 1385 ARG   B CA   1 
ATOM   2441 C  C    . ARG   A 1 333 ? -15.73272 -21.06774 2.12084   1.000 43.08589  ? 1385 ARG   B C    1 
ATOM   2442 O  O    . ARG   A 1 333 ? -14.61968 -20.68068 2.49666   1.000 40.23839  ? 1385 ARG   B O    1 
ATOM   2443 C  CB   . ARG   A 1 333 ? -15.55285 -21.70471 -0.29091  1.000 33.81417  ? 1385 ARG   B CB   1 
ATOM   2444 C  CG   . ARG   A 1 333 ? -16.37090 -21.94614 -1.54379  1.000 43.18472  ? 1385 ARG   B CG   1 
ATOM   2445 C  CD   . ARG   A 1 333 ? -15.76001 -23.04253 -2.39537  1.000 37.24897  ? 1385 ARG   B CD   1 
ATOM   2446 N  NE   . ARG   A 1 333 ? -16.70908 -23.54184 -3.38115  1.000 41.97985  ? 1385 ARG   B NE   1 
ATOM   2447 C  CZ   . ARG   A 1 333 ? -16.99406 -22.92927 -4.52338  1.000 48.91209  ? 1385 ARG   B CZ   1 
ATOM   2448 N  NH1  . ARG   A 1 333 ? -16.41599 -21.78645 -4.85485  1.000 44.82201  ? 1385 ARG   B NH1  1 
ATOM   2449 N  NH2  . ARG   A 1 333 ? -17.88213 -23.47553 -5.34814  1.000 44.38294  ? 1385 ARG   B NH2  1 
ATOM   2450 N  N    . LEU   A 1 334 ? -16.56575 -21.75037 2.89514   1.000 42.32239  ? 1386 LEU   B N    1 
ATOM   2451 C  CA   . LEU   A 1 334 ? -16.19075 -22.22288 4.21631   1.000 41.03617  ? 1386 LEU   B CA   1 
ATOM   2452 C  C    . LEU   A 1 334 ? -15.94887 -23.72293 4.13790   1.000 41.55207  ? 1386 LEU   B C    1 
ATOM   2453 O  O    . LEU   A 1 334 ? -16.76595 -24.45809 3.57222   1.000 45.06036  ? 1386 LEU   B O    1 
ATOM   2454 C  CB   . LEU   A 1 334 ? -17.27270 -21.89538 5.24722   1.000 40.24013  ? 1386 LEU   B CB   1 
ATOM   2455 C  CG   . LEU   A 1 334 ? -16.84065 -21.83084 6.71418   1.000 45.88402  ? 1386 LEU   B CG   1 
ATOM   2456 C  CD1  . LEU   A 1 334 ? -15.74756 -20.79284 6.91274   1.000 44.65581  ? 1386 LEU   B CD1  1 
ATOM   2457 C  CD2  . LEU   A 1 334 ? -18.03160 -21.53039 7.61410   1.000 50.42175  ? 1386 LEU   B CD2  1 
ATOM   2458 N  N    . TYR   A 1 335 ? -14.81689 -24.16780 4.67104   1.000 43.30868  ? 1387 TYR   B N    1 
ATOM   2459 C  CA   . TYR   A 1 335 ? -14.46100 -25.57581 4.72259   1.000 43.60383  ? 1387 TYR   B CA   1 
ATOM   2460 C  C    . TYR   A 1 335 ? -14.28599 -25.99925 6.17075   1.000 46.91938  ? 1387 TYR   B C    1 
ATOM   2461 O  O    . TYR   A 1 335 ? -13.93390 -25.18894 7.03342   1.000 44.82506  ? 1387 TYR   B O    1 
ATOM   2462 C  CB   . TYR   A 1 335 ? -13.16404 -25.87521 3.96067   1.000 38.09523  ? 1387 TYR   B CB   1 
ATOM   2463 C  CG   . TYR   A 1 335 ? -13.14005 -25.45379 2.50850   1.000 42.84085  ? 1387 TYR   B CG   1 
ATOM   2464 C  CD1  . TYR   A 1 335 ? -13.55015 -26.32016 1.50286   1.000 45.73968  ? 1387 TYR   B CD1  1 
ATOM   2465 C  CD2  . TYR   A 1 335 ? -12.67097 -24.20097 2.13999   1.000 44.46158  ? 1387 TYR   B CD2  1 
ATOM   2466 C  CE1  . TYR   A 1 335 ? -13.51216 -25.93969 0.17371   1.000 47.13902  ? 1387 TYR   B CE1  1 
ATOM   2467 C  CE2  . TYR   A 1 335 ? -12.62898 -23.81250 0.81284   1.000 41.77470  ? 1387 TYR   B CE2  1 
ATOM   2468 C  CZ   . TYR   A 1 335 ? -13.05007 -24.68386 -0.16580  1.000 43.76300  ? 1387 TYR   B CZ   1 
ATOM   2469 O  OH   . TYR   A 1 335 ? -13.00608 -24.29338 -1.48496  1.000 38.91757  ? 1387 TYR   B OH   1 
ATOM   2470 N  N    . GLU   A 1 336 ? -14.51108 -27.27713 6.42227   1.000 47.40519  ? 1388 GLU   B N    1 
ATOM   2471 C  CA   . GLU   A 1 336 ? -14.29008 -27.82562 7.77048   1.000 52.83987  ? 1388 GLU   B CA   1 
ATOM   2472 C  C    . GLU   A 1 336 ? -12.82311 -28.23169 7.87059   1.000 48.36669  ? 1388 GLU   B C    1 
ATOM   2473 O  O    . GLU   A 1 336 ? -12.33519 -28.91609 6.96185   1.000 50.33429  ? 1388 GLU   B O    1 
ATOM   2474 C  CB   . GLU   A 1 336 ? -15.15717 -29.06449 7.93399   1.000 53.64722  ? 1388 GLU   B CB   1 
ATOM   2475 C  CG   . GLU   A 1 336 ? -15.28517 -29.55091 9.37319   1.000 59.02719  ? 1388 GLU   B CG   1 
ATOM   2476 C  CD   . GLU   A 1 336 ? -16.31025 -30.66679 9.45966   1.000 68.29000  ? 1388 GLU   B CD   1 
ATOM   2477 O  OE1  . GLU   A 1 336 ? -16.05535 -31.74004 8.87708   1.000 62.90440  ? 1388 GLU   B OE1  1 
ATOM   2478 O  OE2  . GLU   A 1 336 ? -17.36822 -30.45546 10.08361  1.000 63.24808  ? 1388 GLU   B OE2  1 
ATOM   2479 N  N    . VAL   A 1 337 ? -12.14504 -27.76134 8.90139   1.000 49.26292  ? 1389 VAL   B N    1 
ATOM   2480 C  CA   . VAL   A 1 337 ? -10.75007 -28.22237 9.10353   1.000 54.78212  ? 1389 VAL   B CA   1 
ATOM   2481 C  C    . VAL   A 1 337 ? -10.87117 -29.64213 9.67509   1.000 61.24430  ? 1389 VAL   B C    1 
ATOM   2482 O  O    . VAL   A 1 337 ? -11.35816 -29.89866 10.77621  1.000 67.98799  ? 1389 VAL   B O    1 
ATOM   2483 C  CB   . VAL   A 1 337 ? -9.96797  -27.26807 10.01513  1.000 60.32777  ? 1389 VAL   B CB   1 
ATOM   2484 C  CG1  . VAL   A 1 337 ? -8.57501  -27.80207 10.28730  1.000 62.56182  ? 1389 VAL   B CG1  1 
ATOM   2485 C  CG2  . VAL   A 1 337 ? -9.90388  -25.86130 9.43757   1.000 47.91582  ? 1389 VAL   B CG2  1 
ATOM   2486 N  N    . GLY   A 1 338 ? -10.38026 -30.55748 8.87744   1.000 68.58475  ? 1390 GLY   B N    1 
ATOM   2487 C  CA   . GLY   A 1 338 ? -10.49137 -31.98737 9.14101   1.000 66.53165  ? 1390 GLY   B CA   1 
ATOM   2488 C  C    . GLY   A 1 338 ? -10.13735 -32.30983 10.58813  1.000 83.77959  ? 1390 GLY   B C    1 
ATOM   2489 O  O    . GLY   A 1 338 ? -9.19329  -31.80568 11.14990  1.000 76.80784  ? 1390 GLY   B O    1 
ATOM   2490 O  OXT  . GLY   A 1 338 ? -10.81339 -33.10552 11.24046  1.000 94.39099  ? 1390 GLY   B OXT  1 
ATOM   2491 N  N    . PRO   B 2 23  ? -10.13763 45.37842  -25.75085 1.000 59.57289  ? 28   PRO   A N    1 
ATOM   2492 C  CA   . PRO   B 2 23  ? -8.69863  45.59558  -25.56101 1.000 71.68112  ? 28   PRO   A CA   1 
ATOM   2493 C  C    . PRO   B 2 23  ? -8.00744  44.40666  -24.89906 1.000 60.95820  ? 28   PRO   A C    1 
ATOM   2494 O  O    . PRO   B 2 23  ? -8.19229  44.17965  -23.70304 1.000 56.69869  ? 28   PRO   A O    1 
ATOM   2495 C  CB   . PRO   B 2 23  ? -8.65067  46.82659  -24.65103 1.000 60.08318  ? 28   PRO   A CB   1 
ATOM   2496 C  CG   . PRO   B 2 23  ? -9.90278  47.56746  -24.96990 1.000 64.64713  ? 28   PRO   A CG   1 
ATOM   2497 C  CD   . PRO   B 2 23  ? -10.93870 46.51235  -25.25978 1.000 68.99780  ? 28   PRO   A CD   1 
ATOM   2498 N  N    . THR   B 2 24  ? -7.19745  43.68473  -25.68714 1.000 50.61205  ? 29   THR   A N    1 
ATOM   2499 C  CA   . THR   B 2 24  ? -6.42027  42.53782  -25.17421 1.000 50.93027  ? 29   THR   A CA   1 
ATOM   2500 C  C    . THR   B 2 24  ? -5.29224  43.05995  -24.33533 1.000 46.36864  ? 29   THR   A C    1 
ATOM   2501 O  O    . THR   B 2 24  ? -4.49238  43.84902  -24.85843 1.000 47.18949  ? 29   THR   A O    1 
ATOM   2502 C  CB   . THR   B 2 24  ? -5.86031  41.72586  -26.33826 1.000 52.81001  ? 29   THR   A CB   1 
ATOM   2503 O  OG1  . THR   B 2 24  ? -6.96529  40.98574  -26.84213 1.000 61.00781  ? 29   THR   A OG1  1 
ATOM   2504 C  CG2  . THR   B 2 24  ? -4.74117  40.79199  -25.92036 1.000 40.94430  ? 29   THR   A CG2  1 
ATOM   2505 N  N    . PRO   B 2 25  ? -5.16707  42.67198  -23.05234 1.000 44.76243  ? 30   PRO   A N    1 
ATOM   2506 C  CA   . PRO   B 2 25  ? -4.12004  43.26710  -22.21346 1.000 47.72425  ? 30   PRO   A CA   1 
ATOM   2507 C  C    . PRO   B 2 25  ? -2.74102  42.71224  -22.54060 1.000 45.28350  ? 30   PRO   A C    1 
ATOM   2508 O  O    . PRO   B 2 25  ? -2.57698  41.69425  -23.21560 1.000 45.12116  ? 30   PRO   A O    1 
ATOM   2509 C  CB   . PRO   B 2 25  ? -4.55085  42.89007  -20.79441 1.000 45.27379  ? 30   PRO   A CB   1 
ATOM   2510 C  CG   . PRO   B 2 25  ? -5.30774  41.60999  -20.97531 1.000 45.31450  ? 30   PRO   A CG   1 
ATOM   2511 C  CD   . PRO   B 2 25  ? -6.01789  41.73090  -22.30024 1.000 48.10665  ? 30   PRO   A CD   1 
ATOM   2512 N  N    . VAL   B 2 26  ? -1.72804  43.42235  -22.03571 1.000 39.12687  ? 31   VAL   A N    1 
ATOM   2513 C  CA   . VAL   B 2 26  ? -0.35500  42.94049  -22.14485 1.000 42.60461  ? 31   VAL   A CA   1 
ATOM   2514 C  C    . VAL   B 2 26  ? -0.15478  41.70952  -21.27286 1.000 46.32279  ? 31   VAL   A C    1 
ATOM   2515 O  O    . VAL   B 2 26  ? 0.50228   40.74159  -21.67691 1.000 44.46110  ? 31   VAL   A O    1 
ATOM   2516 C  CB   . VAL   B 2 26  ? 0.63392   44.06360  -21.77797 1.000 42.37545  ? 31   VAL   A CB   1 
ATOM   2517 C  CG1  . VAL   B 2 26  ? 2.04799   43.51475  -21.66611 1.000 39.91553  ? 31   VAL   A CG1  1 
ATOM   2518 C  CG2  . VAL   B 2 26  ? 0.57370   45.18458  -22.80898 1.000 38.95123  ? 31   VAL   A CG2  1 
ATOM   2519 N  N    . LYS   B 2 27  ? -0.70865  41.72748  -20.06480 1.000 46.71410  ? 32   LYS   A N    1 
ATOM   2520 C  CA   . LYS   B 2 27  ? -0.73144  40.59149  -19.15878 1.000 47.98975  ? 32   LYS   A CA   1 
ATOM   2521 C  C    . LYS   B 2 27  ? -2.10136  40.53136  -18.50364 1.000 48.52970  ? 32   LYS   A C    1 
ATOM   2522 O  O    . LYS   B 2 27  ? -2.72845  41.57229  -18.27558 1.000 48.23808  ? 32   LYS   A O    1 
ATOM   2523 C  CB   . LYS   B 2 27  ? 0.34867   40.69262  -18.06990 1.000 44.94827  ? 32   LYS   A CB   1 
ATOM   2524 C  CG   . LYS   B 2 27  ? 1.77560   40.76676  -18.58805 1.000 48.86347  ? 32   LYS   A CG   1 
ATOM   2525 C  CD   . LYS   B 2 27  ? 2.77272   40.77788  -17.43715 1.000 39.86494  ? 32   LYS   A CD   1 
ATOM   2526 C  CE   . LYS   B 2 27  ? 4.19065   41.00502  -17.92931 1.000 48.96713  ? 32   LYS   A CE   1 
ATOM   2527 N  NZ   . LYS   B 2 27  ? 5.16976   41.03014  -16.80841 1.000 49.14562  ? 32   LYS   A NZ   1 
ATOM   2528 N  N    . PRO   B 2 28  ? -2.59020  39.33531  -18.19157 1.000 50.96451  ? 33   PRO   A N    1 
ATOM   2529 C  CA   . PRO   B 2 28  ? -3.85312  39.22819  -17.45644 1.000 50.96921  ? 33   PRO   A CA   1 
ATOM   2530 C  C    . PRO   B 2 28  ? -3.67101  39.67622  -16.01546 1.000 41.12564  ? 33   PRO   A C    1 
ATOM   2531 O  O    . PRO   B 2 28  ? -2.55898  39.90735  -15.53958 1.000 43.40434  ? 33   PRO   A O    1 
ATOM   2532 C  CB   . PRO   B 2 28  ? -4.19197  37.74015  -17.54938 1.000 44.89660  ? 33   PRO   A CB   1 
ATOM   2533 C  CG   . PRO   B 2 28  ? -2.85991  37.07729  -17.65951 1.000 44.65257  ? 33   PRO   A CG   1 
ATOM   2534 C  CD   . PRO   B 2 28  ? -1.99009  38.01737  -18.45562 1.000 43.66901  ? 33   PRO   A CD   1 
ATOM   2535 N  N    . ASN   B 2 29  ? -4.79495  39.79512  -15.31034 1.000 47.16496  ? 34   ASN   A N    1 
ATOM   2536 C  CA   . ASN   B 2 29  ? -4.79285  40.23813  -13.92135 1.000 46.72065  ? 34   ASN   A CA   1 
ATOM   2537 C  C    . ASN   B 2 29  ? -5.83668  39.44104  -13.13223 1.000 51.06620  ? 34   ASN   A C    1 
ATOM   2538 O  O    . ASN   B 2 29  ? -6.81768  39.96894  -12.61713 1.000 48.90732  ? 34   ASN   A O    1 
ATOM   2539 C  CB   . ASN   B 2 29  ? -5.04400  41.74211  -13.83334 1.000 58.01915  ? 34   ASN   A CB   1 
ATOM   2540 C  CG   . ASN   B 2 29  ? -5.16190  42.23011  -12.40534 1.000 63.69398  ? 34   ASN   A CG   1 
ATOM   2541 O  OD1  . ASN   B 2 29  ? -4.21680  42.12922  -11.62243 1.000 56.90512  ? 34   ASN   A OD1  1 
ATOM   2542 N  ND2  . ASN   B 2 29  ? -6.32692  42.76700  -12.05622 1.000 69.58481  ? 34   ASN   A ND2  1 
ATOM   2543 N  N    . TYR   B 2 30  ? -5.61653  38.13306  -13.03524 1.000 50.33136  ? 35   TYR   A N    1 
ATOM   2544 C  CA   . TYR   B 2 30  ? -6.56337  37.27697  -12.33712 1.000 43.46602  ? 35   TYR   A CA   1 
ATOM   2545 C  C    . TYR   B 2 30  ? -6.44323  37.45000  -10.82814 1.000 43.93568  ? 35   TYR   A C    1 
ATOM   2546 O  O    . TYR   B 2 30  ? -5.34218  37.54012  -10.27726 1.000 41.37809  ? 35   TYR   A O    1 
ATOM   2547 C  CB   . TYR   B 2 30  ? -6.34426  35.81299  -12.72113 1.000 44.81536  ? 35   TYR   A CB   1 
ATOM   2548 C  CG   . TYR   B 2 30  ? -6.94636  35.45791  -14.06006 1.000 41.13090  ? 35   TYR   A CG   1 
ATOM   2549 C  CD1  . TYR   B 2 30  ? -8.26233  35.02777  -14.15792 1.000 38.28115  ? 35   TYR   A CD1  1 
ATOM   2550 C  CD2  . TYR   B 2 30  ? -6.20150  35.56697  -15.22814 1.000 35.66202  ? 35   TYR   A CD2  1 
ATOM   2551 C  CE1  . TYR   B 2 30  ? -8.82242  34.70969  -15.38085 1.000 37.80859  ? 35   TYR   A CE1  1 
ATOM   2552 C  CE2  . TYR   B 2 30  ? -6.75159  35.25190  -16.45408 1.000 38.68165  ? 35   TYR   A CE2  1 
ATOM   2553 C  CZ   . TYR   B 2 30  ? -8.06056  34.82276  -16.52494 1.000 37.09525  ? 35   TYR   A CZ   1 
ATOM   2554 O  OH   . TYR   B 2 30  ? -8.61165  34.50869  -17.74787 1.000 37.83163  ? 35   TYR   A OH   1 
ATOM   2555 N  N    . ALA   B 2 31  ? -7.59417  37.50489  -10.16802 1.000 43.15665  ? 36   ALA   A N    1 
ATOM   2556 C  CA   . ALA   B 2 31  ? -7.67302  37.56990  -8.71901  1.000 43.54990  ? 36   ALA   A CA   1 
ATOM   2557 C  C    . ALA   B 2 31  ? -8.76387  36.62079  -8.24688  1.000 42.42013  ? 36   ALA   A C    1 
ATOM   2558 O  O    . ALA   B 2 31  ? -9.73292  36.35968  -8.96678  1.000 41.88066  ? 36   ALA   A O    1 
ATOM   2559 C  CB   . ALA   B 2 31  ? -7.96412  38.99388  -8.22500  1.000 43.03662  ? 36   ALA   A CB   1 
ATOM   2560 N  N    . LEU   B 2 32  ? -8.58969  36.10483  -7.03190  1.000 49.94227  ? 37   LEU   A N    1 
ATOM   2561 C  CA   . LEU   B 2 32  ? -9.53253  35.14373  -6.47478  1.000 41.36840  ? 37   LEU   A CA   1 
ATOM   2562 C  C    . LEU   B 2 32  ? -10.85557 35.81960  -6.14065  1.000 48.36807  ? 37   LEU   A C    1 
ATOM   2563 O  O    . LEU   B 2 32  ? -10.87961 36.87461  -5.49966  1.000 45.99862  ? 37   LEU   A O    1 
ATOM   2564 C  CB   . LEU   B 2 32  ? -8.94133  34.50081  -5.22184  1.000 50.07299  ? 37   LEU   A CB   1 
ATOM   2565 C  CG   . LEU   B 2 32  ? -9.81715  33.49773  -4.47173  1.000 43.13941  ? 37   LEU   A CG   1 
ATOM   2566 C  CD1  . LEU   B 2 32  ? -10.01810 32.23770  -5.30370  1.000 46.26276  ? 37   LEU   A CD1  1 
ATOM   2567 C  CD2  . LEU   B 2 32  ? -9.21097  33.16481  -3.11579  1.000 46.95023  ? 37   LEU   A CD2  1 
ATOM   2568 N  N    . LYS   B 2 33  ? -11.96355 35.21448  -6.57253  1.000 46.78864  ? 38   LYS   A N    1 
ATOM   2569 C  CA   . LYS   B 2 33  ? -13.29157 35.70635  -6.23939  1.000 48.21550  ? 38   LYS   A CA   1 
ATOM   2570 C  C    . LYS   B 2 33  ? -14.12138 34.72427  -5.42929  1.000 51.59021  ? 38   LYS   A C    1 
ATOM   2571 O  O    . LYS   B 2 33  ? -14.93234 35.16019  -4.60821  1.000 54.33253  ? 38   LYS   A O    1 
ATOM   2572 C  CB   . LYS   B 2 33  ? -14.06974 36.08025  -7.51232  1.000 44.38414  ? 38   LYS   A CB   1 
ATOM   2573 C  CG   . LYS   B 2 33  ? -13.38594 37.14031  -8.36940  1.000 48.07380  ? 38   LYS   A CG   1 
ATOM   2574 C  CD   . LYS   B 2 33  ? -12.95398 38.34336  -7.53346  1.000 55.06333  ? 38   LYS   A CD   1 
ATOM   2575 C  CE   . LYS   B 2 33  ? -14.03308 39.41425  -7.47336  1.000 62.93941  ? 38   LYS   A CE   1 
ATOM   2576 N  NZ   . LYS   B 2 33  ? -13.63811 40.54230  -6.58042  1.000 53.00354  ? 38   LYS   A NZ   1 
ATOM   2577 N  N    . PHE   B 2 34  ? -13.94426 33.41829  -5.62730  1.000 55.43645  ? 39   PHE   A N    1 
ATOM   2578 C  CA   . PHE   B 2 34  ? -14.72708 32.42921  -4.90220  1.000 50.21290  ? 39   PHE   A CA   1 
ATOM   2579 C  C    . PHE   B 2 34  ? -13.87492 31.20031  -4.62128  1.000 51.33964  ? 39   PHE   A C    1 
ATOM   2580 O  O    . PHE   B 2 34  ? -12.98297 30.85239  -5.39836  1.000 53.10196  ? 39   PHE   A O    1 
ATOM   2581 C  CB   . PHE   B 2 34  ? -15.98112 32.01507  -5.68106  1.000 47.31511  ? 39   PHE   A CB   1 
ATOM   2582 C  CG   . PHE   B 2 34  ? -16.90527 33.15297  -5.99898  1.000 56.95519  ? 39   PHE   A CG   1 
ATOM   2583 C  CD1  . PHE   B 2 34  ? -17.82022 33.60389  -5.06289  1.000 57.30299  ? 39   PHE   A CD1  1 
ATOM   2584 C  CD2  . PHE   B 2 34  ? -16.86747 33.76696  -7.23899  1.000 51.82718  ? 39   PHE   A CD2  1 
ATOM   2585 C  CE1  . PHE   B 2 34  ? -18.67736 34.64979  -5.35581  1.000 54.28703  ? 39   PHE   A CE1  1 
ATOM   2586 C  CE2  . PHE   B 2 34  ? -17.72061 34.81387  -7.53692  1.000 53.43732  ? 39   PHE   A CE2  1 
ATOM   2587 C  CZ   . PHE   B 2 34  ? -18.62656 35.25678  -6.59383  1.000 53.54265  ? 39   PHE   A CZ   1 
ATOM   2588 N  N    . THR   B 2 35  ? -14.16074 30.55129  -3.49624  1.000 54.01441  ? 40   THR   A N    1 
ATOM   2589 C  CA   . THR   B 2 35  ? -13.58657 29.25735  -3.15328  1.000 52.55148  ? 40   THR   A CA   1 
ATOM   2590 C  C    . THR   B 2 35  ? -14.72844 28.28224  -2.93115  1.000 50.49232  ? 40   THR   A C    1 
ATOM   2591 O  O    . THR   B 2 35  ? -15.56537 28.49416  -2.04606  1.000 43.87141  ? 40   THR   A O    1 
ATOM   2592 C  CB   . THR   B 2 35  ? -12.70244 29.34746  -1.90738  1.000 42.37613  ? 40   THR   A CB   1 
ATOM   2593 O  OG1  . THR   B 2 35  ? -11.58056 30.19358  -2.17550  1.000 46.28012  ? 40   THR   A OG1  1 
ATOM   2594 C  CG2  . THR   B 2 35  ? -12.20126 27.96852  -1.51141  1.000 43.82894  ? 40   THR   A CG2  1 
ATOM   2595 N  N    . LEU   B 2 36  ? -14.76441 27.22122  -3.73213  1.000 49.47298  ? 41   LEU   A N    1 
ATOM   2596 C  CA   . LEU   B 2 36  ? -15.84931 26.24911  -3.70200  1.000 49.39131  ? 41   LEU   A CA   1 
ATOM   2597 C  C    . LEU   B 2 36  ? -15.42610 25.04417  -2.87203  1.000 53.11722  ? 41   LEU   A C    1 
ATOM   2598 O  O    . LEU   B 2 36  ? -14.49406 24.32126  -3.24412  1.000 51.60824  ? 41   LEU   A O    1 
ATOM   2599 C  CB   . LEU   B 2 36  ? -16.23642 25.82405  -5.11896  1.000 48.87124  ? 41   LEU   A CB   1 
ATOM   2600 C  CG   . LEU   B 2 36  ? -17.06660 26.81495  -5.93688  1.000 52.13441  ? 41   LEU   A CG   1 
ATOM   2601 C  CD1  . LEU   B 2 36  ? -16.42575 28.19502  -5.95597  1.000 50.22068  ? 41   LEU   A CD1  1 
ATOM   2602 C  CD2  . LEU   B 2 36  ? -17.26870 26.29792  -7.35685  1.000 46.52222  ? 41   LEU   A CD2  1 
ATOM   2603 N  N    . ALA   B 2 37  ? -16.10996 24.83411  -1.75196  1.000 47.92139  ? 42   ALA   A N    1 
ATOM   2604 C  CA   . ALA   B 2 37  ? -15.86675 23.70415  -0.87197  1.000 44.91171  ? 42   ALA   A CA   1 
ATOM   2605 C  C    . ALA   B 2 37  ? -17.07665 22.77802  -0.86483  1.000 47.59891  ? 42   ALA   A C    1 
ATOM   2606 O  O    . ALA   B 2 37  ? -18.20572 23.19890  -1.13172  1.000 52.02904  ? 42   ALA   A O    1 
ATOM   2607 C  CB   . ALA   B 2 37  ? -15.55364 24.17020  0.55299   1.000 38.92621  ? 42   ALA   A CB   1 
ATOM   2608 N  N    . GLY   B 2 38  ? -16.82648 21.50805  -0.56184  1.000 43.52780  ? 43   GLY   A N    1 
ATOM   2609 C  CA   . GLY   B 2 38  ? -17.88038 20.51494  -0.55572  1.000 48.13287  ? 43   GLY   A CA   1 
ATOM   2610 C  C    . GLY   B 2 38  ? -17.34725 19.11299  -0.76175  1.000 49.31758  ? 43   GLY   A C    1 
ATOM   2611 O  O    . GLY   B 2 38  ? -17.74408 18.18096  -0.05770  1.000 51.94167  ? 43   GLY   A O    1 
ATOM   2612 N  N    . HIS   B 2 39  ? -16.44734 18.95107  -1.72885  1.000 45.55939  ? 44   HIS   A N    1 
ATOM   2613 C  CA   . HIS   B 2 39  ? -15.80123 17.66214  -1.92390  1.000 49.00120  ? 44   HIS   A CA   1 
ATOM   2614 C  C    . HIS   B 2 39  ? -15.01405 17.27624  -0.67798  1.000 44.45302  ? 44   HIS   A C    1 
ATOM   2615 O  O    . HIS   B 2 39  ? -14.40407 18.12331  -0.02105  1.000 41.93772  ? 44   HIS   A O    1 
ATOM   2616 C  CB   . HIS   B 2 39  ? -14.88536 17.70422  -3.14600  1.000 37.90924  ? 44   HIS   A CB   1 
ATOM   2617 C  CG   . HIS   B 2 39  ? -15.61649 17.66313  -4.45192  1.000 41.82990  ? 44   HIS   A CG   1 
ATOM   2618 N  ND1  . HIS   B 2 39  ? -16.44242 16.61703  -4.80782  1.000 36.95033  ? 44   HIS   A ND1  1 
ATOM   2619 C  CD2  . HIS   B 2 39  ? -15.64269 18.53111  -5.49093  1.000 45.45981  ? 44   HIS   A CD2  1 
ATOM   2620 C  CE1  . HIS   B 2 39  ? -16.94557 16.84597  -6.00877  1.000 42.24386  ? 44   HIS   A CE1  1 
ATOM   2621 N  NE2  . HIS   B 2 39  ? -16.47674 18.00101  -6.44483  1.000 44.22126  ? 44   HIS   A NE2  1 
ATOM   2622 N  N    . THR   B 2 40  ? -15.03489 15.98824  -0.35196  1.000 42.99027  ? 45   THR   A N    1 
ATOM   2623 C  CA   . THR   B 2 40  ? -14.37771 15.47732  0.84298   1.000 50.46563  ? 45   THR   A CA   1 
ATOM   2624 C  C    . THR   B 2 40  ? -13.04267 14.80746  0.54885   1.000 45.50488  ? 45   THR   A C    1 
ATOM   2625 O  O    . THR   B 2 40  ? -12.35952 14.38454  1.48478   1.000 41.28642  ? 45   THR   A O    1 
ATOM   2626 C  CB   . THR   B 2 40  ? -15.30153 14.49924  1.57409   1.000 39.81848  ? 45   THR   A CB   1 
ATOM   2627 O  OG1  . THR   B 2 40  ? -15.75952 13.49618  0.65915   1.000 50.54127  ? 45   THR   A OG1  1 
ATOM   2628 C  CG2  . THR   B 2 40  ? -16.49954 15.23612  2.15321   1.000 44.11199  ? 45   THR   A CG2  1 
ATOM   2629 N  N    . LYS   B 2 41  ? -12.68580 14.76948  -0.72519  1.000 42.01727  ? 46   LYS   A N    1 
ATOM   2630 C  CA   . LYS   B 2 41  ? -11.38178 14.20261  -1.12032  1.000 46.40707  ? 46   LYS   A CA   1 
ATOM   2631 C  C    . LYS   B 2 41  ? -10.80199 15.08466  -2.22839  1.000 46.79433  ? 46   LYS   A C    1 
ATOM   2632 O  O    . LYS   B 2 41  ? -11.45913 16.05958  -2.61534  1.000 39.22130  ? 46   LYS   A O    1 
ATOM   2633 C  CB   . LYS   B 2 41  ? -11.54568 12.75859  -1.58828  1.000 45.91725  ? 46   LYS   A CB   1 
ATOM   2634 C  CG   . LYS   B 2 41  ? -11.96746 11.74756  -0.53623  1.000 47.33910  ? 46   LYS   A CG   1 
ATOM   2635 C  CD   . LYS   B 2 41  ? -11.36234 10.37162  -0.77627  1.000 54.04804  ? 46   LYS   A CD   1 
ATOM   2636 C  CE   . LYS   B 2 41  ? -10.09224 10.19376  -0.01340  1.000 58.42427  ? 46   LYS   A CE   1 
ATOM   2637 N  NZ   . LYS   B 2 41  ? -10.22215 10.70676  1.35160   1.000 59.72767  ? 46   LYS   A NZ   1 
ATOM   2638 N  N    . ALA   B 2 42  ? -9.61900  14.72577  -2.71151  1.000 41.33624  ? 47   ALA   A N    1 
ATOM   2639 C  CA   . ALA   B 2 42  ? -8.99219  15.50983  -3.76259  1.000 40.55043  ? 47   ALA   A CA   1 
ATOM   2640 C  C    . ALA   B 2 42  ? -9.96534  15.74471  -4.91149  1.000 38.34281  ? 47   ALA   A C    1 
ATOM   2641 O  O    . ALA   B 2 42  ? -10.71229 14.84663  -5.31040  1.000 41.09966  ? 47   ALA   A O    1 
ATOM   2642 C  CB   . ALA   B 2 42  ? -7.73417  14.79995  -4.27371  1.000 35.05374  ? 47   ALA   A CB   1 
ATOM   2643 N  N    . VAL   B 2 43  ? -9.96352  16.97070  -5.42750  1.000 42.79119  ? 48   VAL   A N    1 
ATOM   2644 C  CA   . VAL   B 2 43  ? -10.75768 17.32461  -6.59743  1.000 36.22693  ? 48   VAL   A CA   1 
ATOM   2645 C  C    . VAL   B 2 43  ? -9.91979  17.04768  -7.83651  1.000 40.71690  ? 48   VAL   A C    1 
ATOM   2646 O  O    . VAL   B 2 43  ? -8.78585  17.52879  -7.94964  1.000 42.04660  ? 48   VAL   A O    1 
ATOM   2647 C  CB   . VAL   B 2 43  ? -11.19683 18.79656  -6.54040  1.000 42.65182  ? 48   VAL   A CB   1 
ATOM   2648 C  CG1  . VAL   B 2 43  ? -12.06799 19.13545  -7.74431  1.000 36.80300  ? 48   VAL   A CG1  1 
ATOM   2649 C  CG2  . VAL   B 2 43  ? -11.93372 19.08250  -5.23932  1.000 38.56076  ? 48   VAL   A CG2  1 
ATOM   2650 N  N    . SER   B 2 44  ? -10.46680 16.26861  -8.76544  1.000 40.06427  ? 49   SER   A N    1 
ATOM   2651 C  CA   . SER   B 2 44  ? -9.69387  15.79067  -9.90052  1.000 38.87112  ? 49   SER   A CA   1 
ATOM   2652 C  C    . SER   B 2 44  ? -9.85709  16.63664  -11.15651 1.000 32.87088  ? 49   SER   A C    1 
ATOM   2653 O  O    . SER   B 2 44  ? -8.92218  16.70573  -11.96061 1.000 38.15270  ? 49   SER   A O    1 
ATOM   2654 C  CB   . SER   B 2 44  ? -10.07175 14.34063  -10.22146 1.000 35.15151  ? 49   SER   A CB   1 
ATOM   2655 O  OG   . SER   B 2 44  ? -11.44778 14.22548  -10.54131 1.000 36.69764  ? 49   SER   A OG   1 
ATOM   2656 N  N    . SER   B 2 45  ? -11.00018 17.29552  -11.35240 1.000 36.39152  ? 50   SER   A N    1 
ATOM   2657 C  CA   A SER   B 2 45  ? -11.21639 18.01748  -12.59739 0.821 36.43656  ? 50   SER   A CA   1 
ATOM   2658 C  CA   B SER   B 2 45  ? -11.21039 18.02448  -12.59339 0.179 36.68592  ? 50   SER   A CA   1 
ATOM   2659 C  C    . SER   B 2 45  ? -12.33848 19.02937  -12.42228 1.000 44.21403  ? 50   SER   A C    1 
ATOM   2660 O  O    . SER   B 2 45  ? -13.27537 18.81028  -11.64818 1.000 44.16316  ? 50   SER   A O    1 
ATOM   2661 C  CB   A SER   B 2 45  ? -11.54641 17.05043  -13.73834 0.821 38.89746  ? 50   SER   A CB   1 
ATOM   2662 C  CB   B SER   B 2 45  ? -11.52541 17.06643  -13.74634 0.179 38.92164  ? 50   SER   A CB   1 
ATOM   2663 O  OG   A SER   B 2 45  ? -11.50161 17.70142  -14.99535 0.821 40.66965  ? 50   SER   A OG   1 
ATOM   2664 O  OG   B SER   B 2 45  ? -10.41935 16.22754  -14.03045 0.179 41.26051  ? 50   SER   A OG   1 
ATOM   2665 N  N    . VAL   B 2 46  ? -12.23167 20.13337  -13.16031 1.000 41.26035  ? 51   VAL   A N    1 
ATOM   2666 C  CA   . VAL   B 2 46  ? -13.25178 21.17426  -13.23121 1.000 39.69860  ? 51   VAL   A CA   1 
ATOM   2667 C  C    . VAL   B 2 46  ? -13.45798 21.51522  -14.69919 1.000 36.36446  ? 51   VAL   A C    1 
ATOM   2668 O  O    . VAL   B 2 46  ? -12.48707 21.69131  -15.44230 1.000 36.91477  ? 51   VAL   A O    1 
ATOM   2669 C  CB   . VAL   B 2 46  ? -12.85883 22.43231  -12.43327 1.000 37.57277  ? 51   VAL   A CB   1 
ATOM   2670 C  CG1  . VAL   B 2 46  ? -12.85264 22.13833  -10.94227 1.000 44.82882  ? 51   VAL   A CG1  1 
ATOM   2671 C  CG2  . VAL   B 2 46  ? -11.49693 22.94345  -12.88642 1.000 33.56275  ? 51   VAL   A CG2  1 
ATOM   2672 N  N    . LYS   B 2 47  ? -14.71903 21.60008  -15.12206 1.000 41.69153  ? 52   LYS   A N    1 
ATOM   2673 C  CA   . LYS   B 2 47  ? -15.05420 21.82003  -16.52503 1.000 42.20975  ? 52   LYS   A CA   1 
ATOM   2674 C  C    . LYS   B 2 47  ? -16.20231 22.81291  -16.61392 1.000 37.65706  ? 52   LYS   A C    1 
ATOM   2675 O  O    . LYS   B 2 47  ? -17.27323 22.57680  -16.04581 1.000 40.81682  ? 52   LYS   A O    1 
ATOM   2676 C  CB   . LYS   B 2 47  ? -15.43213 20.50298  -17.21497 1.000 34.39945  ? 52   LYS   A CB   1 
ATOM   2677 C  CG   . LYS   B 2 47  ? -14.28205 19.51110  -17.35508 1.000 35.16139  ? 52   LYS   A CG   1 
ATOM   2678 C  CD   . LYS   B 2 47  ? -13.30121 19.95519  -18.42619 1.000 31.33506  ? 52   LYS   A CD   1 
ATOM   2679 C  CE   . LYS   B 2 47  ? -12.10412 19.01331  -18.52131 1.000 42.50474  ? 52   LYS   A CE   1 
ATOM   2680 N  NZ   . LYS   B 2 47  ? -12.49302 17.63826  -18.96525 1.000 34.03335  ? 52   LYS   A NZ   1 
ATOM   2681 N  N    . PHE   B 2 48  ? -15.98250 23.91892  -17.32296 1.000 38.45715  ? 53   PHE   A N    1 
ATOM   2682 C  CA   . PHE   B 2 48  ? -17.05063 24.86581  -17.60686 1.000 38.61287  ? 53   PHE   A CA   1 
ATOM   2683 C  C    . PHE   B 2 48  ? -17.95769 24.30370  -18.69276 1.000 41.43661  ? 53   PHE   A C    1 
ATOM   2684 O  O    . PHE   B 2 48  ? -17.47874 23.78273  -19.70680 1.000 33.47754  ? 53   PHE   A O    1 
ATOM   2685 C  CB   . PHE   B 2 48  ? -16.48182 26.21186  -18.05294 1.000 35.92067  ? 53   PHE   A CB   1 
ATOM   2686 C  CG   . PHE   B 2 48  ? -15.90379 27.03393  -16.93801 1.000 35.90331  ? 53   PHE   A CG   1 
ATOM   2687 C  CD1  . PHE   B 2 48  ? -16.72474 27.58486  -15.96893 1.000 42.81066  ? 53   PHE   A CD1  1 
ATOM   2688 C  CD2  . PHE   B 2 48  ? -14.54281 27.28108  -16.87415 1.000 40.48951  ? 53   PHE   A CD2  1 
ATOM   2689 C  CE1  . PHE   B 2 48  ? -16.19872 28.35393  -14.94399 1.000 37.73394  ? 53   PHE   A CE1  1 
ATOM   2690 C  CE2  . PHE   B 2 48  ? -14.00678 28.05215  -15.85422 1.000 38.50104  ? 53   PHE   A CE2  1 
ATOM   2691 C  CZ   . PHE   B 2 48  ? -14.83573 28.58607  -14.88614 1.000 38.23702  ? 53   PHE   A CZ   1 
ATOM   2692 N  N    . SER   B 2 49  ? -19.26768 24.41156  -18.48662 1.000 34.92099  ? 54   SER   A N    1 
ATOM   2693 C  CA   . SER   B 2 49  ? -20.19874 24.00045  -19.52452 1.000 39.81717  ? 54   SER   A CA   1 
ATOM   2694 C  C    . SER   B 2 49  ? -20.03897 24.90745  -20.74354 1.000 37.96819  ? 54   SER   A C    1 
ATOM   2695 O  O    . SER   B 2 49  ? -19.73308 26.09749  -20.60759 1.000 37.79121  ? 54   SER   A O    1 
ATOM   2696 C  CB   . SER   B 2 49  ? -21.63770 24.05331  -19.01136 1.000 42.59187  ? 54   SER   A CB   1 
ATOM   2697 O  OG   . SER   B 2 49  ? -21.99779 25.37228  -18.63134 1.000 38.38626  ? 54   SER   A OG   1 
ATOM   2698 N  N    . PRO   B 2 50  ? -20.23904 24.37242  -21.95152 1.000 36.15306  ? 55   PRO   A N    1 
ATOM   2699 C  CA   . PRO   B 2 50  ? -20.04525 25.20142  -23.15355 1.000 35.42511  ? 55   PRO   A CA   1 
ATOM   2700 C  C    . PRO   B 2 50  ? -20.89639 26.45933  -23.17547 1.000 42.95581  ? 55   PRO   A C    1 
ATOM   2701 O  O    . PRO   B 2 50  ? -20.45155 27.48037  -23.71753 1.000 43.40124  ? 55   PRO   A O    1 
ATOM   2702 C  CB   . PRO   B 2 50  ? -20.41327 24.24437  -24.29550 1.000 38.06035  ? 55   PRO   A CB   1 
ATOM   2703 C  CG   . PRO   B 2 50  ? -20.11707 22.88841  -23.74451 1.000 35.96328  ? 55   PRO   A CG   1 
ATOM   2704 C  CD   . PRO   B 2 50  ? -20.48993 22.96139  -22.28847 1.000 33.33920  ? 55   PRO   A CD   1 
ATOM   2705 N  N    . ASN   B 2 51  ? -22.10432 26.43021  -22.61135 1.000 42.97909  ? 56   ASN   A N    1 
ATOM   2706 C  CA   . ASN   B 2 51  ? -22.91744 27.63813  -22.56228 1.000 40.13415  ? 56   ASN   A CA   1 
ATOM   2707 C  C    . ASN   B 2 51  ? -22.47543 28.59819  -21.46334 1.000 48.69792  ? 56   ASN   A C    1 
ATOM   2708 O  O    . ASN   B 2 51  ? -23.12352 29.63413  -21.27128 1.000 43.05464  ? 56   ASN   A O    1 
ATOM   2709 C  CB   . ASN   B 2 51  ? -24.40139 27.28498  -22.38812 1.000 42.43774  ? 56   ASN   A CB   1 
ATOM   2710 C  CG   . ASN   B 2 51  ? -24.71218 26.67096  -21.03407 1.000 38.02360  ? 56   ASN   A CG   1 
ATOM   2711 O  OD1  . ASN   B 2 51  ? -23.91409 26.73206  -20.10116 1.000 43.22662  ? 56   ASN   A OD1  1 
ATOM   2712 N  ND2  . ASN   B 2 51  ? -25.89611 26.08284  -20.92194 1.000 40.69304  ? 56   ASN   A ND2  1 
ATOM   2713 N  N    . GLY   B 2 52  ? -21.40032 28.28031  -20.74344 1.000 42.22673  ? 57   GLY   A N    1 
ATOM   2714 C  CA   . GLY   B 2 52  ? -20.84731 29.16238  -19.73751 1.000 40.30294  ? 57   GLY   A CA   1 
ATOM   2715 C  C    . GLY   B 2 52  ? -21.63218 29.25832  -18.44843 1.000 38.67773  ? 57   GLY   A C    1 
ATOM   2716 O  O    . GLY   B 2 52  ? -21.21716 30.00037  -17.54749 1.000 44.35625  ? 57   GLY   A O    1 
ATOM   2717 N  N    . GLU   B 2 53  ? -22.74209 28.53320  -18.32131 1.000 41.11595  ? 58   GLU   A N    1 
ATOM   2718 C  CA   . GLU   B 2 53  ? -23.59498 28.67813  -17.14722 1.000 42.38669  ? 58   GLU   A CA   1 
ATOM   2719 C  C    . GLU   B 2 53  ? -23.05278 27.93920  -15.93227 1.000 48.28267  ? 58   GLU   A C    1 
ATOM   2720 O  O    . GLU   B 2 53  ? -23.26670 28.38519  -14.79925 1.000 48.28690  ? 58   GLU   A O    1 
ATOM   2721 C  CB   . GLU   B 2 53  ? -25.00796 28.17898  -17.46006 1.000 50.24821  ? 58   GLU   A CB   1 
ATOM   2722 C  CG   . GLU   B 2 53  ? -25.77816 29.06888  -18.41299 1.000 56.88940  ? 58   GLU   A CG   1 
ATOM   2723 C  CD   . GLU   B 2 53  ? -26.11023 30.41686  -17.80298 1.000 56.90364  ? 58   GLU   A CD   1 
ATOM   2724 O  OE1  . GLU   B 2 53  ? -26.89713 30.45279  -16.83389 1.000 67.71545  ? 58   GLU   A OE1  1 
ATOM   2725 O  OE2  . GLU   B 2 53  ? -25.57339 31.43691  -18.28205 1.000 66.43129  ? 58   GLU   A OE2  1 
ATOM   2726 N  N    . TRP   B 2 54  ? -22.35668 26.82127  -16.13132 1.000 48.92042  ? 59   TRP   A N    1 
ATOM   2727 C  CA   . TRP   B 2 54  ? -22.08847 25.90031  -15.04034 1.000 44.93601  ? 59   TRP   A CA   1 
ATOM   2728 C  C    . TRP   B 2 54  ? -20.62842 25.48247  -15.00549 1.000 46.77496  ? 59   TRP   A C    1 
ATOM   2729 O  O    . TRP   B 2 54  ? -19.88854 25.59953  -15.98557 1.000 41.31550  ? 59   TRP   A O    1 
ATOM   2730 C  CB   . TRP   B 2 54  ? -22.97435 24.65722  -15.15023 1.000 39.82338  ? 59   TRP   A CB   1 
ATOM   2731 C  CG   . TRP   B 2 54  ? -24.42140 24.99407  -15.25008 1.000 47.19877  ? 59   TRP   A CG   1 
ATOM   2732 C  CD1  . TRP   B 2 54  ? -25.19051 24.98797  -16.37600 1.000 46.93053  ? 59   TRP   A CD1  1 
ATOM   2733 C  CD2  . TRP   B 2 54  ? -25.27433 25.41499  -14.18200 1.000 49.89975  ? 59   TRP   A CD2  1 
ATOM   2734 N  NE1  . TRP   B 2 54  ? -26.47452 25.36984  -16.07387 1.000 48.24590  ? 59   TRP   A NE1  1 
ATOM   2735 C  CE2  . TRP   B 2 54  ? -26.55141 25.63785  -14.73287 1.000 52.01290  ? 59   TRP   A CE2  1 
ATOM   2736 C  CE3  . TRP   B 2 54  ? -25.08620 25.61903  -12.81202 1.000 50.74657  ? 59   TRP   A CE3  1 
ATOM   2737 C  CZ2  . TRP   B 2 54  ? -27.63237 26.05375  -13.96076 1.000 51.47689  ? 59   TRP   A CZ2  1 
ATOM   2738 C  CZ3  . TRP   B 2 54  ? -26.16017 26.03193  -12.04891 1.000 51.66166  ? 59   TRP   A CZ3  1 
ATOM   2739 C  CH2  . TRP   B 2 54  ? -27.41525 26.24579  -12.62378 1.000 53.87973  ? 59   TRP   A CH2  1 
ATOM   2740 N  N    . LEU   B 2 55  ? -20.22825 24.98652  -13.83753 1.000 42.87158  ? 60   LEU   A N    1 
ATOM   2741 C  CA   . LEU   B 2 55  ? -18.94616 24.33066  -13.62865 1.000 41.02783  ? 60   LEU   A CA   1 
ATOM   2742 C  C    . LEU   B 2 55  ? -19.19995 22.94564  -13.05361 1.000 44.19429  ? 60   LEU   A C    1 
ATOM   2743 O  O    . LEU   B 2 55  ? -19.92683 22.80458  -12.06553 1.000 41.89020  ? 60   LEU   A O    1 
ATOM   2744 C  CB   . LEU   B 2 55  ? -18.05714 25.14176  -12.68176 1.000 38.37580  ? 60   LEU   A CB   1 
ATOM   2745 C  CG   . LEU   B 2 55  ? -16.69704 24.52991  -12.33989 1.000 37.19615  ? 60   LEU   A CG   1 
ATOM   2746 C  CD1  . LEU   B 2 55  ? -15.71818 24.68400  -13.49800 1.000 40.85654  ? 60   LEU   A CD1  1 
ATOM   2747 C  CD2  . LEU   B 2 55  ? -16.12997 25.13399  -11.06196 1.000 36.87203  ? 60   LEU   A CD2  1 
ATOM   2748 N  N    . ALA   B 2 56  ? -18.61691 21.92869  -13.67866 1.000 40.58693  ? 61   ALA   A N    1 
ATOM   2749 C  CA   . ALA   B 2 56  ? -18.70372 20.56169  -13.18863 1.000 42.62598  ? 61   ALA   A CA   1 
ATOM   2750 C  C    . ALA   B 2 56  ? -17.36261 20.15784  -12.59777 1.000 42.92805  ? 61   ALA   A C    1 
ATOM   2751 O  O    . ALA   B 2 56  ? -16.31070 20.42394  -13.18488 1.000 40.63693  ? 61   ALA   A O    1 
ATOM   2752 C  CB   . ALA   B 2 56  ? -19.10073 19.59263  -14.30458 1.000 39.43338  ? 61   ALA   A CB   1 
ATOM   2753 N  N    . SER   B 2 57  ? -17.40542 19.52585  -11.42775 1.000 41.20960  ? 62   SER   A N    1 
ATOM   2754 C  CA   . SER   B 2 57  ? -16.20530 19.03998  -10.76587 1.000 43.89959  ? 62   SER   A CA   1 
ATOM   2755 C  C    . SER   B 2 57  ? -16.37711 17.56897  -10.41684 1.000 44.56919  ? 62   SER   A C    1 
ATOM   2756 O  O    . SER   B 2 57  ? -17.45602 17.14486  -9.99872  1.000 40.04547  ? 62   SER   A O    1 
ATOM   2757 C  CB   . SER   B 2 57  ? -15.89925 19.85303  -9.50192  1.000 38.95266  ? 62   SER   A CB   1 
ATOM   2758 O  OG   . SER   B 2 57  ? -16.97715 19.78993  -8.58780  1.000 42.59633  ? 62   SER   A OG   1 
ATOM   2759 N  N    . SER   B 2 58  ? -15.31705 16.79508  -10.60594 1.000 40.60468  ? 63   SER   A N    1 
ATOM   2760 C  CA   . SER   B 2 58  ? -15.27686 15.40209  -10.19692 1.000 44.04133  ? 63   SER   A CA   1 
ATOM   2761 C  C    . SER   B 2 58  ? -14.28273 15.26021  -9.05203  1.000 39.98082  ? 63   SER   A C    1 
ATOM   2762 O  O    . SER   B 2 58  ? -13.34280 16.05031  -8.92914  1.000 40.75859  ? 63   SER   A O    1 
ATOM   2763 C  CB   . SER   B 2 58  ? -14.88089 14.49511  -11.36795 1.000 36.14491  ? 63   SER   A CB   1 
ATOM   2764 O  OG   . SER   B 2 58  ? -13.71001 14.97223  -12.00808 1.000 34.44600  ? 63   SER   A OG   1 
ATOM   2765 N  N    . SER   B 2 59  ? -14.50053 14.26719  -8.19399  1.000 39.54545  ? 64   SER   A N    1 
ATOM   2766 C  CA   . SER   B 2 59  ? -13.59740 14.11730  -7.06108  1.000 34.43844  ? 64   SER   A CA   1 
ATOM   2767 C  C    . SER   B 2 59  ? -13.19822 12.66235  -6.85311  1.000 47.29293  ? 64   SER   A C    1 
ATOM   2768 O  O    . SER   B 2 59  ? -13.84118 11.73027  -7.34703  1.000 36.91976  ? 64   SER   A O    1 
ATOM   2769 C  CB   . SER   B 2 59  ? -14.21532 14.66725  -5.77203  1.000 34.54817  ? 64   SER   A CB   1 
ATOM   2770 O  OG   . SER   B 2 59  ? -13.31919 14.50436  -4.68212  1.000 36.53211  ? 64   SER   A OG   1 
ATOM   2771 N  N    . ALA   B 2 60  ? -12.10313 12.49147  -6.10722  1.000 38.46514  ? 65   ALA   A N    1 
ATOM   2772 C  CA   . ALA   B 2 60  ? -11.74894 11.17651  -5.59324  1.000 35.85100  ? 65   ALA   A CA   1 
ATOM   2773 C  C    . ALA   B 2 60  ? -12.77878 10.66742  -4.59913  1.000 40.11189  ? 65   ALA   A C    1 
ATOM   2774 O  O    . ALA   B 2 60  ? -12.77362 9.47542   -4.27211  1.000 43.49267  ? 65   ALA   A O    1 
ATOM   2775 C  CB   . ALA   B 2 60  ? -10.36487 11.21767  -4.94239  1.000 39.14718  ? 65   ALA   A CB   1 
ATOM   2776 N  N    . ASP   B 2 61  ? -13.66182 11.53833  -4.11104  1.000 40.87449  ? 66   ASP   A N    1 
ATOM   2777 C  CA   . ASP   B 2 61  ? -14.73568 11.13423  -3.21793  1.000 37.15763  ? 66   ASP   A CA   1 
ATOM   2778 C  C    . ASP   B 2 61  ? -15.88769 10.45810  -3.94880  1.000 39.32723  ? 66   ASP   A C    1 
ATOM   2779 O  O    . ASP   B 2 61  ? -16.93960 10.22600  -3.34468  1.000 39.60104  ? 66   ASP   A O    1 
ATOM   2780 C  CB   . ASP   B 2 61  ? -15.24772 12.34219  -2.42089  1.000 40.39674  ? 66   ASP   A CB   1 
ATOM   2781 C  CG   . ASP   B 2 61  ? -15.93892 13.38011  -3.29083  1.000 44.50349  ? 66   ASP   A CG   1 
ATOM   2782 O  OD1  . ASP   B 2 61  ? -16.22102 13.10306  -4.47580  1.000 40.70461  ? 66   ASP   A OD1  1 
ATOM   2783 O  OD2  . ASP   B 2 61  ? -16.20698 14.48709  -2.77581  1.000 39.38002  ? 66   ASP   A OD2  1 
ATOM   2784 N  N    . LYS   B 2 62  ? -15.71279 10.14611  -5.23281  1.000 35.14927  ? 67   LYS   A N    1 
ATOM   2785 C  CA   . LYS   B 2 62  ? -16.67580 9.42199   -6.05670  1.000 39.29403  ? 67   LYS   A CA   1 
ATOM   2786 C  C    . LYS   B 2 62  ? -17.83394 10.30187  -6.51159  1.000 38.12130  ? 67   LYS   A C    1 
ATOM   2787 O  O    . LYS   B 2 62  ? -18.79495 9.78276   -7.09348  1.000 39.88329  ? 67   LYS   A O    1 
ATOM   2788 C  CB   . LYS   B 2 62  ? -17.23660 8.19594   -5.32662  1.000 44.05003  ? 67   LYS   A CB   1 
ATOM   2789 C  CG   . LYS   B 2 62  ? -16.16344 7.24506   -4.81773  1.000 48.80834  ? 67   LYS   A CG   1 
ATOM   2790 C  CD   . LYS   B 2 62  ? -16.76225 6.00601   -4.16365  1.000 55.97235  ? 67   LYS   A CD   1 
ATOM   2791 C  CE   . LYS   B 2 62  ? -17.11312 6.24799   -2.70161  1.000 50.61864  ? 67   LYS   A CE   1 
ATOM   2792 N  NZ   . LYS   B 2 62  ? -17.55791 4.98995   -2.03455  1.000 63.29466  ? 67   LYS   A NZ   1 
ATOM   2793 N  N    . LEU   B 2 63  ? -17.77505 11.60988  -6.28361  1.000 37.79224  ? 68   LEU   A N    1 
ATOM   2794 C  CA   . LEU   B 2 63  ? -18.89817 12.49176  -6.54150  1.000 39.82871  ? 68   LEU   A CA   1 
ATOM   2795 C  C    . LEU   B 2 63  ? -18.59439 13.46577  -7.67055  1.000 39.95587  ? 68   LEU   A C    1 
ATOM   2796 O  O    . LEU   B 2 63  ? -17.44846 13.89389  -7.86568  1.000 41.49802  ? 68   LEU   A O    1 
ATOM   2797 C  CB   . LEU   B 2 63  ? -19.27512 13.27873  -5.28048  1.000 39.78169  ? 68   LEU   A CB   1 
ATOM   2798 C  CG   . LEU   B 2 63  ? -19.65891 12.46571  -4.04442  1.000 42.24620  ? 68   LEU   A CG   1 
ATOM   2799 C  CD1  . LEU   B 2 63  ? -19.95788 13.38869  -2.87040  1.000 37.90565  ? 68   LEU   A CD1  1 
ATOM   2800 C  CD2  . LEU   B 2 63  ? -20.84484 11.55858  -4.33929  1.000 41.53134  ? 68   LEU   A CD2  1 
ATOM   2801 N  N    . ILE   B 2 64  ? -19.65051 13.80665  -8.42044  1.000 44.21490  ? 69   ILE   A N    1 
ATOM   2802 C  CA   . ILE   B 2 64  ? -19.65072 14.94764  -9.32346  1.000 41.66554  ? 69   ILE   A CA   1 
ATOM   2803 C  C    . ILE   B 2 64  ? -20.45777 16.04757  -8.65139  1.000 45.18972  ? 69   ILE   A C    1 
ATOM   2804 O  O    . ILE   B 2 64  ? -21.38666 15.77748  -7.88728  1.000 47.54149  ? 69   ILE   A O    1 
ATOM   2805 C  CB   . ILE   B 2 64  ? -20.24383 14.57656  -10.69939 1.000 41.78970  ? 69   ILE   A CB   1 
ATOM   2806 C  CG1  . ILE   B 2 64  ? -19.41578 13.46564  -11.35246 1.000 44.35429  ? 69   ILE   A CG1  1 
ATOM   2807 C  CG2  . ILE   B 2 64  ? -20.32305 15.80054  -11.60140 1.000 38.65198  ? 69   ILE   A CG2  1 
ATOM   2808 C  CD1  . ILE   B 2 64  ? -20.07185 12.85256  -12.57239 1.000 45.59452  ? 69   ILE   A CD1  1 
ATOM   2809 N  N    . LYS   B 2 65  ? -20.10193 17.29460  -8.91944  1.000 41.83679  ? 70   LYS   A N    1 
ATOM   2810 C  CA   . LYS   B 2 65  ? -20.81298 18.42053  -8.33438  1.000 41.30372  ? 70   LYS   A CA   1 
ATOM   2811 C  C    . LYS   B 2 65  ? -20.93421 19.53451  -9.36138  1.000 48.03299  ? 70   LYS   A C    1 
ATOM   2812 O  O    . LYS   B 2 65  ? -19.98331 19.83060  -10.09149 1.000 50.55365  ? 70   LYS   A O    1 
ATOM   2813 C  CB   . LYS   B 2 65  ? -20.12290 18.92462  -7.05946  1.000 42.92959  ? 70   LYS   A CB   1 
ATOM   2814 C  CG   . LYS   B 2 65  ? -20.32268 17.99862  -5.86043  1.000 45.68784  ? 70   LYS   A CG   1 
ATOM   2815 C  CD   . LYS   B 2 65  ? -19.66960 18.54170  -4.59850  1.000 43.04123  ? 70   LYS   A CD   1 
ATOM   2816 C  CE   . LYS   B 2 65  ? -19.86338 17.58870  -3.42247  1.000 41.66496  ? 70   LYS   A CE   1 
ATOM   2817 N  NZ   . LYS   B 2 65  ? -21.29432 17.47655  -3.01032  1.000 33.32765  ? 70   LYS   A NZ   1 
ATOM   2818 N  N    . ILE   B 2 66  ? -22.12227 20.13238  -9.41226  1.000 49.98512  ? 71   ILE   A N    1 
ATOM   2819 C  CA   . ILE   B 2 66  ? -22.45948 21.18833  -10.35824 1.000 38.62218  ? 71   ILE   A CA   1 
ATOM   2820 C  C    . ILE   B 2 66  ? -22.59654 22.48933  -9.58224  1.000 51.53529  ? 71   ILE   A C    1 
ATOM   2821 O  O    . ILE   B 2 66  ? -23.34044 22.54927  -8.58817  1.000 43.10181  ? 71   ILE   A O    1 
ATOM   2822 C  CB   . ILE   B 2 66  ? -23.75453 20.86819  -11.12010 1.000 44.65822  ? 71   ILE   A CB   1 
ATOM   2823 C  CG1  . ILE   B 2 66  ? -23.64746 19.50219  -11.80209 1.000 43.14233  ? 71   ILE   A CG1  1 
ATOM   2824 C  CG2  . ILE   B 2 66  ? -24.05775 21.96315  -12.13308 1.000 45.13487  ? 71   ILE   A CG2  1 
ATOM   2825 C  CD1  . ILE   B 2 66  ? -22.56756 19.43029  -12.86021 1.000 37.40088  ? 71   ILE   A CD1  1 
ATOM   2826 N  N    . TRP   B 2 67  ? -21.88869 23.52240  -10.05033 1.000 45.20942  ? 72   TRP   A N    1 
ATOM   2827 C  CA   . TRP   B 2 67  ? -21.82077 24.83541  -9.42436  1.000 48.26066  ? 72   TRP   A CA   1 
ATOM   2828 C  C    . TRP   B 2 67  ? -22.14299 25.91437  -10.45134 1.000 52.73080  ? 72   TRP   A C    1 
ATOM   2829 O  O    . TRP   B 2 67  ? -22.01509 25.71036  -11.66135 1.000 45.65766  ? 72   TRP   A O    1 
ATOM   2830 C  CB   . TRP   B 2 67  ? -20.42673 25.11857  -8.84551  1.000 46.61449  ? 72   TRP   A CB   1 
ATOM   2831 C  CG   . TRP   B 2 67  ? -19.75654 23.93964  -8.21456  1.000 47.21200  ? 72   TRP   A CG   1 
ATOM   2832 C  CD1  . TRP   B 2 67  ? -19.21550 22.85769  -8.85460  1.000 46.39701  ? 72   TRP   A CD1  1 
ATOM   2833 C  CD2  . TRP   B 2 67  ? -19.52138 23.73869  -6.81858  1.000 48.00373  ? 72   TRP   A CD2  1 
ATOM   2834 N  NE1  . TRP   B 2 67  ? -18.67631 21.99076  -7.93865  1.000 39.38961  ? 72   TRP   A NE1  1 
ATOM   2835 C  CE2  . TRP   B 2 67  ? -18.84923 22.50776  -6.68064  1.000 45.10505  ? 72   TRP   A CE2  1 
ATOM   2836 C  CE3  . TRP   B 2 67  ? -19.82433 24.47667  -5.66956  1.000 47.65932  ? 72   TRP   A CE3  1 
ATOM   2837 C  CZ2  . TRP   B 2 67  ? -18.47005 21.99881  -5.43867  1.000 43.11213  ? 72   TRP   A CZ2  1 
ATOM   2838 C  CZ3  . TRP   B 2 67  ? -19.44415 23.97173  -4.43660  1.000 47.74215  ? 72   TRP   A CZ3  1 
ATOM   2839 C  CH2  . TRP   B 2 67  ? -18.77601 22.74480  -4.33165  1.000 43.22082  ? 72   TRP   A CH2  1 
ATOM   2840 N  N    . GLY   B 2 68  ? -22.53306 27.08233  -9.94731  1.000 53.70225  ? 73   GLY   A N    1 
ATOM   2841 C  CA   . GLY   B 2 68  ? -22.72827 28.23030  -10.81930 1.000 47.60485  ? 73   GLY   A CA   1 
ATOM   2842 C  C    . GLY   B 2 68  ? -21.39137 28.77043  -11.30445 1.000 48.66246  ? 73   GLY   A C    1 
ATOM   2843 O  O    . GLY   B 2 68  ? -20.47732 29.01454  -10.50655 1.000 45.24871  ? 73   GLY   A O    1 
ATOM   2844 N  N    . ALA   B 2 69  ? -21.27553 28.96743  -12.61947 1.000 44.41250  ? 74   ALA   A N    1 
ATOM   2845 C  CA   . ALA   B 2 69  ? -19.98663 29.32656  -13.20361 1.000 46.13019  ? 74   ALA   A CA   1 
ATOM   2846 C  C    . ALA   B 2 69  ? -19.49773 30.68961  -12.73168 1.000 49.25907  ? 74   ALA   A C    1 
ATOM   2847 O  O    . ALA   B 2 69  ? -18.28474 30.90874  -12.63281 1.000 47.16541  ? 74   ALA   A O    1 
ATOM   2848 C  CB   . ALA   B 2 69  ? -20.07879 29.29753  -14.72960 1.000 38.14147  ? 74   ALA   A CB   1 
ATOM   2849 N  N    . TYR   B 2 70  ? -20.40879 31.61652  -12.43859 1.000 46.91151  ? 75   TYR   A N    1 
ATOM   2850 C  CA   . TYR   B 2 70  ? -20.03390 32.98757  -12.11565 1.000 50.68474  ? 75   TYR   A CA   1 
ATOM   2851 C  C    . TYR   B 2 70  ? -19.97177 33.26259  -10.61966 1.000 55.23946  ? 75   TYR   A C    1 
ATOM   2852 O  O    . TYR   B 2 70  ? -19.03479 33.91770  -10.15577 1.000 56.46909  ? 75   TYR   A O    1 
ATOM   2853 C  CB   . TYR   B 2 70  ? -21.01107 33.96846  -12.77656 1.000 46.82158  ? 75   TYR   A CB   1 
ATOM   2854 C  CG   . TYR   B 2 70  ? -21.13121 33.77042  -14.27054 1.000 45.44482  ? 75   TYR   A CG   1 
ATOM   2855 C  CD1  . TYR   B 2 70  ? -20.14235 34.22352  -15.13065 1.000 38.82278  ? 75   TYR   A CD1  1 
ATOM   2856 C  CD2  . TYR   B 2 70  ? -22.23120 33.12230  -14.81842 1.000 43.07506  ? 75   TYR   A CD2  1 
ATOM   2857 C  CE1  . TYR   B 2 70  ? -20.24547 34.04049  -16.49664 1.000 43.86533  ? 75   TYR   A CE1  1 
ATOM   2858 C  CE2  . TYR   B 2 70  ? -22.34332 32.93627  -16.18240 1.000 46.51206  ? 75   TYR   A CE2  1 
ATOM   2859 C  CZ   . TYR   B 2 70  ? -21.34746 33.39737  -17.01852 1.000 44.97105  ? 75   TYR   A CZ   1 
ATOM   2860 O  OH   . TYR   B 2 70  ? -21.45358 33.21334  -18.37850 1.000 45.30327  ? 75   TYR   A OH   1 
ATOM   2861 N  N    . ASP   B 2 71  ? -20.94464 32.77850  -9.85155  1.000 50.99705  ? 76   ASP   A N    1 
ATOM   2862 C  CA   . ASP   B 2 71  ? -20.96751 32.99552  -8.41155  1.000 56.36087  ? 76   ASP   A CA   1 
ATOM   2863 C  C    . ASP   B 2 71  ? -20.49630 31.78558  -7.61758  1.000 52.63511  ? 76   ASP   A C    1 
ATOM   2864 O  O    . ASP   B 2 71  ? -20.38118 31.87860  -6.39060  1.000 58.67835  ? 76   ASP   A O    1 
ATOM   2865 C  CB   . ASP   B 2 71  ? -22.38150 33.38437  -7.95841  1.000 53.61595  ? 76   ASP   A CB   1 
ATOM   2866 C  CG   . ASP   B 2 71  ? -23.42744 32.37226  -8.38328  1.000 53.39781  ? 76   ASP   A CG   1 
ATOM   2867 O  OD1  . ASP   B 2 71  ? -23.04637 31.26729  -8.82631  1.000 57.04487  ? 76   ASP   A OD1  1 
ATOM   2868 O  OD2  . ASP   B 2 71  ? -24.63246 32.68213  -8.27916  1.000 59.90510  ? 76   ASP   A OD2  1 
ATOM   2869 N  N    . GLY   B 2 72  ? -20.21525 30.66360  -8.27660  1.000 56.16667  ? 77   GLY   A N    1 
ATOM   2870 C  CA   . GLY   B 2 72  ? -19.81905 29.46065  -7.57263  1.000 48.33859  ? 77   GLY   A CA   1 
ATOM   2871 C  C    . GLY   B 2 72  ? -20.89090 28.85855  -6.69651  1.000 51.84778  ? 77   GLY   A C    1 
ATOM   2872 O  O    . GLY   B 2 72  ? -20.58072 28.00059  -5.86353  1.000 52.53988  ? 77   GLY   A O    1 
ATOM   2873 N  N    . LYS   B 2 73  ? -22.14196 29.27741  -6.85438  1.000 53.72786  ? 78   LYS   A N    1 
ATOM   2874 C  CA   . LYS   B 2 73  ? -23.22182 28.75331  -6.02926  1.000 56.15182  ? 78   LYS   A CA   1 
ATOM   2875 C  C    . LYS   B 2 73  ? -23.39569 27.25929  -6.26922  1.000 52.12800  ? 78   LYS   A C    1 
ATOM   2876 O  O    . LYS   B 2 73  ? -23.59376 26.82425  -7.40719  1.000 50.92362  ? 78   LYS   A O    1 
ATOM   2877 C  CB   . LYS   B 2 73  ? -24.52093 29.49817  -6.33513  1.000 51.65566  ? 78   LYS   A CB   1 
ATOM   2878 C  CG   . LYS   B 2 73  ? -25.69079 29.09606  -5.44900  1.000 56.23298  ? 78   LYS   A CG   1 
ATOM   2879 C  CD   . LYS   B 2 73  ? -26.98291 29.75792  -5.90387  1.000 58.00286  ? 78   LYS   A CD   1 
ATOM   2880 C  CE   . LYS   B 2 73  ? -27.63787 30.52887  -4.76982  1.000 70.04437  ? 78   LYS   A CE   1 
ATOM   2881 N  NZ   . LYS   B 2 73  ? -26.90897 31.79195  -4.46091  1.000 77.56466  ? 78   LYS   A NZ   1 
ATOM   2882 N  N    . PHE   B 2 74  ? -23.32149 26.47731  -5.19522  1.000 53.81750  ? 79   PHE   A N    1 
ATOM   2883 C  CA   . PHE   B 2 74  ? -23.53235 25.04129  -5.31018  1.000 44.95560  ? 79   PHE   A CA   1 
ATOM   2884 C  C    . PHE   B 2 74  ? -24.90239 24.75614  -5.90403  1.000 57.87443  ? 79   PHE   A C    1 
ATOM   2885 O  O    . PHE   B 2 74  ? -25.92339 25.25104  -5.41593  1.000 51.58556  ? 79   PHE   A O    1 
ATOM   2886 C  CB   . PHE   B 2 74  ? -23.39614 24.37132  -3.94418  1.000 48.52341  ? 79   PHE   A CB   1 
ATOM   2887 C  CG   . PHE   B 2 74  ? -23.74699 22.91028  -3.95013  1.000 51.39936  ? 79   PHE   A CG   1 
ATOM   2888 C  CD1  . PHE   B 2 74  ? -22.83494 21.96737  -4.39921  1.000 50.09407  ? 79   PHE   A CD1  1 
ATOM   2889 C  CD2  . PHE   B 2 74  ? -24.98890 22.47816  -3.51199  1.000 46.31951  ? 79   PHE   A CD2  1 
ATOM   2890 C  CE1  . PHE   B 2 74  ? -23.15180 20.62034  -4.40916  1.000 46.78597  ? 79   PHE   A CE1  1 
ATOM   2891 C  CE2  . PHE   B 2 74  ? -25.31376 21.13412  -3.52094  1.000 47.30220  ? 79   PHE   A CE2  1 
ATOM   2892 C  CZ   . PHE   B 2 74  ? -24.39271 20.20422  -3.97002  1.000 51.54939  ? 79   PHE   A CZ   1 
ATOM   2893 N  N    . GLU   B 2 75  ? -24.92442 23.96212  -6.97302  1.000 51.02416  ? 80   GLU   A N    1 
ATOM   2894 C  CA   . GLU   B 2 75  ? -26.17544 23.55298  -7.59688  1.000 45.28513  ? 80   GLU   A CA   1 
ATOM   2895 C  C    . GLU   B 2 75  ? -26.59025 22.14794  -7.19082  1.000 48.09369  ? 80   GLU   A C    1 
ATOM   2896 O  O    . GLU   B 2 75  ? -27.72618 21.94583  -6.75170  1.000 49.01971  ? 80   GLU   A O    1 
ATOM   2897 C  CB   . GLU   B 2 75  ? -26.07261 23.64497  -9.12489  1.000 50.17250  ? 80   GLU   A CB   1 
ATOM   2898 C  CG   . GLU   B 2 75  ? -27.36765 23.29783  -9.85375  1.000 49.90060  ? 80   GLU   A CG   1 
ATOM   2899 C  CD   . GLU   B 2 75  ? -28.47873 24.30472  -9.59765  1.000 55.80298  ? 80   GLU   A CD   1 
ATOM   2900 O  OE1  . GLU   B 2 75  ? -28.18479 25.40475  -9.08169  1.000 54.45561  ? 80   GLU   A OE1  1 
ATOM   2901 O  OE2  . GLU   B 2 75  ? -29.64773 23.99559  -9.91052  1.000 64.59039  ? 80   GLU   A OE2  1 
ATOM   2902 N  N    . LYS   B 2 76  ? -25.70316 21.16204  -7.31590  1.000 48.54237  ? 81   LYS   A N    1 
ATOM   2903 C  CA   . LYS   B 2 76  ? -26.15198 19.81099  -6.98083  1.000 44.03938  ? 81   LYS   A CA   1 
ATOM   2904 C  C    . LYS   B 2 76  ? -24.97887 18.84412  -6.90295  1.000 53.33635  ? 81   LYS   A C    1 
ATOM   2905 O  O    . LYS   B 2 76  ? -23.86395 19.14123  -7.33807  1.000 45.63365  ? 81   LYS   A O    1 
ATOM   2906 C  CB   . LYS   B 2 76  ? -27.18404 19.30487  -7.99172  1.000 39.33483  ? 81   LYS   A CB   1 
ATOM   2907 C  CG   . LYS   B 2 76  ? -26.60014 18.95992  -9.34878  1.000 46.09028  ? 81   LYS   A CG   1 
ATOM   2908 C  CD   . LYS   B 2 76  ? -27.68020 18.51679  -10.32266 1.000 41.14524  ? 81   LYS   A CD   1 
ATOM   2909 C  CE   . LYS   B 2 76  ? -28.69034 19.62468  -10.56756 1.000 47.13316  ? 81   LYS   A CE   1 
ATOM   2910 N  NZ   . LYS   B 2 76  ? -29.59843 19.30757  -11.70146 1.000 45.34960  ? 81   LYS   A NZ   1 
ATOM   2911 N  N    . THR   B 2 77  ? -25.26469 17.66909  -6.34090  1.000 49.25114  ? 82   THR   A N    1 
ATOM   2912 C  CA   . THR   B 2 77  ? -24.35457 16.53219  -6.31698  1.000 45.46862  ? 82   THR   A CA   1 
ATOM   2913 C  C    . THR   B 2 77  ? -24.91455 15.41612  -7.19191  1.000 48.66154  ? 82   THR   A C    1 
ATOM   2914 O  O    . THR   B 2 77  ? -26.11151 15.11499  -7.14278  1.000 46.37190  ? 82   THR   A O    1 
ATOM   2915 C  CB   . THR   B 2 77  ? -24.14237 16.00723  -4.89300  1.000 47.35948  ? 82   THR   A CB   1 
ATOM   2916 O  OG1  . THR   B 2 77  ? -23.41839 16.97132  -4.12009  1.000 40.65818  ? 82   THR   A OG1  1 
ATOM   2917 C  CG2  . THR   B 2 77  ? -23.36423 14.69331  -4.92006  1.000 44.30749  ? 82   THR   A CG2  1 
ATOM   2918 N  N    . ILE   B 2 78  ? -24.04257 14.80520  -7.98599  1.000 50.11388  ? 83   ILE   A N    1 
ATOM   2919 C  CA   . ILE   B 2 78  ? -24.38354 13.69715  -8.86994  1.000 47.75621  ? 83   ILE   A CA   1 
ATOM   2920 C  C    . ILE   B 2 78  ? -23.57237 12.48824  -8.42101  1.000 47.57298  ? 83   ILE   A C    1 
ATOM   2921 O  O    . ILE   B 2 78  ? -22.33537 12.55237  -8.33914  1.000 44.54341  ? 83   ILE   A O    1 
ATOM   2922 C  CB   . ILE   B 2 78  ? -24.11274 14.04616  -10.34098 1.000 41.85347  ? 83   ILE   A CB   1 
ATOM   2923 C  CG1  . ILE   B 2 78  ? -25.06490 15.15306  -10.80389 1.000 47.62088  ? 83   ILE   A CG1  1 
ATOM   2924 C  CG2  . ILE   B 2 78  ? -24.24070 12.81814  -11.21595 1.000 41.31588  ? 83   ILE   A CG2  1 
ATOM   2925 C  CD1  . ILE   B 2 78  ? -24.83210 15.61306  -12.22992 1.000 49.31935  ? 83   ILE   A CD1  1 
ATOM   2926 N  N    . SER   B 2 79  ? -24.26622 11.39218  -8.12192  1.000 47.59401  ? 84   SER   A N    1 
ATOM   2927 C  CA   . SER   B 2 79  ? -23.67804 10.21624  -7.50297  1.000 46.79720  ? 84   SER   A CA   1 
ATOM   2928 C  C    . SER   B 2 79  ? -23.96199 8.97320   -8.33493  1.000 45.61063  ? 84   SER   A C    1 
ATOM   2929 O  O    . SER   B 2 79  ? -24.91707 8.92409   -9.11682  1.000 40.83205  ? 84   SER   A O    1 
ATOM   2930 C  CB   . SER   B 2 79  ? -24.21487 10.01321  -6.07991  1.000 39.95149  ? 84   SER   A CB   1 
ATOM   2931 O  OG   . SER   B 2 79  ? -24.05391 11.18523  -5.29894  1.000 62.98973  ? 84   SER   A OG   1 
ATOM   2932 N  N    . GLY   B 2 80  ? -23.12487 7.95429   -8.14400  1.000 45.47759  ? 85   GLY   A N    1 
ATOM   2933 C  CA   . GLY   B 2 80  ? -23.31781 6.68127   -8.80996  1.000 42.41301  ? 85   GLY   A CA   1 
ATOM   2934 C  C    . GLY   B 2 80  ? -22.06573 5.83839   -8.89909  1.000 43.82802  ? 85   GLY   A C    1 
ATOM   2935 O  O    . GLY   B 2 80  ? -22.12158 4.61239   -8.75606  1.000 43.63130  ? 85   GLY   A O    1 
ATOM   2936 N  N    . HIS   B 2 81  ? -20.92282 6.47851   -9.13721  1.000 40.15644  ? 86   HIS   A N    1 
ATOM   2937 C  CA   . HIS   B 2 81  ? -19.67576 5.74464   -9.27634  1.000 42.57202  ? 86   HIS   A CA   1 
ATOM   2938 C  C    . HIS   B 2 81  ? -19.29555 5.06370   -7.96837  1.000 39.46437  ? 86   HIS   A C    1 
ATOM   2939 O  O    . HIS   B 2 81  ? -19.66348 5.50667   -6.87733  1.000 43.35286  ? 86   HIS   A O    1 
ATOM   2940 C  CB   . HIS   B 2 81  ? -18.55390 6.67575   -9.73447  1.000 36.72629  ? 86   HIS   A CB   1 
ATOM   2941 C  CG   . HIS   B 2 81  ? -18.52708 6.89373   -11.21447 1.000 36.91517  ? 86   HIS   A CG   1 
ATOM   2942 N  ND1  . HIS   B 2 81  ? -18.33707 5.86574   -12.11348 1.000 37.21279  ? 86   HIS   A ND1  1 
ATOM   2943 C  CD2  . HIS   B 2 81  ? -18.66828 8.01871   -11.95447 1.000 39.11544  ? 86   HIS   A CD2  1 
ATOM   2944 C  CE1  . HIS   B 2 81  ? -18.36125 6.34772   -13.34248 1.000 36.89783  ? 86   HIS   A CE1  1 
ATOM   2945 N  NE2  . HIS   B 2 81  ? -18.55838 7.65170   -13.27448 1.000 34.50436  ? 86   HIS   A NE2  1 
ATOM   2946 N  N    . LYS   B 2 82  ? -18.55045 3.96677   -8.09043  1.000 40.62605  ? 87   LYS   A N    1 
ATOM   2947 C  CA   . LYS   B 2 82  ? -18.14724 3.16083   -6.94846  1.000 44.01471  ? 87   LYS   A CA   1 
ATOM   2948 C  C    . LYS   B 2 82  ? -16.71922 3.43198   -6.49462  1.000 43.40652  ? 87   LYS   A C    1 
ATOM   2949 O  O    . LYS   B 2 82  ? -16.34606 3.00404   -5.39865  1.000 45.47781  ? 87   LYS   A O    1 
ATOM   2950 C  CB   . LYS   B 2 82  ? -18.30712 1.67081   -7.27743  1.000 40.91929  ? 87   LYS   A CB   1 
ATOM   2951 C  CG   . LYS   B 2 82  ? -19.69813 1.30866   -7.77028  1.000 47.93370  ? 87   LYS   A CG   1 
ATOM   2952 C  CD   . LYS   B 2 82  ? -19.84800 -0.18736  -7.99824  1.000 55.09088  ? 87   LYS   A CD   1 
ATOM   2953 C  CE   . LYS   B 2 82  ? -21.28800 -0.54652  -8.33709  1.000 54.72194  ? 87   LYS   A CE   1 
ATOM   2954 N  NZ   . LYS   B 2 82  ? -21.47086 -2.01654  -8.49305  1.000 62.97595  ? 87   LYS   A NZ   1 
ATOM   2955 N  N    . LEU   B 2 83  ? -15.92338 4.12706   -7.30371  1.000 38.68987  ? 88   LEU   A N    1 
ATOM   2956 C  CA   . LEU   B 2 83  ? -14.57538 4.53220   -6.93386  1.000 40.60845  ? 88   LEU   A CA   1 
ATOM   2957 C  C    . LEU   B 2 83  ? -14.36358 5.96522   -7.40190  1.000 39.12423  ? 88   LEU   A C    1 
ATOM   2958 O  O    . LEU   B 2 83  ? -15.26171 6.58912   -7.97781  1.000 39.59289  ? 88   LEU   A O    1 
ATOM   2959 C  CB   . LEU   B 2 83  ? -13.52335 3.58530   -7.52996  1.000 37.86950  ? 88   LEU   A CB   1 
ATOM   2960 C  CG   . LEU   B 2 83  ? -13.58515 2.12730   -7.06793  1.000 36.08009  ? 88   LEU   A CG   1 
ATOM   2961 C  CD1  . LEU   B 2 83  ? -12.45413 1.31341   -7.67504  1.000 40.92190  ? 88   LEU   A CD1  1 
ATOM   2962 C  CD2  . LEU   B 2 83  ? -13.55498 2.04433   -5.54893  1.000 52.25178  ? 88   LEU   A CD2  1 
ATOM   2963 N  N    . GLY   B 2 84  ? -13.16861 6.49235   -7.14803  1.000 34.66207  ? 89   GLY   A N    1 
ATOM   2964 C  CA   . GLY   B 2 84  ? -12.84579 7.85338   -7.53208  1.000 34.05494  ? 89   GLY   A CA   1 
ATOM   2965 C  C    . GLY   B 2 84  ? -13.08798 8.14433   -8.99806  1.000 41.66666  ? 89   GLY   A C    1 
ATOM   2966 O  O    . GLY   B 2 84  ? -13.09597 7.22832   -9.82605  1.000 37.85976  ? 89   GLY   A O    1 
ATOM   2967 N  N    . ILE   B 2 85  ? -13.28515 9.41931   -9.33206  1.000 33.21566  ? 90   ILE   A N    1 
ATOM   2968 C  CA   . ILE   B 2 85  ? -13.52534 9.86526   -10.70004 1.000 32.02805  ? 90   ILE   A CA   1 
ATOM   2969 C  C    . ILE   B 2 85  ? -12.34347 10.72338  -11.13417 1.000 30.25922  ? 90   ILE   A C    1 
ATOM   2970 O  O    . ILE   B 2 85  ? -11.92649 11.62943  -10.40023 1.000 33.80319  ? 90   ILE   A O    1 
ATOM   2971 C  CB   . ILE   B 2 85  ? -14.84143 10.65012  -10.81591 1.000 39.01836  ? 90   ILE   A CB   1 
ATOM   2972 C  CG1  . ILE   B 2 85  ? -16.01329 9.81801   -10.28077 1.000 36.19895  ? 90   ILE   A CG1  1 
ATOM   2973 C  CG2  . ILE   B 2 85  ? -15.09363 11.05508  -12.26089 1.000 37.08788  ? 90   ILE   A CG2  1 
ATOM   2974 C  CD1  . ILE   B 2 85  ? -17.31936 10.58087  -10.21365 1.000 30.52759  ? 90   ILE   A CD1  1 
ATOM   2975 N  N    . SER   B 2 86  ? -11.80957 10.44242  -12.32323 1.000 32.66010  ? 91   SER   A N    1 
ATOM   2976 C  CA   . SER   B 2 86  ? -10.65970 11.17754  -12.83436 1.000 36.48701  ? 91   SER   A CA   1 
ATOM   2977 C  C    . SER   B 2 86  ? -11.06392 12.35248  -13.71933 1.000 36.23696  ? 91   SER   A C    1 
ATOM   2978 O  O    . SER   B 2 86  ? -10.46702 13.42955  -13.62341 1.000 38.10199  ? 91   SER   A O    1 
ATOM   2979 C  CB   . SER   B 2 86  ? -9.73568  10.24162  -13.62344 1.000 33.97749  ? 91   SER   A CB   1 
ATOM   2980 O  OG   . SER   B 2 86  ? -9.03750  9.36171   -12.76550 1.000 41.17988  ? 91   SER   A OG   1 
ATOM   2981 N  N    . ASP   B 2 87  ? -12.07099 12.17037  -14.57222 1.000 38.13304  ? 92   ASP   A N    1 
ATOM   2982 C  CA   . ASP   B 2 87  ? -12.39020 13.13332  -15.61520 1.000 39.65421  ? 92   ASP   A CA   1 
ATOM   2983 C  C    . ASP   B 2 87  ? -13.89822 13.32416  -15.68904 1.000 40.61655  ? 92   ASP   A C    1 
ATOM   2984 O  O    . ASP   B 2 87  ? -14.67709 12.45408  -15.28695 1.000 36.48220  ? 92   ASP   A O    1 
ATOM   2985 C  CB   . ASP   B 2 87  ? -11.86129 12.66536  -16.98225 1.000 42.60898  ? 92   ASP   A CB   1 
ATOM   2986 C  CG   . ASP   B 2 87  ? -11.55451 13.81938  -17.92630 1.000 46.46689  ? 92   ASP   A CG   1 
ATOM   2987 O  OD1  . ASP   B 2 87  ? -11.81960 14.97935  -17.56528 1.000 39.88686  ? 92   ASP   A OD1  1 
ATOM   2988 O  OD2  . ASP   B 2 87  ? -11.02160 13.56442  -19.02935 1.000 42.28193  ? 92   ASP   A OD2  1 
ATOM   2989 N  N    . VAL   B 2 88  ? -14.30040 14.47611  -16.22402 1.000 39.55444  ? 93   VAL   A N    1 
ATOM   2990 C  CA   . VAL   B 2 88  ? -15.69346 14.74296  -16.56387 1.000 41.36026  ? 93   VAL   A CA   1 
ATOM   2991 C  C    . VAL   B 2 88  ? -15.69969 15.64895  -17.78488 1.000 38.13067  ? 93   VAL   A C    1 
ATOM   2992 O  O    . VAL   B 2 88  ? -14.77379 16.43804  -17.99599 1.000 45.20733  ? 93   VAL   A O    1 
ATOM   2993 C  CB   . VAL   B 2 88  ? -16.46841 15.37890  -15.38380 1.000 42.44815  ? 93   VAL   A CB   1 
ATOM   2994 C  CG1  . VAL   B 2 88  ? -17.87649 15.75474  -15.81565 1.000 56.53731  ? 93   VAL   A CG1  1 
ATOM   2995 C  CG2  . VAL   B 2 88  ? -16.49418 14.43491  -14.19478 1.000 55.42503  ? 93   VAL   A CG2  1 
ATOM   2996 N  N    . ALA   B 2 89  ? -16.74276 15.53083  -18.60177 1.000 39.14448  ? 94   ALA   A N    1 
ATOM   2997 C  CA   . ALA   B 2 89  ? -16.79997 16.27980  -19.84978 1.000 38.43067  ? 94   ALA   A CA   1 
ATOM   2998 C  C    . ALA   B 2 89  ? -18.24604 16.60265  -20.18963 1.000 39.03349  ? 94   ALA   A C    1 
ATOM   2999 O  O    . ALA   B 2 89  ? -19.13794 15.76756  -20.00952 1.000 37.86753  ? 94   ALA   A O    1 
ATOM   3000 C  CB   . ALA   B 2 89  ? -16.15001 15.50286  -20.99983 1.000 34.98274  ? 94   ALA   A CB   1 
ATOM   3001 N  N    . TRP   B 2 90  ? -18.46222 17.81962  -20.68562 1.000 38.46105  ? 95   TRP   A N    1 
ATOM   3002 C  CA   . TRP   B 2 90  ? -19.78631 18.29548  -21.06749 1.000 39.54660  ? 95   TRP   A CA   1 
ATOM   3003 C  C    . TRP   B 2 90  ? -20.10042 17.92243  -22.51145 1.000 35.14199  ? 95   TRP   A C    1 
ATOM   3004 O  O    . TRP   B 2 90  ? -19.21251 17.90251  -23.36954 1.000 39.43913  ? 95   TRP   A O    1 
ATOM   3005 C  CB   . TRP   B 2 90  ? -19.88345 19.81647  -20.91650 1.000 35.76585  ? 95   TRP   A CB   1 
ATOM   3006 C  CG   . TRP   B 2 90  ? -19.85636 20.33049  -19.51350 1.000 39.39722  ? 95   TRP   A CG   1 
ATOM   3007 C  CD1  . TRP   B 2 90  ? -18.75532 20.70561  -18.79463 1.000 36.96602  ? 95   TRP   A CD1  1 
ATOM   3008 C  CD2  . TRP   B 2 90  ? -20.98629 20.55838  -18.66439 1.000 36.44391  ? 95   TRP   A CD2  1 
ATOM   3009 N  NE1  . TRP   B 2 90  ? -19.13124 21.14359  -17.54759 1.000 40.09237  ? 95   TRP   A NE1  1 
ATOM   3010 C  CE2  . TRP   B 2 90  ? -20.49422 21.06345  -17.44345 1.000 37.21523  ? 95   TRP   A CE2  1 
ATOM   3011 C  CE3  . TRP   B 2 90  ? -22.36529 20.38324  -18.81624 1.000 39.58166  ? 95   TRP   A CE3  1 
ATOM   3012 C  CZ2  . TRP   B 2 90  ? -21.33614 21.39137  -16.38236 1.000 34.73348  ? 95   TRP   A CZ2  1 
ATOM   3013 C  CZ3  . TRP   B 2 90  ? -23.19521 20.71216  -17.76116 1.000 35.51080  ? 95   TRP   A CZ3  1 
ATOM   3014 C  CH2  . TRP   B 2 90  ? -22.68014 21.20623  -16.56122 1.000 31.81499  ? 95   TRP   A CH2  1 
ATOM   3015 N  N    . SER   B 2 91  ? -21.37242 17.64229  -22.77631 1.000 38.27579  ? 96   SER   A N    1 
ATOM   3016 C  CA   . SER   B 2 91  ? -21.81956 17.58722  -24.15626 1.000 40.70107  ? 96   SER   A CA   1 
ATOM   3017 C  C    . SER   B 2 91  ? -21.92877 19.00521  -24.71427 1.000 40.27684  ? 96   SER   A C    1 
ATOM   3018 O  O    . SER   B 2 91  ? -22.03979 19.98720  -23.97527 1.000 38.24490  ? 96   SER   A O    1 
ATOM   3019 C  CB   . SER   B 2 91  ? -23.16250 16.86408  -24.27111 1.000 42.30466  ? 96   SER   A CB   1 
ATOM   3020 O  OG   . SER   B 2 91  ? -24.20652 17.61998  -23.68601 1.000 41.87469  ? 96   SER   A OG   1 
ATOM   3021 N  N    . SER   B 2 92  ? -21.89892 19.10519  -26.04527 1.000 38.75278  ? 97   SER   A N    1 
ATOM   3022 C  CA   . SER   B 2 92  ? -21.84312 20.41919  -26.68230 1.000 39.18762  ? 97   SER   A CA   1 
ATOM   3023 C  C    . SER   B 2 92  ? -23.03618 21.28807  -26.30618 1.000 43.02418  ? 97   SER   A C    1 
ATOM   3024 O  O    . SER   B 2 92  ? -22.90830 22.51408  -26.23421 1.000 40.02221  ? 97   SER   A O    1 
ATOM   3025 C  CB   . SER   B 2 92  ? -21.75227 20.26718  -28.20030 1.000 44.89538  ? 97   SER   A CB   1 
ATOM   3026 O  OG   . SER   B 2 92  ? -20.58923 19.54930  -28.56742 1.000 43.97154  ? 97   SER   A OG   1 
ATOM   3027 N  N    . ASP   B 2 93  ? -24.19909 20.68395  -26.06205 1.000 46.08410  ? 98   ASP   A N    1 
ATOM   3028 C  CA   . ASP   B 2 93  ? -25.39013 21.44383  -25.70894 1.000 40.68309  ? 98   ASP   A CA   1 
ATOM   3029 C  C    . ASP   B 2 93  ? -25.51800 21.68084  -24.20793 1.000 50.62394  ? 98   ASP   A C    1 
ATOM   3030 O  O    . ASP   B 2 93  ? -26.56000 22.16373  -23.75382 1.000 47.01958  ? 98   ASP   A O    1 
ATOM   3031 C  CB   . ASP   B 2 93  ? -26.64811 20.74269  -26.23979 1.000 42.13385  ? 98   ASP   A CB   1 
ATOM   3032 C  CG   . ASP   B 2 93  ? -26.92690 19.42067  -25.54375 1.000 52.89892  ? 98   ASP   A CG   1 
ATOM   3033 O  OD1  . ASP   B 2 93  ? -26.07877 18.96677  -24.74683 1.000 45.61709  ? 98   ASP   A OD1  1 
ATOM   3034 O  OD2  . ASP   B 2 93  ? -28.00087 18.83356  -25.79563 1.000 47.08843  ? 98   ASP   A OD2  1 
ATOM   3035 N  N    . SER   B 2 94  ? -24.48488 21.34896  -23.43103 1.000 45.44701  ? 99   SER   A N    1 
ATOM   3036 C  CA   . SER   B 2 94  ? -24.42175 21.58398  -21.99204 1.000 44.27995  ? 99   SER   A CA   1 
ATOM   3037 C  C    . SER   B 2 94  ? -25.43258 20.76189  -21.20592 1.000 39.10536  ? 99   SER   A C    1 
ATOM   3038 O  O    . SER   B 2 94  ? -25.62148 21.00988  -20.00791 1.000 42.73728  ? 99   SER   A O    1 
ATOM   3039 C  CB   . SER   B 2 94  ? -24.61087 23.06797  -21.65204 1.000 46.12602  ? 99   SER   A CB   1 
ATOM   3040 O  OG   . SER   B 2 94  ? -23.62602 23.87206  -22.28115 1.000 39.39743  ? 99   SER   A OG   1 
ATOM   3041 N  N    . ASN   B 2 95  ? -26.07955 19.78481  -21.83284 1.000 44.33389  ? 100  ASN   A N    1 
ATOM   3042 C  CA   . ASN   B 2 95  ? -27.12340 19.00871  -21.17272 1.000 38.55537  ? 100  ASN   A CA   1 
ATOM   3043 C  C    . ASN   B 2 95  ? -26.62520 17.70777  -20.56276 1.000 49.41391  ? 100  ASN   A C    1 
ATOM   3044 O  O    . ASN   B 2 95  ? -27.22204 17.22972  -19.59169 1.000 47.46697  ? 100  ASN   A O    1 
ATOM   3045 C  CB   . ASN   B 2 95  ? -28.25047 18.69358  -22.16260 1.000 44.82190  ? 100  ASN   A CB   1 
ATOM   3046 C  CG   . ASN   B 2 95  ? -29.08863 19.91249  -22.49853 1.000 56.98043  ? 100  ASN   A CG   1 
ATOM   3047 O  OD1  . ASN   B 2 95  ? -29.23864 20.82548  -21.68152 1.000 49.47929  ? 100  ASN   A OD1  1 
ATOM   3048 N  ND2  . ASN   B 2 95  ? -29.64076 19.93441  -23.70547 1.000 48.39179  ? 100  ASN   A ND2  1 
ATOM   3049 N  N    . LEU   B 2 96  ? -25.55619 17.12487  -21.09486 1.000 48.29384  ? 101  LEU   A N    1 
ATOM   3050 C  CA   . LEU   B 2 96  ? -25.07501 15.82993  -20.64090 1.000 49.95958  ? 101  LEU   A CA   1 
ATOM   3051 C  C    . LEU   B 2 96  ? -23.67496 15.95008  -20.06005 1.000 46.44946  ? 101  LEU   A C    1 
ATOM   3052 O  O    . LEU   B 2 96  ? -22.91209 16.85816  -20.40814 1.000 40.05297  ? 101  LEU   A O    1 
ATOM   3053 C  CB   . LEU   B 2 96  ? -25.06102 14.80392  -21.78189 1.000 43.76604  ? 101  LEU   A CB   1 
ATOM   3054 C  CG   . LEU   B 2 96  ? -26.37307 14.53277  -22.51674 1.000 39.05402  ? 101  LEU   A CG   1 
ATOM   3055 C  CD1  . LEU   B 2 96  ? -26.19506 13.39078  -23.50775 1.000 42.62177  ? 101  LEU   A CD1  1 
ATOM   3056 C  CD2  . LEU   B 2 96  ? -27.49794 14.23367  -21.53562 1.000 43.07664  ? 101  LEU   A CD2  1 
ATOM   3057 N  N    . LEU   B 2 97  ? -23.33877 14.96813  -19.22807 1.000 44.01684  ? 102  LEU   A N    1 
ATOM   3058 C  CA   . LEU   B 2 97  ? -21.97570 14.89128  -18.66021 1.000 46.64290  ? 102  LEU   A CA   1 
ATOM   3059 C  C    . LEU   B 2 97  ? -21.48856 13.44833  -18.79224 1.000 40.11661  ? 102  LEU   A C    1 
ATOM   3060 O  O    . LEU   B 2 97  ? -22.29945 12.53025  -18.61415 1.000 45.01463  ? 102  LEU   A O    1 
ATOM   3061 C  CB   . LEU   B 2 97  ? -21.91059 15.31830  -17.19522 1.000 42.10873  ? 102  LEU   A CB   1 
ATOM   3062 C  CG   . LEU   B 2 97  ? -21.73571 16.80433  -16.88326 1.000 49.28040  ? 102  LEU   A CG   1 
ATOM   3063 C  CD1  . LEU   B 2 97  ? -21.73557 16.94735  -15.37826 1.000 40.56851  ? 102  LEU   A CD1  1 
ATOM   3064 C  CD2  . LEU   B 2 97  ? -20.45483 17.35645  -17.45840 1.000 50.40571  ? 102  LEU   A CD2  1 
ATOM   3065 N  N    . VAL   B 2 98  ? -20.23358 13.27145  -19.15537 1.000 42.58204  ? 103  VAL   A N    1 
ATOM   3066 C  CA   . VAL   B 2 98  ? -19.60645 11.95752  -19.16242 1.000 38.27214  ? 103  VAL   A CA   1 
ATOM   3067 C  C    . VAL   B 2 98  ? -18.48534 11.97265  -18.13654 1.000 44.44096  ? 103  VAL   A C    1 
ATOM   3068 O  O    . VAL   B 2 98  ? -17.73043 12.94773  -18.04063 1.000 38.66443  ? 103  VAL   A O    1 
ATOM   3069 C  CB   . VAL   B 2 98  ? -19.07155 11.55456  -20.55247 1.000 41.66099  ? 103  VAL   A CB   1 
ATOM   3070 C  CG1  . VAL   B 2 98  ? -18.00170 12.52366  -21.01960 1.000 38.58669  ? 103  VAL   A CG1  1 
ATOM   3071 C  CG2  . VAL   B 2 98  ? -18.52240 10.13262  -20.50551 1.000 36.25052  ? 103  VAL   A CG2  1 
ATOM   3072 N  N    . SER   B 2 99  ? -18.39415 10.89867  -17.36054 1.000 42.53091  ? 104  SER   A N    1 
ATOM   3073 C  CA   . SER   B 2 99  ? -17.40002 10.77879  -16.30464 1.000 38.16963  ? 104  SER   A CA   1 
ATOM   3074 C  C    . SER   B 2 99  ? -16.63391 9.47786   -16.48071 1.000 41.96545  ? 104  SER   A C    1 
ATOM   3075 O  O    . SER   B 2 99  ? -17.21484 8.45680   -16.85463 1.000 43.06563  ? 104  SER   A O    1 
ATOM   3076 C  CB   . SER   B 2 99  ? -18.05888 10.81474  -14.91757 1.000 38.11222  ? 104  SER   A CB   1 
ATOM   3077 O  OG   . SER   B 2 99  ? -18.99275 9.75664   -14.76946 1.000 36.42728  ? 104  SER   A OG   1 
ATOM   3078 N  N    . ALA   B 2 100 ? -15.33188 9.52200   -16.21184 1.000 39.97730  ? 105  ALA   A N    1 
ATOM   3079 C  CA   . ALA   B 2 100 ? -14.46676 8.35009   -16.24092 1.000 42.20256  ? 105  ALA   A CA   1 
ATOM   3080 C  C    . ALA   B 2 100 ? -14.02658 8.04416   -14.81796 1.000 39.29773  ? 105  ALA   A C    1 
ATOM   3081 O  O    . ALA   B 2 100 ? -13.54660 8.93822   -14.11202 1.000 38.85254  ? 105  ALA   A O    1 
ATOM   3082 C  CB   . ALA   B 2 100 ? -13.24988 8.58621   -17.13505 1.000 37.25060  ? 105  ALA   A CB   1 
ATOM   3083 N  N    . SER   B 2 101 ? -14.19041 6.78915   -14.38993 1.000 34.95821  ? 106  SER   A N    1 
ATOM   3084 C  CA   . SER   B 2 101 ? -13.97222 6.45219   -12.99095 1.000 33.36972  ? 106  SER   A CA   1 
ATOM   3085 C  C    . SER   B 2 101 ? -12.99209 5.29529   -12.84104 1.000 38.40835  ? 106  SER   A C    1 
ATOM   3086 O  O    . SER   B 2 101 ? -12.78510 4.49630   -13.76005 1.000 33.89086  ? 106  SER   A O    1 
ATOM   3087 C  CB   . SER   B 2 101 ? -15.29211 6.09706   -12.29580 1.000 35.52105  ? 106  SER   A CB   1 
ATOM   3088 O  OG   . SER   B 2 101 ? -15.06492 5.60310   -10.99082 1.000 39.77012  ? 106  SER   A OG   1 
ATOM   3089 N  N    . ASP   B 2 102 ? -12.39595 5.21837   -11.64910 1.000 34.19723  ? 107  ASP   A N    1 
ATOM   3090 C  CA   . ASP   B 2 102 ? -11.54180 4.09846   -11.28217 1.000 39.05820  ? 107  ASP   A CA   1 
ATOM   3091 C  C    . ASP   B 2 102 ? -12.30865 2.78638   -11.16907 1.000 39.63397  ? 107  ASP   A C    1 
ATOM   3092 O  O    . ASP   B 2 102 ? -11.67652 1.73245   -11.04513 1.000 37.48495  ? 107  ASP   A O    1 
ATOM   3093 C  CB   . ASP   B 2 102 ? -10.83269 4.37955   -9.95525  1.000 32.81357  ? 107  ASP   A CB   1 
ATOM   3094 C  CG   . ASP   B 2 102 ? -9.84081  5.51766   -10.05237 1.000 43.50659  ? 107  ASP   A CG   1 
ATOM   3095 O  OD1  . ASP   B 2 102 ? -9.41697  5.85369   -11.18042 1.000 38.13342  ? 107  ASP   A OD1  1 
ATOM   3096 O  OD2  . ASP   B 2 102 ? -9.47976  6.08071   -8.99542  1.000 45.93260  ? 107  ASP   A OD2  1 
ATOM   3097 N  N    . ASP   B 2 103 ? -13.64165 2.82124   -11.18593 1.000 32.90445  ? 108  ASP   A N    1 
ATOM   3098 C  CA   . ASP   B 2 103 ? -14.42853 1.59716   -11.19184 1.000 34.43707  ? 108  ASP   A CA   1 
ATOM   3099 C  C    . ASP   B 2 103 ? -14.49560 0.95814   -12.57082 1.000 39.16650  ? 108  ASP   A C    1 
ATOM   3100 O  O    . ASP   B 2 103 ? -15.31953 0.06305   -12.78972 1.000 36.41172  ? 108  ASP   A O    1 
ATOM   3101 C  CB   . ASP   B 2 103 ? -15.84050 1.86102   -10.65169 1.000 33.92523  ? 108  ASP   A CB   1 
ATOM   3102 C  CG   . ASP   B 2 103 ? -16.64669 2.80693   -11.52962 1.000 40.66188  ? 108  ASP   A CG   1 
ATOM   3103 O  OD1  . ASP   B 2 103 ? -16.24884 3.06195   -12.68766 1.000 38.97849  ? 108  ASP   A OD1  1 
ATOM   3104 O  OD2  . ASP   B 2 103 ? -17.68969 3.29982   -11.04851 1.000 37.05886  ? 108  ASP   A OD2  1 
ATOM   3105 N  N    . LYS   B 2 104 ? -13.63675 1.41722   -13.48792 1.000 35.44260  ? 109  LYS   A N    1 
ATOM   3106 C  CA   . LYS   B 2 104 ? -13.48783 0.83021   -14.85093 1.000 36.79804  ? 109  LYS   A CA   1 
ATOM   3107 C  C    . LYS   B 2 104 ? -14.63397 1.23108   -15.79981 1.000 39.85403  ? 109  LYS   A C    1 
ATOM   3108 O  O    . LYS   B 2 104 ? -14.67204 0.71606   -16.91880 1.000 36.92187  ? 109  LYS   A O    1 
ATOM   3109 C  CB   . LYS   B 2 104 ? -13.28367 -0.69176  -14.81393 1.000 39.78941  ? 109  LYS   A CB   1 
ATOM   3110 C  CG   . LYS   B 2 104 ? -12.23851 -1.21764  -13.85303 1.000 43.98421  ? 109  LYS   A CG   1 
ATOM   3111 C  CD   . LYS   B 2 104 ? -11.98738 -2.69962  -14.09504 1.000 44.53305  ? 109  LYS   A CD   1 
ATOM   3112 C  CE   . LYS   B 2 104 ? -11.17720 -3.31652  -13.01012 1.000 47.76131  ? 109  LYS   A CE   1 
ATOM   3113 N  NZ   . LYS   B 2 104 ? -11.87108 -3.20758  -11.72904 1.000 47.18350  ? 109  LYS   A NZ   1 
ATOM   3114 N  N    . THR   B 2 105 ? -15.51902 2.11500   -15.36073 1.000 38.79186  ? 110  THR   A N    1 
ATOM   3115 C  CA   . THR   B 2 105 ? -16.63215 2.51387   -16.20562 1.000 38.75573  ? 110  THR   A CA   1 
ATOM   3116 C  C    . THR   B 2 105 ? -16.57034 4.00287   -16.50864 1.000 37.03821  ? 110  THR   A C    1 
ATOM   3117 O  O    . THR   B 2 105 ? -15.93135 4.79395   -15.79672 1.000 38.76094  ? 110  THR   A O    1 
ATOM   3118 C  CB   . THR   B 2 105 ? -17.98905 2.20273   -15.55347 1.000 39.12476  ? 110  THR   A CB   1 
ATOM   3119 O  OG1  . THR   B 2 105 ? -18.25904 3.16272   -14.52345 1.000 35.25819  ? 110  THR   A OG1  1 
ATOM   3120 C  CG2  . THR   B 2 105 ? -17.99484 0.80374   -14.96145 1.000 32.49510  ? 110  THR   A CG2  1 
ATOM   3121 N  N    . LEU   B 2 106 ? -17.25949 4.36879   -17.58157 1.000 40.30474  ? 111  LEU   A N    1 
ATOM   3122 C  CA   . LEU   B 2 106 ? -17.69865 5.73974   -17.77454 1.000 36.71908  ? 111  LEU   A CA   1 
ATOM   3123 C  C    . LEU   B 2 106 ? -19.19663 5.79958   -17.51839 1.000 42.58233  ? 111  LEU   A C    1 
ATOM   3124 O  O    . LEU   B 2 106 ? -19.89453 4.78651   -17.55230 1.000 45.24743  ? 111  LEU   A O    1 
ATOM   3125 C  CB   . LEU   B 2 106 ? -17.37585 6.25175   -19.18159 1.000 37.56496  ? 111  LEU   A CB   1 
ATOM   3126 C  CG   . LEU   B 2 106 ? -15.90290 6.27590   -19.59074 1.000 36.64656  ? 111  LEU   A CG   1 
ATOM   3127 C  CD1  . LEU   B 2 106 ? -15.57587 5.07992   -20.46576 1.000 35.82934  ? 111  LEU   A CD1  1 
ATOM   3128 C  CD2  . LEU   B 2 106 ? -15.56011 7.58193   -20.29879 1.000 34.96458  ? 111  LEU   A CD2  1 
ATOM   3129 N  N    . LYS   B 2 107 ? -19.68673 6.99854   -17.24935 1.000 41.13778  ? 112  LYS   A N    1 
ATOM   3130 C  CA   . LYS   B 2 107 ? -21.11473 7.18539   -17.04120 1.000 43.41525  ? 112  LYS   A CA   1 
ATOM   3131 C  C    . LYS   B 2 107 ? -21.58393 8.44733   -17.74617 1.000 43.60832  ? 112  LYS   A C    1 
ATOM   3132 O  O    . LYS   B 2 107 ? -20.93203 9.49340   -17.67125 1.000 44.13732  ? 112  LYS   A O    1 
ATOM   3133 C  CB   . LYS   B 2 107 ? -21.46857 7.24237   -15.54917 1.000 39.38802  ? 112  LYS   A CB   1 
ATOM   3134 C  CG   . LYS   B 2 107 ? -21.50936 5.87138   -14.88114 1.000 45.42929  ? 112  LYS   A CG   1 
ATOM   3135 C  CD   . LYS   B 2 107 ? -21.91322 5.96135   -13.41610 1.000 41.66703  ? 112  LYS   A CD   1 
ATOM   3136 C  CE   . LYS   B 2 107 ? -21.84500 4.59837   -12.74009 1.000 46.38537  ? 112  LYS   A CE   1 
ATOM   3137 N  NZ   . LYS   B 2 107 ? -22.82296 3.62926   -13.31298 1.000 40.59892  ? 112  LYS   A NZ   1 
ATOM   3138 N  N    . ILE   B 2 108 ? -22.70799 8.32120   -18.45005 1.000 42.99045  ? 113  ILE   A N    1 
ATOM   3139 C  CA   . ILE   B 2 108 ? -23.38318 9.43113   -19.11099 1.000 43.48171  ? 113  ILE   A CA   1 
ATOM   3140 C  C    . ILE   B 2 108 ? -24.56813 9.83601   -18.25187 1.000 45.69028  ? 113  ILE   A C    1 
ATOM   3141 O  O    . ILE   B 2 108 ? -25.43401 9.00093   -17.94377 1.000 47.31724  ? 113  ILE   A O    1 
ATOM   3142 C  CB   . ILE   B 2 108 ? -23.84329 9.04806   -20.52694 1.000 46.73578  ? 113  ILE   A CB   1 
ATOM   3143 C  CG1  . ILE   B 2 108 ? -22.67931 8.48317   -21.34105 1.000 40.28692  ? 113  ILE   A CG1  1 
ATOM   3144 C  CG2  . ILE   B 2 108 ? -24.45449 10.25599  -21.22289 1.000 42.55804  ? 113  ILE   A CG2  1 
ATOM   3145 C  CD1  . ILE   B 2 108 ? -23.06942 8.06011   -22.73801 1.000 41.29751  ? 113  ILE   A CD1  1 
ATOM   3146 N  N    . TRP   B 2 109 ? -24.60723 11.12401  -17.89389 1.000 43.78581  ? 114  TRP   A N    1 
ATOM   3147 C  CA   . TRP   B 2 109 ? -25.52319 11.70893  -16.92780 1.000 42.02317  ? 114  TRP   A CA   1 
ATOM   3148 C  C    . TRP   B 2 109 ? -26.36037 12.80883  -17.56372 1.000 52.58537  ? 114  TRP   A C    1 
ATOM   3149 O  O    . TRP   B 2 109 ? -25.84954 13.62488  -18.34279 1.000 40.97733  ? 114  TRP   A O    1 
ATOM   3150 C  CB   . TRP   B 2 109 ? -24.77113 12.33902  -15.75188 1.000 36.46198  ? 114  TRP   A CB   1 
ATOM   3151 C  CG   . TRP   B 2 109 ? -23.74897 11.48614  -15.10098 1.000 51.02092  ? 114  TRP   A CG   1 
ATOM   3152 C  CD1  . TRP   B 2 109 ? -22.44199 11.34527  -15.46612 1.000 45.59800  ? 114  TRP   A CD1  1 
ATOM   3153 C  CD2  . TRP   B 2 109 ? -23.93276 10.67514  -13.93895 1.000 42.28354  ? 114  TRP   A CD2  1 
ATOM   3154 N  NE1  . TRP   B 2 109 ? -21.80381 10.48335  -14.60817 1.000 42.33651  ? 114  TRP   A NE1  1 
ATOM   3155 C  CE2  . TRP   B 2 109 ? -22.69767 10.05627  -13.66207 1.000 46.03194  ? 114  TRP   A CE2  1 
ATOM   3156 C  CE3  . TRP   B 2 109 ? -25.02465 10.40203  -13.11083 1.000 42.89110  ? 114  TRP   A CE3  1 
ATOM   3157 C  CZ2  . TRP   B 2 109 ? -22.52447 9.18530   -12.59008 1.000 40.81302  ? 114  TRP   A CZ2  1 
ATOM   3158 C  CZ3  . TRP   B 2 109 ? -24.85045 9.53906   -12.04884 1.000 44.22516  ? 114  TRP   A CZ3  1 
ATOM   3159 C  CH2  . TRP   B 2 109 ? -23.60936 8.94120   -11.79596 1.000 42.52854  ? 114  TRP   A CH2  1 
ATOM   3160 N  N    . ASP   B 2 110 ? -27.63533 12.84071  -17.17859 1.000 52.24000  ? 115  ASP   A N    1 
ATOM   3161 C  CA   . ASP   B 2 110 ? -28.51848 13.97661  -17.42551 1.000 48.60263  ? 115  ASP   A CA   1 
ATOM   3162 C  C    . ASP   B 2 110 ? -28.27247 15.01065  -16.33255 1.000 45.80480  ? 115  ASP   A C    1 
ATOM   3163 O  O    . ASP   B 2 110 ? -28.55632 14.76364  -15.15652 1.000 46.84854  ? 115  ASP   A O    1 
ATOM   3164 C  CB   . ASP   B 2 110 ? -29.97143 13.50946  -17.44435 1.000 51.90570  ? 115  ASP   A CB   1 
ATOM   3165 C  CG   . ASP   B 2 110 ? -30.95258 14.63135  -17.75026 1.000 49.55635  ? 115  ASP   A CG   1 
ATOM   3166 O  OD1  . ASP   B 2 110 ? -30.75465 15.76338  -17.26430 1.000 59.37243  ? 115  ASP   A OD1  1 
ATOM   3167 O  OD2  . ASP   B 2 110 ? -31.93263 14.37224  -18.47615 1.000 60.03315  ? 115  ASP   A OD2  1 
ATOM   3168 N  N    . VAL   B 2 111 ? -27.73563 16.17270  -16.71362 1.000 46.84419  ? 116  VAL   A N    1 
ATOM   3169 C  CA   . VAL   B 2 111 ? -27.32063 17.15176  -15.71068 1.000 48.36277  ? 116  VAL   A CA   1 
ATOM   3170 C  C    . VAL   B 2 111 ? -28.52260 17.69164  -14.94456 1.000 49.69924  ? 116  VAL   A C    1 
ATOM   3171 O  O    . VAL   B 2 111 ? -28.45649 17.89567  -13.72557 1.000 47.84313  ? 116  VAL   A O    1 
ATOM   3172 C  CB   . VAL   B 2 111 ? -26.51981 18.28883  -16.36878 1.000 51.46673  ? 116  VAL   A CB   1 
ATOM   3173 C  CG1  . VAL   B 2 111 ? -26.20582 19.37088  -15.34882 1.000 46.68383  ? 116  VAL   A CG1  1 
ATOM   3174 C  CG2  . VAL   B 2 111 ? -25.23982 17.74596  -16.98590 1.000 47.53567  ? 116  VAL   A CG2  1 
ATOM   3175 N  N    . SER   B 2 112 ? -29.63370 17.94752  -15.64044 1.000 51.29148  ? 117  SER   A N    1 
ATOM   3176 C  CA   . SER   B 2 112 ? -30.78970 18.55241  -14.98333 1.000 55.74635  ? 117  SER   A CA   1 
ATOM   3177 C  C    . SER   B 2 112 ? -31.36849 17.62436  -13.92326 1.000 50.87785  ? 117  SER   A C    1 
ATOM   3178 O  O    . SER   B 2 112 ? -31.63141 18.04835  -12.79223 1.000 44.66269  ? 117  SER   A O    1 
ATOM   3179 C  CB   . SER   B 2 112 ? -31.85084 18.92928  -16.02022 1.000 45.73915  ? 117  SER   A CB   1 
ATOM   3180 O  OG   . SER   B 2 112 ? -32.21881 17.81123  -16.80617 1.000 63.94441  ? 117  SER   A OG   1 
ATOM   3181 N  N    . SER   B 2 113 ? -31.57239 16.35133  -14.26822 1.000 42.05337  ? 118  SER   A N    1 
ATOM   3182 C  CA   . SER   B 2 113 ? -32.09919 15.38129  -13.31615 1.000 47.59651  ? 118  SER   A CA   1 
ATOM   3183 C  C    . SER   B 2 113 ? -31.01803 14.73741  -12.46326 1.000 56.81658  ? 118  SER   A C    1 
ATOM   3184 O  O    . SER   B 2 113 ? -31.32786 14.22640  -11.37922 1.000 52.86728  ? 118  SER   A O    1 
ATOM   3185 C  CB   . SER   B 2 113 ? -32.87515 14.28320  -14.04705 1.000 47.61211  ? 118  SER   A CB   1 
ATOM   3186 O  OG   . SER   B 2 113 ? -31.99714 13.42228  -14.75414 1.000 53.57395  ? 118  SER   A OG   1 
ATOM   3187 N  N    . GLY   B 2 114 ? -29.76608 14.75254  -12.91239 1.000 60.26435  ? 119  GLY   A N    1 
ATOM   3188 C  CA   . GLY   B 2 114 ? -28.70993 14.06666  -12.19949 1.000 48.71477  ? 119  GLY   A CA   1 
ATOM   3189 C  C    . GLY   B 2 114 ? -28.75079 12.56065  -12.29347 1.000 47.59225  ? 119  GLY   A C    1 
ATOM   3190 O  O    . GLY   B 2 114 ? -28.03864 11.88674  -11.54553 1.000 45.01305  ? 119  GLY   A O    1 
ATOM   3191 N  N    . LYS   B 2 115 ? -29.56782 12.01256  -13.18837 1.000 47.69972  ? 120  LYS   A N    1 
ATOM   3192 C  CA   . LYS   B 2 115 ? -29.70769 10.57154  -13.33734 1.000 45.93690  ? 120  LYS   A CA   1 
ATOM   3193 C  C    . LYS   B 2 115 ? -28.63773 10.02864  -14.27445 1.000 52.40163  ? 120  LYS   A C    1 
ATOM   3194 O  O    . LYS   B 2 115 ? -28.26890 10.67767  -15.25849 1.000 48.98221  ? 120  LYS   A O    1 
ATOM   3195 C  CB   . LYS   B 2 115 ? -31.09171 10.21539  -13.88519 1.000 45.13195  ? 120  LYS   A CB   1 
ATOM   3196 C  CG   . LYS   B 2 115 ? -32.25569 10.83128  -13.12508 1.000 57.33368  ? 120  LYS   A CG   1 
ATOM   3197 C  CD   . LYS   B 2 115 ? -32.67948 9.97125   -11.94802 1.000 68.63877  ? 120  LYS   A CD   1 
ATOM   3198 C  CE   . LYS   B 2 115 ? -34.03547 10.41311  -11.41388 1.000 68.71863  ? 120  LYS   A CE   1 
ATOM   3199 N  NZ   . LYS   B 2 115 ? -35.07858 10.36699  -12.47977 1.000 73.94861  ? 120  LYS   A NZ   1 
ATOM   3200 N  N    . CYS   B 2 116 ? -28.14657 8.82869   -13.96948 1.000 53.66126  ? 121  CYS   A N    1 
ATOM   3201 C  CA   . CYS   B 2 116 ? -27.20859 8.14278   -14.84857 1.000 48.59954  ? 121  CYS   A CA   1 
ATOM   3202 C  C    . CYS   B 2 116 ? -27.98166 7.56669   -16.02748 1.000 45.57652  ? 121  CYS   A C    1 
ATOM   3203 O  O    . CYS   B 2 116 ? -28.74154 6.60461   -15.87339 1.000 52.33128  ? 121  CYS   A O    1 
ATOM   3204 C  CB   . CYS   B 2 116 ? -26.46240 7.04587   -14.09564 1.000 41.85106  ? 121  CYS   A CB   1 
ATOM   3205 S  SG   . CYS   B 2 116 ? -25.39541 6.02697   -15.14974 1.000 46.81704  ? 121  CYS   A SG   1 
ATOM   3206 N  N    . LEU   B 2 117 ? -27.79785 8.15869   -17.20651 1.000 49.54081  ? 122  LEU   A N    1 
ATOM   3207 C  CA   . LEU   B 2 117 ? -28.47092 7.64960   -18.39443 1.000 40.36540  ? 122  LEU   A CA   1 
ATOM   3208 C  C    . LEU   B 2 117 ? -27.81384 6.37467   -18.90049 1.000 42.42707  ? 122  LEU   A C    1 
ATOM   3209 O  O    . LEU   B 2 117 ? -28.50678 5.44059   -19.31740 1.000 46.15756  ? 122  LEU   A O    1 
ATOM   3210 C  CB   . LEU   B 2 117 ? -28.48714 8.71159   -19.49545 1.000 46.87126  ? 122  LEU   A CB   1 
ATOM   3211 C  CG   . LEU   B 2 117 ? -29.09825 10.07153  -19.15140 1.000 52.98646  ? 122  LEU   A CG   1 
ATOM   3212 C  CD1  . LEU   B 2 117 ? -29.09047 10.97351  -20.37641 1.000 46.24212  ? 122  LEU   A CD1  1 
ATOM   3213 C  CD2  . LEU   B 2 117 ? -30.51018 9.91239   -18.60425 1.000 42.05707  ? 122  LEU   A CD2  1 
ATOM   3214 N  N    . LYS   B 2 118 ? -26.48283 6.31181   -18.86663 1.000 44.85615  ? 123  LYS   A N    1 
ATOM   3215 C  CA   . LYS   B 2 118 ? -25.79076 5.13587   -19.38768 1.000 39.91730  ? 123  LYS   A CA   1 
ATOM   3216 C  C    . LYS   B 2 118 ? -24.54064 4.84301   -18.57181 1.000 47.62113  ? 123  LYS   A C    1 
ATOM   3217 O  O    . LYS   B 2 118 ? -23.91468 5.74908   -18.01889 1.000 47.41276  ? 123  LYS   A O    1 
ATOM   3218 C  CB   . LYS   B 2 118 ? -25.40593 5.30989   -20.86473 1.000 42.65618  ? 123  LYS   A CB   1 
ATOM   3219 C  CG   . LYS   B 2 118 ? -26.57904 5.32176   -21.83160 1.000 52.92543  ? 123  LYS   A CG   1 
ATOM   3220 C  CD   . LYS   B 2 118 ? -27.27690 3.97068   -21.89251 1.000 57.62144  ? 123  LYS   A CD   1 
ATOM   3221 C  CE   . LYS   B 2 118 ? -28.43601 3.99455   -22.88339 1.000 63.65888  ? 123  LYS   A CE   1 
ATOM   3222 N  NZ   . LYS   B 2 118 ? -29.23388 2.73447   -22.86529 1.000 72.62700  ? 123  LYS   A NZ   1 
ATOM   3223 N  N    . THR   B 2 119 ? -24.18250 3.56005   -18.51083 1.000 41.91143  ? 124  THR   A N    1 
ATOM   3224 C  CA   . THR   B 2 119 ? -22.92739 3.10519   -17.92096 1.000 44.57869  ? 124  THR   A CA   1 
ATOM   3225 C  C    . THR   B 2 119 ? -22.12743 2.39926   -19.00903 1.000 45.54558  ? 124  THR   A C    1 
ATOM   3226 O  O    . THR   B 2 119 ? -22.48836 1.29622   -19.43598 1.000 48.03734  ? 124  THR   A O    1 
ATOM   3227 C  CB   . THR   B 2 119 ? -23.16417 2.17418   -16.73092 1.000 39.23891  ? 124  THR   A CB   1 
ATOM   3228 O  OG1  . THR   B 2 119 ? -23.76913 2.90413   -15.65887 1.000 38.90754  ? 124  THR   A OG1  1 
ATOM   3229 C  CG2  . THR   B 2 119 ? -21.84106 1.58732   -16.24505 1.000 36.93198  ? 124  THR   A CG2  1 
ATOM   3230 N  N    . LEU   B 2 120 ? -21.05455 3.04036   -19.46016 1.000 36.80346  ? 125  LEU   A N    1 
ATOM   3231 C  CA   . LEU   B 2 120 ? -20.17660 2.48044   -20.48024 1.000 43.03845  ? 125  LEU   A CA   1 
ATOM   3232 C  C    . LEU   B 2 120 ? -19.19043 1.53655   -19.80833 1.000 44.22962  ? 125  LEU   A C    1 
ATOM   3233 O  O    . LEU   B 2 120 ? -18.32139 1.97766   -19.04243 1.000 41.64435  ? 125  LEU   A O    1 
ATOM   3234 C  CB   . LEU   B 2 120 ? -19.45279 3.59451   -21.22933 1.000 41.47734  ? 125  LEU   A CB   1 
ATOM   3235 C  CG   . LEU   B 2 120 ? -20.34996 4.73741   -21.71425 1.000 46.52681  ? 125  LEU   A CG   1 
ATOM   3236 C  CD1  . LEU   B 2 120 ? -19.54115 5.76248   -22.49335 1.000 39.15112  ? 125  LEU   A CD1  1 
ATOM   3237 C  CD2  . LEU   B 2 120 ? -21.49700 4.20428   -22.55012 1.000 43.93963  ? 125  LEU   A CD2  1 
ATOM   3238 N  N    . LYS   B 2 121 ? -19.34832 0.24253   -20.07930 1.000 46.36691  ? 126  LYS   A N    1 
ATOM   3239 C  CA   . LYS   B 2 121 ? -18.47016 -0.80837  -19.58638 1.000 39.51964  ? 126  LYS   A CA   1 
ATOM   3240 C  C    . LYS   B 2 121 ? -17.69822 -1.40830  -20.75345 1.000 46.52252  ? 126  LYS   A C    1 
ATOM   3241 O  O    . LYS   B 2 121 ? -18.26131 -1.63037  -21.83139 1.000 41.33277  ? 126  LYS   A O    1 
ATOM   3242 C  CB   . LYS   B 2 121 ? -19.26497 -1.90944  -18.87828 1.000 47.38315  ? 126  LYS   A CB   1 
ATOM   3243 C  CG   . LYS   B 2 121 ? -20.16490 -1.42252  -17.75519 1.000 50.96513  ? 126  LYS   A CG   1 
ATOM   3244 C  CD   . LYS   B 2 121 ? -20.76070 -2.59957  -16.99511 1.000 48.64900  ? 126  LYS   A CD   1 
ATOM   3245 C  CE   . LYS   B 2 121 ? -21.61862 -2.13465  -15.82703 1.000 50.81308  ? 126  LYS   A CE   1 
ATOM   3246 N  NZ   . LYS   B 2 121 ? -22.00641 -3.27468  -14.94597 1.000 58.30263  ? 126  LYS   A NZ   1 
ATOM   3247 N  N    . GLY   B 2 122 ? -16.41517 -1.67516  -20.53258 1.000 37.22840  ? 127  GLY   A N    1 
ATOM   3248 C  CA   . GLY   B 2 122 ? -15.57722 -2.24409  -21.56767 1.000 37.99130  ? 127  GLY   A CA   1 
ATOM   3249 C  C    . GLY   B 2 122 ? -14.11218 -2.23593  -21.19182 1.000 35.85572  ? 127  GLY   A C    1 
ATOM   3250 O  O    . GLY   B 2 122 ? -13.39710 -3.21486  -21.42488 1.000 45.58876  ? 127  GLY   A O    1 
ATOM   3251 N  N    . HIS   B 2 123 ? -13.65023 -1.13188  -20.61288 1.000 39.72725  ? 128  HIS   A N    1 
ATOM   3252 C  CA   . HIS   B 2 123 ? -12.27819 -1.07073  -20.12903 1.000 37.75815  ? 128  HIS   A CA   1 
ATOM   3253 C  C    . HIS   B 2 123 ? -12.05797 -2.09669  -19.02504 1.000 36.66876  ? 128  HIS   A C    1 
ATOM   3254 O  O    . HIS   B 2 123 ? -12.95885 -2.39977  -18.23594 1.000 36.52670  ? 128  HIS   A O    1 
ATOM   3255 C  CB   . HIS   B 2 123 ? -11.95428 0.32931   -19.61108 1.000 35.49952  ? 128  HIS   A CB   1 
ATOM   3256 C  CG   . HIS   B 2 123 ? -11.78850 1.34932   -20.69311 1.000 36.34318  ? 128  HIS   A CG   1 
ATOM   3257 N  ND1  . HIS   B 2 123 ? -10.77759 1.28341   -21.62822 1.000 38.39548  ? 128  HIS   A ND1  1 
ATOM   3258 C  CD2  . HIS   B 2 123 ? -12.49765 2.46524   -20.98105 1.000 40.34157  ? 128  HIS   A CD2  1 
ATOM   3259 C  CE1  . HIS   B 2 123 ? -10.87379 2.31539   -22.44822 1.000 38.30414  ? 128  HIS   A CE1  1 
ATOM   3260 N  NE2  . HIS   B 2 123 ? -11.90782 3.04929   -22.07612 1.000 36.75853  ? 128  HIS   A NE2  1 
ATOM   3261 N  N    . SER   B 2 124 ? -10.84490 -2.63556  -18.97016 1.000 36.86097  ? 129  SER   A N    1 
ATOM   3262 C  CA   . SER   B 2 124 ? -10.48269 -3.64751  -17.98918 1.000 42.60131  ? 129  SER   A CA   1 
ATOM   3263 C  C    . SER   B 2 124 ? -9.74963  -3.06642  -16.78227 1.000 45.58266  ? 129  SER   A C    1 
ATOM   3264 O  O    . SER   B 2 124 ? -9.23346  -3.82936  -15.96131 1.000 38.85118  ? 129  SER   A O    1 
ATOM   3265 C  CB   . SER   B 2 124 ? -9.63065  -4.73543  -18.64626 1.000 39.37989  ? 129  SER   A CB   1 
ATOM   3266 O  OG   . SER   B 2 124 ? -8.44877  -4.19032  -19.20939 1.000 43.55891  ? 129  SER   A OG   1 
ATOM   3267 N  N    . ASN   B 2 125 ? -9.69575  -1.74641  -16.65629 1.000 37.65599  ? 130  ASN   A N    1 
ATOM   3268 C  CA   . ASN   B 2 125 ? -9.03370  -1.09833  -15.52637 1.000 36.74160  ? 130  ASN   A CA   1 
ATOM   3269 C  C    . ASN   B 2 125 ? -9.45585  0.36863   -15.51034 1.000 40.11151  ? 130  ASN   A C    1 
ATOM   3270 O  O    . ASN   B 2 125 ? -10.32198 0.78453   -16.28926 1.000 36.86423  ? 130  ASN   A O    1 
ATOM   3271 C  CB   . ASN   B 2 125 ? -7.51369  -1.26817  -15.60953 1.000 37.57100  ? 130  ASN   A CB   1 
ATOM   3272 C  CG   . ASN   B 2 125 ? -6.87153  -1.39809  -14.24459 1.000 35.49941  ? 130  ASN   A CG   1 
ATOM   3273 O  OD1  . ASN   B 2 125 ? -7.39048  -0.88813  -13.25455 1.000 39.10010  ? 130  ASN   A OD1  1 
ATOM   3274 N  ND2  . ASN   B 2 125 ? -5.73446  -2.08597  -14.18571 1.000 39.59764  ? 130  ASN   A ND2  1 
ATOM   3275 N  N    . TYR   B 2 126 ? -8.82984  1.15770   -14.63442 1.000 36.61131  ? 131  TYR   A N    1 
ATOM   3276 C  CA   . TYR   B 2 126 ? -9.27296  2.53066   -14.40539 1.000 35.65783  ? 131  TYR   A CA   1 
ATOM   3277 C  C    . TYR   B 2 126 ? -9.39718  3.30363   -15.71339 1.000 35.52795  ? 131  TYR   A C    1 
ATOM   3278 O  O    . TYR   B 2 126 ? -8.50427  3.26771   -16.56548 1.000 34.04047  ? 131  TYR   A O    1 
ATOM   3279 C  CB   . TYR   B 2 126 ? -8.30194  3.27077   -13.48150 1.000 36.40455  ? 131  TYR   A CB   1 
ATOM   3280 C  CG   . TYR   B 2 126 ? -7.64874  2.44986   -12.38956 1.000 39.39742  ? 131  TYR   A CG   1 
ATOM   3281 C  CD1  . TYR   B 2 126 ? -8.39058  1.94879   -11.32848 1.000 35.58836  ? 131  TYR   A CD1  1 
ATOM   3282 C  CD2  . TYR   B 2 126 ? -6.27772  2.21500   -12.40370 1.000 40.84507  ? 131  TYR   A CD2  1 
ATOM   3283 C  CE1  . TYR   B 2 126 ? -7.78639  1.21087   -10.32453 1.000 39.16017  ? 131  TYR   A CE1  1 
ATOM   3284 C  CE2  . TYR   B 2 126 ? -5.66954  1.47707   -11.40976 1.000 41.44403  ? 131  TYR   A CE2  1 
ATOM   3285 C  CZ   . TYR   B 2 126 ? -6.42537  0.98101   -10.37267 1.000 40.74757  ? 131  TYR   A CZ   1 
ATOM   3286 O  OH   . TYR   B 2 126 ? -5.81519  0.25009   -9.37973  1.000 55.93234  ? 131  TYR   A OH   1 
ATOM   3287 N  N    . VAL   B 2 127 ? -10.50627 4.01751   -15.85828 1.000 33.38275  ? 132  VAL   A N    1 
ATOM   3288 C  CA   . VAL   B 2 127 ? -10.68648 4.95648   -16.95827 1.000 38.07366  ? 132  VAL   A CA   1 
ATOM   3289 C  C    . VAL   B 2 127 ? -10.25158 6.33053   -16.47234 1.000 33.29805  ? 132  VAL   A C    1 
ATOM   3290 O  O    . VAL   B 2 127 ? -10.77252 6.83949   -15.47429 1.000 30.73602  ? 132  VAL   A O    1 
ATOM   3291 C  CB   . VAL   B 2 127 ? -12.14454 4.97632   -17.44312 1.000 43.11705  ? 132  VAL   A CB   1 
ATOM   3292 C  CG1  . VAL   B 2 127 ? -12.25876 5.77329   -18.73812 1.000 34.09204  ? 132  VAL   A CG1  1 
ATOM   3293 C  CG2  . VAL   B 2 127 ? -12.65941 3.55926   -17.62505 1.000 31.46114  ? 132  VAL   A CG2  1 
ATOM   3294 N  N    . PHE   B 2 128 ? -9.29471  6.93462   -17.17745 1.000 28.25587  ? 133  PHE   A N    1 
ATOM   3295 C  CA   . PHE   B 2 128 ? -8.69280  8.18269   -16.73053 1.000 36.92677  ? 133  PHE   A CA   1 
ATOM   3296 C  C    . PHE   B 2 128 ? -9.21900  9.41663   -17.44949 1.000 35.62150  ? 133  PHE   A C    1 
ATOM   3297 O  O    . PHE   B 2 128 ? -9.28505  10.48363  -16.83849 1.000 38.42310  ? 133  PHE   A O    1 
ATOM   3298 C  CB   . PHE   B 2 128 ? -7.16881  8.12185   -16.89369 1.000 34.81671  ? 133  PHE   A CB   1 
ATOM   3299 C  CG   . PHE   B 2 128 ? -6.48661  7.23293   -15.89075 1.000 39.50423  ? 133  PHE   A CG   1 
ATOM   3300 C  CD1  . PHE   B 2 128 ? -7.02846  7.05389   -14.62669 1.000 31.92711  ? 133  PHE   A CD1  1 
ATOM   3301 C  CD2  . PHE   B 2 128 ? -5.31057  6.57605   -16.21086 1.000 34.26423  ? 133  PHE   A CD2  1 
ATOM   3302 C  CE1  . PHE   B 2 128 ? -6.40527  6.23497   -13.69774 1.000 33.52355  ? 133  PHE   A CE1  1 
ATOM   3303 C  CE2  . PHE   B 2 128 ? -4.68239  5.75513   -15.28892 1.000 32.03149  ? 133  PHE   A CE2  1 
ATOM   3304 C  CZ   . PHE   B 2 128 ? -5.22824  5.58509   -14.02886 1.000 36.36833  ? 133  PHE   A CZ   1 
ATOM   3305 N  N    . CYS   B 2 129 ? -9.60912  9.31257   -18.71844 1.000 36.15427  ? 134  CYS   A N    1 
ATOM   3306 C  CA   . CYS   B 2 129 ? -9.94933  10.49352  -19.49642 1.000 37.35498  ? 134  CYS   A CA   1 
ATOM   3307 C  C    . CYS   B 2 129 ? -11.17139 10.22138  -20.36329 1.000 35.92039  ? 134  CYS   A C    1 
ATOM   3308 O  O    . CYS   B 2 129 ? -11.44431 9.07935   -20.73825 1.000 37.70797  ? 134  CYS   A O    1 
ATOM   3309 C  CB   . CYS   B 2 129 ? -8.76647  10.93464  -20.36755 1.000 37.26040  ? 134  CYS   A CB   1 
ATOM   3310 S  SG   . CYS   B 2 129 ? -7.82440  9.55473   -21.06663 1.000 36.30605  ? 134  CYS   A SG   1 
ATOM   3311 N  N    . CYS   B 2 130 ? -11.90154 11.29130  -20.68023 1.000 36.26929  ? 135  CYS   A N    1 
ATOM   3312 C  CA   . CYS   B 2 130 ? -13.11361 11.18317  -21.48010 1.000 39.50424  ? 135  CYS   A CA   1 
ATOM   3313 C  C    . CYS   B 2 130 ? -13.43782 12.53513  -22.10208 1.000 38.16121  ? 135  CYS   A C    1 
ATOM   3314 O  O    . CYS   B 2 130 ? -13.03387 13.58617  -21.59514 1.000 36.96392  ? 135  CYS   A O    1 
ATOM   3315 C  CB   . CYS   B 2 130 ? -14.29647 10.69006  -20.63897 1.000 34.42996  ? 135  CYS   A CB   1 
ATOM   3316 S  SG   . CYS   B 2 130 ? -14.62042 11.70204  -19.16295 1.000 37.30941  ? 135  CYS   A SG   1 
ATOM   3317 N  N    . ASN   B 2 131 ? -14.17293 12.48903  -23.21100 1.000 36.17827  ? 136  ASN   A N    1 
ATOM   3318 C  CA   . ASN   B 2 131 ? -14.57613 13.69098  -23.92398 1.000 42.75826  ? 136  ASN   A CA   1 
ATOM   3319 C  C    . ASN   B 2 131 ? -15.66820 13.33586  -24.91986 1.000 42.18599  ? 136  ASN   A C    1 
ATOM   3320 O  O    . ASN   B 2 131 ? -15.70514 12.21785  -25.44884 1.000 40.44105  ? 136  ASN   A O    1 
ATOM   3321 C  CB   . ASN   B 2 131 ? -13.39428 14.34310  -24.65111 1.000 29.93423  ? 136  ASN   A CB   1 
ATOM   3322 C  CG   . ASN   B 2 131 ? -12.83332 15.53317  -23.90318 1.000 41.35291  ? 136  ASN   A CG   1 
ATOM   3323 O  OD1  . ASN   B 2 131 ? -13.58035 16.36709  -23.38512 1.000 36.49897  ? 136  ASN   A OD1  1 
ATOM   3324 N  ND2  . ASN   B 2 131 ? -11.50932 15.62031  -23.83732 1.000 42.06404  ? 136  ASN   A ND2  1 
ATOM   3325 N  N    . PHE   B 2 132 ? -16.55832 14.29376  -25.15277 1.000 38.35902  ? 137  PHE   A N    1 
ATOM   3326 C  CA   . PHE   B 2 132 ? -17.49243 14.22565  -26.26368 1.000 41.33835  ? 137  PHE   A CA   1 
ATOM   3327 C  C    . PHE   B 2 132 ? -16.83262 14.76970  -27.52475 1.000 37.83396  ? 137  PHE   A C    1 
ATOM   3328 O  O    . PHE   B 2 132 ? -15.91370 15.59080  -27.46286 1.000 37.55924  ? 137  PHE   A O    1 
ATOM   3329 C  CB   . PHE   B 2 132 ? -18.76149 15.03252  -25.97255 1.000 36.08347  ? 137  PHE   A CB   1 
ATOM   3330 C  CG   . PHE   B 2 132 ? -19.70932 14.36943  -25.01444 1.000 39.67949  ? 137  PHE   A CG   1 
ATOM   3331 C  CD1  . PHE   B 2 132 ? -20.68227 13.49633  -25.47233 1.000 37.22017  ? 137  PHE   A CD1  1 
ATOM   3332 C  CD2  . PHE   B 2 132 ? -19.64420 14.63846  -23.65745 1.000 37.35091  ? 137  PHE   A CD2  1 
ATOM   3333 C  CE1  . PHE   B 2 132 ? -21.56212 12.89125  -24.59423 1.000 42.03232  ? 137  PHE   A CE1  1 
ATOM   3334 C  CE2  . PHE   B 2 132 ? -20.52205 14.03638  -22.77135 1.000 38.77967  ? 137  PHE   A CE2  1 
ATOM   3335 C  CZ   . PHE   B 2 132 ? -21.48200 13.16127  -23.24124 1.000 38.71895  ? 137  PHE   A CZ   1 
ATOM   3336 N  N    . ASN   B 2 133 ? -17.29970 14.29864  -28.67170 1.000 43.20926  ? 138  ASN   A N    1 
ATOM   3337 C  CA   . ASN   B 2 133 ? -16.93889 14.93466  -29.92574 1.000 42.78820  ? 138  ASN   A CA   1 
ATOM   3338 C  C    . ASN   B 2 133 ? -17.79804 16.18057  -30.10467 1.000 41.67635  ? 138  ASN   A C    1 
ATOM   3339 O  O    . ASN   B 2 133 ? -18.77099 16.38548  -29.37757 1.000 40.28933  ? 138  ASN   A O    1 
ATOM   3340 C  CB   . ASN   B 2 133 ? -17.09691 13.94863  -31.08271 1.000 41.57457  ? 138  ASN   A CB   1 
ATOM   3341 C  CG   . ASN   B 2 133 ? -18.53389 13.50348  -31.29056 1.000 39.63228  ? 138  ASN   A CG   1 
ATOM   3342 O  OD1  . ASN   B 2 133 ? -19.36980 13.60540  -30.39347 1.000 39.87684  ? 138  ASN   A OD1  1 
ATOM   3343 N  ND2  . ASN   B 2 133 ? -18.82196 12.99343  -32.48452 1.000 45.08685  ? 138  ASN   A ND2  1 
ATOM   3344 N  N    . PRO   B 2 134 ? -17.45223 17.05259  -31.05472 1.000 39.92538  ? 139  PRO   A N    1 
ATOM   3345 C  CA   . PRO   B 2 134 ? -18.23038 18.29651  -31.19665 1.000 42.13742  ? 139  PRO   A CA   1 
ATOM   3346 C  C    . PRO   B 2 134 ? -19.71337 18.04635  -31.40349 1.000 40.14337  ? 139  PRO   A C    1 
ATOM   3347 O  O    . PRO   B 2 134 ? -20.54638 18.71427  -30.77641 1.000 42.82059  ? 139  PRO   A O    1 
ATOM   3348 C  CB   . PRO   B 2 134 ? -17.58258 18.97456  -32.41173 1.000 42.96253  ? 139  PRO   A CB   1 
ATOM   3349 C  CG   . PRO   B 2 134 ? -16.19352 18.42971  -32.44487 1.000 47.91266  ? 139  PRO   A CG   1 
ATOM   3350 C  CD   . PRO   B 2 134 ? -16.30733 17.00470  -31.97784 1.000 38.80455  ? 139  PRO   A CD   1 
ATOM   3351 N  N    . GLN   B 2 135 ? -20.06636 17.08830  -32.26044 1.000 38.48277  ? 140  GLN   A N    1 
ATOM   3352 C  CA   . GLN   B 2 135 ? -21.46935 16.73215  -32.43529 1.000 42.76287  ? 140  GLN   A CA   1 
ATOM   3353 C  C    . GLN   B 2 135 ? -22.05215 16.12811  -31.16622 1.000 43.51739  ? 140  GLN   A C    1 
ATOM   3354 O  O    . GLN   B 2 135 ? -23.26713 16.19699  -30.94609 1.000 38.73641  ? 140  GLN   A O    1 
ATOM   3355 C  CB   . GLN   B 2 135 ? -21.61937 15.76412  -33.60926 1.000 42.19711  ? 140  GLN   A CB   1 
ATOM   3356 C  CG   . GLN   B 2 135 ? -23.02934 15.23397  -33.81410 1.000 44.94108  ? 140  GLN   A CG   1 
ATOM   3357 C  CD   . GLN   B 2 135 ? -23.13036 14.30795  -35.01208 1.000 51.35854  ? 140  GLN   A CD   1 
ATOM   3358 O  OE1  . GLN   B 2 135 ? -22.19144 14.19004  -35.80118 1.000 48.55640  ? 140  GLN   A OE1  1 
ATOM   3359 N  NE2  . GLN   B 2 135 ? -24.27031 13.64683  -35.15495 1.000 51.05684  ? 140  GLN   A NE2  1 
ATOM   3360 N  N    . SER   B 2 136 ? -21.20700 15.53121  -30.32630 1.000 41.58023  ? 141  SER   A N    1 
ATOM   3361 C  CA   . SER   B 2 136 ? -21.60780 14.93018  -29.05925 1.000 36.88077  ? 141  SER   A CA   1 
ATOM   3362 C  C    . SER   B 2 136 ? -22.41969 13.65510  -29.24015 1.000 42.65104  ? 141  SER   A C    1 
ATOM   3363 O  O    . SER   B 2 136 ? -23.12955 13.23503  -28.31907 1.000 39.47051  ? 141  SER   A O    1 
ATOM   3364 C  CB   . SER   B 2 136 ? -22.38581 15.92611  -28.19118 1.000 43.84381  ? 141  SER   A CB   1 
ATOM   3365 O  OG   . SER   B 2 136 ? -21.51886 16.91321  -27.65829 1.000 39.48020  ? 141  SER   A OG   1 
ATOM   3366 N  N    . ASN   B 2 137 ? -22.33875 13.02709  -30.41215 1.000 42.61982  ? 142  ASN   A N    1 
ATOM   3367 C  CA   . ASN   B 2 137 ? -22.89863 11.69503  -30.59307 1.000 37.56630  ? 142  ASN   A CA   1 
ATOM   3368 C  C    . ASN   B 2 137 ? -21.92747 10.59714  -30.18316 1.000 47.06524  ? 142  ASN   A C    1 
ATOM   3369 O  O    . ASN   B 2 137 ? -22.35233 9.45409   -29.98210 1.000 46.31807  ? 142  ASN   A O    1 
ATOM   3370 C  CB   . ASN   B 2 137 ? -23.31376 11.47997  -32.05003 1.000 45.97170  ? 142  ASN   A CB   1 
ATOM   3371 C  CG   . ASN   B 2 137 ? -22.13886 11.53108  -33.00515 1.000 46.53269  ? 142  ASN   A CG   1 
ATOM   3372 O  OD1  . ASN   B 2 137 ? -21.33596 12.46316  -32.97025 1.000 43.10798  ? 142  ASN   A OD1  1 
ATOM   3373 N  ND2  . ASN   B 2 137 ? -22.02085 10.51608  -33.85515 1.000 54.44309  ? 142  ASN   A ND2  1 
ATOM   3374 N  N    . LEU   B 2 138 ? -20.64249 10.91927  -30.05430 1.000 45.59524  ? 143  LEU   A N    1 
ATOM   3375 C  CA   . LEU   B 2 138 ? -19.61735 9.95938   -29.68540 1.000 43.30049  ? 143  LEU   A CA   1 
ATOM   3376 C  C    . LEU   B 2 138 ? -18.91026 10.40947  -28.41248 1.000 43.44846  ? 143  LEU   A C    1 
ATOM   3377 O  O    . LEU   B 2 138 ? -18.83036 11.60549  -28.11550 1.000 41.76041  ? 143  LEU   A O    1 
ATOM   3378 C  CB   . LEU   B 2 138 ? -18.57745 9.78848   -30.80050 1.000 44.25618  ? 143  LEU   A CB   1 
ATOM   3379 C  CG   . LEU   B 2 138 ? -19.02954 9.29241   -32.17445 1.000 42.98487  ? 143  LEU   A CG   1 
ATOM   3380 C  CD1  . LEU   B 2 138 ? -17.83263 9.19653   -33.10958 1.000 43.46548  ? 143  LEU   A CD1  1 
ATOM   3381 C  CD2  . LEU   B 2 138 ? -19.72939 7.94934   -32.05836 1.000 37.01728  ? 143  LEU   A CD2  1 
ATOM   3382 N  N    . ILE   B 2 139 ? -18.39308 9.43454   -27.67252 1.000 44.75942  ? 144  ILE   A N    1 
ATOM   3383 C  CA   . ILE   B 2 139 ? -17.52399 9.68564   -26.52961 1.000 41.74133  ? 144  ILE   A CA   1 
ATOM   3384 C  C    . ILE   B 2 139 ? -16.21693 8.93778   -26.74974 1.000 40.64127  ? 144  ILE   A C    1 
ATOM   3385 O  O    . ILE   B 2 139 ? -16.21387 7.81077   -27.25173 1.000 41.33834  ? 144  ILE   A O    1 
ATOM   3386 C  CB   . ILE   B 2 139 ? -18.17380 9.25959   -25.19754 1.000 46.45593  ? 144  ILE   A CB   1 
ATOM   3387 C  CG1  . ILE   B 2 139 ? -19.40686 10.11847  -24.90142 1.000 41.03964  ? 144  ILE   A CG1  1 
ATOM   3388 C  CG2  . ILE   B 2 139 ? -17.16569 9.35271   -24.06165 1.000 35.22897  ? 144  ILE   A CG2  1 
ATOM   3389 C  CD1  . ILE   B 2 139 ? -20.14569 9.70341   -23.64834 1.000 36.99064  ? 144  ILE   A CD1  1 
ATOM   3390 N  N    . VAL   B 2 140 ? -15.10596 9.56890   -26.39287 1.000 40.88722  ? 145  VAL   A N    1 
ATOM   3391 C  CA   . VAL   B 2 140 ? -13.79790 8.92803   -26.44400 1.000 33.42805  ? 145  VAL   A CA   1 
ATOM   3392 C  C    . VAL   B 2 140 ? -13.27774 8.79811   -25.02005 1.000 41.36989  ? 145  VAL   A C    1 
ATOM   3393 O  O    . VAL   B 2 140 ? -13.45674 9.70510   -24.20004 1.000 37.86180  ? 145  VAL   A O    1 
ATOM   3394 C  CB   . VAL   B 2 140 ? -12.80207 9.70713   -27.32611 1.000 38.20121  ? 145  VAL   A CB   1 
ATOM   3395 C  CG1  . VAL   B 2 140 ? -12.55916 11.09716  -26.75616 1.000 33.98562  ? 145  VAL   A CG1  1 
ATOM   3396 C  CG2  . VAL   B 2 140 ? -11.49701 8.93526   -27.45224 1.000 27.19776  ? 145  VAL   A CG2  1 
ATOM   3397 N  N    . SER   B 2 141 ? -12.64259 7.66518   -24.72610 1.000 35.75421  ? 146  SER   A N    1 
ATOM   3398 C  CA   . SER   B 2 141 ? -12.13542 7.40125   -23.38915 1.000 35.70808  ? 146  SER   A CA   1 
ATOM   3399 C  C    . SER   B 2 141 ? -10.75036 6.77939   -23.47729 1.000 41.71464  ? 146  SER   A C    1 
ATOM   3400 O  O    . SER   B 2 141 ? -10.42739 6.07841   -24.44032 1.000 38.44082  ? 146  SER   A O    1 
ATOM   3401 C  CB   . SER   B 2 141 ? -13.06624 6.47216   -22.60104 1.000 34.34735  ? 146  SER   A CB   1 
ATOM   3402 O  OG   . SER   B 2 141 ? -13.03616 5.15515   -23.12503 1.000 38.25210  ? 146  SER   A OG   1 
ATOM   3403 N  N    . GLY   B 2 142 ? -9.93828  7.05749   -22.46438 1.000 34.20668  ? 147  GLY   A N    1 
ATOM   3404 C  CA   . GLY   B 2 142 ? -8.65720  6.40062   -22.30751 1.000 33.82390  ? 147  GLY   A CA   1 
ATOM   3405 C  C    . GLY   B 2 142 ? -8.57199  5.78465   -20.92751 1.000 32.79819  ? 147  GLY   A C    1 
ATOM   3406 O  O    . GLY   B 2 142 ? -9.21594  6.23559   -19.98245 1.000 34.93382  ? 147  GLY   A O    1 
ATOM   3407 N  N    . SER   B 2 143 ? -7.77087  4.72773   -20.81958 1.000 33.15236  ? 148  SER   A N    1 
ATOM   3408 C  CA   . SER   B 2 143 ? -7.78666  3.90375   -19.62157 1.000 32.75736  ? 148  SER   A CA   1 
ATOM   3409 C  C    . SER   B 2 143 ? -6.37857  3.49690   -19.20771 1.000 36.79062  ? 148  SER   A C    1 
ATOM   3410 O  O    . SER   B 2 143 ? -5.44065  3.49399   -20.00881 1.000 30.59543  ? 148  SER   A O    1 
ATOM   3411 C  CB   . SER   B 2 143 ? -8.64155  2.64566   -19.82646 1.000 30.34631  ? 148  SER   A CB   1 
ATOM   3412 O  OG   . SER   B 2 143 ? -8.39134  1.69670   -18.80747 1.000 33.81794  ? 148  SER   A OG   1 
ATOM   3413 N  N    . PHE   B 2 144 ? -6.25340  3.15693   -17.92372 1.000 36.12998  ? 149  PHE   A N    1 
ATOM   3414 C  CA   . PHE   B 2 144 ? -5.05528  2.48906   -17.43084 1.000 33.12870  ? 149  PHE   A CA   1 
ATOM   3415 C  C    . PHE   B 2 144 ? -4.77122  1.20608   -18.20185 1.000 32.97524  ? 149  PHE   A C    1 
ATOM   3416 O  O    . PHE   B 2 144 ? -3.61918  0.76120   -18.24897 1.000 34.00313  ? 149  PHE   A O    1 
ATOM   3417 C  CB   . PHE   B 2 144 ? -5.21709  2.19506   -15.93582 1.000 34.40213  ? 149  PHE   A CB   1 
ATOM   3418 C  CG   . PHE   B 2 144 ? -3.99396  1.60920   -15.28394 1.000 37.43096  ? 149  PHE   A CG   1 
ATOM   3419 C  CD1  . PHE   B 2 144 ? -3.78181  0.23822   -15.27494 1.000 37.90485  ? 149  PHE   A CD1  1 
ATOM   3420 C  CD2  . PHE   B 2 144 ? -3.06798  2.42830   -14.66004 1.000 38.86046  ? 149  PHE   A CD2  1 
ATOM   3421 C  CE1  . PHE   B 2 144 ? -2.66069  -0.30365  -14.66505 1.000 34.33078  ? 149  PHE   A CE1  1 
ATOM   3422 C  CE2  . PHE   B 2 144 ? -1.94286  1.89643   -14.05016 1.000 38.96953  ? 149  PHE   A CE2  1 
ATOM   3423 C  CZ   . PHE   B 2 144 ? -1.73872  0.52945   -14.05316 1.000 34.92294  ? 149  PHE   A CZ   1 
ATOM   3424 N  N    . ASP   B 2 145 ? -5.79323  0.60697   -18.81773 1.000 35.13511  ? 150  ASP   A N    1 
ATOM   3425 C  CA   . ASP   B 2 145 ? -5.60218  -0.61602  -19.58874 1.000 31.23870  ? 150  ASP   A CA   1 
ATOM   3426 C  C    . ASP   B 2 145 ? -4.90935  -0.37497  -20.92181 1.000 40.00847  ? 150  ASP   A C    1 
ATOM   3427 O  O    . ASP   B 2 145 ? -4.76433  -1.32196  -21.70382 1.000 38.43342  ? 150  ASP   A O    1 
ATOM   3428 C  CB   . ASP   B 2 145 ? -6.94713  -1.32217  -19.80459 1.000 33.06036  ? 150  ASP   A CB   1 
ATOM   3429 C  CG   . ASP   B 2 145 ? -7.84031  -0.61627  -20.82150 1.000 38.50621  ? 150  ASP   A CG   1 
ATOM   3430 O  OD1  . ASP   B 2 145 ? -7.40248  0.35976   -21.46556 1.000 37.30809  ? 150  ASP   A OD1  1 
ATOM   3431 O  OD2  . ASP   B 2 145 ? -8.99628  -1.05640  -20.98037 1.000 37.37647  ? 150  ASP   A OD2  1 
ATOM   3432 N  N    . GLU   B 2 146 ? -4.49350  0.85907   -21.20687 1.000 38.77204  ? 151  GLU   A N    1 
ATOM   3433 C  CA   . GLU   B 2 146 ? -3.64966  1.21614   -22.34397 1.000 36.65667  ? 151  GLU   A CA   1 
ATOM   3434 C  C    . GLU   B 2 146 ? -4.42281  1.29305   -23.65389 1.000 35.10718  ? 151  GLU   A C    1 
ATOM   3435 O  O    . GLU   B 2 146 ? -3.79693  1.40510   -24.72395 1.000 36.37943  ? 151  GLU   A O    1 
ATOM   3436 C  CB   . GLU   B 2 146 ? -2.47858  0.24027   -22.50008 1.000 39.84810  ? 151  GLU   A CB   1 
ATOM   3437 C  CG   . GLU   B 2 146 ? -1.74141  -0.01464  -21.19615 1.000 41.75899  ? 151  GLU   A CG   1 
ATOM   3438 C  CD   . GLU   B 2 146 ? -0.61032  -1.01252  -21.33726 1.000 44.43832  ? 151  GLU   A CD   1 
ATOM   3439 O  OE1  . GLU   B 2 146 ? -0.36639  -1.49251  -22.46528 1.000 45.59816  ? 151  GLU   A OE1  1 
ATOM   3440 O  OE2  . GLU   B 2 146 ? 0.03982   -1.31444  -20.31532 1.000 41.32944  ? 151  GLU   A OE2  1 
ATOM   3441 N  N    . SER   B 2 147 ? -5.74980  1.24591   -23.61675 1.000 31.68310  ? 152  SER   A N    1 
ATOM   3442 C  CA   . SER   B 2 147 ? -6.56693  1.30281   -24.81566 1.000 37.64991  ? 152  SER   A CA   1 
ATOM   3443 C  C    . SER   B 2 147 ? -7.31708  2.62673   -24.87960 1.000 45.56795  ? 152  SER   A C    1 
ATOM   3444 O  O    . SER   B 2 147 ? -7.51704  3.30772   -23.86859 1.000 38.02838  ? 152  SER   A O    1 
ATOM   3445 C  CB   . SER   B 2 147 ? -7.56681  0.14270   -24.85654 1.000 35.11057  ? 152  SER   A CB   1 
ATOM   3446 O  OG   . SER   B 2 147 ? -8.60674  0.33861   -23.91343 1.000 42.65637  ? 152  SER   A OG   1 
ATOM   3447 N  N    . VAL   B 2 148 ? -7.72424  2.99267   -26.09256 1.000 38.70977  ? 153  VAL   A N    1 
ATOM   3448 C  CA   . VAL   B 2 148 ? -8.64738  4.10257   -26.29248 1.000 36.09390  ? 153  VAL   A CA   1 
ATOM   3449 C  C    . VAL   B 2 148 ? -9.94138  3.53243   -26.85133 1.000 38.72397  ? 153  VAL   A C    1 
ATOM   3450 O  O    . VAL   B 2 148 ? -9.92137  2.63542   -27.69532 1.000 45.61729  ? 153  VAL   A O    1 
ATOM   3451 C  CB   . VAL   B 2 148 ? -8.07459  5.19262   -27.22155 1.000 38.93219  ? 153  VAL   A CB   1 
ATOM   3452 C  CG1  . VAL   B 2 148 ? -9.16073  6.18750   -27.59645 1.000 35.29184  ? 153  VAL   A CG1  1 
ATOM   3453 C  CG2  . VAL   B 2 148 ? -6.91659  5.90675   -26.54368 1.000 34.41312  ? 153  VAL   A CG2  1 
ATOM   3454 N  N    . ARG   B 2 149 ? -11.06938 4.02632   -26.36922 1.000 40.05468  ? 154  ARG   A N    1 
ATOM   3455 C  CA   . ARG   B 2 149 ? -12.34437 3.48518   -26.81508 1.000 40.29077  ? 154  ARG   A CA   1 
ATOM   3456 C  C    . ARG   B 2 149 ? -13.24654 4.59708   -27.32300 1.000 43.69855  ? 154  ARG   A C    1 
ATOM   3457 O  O    . ARG   B 2 149 ? -13.27660 5.69808   -26.76401 1.000 38.61486  ? 154  ARG   A O    1 
ATOM   3458 C  CB   . ARG   B 2 149 ? -13.03617 2.68512   -25.70300 1.000 40.68595  ? 154  ARG   A CB   1 
ATOM   3459 C  CG   . ARG   B 2 149 ? -12.50601 1.26118   -25.58803 1.000 35.85135  ? 154  ARG   A CG   1 
ATOM   3460 C  CD   . ARG   B 2 149 ? -13.15981 0.48212   -24.45996 1.000 42.86550  ? 154  ARG   A CD   1 
ATOM   3461 N  NE   . ARG   B 2 149 ? -12.53765 -0.82681  -24.29000 1.000 37.68284  ? 154  ARG   A NE   1 
ATOM   3462 C  CZ   . ARG   B 2 149 ? -13.06958 -1.97387  -24.69293 1.000 46.40294  ? 154  ARG   A CZ   1 
ATOM   3463 N  NH1  . ARG   B 2 149 ? -14.25663 -2.02100  -25.27281 1.000 45.96388  ? 154  ARG   A NH1  1 
ATOM   3464 N  NH2  . ARG   B 2 149 ? -12.39244 -3.10280  -24.50199 1.000 35.43132  ? 154  ARG   A NH2  1 
ATOM   3465 N  N    . ILE   B 2 150 ? -13.96062 4.29399   -28.40492 1.000 42.43429  ? 155  ILE   A N    1 
ATOM   3466 C  CA   . ILE   B 2 150 ? -14.94678 5.18588   -28.99983 1.000 39.91258  ? 155  ILE   A CA   1 
ATOM   3467 C  C    . ILE   B 2 150 ? -16.31269 4.54674   -28.79568 1.000 45.26912  ? 155  ILE   A C    1 
ATOM   3468 O  O    . ILE   B 2 150 ? -16.54162 3.40671   -29.22864 1.000 40.22050  ? 155  ILE   A O    1 
ATOM   3469 C  CB   . ILE   B 2 150 ? -14.66296 5.43689   -30.48986 1.000 38.17945  ? 155  ILE   A CB   1 
ATOM   3470 C  CG1  . ILE   B 2 150 ? -13.26204 6.03003   -30.66502 1.000 31.51125  ? 155  ILE   A CG1  1 
ATOM   3471 C  CG2  . ILE   B 2 150 ? -15.71912 6.35677   -31.08076 1.000 38.71458  ? 155  ILE   A CG2  1 
ATOM   3472 C  CD1  . ILE   B 2 150 ? -12.83121 6.15806   -32.10806 1.000 33.05673  ? 155  ILE   A CD1  1 
ATOM   3473 N  N    . TRP   B 2 151 ? -17.20670 5.29065   -28.13859 1.000 39.09478  ? 156  TRP   A N    1 
ATOM   3474 C  CA   . TRP   B 2 151 ? -18.51660 4.83552   -27.70145 1.000 40.14072  ? 156  TRP   A CA   1 
ATOM   3475 C  C    . TRP   B 2 151 ? -19.60976 5.65140   -28.37334 1.000 47.94702  ? 156  TRP   A C    1 
ATOM   3476 O  O    . TRP   B 2 151 ? -19.45091 6.85441   -28.61737 1.000 42.01266  ? 156  TRP   A O    1 
ATOM   3477 C  CB   . TRP   B 2 151 ? -18.68746 4.98353   -26.18343 1.000 37.38719  ? 156  TRP   A CB   1 
ATOM   3478 C  CG   . TRP   B 2 151 ? -17.55532 4.48065   -25.34654 1.000 42.02000  ? 156  TRP   A CG   1 
ATOM   3479 C  CD1  . TRP   B 2 151 ? -16.34436 5.07778   -25.15668 1.000 40.52284  ? 156  TRP   A CD1  1 
ATOM   3480 C  CD2  . TRP   B 2 151 ? -17.54911 3.29067   -24.55053 1.000 35.74559  ? 156  TRP   A CD2  1 
ATOM   3481 N  NE1  . TRP   B 2 151 ? -15.57419 4.32687   -24.30075 1.000 40.49701  ? 156  TRP   A NE1  1 
ATOM   3482 C  CE2  . TRP   B 2 151 ? -16.29104 3.22280   -23.91566 1.000 41.49310  ? 156  TRP   A CE2  1 
ATOM   3483 C  CE3  . TRP   B 2 151 ? -18.47798 2.27557   -24.31542 1.000 31.30510  ? 156  TRP   A CE3  1 
ATOM   3484 C  CZ2  . TRP   B 2 151 ? -15.93984 2.17685   -23.06668 1.000 37.50030  ? 156  TRP   A CZ2  1 
ATOM   3485 C  CZ3  . TRP   B 2 151 ? -18.12878 1.23662   -23.47344 1.000 42.10993  ? 156  TRP   A CZ3  1 
ATOM   3486 C  CH2  . TRP   B 2 151 ? -16.87171 1.19576   -22.85757 1.000 35.92932  ? 156  TRP   A CH2  1 
ATOM   3487 N  N    . ASP   B 2 152 ? -20.73972 4.99528   -28.62021 1.000 43.80413  ? 157  ASP   A N    1 
ATOM   3488 C  CA   . ASP   B 2 152 ? -21.92884 5.64315   -29.15510 1.000 40.33646  ? 157  ASP   A CA   1 
ATOM   3489 C  C    . ASP   B 2 152 ? -22.78177 6.15307   -27.99701 1.000 42.84499  ? 157  ASP   A C    1 
ATOM   3490 O  O    . ASP   B 2 152 ? -23.24460 5.36304   -27.16596 1.000 37.22131  ? 157  ASP   A O    1 
ATOM   3491 C  CB   . ASP   B 2 152 ? -22.71383 4.67206   -30.03400 1.000 50.11261  ? 157  ASP   A CB   1 
ATOM   3492 C  CG   . ASP   B 2 152 ? -24.00295 5.26991   -30.55487 1.000 53.52980  ? 157  ASP   A CG   1 
ATOM   3493 O  OD1  . ASP   B 2 152 ? -24.93189 5.49083   -29.74878 1.000 61.46548  ? 157  ASP   A OD1  1 
ATOM   3494 O  OD2  . ASP   B 2 152 ? -24.08711 5.52189   -31.77387 1.000 63.13856  ? 157  ASP   A OD2  1 
ATOM   3495 N  N    . VAL   B 2 153 ? -22.99391 7.47005   -27.95301 1.000 37.94132  ? 158  VAL   A N    1 
ATOM   3496 C  CA   . VAL   B 2 153 ? -23.65885 8.08500   -26.80595 1.000 42.67963  ? 158  VAL   A CA   1 
ATOM   3497 C  C    . VAL   B 2 153 ? -25.08478 7.56885   -26.66179 1.000 45.86180  ? 158  VAL   A C    1 
ATOM   3498 O  O    . VAL   B 2 153 ? -25.55263 7.29482   -25.54874 1.000 41.86068  ? 158  VAL   A O    1 
ATOM   3499 C  CB   . VAL   B 2 153 ? -23.62802 9.61900   -26.93697 1.000 45.34486  ? 158  VAL   A CB   1 
ATOM   3500 C  CG1  . VAL   B 2 153 ? -24.44097 10.26193  -25.82189 1.000 44.95433  ? 158  VAL   A CG1  1 
ATOM   3501 C  CG2  . VAL   B 2 153 ? -22.18907 10.12115  -26.91813 1.000 41.99692  ? 158  VAL   A CG2  1 
ATOM   3502 N  N    . LYS   B 2 154 ? -25.80688 7.43876   -27.76671 1.000 47.12750  ? 159  LYS   A N    1 
ATOM   3503 C  CA   . LYS   B 2 154 ? -27.24384 7.06061   -27.68656 1.000 52.28111  ? 159  LYS   A CA   1 
ATOM   3504 C  C    . LYS   B 2 154 ? -27.41563 5.64260   -27.13652 1.000 49.84289  ? 159  LYS   A C    1 
ATOM   3505 O  O    . LYS   B 2 154 ? -28.25852 5.45153   -26.24843 1.000 56.81589  ? 159  LYS   A O    1 
ATOM   3506 C  CB   . LYS   B 2 154 ? -27.84600 7.17853   -29.08549 1.000 48.57566  ? 159  LYS   A CB   1 
ATOM   3507 C  CG   . LYS   B 2 154 ? -27.90820 8.60452   -29.59451 1.000 63.88295  ? 159  LYS   A CG   1 
ATOM   3508 C  CD   . LYS   B 2 154 ? -28.48836 8.70244   -30.99845 1.000 60.72632  ? 159  LYS   A CD   1 
ATOM   3509 C  CE   . LYS   B 2 154 ? -28.56355 10.11843  -31.46946 1.000 67.81736  ? 159  LYS   A CE   1 
ATOM   3510 N  NZ   . LYS   B 2 154 ? -29.10071 10.19535  -32.83040 1.000 75.38309  ? 159  LYS   A NZ   1 
ATOM   3511 N  N    . THR   B 2 155 ? -26.64158 4.69568   -27.64059 1.000 48.82355  ? 160  THR   A N    1 
ATOM   3512 C  CA   . THR   B 2 155 ? -26.80640 3.30766   -27.22955 1.000 51.69966  ? 160  THR   A CA   1 
ATOM   3513 C  C    . THR   B 2 155 ? -25.86023 2.89278   -26.11365 1.000 56.60182  ? 160  THR   A C    1 
ATOM   3514 O  O    . THR   B 2 155 ? -26.10606 1.86876   -25.46461 1.000 58.02346  ? 160  THR   A O    1 
ATOM   3515 C  CB   . THR   B 2 155 ? -26.60042 2.37267   -28.42556 1.000 52.54074  ? 160  THR   A CB   1 
ATOM   3516 O  OG1  . THR   B 2 155 ? -25.22847 2.42381   -28.84171 1.000 52.58776  ? 160  THR   A OG1  1 
ATOM   3517 C  CG2  . THR   B 2 155 ? -27.49359 2.78856   -29.58447 1.000 52.91279  ? 160  THR   A CG2  1 
ATOM   3518 N  N    . GLY   B 2 156 ? -24.79229 3.65089   -25.87477 1.000 52.37149  ? 161  GLY   A N    1 
ATOM   3519 C  CA   . GLY   B 2 156 ? -23.81514 3.28101   -24.87487 1.000 53.46862  ? 161  GLY   A CA   1 
ATOM   3520 C  C    . GLY   B 2 156 ? -22.89307 2.14710   -25.26295 1.000 49.37364  ? 161  GLY   A C    1 
ATOM   3521 O  O    . GLY   B 2 156 ? -22.04794 1.75320   -24.45003 1.000 52.15137  ? 161  GLY   A O    1 
ATOM   3522 N  N    . LYS   B 2 157 ? -23.02014 1.61007   -26.47193 1.000 51.67307  ? 162  LYS   A N    1 
ATOM   3523 C  CA   . LYS   B 2 157 ? -22.16307 0.52315   -26.91101 1.000 51.80466  ? 162  LYS   A CA   1 
ATOM   3524 C  C    . LYS   B 2 157 ? -20.83218 1.06529   -27.42115 1.000 49.04363  ? 162  LYS   A C    1 
ATOM   3525 O  O    . LYS   B 2 157 ? -20.75636 2.16129   -27.98718 1.000 43.87095  ? 162  LYS   A O    1 
ATOM   3526 C  CB   . LYS   B 2 157 ? -22.84810 -0.29493  -28.00592 1.000 49.58247  ? 162  LYS   A CB   1 
ATOM   3527 C  CG   . LYS   B 2 157 ? -22.35128 0.00410   -29.41398 1.000 57.27178  ? 162  LYS   A CG   1 
ATOM   3528 C  CD   . LYS   B 2 157 ? -23.29033 -0.56101  -30.47487 1.000 72.18254  ? 162  LYS   A CD   1 
ATOM   3529 C  CE   . LYS   B 2 157 ? -24.34748 0.45287   -30.88578 1.000 64.98814  ? 162  LYS   A CE   1 
ATOM   3530 N  NZ   . LYS   B 2 157 ? -23.76869 1.52792   -31.74285 1.000 68.70070  ? 162  LYS   A NZ   1 
ATOM   3531 N  N    . CYS   B 2 158 ? -19.78008 0.28140   -27.21525 1.000 43.88842  ? 163  CYS   A N    1 
ATOM   3532 C  CA   . CYS   B 2 158 ? -18.45117 0.65153   -27.68540 1.000 37.55117  ? 163  CYS   A CA   1 
ATOM   3533 C  C    . CYS   B 2 158 ? -18.36930 0.41952   -29.18941 1.000 45.43222  ? 163  CYS   A C    1 
ATOM   3534 O  O    . CYS   B 2 158 ? -18.59123 -0.69951  -29.66537 1.000 45.11592  ? 163  CYS   A O    1 
ATOM   3535 C  CB   . CYS   B 2 158 ? -17.37601 -0.14635  -26.95450 1.000 35.43920  ? 163  CYS   A CB   1 
ATOM   3536 S  SG   . CYS   B 2 158 ? -15.67510 0.28882   -27.44069 1.000 38.87202  ? 163  CYS   A SG   1 
ATOM   3537 N  N    . LEU   B 2 159 ? -18.05649 1.47654   -29.93845 1.000 43.48919  ? 164  LEU   A N    1 
ATOM   3538 C  CA   . LEU   B 2 159 ? -17.91663 1.33554   -31.38247 1.000 39.02693  ? 164  LEU   A CA   1 
ATOM   3539 C  C    . LEU   B 2 159 ? -16.53961 0.80168   -31.75160 1.000 40.80455  ? 164  LEU   A C    1 
ATOM   3540 O  O    . LEU   B 2 159 ? -16.41760 -0.09932  -32.58860 1.000 47.72062  ? 164  LEU   A O    1 
ATOM   3541 C  CB   . LEU   B 2 159 ? -18.17284 2.67550   -32.07046 1.000 47.41489  ? 164  LEU   A CB   1 
ATOM   3542 C  CG   . LEU   B 2 159 ? -19.59588 3.22136   -31.95631 1.000 48.29920  ? 164  LEU   A CG   1 
ATOM   3543 C  CD1  . LEU   B 2 159 ? -19.73610 4.52533   -32.72331 1.000 45.70314  ? 164  LEU   A CD1  1 
ATOM   3544 C  CD2  . LEU   B 2 159 ? -20.60083 2.18824   -32.44419 1.000 48.27779  ? 164  LEU   A CD2  1 
ATOM   3545 N  N    . LYS   B 2 160 ? -15.49060 1.33580   -31.12972 1.000 37.20033  ? 165  LYS   A N    1 
ATOM   3546 C  CA   . LYS   B 2 160 ? -14.14060 0.92093   -31.48686 1.000 41.06948  ? 165  LYS   A CA   1 
ATOM   3547 C  C    . LYS   B 2 160 ? -13.26545 0.81604   -30.24795 1.000 47.36289  ? 165  LYS   A C    1 
ATOM   3548 O  O    . LYS   B 2 160 ? -13.40544 1.59604   -29.30294 1.000 40.00247  ? 165  LYS   A O    1 
ATOM   3549 C  CB   . LYS   B 2 160 ? -13.48780 1.88799   -32.48594 1.000 40.12576  ? 165  LYS   A CB   1 
ATOM   3550 C  CG   . LYS   B 2 160 ? -14.29596 2.13189   -33.74886 1.000 49.66158  ? 165  LYS   A CG   1 
ATOM   3551 C  CD   . LYS   B 2 160 ? -13.43714 2.77396   -34.83196 1.000 48.22055  ? 165  LYS   A CD   1 
ATOM   3552 C  CE   . LYS   B 2 160 ? -14.29232 3.44386   -35.89787 1.000 60.70614  ? 165  LYS   A CE   1 
ATOM   3553 N  NZ   . LYS   B 2 160 ? -15.29029 2.51275   -36.48776 1.000 57.89573  ? 165  LYS   A NZ   1 
ATOM   3554 N  N    . THR   B 2 161 ? -12.34936 -0.15487  -30.27903 1.000 37.13631  ? 166  THR   A N    1 
ATOM   3555 C  CA   . THR   B 2 161 ? -11.29423 -0.30374  -29.28114 1.000 40.35284  ? 166  THR   A CA   1 
ATOM   3556 C  C    . THR   B 2 161 ? -9.95832  -0.20261  -30.00528 1.000 39.15564  ? 166  THR   A C    1 
ATOM   3557 O  O    . THR   B 2 161 ? -9.61432  -1.07359  -30.81231 1.000 40.26671  ? 166  THR   A O    1 
ATOM   3558 C  CB   . THR   B 2 161 ? -11.40902 -1.63174  -28.53311 1.000 41.26805  ? 166  THR   A CB   1 
ATOM   3559 O  OG1  . THR   B 2 161 ? -12.70094 -1.73487  -27.92198 1.000 41.74422  ? 166  THR   A OG1  1 
ATOM   3560 C  CG2  . THR   B 2 161 ? -10.34089 -1.72162  -27.45022 1.000 38.87517  ? 166  THR   A CG2  1 
ATOM   3561 N  N    . LEU   B 2 162 ? -9.22040  0.86747   -29.73638 1.000 39.56103  ? 167  LEU   A N    1 
ATOM   3562 C  CA   . LEU   B 2 162 ? -7.92149  1.10060   -30.33452 1.000 40.04713  ? 167  LEU   A CA   1 
ATOM   3563 C  C    . LEU   B 2 162 ? -6.83434  0.62272   -29.38962 1.000 41.00391  ? 167  LEU   A C    1 
ATOM   3564 O  O    . LEU   B 2 162 ? -6.77027  1.08774   -28.23464 1.000 43.26979  ? 167  LEU   A O    1 
ATOM   3565 C  CB   . LEU   B 2 162 ? -7.73568  2.58261   -30.63955 1.000 35.98168  ? 167  LEU   A CB   1 
ATOM   3566 C  CG   . LEU   B 2 162 ? -8.88083  3.25548   -31.39644 1.000 42.79998  ? 167  LEU   A CG   1 
ATOM   3567 C  CD1  . LEU   B 2 162 ? -8.60900  4.74051   -31.57949 1.000 35.70308  ? 167  LEU   A CD1  1 
ATOM   3568 C  CD2  . LEU   B 2 162 ? -9.08790  2.57644   -32.73841 1.000 49.81648  ? 167  LEU   A CD2  1 
ATOM   3569 N  N    . PRO   B 2 163 ? -5.96729  -0.29719  -29.83370 1.000 44.87704  ? 168  PRO   A N    1 
ATOM   3570 C  CA   . PRO   B 2 163 ? -4.77318  -0.64006  -29.05083 1.000 39.17091  ? 168  PRO   A CA   1 
ATOM   3571 C  C    . PRO   B 2 163 ? -3.79830  0.52104   -29.07794 1.000 44.90460  ? 168  PRO   A C    1 
ATOM   3572 O  O    . PRO   B 2 163 ? -2.76437  0.47414   -29.75305 1.000 41.04338  ? 168  PRO   A O    1 
ATOM   3573 C  CB   . PRO   B 2 163 ? -4.22512  -1.87501  -29.77887 1.000 37.62060  ? 168  PRO   A CB   1 
ATOM   3574 C  CG   . PRO   B 2 163 ? -4.62830  -1.65307  -31.20283 1.000 41.32610  ? 168  PRO   A CG   1 
ATOM   3575 C  CD   . PRO   B 2 163 ? -5.97736  -0.95921  -31.14969 1.000 45.08307  ? 168  PRO   A CD   1 
ATOM   3576 N  N    . ALA   B 2 164 ? -4.13533  1.58102   -28.34092 1.000 39.19183  ? 169  ALA   A N    1 
ATOM   3577 C  CA   . ALA   B 2 164 ? -3.53450  2.88208   -28.60800 1.000 39.27606  ? 169  ALA   A CA   1 
ATOM   3578 C  C    . ALA   B 2 164 ? -2.09045  2.95723   -28.13315 1.000 36.88364  ? 169  ALA   A C    1 
ATOM   3579 O  O    . ALA   B 2 164 ? -1.24959  3.57831   -28.79225 1.000 34.27363  ? 169  ALA   A O    1 
ATOM   3580 C  CB   . ALA   B 2 164 ? -4.37154  3.98400   -27.95793 1.000 39.51898  ? 169  ALA   A CB   1 
ATOM   3581 N  N    . HIS   B 2 165 ? -1.77827  2.34828   -26.99118 1.000 36.60451  ? 170  HIS   A N    1 
ATOM   3582 C  CA   . HIS   B 2 165 ? -0.48223  2.55642   -26.36532 1.000 39.57530  ? 170  HIS   A CA   1 
ATOM   3583 C  C    . HIS   B 2 165 ? -0.05702  1.28248   -25.64835 1.000 38.30405  ? 170  HIS   A C    1 
ATOM   3584 O  O    . HIS   B 2 165 ? -0.80091  0.30140   -25.58026 1.000 34.80960  ? 170  HIS   A O    1 
ATOM   3585 C  CB   . HIS   B 2 165 ? -0.53625  3.74943   -25.40533 1.000 36.59701  ? 170  HIS   A CB   1 
ATOM   3586 C  CG   . HIS   B 2 165 ? -0.85446  5.05039   -26.07631 1.000 37.29041  ? 170  HIS   A CG   1 
ATOM   3587 N  ND1  . HIS   B 2 165 ? 0.11640   5.87548   -26.59542 1.000 34.23803  ? 170  HIS   A ND1  1 
ATOM   3588 C  CD2  . HIS   B 2 165 ? -2.03855  5.66426   -26.31919 1.000 35.40269  ? 170  HIS   A CD2  1 
ATOM   3589 C  CE1  . HIS   B 2 165 ? -0.45176  6.94342   -27.12738 1.000 36.44538  ? 170  HIS   A CE1  1 
ATOM   3590 N  NE2  . HIS   B 2 165 ? -1.75974  6.84028   -26.97324 1.000 33.96852  ? 170  HIS   A NE2  1 
ATOM   3591 N  N    . SER   B 2 166 ? 1.16404   1.31261   -25.11048 1.000 41.00713  ? 171  SER   A N    1 
ATOM   3592 C  CA   . SER   B 2 166 ? 1.71023   0.22768   -24.30852 1.000 47.43726  ? 171  SER   A CA   1 
ATOM   3593 C  C    . SER   B 2 166 ? 1.90434   0.65472   -22.85555 1.000 43.60884  ? 171  SER   A C    1 
ATOM   3594 O  O    . SER   B 2 166 ? 2.78547   0.14182   -22.15763 1.000 47.88019  ? 171  SER   A O    1 
ATOM   3595 C  CB   . SER   B 2 166 ? 3.02722   -0.27019  -24.90365 1.000 40.19024  ? 171  SER   A CB   1 
ATOM   3596 O  OG   . SER   B 2 166 ? 4.01812   0.74291   -24.87177 1.000 42.55074  ? 171  SER   A OG   1 
ATOM   3597 N  N    . ASP   B 2 167 ? 1.08829   1.60064   -22.39647 1.000 42.21077  ? 172  ASP   A N    1 
ATOM   3598 C  CA   . ASP   B 2 167 ? 1.09039   2.09566   -21.02748 1.000 39.86015  ? 172  ASP   A CA   1 
ATOM   3599 C  C    . ASP   B 2 167 ? -0.19567  2.88253   -20.79635 1.000 38.03985  ? 172  ASP   A C    1 
ATOM   3600 O  O    . ASP   B 2 167 ? -0.94880  3.12543   -21.74928 1.000 37.93830  ? 172  ASP   A O    1 
ATOM   3601 C  CB   . ASP   B 2 167 ? 2.32432   2.96079   -20.75762 1.000 39.35096  ? 172  ASP   A CB   1 
ATOM   3602 C  CG   . ASP   B 2 167 ? 3.47447   2.17092   -20.15873 1.000 49.54506  ? 172  ASP   A CG   1 
ATOM   3603 O  OD1  . ASP   B 2 167 ? 3.21365   1.31290   -19.28569 1.000 48.16248  ? 172  ASP   A OD1  1 
ATOM   3604 O  OD2  . ASP   B 2 167 ? 4.63440   2.40103   -20.56086 1.000 51.52122  ? 172  ASP   A OD2  1 
ATOM   3605 N  N    . PRO   B 2 168 ? -0.48658  3.29151   -19.56133 1.000 33.53100  ? 173  PRO   A N    1 
ATOM   3606 C  CA   . PRO   B 2 168 ? -1.77062  3.95038   -19.28720 1.000 34.00455  ? 173  PRO   A CA   1 
ATOM   3607 C  C    . PRO   B 2 168 ? -1.97984  5.18635   -20.14919 1.000 35.90685  ? 173  PRO   A C    1 
ATOM   3608 O  O    . PRO   B 2 168 ? -1.04395  5.93044   -20.44530 1.000 32.64099  ? 173  PRO   A O    1 
ATOM   3609 C  CB   . PRO   B 2 168 ? -1.67051  4.31041   -17.80222 1.000 34.42180  ? 173  PRO   A CB   1 
ATOM   3610 C  CG   . PRO   B 2 168 ? -0.71734  3.30452   -17.24330 1.000 37.14499  ? 173  PRO   A CG   1 
ATOM   3611 C  CD   . PRO   B 2 168 ? 0.29057   3.05861   -18.33141 1.000 35.18621  ? 173  PRO   A CD   1 
ATOM   3612 N  N    . VAL   B 2 169 ? -3.23191  5.39421   -20.55207 1.000 36.20727  ? 174  VAL   A N    1 
ATOM   3613 C  CA   . VAL   B 2 169 ? -3.61811  6.53616   -21.37204 1.000 36.77031  ? 174  VAL   A CA   1 
ATOM   3614 C  C    . VAL   B 2 169 ? -4.02414  7.67413   -20.44501 1.000 37.16637  ? 174  VAL   A C    1 
ATOM   3615 O  O    . VAL   B 2 169 ? -4.92903  7.52105   -19.61791 1.000 35.05379  ? 174  VAL   A O    1 
ATOM   3616 C  CB   . VAL   B 2 169 ? -4.76018  6.16903   -22.32991 1.000 34.15517  ? 174  VAL   A CB   1 
ATOM   3617 C  CG1  . VAL   B 2 169 ? -5.11439  7.34998   -23.22089 1.000 31.40112  ? 174  VAL   A CG1  1 
ATOM   3618 C  CG2  . VAL   B 2 169 ? -4.38014  4.95506   -23.16994 1.000 43.35132  ? 174  VAL   A CG2  1 
ATOM   3619 N  N    . SER   B 2 170 ? -3.36027  8.82220   -20.59010 1.000 35.93485  ? 175  SER   A N    1 
ATOM   3620 C  CA   . SER   B 2 170 ? -3.54429  9.94319   -19.67609 1.000 35.54909  ? 175  SER   A CA   1 
ATOM   3621 C  C    . SER   B 2 170 ? -4.55045  10.97808  -20.16000 1.000 37.02211  ? 175  SER   A C    1 
ATOM   3622 O  O    . SER   B 2 170 ? -5.13944  11.68003  -19.33195 1.000 37.71617  ? 175  SER   A O    1 
ATOM   3623 C  CB   . SER   B 2 170 ? -2.20334  10.63733  -19.40524 1.000 30.99049  ? 175  SER   A CB   1 
ATOM   3624 O  OG   . SER   B 2 170 ? -1.59651  11.08338  -20.60631 1.000 37.55395  ? 175  SER   A OG   1 
ATOM   3625 N  N    . ALA   B 2 171 ? -4.77060  11.09904  -21.46698 1.000 37.01361  ? 176  ALA   A N    1 
ATOM   3626 C  CA   . ALA   B 2 171 ? -5.72376  12.08293  -21.96589 1.000 36.26540  ? 176  ALA   A CA   1 
ATOM   3627 C  C    . ALA   B 2 171 ? -6.16587  11.70787  -23.37084 1.000 36.82551  ? 176  ALA   A C    1 
ATOM   3628 O  O    . ALA   B 2 171 ? -5.39989  11.12694  -24.14291 1.000 37.19884  ? 176  ALA   A O    1 
ATOM   3629 C  CB   . ALA   B 2 171 ? -5.12390  13.49400  -21.95797 1.000 34.16874  ? 176  ALA   A CB   1 
ATOM   3630 N  N    . VAL   B 2 172 ? -7.41294  12.05673  -23.68771 1.000 39.23775  ? 177  VAL   A N    1 
ATOM   3631 C  CA   . VAL   B 2 172 ? -7.98706  11.88266  -25.01865 1.000 31.34666  ? 177  VAL   A CA   1 
ATOM   3632 C  C    . VAL   B 2 172 ? -8.79822  13.12757  -25.35158 1.000 39.17259  ? 177  VAL   A C    1 
ATOM   3633 O  O    . VAL   B 2 172 ? -9.41519  13.73152  -24.46752 1.000 36.21058  ? 177  VAL   A O    1 
ATOM   3634 C  CB   . VAL   B 2 172 ? -8.86393  10.61556  -25.10754 1.000 28.89696  ? 177  VAL   A CB   1 
ATOM   3635 C  CG1  . VAL   B 2 172 ? -7.99480  9.36266   -25.06461 1.000 35.67126  ? 177  VAL   A CG1  1 
ATOM   3636 C  CG2  . VAL   B 2 172 ? -9.88081  10.60147  -23.98343 1.000 32.11077  ? 177  VAL   A CG2  1 
ATOM   3637 N  N    . HIS   B 2 173 ? -8.79440  13.51555  -26.62658 1.000 36.84238  ? 178  HIS   A N    1 
ATOM   3638 C  CA   . HIS   B 2 173 ? -9.44757  14.75248  -27.02853 1.000 35.69458  ? 178  HIS   A CA   1 
ATOM   3639 C  C    . HIS   B 2 173 ? -9.77572  14.70643  -28.51550 1.000 41.04498  ? 178  HIS   A C    1 
ATOM   3640 O  O    . HIS   B 2 173 ? -8.95976  14.25450  -29.32558 1.000 39.61347  ? 178  HIS   A O    1 
ATOM   3641 C  CB   . HIS   B 2 173 ? -8.55766  15.96458  -26.71264 1.000 36.79930  ? 178  HIS   A CB   1 
ATOM   3642 C  CG   . HIS   B 2 173 ? -9.21283  17.28550  -26.96059 1.000 42.58700  ? 178  HIS   A CG   1 
ATOM   3643 N  ND1  . HIS   B 2 173 ? -8.62301  18.28256  -27.70466 1.000 43.76253  ? 178  HIS   A ND1  1 
ATOM   3644 C  CD2  . HIS   B 2 173 ? -10.40884 17.77739  -26.55647 1.000 44.04554  ? 178  HIS   A CD2  1 
ATOM   3645 C  CE1  . HIS   B 2 173 ? -9.42712  19.32947  -27.75559 1.000 41.22401  ? 178  HIS   A CE1  1 
ATOM   3646 N  NE2  . HIS   B 2 173 ? -10.51902 19.04937  -27.06647 1.000 41.72265  ? 178  HIS   A NE2  1 
ATOM   3647 N  N    . PHE   B 2 174 ? -10.97081 15.17930  -28.86138 1.000 37.97837  ? 179  PHE   A N    1 
ATOM   3648 C  CA   . PHE   B 2 174 ? -11.37697 15.35324  -30.25033 1.000 40.21359  ? 179  PHE   A CA   1 
ATOM   3649 C  C    . PHE   B 2 174 ? -10.90517 16.70628  -30.77240 1.000 42.01690  ? 179  PHE   A C    1 
ATOM   3650 O  O    . PHE   B 2 174 ? -10.74019 17.66331  -30.01143 1.000 37.12170  ? 179  PHE   A O    1 
ATOM   3651 C  CB   . PHE   B 2 174 ? -12.89898 15.26908  -30.39617 1.000 36.74578  ? 179  PHE   A CB   1 
ATOM   3652 C  CG   . PHE   B 2 174 ? -13.44583 13.87002  -30.37210 1.000 33.59817  ? 179  PHE   A CG   1 
ATOM   3653 C  CD1  . PHE   B 2 174 ? -13.39687 13.07201  -31.50309 1.000 40.64600  ? 179  PHE   A CD1  1 
ATOM   3654 C  CD2  . PHE   B 2 174 ? -14.04266 13.36597  -29.22903 1.000 38.57819  ? 179  PHE   A CD2  1 
ATOM   3655 C  CE1  . PHE   B 2 174 ? -13.91273 11.78796  -31.49102 1.000 35.94824  ? 179  PHE   A CE1  1 
ATOM   3656 C  CE2  . PHE   B 2 174 ? -14.56152 12.07892  -29.20796 1.000 36.74219  ? 179  PHE   A CE2  1 
ATOM   3657 C  CZ   . PHE   B 2 174 ? -14.49656 11.29191  -30.34195 1.000 35.32571  ? 179  PHE   A CZ   1 
ATOM   3658 N  N    . ASN   B 2 175 ? -10.69531 16.78228  -32.08543 1.000 42.10760  ? 180  ASN   A N    1 
ATOM   3659 C  CA   . ASN   B 2 175 ? -10.39051 18.06431  -32.69947 1.000 40.69989  ? 180  ASN   A CA   1 
ATOM   3660 C  C    . ASN   B 2 175 ? -11.68962 18.80417  -32.99935 1.000 38.07122  ? 180  ASN   A C    1 
ATOM   3661 O  O    . ASN   B 2 175 ? -12.79154 18.32706  -32.70122 1.000 33.14993  ? 180  ASN   A O    1 
ATOM   3662 C  CB   . ASN   B 2 175 ? -9.52763  17.87638  -33.94956 1.000 38.81543  ? 180  ASN   A CB   1 
ATOM   3663 C  CG   . ASN   B 2 175 ? -10.29368 17.27229  -35.10347 1.000 40.00460  ? 180  ASN   A CG   1 
ATOM   3664 O  OD1  . ASN   B 2 175 ? -11.31259 16.61418  -34.91036 1.000 37.99431  ? 180  ASN   A OD1  1 
ATOM   3665 N  ND2  . ASN   B 2 175 ? -9.80183  17.49432  -36.31653 1.000 42.00256  ? 180  ASN   A ND2  1 
ATOM   3666 N  N    . ARG   B 2 176 ? -11.55980 20.03018  -33.51638 1.000 39.53105  ? 181  ARG   A N    1 
ATOM   3667 C  CA   . ARG   B 2 176 ? -12.71692 20.95505  -33.69327 1.000 44.77977  ? 181  ARG   A CA   1 
ATOM   3668 C  C    . ARG   B 2 176 ? -13.90393 20.33992  -34.43713 1.000 42.16987  ? 181  ARG   A C    1 
ATOM   3669 O  O    . ARG   B 2 176 ? -15.03594 20.69180  -34.11802 1.000 42.48824  ? 181  ARG   A O    1 
ATOM   3670 C  CB   . ARG   B 2 176 ? -12.29013 22.22709  -34.43233 1.000 33.18423  ? 181  ARG   A CB   1 
ATOM   3671 C  CG   . ARG   B 2 176 ? -11.24424 22.13918  -35.53044 1.000 54.67693  ? 181  ARG   A CG   1 
ATOM   3672 C  CD   . ARG   B 2 176 ? -10.90843 23.55621  -35.95849 1.000 63.86299  ? 181  ARG   A CD   1 
ATOM   3673 N  NE   . ARG   B 2 176 ? -10.93660 23.75419  -37.41049 1.000 72.09244  ? 181  ARG   A NE   1 
ATOM   3674 C  CZ   . ARG   B 2 176 ? -10.79079 24.92920  -38.00752 1.000 79.51488  ? 181  ARG   A CZ   1 
ATOM   3675 N  NH1  . ARG   B 2 176 ? -9.67584  25.62032  -37.84865 1.000 68.37645  ? 181  ARG   A NH1  1 
ATOM   3676 N  NH2  . ARG   B 2 176 ? -11.75992 25.41009  -38.76442 1.000 75.95727  ? 181  ARG   A NH2  1 
ATOM   3677 N  N    . ASP   B 2 177 ? -13.63096 19.53493  -35.44315 1.000 37.94970  ? 182  ASP   A N    1 
ATOM   3678 C  CA   . ASP   B 2 177 ? -14.71798 18.94481  -36.21803 1.000 46.20450  ? 182  ASP   A CA   1 
ATOM   3679 C  C    . ASP   B 2 177 ? -14.93979 17.46879  -35.90999 1.000 46.12733  ? 182  ASP   A C    1 
ATOM   3680 O  O    . ASP   B 2 177 ? -15.77579 16.83270  -36.55789 1.000 42.90978  ? 182  ASP   A O    1 
ATOM   3681 C  CB   . ASP   B 2 177 ? -14.48216 19.14182  -37.72306 1.000 45.63704  ? 182  ASP   A CB   1 
ATOM   3682 C  CG   . ASP   B 2 177 ? -13.38512 18.25192  -38.27216 1.000 48.84115  ? 182  ASP   A CG   1 
ATOM   3683 O  OD1  . ASP   B 2 177 ? -12.71896 17.54200  -37.49222 1.000 50.68652  ? 182  ASP   A OD1  1 
ATOM   3684 O  OD2  . ASP   B 2 177 ? -13.18925 18.26293  -39.50618 1.000 44.90780  ? 182  ASP   A OD2  1 
ATOM   3685 N  N    . GLY   B 2 178 ? -14.21863 16.91488  -34.93606 1.000 41.10896  ? 183  GLY   A N    1 
ATOM   3686 C  CA   . GLY   B 2 178 ? -14.42544 15.54986  -34.50402 1.000 37.26282  ? 183  GLY   A CA   1 
ATOM   3687 C  C    . GLY   B 2 178 ? -13.87343 14.48391  -35.41906 1.000 39.69199  ? 183  GLY   A C    1 
ATOM   3688 O  O    . GLY   B 2 178 ? -14.10227 13.29489  -35.16102 1.000 41.53968  ? 183  GLY   A O    1 
ATOM   3689 N  N    . SER   B 2 179 ? -13.15358 14.85697  -36.47814 1.000 43.78577  ? 184  SER   A N    1 
ATOM   3690 C  CA   . SER   B 2 179 ? -12.59257 13.86602  -37.38719 1.000 46.86359  ? 184  SER   A CA   1 
ATOM   3691 C  C    . SER   B 2 179 ? -11.30145 13.25216  -36.86332 1.000 45.53118  ? 184  SER   A C    1 
ATOM   3692 O  O    . SER   B 2 179 ? -10.88639 12.19820  -37.35635 1.000 42.87121  ? 184  SER   A O    1 
ATOM   3693 C  CB   . SER   B 2 179 ? -12.33778 14.48603  -38.76222 1.000 39.70212  ? 184  SER   A CB   1 
ATOM   3694 O  OG   . SER   B 2 179 ? -11.33588 15.48313  -38.69434 1.000 45.72268  ? 184  SER   A OG   1 
ATOM   3695 N  N    . LEU   B 2 180 ? -10.66041 13.88424  -35.88139 1.000 39.49453  ? 185  LEU   A N    1 
ATOM   3696 C  CA   . LEU   B 2 180 ? -9.40530  13.39838  -35.32952 1.000 36.92854  ? 185  LEU   A CA   1 
ATOM   3697 C  C    . LEU   B 2 180 ? -9.51613  13.25438  -33.81950 1.000 47.77852  ? 185  LEU   A C    1 
ATOM   3698 O  O    . LEU   B 2 180 ? -10.19714 14.03632  -33.14744 1.000 38.01113  ? 185  LEU   A O    1 
ATOM   3699 C  CB   . LEU   B 2 180 ? -8.23644  14.33549  -35.66265 1.000 40.15654  ? 185  LEU   A CB   1 
ATOM   3700 C  CG   . LEU   B 2 180 ? -7.75560  14.41253  -37.11270 1.000 40.01573  ? 185  LEU   A CG   1 
ATOM   3701 C  CD1  . LEU   B 2 180 ? -6.60371  15.40265  -37.22484 1.000 38.98516  ? 185  LEU   A CD1  1 
ATOM   3702 C  CD2  . LEU   B 2 180 ? -7.34151  13.04456  -37.61973 1.000 41.86751  ? 185  LEU   A CD2  1 
ATOM   3703 N  N    . ILE   B 2 181 ? -8.83097  12.24246  -33.29356 1.000 44.49284  ? 186  ILE   A N    1 
ATOM   3704 C  CA   . ILE   B 2 181 ? -8.66180  12.05150  -31.85958 1.000 38.90693  ? 186  ILE   A CA   1 
ATOM   3705 C  C    . ILE   B 2 181 ? -7.17277  12.12466  -31.55174 1.000 39.95845  ? 186  ILE   A C    1 
ATOM   3706 O  O    . ILE   B 2 181 ? -6.34481  11.68673  -32.35382 1.000 40.68198  ? 186  ILE   A O    1 
ATOM   3707 C  CB   . ILE   B 2 181 ? -9.25661  10.71044  -31.38250 1.000 41.65006  ? 186  ILE   A CB   1 
ATOM   3708 C  CG1  . ILE   B 2 181 ? -10.78561 10.76228  -31.41034 1.000 34.78447  ? 186  ILE   A CG1  1 
ATOM   3709 C  CG2  . ILE   B 2 181 ? -8.74842  10.36451  -29.98955 1.000 32.94296  ? 186  ILE   A CG2  1 
ATOM   3710 C  CD1  . ILE   B 2 181 ? -11.44445 9.41622   -31.15725 1.000 40.65364  ? 186  ILE   A CD1  1 
ATOM   3711 N  N    . VAL   B 2 182 ? -6.83071  12.69871  -30.40478 1.000 37.27701  ? 187  VAL   A N    1 
ATOM   3712 C  CA   . VAL   B 2 182 ? -5.44967  12.74486  -29.94093 1.000 36.33232  ? 187  VAL   A CA   1 
ATOM   3713 C  C    . VAL   B 2 182 ? -5.38445  12.06188  -28.58592 1.000 37.94138  ? 187  VAL   A C    1 
ATOM   3714 O  O    . VAL   B 2 182 ? -6.23639  12.29981  -27.72384 1.000 37.30901  ? 187  VAL   A O    1 
ATOM   3715 C  CB   . VAL   B 2 182 ? -4.91381  14.18692  -29.85700 1.000 38.30142  ? 187  VAL   A CB   1 
ATOM   3716 C  CG1  . VAL   B 2 182 ? -5.67278  14.97685  -28.80193 1.000 36.82206  ? 187  VAL   A CG1  1 
ATOM   3717 C  CG2  . VAL   B 2 182 ? -3.42678  14.17408  -29.55716 1.000 32.47535  ? 187  VAL   A CG2  1 
ATOM   3718 N  N    . SER   B 2 183 ? -4.38334  11.20499  -28.40702 1.000 35.42886  ? 188  SER   A N    1 
ATOM   3719 C  CA   . SER   B 2 183 ? -4.19714  10.47403  -27.16403 1.000 38.83432  ? 188  SER   A CA   1 
ATOM   3720 C  C    . SER   B 2 183 ? -2.76810  10.64918  -26.67218 1.000 35.95775  ? 188  SER   A C    1 
ATOM   3721 O  O    . SER   B 2 183 ? -1.83420  10.79927  -27.46428 1.000 37.24135  ? 188  SER   A O    1 
ATOM   3722 C  CB   . SER   B 2 183 ? -4.51300  8.98199   -27.33398 1.000 36.50710  ? 188  SER   A CB   1 
ATOM   3723 O  OG   . SER   B 2 183 ? -3.61003  8.36907   -28.23806 1.000 35.93247  ? 188  SER   A OG   1 
ATOM   3724 N  N    . SER   B 2 184 ? -2.61796  10.63221  -25.35020 1.000 34.59168  ? 189  SER   A N    1 
ATOM   3725 C  CA   . SER   B 2 184 ? -1.32290  10.71936  -24.69234 1.000 37.91664  ? 189  SER   A CA   1 
ATOM   3726 C  C    . SER   B 2 184 ? -1.16468  9.54739   -23.73534 1.000 36.01136  ? 189  SER   A C    1 
ATOM   3727 O  O    . SER   B 2 184 ? -2.14657  9.04229   -23.18623 1.000 33.49993  ? 189  SER   A O    1 
ATOM   3728 C  CB   . SER   B 2 184 ? -1.17596  12.04338  -23.93237 1.000 36.77325  ? 189  SER   A CB   1 
ATOM   3729 O  OG   . SER   B 2 184 ? -2.17387  12.16629  -22.93026 1.000 36.90472  ? 189  SER   A OG   1 
ATOM   3730 N  N    . SER   B 2 185 ? 0.07839   9.12452   -23.51446 1.000 32.89240  ? 190  SER   A N    1 
ATOM   3731 C  CA   . SER   B 2 185 ? 0.30460   7.93255   -22.70747 1.000 37.98839  ? 190  SER   A CA   1 
ATOM   3732 C  C    . SER   B 2 185 ? 1.61767   8.04370   -21.95061 1.000 38.98124  ? 190  SER   A C    1 
ATOM   3733 O  O    . SER   B 2 185 ? 2.53355   8.76679   -22.34872 1.000 36.78154  ? 190  SER   A O    1 
ATOM   3734 C  CB   . SER   B 2 185 ? 0.31464   6.66654   -23.57046 1.000 28.70718  ? 190  SER   A CB   1 
ATOM   3735 O  OG   . SER   B 2 185 ? 0.79583   5.55560   -22.83649 1.000 38.57435  ? 190  SER   A OG   1 
ATOM   3736 N  N    . TYR   B 2 186 ? 1.69086   7.29572   -20.84461 1.000 42.70182  ? 191  TYR   A N    1 
ATOM   3737 C  CA   . TYR   B 2 186 ? 2.93196   7.13086   -20.09874 1.000 33.29741  ? 191  TYR   A CA   1 
ATOM   3738 C  C    . TYR   B 2 186 ? 4.02094   6.45096   -20.91684 1.000 38.98887  ? 191  TYR   A C    1 
ATOM   3739 O  O    . TYR   B 2 186 ? 5.18299   6.46509   -20.49697 1.000 40.17278  ? 191  TYR   A O    1 
ATOM   3740 C  CB   . TYR   B 2 186 ? 2.67218   6.32185   -18.82470 1.000 34.46320  ? 191  TYR   A CB   1 
ATOM   3741 C  CG   . TYR   B 2 186 ? 2.39422   7.15984   -17.59568 1.000 37.36391  ? 191  TYR   A CG   1 
ATOM   3742 C  CD1  . TYR   B 2 186 ? 1.36712   8.09373   -17.58059 1.000 38.56702  ? 191  TYR   A CD1  1 
ATOM   3743 C  CD2  . TYR   B 2 186 ? 3.15236   7.00393   -16.44276 1.000 38.38024  ? 191  TYR   A CD2  1 
ATOM   3744 C  CE1  . TYR   B 2 186 ? 1.11016   8.85672   -16.45157 1.000 38.13226  ? 191  TYR   A CE1  1 
ATOM   3745 C  CE2  . TYR   B 2 186 ? 2.90340   7.76092   -15.31274 1.000 40.99472  ? 191  TYR   A CE2  1 
ATOM   3746 C  CZ   . TYR   B 2 186 ? 1.88130   8.68481   -15.32265 1.000 36.58264  ? 191  TYR   A CZ   1 
ATOM   3747 O  OH   . TYR   B 2 186 ? 1.63034   9.43780   -14.19863 1.000 41.49748  ? 191  TYR   A OH   1 
ATOM   3748 N  N    . ASP   B 2 187 ? 3.68288   5.85391   -22.05980 1.000 36.98112  ? 192  ASP   A N    1 
ATOM   3749 C  CA   . ASP   B 2 187 ? 4.71885   5.30801   -22.92790 1.000 36.37980  ? 192  ASP   A CA   1 
ATOM   3750 C  C    . ASP   B 2 187 ? 5.52466   6.39309   -23.63700 1.000 42.39349  ? 192  ASP   A C    1 
ATOM   3751 O  O    . ASP   B 2 187 ? 6.39061   6.06117   -24.45309 1.000 41.88716  ? 192  ASP   A O    1 
ATOM   3752 C  CB   . ASP   B 2 187 ? 4.10484   4.34593   -23.95183 1.000 36.76479  ? 192  ASP   A CB   1 
ATOM   3753 C  CG   . ASP   B 2 187 ? 3.12267   5.02382   -24.89173 1.000 44.62378  ? 192  ASP   A CG   1 
ATOM   3754 O  OD1  . ASP   B 2 187 ? 3.01254   6.26781   -24.87274 1.000 40.58507  ? 192  ASP   A OD1  1 
ATOM   3755 O  OD2  . ASP   B 2 187 ? 2.45267   4.29974   -25.65965 1.000 42.37859  ? 192  ASP   A OD2  1 
ATOM   3756 N  N    . GLY   B 2 188 ? 5.25556   7.66506   -23.34899 1.000 39.25092  ? 193  GLY   A N    1 
ATOM   3757 C  CA   . GLY   B 2 188 ? 6.01639   8.76513   -23.90408 1.000 37.58959  ? 193  GLY   A CA   1 
ATOM   3758 C  C    . GLY   B 2 188 ? 5.57119   9.24407   -25.26604 1.000 44.93947  ? 193  GLY   A C    1 
ATOM   3759 O  O    . GLY   B 2 188 ? 6.23304   10.11513  -25.84212 1.000 44.30016  ? 193  GLY   A O    1 
ATOM   3760 N  N    . LEU   B 2 189 ? 4.47119   8.72195   -25.79492 1.000 36.70887  ? 194  LEU   A N    1 
ATOM   3761 C  CA   . LEU   B 2 189 ? 4.04702   9.00889   -27.15588 1.000 42.93082  ? 194  LEU   A CA   1 
ATOM   3762 C  C    . LEU   B 2 189 ? 2.73893   9.78475   -27.17175 1.000 44.79924  ? 194  LEU   A C    1 
ATOM   3763 O  O    . LEU   B 2 189 ? 1.90404   9.65267   -26.27266 1.000 34.46896  ? 194  LEU   A O    1 
ATOM   3764 C  CB   . LEU   B 2 189 ? 3.84807   7.71586   -27.95584 1.000 36.86738  ? 194  LEU   A CB   1 
ATOM   3765 C  CG   . LEU   B 2 189 ? 5.01116   6.73398   -28.07695 1.000 45.72149  ? 194  LEU   A CG   1 
ATOM   3766 C  CD1  . LEU   B 2 189 ? 4.58620   5.52192   -28.89189 1.000 43.18871  ? 194  LEU   A CD1  1 
ATOM   3767 C  CD2  . LEU   B 2 189 ? 6.21002   7.41509   -28.70509 1.000 44.96254  ? 194  LEU   A CD2  1 
ATOM   3768 N  N    A CYS   B 2 190 ? 2.57574   10.61672  -28.19175 0.802 39.09945  ? 195  CYS   A N    1 
ATOM   3769 N  N    B CYS   B 2 190 ? 2.55274   10.58072  -28.22274 0.198 39.23180  ? 195  CYS   A N    1 
ATOM   3770 C  CA   A CYS   B 2 190 ? 1.27165   11.16758  -28.52961 0.802 38.07291  ? 195  CYS   A CA   1 
ATOM   3771 C  CA   B CYS   B 2 190 ? 1.25965   11.19058  -28.52061 0.198 38.16953  ? 195  CYS   A CA   1 
ATOM   3772 C  C    A CYS   B 2 190 ? 0.82757   10.54152  -29.84256 0.802 38.37379  ? 195  CYS   A C    1 
ATOM   3773 C  C    B CYS   B 2 190 ? 0.79156   10.67151  -29.87256 0.198 38.45126  ? 195  CYS   A C    1 
ATOM   3774 O  O    A CYS   B 2 190 ? 1.64950   10.30859  -30.73064 0.802 38.16803  ? 195  CYS   A O    1 
ATOM   3775 O  O    B CYS   B 2 190 ? 1.56546   10.64658  -30.82664 0.198 39.13722  ? 195  CYS   A O    1 
ATOM   3776 C  CB   A CYS   B 2 190 ? 1.31148   12.69358  -28.64764 0.802 43.04752  ? 195  CYS   A CB   1 
ATOM   3777 C  CB   B CYS   B 2 190 ? 1.34549   12.71959  -28.52864 0.198 42.82135  ? 195  CYS   A CB   1 
ATOM   3778 S  SG   A CYS   B 2 190 ? 1.39755   13.55361  -27.06066 0.802 38.82199  ? 195  CYS   A SG   1 
ATOM   3779 S  SG   B CYS   B 2 190 ? -0.22963  13.54942  -28.84049 0.198 43.20311  ? 195  CYS   A SG   1 
ATOM   3780 N  N    . ARG   B 2 191 ? -0.46041  10.24138  -29.96142 1.000 34.36206  ? 196  ARG   A N    1 
ATOM   3781 C  CA   . ARG   B 2 191 ? -0.94747  9.60631   -31.17736 1.000 38.57274  ? 196  ARG   A CA   1 
ATOM   3782 C  C    . ARG   B 2 191 ? -2.18360  10.30118  -31.72024 1.000 39.40285  ? 196  ARG   A C    1 
ATOM   3783 O  O    . ARG   B 2 191 ? -3.12055  10.60309  -30.97414 1.000 38.00046  ? 196  ARG   A O    1 
ATOM   3784 C  CB   . ARG   B 2 191 ? -1.17929  8.10829   -30.95732 1.000 36.73704  ? 196  ARG   A CB   1 
ATOM   3785 C  CG   . ARG   B 2 191 ? 0.12477   7.34443   -31.17744 1.000 33.05948  ? 196  ARG   A CG   1 
ATOM   3786 C  CD   . ARG   B 2 191 ? 0.01593   5.83542   -31.08841 1.000 40.92459  ? 196  ARG   A CD   1 
ATOM   3787 N  NE   . ARG   B 2 191 ? 1.22394   5.22253   -31.62953 1.000 40.77074  ? 196  ARG   A NE   1 
ATOM   3788 C  CZ   . ARG   B 2 191 ? 1.79011   4.12060   -31.15658 1.000 37.79582  ? 196  ARG   A CZ   1 
ATOM   3789 N  NH1  . ARG   B 2 191 ? 1.28928   3.47956   -30.11352 1.000 34.95481  ? 196  ARG   A NH1  1 
ATOM   3790 N  NH2  . ARG   B 2 191 ? 2.89009   3.65571   -31.74069 1.000 40.33217  ? 196  ARG   A NH2  1 
ATOM   3791 N  N    . ILE   B 2 192 ? -2.14676  10.56716  -33.02525 1.000 33.59366  ? 197  ILE   A N    1 
ATOM   3792 C  CA   . ILE   B 2 192 ? -3.24391  11.17204  -33.77214 1.000 40.15968  ? 197  ILE   A CA   1 
ATOM   3793 C  C    . ILE   B 2 192 ? -3.93887  10.06696  -34.54905 1.000 42.10415  ? 197  ILE   A C    1 
ATOM   3794 O  O    . ILE   B 2 192 ? -3.30789  9.38301   -35.37211 1.000 44.58609  ? 197  ILE   A O    1 
ATOM   3795 C  CB   . ILE   B 2 192 ? -2.74012  12.27208  -34.71821 1.000 35.28354  ? 197  ILE   A CB   1 
ATOM   3796 C  CG1  . ILE   B 2 192 ? -2.00515  13.36517  -33.94030 1.000 40.98041  ? 197  ILE   A CG1  1 
ATOM   3797 C  CG2  . ILE   B 2 192 ? -3.90027  12.85395  -35.51509 1.000 42.25846  ? 197  ILE   A CG2  1 
ATOM   3798 C  CD1  . ILE   B 2 192 ? -2.89814  14.15309  -33.01221 1.000 41.35157  ? 197  ILE   A CD1  1 
ATOM   3799 N  N    . TRP   B 2 193 ? -5.24183  9.91982   -34.30091 1.000 36.41313  ? 198  TRP   A N    1 
ATOM   3800 C  CA   . TRP   B 2 193 ? -6.07477  8.84673   -34.81981 1.000 40.96663  ? 198  TRP   A CA   1 
ATOM   3801 C  C    . TRP   B 2 193 ? -7.18493  9.42460   -35.68170 1.000 46.71350  ? 198  TRP   A C    1 
ATOM   3802 O  O    . TRP   B 2 193 ? -7.74700  10.48055  -35.36366 1.000 42.34649  ? 198  TRP   A O    1 
ATOM   3803 C  CB   . TRP   B 2 193 ? -6.71557  8.04868   -33.68273 1.000 41.78402  ? 198  TRP   A CB   1 
ATOM   3804 C  CG   . TRP   B 2 193 ? -5.74841  7.50879   -32.69683 1.000 41.45385  ? 198  TRP   A CG   1 
ATOM   3805 C  CD1  . TRP   B 2 193 ? -5.21737  8.16186   -31.62189 1.000 39.54135  ? 198  TRP   A CD1  1 
ATOM   3806 C  CD2  . TRP   B 2 193 ? -5.20427  6.18785   -32.67487 1.000 42.53189  ? 198  TRP   A CD2  1 
ATOM   3807 N  NE1  . TRP   B 2 193 ? -4.36421  7.32896   -30.93797 1.000 48.37935  ? 198  TRP   A NE1  1 
ATOM   3808 C  CE2  . TRP   B 2 193 ? -4.33815  6.11095   -31.56596 1.000 44.41293  ? 198  TRP   A CE2  1 
ATOM   3809 C  CE3  . TRP   B 2 193 ? -5.35824  5.06482   -33.49284 1.000 40.03512  ? 198  TRP   A CE3  1 
ATOM   3810 C  CZ2  . TRP   B 2 193 ? -3.62899  4.95103   -31.25402 1.000 42.19793  ? 198  TRP   A CZ2  1 
ATOM   3811 C  CZ3  . TRP   B 2 193 ? -4.65509  3.91490   -33.17990 1.000 39.21281  ? 198  TRP   A CZ3  1 
ATOM   3812 C  CH2  . TRP   B 2 193 ? -3.80096  3.86600   -32.07099 1.000 42.50246  ? 198  TRP   A CH2  1 
ATOM   3813 N  N    . ASP   B 2 194 ? -7.52596  8.70455   -36.74966 1.000 43.51053  ? 199  ASP   A N    1 
ATOM   3814 C  CA   . ASP   B 2 194 ? -8.68608  9.04342   -37.56554 1.000 42.34545  ? 199  ASP   A CA   1 
ATOM   3815 C  C    . ASP   B 2 194 ? -9.93596  8.47830   -36.90340 1.000 35.43075  ? 199  ASP   A C    1 
ATOM   3816 O  O    . ASP   B 2 194 ? -10.07181 7.25829   -36.76137 1.000 41.59704  ? 199  ASP   A O    1 
ATOM   3817 C  CB   . ASP   B 2 194 ? -8.51818  8.49642   -38.98255 1.000 45.63515  ? 199  ASP   A CB   1 
ATOM   3818 C  CG   . ASP   B 2 194 ? -9.62432  8.94330   -39.91444 1.000 46.69864  ? 199  ASP   A CG   1 
ATOM   3819 O  OD1  . ASP   B 2 194 ? -10.78126 8.51218   -39.71831 1.000 50.87762  ? 199  ASP   A OD1  1 
ATOM   3820 O  OD2  . ASP   B 2 194 ? -9.33650  9.73631   -40.83448 1.000 50.56804  ? 199  ASP   A OD2  1 
ATOM   3821 N  N    . THR   B 2 195 ? -10.84600 9.36221   -36.48931 1.000 40.09163  ? 200  THR   A N    1 
ATOM   3822 C  CA   . THR   B 2 195 ? -12.04188 8.92610   -35.77718 1.000 39.89856  ? 200  THR   A CA   1 
ATOM   3823 C  C    . THR   B 2 195 ? -12.81586 7.87900   -36.57109 1.000 47.84064  ? 200  THR   A C    1 
ATOM   3824 O  O    . THR   B 2 195 ? -13.17769 6.81997   -36.04204 1.000 45.41008  ? 200  THR   A O    1 
ATOM   3825 C  CB   . THR   B 2 195 ? -12.93898 10.13001  -35.47310 1.000 42.08853  ? 200  THR   A CB   1 
ATOM   3826 O  OG1  . THR   B 2 195 ? -12.20400 11.10409  -34.72219 1.000 42.65202  ? 200  THR   A OG1  1 
ATOM   3827 C  CG2  . THR   B 2 195 ? -14.15985 9.69589   -34.67597 1.000 34.42206  ? 200  THR   A CG2  1 
ATOM   3828 N  N    . ALA   B 2 196 ? -13.07002 8.15696   -37.85106 1.000 48.81421  ? 201  ALA   A N    1 
ATOM   3829 C  CA   . ALA   B 2 196 ? -13.93701 7.28886   -38.64496 1.000 46.30596  ? 201  ALA   A CA   1 
ATOM   3830 C  C    . ALA   B 2 196 ? -13.31489 5.91592   -38.86001 1.000 41.76347  ? 201  ALA   A C    1 
ATOM   3831 O  O    . ALA   B 2 196 ? -13.99277 4.89185   -38.70892 1.000 43.19347  ? 201  ALA   A O    1 
ATOM   3832 C  CB   . ALA   B 2 196 ? -14.25523 7.95081   -39.98594 1.000 47.53082  ? 201  ALA   A CB   1 
ATOM   3833 N  N    . SER   B 2 197 ? -12.03193 5.86705   -39.21514 1.000 44.81334  ? 202  SER   A N    1 
ATOM   3834 C  CA   . SER   B 2 197 ? -11.39283 4.60412   -39.55920 1.000 45.96748  ? 202  SER   A CA   1 
ATOM   3835 C  C    . SER   B 2 197 ? -10.67964 3.94620   -38.38626 1.000 53.90491  ? 202  SER   A C    1 
ATOM   3836 O  O    . SER   B 2 197 ? -10.37152 2.75224   -38.46228 1.000 47.69229  ? 202  SER   A O    1 
ATOM   3837 C  CB   . SER   B 2 197 ? -10.38497 4.81221   -40.69330 1.000 40.90729  ? 202  SER   A CB   1 
ATOM   3838 O  OG   . SER   B 2 197 ? -9.27301  5.57233   -40.25643 1.000 46.20923  ? 202  SER   A OG   1 
ATOM   3839 N  N    . GLY   B 2 198 ? -10.41060 4.68625   -37.31130 1.000 45.31991  ? 203  GLY   A N    1 
ATOM   3840 C  CA   . GLY   B 2 198 ? -9.68643  4.11834   -36.19337 1.000 48.11368  ? 203  GLY   A CA   1 
ATOM   3841 C  C    . GLY   B 2 198 ? -8.21043  3.90449   -36.43452 1.000 42.89579  ? 203  GLY   A C    1 
ATOM   3842 O  O    . GLY   B 2 198 ? -7.53228  3.33757   -35.57059 1.000 46.99271  ? 203  GLY   A O    1 
ATOM   3843 N  N    . GLN   B 2 199 ? -7.68859  4.34153   -37.57558 1.000 41.01244  ? 204  GLN   A N    1 
ATOM   3844 C  CA   . GLN   B 2 199 ? -6.27861  4.16967   -37.88673 1.000 43.40225  ? 204  GLN   A CA   1 
ATOM   3845 C  C    . GLN   B 2 199 ? -5.44565  5.25677   -37.22183 1.000 49.84149  ? 204  GLN   A C    1 
ATOM   3846 O  O    . GLN   B 2 199 ? -5.88376  6.40072   -37.06980 1.000 43.55158  ? 204  GLN   A O    1 
ATOM   3847 C  CB   . GLN   B 2 199 ? -6.05877  4.19867   -39.39975 1.000 54.94682  ? 204  GLN   A CB   1 
ATOM   3848 C  CG   . GLN   B 2 199 ? -6.91675  3.20457   -40.16365 1.000 59.33755  ? 204  GLN   A CG   1 
ATOM   3849 C  CD   . GLN   B 2 199 ? -6.74555  1.78360   -39.65965 1.000 63.82571  ? 204  GLN   A CD   1 
ATOM   3850 O  OE1  . GLN   B 2 199 ? -5.63949  1.24071   -39.65976 1.000 57.82992  ? 204  GLN   A OE1  1 
ATOM   3851 N  NE2  . GLN   B 2 199 ? -7.84044  1.17749   -39.21353 1.000 59.57586  ? 204  GLN   A NE2  1 
ATOM   3852 N  N    . CYS   B 2 200 ? -4.23457  4.88590   -36.81995 1.000 43.94027  ? 205  CYS   A N    1 
ATOM   3853 C  CA   . CYS   B 2 200 ? -3.29161  5.84100   -36.25207 1.000 44.56320  ? 205  CYS   A CA   1 
ATOM   3854 C  C    . CYS   B 2 200 ? -2.63381  6.60506   -37.38914 1.000 48.41822  ? 205  CYS   A C    1 
ATOM   3855 O  O    . CYS   B 2 200 ? -1.85683  6.03713   -38.16322 1.000 51.46035  ? 205  CYS   A O    1 
ATOM   3856 C  CB   . CYS   B 2 200 ? -2.25145  5.13212   -35.39317 1.000 45.52877  ? 205  CYS   A CB   1 
ATOM   3857 S  SG   . CYS   B 2 200 ? -0.98949  6.23926   -34.71831 1.000 44.32103  ? 205  CYS   A SG   1 
ATOM   3858 N  N    . LEU   B 2 201 ? -2.94696  7.89402   -37.49713 1.000 41.97651  ? 206  LEU   A N    1 
ATOM   3859 C  CA   . LEU   B 2 201 ? -2.39515  8.71607   -38.56120 1.000 43.32335  ? 206  LEU   A CA   1 
ATOM   3860 C  C    . LEU   B 2 201 ? -1.02718  9.28321   -38.21935 1.000 41.16058  ? 206  LEU   A C    1 
ATOM   3861 O  O    . LEU   B 2 201 ? -0.22130  9.51629   -39.12744 1.000 48.22167  ? 206  LEU   A O    1 
ATOM   3862 C  CB   . LEU   B 2 201 ? -3.35431  9.86496   -38.89511 1.000 44.55757  ? 206  LEU   A CB   1 
ATOM   3863 C  CG   . LEU   B 2 201 ? -4.75831  9.45881   -39.34396 1.000 44.70484  ? 206  LEU   A CG   1 
ATOM   3864 C  CD1  . LEU   B 2 201 ? -5.60947  10.68872  -39.61288 1.000 38.86434  ? 206  LEU   A CD1  1 
ATOM   3865 C  CD2  . LEU   B 2 201 ? -4.69635  8.56480   -40.57995 1.000 37.12943  ? 206  LEU   A CD2  1 
ATOM   3866 N  N    . LYS   B 2 202 ? -0.73607  9.51726   -36.93938 1.000 41.28691  ? 207  LYS   A N    1 
ATOM   3867 C  CA   . LYS   B 2 202 ? 0.56791   10.07640  -36.60253 1.000 47.81436  ? 207  LYS   A CA   1 
ATOM   3868 C  C    . LYS   B 2 202 ? 1.00310   9.63847   -35.21057 1.000 41.52534  ? 207  LYS   A C    1 
ATOM   3869 O  O    . LYS   B 2 202 ? 0.17422   9.42839   -34.32048 1.000 41.21987  ? 207  LYS   A O    1 
ATOM   3870 C  CB   . LYS   B 2 202 ? 0.55574   11.60940  -36.68455 1.000 47.12346  ? 207  LYS   A CB   1 
ATOM   3871 C  CG   . LYS   B 2 202 ? 1.93066   12.23954  -36.87170 1.000 48.05653  ? 207  LYS   A CG   1 
ATOM   3872 C  CD   . LYS   B 2 202 ? 2.28249   12.37856  -38.34674 1.000 61.63798  ? 207  LYS   A CD   1 
ATOM   3873 C  CE   . LYS   B 2 202 ? 3.64240   13.03970  -38.53789 1.000 69.46703  ? 207  LYS   A CE   1 
ATOM   3874 N  NZ   . LYS   B 2 202 ? 3.96522   13.25771  -39.97893 1.000 65.45793  ? 207  LYS   A NZ   1 
ATOM   3875 N  N    . THR   B 2 203 ? 2.32013   9.52061   -35.03170 1.000 45.23611  ? 208  THR   A N    1 
ATOM   3876 C  CA   . THR   B 2 203 ? 2.92730   9.22069   -33.73576 1.000 42.66144  ? 208  THR   A CA   1 
ATOM   3877 C  C    . THR   B 2 203 ? 4.00022   10.26480  -33.44989 1.000 47.07497  ? 208  THR   A C    1 
ATOM   3878 O  O    . THR   B 2 203 ? 5.06116   10.25990  -34.08200 1.000 53.39804  ? 208  THR   A O    1 
ATOM   3879 C  CB   . THR   B 2 203 ? 3.52045   7.81175   -33.70781 1.000 41.21059  ? 208  THR   A CB   1 
ATOM   3880 O  OG1  . THR   B 2 203 ? 2.47654   6.84464   -33.85269 1.000 42.41503  ? 208  THR   A OG1  1 
ATOM   3881 C  CG2  . THR   B 2 203 ? 4.24762   7.56584   -32.39288 1.000 46.45060  ? 208  THR   A CG2  1 
ATOM   3882 N  N    . LEU   B 2 204 ? 3.72524   11.11478  -32.47287 1.000 44.70132  ? 209  LEU   A N    1 
ATOM   3883 C  CA   . LEU   B 2 204 ? 4.70017   12.15789  -32.09899 1.000 46.72101  ? 209  LEU   A CA   1 
ATOM   3884 C  C    . LEU   B 2 204 ? 5.65734   11.57300  -31.05608 1.000 47.70240  ? 209  LEU   A C    1 
ATOM   3885 O  O    . LEU   B 2 204 ? 5.20050   11.15497  -29.98003 1.000 39.83970  ? 209  LEU   A O    1 
ATOM   3886 C  CB   . LEU   B 2 204 ? 3.99209   13.41082  -31.59193 1.000 43.93320  ? 209  LEU   A CB   1 
ATOM   3887 C  CG   . LEU   B 2 204 ? 3.67887   14.47178  -32.64891 1.000 55.58441  ? 209  LEU   A CG   1 
ATOM   3888 C  CD1  . LEU   B 2 204 ? 2.50582   14.03664  -33.50178 1.000 54.37641  ? 209  LEU   A CD1  1 
ATOM   3889 C  CD2  . LEU   B 2 204 ? 3.38280   15.79076  -31.97290 1.000 56.74594  ? 209  LEU   A CD2  1 
ATOM   3890 N  N    . ILE   B 2 205 ? 6.93431   11.53513  -31.40022 1.000 47.79855  ? 210  ILE   A N    1 
ATOM   3891 C  CA   . ILE   B 2 205 ? 7.95546   11.02325  -30.44932 1.000 61.41776  ? 210  ILE   A CA   1 
ATOM   3892 C  C    . ILE   B 2 205 ? 8.94037   12.16336  -30.18444 1.000 64.92504  ? 210  ILE   A C    1 
ATOM   3893 O  O    . ILE   B 2 205 ? 9.09619   13.04136  -31.05646 1.000 61.81152  ? 210  ILE   A O    1 
ATOM   3894 C  CB   . ILE   B 2 205 ? 8.66653   9.76932   -30.98838 1.000 62.46273  ? 210  ILE   A CB   1 
ATOM   3895 C  CG1  . ILE   B 2 205 ? 9.90741   10.11644  -31.80451 1.000 71.96058  ? 210  ILE   A CG1  1 
ATOM   3896 C  CG2  . ILE   B 2 205 ? 7.70554   8.89221   -31.79026 1.000 64.64568  ? 210  ILE   A CG2  1 
ATOM   3897 C  CD1  . ILE   B 2 205 ? 9.63523   10.32139  -33.28249 1.000 69.45299  ? 210  ILE   A CD1  1 
ATOM   3898 N  N    . ASP   B 2 206 ? 9.55749   12.15244  -29.00850 1.000 66.82050  ? 211  ASP   A N    1 
ATOM   3899 C  CA   . ASP   B 2 206 ? 10.59341  13.17555  -28.74262 1.000 65.75619  ? 211  ASP   A CA   1 
ATOM   3900 C  C    . ASP   B 2 206 ? 11.92252  12.48769  -28.44775 1.000 74.24285  ? 211  ASP   A C    1 
ATOM   3901 O  O    . ASP   B 2 206 ? 11.92467  11.27870  -28.15674 1.000 71.66449  ? 211  ASP   A O    1 
ATOM   3902 C  CB   . ASP   B 2 206 ? 10.17843  14.15752  -27.66159 1.000 71.80408  ? 211  ASP   A CB   1 
ATOM   3903 C  CG   . ASP   B 2 206 ? 10.70726  15.57357  -27.82567 1.000 62.25824  ? 211  ASP   A CG   1 
ATOM   3904 O  OD1  . ASP   B 2 206 ? 11.61515  15.76866  -28.65676 1.000 65.00787  ? 211  ASP   A OD1  1 
ATOM   3905 O  OD2  . ASP   B 2 206 ? 10.20424  16.46853  -27.12462 1.000 73.78416  ? 211  ASP   A OD2  1 
ATOM   3906 N  N    . ASP   B 2 207 ? 13.00343  13.24380  -28.55888 1.000 81.45228  ? 212  ASP   A N    1 
ATOM   3907 C  CA   . ASP   B 2 207 ? 14.34651  12.73995  -28.28601 1.000 80.85133  ? 212  ASP   A CA   1 
ATOM   3908 C  C    . ASP   B 2 207 ? 14.32373  11.79096  -27.09500 1.000 75.99731  ? 212  ASP   A C    1 
ATOM   3909 O  O    . ASP   B 2 207 ? 14.57384  10.59098  -27.24301 1.000 84.43917  ? 212  ASP   A O    1 
ATOM   3910 C  CB   . ASP   B 2 207 ? 15.31741  13.89405  -28.03613 1.000 79.29276  ? 212  ASP   A CB   1 
ATOM   3911 C  CG   . ASP   B 2 207 ? 15.68920  14.63207  -29.30918 1.000 93.38874  ? 212  ASP   A CG   1 
ATOM   3912 O  OD1  . ASP   B 2 207 ? 15.85316  13.96908  -30.35619 1.000 96.85506  ? 212  ASP   A OD1  1 
ATOM   3913 O  OD2  . ASP   B 2 207 ? 15.81308  15.87409  -29.26421 1.000 88.48506  ? 212  ASP   A OD2  1 
ATOM   3914 N  N    . ASP   B 2 208 ? 14.02780  12.31994  -25.91497 1.000 77.26983  ? 213  ASP   A N    1 
ATOM   3915 C  CA   . ASP   B 2 208 ? 13.62201  11.48292  -24.79992 1.000 74.48323  ? 213  ASP   A CA   1 
ATOM   3916 C  C    . ASP   B 2 208 ? 12.11002  11.29576  -24.84376 1.000 79.00968  ? 213  ASP   A C    1 
ATOM   3917 O  O    . ASP   B 2 208 ? 11.38088  12.10967  -25.41669 1.000 77.75718  ? 213  ASP   A O    1 
ATOM   3918 C  CB   . ASP   B 2 208 ? 14.04708  12.09798  -23.46497 1.000 77.00439  ? 213  ASP   A CB   1 
ATOM   3919 C  CG   . ASP   B 2 208 ? 15.54811  12.03714  -23.24413 1.000 102.21657 ? 213  ASP   A CG   1 
ATOM   3920 O  OD1  . ASP   B 2 208 ? 16.23212  11.28220  -23.96619 1.000 103.72712 ? 213  ASP   A OD1  1 
ATOM   3921 O  OD2  . ASP   B 2 208 ? 16.04713  12.74820  -22.34319 1.000 100.11603 ? 213  ASP   A OD2  1 
ATOM   3922 N  N    . ASN   B 2 209 ? 11.64220  10.20572  -24.24370 1.000 66.60990  ? 214  ASN   A N    1 
ATOM   3923 C  CA   . ASN   B 2 209 ? 10.21824  9.87257   -24.21954 1.000 58.42520  ? 214  ASN   A CA   1 
ATOM   3924 C  C    . ASN   B 2 209 ? 9.70639   9.84353   -22.78449 1.000 51.51278  ? 214  ASN   A C    1 
ATOM   3925 O  O    . ASN   B 2 209 ? 9.24755   8.80149   -22.29643 1.000 49.70517  ? 214  ASN   A O    1 
ATOM   3926 C  CB   . ASN   B 2 209 ? 9.95930   8.54153   -24.92050 1.000 57.35833  ? 214  ASN   A CB   1 
ATOM   3927 C  CG   . ASN   B 2 209 ? 10.77748  7.40563   -24.34257 1.000 65.27984  ? 214  ASN   A CG   1 
ATOM   3928 O  OD1  . ASN   B 2 209 ? 11.47357  7.57071   -23.34064 1.000 70.17707  ? 214  ASN   A OD1  1 
ATOM   3929 N  ND2  . ASN   B 2 209 ? 10.69154  6.23761   -24.96854 1.000 59.98105  ? 214  ASN   A ND2  1 
ATOM   3930 N  N    . PRO   B 2 210 ? 9.75535   10.96955  -22.07851 1.000 46.95848  ? 215  PRO   A N    1 
ATOM   3931 C  CA   . PRO   B 2 210 ? 9.16248   11.01350  -20.75044 1.000 43.16007  ? 215  PRO   A CA   1 
ATOM   3932 C  C    . PRO   B 2 210 ? 7.66750   10.79235  -20.83928 1.000 42.68555  ? 215  PRO   A C    1 
ATOM   3933 O  O    . PRO   B 2 210 ? 7.04436   11.04727  -21.88722 1.000 42.25716  ? 215  PRO   A O    1 
ATOM   3934 C  CB   . PRO   B 2 210 ? 9.49539   12.42954  -20.26050 1.000 41.23736  ? 215  PRO   A CB   1 
ATOM   3935 C  CG   . PRO   B 2 210 ? 9.64917   13.22554  -21.51052 1.000 47.50793  ? 215  PRO   A CG   1 
ATOM   3936 C  CD   . PRO   B 2 210 ? 10.26917  12.28560  -22.50058 1.000 54.66316  ? 215  PRO   A CD   1 
ATOM   3937 N  N    . PRO   B 2 211 ? 7.04666   10.29829  -19.77021 1.000 33.75835  ? 216  PRO   A N    1 
ATOM   3938 C  CA   . PRO   B 2 211 ? 5.59868   10.07214  -19.79806 1.000 36.01450  ? 216  PRO   A CA   1 
ATOM   3939 C  C    . PRO   B 2 211 ? 4.84751   11.32706  -20.22199 1.000 42.96351  ? 216  PRO   A C    1 
ATOM   3940 O  O    . PRO   B 2 211 ? 5.13744   12.43210  -19.76004 1.000 35.23512  ? 216  PRO   A O    1 
ATOM   3941 C  CB   . PRO   B 2 211 ? 5.27488   9.67913   -18.35302 1.000 36.04587  ? 216  PRO   A CB   1 
ATOM   3942 C  CG   . PRO   B 2 211 ? 6.53899   9.06427   -17.84814 1.000 37.41577  ? 216  PRO   A CG   1 
ATOM   3943 C  CD   . PRO   B 2 211 ? 7.65784   9.82737   -18.51427 1.000 47.77933  ? 216  PRO   A CD   1 
ATOM   3944 N  N    . VAL   B 2 212 ? 3.88043   11.14595  -21.11389 1.000 39.99482  ? 217  VAL   A N    1 
ATOM   3945 C  CA   . VAL   B 2 212 ? 3.02627   12.23685  -21.57381 1.000 36.03997  ? 217  VAL   A CA   1 
ATOM   3946 C  C    . VAL   B 2 212 ? 1.77036   12.23173  -20.71168 1.000 35.90537  ? 217  VAL   A C    1 
ATOM   3947 O  O    . VAL   B 2 212 ? 0.94745   11.31764  -20.79758 1.000 39.83951  ? 217  VAL   A O    1 
ATOM   3948 C  CB   . VAL   B 2 212 ? 2.68613   12.09680  -23.06278 1.000 39.03435  ? 217  VAL   A CB   1 
ATOM   3949 C  CG1  . VAL   B 2 212 ? 1.85795   13.28470  -23.53170 1.000 38.17271  ? 217  VAL   A CG1  1 
ATOM   3950 C  CG2  . VAL   B 2 212 ? 3.96405   11.97192  -23.88591 1.000 37.70362  ? 217  VAL   A CG2  1 
ATOM   3951 N  N    . SER   B 2 213 ? 1.62634   13.26073  -19.87668 1.000 37.77910  ? 218  SER   A N    1 
ATOM   3952 C  CA   . SER   B 2 213 ? 0.59344   13.30663  -18.85057 1.000 36.00541  ? 218  SER   A CA   1 
ATOM   3953 C  C    . SER   B 2 213 ? -0.65468  14.07050  -19.27145 1.000 33.67323  ? 218  SER   A C    1 
ATOM   3954 O  O    . SER   B 2 213 ? -1.64560  14.04640  -18.53434 1.000 33.24118  ? 218  SER   A O    1 
ATOM   3955 C  CB   . SER   B 2 213 ? 1.15851   13.92771  -17.56564 1.000 34.56846  ? 218  SER   A CB   1 
ATOM   3956 O  OG   . SER   B 2 213 ? 1.81236   15.15077  -17.84572 1.000 38.07054  ? 218  SER   A OG   1 
ATOM   3957 N  N    . PHE   B 2 214 ? -0.63887  14.73548  -20.42246 1.000 32.56925  ? 219  PHE   A N    1 
ATOM   3958 C  CA   . PHE   B 2 214 ? -1.81200  15.46236  -20.89434 1.000 33.85864  ? 219  PHE   A CA   1 
ATOM   3959 C  C    . PHE   B 2 214 ? -1.59319  15.88036  -22.33937 1.000 35.99714  ? 219  PHE   A C    1 
ATOM   3960 O  O    . PHE   B 2 214 ? -0.46326  16.15647  -22.75050 1.000 34.75101  ? 219  PHE   A O    1 
ATOM   3961 C  CB   . PHE   B 2 214 ? -2.10103  16.69834  -20.02833 1.000 33.83185  ? 219  PHE   A CB   1 
ATOM   3962 C  CG   . PHE   B 2 214 ? -3.09820  17.64422  -20.64624 1.000 34.64421  ? 219  PHE   A CG   1 
ATOM   3963 C  CD1  . PHE   B 2 214 ? -4.45516  17.46909  -20.44309 1.000 38.94016  ? 219  PHE   A CD1  1 
ATOM   3964 C  CD2  . PHE   B 2 214 ? -2.67739  18.69426  -21.44630 1.000 34.83059  ? 219  PHE   A CD2  1 
ATOM   3965 C  CE1  . PHE   B 2 214 ? -5.37231  18.32598  -21.01501 1.000 37.73533  ? 219  PHE   A CE1  1 
ATOM   3966 C  CE2  . PHE   B 2 214 ? -3.59054  19.55116  -22.02321 1.000 36.75740  ? 219  PHE   A CE2  1 
ATOM   3967 C  CZ   . PHE   B 2 214 ? -4.93950  19.36702  -21.80907 1.000 39.00307  ? 219  PHE   A CZ   1 
ATOM   3968 N  N    . VAL   B 2 215 ? -2.68828  15.94124  -23.09626 1.000 34.49117  ? 220  VAL   A N    1 
ATOM   3969 C  CA   . VAL   B 2 215 ? -2.65348  16.46722  -24.45527 1.000 36.84712  ? 220  VAL   A CA   1 
ATOM   3970 C  C    . VAL   B 2 215 ? -4.04857  16.94307  -24.82113 1.000 37.58021  ? 220  VAL   A C    1 
ATOM   3971 O  O    . VAL   B 2 215 ? -5.04746  16.45297  -24.28402 1.000 29.41662  ? 220  VAL   A O    1 
ATOM   3972 C  CB   . VAL   B 2 215 ? -2.13447  15.40826  -25.46131 1.000 36.47316  ? 220  VAL   A CB   1 
ATOM   3973 C  CG1  . VAL   B 2 215 ? -3.13237  14.26316  -25.58819 1.000 31.07643  ? 220  VAL   A CG1  1 
ATOM   3974 C  CG2  . VAL   B 2 215 ? -1.87368  16.05027  -26.81235 1.000 37.55373  ? 220  VAL   A CG2  1 
ATOM   3975 N  N    . LYS   B 2 216 ? -4.11276  17.90405  -25.74113 1.000 36.79280  ? 221  LYS   A N    1 
ATOM   3976 C  CA   . LYS   B 2 216 ? -5.36587  18.36491  -26.31301 1.000 34.54689  ? 221  LYS   A CA   1 
ATOM   3977 C  C    . LYS   B 2 216 ? -5.04109  19.17993  -27.55505 1.000 43.88015  ? 221  LYS   A C    1 
ATOM   3978 O  O    . LYS   B 2 216 ? -3.96316  19.77304  -27.65717 1.000 38.02634  ? 221  LYS   A O    1 
ATOM   3979 C  CB   . LYS   B 2 216 ? -6.17885  19.20284  -25.32093 1.000 38.47575  ? 221  LYS   A CB   1 
ATOM   3980 C  CG   . LYS   B 2 216 ? -5.74200  20.65989  -25.24100 1.000 41.44250  ? 221  LYS   A CG   1 
ATOM   3981 C  CD   . LYS   B 2 216 ? -6.44395  21.39583  -24.10693 1.000 43.81278  ? 221  LYS   A CD   1 
ATOM   3982 C  CE   . LYS   B 2 216 ? -7.95398  21.40767  -24.28877 1.000 52.33700  ? 221  LYS   A CE   1 
ATOM   3983 N  NZ   . LYS   B 2 216 ? -8.35718  22.13961  -25.52074 1.000 49.09035  ? 221  LYS   A NZ   1 
ATOM   3984 N  N    . PHE   B 2 217 ? -5.97419  19.18982  -28.50095 1.000 37.58320  ? 222  PHE   A N    1 
ATOM   3985 C  CA   . PHE   B 2 217 ? -5.81640  20.02382  -29.68198 1.000 44.82091  ? 222  PHE   A CA   1 
ATOM   3986 C  C    . PHE   B 2 217 ? -5.94451  21.49682  -29.31299 1.000 40.70740  ? 222  PHE   A C    1 
ATOM   3987 O  O    . PHE   B 2 217 ? -6.64045  21.86476  -28.36392 1.000 39.44248  ? 222  PHE   A O    1 
ATOM   3988 C  CB   . PHE   B 2 217 ? -6.86847  19.67970  -30.73687 1.000 38.53756  ? 222  PHE   A CB   1 
ATOM   3989 C  CG   . PHE   B 2 217 ? -6.63941  18.36472  -31.43087 1.000 38.53726  ? 222  PHE   A CG   1 
ATOM   3990 C  CD1  . PHE   B 2 217 ? -5.71951  18.26080  -32.46097 1.000 39.26813  ? 222  PHE   A CD1  1 
ATOM   3991 C  CD2  . PHE   B 2 217 ? -7.36425  17.24164  -31.06778 1.000 33.57857  ? 222  PHE   A CD2  1 
ATOM   3992 C  CE1  . PHE   B 2 217 ? -5.51445  17.05381  -33.10898 1.000 44.28900  ? 222  PHE   A CE1  1 
ATOM   3993 C  CE2  . PHE   B 2 217 ? -7.16720  16.03266  -31.71179 1.000 40.77190  ? 222  PHE   A CE2  1 
ATOM   3994 C  CZ   . PHE   B 2 217 ? -6.24129  15.93774  -32.73188 1.000 37.44506  ? 222  PHE   A CZ   1 
ATOM   3995 N  N    . SER   B 2 218 ? -5.25868  22.34488  -30.07607 1.000 43.31637  ? 223  SER   A N    1 
ATOM   3996 C  CA   . SER   B 2 218 ? -5.49282  23.77185  -29.97806 1.000 46.54231  ? 223  SER   A CA   1 
ATOM   3997 C  C    . SER   B 2 218 ? -6.84592  24.10971  -30.59893 1.000 44.66100  ? 223  SER   A C    1 
ATOM   3998 O  O    . SER   B 2 218 ? -7.39392  23.32464  -31.37686 1.000 47.74789  ? 223  SER   A O    1 
ATOM   3999 C  CB   . SER   B 2 218 ? -4.37998  24.54796  -30.67719 1.000 41.61464  ? 223  SER   A CB   1 
ATOM   4000 O  OG   . SER   B 2 218 ? -4.29708  24.19595  -32.04720 1.000 48.95212  ? 223  SER   A OG   1 
ATOM   4001 N  N    . PRO   B 2 219 ? -7.41201  25.26965  -30.26288 1.000 48.23284  ? 224  PRO   A N    1 
ATOM   4002 C  CA   . PRO   B 2 219 ? -8.73110  25.61451  -30.82075 1.000 46.05462  ? 224  PRO   A CA   1 
ATOM   4003 C  C    . PRO   B 2 219 ? -8.77026  25.55248  -32.33774 1.000 46.23088  ? 224  PRO   A C    1 
ATOM   4004 O  O    . PRO   B 2 219 ? -9.77327  25.11037  -32.91263 1.000 50.34734  ? 224  PRO   A O    1 
ATOM   4005 C  CB   . PRO   B 2 219 ? -8.97220  27.03949  -30.29574 1.000 45.70986  ? 224  PRO   A CB   1 
ATOM   4006 C  CG   . PRO   B 2 219 ? -7.61821  27.54863  -29.89789 1.000 52.46271  ? 224  PRO   A CG   1 
ATOM   4007 C  CD   . PRO   B 2 219 ? -6.86103  26.34772  -29.42695 1.000 48.88777  ? 224  PRO   A CD   1 
ATOM   4008 N  N    . ASN   B 2 220 ? -7.69537  25.97859  -33.00486 1.000 45.58662  ? 225  ASN   A N    1 
ATOM   4009 C  CA   . ASN   B 2 220 ? -7.64452  25.92257  -34.46086 1.000 57.56754  ? 225  ASN   A CA   1 
ATOM   4010 C  C    . ASN   B 2 220 ? -7.47943  24.50158  -34.98386 1.000 62.70156  ? 225  ASN   A C    1 
ATOM   4011 O  O    . ASN   B 2 220 ? -7.77152  24.24954  -36.15783 1.000 62.48827  ? 225  ASN   A O    1 
ATOM   4012 C  CB   . ASN   B 2 220 ? -6.50767  26.80368  -34.97600 1.000 58.29765  ? 225  ASN   A CB   1 
ATOM   4013 C  CG   . ASN   B 2 220 ? -5.18756  26.50983  -34.28913 1.000 64.84817  ? 225  ASN   A CG   1 
ATOM   4014 O  OD1  . ASN   B 2 220 ? -4.45951  25.60290  -34.69020 1.000 62.87482  ? 225  ASN   A OD1  1 
ATOM   4015 N  ND2  . ASN   B 2 220 ? -4.87753  27.27288  -33.24317 1.000 63.06594  ? 225  ASN   A ND2  1 
ATOM   4016 N  N    . GLY   B 2 221 ? -7.01124  23.57364  -34.14990 1.000 62.73889  ? 226  GLY   A N    1 
ATOM   4017 C  CA   . GLY   B 2 221 ? -6.87714  22.18465  -34.53490 1.000 51.80486  ? 226  GLY   A CA   1 
ATOM   4018 C  C    . GLY   B 2 221 ? -5.57017  21.81478  -35.20303 1.000 48.48116  ? 226  GLY   A C    1 
ATOM   4019 O  O    . GLY   B 2 221 ? -5.36108  20.63280  -35.50104 1.000 51.26703  ? 226  GLY   A O    1 
ATOM   4020 N  N    . LYS   B 2 222 ? -4.68329  22.77887  -35.44414 1.000 46.65393  ? 227  LYS   A N    1 
ATOM   4021 C  CA   . LYS   B 2 222 ? -3.42034  22.50299  -36.11527 1.000 54.14876  ? 227  LYS   A CA   1 
ATOM   4022 C  C    . LYS   B 2 222 ? -2.30020  22.15012  -35.15238 1.000 50.75865  ? 227  LYS   A C    1 
ATOM   4023 O  O    . LYS   B 2 222 ? -1.29518  21.56822  -35.57748 1.000 45.42729  ? 227  LYS   A O    1 
ATOM   4024 C  CB   . LYS   B 2 222 ? -3.00355  23.70802  -36.96033 1.000 55.10575  ? 227  LYS   A CB   1 
ATOM   4025 C  CG   . LYS   B 2 222 ? -4.17369  24.37089  -37.65921 1.000 72.36579  ? 227  LYS   A CG   1 
ATOM   4026 C  CD   . LYS   B 2 222 ? -3.74390  25.09592  -38.91727 1.000 86.18824  ? 227  LYS   A CD   1 
ATOM   4027 C  CE   . LYS   B 2 222 ? -4.96103  25.53278  -39.71714 1.000 88.36168  ? 227  LYS   A CE   1 
ATOM   4028 N  NZ   . LYS   B 2 222 ? -4.57724  26.26481  -40.95419 1.000 91.31178  ? 227  LYS   A NZ   1 
ATOM   4029 N  N    . TYR   B 2 223 ? -2.44410  22.48812  -33.87737 1.000 43.37125  ? 228  TYR   A N    1 
ATOM   4030 C  CA   . TYR   B 2 223 ? -1.43596  22.21724  -32.87047 1.000 43.82987  ? 228  TYR   A CA   1 
ATOM   4031 C  C    . TYR   B 2 223 ? -2.01176  21.30519  -31.79640 1.000 47.14177  ? 228  TYR   A C    1 
ATOM   4032 O  O    . TYR   B 2 223 ? -3.22973  21.17707  -31.63827 1.000 40.92380  ? 228  TYR   A O    1 
ATOM   4033 C  CB   . TYR   B 2 223 ? -0.92803  23.51330  -32.22754 1.000 48.32651  ? 228  TYR   A CB   1 
ATOM   4034 C  CG   . TYR   B 2 223 ? -0.45224  24.54434  -33.22061 1.000 50.16058  ? 228  TYR   A CG   1 
ATOM   4035 C  CD1  . TYR   B 2 223 ? 0.43268   24.20442  -34.23369 1.000 54.93641  ? 228  TYR   A CD1  1 
ATOM   4036 C  CD2  . TYR   B 2 223 ? -0.89937  25.85629  -33.15257 1.000 51.73932  ? 228  TYR   A CD2  1 
ATOM   4037 C  CE1  . TYR   B 2 223 ? 0.86649   25.14445  -35.14575 1.000 52.47235  ? 228  TYR   A CE1  1 
ATOM   4038 C  CE2  . TYR   B 2 223 ? -0.46957  26.80533  -34.06163 1.000 59.50653  ? 228  TYR   A CE2  1 
ATOM   4039 C  CZ   . TYR   B 2 223 ? 0.41436   26.44341  -35.05572 1.000 63.77241  ? 228  TYR   A CZ   1 
ATOM   4040 O  OH   . TYR   B 2 223 ? 0.84117   27.38344  -35.96478 1.000 65.32728  ? 228  TYR   A OH   1 
ATOM   4041 N  N    . ILE   B 2 224 ? -1.11161  20.66730  -31.05749 1.000 39.97717  ? 229  ILE   A N    1 
ATOM   4042 C  CA   . ILE   B 2 224 ? -1.47741  19.93728  -29.85044 1.000 44.65236  ? 229  ILE   A CA   1 
ATOM   4043 C  C    . ILE   B 2 224 ? -0.61834  20.44438  -28.70153 1.000 34.87862  ? 229  ILE   A C    1 
ATOM   4044 O  O    . ILE   B 2 224 ? 0.58462   20.67650  -28.86766 1.000 38.95919  ? 229  ILE   A O    1 
ATOM   4045 C  CB   . ILE   B 2 224 ? -1.32626  18.40829  -30.00443 1.000 39.96202  ? 229  ILE   A CB   1 
ATOM   4046 C  CG1  . ILE   B 2 224 ? 0.13375   18.02844  -30.26158 1.000 44.03105  ? 229  ILE   A CG1  1 
ATOM   4047 C  CG2  . ILE   B 2 224 ? -2.24233  17.88418  -31.10433 1.000 40.63281  ? 229  ILE   A CG2  1 
ATOM   4048 C  CD1  . ILE   B 2 224 ? 0.49094   16.64048  -29.78160 1.000 55.01211  ? 229  ILE   A CD1  1 
ATOM   4049 N  N    . LEU   B 2 225 ? -1.24324  20.63133  -27.54547 1.000 41.14028  ? 230  LEU   A N    1 
ATOM   4050 C  CA   . LEU   B 2 225 ? -0.55215  21.00942  -26.32055 1.000 37.70705  ? 230  LEU   A CA   1 
ATOM   4051 C  C    . LEU   B 2 225 ? -0.35293  19.75245  -25.48455 1.000 38.96224  ? 230  LEU   A C    1 
ATOM   4052 O  O    . LEU   B 2 225 ? -1.32882  19.12835  -25.05544 1.000 35.21641  ? 230  LEU   A O    1 
ATOM   4053 C  CB   . LEU   B 2 225 ? -1.35018  22.05734  -25.54748 1.000 37.03624  ? 230  LEU   A CB   1 
ATOM   4054 C  CG   . LEU   B 2 225 ? -0.72010  22.59843  -24.26255 1.000 30.49057  ? 230  LEU   A CG   1 
ATOM   4055 C  CD1  . LEU   B 2 225 ? 0.48578   23.47455  -24.58069 1.000 26.72945  ? 230  LEU   A CD1  1 
ATOM   4056 C  CD2  . LEU   B 2 225 ? -1.75209  23.36433  -23.44745 1.000 32.08600  ? 230  LEU   A CD2  1 
ATOM   4057 N  N    . ALA   B 2 226 ? 0.90513   19.37958  -25.26368 1.000 36.28793  ? 231  ALA   A N    1 
ATOM   4058 C  CA   . ALA   B 2 226 ? 1.24534   18.14763  -24.56470 1.000 41.36148  ? 231  ALA   A CA   1 
ATOM   4059 C  C    . ALA   B 2 226 ? 2.11143   18.46073  -23.35380 1.000 43.25182  ? 231  ALA   A C    1 
ATOM   4060 O  O    . ALA   B 2 226 ? 3.13535   19.13784  -23.47591 1.000 37.37863  ? 231  ALA   A O    1 
ATOM   4061 C  CB   . ALA   B 2 226 ? 1.97234   17.17069  -25.49377 1.000 36.19249  ? 231  ALA   A CB   1 
ATOM   4062 N  N    . ALA   B 2 227 ? 1.69760   17.96871  -22.19475 1.000 34.43939  ? 232  ALA   A N    1 
ATOM   4063 C  CA   . ALA   B 2 227 ? 2.49372   18.06580  -20.98083 1.000 40.15508  ? 232  ALA   A CA   1 
ATOM   4064 C  C    . ALA   B 2 227 ? 3.26688   16.77189  -20.77890 1.000 38.51243  ? 232  ALA   A C    1 
ATOM   4065 O  O    . ALA   B 2 227 ? 2.73097   15.67983  -20.99083 1.000 38.70597  ? 232  ALA   A O    1 
ATOM   4066 C  CB   . ALA   B 2 227 ? 1.60782   18.34173  -19.76474 1.000 33.65593  ? 232  ALA   A CB   1 
ATOM   4067 N  N    . THR   B 2 228 ? 4.52991   16.89302  -20.38103 1.000 36.05553  ? 233  THR   A N    1 
ATOM   4068 C  CA   . THR   B 2 228 ? 5.32107   15.72411  -20.02110 1.000 36.80032  ? 233  THR   A CA   1 
ATOM   4069 C  C    . THR   B 2 228 ? 5.78921   15.85218  -18.57915 1.000 40.32386  ? 233  THR   A C    1 
ATOM   4070 O  O    . THR   B 2 228 ? 5.99515   16.95921  -18.07119 1.000 41.19064  ? 233  THR   A O    1 
ATOM   4071 C  CB   . THR   B 2 228 ? 6.52399   15.53723  -20.95922 1.000 42.70826  ? 233  THR   A CB   1 
ATOM   4072 O  OG1  . THR   B 2 228 ? 7.19384   16.78929  -21.15731 1.000 40.06874  ? 233  THR   A OG1  1 
ATOM   4073 C  CG2  . THR   B 2 228 ? 6.06690   14.98516  -22.30417 1.000 40.80076  ? 233  THR   A CG2  1 
ATOM   4074 N  N    . LEU   B 2 229 ? 5.95040   14.70420  -17.92115 1.000 39.61582  ? 234  LEU   A N    1 
ATOM   4075 C  CA   . LEU   B 2 229 ? 6.28855   14.68626  -16.50319 1.000 37.40265  ? 234  LEU   A CA   1 
ATOM   4076 C  C    . LEU   B 2 229 ? 7.74153   15.07541  -16.26935 1.000 42.34501  ? 234  LEU   A C    1 
ATOM   4077 O  O    . LEU   B 2 229 ? 8.41668   14.50249  -15.40641 1.000 38.62508  ? 234  LEU   A O    1 
ATOM   4078 C  CB   . LEU   B 2 229 ? 5.99575   13.31323  -15.89814 1.000 36.60815  ? 234  LEU   A CB   1 
ATOM   4079 C  CG   . LEU   B 2 229 ? 4.50980   12.96108  -15.78898 1.000 43.60450  ? 234  LEU   A CG   1 
ATOM   4080 C  CD1  . LEU   B 2 229 ? 4.31402   11.69207  -14.97194 1.000 46.42115  ? 234  LEU   A CD1  1 
ATOM   4081 C  CD2  . LEU   B 2 229 ? 3.73075   14.12101  -15.18691 1.000 45.18058  ? 234  LEU   A CD2  1 
ATOM   4082 N  N    . ASP   B 2 230 ? 8.22935   16.04945  -17.03541 1.000 43.73594  ? 235  ASP   A N    1 
ATOM   4083 C  CA   . ASP   B 2 230 ? 9.53831   16.65459  -16.81856 1.000 40.70604  ? 235  ASP   A CA   1 
ATOM   4084 C  C    . ASP   B 2 230 ? 9.41016   18.16858  -16.68756 1.000 44.32928  ? 235  ASP   A C    1 
ATOM   4085 O  O    . ASP   B 2 230 ? 10.30104  18.91667  -17.10367 1.000 44.99721  ? 235  ASP   A O    1 
ATOM   4086 C  CB   . ASP   B 2 230 ? 10.50923  16.27868  -17.93665 1.000 33.64546  ? 235  ASP   A CB   1 
ATOM   4087 C  CG   . ASP   B 2 230 ? 10.03404  16.73361  -19.30361 1.000 39.85756  ? 235  ASP   A CG   1 
ATOM   4088 O  OD1  . ASP   B 2 230 ? 8.93897   17.32650  -19.39350 1.000 39.70763  ? 235  ASP   A OD1  1 
ATOM   4089 O  OD2  . ASP   B 2 230 ? 10.76396  16.50168  -20.28768 1.000 46.74746  ? 235  ASP   A OD2  1 
ATOM   4090 N  N    . ASN   B 2 231 ? 8.29718   18.63247  -16.11745 1.000 40.67248  ? 236  ASN   A N    1 
ATOM   4091 C  CA   . ASN   B 2 231 ? 8.08506   20.04645  -15.83345 1.000 43.37842  ? 236  ASN   A CA   1 
ATOM   4092 C  C    . ASN   B 2 231 ? 7.95484   20.87542  -17.10744 1.000 42.15010  ? 236  ASN   A C    1 
ATOM   4093 O  O    . ASN   B 2 231 ? 8.37071   22.03647  -17.14250 1.000 47.71952  ? 236  ASN   A O    1 
ATOM   4094 C  CB   . ASN   B 2 231 ? 9.21209   20.60158  -14.95757 1.000 46.05654  ? 236  ASN   A CB   1 
ATOM   4095 C  CG   . ASN   B 2 231 ? 9.49431   19.72763  -13.75159 1.000 50.91410  ? 236  ASN   A CG   1 
ATOM   4096 O  OD1  . ASN   B 2 231 ? 8.60443   19.44455  -12.94849 1.000 47.18214  ? 236  ASN   A OD1  1 
ATOM   4097 N  ND2  . ASN   B 2 231 ? 10.73937  19.28276  -13.62572 1.000 47.69184  ? 236  ASN   A ND2  1 
ATOM   4098 N  N    . THR   B 2 232 ? 7.37379   20.30735  -18.16138 1.000 42.99549  ? 237  THR   A N    1 
ATOM   4099 C  CA   . THR   B 2 232 ? 7.38158   20.95833  -19.46238 1.000 41.11892  ? 237  THR   A CA   1 
ATOM   4100 C  C    . THR   B 2 232 ? 6.05252   20.80019  -20.18224 1.000 44.33635  ? 237  THR   A C    1 
ATOM   4101 O  O    . THR   B 2 232 ? 5.45763   19.71212  -20.19617 1.000 40.49109  ? 237  THR   A O    1 
ATOM   4102 C  CB   . THR   B 2 232 ? 8.49655   20.39644  -20.35450 1.000 40.65422  ? 237  THR   A CB   1 
ATOM   4103 O  OG1  . THR   B 2 232 ? 9.74661   20.46158  -19.65763 1.000 46.59235  ? 237  THR   A OG1  1 
ATOM   4104 C  CG2  . THR   B 2 232 ? 8.59933   21.19843  -21.63952 1.000 44.49562  ? 237  THR   A CG2  1 
ATOM   4105 N  N    . LEU   B 2 233 ? 5.58734   21.90713  -20.76021 1.000 37.48813  ? 238  LEU   A N    1 
ATOM   4106 C  CA   A LEU   B 2 233 ? 4.48924   21.91200  -21.71509 0.998 39.87036  ? 238  LEU   A CA   1 
ATOM   4107 C  CA   B LEU   B 2 233 ? 4.48724   21.92500  -21.71509 0.002 39.96092  ? 238  LEU   A CA   1 
ATOM   4108 C  C    . LEU   B 2 233 ? 5.05006   22.23504  -23.09216 1.000 44.35921  ? 238  LEU   A C    1 
ATOM   4109 O  O    . LEU   B 2 233 ? 5.95296   23.06314  -23.22726 1.000 45.00986  ? 238  LEU   A O    1 
ATOM   4110 C  CB   A LEU   B 2 233 ? 3.41418   22.93190  -21.32199 0.998 40.07481  ? 238  LEU   A CB   1 
ATOM   4111 C  CB   B LEU   B 2 233 ? 3.43317   22.97290  -21.34699 0.002 40.05845  ? 238  LEU   A CB   1 
ATOM   4112 C  CG   A LEU   B 2 233 ? 2.41734   22.51981  -20.23388 0.998 41.90753  ? 238  LEU   A CG   1 
ATOM   4113 C  CG   B LEU   B 2 233 ? 2.38232   22.62980  -20.29388 0.002 41.52659  ? 238  LEU   A CG   1 
ATOM   4114 C  CD1  A LEU   B 2 233 ? 1.81828   23.74875  -19.56783 0.998 37.37154  ? 238  LEU   A CD1  1 
ATOM   4115 C  CD1  B LEU   B 2 233 ? 3.05449   22.28989  -18.98995 0.002 40.25536  ? 238  LEU   A CD1  1 
ATOM   4116 C  CD2  A LEU   B 2 233 ? 1.32036   21.65068  -20.82775 0.998 37.02512  ? 238  LEU   A CD2  1 
ATOM   4117 C  CD2  B LEU   B 2 233 ? 1.41622   23.79170  -20.11279 0.002 38.82664  ? 238  LEU   A CD2  1 
ATOM   4118 N  N    . LYS   B 2 234 ? 4.47303   21.60297  -24.09509 1.000 35.90572  ? 239  LYS   A N    1 
ATOM   4119 C  CA   . LYS   B 2 234 ? 5.00387   21.75001  -25.46114 1.000 41.13299  ? 239  LYS   A CA   1 
ATOM   4120 C  C    . LYS   B 2 234 ? 3.86274   21.90088  -26.46503 1.000 41.67526  ? 239  LYS   A C    1 
ATOM   4121 O  O    . LYS   B 2 234 ? 2.92983   21.08778  -26.41892 1.000 40.11938  ? 239  LYS   A O    1 
ATOM   4122 C  CB   . LYS   B 2 234 ? 5.91195   20.57010  -25.80723 1.000 42.08927  ? 239  LYS   A CB   1 
ATOM   4123 C  CG   . LYS   B 2 234 ? 7.34899   20.67725  -25.33838 1.000 47.16506  ? 239  LYS   A CG   1 
ATOM   4124 C  CD   . LYS   B 2 234 ? 8.20106   19.51534  -25.83045 1.000 48.22973  ? 239  LYS   A CD   1 
ATOM   4125 C  CE   . LYS   B 2 234 ? 8.53228   18.55039  -24.74448 1.000 53.77334  ? 239  LYS   A CE   1 
ATOM   4126 N  NZ   . LYS   B 2 234 ? 9.92731   18.11653  -24.82762 1.000 66.40260  ? 239  LYS   A NZ   1 
ATOM   4127 N  N    . LEU   B 2 235 ? 3.92555   22.94687  -27.27805 1.000 35.12626  ? 240  LEU   A N    1 
ATOM   4128 C  CA   . LEU   B 2 235 ? 2.99041   23.15476  -28.37195 1.000 37.55178  ? 240  LEU   A CA   1 
ATOM   4129 C  C    . LEU   B 2 235 ? 3.62833   22.61181  -29.64401 1.000 38.82065  ? 240  LEU   A C    1 
ATOM   4130 O  O    . LEU   B 2 235 ? 4.68624   23.10292  -30.07113 1.000 38.62026  ? 240  LEU   A O    1 
ATOM   4131 C  CB   . LEU   B 2 235 ? 2.65124   24.63672  -28.52493 1.000 34.99271  ? 240  LEU   A CB   1 
ATOM   4132 C  CG   . LEU   B 2 235 ? 1.55710   25.00360  -29.52782 1.000 33.01203  ? 240  LEU   A CG   1 
ATOM   4133 C  CD1  . LEU   B 2 235 ? 0.20320   24.50546  -29.04267 1.000 35.18840  ? 240  LEU   A CD1  1 
ATOM   4134 C  CD2  . LEU   B 2 235 ? 1.53291   26.50759  -29.76884 1.000 40.23047  ? 240  LEU   A CD2  1 
ATOM   4135 N  N    . TRP   B 2 236 ? 2.97438   21.60774  -30.23593 1.000 36.29466  ? 241  TRP   A N    1 
ATOM   4136 C  CA   . TRP   B 2 236 ? 3.47634   20.83777  -31.36697 1.000 37.70914  ? 241  TRP   A CA   1 
ATOM   4137 C  C    . TRP   B 2 236 ? 2.62218   21.07967  -32.60188 1.000 44.80677  ? 241  TRP   A C    1 
ATOM   4138 O  O    . TRP   B 2 236 ? 1.38919   21.12454  -32.51776 1.000 39.61602  ? 241  TRP   A O    1 
ATOM   4139 C  CB   . TRP   B 2 236 ? 3.43553   19.32977  -31.08395 1.000 39.49408  ? 241  TRP   A CB   1 
ATOM   4140 C  CG   . TRP   B 2 236 ? 4.39969   18.81089  -30.08204 1.000 41.98318  ? 241  TRP   A CG   1 
ATOM   4141 C  CD1  . TRP   B 2 236 ? 4.21784   18.72988  -28.73302 1.000 44.43995  ? 241  TRP   A CD1  1 
ATOM   4142 C  CD2  . TRP   B 2 236 ? 5.68272   18.24302  -30.35017 1.000 48.13377  ? 241  TRP   A CD2  1 
ATOM   4143 N  NE1  . TRP   B 2 236 ? 5.32396   18.16601  -28.14013 1.000 43.86501  ? 241  TRP   A NE1  1 
ATOM   4144 C  CE2  . TRP   B 2 236 ? 6.23889   17.86009  -29.11322 1.000 50.99435  ? 241  TRP   A CE2  1 
ATOM   4145 C  CE3  . TRP   B 2 236 ? 6.42461   18.03508  -31.51725 1.000 53.11933  ? 241  TRP   A CE3  1 
ATOM   4146 C  CZ2  . TRP   B 2 236 ? 7.50096   17.27922  -29.01035 1.000 45.85626  ? 241  TRP   A CZ2  1 
ATOM   4147 C  CZ3  . TRP   B 2 236 ? 7.67969   17.45821  -31.41437 1.000 51.42035  ? 241  TRP   A CZ3  1 
ATOM   4148 C  CH2  . TRP   B 2 236 ? 8.20286   17.08828  -30.16842 1.000 47.99440  ? 241  TRP   A CH2  1 
ATOM   4149 N  N    . ASP   B 2 237 ? 3.28605   21.18872  -33.75096 1.000 44.42774  ? 242  ASP   A N    1 
ATOM   4150 C  CA   . ASP   B 2 237 ? 2.64694   20.97864  -35.04789 1.000 52.83408  ? 242  ASP   A CA   1 
ATOM   4151 C  C    . ASP   B 2 237 ? 2.72806   19.48164  -35.32188 1.000 46.16745  ? 242  ASP   A C    1 
ATOM   4152 O  O    . ASP   B 2 237 ? 3.78408   18.96175  -35.69198 1.000 49.53910  ? 242  ASP   A O    1 
ATOM   4153 C  CB   . ASP   B 2 237 ? 3.33474   21.79470  -36.13597 1.000 53.29907  ? 242  ASP   A CB   1 
ATOM   4154 C  CG   . ASP   B 2 237 ? 2.71461   21.59061  -37.51290 1.000 53.89007  ? 242  ASP   A CG   1 
ATOM   4155 O  OD1  . ASP   B 2 237 ? 2.12270   20.51755  -37.76482 1.000 54.08974  ? 242  ASP   A OD1  1 
ATOM   4156 O  OD2  . ASP   B 2 237 ? 2.82643   22.50662  -38.35492 1.000 52.70969  ? 242  ASP   A OD2  1 
ATOM   4157 N  N    . TYR   B 2 238 ? 1.60716   18.77853  -35.13775 1.000 52.39452  ? 243  TYR   A N    1 
ATOM   4158 C  CA   . TYR   B 2 238 ? 1.64630   17.31953  -35.17573 1.000 61.51858  ? 243  TYR   A CA   1 
ATOM   4159 C  C    . TYR   B 2 238 ? 1.80621   16.79653  -36.59874 1.000 59.21458  ? 243  TYR   A C    1 
ATOM   4160 O  O    . TYR   B 2 238 ? 2.47829   15.78360  -36.81780 1.000 62.55335  ? 243  TYR   A O    1 
ATOM   4161 C  CB   . TYR   B 2 238 ? 0.39443   16.73741  -34.51859 1.000 48.98619  ? 243  TYR   A CB   1 
ATOM   4162 C  CG   . TYR   B 2 238 ? -0.89968  17.06927  -35.22746 1.000 53.98642  ? 243  TYR   A CG   1 
ATOM   4163 C  CD1  . TYR   B 2 238 ? -1.40269  16.23820  -36.22140 1.000 50.43612  ? 243  TYR   A CD1  1 
ATOM   4164 C  CD2  . TYR   B 2 238 ? -1.62176  18.20620  -34.89440 1.000 55.73851  ? 243  TYR   A CD2  1 
ATOM   4165 C  CE1  . TYR   B 2 238 ? -2.58679  16.53507  -36.86828 1.000 56.25717  ? 243  TYR   A CE1  1 
ATOM   4166 C  CE2  . TYR   B 2 238 ? -2.80586  18.51206  -35.53528 1.000 53.60284  ? 243  TYR   A CE2  1 
ATOM   4167 C  CZ   . TYR   B 2 238 ? -3.28288  17.67600  -36.52122 1.000 57.95336  ? 243  TYR   A CZ   1 
ATOM   4168 O  OH   . TYR   B 2 238 ? -4.46397  17.98587  -37.15510 1.000 69.00183  ? 243  TYR   A OH   1 
ATOM   4169 N  N    . SER   B 2 239 ? 1.19304   17.46645  -37.57769 1.000 57.48144  ? 244  SER   A N    1 
ATOM   4170 C  CA   . SER   B 2 239 ? 1.35493   17.04545  -38.96670 1.000 63.21784  ? 244  SER   A CA   1 
ATOM   4171 C  C    . SER   B 2 239 ? 2.82690   16.98560  -39.35085 1.000 63.73277  ? 244  SER   A C    1 
ATOM   4172 O  O    . SER   B 2 239 ? 3.26993   16.03464  -40.00689 1.000 70.73909  ? 244  SER   A O    1 
ATOM   4173 C  CB   . SER   B 2 239 ? 0.60074   17.99336  -39.89763 1.000 62.24307  ? 244  SER   A CB   1 
ATOM   4174 O  OG   . SER   B 2 239 ? -0.80023  17.90022  -39.70148 1.000 76.79196  ? 244  SER   A OG   1 
ATOM   4175 N  N    . LYS   B 2 240 ? 3.58784   17.97669  -38.89195 1.000 61.03844  ? 245  LYS   A N    1 
ATOM   4176 C  CA   . LYS   B 2 240 ? 5.01980   18.06483  -39.25210 1.000 58.36183  ? 245  LYS   A CA   1 
ATOM   4177 C  C    . LYS   B 2 240 ? 5.90197   17.49894  -38.12818 1.000 61.13201  ? 245  LYS   A C    1 
ATOM   4178 O  O    . LYS   B 2 240 ? 7.10497   17.31406  -38.37331 1.000 63.78734  ? 245  LYS   A O    1 
ATOM   4179 C  CB   . LYS   B 2 240 ? 5.29861   19.53786  -39.54415 1.000 56.68614  ? 245  LYS   A CB   1 
ATOM   4180 C  CG   . LYS   B 2 240 ? 4.58943   20.05377  -40.78408 1.000 66.23121  ? 245  LYS   A CG   1 
ATOM   4181 C  CD   . LYS   B 2 240 ? 4.84324   21.52779  -41.06512 1.000 70.02639  ? 245  LYS   A CD   1 
ATOM   4182 C  CE   . LYS   B 2 240 ? 4.14706   21.98570  -42.30506 1.000 73.80393  ? 245  LYS   A CE   1 
ATOM   4183 N  NZ   . LYS   B 2 240 ? 4.37389   23.40872  -42.56410 1.000 85.80235  ? 245  LYS   A NZ   1 
ATOM   4184 N  N    . GLY   B 2 241 ? 5.32813   17.22289  -36.95912 1.000 60.15791  ? 246  GLY   A N    1 
ATOM   4185 C  CA   . GLY   B 2 241 ? 6.10430   16.67799  -35.86420 1.000 48.74446  ? 246  GLY   A CA   1 
ATOM   4186 C  C    . GLY   B 2 241 ? 7.13226   17.61710  -35.28432 1.000 53.15638  ? 246  GLY   A C    1 
ATOM   4187 O  O    . GLY   B 2 241 ? 8.10837   17.15921  -34.68641 1.000 56.39591  ? 246  GLY   A O    1 
ATOM   4188 N  N    . LYS   B 2 242 ? 6.94411   18.92408  -35.43831 1.000 54.44369  ? 247  LYS   A N    1 
ATOM   4189 C  CA   . LYS   B 2 242 ? 7.87006   19.91919  -34.91642 1.000 48.98136  ? 247  LYS   A CA   1 
ATOM   4190 C  C    . LYS   B 2 242 ? 7.31313   20.53014  -33.63937 1.000 49.58528  ? 247  LYS   A C    1 
ATOM   4191 O  O    . LYS   B 2 242 ? 6.12311   20.85602  -33.55825 1.000 42.15025  ? 247  LYS   A O    1 
ATOM   4192 C  CB   . LYS   B 2 242 ? 8.12484   21.02120  -35.94646 1.000 60.21790  ? 247  LYS   A CB   1 
ATOM   4193 C  CG   . LYS   B 2 242 ? 8.60675   20.51123  -37.29351 1.000 66.06033  ? 247  LYS   A CG   1 
ATOM   4194 C  CD   . LYS   B 2 242 ? 9.84985   19.65436  -37.14163 1.000 63.47317  ? 247  LYS   A CD   1 
ATOM   4195 C  CE   . LYS   B 2 242 ? 10.28977  19.08439  -38.47867 1.000 71.90590  ? 247  LYS   A CE   1 
ATOM   4196 N  NZ   . LYS   B 2 242 ? 11.46588  18.18752  -38.33678 1.000 74.57617  ? 247  LYS   A NZ   1 
ATOM   4197 N  N    . CYS   B 2 243 ? 8.17822   20.67625  -32.63747 1.000 44.97347  ? 248  CYS   A N    1 
ATOM   4198 C  CA   . CYS   B 2 243 ? 7.80928   21.36322  -31.40444 1.000 47.77780  ? 248  CYS   A CA   1 
ATOM   4199 C  C    . CYS   B 2 243 ? 7.95410   22.86124  -31.63247 1.000 49.83849  ? 248  CYS   A C    1 
ATOM   4200 O  O    . CYS   B 2 243 ? 9.06703   23.36335  -31.82459 1.000 46.14260  ? 248  CYS   A O    1 
ATOM   4201 C  CB   . CYS   B 2 243 ? 8.67745   20.89733  -30.23952 1.000 44.26495  ? 248  CYS   A CB   1 
ATOM   4202 S  SG   . CYS   B 2 243 ? 8.40651   21.83232  -28.71650 1.000 47.48767  ? 248  CYS   A SG   1 
ATOM   4203 N  N    . LEU   B 2 244 ? 6.83203   23.57612  -31.62236 1.000 47.22055  ? 249  LEU   A N    1 
ATOM   4204 C  CA   . LEU   B 2 244 ? 6.85485   25.00512  -31.90338 1.000 47.08555  ? 249  LEU   A CA   1 
ATOM   4205 C  C    . LEU   B 2 244 ? 7.11489   25.83616  -30.65542 1.000 54.39310  ? 249  LEU   A C    1 
ATOM   4206 O  O    . LEU   B 2 244 ? 7.88779   26.79924  -30.70851 1.000 49.91434  ? 249  LEU   A O    1 
ATOM   4207 C  CB   . LEU   B 2 244 ? 5.53973   25.43397  -32.55525 1.000 47.85359  ? 249  LEU   A CB   1 
ATOM   4208 C  CG   . LEU   B 2 244 ? 5.22867   24.70992  -33.86421 1.000 58.18589  ? 249  LEU   A CG   1 
ATOM   4209 C  CD1  . LEU   B 2 244 ? 3.96555   25.25678  -34.48908 1.000 49.94912  ? 249  LEU   A CD1  1 
ATOM   4210 C  CD2  . LEU   B 2 244 ? 6.40456   24.82203  -34.82833 1.000 57.38430  ? 249  LEU   A CD2  1 
ATOM   4211 N  N    . LYS   B 2 245 ? 6.50005   25.49111  -29.52935 1.000 51.58962  ? 250  LYS   A N    1 
ATOM   4212 C  CA   . LYS   B 2 245 ? 6.67209   26.29015  -28.32138 1.000 43.54087  ? 250  LYS   A CA   1 
ATOM   4213 C  C    . LYS   B 2 245 ? 6.92631   25.39219  -27.12039 1.000 40.87577  ? 250  LYS   A C    1 
ATOM   4214 O  O    . LYS   B 2 245 ? 6.45043   24.25914  -27.06633 1.000 40.85864  ? 250  LYS   A O    1 
ATOM   4215 C  CB   . LYS   B 2 245 ? 5.44802   27.18202  -28.05526 1.000 40.62647  ? 250  LYS   A CB   1 
ATOM   4216 C  CG   . LYS   B 2 245 ? 5.18580   28.22798  -29.13325 1.000 44.05076  ? 250  LYS   A CG   1 
ATOM   4217 C  CD   . LYS   B 2 245 ? 6.23669   29.33009  -29.12737 1.000 47.19889  ? 250  LYS   A CD   1 
ATOM   4218 C  CE   . LYS   B 2 245 ? 6.02446   30.29805  -30.28736 1.000 42.19402  ? 250  LYS   A CE   1 
ATOM   4219 N  NZ   . LYS   B 2 245 ? 7.04335   31.39016  -30.30948 1.000 46.15473  ? 250  LYS   A NZ   1 
ATOM   4220 N  N    . THR   B 2 246 ? 7.67636   25.91828  -26.15148 1.000 45.03179  ? 251  THR   A N    1 
ATOM   4221 C  CA   . THR   B 2 246 ? 7.93556   25.23432  -24.88950 1.000 44.08813  ? 251  THR   A CA   1 
ATOM   4222 C  C    . THR   B 2 246 ? 7.65258   26.18731  -23.73748 1.000 42.31673  ? 251  THR   A C    1 
ATOM   4223 O  O    . THR   B 2 246 ? 8.10246   27.33735  -23.74954 1.000 50.65779  ? 251  THR   A O    1 
ATOM   4224 C  CB   . THR   B 2 246 ? 9.37762   24.71947  -24.80764 1.000 44.53407  ? 251  THR   A CB   1 
ATOM   4225 O  OG1  . THR   B 2 246 ? 9.57563   23.68548  -25.77965 1.000 48.70369  ? 251  THR   A OG1  1 
ATOM   4226 C  CG2  . THR   B 2 246 ? 9.66183   24.16652  -23.42067 1.000 44.81141  ? 251  THR   A CG2  1 
ATOM   4227 N  N    . TYR   B 2 247 ? 6.90674   25.70724  -22.74840 1.000 35.65160  ? 252  TYR   A N    1 
ATOM   4228 C  CA   . TYR   B 2 247 ? 6.53378   26.47922  -21.57237 1.000 37.31162  ? 252  TYR   A CA   1 
ATOM   4229 C  C    . TYR   B 2 247 ? 7.03199   25.75229  -20.33341 1.000 47.75127  ? 252  TYR   A C    1 
ATOM   4230 O  O    . TYR   B 2 247 ? 6.72313   24.56926  -20.13336 1.000 40.36785  ? 252  TYR   A O    1 
ATOM   4231 C  CB   . TYR   B 2 247 ? 5.01677   26.67706  -21.49821 1.000 41.96291  ? 252  TYR   A CB   1 
ATOM   4232 C  CG   . TYR   B 2 247 ? 4.39958   27.13498  -22.80115 1.000 42.73329  ? 252  TYR   A CG   1 
ATOM   4233 C  CD1  . TYR   B 2 247 ? 4.30041   28.48697  -23.10816 1.000 38.35893  ? 252  TYR   A CD1  1 
ATOM   4234 C  CD2  . TYR   B 2 247 ? 3.91858   26.21692  -23.72509 1.000 39.79056  ? 252  TYR   A CD2  1 
ATOM   4235 C  CE1  . TYR   B 2 247 ? 3.74024   28.90989  -24.29810 1.000 40.22420  ? 252  TYR   A CE1  1 
ATOM   4236 C  CE2  . TYR   B 2 247 ? 3.35241   26.62984  -24.91803 1.000 44.89815  ? 252  TYR   A CE2  1 
ATOM   4237 C  CZ   . TYR   B 2 247 ? 3.26724   27.97683  -25.19904 1.000 41.11702  ? 252  TYR   A CZ   1 
ATOM   4238 O  OH   . TYR   B 2 247 ? 2.70507   28.39476  -26.38299 1.000 41.72940  ? 252  TYR   A OH   1 
ATOM   4239 N  N    . THR   B 2 248 ? 7.80300   26.45938  -19.50950 1.000 46.32343  ? 253  THR   A N    1 
ATOM   4240 C  CA   . THR   B 2 248 ? 8.39319   25.89245  -18.30456 1.000 42.94297  ? 253  THR   A CA   1 
ATOM   4241 C  C    . THR   B 2 248 ? 8.26420   26.91446  -17.17955 1.000 45.93587  ? 253  THR   A C    1 
ATOM   4242 O  O    . THR   B 2 248 ? 7.62207   27.96039  -17.32850 1.000 46.94444  ? 253  THR   A O    1 
ATOM   4243 C  CB   . THR   B 2 248 ? 9.85520   25.49660  -18.54670 1.000 46.78527  ? 253  THR   A CB   1 
ATOM   4244 O  OG1  . THR   B 2 248 ? 10.63005  26.66868  -18.83480 1.000 43.86602  ? 253  THR   A OG1  1 
ATOM   4245 C  CG2  . THR   B 2 248 ? 9.95418   24.52760  -19.71570 1.000 44.78512  ? 253  THR   A CG2  1 
ATOM   4246 N  N    . GLY   B 2 249 ? 8.89435   26.61154  -16.04562 1.000 45.24939  ? 254  GLY   A N    1 
ATOM   4247 C  CA   . GLY   B 2 249 ? 8.81539   27.42254  -14.85062 1.000 36.59677  ? 254  GLY   A CA   1 
ATOM   4248 C  C    . GLY   B 2 249 ? 7.96257   26.81347  -13.75952 1.000 43.73174  ? 254  GLY   A C    1 
ATOM   4249 O  O    . GLY   B 2 249 ? 8.15166   27.14750  -12.58155 1.000 42.82210  ? 254  GLY   A O    1 
ATOM   4250 N  N    . HIS   B 2 250 ? 7.03663   25.92737  -14.11641 1.000 39.94728  ? 255  HIS   A N    1 
ATOM   4251 C  CA   . HIS   B 2 250 ? 6.17180   25.27529  -13.15031 1.000 37.24334  ? 255  HIS   A CA   1 
ATOM   4252 C  C    . HIS   B 2 250 ? 6.77798   23.94136  -12.70936 1.000 34.48558  ? 255  HIS   A C    1 
ATOM   4253 O  O    . HIS   B 2 250 ? 7.88698   23.56847  -13.09947 1.000 38.62322  ? 255  HIS   A O    1 
ATOM   4254 C  CB   . HIS   B 2 250 ? 4.77675   25.08414  -13.74016 1.000 38.58196  ? 255  HIS   A CB   1 
ATOM   4255 C  CG   . HIS   B 2 250 ? 4.73973   24.15412  -14.91215 1.000 39.92701  ? 255  HIS   A CG   1 
ATOM   4256 N  ND1  . HIS   B 2 250 ? 5.59160   24.28019  -15.98924 1.000 39.96303  ? 255  HIS   A ND1  1 
ATOM   4257 C  CD2  . HIS   B 2 250 ? 3.95181   23.08503  -15.18105 1.000 41.66229  ? 255  HIS   A CD2  1 
ATOM   4258 C  CE1  . HIS   B 2 250 ? 5.33461   23.32615  -16.86620 1.000 37.86395  ? 255  HIS   A CE1  1 
ATOM   4259 N  NE2  . HIS   B 2 250 ? 4.34473   22.58606  -16.39909 1.000 38.93794  ? 255  HIS   A NE2  1 
ATOM   4260 N  N    . LYS   B 2 251 ? 6.06115   23.25529  -11.81828 1.000 42.21843  ? 256  LYS   A N    1 
ATOM   4261 C  CA   . LYS   B 2 251 ? 6.52234   21.93535  -11.32131 1.000 44.85714  ? 256  LYS   A CA   1 
ATOM   4262 C  C    . LYS   B 2 251 ? 5.50041   20.85724  -11.69019 1.000 37.41509  ? 256  LYS   A C    1 
ATOM   4263 O  O    . LYS   B 2 251 ? 4.35145   20.95112  -11.24207 1.000 41.66532  ? 256  LYS   A O    1 
ATOM   4264 C  CB   . LYS   B 2 251 ? 6.75250   21.88039  -9.80833  1.000 44.83555  ? 256  LYS   A CB   1 
ATOM   4265 C  CG   . LYS   B 2 251 ? 7.45568   20.61147  -9.35139  1.000 50.97065  ? 256  LYS   A CG   1 
ATOM   4266 C  CD   . LYS   B 2 251 ? 7.68285   20.52851  -7.84741  1.000 62.54248  ? 256  LYS   A CD   1 
ATOM   4267 C  CE   . LYS   B 2 251 ? 7.36305   19.18049  -7.29036  1.000 66.54328  ? 256  LYS   A CE   1 
ATOM   4268 N  NZ   . LYS   B 2 251 ? 7.08120   19.23548  -5.85333  1.000 64.51615  ? 256  LYS   A NZ   1 
ATOM   4269 N  N    . ASN   B 2 252 ? 5.93443   19.87327  -12.46322 1.000 40.21088  ? 257  ASN   A N    1 
ATOM   4270 C  CA   . ASN   B 2 252 ? 5.04650   18.79217  -12.90011 1.000 41.76187  ? 257  ASN   A CA   1 
ATOM   4271 C  C    . ASN   B 2 252 ? 5.90060   17.55626  -13.18719 1.000 40.52613  ? 257  ASN   A C    1 
ATOM   4272 O  O    . ASN   B 2 252 ? 6.40750   17.37730  -14.29824 1.000 39.50344  ? 257  ASN   A O    1 
ATOM   4273 C  CB   . ASN   B 2 252 ? 4.22333   19.20107  -14.11403 1.000 43.28055  ? 257  ASN   A CB   1 
ATOM   4274 C  CG   . ASN   B 2 252 ? 3.17740   18.17096  -14.47891 1.000 44.41552  ? 257  ASN   A CG   1 
ATOM   4275 O  OD1  . ASN   B 2 252 ? 2.81557   17.32193  -13.66486 1.000 43.96559  ? 257  ASN   A OD1  1 
ATOM   4276 N  ND2  . ASN   B 2 252 ? 2.67726   18.24189  -15.70785 1.000 38.55412  ? 257  ASN   A ND2  1 
ATOM   4277 N  N    . GLU   B 2 253 ? 6.04879   16.70529  -12.17219 1.000 42.50159  ? 258  GLU   A N    1 
ATOM   4278 C  CA   . GLU   B 2 253 ? 6.78191   15.45536  -12.29725 1.000 45.06520  ? 258  GLU   A CA   1 
ATOM   4279 C  C    . GLU   B 2 253 ? 5.97208   14.22928  -11.90915 1.000 34.13760  ? 258  GLU   A C    1 
ATOM   4280 O  O    . GLU   B 2 253 ? 6.40817   13.11033  -12.20018 1.000 42.68875  ? 258  GLU   A O    1 
ATOM   4281 C  CB   . GLU   B 2 253 ? 8.05200   15.47851  -11.43039 1.000 45.55897  ? 258  GLU   A CB   1 
ATOM   4282 C  CG   . GLU   B 2 253 ? 9.25886   16.12962  -12.07852 1.000 49.67101  ? 258  GLU   A CG   1 
ATOM   4283 C  CD   . GLU   B 2 253 ? 10.41395  16.29376  -11.10564 1.000 65.70459  ? 258  GLU   A CD   1 
ATOM   4284 O  OE1  . GLU   B 2 253 ? 10.25811  15.90376  -9.92962  1.000 61.39127  ? 258  GLU   A OE1  1 
ATOM   4285 O  OE2  . GLU   B 2 253 ? 11.46685  16.83386  -11.51176 1.000 62.26892  ? 258  GLU   A OE2  1 
ATOM   4286 N  N    . LYS   B 2 254 ? 4.82113   14.39617  -11.26703 1.000 36.99317  ? 259  LYS   A N    1 
ATOM   4287 C  CA   . LYS   B 2 254 ? 4.15731   13.26311  -10.63995 1.000 42.73201  ? 259  LYS   A CA   1 
ATOM   4288 C  C    . LYS   B 2 254 ? 2.72228   13.10095  -11.12079 1.000 40.32550  ? 259  LYS   A C    1 
ATOM   4289 O  O    . LYS   B 2 254 ? 2.30536   11.99491  -11.48073 1.000 48.33498  ? 259  LYS   A O    1 
ATOM   4290 C  CB   . LYS   B 2 254 ? 4.19446   13.42313  -9.11895  1.000 41.87614  ? 259  LYS   A CB   1 
ATOM   4291 C  CG   . LYS   B 2 254 ? 3.56866   12.28408  -8.34387  1.000 46.25710  ? 259  LYS   A CG   1 
ATOM   4292 C  CD   . LYS   B 2 254 ? 3.73979   12.51612  -6.84889  1.000 53.33040  ? 259  LYS   A CD   1 
ATOM   4293 C  CE   . LYS   B 2 254 ? 3.02399   11.45505  -6.02980  1.000 51.23074  ? 259  LYS   A CE   1 
ATOM   4294 N  NZ   . LYS   B 2 254 ? 3.18212   11.70809  -4.57182  1.000 55.31705  ? 259  LYS   A NZ   1 
ATOM   4295 N  N    . TYR   B 2 255 ? 1.96217   14.19088  -11.13573 1.000 38.77041  ? 260  TYR   A N    1 
ATOM   4296 C  CA   . TYR   B 2 255 ? 0.54214   14.13572  -11.44058 1.000 37.52684  ? 260  TYR   A CA   1 
ATOM   4297 C  C    . TYR   B 2 255 ? 0.27894   14.56868  -12.87455 1.000 38.85201  ? 260  TYR   A C    1 
ATOM   4298 O  O    . TYR   B 2 255 ? 1.04080   15.33675  -13.46764 1.000 40.75683  ? 260  TYR   A O    1 
ATOM   4299 C  CB   . TYR   B 2 255 ? -0.24885  15.00965  -10.47150 1.000 39.41101  ? 260  TYR   A CB   1 
ATOM   4300 C  CG   . TYR   B 2 255 ? -0.16565  14.51268  -9.04951  1.000 43.26527  ? 260  TYR   A CG   1 
ATOM   4301 C  CD1  . TYR   B 2 255 ? -1.03150  13.53060  -8.59240  1.000 43.32702  ? 260  TYR   A CD1  1 
ATOM   4302 C  CD2  . TYR   B 2 255 ? 0.79239   15.00679  -8.17561  1.000 37.17218  ? 260  TYR   A CD2  1 
ATOM   4303 C  CE1  . TYR   B 2 255 ? -0.95531  13.06462  -7.29540  1.000 47.49591  ? 260  TYR   A CE1  1 
ATOM   4304 C  CE2  . TYR   B 2 255 ? 0.87558   14.54582  -6.87862  1.000 43.26444  ? 260  TYR   A CE2  1 
ATOM   4305 C  CZ   . TYR   B 2 255 ? -0.00128  13.57473  -6.44251  1.000 51.01629  ? 260  TYR   A CZ   1 
ATOM   4306 O  OH   . TYR   B 2 255 ? 0.08091   13.11676  -5.14951  1.000 45.10510  ? 260  TYR   A OH   1 
ATOM   4307 N  N    . CYS   B 2 256 ? -0.81506  14.05756  -13.42843 1.000 36.66125  ? 261  CYS   A N    1 
ATOM   4308 C  CA   . CYS   B 2 256 ? -1.23124  14.39149  -14.78639 1.000 37.74187  ? 261  CYS   A CA   1 
ATOM   4309 C  C    . CYS   B 2 256 ? -2.09036  15.64141  -14.70532 1.000 36.33530  ? 261  CYS   A C    1 
ATOM   4310 O  O    . CYS   B 2 256 ? -3.30534  15.58428  -14.50419 1.000 32.26352  ? 261  CYS   A O    1 
ATOM   4311 C  CB   . CYS   B 2 256 ? -1.96019  13.21841  -15.42230 1.000 37.66599  ? 261  CYS   A CB   1 
ATOM   4312 S  SG   . CYS   B 2 256 ? -0.86207  11.82252  -15.72340 1.000 34.99978  ? 261  CYS   A SG   1 
ATOM   4313 N  N    . ILE   B 2 257 ? -1.44350  16.78947  -14.86440 1.000 41.12267  ? 262  ILE   A N    1 
ATOM   4314 C  CA   . ILE   B 2 257 ? -2.07561  18.08641  -14.67035 1.000 35.90309  ? 262  ILE   A CA   1 
ATOM   4315 C  C    . ILE   B 2 257 ? -2.69180  18.54533  -15.98529 1.000 28.96237  ? 262  ILE   A C    1 
ATOM   4316 O  O    . ILE   B 2 257 ? -2.03491  18.52438  -17.03536 1.000 35.16906  ? 262  ILE   A O    1 
ATOM   4317 C  CB   . ILE   B 2 257 ? -1.06166  19.11052  -14.13847 1.000 40.08363  ? 262  ILE   A CB   1 
ATOM   4318 C  CG1  . ILE   B 2 257 ? -0.50647  18.64560  -12.78652 1.000 39.89238  ? 262  ILE   A CG1  1 
ATOM   4319 C  CG2  . ILE   B 2 257 ? -1.69480  20.48746  -14.02442 1.000 39.13576  ? 262  ILE   A CG2  1 
ATOM   4320 C  CD1  . ILE   B 2 257 ? 0.63749   19.49072  -12.26265 1.000 33.65353  ? 262  ILE   A CD1  1 
ATOM   4321 N  N    . PHE   B 2 258 ? -3.95584  18.95820  -15.92616 1.000 33.73661  ? 263  PHE   A N    1 
ATOM   4322 C  CA   . PHE   B 2 258 ? -4.66001  19.45811  -17.09810 1.000 35.35324  ? 263  PHE   A CA   1 
ATOM   4323 C  C    . PHE   B 2 258 ? -4.13220  20.83816  -17.48717 1.000 42.79716  ? 263  PHE   A C    1 
ATOM   4324 O  O    . PHE   B 2 258 ? -3.66119  21.60522  -16.64423 1.000 43.90947  ? 263  PHE   A O    1 
ATOM   4325 C  CB   . PHE   B 2 258 ? -6.15999  19.52795  -16.80394 1.000 37.14543  ? 263  PHE   A CB   1 
ATOM   4326 C  CG   . PHE   B 2 258 ? -7.03708  19.22285  -17.98784 1.000 40.38522  ? 263  PHE   A CG   1 
ATOM   4327 C  CD1  . PHE   B 2 258 ? -7.38898  17.91581  -18.28979 1.000 38.83929  ? 263  PHE   A CD1  1 
ATOM   4328 C  CD2  . PHE   B 2 258 ? -7.53327  20.24479  -18.78080 1.000 37.99446  ? 263  PHE   A CD2  1 
ATOM   4329 C  CE1  . PHE   B 2 258 ? -8.20706  17.63271  -19.37070 1.000 41.62378  ? 263  PHE   A CE1  1 
ATOM   4330 C  CE2  . PHE   B 2 258 ? -8.35336  19.96869  -19.86071 1.000 45.06386  ? 263  PHE   A CE2  1 
ATOM   4331 C  CZ   . PHE   B 2 258 ? -8.69025  18.65965  -20.15666 1.000 37.27048  ? 263  PHE   A CZ   1 
ATOM   4332 N  N    . ALA   B 2 259 ? -4.21337  21.14813  -18.78016 1.000 40.47000  ? 264  ALA   A N    1 
ATOM   4333 C  CA   . ALA   B 2 259 ? -3.76656  22.43817  -19.29623 1.000 37.86403  ? 264  ALA   A CA   1 
ATOM   4334 C  C    . ALA   B 2 259 ? -4.80172  22.97505  -20.27813 1.000 41.07112  ? 264  ALA   A C    1 
ATOM   4335 O  O    . ALA   B 2 259 ? -5.58770  22.22096  -20.85503 1.000 37.58793  ? 264  ALA   A O    1 
ATOM   4336 C  CB   . ALA   B 2 259 ? -2.39262  22.33331  -19.96937 1.000 36.28248  ? 264  ALA   A CB   1 
ATOM   4337 N  N    . ASN   B 2 260 ? -4.78687  24.29605  -20.47114 1.000 40.40051  ? 265  ASN   A N    1 
ATOM   4338 C  CA   . ASN   B 2 260 ? -5.82503  24.96493  -21.24304 1.000 38.49127  ? 265  ASN   A CA   1 
ATOM   4339 C  C    . ASN   B 2 260 ? -5.23923  26.06198  -22.12112 1.000 39.69213  ? 265  ASN   A C    1 
ATOM   4340 O  O    . ASN   B 2 260 ? -4.21226  26.66709  -21.79624 1.000 38.02302  ? 265  ASN   A O    1 
ATOM   4341 C  CB   . ASN   B 2 260 ? -6.89500  25.59583  -20.33894 1.000 40.16087  ? 265  ASN   A CB   1 
ATOM   4342 C  CG   . ASN   B 2 260 ? -7.19478  24.76282  -19.11590 1.000 44.54481  ? 265  ASN   A CG   1 
ATOM   4343 O  OD1  . ASN   B 2 260 ? -6.67469  25.02188  -18.03096 1.000 51.82632  ? 265  ASN   A OD1  1 
ATOM   4344 N  ND2  . ASN   B 2 260 ? -8.04269  23.75873  -19.28079 1.000 41.49531  ? 265  ASN   A ND2  1 
ATOM   4345 N  N    . PHE   B 2 261 ? -5.92438  26.30390  -23.23805 1.000 37.13388  ? 266  PHE   A N    1 
ATOM   4346 C  CA   . PHE   B 2 261 ? -5.75559  27.50990  -24.03808 1.000 39.85939  ? 266  PHE   A CA   1 
ATOM   4347 C  C    . PHE   B 2 261 ? -6.75664  28.55581  -23.55599 1.000 44.49391  ? 266  PHE   A C    1 
ATOM   4348 O  O    . PHE   B 2 261 ? -7.96963  28.33368  -23.62686 1.000 39.34121  ? 266  PHE   A O    1 
ATOM   4349 C  CB   . PHE   B 2 261 ? -5.99271  27.22686  -25.52006 1.000 38.22150  ? 266  PHE   A CB   1 
ATOM   4350 C  CG   . PHE   B 2 261 ? -4.93669  26.37996  -26.17016 1.000 39.09192  ? 266  PHE   A CG   1 
ATOM   4351 C  CD1  . PHE   B 2 261 ? -5.03055  24.99795  -26.15413 1.000 43.89996  ? 266  PHE   A CD1  1 
ATOM   4352 C  CD2  . PHE   B 2 261 ? -3.86882  26.97006  -26.83228 1.000 37.65310  ? 266  PHE   A CD2  1 
ATOM   4353 C  CE1  . PHE   B 2 261 ? -4.06853  24.21404  -26.76822 1.000 37.67289  ? 266  PHE   A CE1  1 
ATOM   4354 C  CE2  . PHE   B 2 261 ? -2.90381  26.19016  -27.44937 1.000 36.72492  ? 266  PHE   A CE2  1 
ATOM   4355 C  CZ   . PHE   B 2 261 ? -3.00266  24.81015  -27.41534 1.000 34.16595  ? 266  PHE   A CZ   1 
ATOM   4356 N  N    . SER   B 2 262 ? -6.25871  29.69086  -23.07106 1.000 38.47768  ? 267  SER   A N    1 
ATOM   4357 C  CA   . SER   B 2 262 ? -7.09979  30.81478  -22.68398 1.000 41.58637  ? 267  SER   A CA   1 
ATOM   4358 C  C    . SER   B 2 262 ? -7.16101  31.79276  -23.85199 1.000 39.07881  ? 267  SER   A C    1 
ATOM   4359 O  O    . SER   B 2 262 ? -6.12111  32.26086  -24.32911 1.000 43.14204  ? 267  SER   A O    1 
ATOM   4360 C  CB   . SER   B 2 262 ? -6.55873  31.50185  -21.43005 1.000 39.37411  ? 267  SER   A CB   1 
ATOM   4361 O  OG   . SER   B 2 262 ? -7.32481  32.64578  -21.10398 1.000 43.16246  ? 267  SER   A OG   1 
ATOM   4362 N  N    . VAL   B 2 263 ? -8.37809  32.09763  -24.30987 1.000 44.63663  ? 268  VAL   A N    1 
ATOM   4363 C  CA   . VAL   B 2 263 ? -8.58030  32.86059  -25.53686 1.000 46.49459  ? 268  VAL   A CA   1 
ATOM   4364 C  C    . VAL   B 2 263 ? -9.52141  34.04049  -25.36577 1.000 47.51924  ? 268  VAL   A C    1 
ATOM   4365 O  O    . VAL   B 2 263 ? -9.72759  34.79146  -26.32276 1.000 43.70793  ? 268  VAL   A O    1 
ATOM   4366 C  CB   . VAL   B 2 263 ? -9.08133  31.94852  -26.67579 1.000 46.69127  ? 268  VAL   A CB   1 
ATOM   4367 C  CG1  . VAL   B 2 263 ? -8.07424  30.84162  -26.95588 1.000 39.81488  ? 268  VAL   A CG1  1 
ATOM   4368 C  CG2  . VAL   B 2 263 ? -10.44223 31.36338  -26.32364 1.000 38.59142  ? 268  VAL   A CG2  1 
ATOM   4369 N  N    . THR   B 2 264 ? -10.10230 34.24745  -24.18171 1.000 42.50917  ? 269  THR   A N    1 
ATOM   4370 C  CA   . THR   B 2 264 ? -11.12640 35.27634  -24.02962 1.000 47.32754  ? 269  THR   A CA   1 
ATOM   4371 C  C    . THR   B 2 264 ? -10.55752 36.66941  -23.79170 1.000 46.93023  ? 269  THR   A C    1 
ATOM   4372 O  O    . THR   B 2 264 ? -11.22365 37.65833  -24.11464 1.000 46.04996  ? 269  THR   A O    1 
ATOM   4373 C  CB   . THR   B 2 264 ? -12.07724 34.91726  -22.88051 1.000 49.32857  ? 269  THR   A CB   1 
ATOM   4374 O  OG1  . THR   B 2 264 ? -11.32709 34.73335  -21.67059 1.000 39.61772  ? 269  THR   A OG1  1 
ATOM   4375 C  CG2  . THR   B 2 264 ? -12.84214 33.64217  -23.20042 1.000 45.11823  ? 269  THR   A CG2  1 
ATOM   4376 N  N    . GLY   B 2 265 ? -9.35847  36.77654  -23.22682 1.000 44.47041  ? 270  GLY   A N    1 
ATOM   4377 C  CA   . GLY   B 2 265 ? -8.74658  38.07160  -22.99690 1.000 39.35902  ? 270  GLY   A CA   1 
ATOM   4378 C  C    . GLY   B 2 265 ? -7.24660  38.03576  -23.20206 1.000 42.07464  ? 270  GLY   A C    1 
ATOM   4379 O  O    . GLY   B 2 265 ? -6.47553  38.30385  -22.27415 1.000 41.33327  ? 270  GLY   A O    1 
ATOM   4380 N  N    . GLY   B 2 266 ? -6.82769  37.71379  -24.41510 1.000 40.86287  ? 271  GLY   A N    1 
ATOM   4381 C  CA   . GLY   B 2 266 ? -5.44169  37.42293  -24.70324 1.000 45.80822  ? 271  GLY   A CA   1 
ATOM   4382 C  C    . GLY   B 2 266 ? -5.20755  35.93095  -24.87725 1.000 40.98734  ? 271  GLY   A C    1 
ATOM   4383 O  O    . GLY   B 2 266 ? -5.99342  35.08787  -24.43916 1.000 46.09133  ? 271  GLY   A O    1 
ATOM   4384 N  N    . LYS   B 2 267 ? -4.10259  35.60506  -25.54136 1.000 39.93925  ? 272  LYS   A N    1 
ATOM   4385 C  CA   . LYS   B 2 267 ? -3.75248  34.22209  -25.87238 1.000 39.00136  ? 272  LYS   A CA   1 
ATOM   4386 C  C    . LYS   B 2 267 ? -2.79631  33.70020  -24.80748 1.000 43.17529  ? 272  LYS   A C    1 
ATOM   4387 O  O    . LYS   B 2 267 ? -1.59235  33.96833  -24.85261 1.000 39.51212  ? 272  LYS   A O    1 
ATOM   4388 C  CB   . LYS   B 2 267 ? -3.13262  34.14314  -27.26345 1.000 40.87738  ? 272  LYS   A CB   1 
ATOM   4389 C  CG   . LYS   B 2 267 ? -4.08768  33.67902  -28.34934 1.000 58.01744  ? 272  LYS   A CG   1 
ATOM   4390 C  CD   . LYS   B 2 267 ? -5.42675  34.39188  -28.26621 1.000 49.10961  ? 272  LYS   A CD   1 
ATOM   4391 C  CE   . LYS   B 2 267 ? -6.34182  33.94677  -29.39811 1.000 53.58092  ? 272  LYS   A CE   1 
ATOM   4392 N  NZ   . LYS   B 2 267 ? -7.74285  34.40763  -29.20596 1.000 56.75307  ? 272  LYS   A NZ   1 
ATOM   4393 N  N    . TRP   B 2 268 ? -3.32713  32.94416  -23.85041 1.000 37.82323  ? 273  TRP   A N    1 
ATOM   4394 C  CA   . TRP   B 2 268 ? -2.52296  32.41826  -22.75749 1.000 42.25181  ? 273  TRP   A CA   1 
ATOM   4395 C  C    . TRP   B 2 268 ? -2.53481  30.89526  -22.76547 1.000 38.40483  ? 273  TRP   A C    1 
ATOM   4396 O  O    . TRP   B 2 268 ? -3.44180  30.25715  -23.30636 1.000 37.32328  ? 273  TRP   A O    1 
ATOM   4397 C  CB   . TRP   B 2 268 ? -3.02487  32.90922  -21.39444 1.000 40.89091  ? 273  TRP   A CB   1 
ATOM   4398 C  CG   . TRP   B 2 268 ? -3.49202  34.33017  -21.38141 1.000 45.59540  ? 273  TRP   A CG   1 
ATOM   4399 C  CD1  . TRP   B 2 268 ? -4.76604  34.77204  -21.16428 1.000 42.08486  ? 273  TRP   A CD1  1 
ATOM   4400 C  CD2  . TRP   B 2 268 ? -2.69316  35.49825  -21.59951 1.000 39.22661  ? 273  TRP   A CD2  1 
ATOM   4401 N  NE1  . TRP   B 2 268 ? -4.80719  36.14204  -21.22830 1.000 48.20714  ? 273  TRP   A NE1  1 
ATOM   4402 C  CE2  . TRP   B 2 268 ? -3.54927  36.61317  -21.49543 1.000 43.76391  ? 273  TRP   A CE2  1 
ATOM   4403 C  CE3  . TRP   B 2 268 ? -1.33721  35.70939  -21.87066 1.000 35.21101  ? 273  TRP   A CE3  1 
ATOM   4404 C  CZ2  . TRP   B 2 268 ? -3.09542  37.92021  -21.65450 1.000 45.13551  ? 273  TRP   A CZ2  1 
ATOM   4405 C  CZ3  . TRP   B 2 268 ? -0.88937  37.00844  -22.02572 1.000 48.31095  ? 273  TRP   A CZ3  1 
ATOM   4406 C  CH2  . TRP   B 2 268 ? -1.76547  38.09735  -21.91864 1.000 45.73530  ? 273  TRP   A CH2  1 
ATOM   4407 N  N    . ILE   B 2 269 ? -1.51268  30.32237  -22.13957 1.000 40.73768  ? 274  ILE   A N    1 
ATOM   4408 C  CA   . ILE   B 2 269 ? -1.50049  28.91438  -21.75455 1.000 37.50203  ? 274  ILE   A CA   1 
ATOM   4409 C  C    . ILE   B 2 269 ? -1.63833  28.86038  -20.24054 1.000 36.82249  ? 274  ILE   A C    1 
ATOM   4410 O  O    . ILE   B 2 269 ? -0.89532  29.54147  -19.52362 1.000 42.39215  ? 274  ILE   A O    1 
ATOM   4411 C  CB   . ILE   B 2 269 ? -0.21947  28.19850  -22.22268 1.000 43.10169  ? 274  ILE   A CB   1 
ATOM   4412 C  CG1  . ILE   B 2 269 ? -0.15762  28.14249  -23.75068 1.000 36.01984  ? 274  ILE   A CG1  1 
ATOM   4413 C  CG2  . ILE   B 2 269 ? -0.14826  26.79752  -21.63467 1.000 37.18652  ? 274  ILE   A CG2  1 
ATOM   4414 C  CD1  . ILE   B 2 269 ? -1.29461  27.38336  -24.38155 1.000 34.88956  ? 274  ILE   A CD1  1 
ATOM   4415 N  N    . VAL   B 2 270 ? -2.59519  28.07229  -19.75442 1.000 33.23176  ? 275  VAL   A N    1 
ATOM   4416 C  CA   . VAL   B 2 270 ? -2.89103  27.99328  -18.32639 1.000 33.96637  ? 275  VAL   A CA   1 
ATOM   4417 C  C    . VAL   B 2 270 ? -2.68583  26.56030  -17.85640 1.000 36.56612  ? 275  VAL   A C    1 
ATOM   4418 O  O    . VAL   B 2 270 ? -3.08981  25.61225  -18.53834 1.000 36.24242  ? 275  VAL   A O    1 
ATOM   4419 C  CB   . VAL   B 2 270 ? -4.32505  28.46913  -18.01725 1.000 33.48905  ? 275  VAL   A CB   1 
ATOM   4420 C  CG1  . VAL   B 2 270 ? -4.64487  28.25012  -16.54621 1.000 33.15054  ? 275  VAL   A CG1  1 
ATOM   4421 C  CG2  . VAL   B 2 270 ? -4.49024  29.93611  -18.39125 1.000 36.51436  ? 275  VAL   A CG2  1 
ATOM   4422 N  N    . SER   B 2 271 ? -2.06570  26.40238  -16.68746 1.000 37.76568  ? 276  SER   A N    1 
ATOM   4423 C  CA   . SER   B 2 271 ? -1.82650  25.06541  -16.16447 1.000 42.04464  ? 276  SER   A CA   1 
ATOM   4424 C  C    . SER   B 2 271 ? -1.74634  25.08944  -14.64548 1.000 44.59633  ? 276  SER   A C    1 
ATOM   4425 O  O    . SER   B 2 271 ? -1.36338  26.09149  -14.04353 1.000 39.90259  ? 276  SER   A O    1 
ATOM   4426 C  CB   . SER   B 2 271 ? -0.53650  24.46554  -16.73260 1.000 42.78736  ? 276  SER   A CB   1 
ATOM   4427 O  OG   . SER   B 2 271 ? -0.23730  23.22958  -16.10661 1.000 43.69995  ? 276  SER   A OG   1 
ATOM   4428 N  N    . GLY   B 2 272 ? -2.11716  23.97041  -14.03142 1.000 41.26679  ? 277  GLY   A N    1 
ATOM   4429 C  CA   . GLY   B 2 272 ? -1.84699  23.76346  -12.62645 1.000 29.86929  ? 277  GLY   A CA   1 
ATOM   4430 C  C    . GLY   B 2 272 ? -0.37894  23.44261  -12.41360 1.000 40.07066  ? 277  GLY   A C    1 
ATOM   4431 O  O    . GLY   B 2 272 ? 0.41198   23.32368  -13.34968 1.000 39.34284  ? 277  GLY   A O    1 
ATOM   4432 N  N    . SER   B 2 273 ? -0.00579  23.30067  -11.14564 1.000 36.98054  ? 278  SER   A N    1 
ATOM   4433 C  CA   . SER   B 2 273 ? 1.38827   23.04782  -10.81178 1.000 37.59552  ? 278  SER   A CA   1 
ATOM   4434 C  C    . SER   B 2 273 ? 1.47249   22.30685  -9.48778  1.000 37.65460  ? 278  SER   A C    1 
ATOM   4435 O  O    . SER   B 2 273 ? 0.58957   22.42476  -8.63269  1.000 41.63996  ? 278  SER   A O    1 
ATOM   4436 C  CB   . SER   B 2 273 ? 2.19215   24.35090  -10.74288 1.000 39.14967  ? 278  SER   A CB   1 
ATOM   4437 O  OG   . SER   B 2 273 ? 3.55420   24.09405  -10.43902 1.000 37.25757  ? 278  SER   A OG   1 
ATOM   4438 N  N    . GLU   B 2 274 ? 2.54759   21.53696  -9.33088  1.000 40.86763  ? 279  GLU   A N    1 
ATOM   4439 C  CA   . GLU   B 2 274 ? 2.78280   20.77900  -8.10990  1.000 43.30079  ? 279  GLU   A CA   1 
ATOM   4440 C  C    . GLU   B 2 274 ? 3.38083   21.62508  -6.99397  1.000 48.63128  ? 279  GLU   A C    1 
ATOM   4441 O  O    . GLU   B 2 274 ? 3.67200   21.08812  -5.92100  1.000 43.58029  ? 279  GLU   A O    1 
ATOM   4442 C  CB   . GLU   B 2 274 ? 3.68289   19.57709  -8.40698  1.000 36.42543  ? 279  GLU   A CB   1 
ATOM   4443 C  CG   . GLU   B 2 274 ? 2.96593   18.46501  -9.16089  1.000 38.85058  ? 279  GLU   A CG   1 
ATOM   4444 C  CD   . GLU   B 2 274 ? 3.90994   17.54609  -9.91397  1.000 40.96559  ? 279  GLU   A CD   1 
ATOM   4445 O  OE1  . GLU   B 2 274 ? 5.13995   17.65923  -9.72211  1.000 41.73093  ? 279  GLU   A OE1  1 
ATOM   4446 O  OE2  . GLU   B 2 274 ? 3.41795   16.71803  -10.70791 1.000 40.00551  ? 279  GLU   A OE2  1 
ATOM   4447 N  N    . ASP   B 2 275 ? 3.57367   22.92809  -7.21701  1.000 43.67755  ? 280  ASP   A N    1 
ATOM   4448 C  CA   . ASP   B 2 275 ? 3.90068   23.85714  -6.14806  1.000 41.27628  ? 280  ASP   A CA   1 
ATOM   4449 C  C    . ASP   B 2 275 ? 2.67665   24.62902  -5.67194  1.000 46.12721  ? 280  ASP   A C    1 
ATOM   4450 O  O    . ASP   B 2 275 ? 2.81762   25.64204  -4.98096  1.000 45.16655  ? 280  ASP   A O    1 
ATOM   4451 C  CB   . ASP   B 2 275 ? 5.01254   24.81625  -6.58518  1.000 42.17604  ? 280  ASP   A CB   1 
ATOM   4452 C  CG   . ASP   B 2 275 ? 4.62632   25.66020  -7.78515  1.000 47.71068  ? 280  ASP   A CG   1 
ATOM   4453 O  OD1  . ASP   B 2 275 ? 3.47928   25.53507  -8.26603  1.000 42.94124  ? 280  ASP   A OD1  1 
ATOM   4454 O  OD2  . ASP   B 2 275 ? 5.47419   26.45028  -8.25125  1.000 44.36734  ? 280  ASP   A OD2  1 
ATOM   4455 N  N    . ASN   B 2 276 ? 1.47866   24.16789  -6.03880  1.000 44.60995  ? 281  ASN   A N    1 
ATOM   4456 C  CA   . ASN   B 2 276 ? 0.19166   24.68576  -5.57767  1.000 41.02596  ? 281  ASN   A CA   1 
ATOM   4457 C  C    . ASN   B 2 276 ? -0.21055  25.98071  -6.26965  1.000 44.69437  ? 281  ASN   A C    1 
ATOM   4458 O  O    . ASN   B 2 276 ? -1.16657  26.63862  -5.82456  1.000 37.24068  ? 281  ASN   A O    1 
ATOM   4459 C  CB   . ASN   B 2 276 ? 0.18579   24.90478  -4.06168  1.000 42.59951  ? 281  ASN   A CB   1 
ATOM   4460 C  CG   . ASN   B 2 276 ? 0.62100   23.66984  -3.29371  1.000 50.25111  ? 281  ASN   A CG   1 
ATOM   4461 O  OD1  . ASN   B 2 276 ? 1.01505   22.66287  -3.88574  1.000 45.18311  ? 281  ASN   A OD1  1 
ATOM   4462 N  ND2  . ASN   B 2 276 ? 0.56213   23.74285  -1.96870  1.000 54.30526  ? 281  ASN   A ND2  1 
ATOM   4463 N  N    . LEU   B 2 277 ? 0.47229   26.37177  -7.33873  1.000 34.98236  ? 282  LEU   A N    1 
ATOM   4464 C  CA   . LEU   B 2 277 ? 0.18309   27.60773  -8.04571  1.000 42.08828  ? 282  LEU   A CA   1 
ATOM   4465 C  C    . LEU   B 2 277 ? -0.46202  27.31564  -9.39264  1.000 44.82422  ? 282  LEU   A C    1 
ATOM   4466 O  O    . LEU   B 2 277 ? -0.29597  26.23565  -9.96764  1.000 42.12220  ? 282  LEU   A O    1 
ATOM   4467 C  CB   . LEU   B 2 277 ? 1.46198   28.42886  -8.25486  1.000 39.21364  ? 282  LEU   A CB   1 
ATOM   4468 C  CG   . LEU   B 2 277 ? 2.25607   28.80896  -7.00595  1.000 45.93410  ? 282  LEU   A CG   1 
ATOM   4469 C  CD1  . LEU   B 2 277 ? 3.52896   29.54809  -7.39209  1.000 43.95614  ? 282  LEU   A CD1  1 
ATOM   4470 C  CD2  . LEU   B 2 277 ? 1.40409   29.64788  -6.07287  1.000 39.21110  ? 282  LEU   A CD2  1 
ATOM   4471 N  N    . VAL   B 2 278 ? -1.20218  28.29956  -9.89657  1.000 43.45875  ? 283  VAL   A N    1 
ATOM   4472 C  CA   . VAL   B 2 278 ? -1.71332  28.26649  -11.26252 1.000 38.51796  ? 283  VAL   A CA   1 
ATOM   4473 C  C    . VAL   B 2 278 ? -0.80050  29.12657  -12.12463 1.000 43.38249  ? 283  VAL   A C    1 
ATOM   4474 O  O    . VAL   B 2 278 ? -0.63459  30.31959  -11.85866 1.000 42.08838  ? 283  VAL   A O    1 
ATOM   4475 C  CB   . VAL   B 2 278 ? -3.16638  28.75934  -11.33437 1.000 40.06907  ? 283  VAL   A CB   1 
ATOM   4476 C  CG1  . VAL   B 2 278 ? -3.63453  28.81327  -12.78032 1.000 40.81364  ? 283  VAL   A CG1  1 
ATOM   4477 C  CG2  . VAL   B 2 278 ? -4.08020  27.86525  -10.50927 1.000 32.34643  ? 283  VAL   A CG2  1 
ATOM   4478 N  N    . TYR   B 2 279 ? -0.20154  28.53462  -13.14968 1.000 36.73983  ? 284  TYR   A N    1 
ATOM   4479 C  CA   . TYR   B 2 279 ? 0.69829   29.24971  -14.03979 1.000 39.76887  ? 284  TYR   A CA   1 
ATOM   4480 C  C    . TYR   B 2 279 ? -0.03589  29.70261  -15.29272 1.000 46.23567  ? 284  TYR   A C    1 
ATOM   4481 O  O    . TYR   B 2 279 ? -0.87987  28.97552  -15.83062 1.000 38.79914  ? 284  TYR   A O    1 
ATOM   4482 C  CB   . TYR   B 2 279 ? 1.89234   28.37283  -14.42090 1.000 38.61903  ? 284  TYR   A CB   1 
ATOM   4483 C  CG   . TYR   B 2 279 ? 2.93146   28.27395  -13.33101 1.000 41.21063  ? 284  TYR   A CG   1 
ATOM   4484 C  CD1  . TYR   B 2 279 ? 2.64866   27.63393  -12.12997 1.000 39.00983  ? 284  TYR   A CD1  1 
ATOM   4485 C  CD2  . TYR   B 2 279 ? 4.19439   28.82608  -13.49815 1.000 39.15528  ? 284  TYR   A CD2  1 
ATOM   4486 C  CE1  . TYR   B 2 279 ? 3.59177   27.54305  -11.12907 1.000 45.11700  ? 284  TYR   A CE1  1 
ATOM   4487 C  CE2  . TYR   B 2 279 ? 5.14650   28.73919  -12.50225 1.000 48.13607  ? 284  TYR   A CE2  1 
ATOM   4488 C  CZ   . TYR   B 2 279 ? 4.84069   28.09817  -11.32021 1.000 49.42680  ? 284  TYR   A CZ   1 
ATOM   4489 O  OH   . TYR   B 2 279 ? 5.78281   28.00928  -10.32731 1.000 47.89661  ? 284  TYR   A OH   1 
ATOM   4490 N  N    . ILE   B 2 280 ? 0.30193   30.90864  -15.75377 1.000 41.95333  ? 285  ILE   A N    1 
ATOM   4491 C  CA   . ILE   B 2 280 ? -0.23126  31.48457  -16.98072 1.000 39.46918  ? 285  ILE   A CA   1 
ATOM   4492 C  C    . ILE   B 2 280 ? 0.93760   32.06068  -17.76685 1.000 45.31529  ? 285  ILE   A C    1 
ATOM   4493 O  O    . ILE   B 2 280 ? 1.59955   32.99976  -17.29693 1.000 45.05970  ? 285  ILE   A O    1 
ATOM   4494 C  CB   . ILE   B 2 280 ? -1.28034  32.57146  -16.71062 1.000 41.04604  ? 285  ILE   A CB   1 
ATOM   4495 C  CG1  . ILE   B 2 280 ? -2.41919  32.03036  -15.84749 1.000 37.28496  ? 285  ILE   A CG1  1 
ATOM   4496 C  CG2  . ILE   B 2 280 ? -1.81554  33.12039  -18.02257 1.000 38.29170  ? 285  ILE   A CG2  1 
ATOM   4497 C  CD1  . ILE   B 2 280 ? -3.45427  33.07325  -15.49940 1.000 45.26797  ? 285  ILE   A CD1  1 
ATOM   4498 N  N    . TRP   B 2 281 ? 1.18253   31.50169  -18.95287 1.000 44.05122  ? 286  TRP   A N    1 
ATOM   4499 C  CA   . TRP   B 2 281 ? 2.21339   31.94579  -19.87798 1.000 35.95088  ? 286  TRP   A CA   1 
ATOM   4500 C  C    . TRP   B 2 281 ? 1.59819   32.68671  -21.05693 1.000 45.54303  ? 286  TRP   A C    1 
ATOM   4501 O  O    . TRP   B 2 281 ? 0.48117   32.38259  -21.49280 1.000 41.11458  ? 286  TRP   A O    1 
ATOM   4502 C  CB   . TRP   B 2 281 ? 3.02045   30.77587  -20.45605 1.000 36.39000  ? 286  TRP   A CB   1 
ATOM   4503 C  CG   . TRP   B 2 281 ? 3.78064   29.92896  -19.49512 1.000 40.83221  ? 286  TRP   A CG   1 
ATOM   4504 C  CD1  . TRP   B 2 281 ? 5.10466   30.02810  -19.18026 1.000 37.78951  ? 286  TRP   A CD1  1 
ATOM   4505 C  CD2  . TRP   B 2 281 ? 3.27983   28.80291  -18.76905 1.000 40.51854  ? 286  TRP   A CD2  1 
ATOM   4506 N  NE1  . TRP   B 2 281 ? 5.45386   29.04915  -18.28229 1.000 44.10981  ? 286  TRP   A NE1  1 
ATOM   4507 C  CE2  . TRP   B 2 281 ? 4.34897   28.28204  -18.01216 1.000 44.63533  ? 286  TRP   A CE2  1 
ATOM   4508 C  CE3  . TRP   B 2 281 ? 2.02491   28.18778  -18.67491 1.000 39.68207  ? 286  TRP   A CE3  1 
ATOM   4509 C  CZ2  . TRP   B 2 281 ? 4.20317   27.18003  -17.17413 1.000 40.73049  ? 286  TRP   A CZ2  1 
ATOM   4510 C  CZ3  . TRP   B 2 281 ? 1.88311   27.09278  -17.84188 1.000 40.89521  ? 286  TRP   A CZ3  1 
ATOM   4511 C  CH2  . TRP   B 2 281 ? 2.96624   26.60090  -17.10199 1.000 39.88133  ? 286  TRP   A CH2  1 
ATOM   4512 N  N    . ASN   B 2 282 ? 2.36203   33.63378  -21.59302 1.000 38.51378  ? 287  ASN   A N    1 
ATOM   4513 C  CA   . ASN   B 2 282 ? 2.07284   34.18674  -22.91000 1.000 36.16796  ? 287  ASN   A CA   1 
ATOM   4514 C  C    . ASN   B 2 282 ? 2.30384   33.10275  -23.95701 1.000 34.84978  ? 287  ASN   A C    1 
ATOM   4515 O  O    . ASN   B 2 282 ? 3.43587   32.63786  -24.13712 1.000 40.22683  ? 287  ASN   A O    1 
ATOM   4516 C  CB   . ASN   B 2 282 ? 2.95768   35.40282  -23.17410 1.000 42.08148  ? 287  ASN   A CB   1 
ATOM   4517 C  CG   . ASN   B 2 282 ? 2.73247   36.01378  -24.55109 1.000 42.82987  ? 287  ASN   A CG   1 
ATOM   4518 O  OD1  . ASN   B 2 282 ? 2.71844   35.31077  -25.56208 1.000 39.53265  ? 287  ASN   A OD1  1 
ATOM   4519 N  ND2  . ASN   B 2 282 ? 2.56933   37.33277  -24.59209 1.000 39.52272  ? 287  ASN   A ND2  1 
ATOM   4520 N  N    . LEU   B 2 283 ? 1.24681   32.67563  -24.63489 1.000 32.67725  ? 288  LEU   A N    1 
ATOM   4521 C  CA   . LEU   B 2 283 ? 1.37783   31.56063  -25.60389 1.000 35.50948  ? 288  LEU   A CA   1 
ATOM   4522 C  C    . LEU   B 2 283 ? 2.46369   31.87173  -26.63401 1.000 39.81355  ? 288  LEU   A C    1 
ATOM   4523 O  O    . LEU   B 2 283 ? 3.29675   30.99781  -26.89508 1.000 40.89525  ? 288  LEU   A O    1 
ATOM   4524 C  CB   . LEU   B 2 283 ? 0.03678   31.33248  -26.29074 1.000 37.30467  ? 288  LEU   A CB   1 
ATOM   4525 C  CG   . LEU   B 2 283 ? -0.09819  30.09045  -27.17671 1.000 40.39499  ? 288  LEU   A CG   1 
ATOM   4526 C  CD1  . LEU   B 2 283 ? -1.55315  29.68230  -27.21056 1.000 38.82771  ? 288  LEU   A CD1  1 
ATOM   4527 C  CD2  . LEU   B 2 283 ? 0.39064   30.32049  -28.59177 1.000 37.20017  ? 288  LEU   A CD2  1 
ATOM   4528 N  N    . GLN   B 2 284 ? 2.45450   33.08272  -27.18402 1.000 45.97684  ? 289  GLN   A N    1 
ATOM   4529 C  CA   . GLN   B 2 284 ? 3.37335   33.37880  -28.28012 1.000 37.77717  ? 289  GLN   A CA   1 
ATOM   4530 C  C    . GLN   B 2 284 ? 4.81639   33.47796  -27.79528 1.000 40.63935  ? 289  GLN   A C    1 
ATOM   4531 O  O    . GLN   B 2 284 ? 5.72639   32.92405  -28.42736 1.000 36.04999  ? 289  GLN   A O    1 
ATOM   4532 C  CB   . GLN   B 2 284 ? 2.94715   34.67075  -28.97809 1.000 44.47680  ? 289  GLN   A CB   1 
ATOM   4533 C  CG   . GLN   B 2 284 ? 3.94198   35.17184  -30.01521 1.000 46.31851  ? 289  GLN   A CG   1 
ATOM   4534 C  CD   . GLN   B 2 284 ? 4.08496   34.23084  -31.19821 1.000 56.99290  ? 289  GLN   A CD   1 
ATOM   4535 O  OE1  . GLN   B 2 284 ? 3.09494   33.82573  -31.80910 1.000 53.67783  ? 289  GLN   A OE1  1 
ATOM   4536 N  NE2  . GLN   B 2 284 ? 5.32396   33.87596  -31.52633 1.000 51.64267  ? 289  GLN   A NE2  1 
ATOM   4537 N  N    . THR   B 2 285 ? 5.05044   34.16900  -26.67931 1.000 43.08532  ? 290  THR   A N    1 
ATOM   4538 C  CA   . THR   B 2 285 ? 6.41046   34.43915  -26.23046 1.000 38.79008  ? 290  THR   A CA   1 
ATOM   4539 C  C    . THR   B 2 285 ? 6.93967   33.41821  -25.23550 1.000 44.56329  ? 290  THR   A C    1 
ATOM   4540 O  O    . THR   B 2 285 ? 8.16070   33.32034  -25.06763 1.000 42.27990  ? 290  THR   A O    1 
ATOM   4541 C  CB   . THR   B 2 285 ? 6.49238   35.83116  -25.59948 1.000 46.54283  ? 290  THR   A CB   1 
ATOM   4542 O  OG1  . THR   B 2 285 ? 5.78951   35.83310  -24.35141 1.000 40.47675  ? 290  THR   A OG1  1 
ATOM   4543 C  CG2  . THR   B 2 285 ? 5.87917   36.87209  -26.52743 1.000 38.33133  ? 290  THR   A CG2  1 
ATOM   4544 N  N    . LYS   B 2 286 ? 6.06282   32.67013  -24.56740 1.000 42.57812  ? 291  LYS   A N    1 
ATOM   4545 C  CA   . LYS   B 2 286 ? 6.40303   31.61218  -23.61842 1.000 39.30363  ? 291  LYS   A CA   1 
ATOM   4546 C  C    . LYS   B 2 286 ? 6.80812   32.15524  -22.25047 1.000 47.34294  ? 291  LYS   A C    1 
ATOM   4547 O  O    . LYS   B 2 286 ? 7.16929   31.35729  -21.37750 1.000 48.98907  ? 291  LYS   A O    1 
ATOM   4548 C  CB   . LYS   B 2 286 ? 7.52707   30.70029  -24.13153 1.000 37.53359  ? 291  LYS   A CB   1 
ATOM   4549 C  CG   . LYS   B 2 286 ? 7.24199   30.06724  -25.48349 1.000 38.55694  ? 291  LYS   A CG   1 
ATOM   4550 C  CD   . LYS   B 2 286 ? 8.50000   29.45537  -26.07961 1.000 42.92880  ? 291  LYS   A CD   1 
ATOM   4551 C  CE   . LYS   B 2 286 ? 9.55386   30.52247  -26.35774 1.000 40.88247  ? 291  LYS   A CE   1 
ATOM   4552 N  NZ   . LYS   B 2 286 ? 10.72284  29.96858  -27.09285 1.000 42.16371  ? 291  LYS   A NZ   1 
ATOM   4553 N  N    . GLU   B 2 287 ? 6.64300   33.46022  -22.05147 1.000 44.27407  ? 292  GLU   A N    1 
ATOM   4554 C  CA   . GLU   B 2 287 ? 7.02307   34.09028  -20.76652 1.000 46.81270  ? 292  GLU   A CA   1 
ATOM   4555 C  C    . GLU   B 2 287 ? 5.88920   33.92217  -19.76039 1.000 40.68635  ? 292  GLU   A C    1 
ATOM   4556 O  O    . GLU   B 2 287 ? 4.72214   34.08005  -20.14327 1.000 42.09123  ? 292  GLU   A O    1 
ATOM   4557 C  CB   . GLU   B 2 287 ? 7.26391   35.59530  -20.83956 1.000 46.89070  ? 292  GLU   A CB   1 
ATOM   4558 C  CG   . GLU   B 2 287 ? 8.02473   36.07937  -22.06765 1.000 58.18388  ? 292  GLU   A CG   1 
ATOM   4559 C  CD   . GLU   B 2 287 ? 7.83555   37.57635  -22.25265 1.000 65.48139  ? 292  GLU   A CD   1 
ATOM   4560 O  OE1  . GLU   B 2 287 ? 8.55154   38.33843  -21.57873 1.000 55.05300  ? 292  GLU   A OE1  1 
ATOM   4561 O  OE2  . GLU   B 2 287 ? 6.96543   37.98224  -23.04656 1.000 48.74866  ? 292  GLU   A OE2  1 
ATOM   4562 N  N    . ILE   B 2 288 ? 6.23536   33.63023  -18.51343 1.000 42.70563  ? 293  ILE   A N    1 
ATOM   4563 C  CA   . ILE   B 2 288 ? 5.18147   33.57513  -17.50932 1.000 43.54017  ? 293  ILE   A CA   1 
ATOM   4564 C  C    . ILE   B 2 288 ? 4.58834   34.96507  -17.33227 1.000 44.64552  ? 293  ILE   A C    1 
ATOM   4565 O  O    . ILE   B 2 288 ? 5.31027   35.94215  -17.09936 1.000 49.81130  ? 293  ILE   A O    1 
ATOM   4566 C  CB   . ILE   B 2 288 ? 5.72367   33.02720  -16.18237 1.000 41.45259  ? 293  ILE   A CB   1 
ATOM   4567 C  CG1  . ILE   B 2 288 ? 6.36879   31.65527  -16.38942 1.000 39.63026  ? 293  ILE   A CG1  1 
ATOM   4568 C  CG2  . ILE   B 2 288 ? 4.60978   32.94210  -15.14825 1.000 43.65298  ? 293  ILE   A CG2  1 
ATOM   4569 C  CD1  . ILE   B 2 288 ? 6.97198   31.06935  -15.12747 1.000 34.89243  ? 293  ILE   A CD1  1 
ATOM   4570 N  N    . VAL   B 2 289 ? 3.26832   35.05993  -17.45113 1.000 44.98030  ? 294  VAL   A N    1 
ATOM   4571 C  CA   . VAL   B 2 289 ? 2.57621   36.32286  -17.24908 1.000 46.05480  ? 294  VAL   A CA   1 
ATOM   4572 C  C    . VAL   B 2 289 ? 1.84034   36.37980  -15.92000 1.000 54.55811  ? 294  VAL   A C    1 
ATOM   4573 O  O    . VAL   B 2 289 ? 1.52228   37.48777  -15.45798 1.000 46.59258  ? 294  VAL   A O    1 
ATOM   4574 C  CB   . VAL   B 2 289 ? 1.60706   36.62974  -18.40898 1.000 46.26705  ? 294  VAL   A CB   1 
ATOM   4575 C  CG1  . VAL   B 2 289 ? 2.37790   36.80881  -19.70806 1.000 43.52214  ? 294  VAL   A CG1  1 
ATOM   4576 C  CG2  . VAL   B 2 289 ? 0.56816   35.52663  -18.54085 1.000 43.95799  ? 294  VAL   A CG2  1 
ATOM   4577 N  N    . GLN   B 2 290 ? 1.55053   35.24278  -15.28895 1.000 42.12516  ? 295  GLN   A N    1 
ATOM   4578 C  CA   . GLN   B 2 290 ? 0.96166   35.32573  -13.95989 1.000 37.44299  ? 295  GLN   A CA   1 
ATOM   4579 C  C    . GLN   B 2 290 ? 1.06988   33.98675  -13.24489 1.000 49.33980  ? 295  GLN   A C    1 
ATOM   4580 O  O    . GLN   B 2 290 ? 1.18192   32.92776  -13.86789 1.000 47.62231  ? 295  GLN   A O    1 
ATOM   4581 C  CB   . GLN   B 2 290 ? -0.50039  35.78458  -14.01874 1.000 42.88096  ? 295  GLN   A CB   1 
ATOM   4582 C  CG   . GLN   B 2 290 ? -0.87937  36.72856  -12.88672 1.000 40.17263  ? 295  GLN   A CG   1 
ATOM   4583 C  CD   . GLN   B 2 290 ? -2.35740  37.06040  -12.85857 1.000 46.36809  ? 295  GLN   A CD   1 
ATOM   4584 O  OE1  . GLN   B 2 290 ? -3.07449  36.85531  -13.83749 1.000 46.24890  ? 295  GLN   A OE1  1 
ATOM   4585 N  NE2  . GLN   B 2 290 ? -2.82334  37.57137  -11.72752 1.000 46.00320  ? 295  GLN   A NE2  1 
ATOM   4586 N  N    . LYS   B 2 291 ? 1.03201   34.05877  -11.91588 1.000 46.54421  ? 296  LYS   A N    1 
ATOM   4587 C  CA   . LYS   B 2 291 ? 1.05122   32.88078  -11.05587 1.000 41.89419  ? 296  LYS   A CA   1 
ATOM   4588 C  C    . LYS   B 2 291 ? 0.05332   33.10869  -9.92977  1.000 47.70994  ? 296  LYS   A C    1 
ATOM   4589 O  O    . LYS   B 2 291 ? 0.28932   33.93273  -9.04080  1.000 51.81352  ? 296  LYS   A O    1 
ATOM   4590 C  CB   . LYS   B 2 291 ? 2.45431   32.60893  -10.51502 1.000 43.37851  ? 296  LYS   A CB   1 
ATOM   4591 C  CG   . LYS   B 2 291 ? 3.41725   32.12002  -11.58411 1.000 45.75931  ? 296  LYS   A CG   1 
ATOM   4592 C  CD   . LYS   B 2 291 ? 4.86726   32.35418  -11.20527 1.000 46.05980  ? 296  LYS   A CD   1 
ATOM   4593 C  CE   . LYS   B 2 291 ? 5.26547   31.56623  -9.97330  1.000 53.20685  ? 296  LYS   A CE   1 
ATOM   4594 N  NZ   . LYS   B 2 291 ? 6.72849   31.67339  -9.70945  1.000 53.93940  ? 296  LYS   A NZ   1 
ATOM   4595 N  N    . LEU   B 2 292 ? -1.06361  32.39157  -9.98764  1.000 42.20513  ? 297  LEU   A N    1 
ATOM   4596 C  CA   . LEU   B 2 292 ? -2.13352  32.52247  -9.00753  1.000 38.70755  ? 297  LEU   A CA   1 
ATOM   4597 C  C    . LEU   B 2 292 ? -1.82831  31.67152  -7.78355  1.000 48.06200  ? 297  LEU   A C    1 
ATOM   4598 O  O    . LEU   B 2 292 ? -1.56519  30.46655  -7.89856  1.000 44.43154  ? 297  LEU   A O    1 
ATOM   4599 C  CB   . LEU   B 2 292 ? -3.46855  32.10133  -9.62538  1.000 41.40813  ? 297  LEU   A CB   1 
ATOM   4600 C  CG   . LEU   B 2 292 ? -3.75575  32.66728  -11.01736 1.000 37.32457  ? 297  LEU   A CG   1 
ATOM   4601 C  CD1  . LEU   B 2 292 ? -5.17976  32.35313  -11.44621 1.000 36.05530  ? 297  LEU   A CD1  1 
ATOM   4602 C  CD2  . LEU   B 2 292 ? -3.49491  34.16931  -11.05541 1.000 42.15555  ? 297  LEU   A CD2  1 
ATOM   4603 N  N    . GLN   B 2 293 ? -1.86725  32.30653  -6.61456  1.000 42.44085  ? 298  GLN   A N    1 
ATOM   4604 C  CA   . GLN   B 2 293 ? -1.57605  31.67458  -5.33858  1.000 52.00592  ? 298  GLN   A CA   1 
ATOM   4605 C  C    . GLN   B 2 293 ? -2.84695  31.60746  -4.50144  1.000 47.39471  ? 298  GLN   A C    1 
ATOM   4606 O  O    . GLN   B 2 293 ? -3.69505  32.49837  -4.56337  1.000 45.92676  ? 298  GLN   A O    1 
ATOM   4607 C  CB   . GLN   B 2 293 ? -0.49405  32.45070  -4.58270  1.000 55.21512  ? 298  GLN   A CB   1 
ATOM   4608 C  CG   . GLN   B 2 293 ? 0.22915   31.64679  -3.51877  1.000 59.65291  ? 298  GLN   A CG   1 
ATOM   4609 C  CD   . GLN   B 2 293 ? 0.75917   32.51786  -2.39684  1.000 68.45181  ? 298  GLN   A CD   1 
ATOM   4610 O  OE1  . GLN   B 2 293 ? 1.86011   33.06598  -2.47796  1.000 75.80416  ? 298  GLN   A OE1  1 
ATOM   4611 N  NE2  . GLN   B 2 293 ? -0.03373  32.65779  -1.34175  1.000 70.53015  ? 298  GLN   A NE2  1 
ATOM   4612 N  N    . GLY   B 2 294 ? -2.96776  30.53846  -3.71542  1.000 47.12943  ? 299  GLY   A N    1 
ATOM   4613 C  CA   . GLY   B 2 294 ? -4.13765  30.35834  -2.87529  1.000 43.32879  ? 299  GLY   A CA   1 
ATOM   4614 C  C    . GLY   B 2 294 ? -4.36946  28.92033  -2.46225  1.000 49.13743  ? 299  GLY   A C    1 
ATOM   4615 O  O    . GLY   B 2 294 ? -4.74931  28.65330  -1.31920  1.000 46.82452  ? 299  GLY   A O    1 
ATOM   4616 N  N    . HIS   B 2 295 ? -4.14846  27.98234  -3.37926  1.000 43.73952  ? 300  HIS   A N    1 
ATOM   4617 C  CA   . HIS   B 2 295 ? -4.35228  26.57332  -3.07122  1.000 41.78576  ? 300  HIS   A CA   1 
ATOM   4618 C  C    . HIS   B 2 295 ? -3.28312  26.07244  -2.10433  1.000 46.47637  ? 300  HIS   A C    1 
ATOM   4619 O  O    . HIS   B 2 295 ? -2.14817  26.55656  -2.08945  1.000 54.45802  ? 300  HIS   A O    1 
ATOM   4620 C  CB   . HIS   B 2 295 ? -4.33732  25.73230  -4.35021  1.000 46.22114  ? 300  HIS   A CB   1 
ATOM   4621 C  CG   . HIS   B 2 295 ? -5.58442  25.85216  -5.16908  1.000 36.69009  ? 300  HIS   A CG   1 
ATOM   4622 N  ND1  . HIS   B 2 295 ? -6.80733  25.38304  -4.73295  1.000 39.40402  ? 300  HIS   A ND1  1 
ATOM   4623 C  CD2  . HIS   B 2 295 ? -5.79861  26.37713  -6.39806  1.000 37.62351  ? 300  HIS   A CD2  1 
ATOM   4624 C  CE1  . HIS   B 2 295 ? -7.72045  25.61993  -5.65685  1.000 44.30498  ? 300  HIS   A CE1  1 
ATOM   4625 N  NE2  . HIS   B 2 295 ? -7.13462  26.22098  -6.67792  1.000 36.89451  ? 300  HIS   A NE2  1 
ATOM   4626 N  N    . THR   B 2 296 ? -3.66093  25.08341  -1.29327  1.000 46.32508  ? 301  THR   A N    1 
ATOM   4627 C  CA   . THR   B 2 296 ? -2.77277  24.49252  -0.29936  1.000 42.91446  ? 301  THR   A CA   1 
ATOM   4628 C  C    . THR   B 2 296 ? -2.32666  23.08356  -0.68039  1.000 50.86980  ? 301  THR   A C    1 
ATOM   4629 O  O    . THR   B 2 296 ? -1.90049  22.31562  0.18658   1.000 49.83228  ? 301  THR   A O    1 
ATOM   4630 C  CB   . THR   B 2 296 ? -3.44562  24.47747  1.07271   1.000 44.02173  ? 301  THR   A CB   1 
ATOM   4631 O  OG1  . THR   B 2 296 ? -4.70856  23.80833  0.97285   1.000 44.07107  ? 301  THR   A OG1  1 
ATOM   4632 C  CG2  . THR   B 2 296 ? -3.66372  25.90045  1.57472   1.000 39.12085  ? 301  THR   A CG2  1 
ATOM   4633 N  N    . ASP   B 2 297 ? -2.41876  22.73154  -1.95837  1.000 49.15035  ? 302  ASP   A N    1 
ATOM   4634 C  CA   . ASP   B 2 297 ? -1.94067  21.44058  -2.43841  1.000 50.30554  ? 302  ASP   A CA   1 
ATOM   4635 C  C    . ASP   B 2 297 ? -1.79284  21.53058  -3.95442  1.000 48.41495  ? 302  ASP   A C    1 
ATOM   4636 O  O    . ASP   B 2 297 ? -2.03202  22.57954  -4.55841  1.000 43.06746  ? 302  ASP   A O    1 
ATOM   4637 C  CB   . ASP   B 2 297 ? -2.88051  20.30849  -2.01929  1.000 37.16794  ? 302  ASP   A CB   1 
ATOM   4638 C  CG   . ASP   B 2 297 ? -2.20837  18.94956  -2.05735  1.000 41.00204  ? 302  ASP   A CG   1 
ATOM   4639 O  OD1  . ASP   B 2 297 ? -1.08342  18.85367  -2.58747  1.000 48.48415  ? 302  ASP   A OD1  1 
ATOM   4640 O  OD2  . ASP   B 2 297 ? -2.79722  17.97550  -1.54727  1.000 46.04096  ? 302  ASP   A OD2  1 
ATOM   4641 N  N    . VAL   B 2 298 ? -1.38979  20.41561  -4.56545  1.000 45.81841  ? 303  VAL   A N    1 
ATOM   4642 C  CA   . VAL   B 2 298 ? -1.17994  20.38861  -6.00647  1.000 41.22609  ? 303  VAL   A CA   1 
ATOM   4643 C  C    . VAL   B 2 298 ? -2.43707  20.86247  -6.71635  1.000 37.55158  ? 303  VAL   A C    1 
ATOM   4644 O  O    . VAL   B 2 298 ? -3.55199  20.43836  -6.39323  1.000 41.08810  ? 303  VAL   A O    1 
ATOM   4645 C  CB   . VAL   B 2 298 ? -0.77284  18.97665  -6.46250  1.000 43.86809  ? 303  VAL   A CB   1 
ATOM   4646 C  CG1  . VAL   B 2 298 ? -0.76499  18.88863  -7.98350  1.000 35.29600  ? 303  VAL   A CG1  1 
ATOM   4647 C  CG2  . VAL   B 2 298 ? 0.58826   18.60880  -5.89564  1.000 38.64858  ? 303  VAL   A CG2  1 
ATOM   4648 N  N    . VAL   B 2 299 ? -2.25826  21.75448  -7.68738  1.000 35.61250  ? 304  VAL   A N    1 
ATOM   4649 C  CA   . VAL   B 2 299 ? -3.33940  22.17135  -8.57127  1.000 41.74577  ? 304  VAL   A CA   1 
ATOM   4650 C  C    . VAL   B 2 299 ? -3.29043  21.26434  -9.79326  1.000 41.52232  ? 304  VAL   A C    1 
ATOM   4651 O  O    . VAL   B 2 299 ? -2.42954  21.42042  -10.66336 1.000 36.84227  ? 304  VAL   A O    1 
ATOM   4652 C  CB   . VAL   B 2 299 ? -3.22059  23.64836  -8.96130  1.000 40.50646  ? 304  VAL   A CB   1 
ATOM   4653 C  CG1  . VAL   B 2 299 ? -4.31674  24.01723  -9.95519  1.000 35.01708  ? 304  VAL   A CG1  1 
ATOM   4654 C  CG2  . VAL   B 2 299 ? -3.29855  24.53137  -7.71830  1.000 36.55417  ? 304  VAL   A CG2  1 
ATOM   4655 N  N    . ILE   B 2 300 ? -4.21434  20.30925  -9.85615  1.000 36.55637  ? 305  ILE   A N    1 
ATOM   4656 C  CA   . ILE   B 2 300 ? -4.16034  19.27124  -10.87715 1.000 39.43248  ? 305  ILE   A CA   1 
ATOM   4657 C  C    . ILE   B 2 300 ? -5.05849  19.57013  -12.07106 1.000 35.85638  ? 305  ILE   A C    1 
ATOM   4658 O  O    . ILE   B 2 300 ? -4.89854  18.93113  -13.12106 1.000 35.85459  ? 305  ILE   A O    1 
ATOM   4659 C  CB   . ILE   B 2 300 ? -4.52613  17.89921  -10.27409 1.000 34.32289  ? 305  ILE   A CB   1 
ATOM   4660 C  CG1  . ILE   B 2 300 ? -3.94710  16.76526  -11.12114 1.000 34.79818  ? 305  ILE   A CG1  1 
ATOM   4661 C  CG2  . ILE   B 2 300 ? -6.03710  17.75305  -10.14993 1.000 34.18024  ? 305  ILE   A CG2  1 
ATOM   4662 C  CD1  . ILE   B 2 300 ? -4.02089  15.40826  -10.43711 1.000 34.05150  ? 305  ILE   A CD1  1 
ATOM   4663 N  N    . SER   B 2 301 ? -5.99258  20.51103  -11.94597 1.000 39.89349  ? 306  SER   A N    1 
ATOM   4664 C  CA   . SER   B 2 301 ? -6.93372  20.80292  -13.01687 1.000 37.98975  ? 306  SER   A CA   1 
ATOM   4665 C  C    . SER   B 2 301 ? -7.21989  22.29589  -13.07386 1.000 42.48753  ? 306  SER   A C    1 
ATOM   4666 O  O    . SER   B 2 301 ? -7.40384  22.94489  -12.03885 1.000 37.90278  ? 306  SER   A O    1 
ATOM   4667 C  CB   . SER   B 2 301 ? -8.24462  20.03279  -12.82773 1.000 34.35039  ? 306  SER   A CB   1 
ATOM   4668 O  OG   . SER   B 2 301 ? -9.16176  20.32968  -13.86563 1.000 38.15041  ? 306  SER   A OG   1 
ATOM   4669 N  N    . THR   B 2 302 ? -7.25407  22.82687  -14.29287 1.000 39.20546  ? 307  THR   A N    1 
ATOM   4670 C  CA   . THR   B 2 302 ? -7.69124  24.18882  -14.54884 1.000 43.37835  ? 307  THR   A CA   1 
ATOM   4671 C  C    . THR   B 2 302 ? -8.61936  24.18171  -15.75474 1.000 39.06364  ? 307  THR   A C    1 
ATOM   4672 O  O    . THR   B 2 302 ? -8.57936  23.27970  -16.59473 1.000 35.97677  ? 307  THR   A O    1 
ATOM   4673 C  CB   . THR   B 2 302 ? -6.51636  25.14494  -14.79397 1.000 39.33440  ? 307  THR   A CB   1 
ATOM   4674 O  OG1  . THR   B 2 302 ? -5.64941  24.59502  -15.79506 1.000 41.06984  ? 307  THR   A OG1  1 
ATOM   4675 C  CG2  . THR   B 2 302 ? -5.73025  25.37504  -13.50906 1.000 37.79762  ? 307  THR   A CG2  1 
ATOM   4676 N  N    . ALA   B 2 303 ? -9.46548  25.20562  -15.82266 1.000 35.85132  ? 308  ALA   A N    1 
ATOM   4677 C  CA   . ALA   B 2 303 ? -10.41761 25.37351  -16.90657 1.000 38.60070  ? 308  ALA   A CA   1 
ATOM   4678 C  C    . ALA   B 2 303 ? -10.62179 26.86248  -17.13856 1.000 42.36999  ? 308  ALA   A C    1 
ATOM   4679 O  O    . ALA   B 2 303 ? -10.55778 27.66250  -16.20358 1.000 38.01794  ? 308  ALA   A O    1 
ATOM   4680 C  CB   . ALA   B 2 303 ? -11.75251 24.68237  -16.59842 1.000 34.82767  ? 308  ALA   A CB   1 
ATOM   4681 N  N    . CYS   B 2 304 ? -10.86496 27.22544  -18.39554 1.000 41.74773  ? 309  CYS   A N    1 
ATOM   4682 C  CA   . CYS   B 2 304 ? -11.02415 28.61742  -18.79854 1.000 41.58939  ? 309  CYS   A CA   1 
ATOM   4683 C  C    . CYS   B 2 304 ? -12.44522 28.82227  -19.30140 1.000 43.93262  ? 309  CYS   A C    1 
ATOM   4684 O  O    . CYS   B 2 304 ? -12.89424 28.11021  -20.20434 1.000 42.02536  ? 309  CYS   A O    1 
ATOM   4685 C  CB   . CYS   B 2 304 ? -10.00430 28.99451  -19.87366 1.000 40.62339  ? 309  CYS   A CB   1 
ATOM   4686 S  SG   . CYS   B 2 304 ? -8.28022  28.78070  -19.35483 1.000 40.46741  ? 309  CYS   A SG   1 
ATOM   4687 N  N    . HIS   B 2 305 ? -13.14426 29.79320  -18.72033 1.000 40.18866  ? 310  HIS   A N    1 
ATOM   4688 C  CA   . HIS   B 2 305 ? -14.53033 30.03405  -19.08919 1.000 39.26629  ? 310  HIS   A CA   1 
ATOM   4689 C  C    . HIS   B 2 305 ? -14.63352 30.32202  -20.58618 1.000 42.04679  ? 310  HIS   A C    1 
ATOM   4690 O  O    . HIS   B 2 305 ? -13.72964 30.93611  -21.16629 1.000 31.35009  ? 310  HIS   A O    1 
ATOM   4691 C  CB   . HIS   B 2 305 ? -15.10436 31.20000  -18.28015 1.000 41.64473  ? 310  HIS   A CB   1 
ATOM   4692 C  CG   . HIS   B 2 305 ? -16.59139 31.33284  -18.38199 1.000 38.87649  ? 310  HIS   A CG   1 
ATOM   4693 N  ND1  . HIS   B 2 305 ? -17.20857 31.99177  -19.42293 1.000 42.92739  ? 310  HIS   A ND1  1 
ATOM   4694 C  CD2  . HIS   B 2 305 ? -17.58426 30.89075  -17.57488 1.000 39.57989  ? 310  HIS   A CD2  1 
ATOM   4695 C  CE1  . HIS   B 2 305 ? -18.51854 31.94963  -19.25180 1.000 47.30431  ? 310  HIS   A CE1  1 
ATOM   4696 N  NE2  . HIS   B 2 305 ? -18.77336 31.28462  -18.13776 1.000 39.87249  ? 310  HIS   A NE2  1 
ATOM   4697 N  N    . PRO   B 2 306 ? -15.71354 29.89090  -21.24406 1.000 38.35660  ? 311  PRO   A N    1 
ATOM   4698 C  CA   . PRO   B 2 306 ? -15.78171 30.02987  -22.70806 1.000 38.98421  ? 311  PRO   A CA   1 
ATOM   4699 C  C    . PRO   B 2 306 ? -15.93191 31.46285  -23.19806 1.000 41.72353  ? 311  PRO   A C    1 
ATOM   4700 O  O    . PRO   B 2 306 ? -15.56906 31.73287  -24.35010 1.000 46.07313  ? 311  PRO   A O    1 
ATOM   4701 C  CB   . PRO   B 2 306 ? -16.99966 29.17774  -23.08792 1.000 29.99703  ? 311  PRO   A CB   1 
ATOM   4702 C  CG   . PRO   B 2 306 ? -17.82652 29.11567  -21.85383 1.000 34.32490  ? 311  PRO   A CG   1 
ATOM   4703 C  CD   . PRO   B 2 306 ? -16.85440 29.12879  -20.70693 1.000 35.86585  ? 311  PRO   A CD   1 
ATOM   4704 N  N    . THR   B 2 307 ? -16.44892 32.38781  -22.38902 1.000 43.36957  ? 312  THR   A N    1 
ATOM   4705 C  CA   . THR   B 2 307 ? -16.66012 33.74778  -22.88101 1.000 44.83350  ? 312  THR   A CA   1 
ATOM   4706 C  C    . THR   B 2 307 ? -16.04513 34.79786  -21.96209 1.000 46.85971  ? 312  THR   A C    1 
ATOM   4707 O  O    . THR   B 2 307 ? -15.58729 35.84390  -22.43115 1.000 46.75867  ? 312  THR   A O    1 
ATOM   4708 C  CB   . THR   B 2 307 ? -18.15416 34.03362  -23.06686 1.000 38.45696  ? 312  THR   A CB   1 
ATOM   4709 O  OG1  . THR   B 2 307 ? -18.84501 33.83557  -21.82379 1.000 38.91630  ? 312  THR   A OG1  1 
ATOM   4710 C  CG2  . THR   B 2 307 ? -18.74518 33.11755  -24.12679 1.000 38.25714  ? 312  THR   A CG2  1 
ATOM   4711 N  N    . GLU   B 2 308 ? -16.03096 34.53687  -20.66009 1.000 41.64231  ? 313  GLU   A N    1 
ATOM   4712 C  CA   . GLU   B 2 308 ? -15.49396 35.48294  -19.69416 1.000 38.71450  ? 313  GLU   A CA   1 
ATOM   4713 C  C    . GLU   B 2 308 ? -14.07988 35.09010  -19.27630 1.000 45.59613  ? 313  GLU   A C    1 
ATOM   4714 O  O    . GLU   B 2 308 ? -13.64877 33.94814  -19.44533 1.000 41.32357  ? 313  GLU   A O    1 
ATOM   4715 C  CB   . GLU   B 2 308 ? -16.39884 35.57286  -18.46307 1.000 43.14191  ? 313  GLU   A CB   1 
ATOM   4716 C  CG   . GLU   B 2 308 ? -17.81892 36.01071  -18.78292 1.000 49.15037  ? 313  GLU   A CG   1 
ATOM   4717 C  CD   . GLU   B 2 308 ? -17.86214 37.34070  -19.50993 1.000 49.26983  ? 313  GLU   A CD   1 
ATOM   4718 O  OE1  . GLU   B 2 308 ? -17.36818 38.34276  -18.94900 1.000 46.20038  ? 313  GLU   A OE1  1 
ATOM   4719 O  OE2  . GLU   B 2 308 ? -18.37726 37.38063  -20.64788 1.000 64.09639  ? 313  GLU   A OE2  1 
ATOM   4720 N  N    . ASN   B 2 309 ? -13.35792 36.06718  -18.72639 1.000 34.83437  ? 314  ASN   A N    1 
ATOM   4721 C  CA   . ASN   B 2 309 ? -11.99285 35.85333  -18.24053 1.000 35.16756  ? 314  ASN   A CA   1 
ATOM   4722 C  C    . ASN   B 2 309 ? -12.04863 35.21834  -16.84852 1.000 45.11971  ? 314  ASN   A C    1 
ATOM   4723 O  O    . ASN   B 2 309 ? -11.70559 35.82339  -15.83156 1.000 43.34204  ? 314  ASN   A O    1 
ATOM   4724 C  CB   . ASN   B 2 309 ? -11.21898 37.16441  -18.21763 1.000 37.41314  ? 314  ASN   A CB   1 
ATOM   4725 C  CG   . ASN   B 2 309 ? -11.00519 37.74841  -19.60166 1.000 45.46908  ? 314  ASN   A CG   1 
ATOM   4726 O  OD1  . ASN   B 2 309 ? -11.17522 37.06438  -20.61064 1.000 42.71523  ? 314  ASN   A OD1  1 
ATOM   4727 N  ND2  . ASN   B 2 309 ? -10.61933 39.01945  -19.65372 1.000 43.34841  ? 314  ASN   A ND2  1 
ATOM   4728 N  N    . ILE   B 2 310 ? -12.49150 33.96329  -16.82046 1.000 41.09281  ? 315  ILE   A N    1 
ATOM   4729 C  CA   . ILE   B 2 310 ? -12.65929 33.22429  -15.57543 1.000 37.94367  ? 315  ILE   A CA   1 
ATOM   4730 C  C    . ILE   B 2 310 ? -11.87416 31.92537  -15.66650 1.000 43.78040  ? 315  ILE   A C    1 
ATOM   4731 O  O    . ILE   B 2 310 ? -11.99719 31.18735  -16.65147 1.000 37.88908  ? 315  ILE   A O    1 
ATOM   4732 C  CB   . ILE   B 2 310 ? -14.14123 32.93314  -15.27027 1.000 44.55462  ? 315  ILE   A CB   1 
ATOM   4733 C  CG1  . ILE   B 2 310 ? -14.95536 34.22606  -15.28220 1.000 43.28845  ? 315  ILE   A CG1  1 
ATOM   4734 C  CG2  . ILE   B 2 310 ? -14.27901 32.23414  -13.92625 1.000 43.58822  ? 315  ILE   A CG2  1 
ATOM   4735 C  CD1  . ILE   B 2 310 ? -16.43432 34.01690  -15.04904 1.000 39.55393  ? 315  ILE   A CD1  1 
ATOM   4736 N  N    . ILE   B 2 311 ? -11.07703 31.64647  -14.63858 1.000 38.80616  ? 316  ILE   A N    1 
ATOM   4737 C  CA   . ILE   B 2 311 ? -10.30589 30.41155  -14.53564 1.000 42.62676  ? 316  ILE   A CA   1 
ATOM   4738 C  C    . ILE   B 2 311 ? -10.76368 29.65652  -13.29658 1.000 40.12993  ? 316  ILE   A C    1 
ATOM   4739 O  O    . ILE   B 2 311 ? -10.74862 30.20153  -12.18759 1.000 46.25415  ? 316  ILE   A O    1 
ATOM   4740 C  CB   . ILE   B 2 311 ? -8.79291  30.68271  -14.46480 1.000 38.95393  ? 316  ILE   A CB   1 
ATOM   4741 C  CG1  . ILE   B 2 311 ? -8.29411  31.28774  -15.77687 1.000 36.81020  ? 316  ILE   A CG1  1 
ATOM   4742 C  CG2  . ILE   B 2 311 ? -8.04474  29.39779  -14.14187 1.000 36.78808  ? 316  ILE   A CG2  1 
ATOM   4743 C  CD1  . ILE   B 2 311 ? -6.80814  31.57790  -15.77803 1.000 43.70115  ? 316  ILE   A CD1  1 
ATOM   4744 N  N    . ALA   B 2 312 ? -11.16257 28.40647  -13.48453 1.000 39.74307  ? 317  ALA   A N    1 
ATOM   4745 C  CA   . ALA   B 2 312 ? -11.46936 27.51046  -12.37948 1.000 39.20156  ? 317  ALA   A CA   1 
ATOM   4746 C  C    . ALA   B 2 312 ? -10.27524 26.59858  -12.14560 1.000 39.02591  ? 317  ALA   A C    1 
ATOM   4747 O  O    . ALA   B 2 312 ? -9.72428  26.03763  -13.09765 1.000 38.23770  ? 317  ALA   A O    1 
ATOM   4748 C  CB   . ALA   B 2 312 ? -12.72030 26.67732  -12.67234 1.000 36.40017  ? 317  ALA   A CB   1 
ATOM   4749 N  N    . SER   B 2 313 ? -9.86109  26.46964  -10.88864 1.000 41.89581  ? 318  SER   A N    1 
ATOM   4750 C  CA   . SER   B 2 313 ? -8.76496  25.58076  -10.53074 1.000 44.33464  ? 318  SER   A CA   1 
ATOM   4751 C  C    . SER   B 2 313 ? -9.21374  24.63373  -9.42668  1.000 42.42907  ? 318  SER   A C    1 
ATOM   4752 O  O    . SER   B 2 313 ? -10.05569 24.98765  -8.59160  1.000 41.78664  ? 318  SER   A O    1 
ATOM   4753 C  CB   . SER   B 2 313 ? -7.51500  26.36490  -10.09188 1.000 35.36044  ? 318  SER   A CB   1 
ATOM   4754 O  OG   . SER   B 2 313 ? -7.83099  27.33888  -9.11286  1.000 39.58925  ? 318  SER   A OG   1 
ATOM   4755 N  N    . ALA   B 2 314 ? -8.64562  23.42979  -9.43673  1.000 39.01994  ? 319  ALA   A N    1 
ATOM   4756 C  CA   . ALA   B 2 314 ? -8.96341  22.39477  -8.46168  1.000 39.62625  ? 319  ALA   A CA   1 
ATOM   4757 C  C    . ALA   B 2 314 ? -7.67729  21.77891  -7.92481  1.000 36.40972  ? 319  ALA   A C    1 
ATOM   4758 O  O    . ALA   B 2 314 ? -6.70935  21.59500  -8.66791  1.000 40.37722  ? 319  ALA   A O    1 
ATOM   4759 C  CB   . ALA   B 2 314 ? -9.85336  21.31267  -9.07457  1.000 30.56464  ? 319  ALA   A CB   1 
ATOM   4760 N  N    . ALA   B 2 315 ? -7.67412  21.45693  -6.62980  1.000 36.82380  ? 320  ALA   A N    1 
ATOM   4761 C  CA   . ALA   B 2 315 ? -6.48100  20.98806  -5.93892  1.000 34.51826  ? 320  ALA   A CA   1 
ATOM   4762 C  C    . ALA   B 2 315 ? -6.76678  19.67604  -5.21588  1.000 38.93405  ? 320  ALA   A C    1 
ATOM   4763 O  O    . ALA   B 2 315 ? -7.91972  19.26192  -5.05775  1.000 39.00233  ? 320  ALA   A O    1 
ATOM   4764 C  CB   . ALA   B 2 315 ? -5.96100  22.04313  -4.94899  1.000 39.34745  ? 320  ALA   A CB   1 
ATOM   4765 N  N    . LEU   B 2 316 ? -5.69667  19.03816  -4.74498  1.000 37.81837  ? 321  LEU   A N    1 
ATOM   4766 C  CA   . LEU   B 2 316 ? -5.76447  17.65816  -4.27296  1.000 44.27963  ? 321  LEU   A CA   1 
ATOM   4767 C  C    . LEU   B 2 316 ? -6.08630  17.53014  -2.78492  1.000 44.99259  ? 321  LEU   A C    1 
ATOM   4768 O  O    . LEU   B 2 316 ? -6.70533  18.42008  -2.19487  1.000 40.28848  ? 321  LEU   A O    1 
ATOM   4769 C  CB   . LEU   B 2 316 ? -4.45243  16.93629  -4.58809  1.000 41.59494  ? 321  LEU   A CB   1 
ATOM   4770 C  CG   . LEU   B 2 316 ? -4.12457  16.78530  -6.07612  1.000 38.35743  ? 321  LEU   A CG   1 
ATOM   4771 C  CD1  . LEU   B 2 316 ? -2.83451  15.99344  -6.27824  1.000 35.37566  ? 321  LEU   A CD1  1 
ATOM   4772 C  CD2  . LEU   B 2 316 ? -5.28158  16.13717  -6.81699  1.000 32.86143  ? 321  LEU   A CD2  1 
ATOM   4773 N  N    . GLU   B 2 317 ? -5.63512  16.42720  -2.17595  1.000 49.92971  ? 322  GLU   A N    1 
ATOM   4774 C  CA   . GLU   B 2 317 ? -6.21694  15.95815  -0.91989  1.000 46.27305  ? 322  GLU   A CA   1 
ATOM   4775 C  C    . GLU   B 2 317 ? -6.09793  16.99118  0.19709   1.000 42.72903  ? 322  GLU   A C    1 
ATOM   4776 O  O    . GLU   B 2 317 ? -7.05087  17.20209  0.95719   1.000 49.52961  ? 322  GLU   A O    1 
ATOM   4777 C  CB   . GLU   B 2 317 ? -5.56076  14.64123  -0.50194  1.000 44.81534  ? 322  GLU   A CB   1 
ATOM   4778 C  CG   . GLU   B 2 317 ? -6.23456  13.95217  0.67314   1.000 45.74566  ? 322  GLU   A CG   1 
ATOM   4779 C  CD   . GLU   B 2 317 ? -7.58654  13.35803  0.31329   1.000 52.23915  ? 322  GLU   A CD   1 
ATOM   4780 O  OE1  . GLU   B 2 317 ? -7.90766  13.28198  -0.89367  1.000 53.77037  ? 322  GLU   A OE1  1 
ATOM   4781 O  OE2  . GLU   B 2 317 ? -8.32940  12.96796  1.23837   1.000 57.56740  ? 322  GLU   A OE2  1 
ATOM   4782 N  N    . ASN   B 2 318 ? -4.93698  17.62930  0.32896   1.000 43.81292  ? 323  ASN   A N    1 
ATOM   4783 C  CA   . ASN   B 2 318 ? -4.76297  18.60333  1.40293   1.000 45.22123  ? 323  ASN   A CA   1 
ATOM   4784 C  C    . ASN   B 2 318 ? -5.50314  19.91025  1.15199   1.000 46.81705  ? 323  ASN   A C    1 
ATOM   4785 O  O    . ASN   B 2 318 ? -5.44714  20.80627  2.00297   1.000 52.51228  ? 323  ASN   A O    1 
ATOM   4786 C  CB   . ASN   B 2 318 ? -3.27498  18.88549  1.62477   1.000 44.82889  ? 323  ASN   A CB   1 
ATOM   4787 C  CG   . ASN   B 2 318 ? -2.52480  17.67058  2.13570   1.000 48.26342  ? 323  ASN   A CG   1 
ATOM   4788 O  OD1  . ASN   B 2 318 ? -3.09064  16.81953  2.82477   1.000 48.53610  ? 323  ASN   A OD1  1 
ATOM   4789 N  ND2  . ASN   B 2 318 ? -1.24382  17.58371  1.79957   1.000 49.48858  ? 323  ASN   A ND2  1 
ATOM   4790 N  N    . ASP   B 2 319 ? -6.19427  20.04417  0.01806   1.000 45.29501  ? 324  ASP   A N    1 
ATOM   4791 C  CA   . ASP   B 2 319 ? -6.92343  21.26709  -0.30988  1.000 39.88615  ? 324  ASP   A CA   1 
ATOM   4792 C  C    . ASP   B 2 319 ? -8.41142  20.97593  -0.45672  1.000 43.18126  ? 324  ASP   A C    1 
ATOM   4793 O  O    . ASP   B 2 319 ? -9.20538  21.45686  0.35536   1.000 41.85452  ? 324  ASP   A O    1 
ATOM   4794 C  CB   . ASP   B 2 319 ? -6.33463  21.89313  -1.57595  1.000 41.90896  ? 324  ASP   A CB   1 
ATOM   4795 C  CG   . ASP   B 2 319 ? -6.97881  23.22006  -1.93490  1.000 39.19529  ? 324  ASP   A CG   1 
ATOM   4796 O  OD1  . ASP   B 2 319 ? -8.22382  23.28093  -2.02277  1.000 43.56479  ? 324  ASP   A OD1  1 
ATOM   4797 O  OD2  . ASP   B 2 319 ? -6.23593  24.20313  -2.12999  1.000 43.85765  ? 324  ASP   A OD2  1 
ATOM   4798 N  N    . LYS   B 2 320 ? -8.81844  20.20987  -1.46667  1.000 39.52372  ? 325  LYS   A N    1 
ATOM   4799 C  CA   . LYS   B 2 320 ? -10.19042 19.75273  -1.66752  1.000 38.18258  ? 325  LYS   A CA   1 
ATOM   4800 C  C    . LYS   B 2 320 ? -11.13058 20.84462  -2.15743  1.000 39.75152  ? 325  LYS   A C    1 
ATOM   4801 O  O    . LYS   B 2 320 ? -12.34357 20.60850  -2.24230  1.000 41.85783  ? 325  LYS   A O    1 
ATOM   4802 C  CB   . LYS   B 2 320 ? -10.77622 19.14068  -0.38945  1.000 49.30105  ? 325  LYS   A CB   1 
ATOM   4803 C  CG   . LYS   B 2 320 ? -9.94204  18.03678  0.24248   1.000 46.21926  ? 325  LYS   A CG   1 
ATOM   4804 C  CD   . LYS   B 2 320 ? -10.72685 17.35371  1.35957   1.000 41.12230  ? 325  LYS   A CD   1 
ATOM   4805 C  CE   . LYS   B 2 320 ? -9.89366  16.31581  2.09650   1.000 47.54256  ? 325  LYS   A CE   1 
ATOM   4806 N  NZ   . LYS   B 2 320 ? -9.28759  16.86789  3.34243   1.000 55.20969  ? 325  LYS   A NZ   1 
ATOM   4807 N  N    . THR   B 2 321 ? -10.62474 22.03067  -2.48450  1.000 42.16765  ? 326  THR   A N    1 
ATOM   4808 C  CA   . THR   B 2 321 ? -11.47890 23.14058  -2.87442  1.000 49.25719  ? 326  THR   A CA   1 
ATOM   4809 C  C    . THR   B 2 321 ? -11.28609 23.49858  -4.34145  1.000 40.36177  ? 326  THR   A C    1 
ATOM   4810 O  O    . THR   B 2 321 ? -10.26612 23.18868  -4.96355  1.000 37.72806  ? 326  THR   A O    1 
ATOM   4811 C  CB   . THR   B 2 321 ? -11.21394 24.37962  -2.01147  1.000 44.32729  ? 326  THR   A CB   1 
ATOM   4812 O  OG1  . THR   B 2 321 ? -9.85300  24.80176  -2.17062  1.000 46.06882  ? 326  THR   A OG1  1 
ATOM   4813 C  CG2  . THR   B 2 321 ? -11.49075 24.08061  -0.54244  1.000 48.78493  ? 326  THR   A CG2  1 
ATOM   4814 N  N    . ILE   B 2 322 ? -12.30322 24.16347  -4.88335  1.000 47.64529  ? 327  ILE   A N    1 
ATOM   4815 C  CA   . ILE   B 2 322 ? -12.26542 24.76145  -6.21136  1.000 46.69794  ? 327  ILE   A CA   1 
ATOM   4816 C  C    . ILE   B 2 322 ? -12.22556 26.27146  -6.03839  1.000 47.60312  ? 327  ILE   A C    1 
ATOM   4817 O  O    . ILE   B 2 322 ? -12.92953 26.82240  -5.18332  1.000 50.50400  ? 327  ILE   A O    1 
ATOM   4818 C  CB   . ILE   B 2 322 ? -13.48446 24.34131  -7.05723  1.000 46.92067  ? 327  ILE   A CB   1 
ATOM   4819 C  CG1  . ILE   B 2 322 ? -13.59931 22.81730  -7.11320  1.000 37.67701  ? 327  ILE   A CG1  1 
ATOM   4820 C  CG2  . ILE   B 2 322 ? -13.39768 24.94231  -8.45825  1.000 43.11598  ? 327  ILE   A CG2  1 
ATOM   4821 C  CD1  . ILE   B 2 322 ? -14.92232 22.33116  -7.65905  1.000 46.30117  ? 327  ILE   A CD1  1 
ATOM   4822 N  N    . LYS   B 2 323 ? -11.40571 26.94153  -6.83848  1.000 41.35127  ? 328  LYS   A N    1 
ATOM   4823 C  CA   . LYS   B 2 323 ? -11.31786 28.39554  -6.79451  1.000 46.81623  ? 328  LYS   A CA   1 
ATOM   4824 C  C    . LYS   B 2 323 ? -11.61507 28.98550  -8.16549  1.000 45.02807  ? 328  LYS   A C    1 
ATOM   4825 O  O    . LYS   B 2 323 ? -11.20012 28.44253  -9.19552  1.000 44.57746  ? 328  LYS   A O    1 
ATOM   4826 C  CB   . LYS   B 2 323 ? -9.93886  28.86869  -6.31266  1.000 47.69248  ? 328  LYS   A CB   1 
ATOM   4827 C  CG   . LYS   B 2 323 ? -9.60567  28.47875  -4.88769  1.000 42.12602  ? 328  LYS   A CG   1 
ATOM   4828 C  CD   . LYS   B 2 323 ? -8.23868  28.99890  -4.48684  1.000 42.54295  ? 328  LYS   A CD   1 
ATOM   4829 C  CE   . LYS   B 2 323 ? -7.87048  28.55195  -3.08087  1.000 43.10889  ? 328  LYS   A CE   1 
ATOM   4830 N  NZ   . LYS   B 2 323 ? -8.84543  29.05386  -2.06778  1.000 46.19040  ? 328  LYS   A NZ   1 
ATOM   4831 N  N    . LEU   B 2 324 ? -12.34718 30.09542  -8.16242  1.000 47.98299  ? 329  LEU   A N    1 
ATOM   4832 C  CA   . LEU   B 2 324 ? -12.64539 30.85737  -9.36440  1.000 42.45833  ? 329  LEU   A CA   1 
ATOM   4833 C  C    . LEU   B 2 324 ? -11.85452 32.15846  -9.32950  1.000 47.97941  ? 329  LEU   A C    1 
ATOM   4834 O  O    . LEU   B 2 324 ? -11.91149 32.90246  -8.34150  1.000 52.56298  ? 329  LEU   A O    1 
ATOM   4835 C  CB   . LEU   B 2 324 ? -14.14443 31.14121  -9.47225  1.000 43.68271  ? 329  LEU   A CB   1 
ATOM   4836 C  CG   . LEU   B 2 324 ? -15.06432 29.92912  -9.63413  1.000 44.27593  ? 329  LEU   A CG   1 
ATOM   4837 C  CD1  . LEU   B 2 324 ? -16.52737 30.35296  -9.64798  1.000 43.14506  ? 329  LEU   A CD1  1 
ATOM   4838 C  CD2  . LEU   B 2 324 ? -14.71637 29.15514  -10.89516 1.000 40.50388  ? 329  LEU   A CD2  1 
ATOM   4839 N  N    . TRP   B 2 325 ? -11.10166 32.41352  -10.39158 1.000 44.72115  ? 330  TRP   A N    1 
ATOM   4840 C  CA   . TRP   B 2 325 ? -10.31980 33.62560  -10.54168 1.000 44.69921  ? 330  TRP   A CA   1 
ATOM   4841 C  C    . TRP   B 2 325 ? -10.87101 34.41753  -11.71563 1.000 48.58595  ? 330  TRP   A C    1 
ATOM   4842 O  O    . TRP   B 2 325 ? -11.22706 33.84348  -12.74959 1.000 44.70810  ? 330  TRP   A O    1 
ATOM   4843 C  CB   . TRP   B 2 325 ? -8.83979  33.31575  -10.77983 1.000 42.76230  ? 330  TRP   A CB   1 
ATOM   4844 C  CG   . TRP   B 2 325 ? -8.29959  32.18182  -9.96488  1.000 40.63785  ? 330  TRP   A CG   1 
ATOM   4845 C  CD1  . TRP   B 2 325 ? -8.53347  30.85179  -10.15883 1.000 42.46962  ? 330  TRP   A CD1  1 
ATOM   4846 C  CD2  . TRP   B 2 325 ? -7.40848  32.27093  -8.84597  1.000 47.58755  ? 330  TRP   A CD2  1 
ATOM   4847 N  NE1  . TRP   B 2 325 ? -7.85830  30.10887  -9.22390  1.000 50.95409  ? 330  TRP   A NE1  1 
ATOM   4848 C  CE2  . TRP   B 2 325 ? -7.15830  30.95596  -8.40698  1.000 49.59036  ? 330  TRP   A CE2  1 
ATOM   4849 C  CE3  . TRP   B 2 325 ? -6.80552  33.33500  -8.16905  1.000 48.20605  ? 330  TRP   A CE3  1 
ATOM   4850 C  CZ2  . TRP   B 2 325 ? -6.32815  30.67606  -7.32006  1.000 48.66979  ? 330  TRP   A CZ2  1 
ATOM   4851 C  CZ3  . TRP   B 2 325 ? -5.98138  33.05510  -7.09013  1.000 45.59082  ? 330  TRP   A CZ3  1 
ATOM   4852 C  CH2  . TRP   B 2 325 ? -5.75020  31.73813  -6.67814  1.000 43.68760  ? 330  TRP   A CH2  1 
ATOM   4853 N  N    . LYS   B 2 326 ? -10.94113 35.73552  -11.54964 1.000 43.39632  ? 331  LYS   A N    1 
ATOM   4854 C  CA   . LYS   B 2 326 ? -11.43933 36.61646  -12.59360 1.000 47.84886  ? 331  LYS   A CA   1 
ATOM   4855 C  C    . LYS   B 2 326 ? -10.41247 37.69556  -12.88272 1.000 43.58030  ? 331  LYS   A C    1 
ATOM   4856 O  O    . LYS   B 2 326 ? -9.74443  38.19064  -11.96980 1.000 47.37124  ? 331  LYS   A O    1 
ATOM   4857 C  CB   . LYS   B 2 326 ? -12.78335 37.24232  -12.20647 1.000 42.19887  ? 331  LYS   A CB   1 
ATOM   4858 C  CG   . LYS   B 2 326 ? -13.91324 36.23120  -12.12734 1.000 55.65163  ? 331  LYS   A CG   1 
ATOM   4859 C  CD   . LYS   B 2 326 ? -15.22226 36.87007  -11.69721 1.000 53.26696  ? 331  LYS   A CD   1 
ATOM   4860 C  CE   . LYS   B 2 326 ? -16.34415 35.84296  -11.67207 1.000 52.04207  ? 331  LYS   A CE   1 
ATOM   4861 N  NZ   . LYS   B 2 326 ? -17.64017 36.43083  -11.23995 1.000 54.48765  ? 331  LYS   A NZ   1 
ATOM   4862 N  N    . SER   B 2 327 ? -10.26864 38.03256  -14.16174 1.000 42.23967  ? 332  SER   A N    1 
ATOM   4863 C  CA   . SER   B 2 327 ? -9.35480  39.07165  -14.61185 1.000 47.57555  ? 332  SER   A CA   1 
ATOM   4864 C  C    . SER   B 2 327 ? -10.16498 40.18156  -15.26378 1.000 52.85213  ? 332  SER   A C    1 
ATOM   4865 O  O    . SER   B 2 327 ? -10.91406 39.92947  -16.21470 1.000 50.18932  ? 332  SER   A O    1 
ATOM   4866 C  CB   . SER   B 2 327 ? -8.32084  38.51274  -15.59496 1.000 50.26439  ? 332  SER   A CB   1 
ATOM   4867 O  OG   . SER   B 2 327 ? -7.44300  39.53083  -16.05506 1.000 49.09215  ? 332  SER   A OG   1 
ATOM   4868 N  N    . ASP   B 2 328 ? -10.02206 41.40358  -14.74981 1.000 59.95133  ? 333  ASP   A N    1 
ATOM   4869 C  CA   . ASP   B 2 328 ? -10.67324 42.55050  -15.36976 1.000 60.05966  ? 333  ASP   A CA   1 
ATOM   4870 C  C    . ASP   B 2 328 ? -9.88642  43.08957  -16.55485 1.000 58.44462  ? 333  ASP   A C    1 
ATOM   4871 O  O    . ASP   B 2 328 ? -10.47858 43.71650  -17.43979 1.000 64.20726  ? 333  ASP   A O    1 
ATOM   4872 C  CB   . ASP   B 2 328 ? -10.89225 43.66149  -14.34175 1.000 58.05424  ? 333  ASP   A CB   1 
ATOM   4873 C  CG   . ASP   B 2 328 ? -11.96611 43.31239  -13.33263 1.000 74.59616  ? 333  ASP   A CG   1 
ATOM   4874 O  OD1  . ASP   B 2 328 ? -12.73003 42.35531  -13.58654 1.000 83.19671  ? 333  ASP   A OD1  1 
ATOM   4875 O  OD2  . ASP   B 2 328 ? -12.04707 43.99740  -12.29063 1.000 94.89609  ? 333  ASP   A OD2  1 
ATOM   4876 N  N    . CYS   B 2 329 ? -8.57840  42.85970  -16.59498 1.000 60.25953  ? 334  CYS   A N    1 
ATOM   4877 C  CA   . CYS   B 2 329 ? -7.78456  43.19577  -17.77007 1.000 59.34152  ? 334  CYS   A CA   1 
ATOM   4878 C  C    . CYS   B 2 329 ? -8.11458  42.22272  -18.90102 1.000 63.25503  ? 334  CYS   A C    1 
ATOM   4879 O  O    . CYS   B 2 329 ? -8.09374  42.57071  -20.08203 1.000 55.26705  ? 334  CYS   A O    1 
ATOM   4880 C  CB   . CYS   B 2 329 ? -6.28653  43.15593  -17.45123 1.000 41.37256  ? 334  CYS   A CB   1 
ATOM   4881 S  SG   . CYS   B 2 329 ? -5.77050  44.28200  -16.13630 1.000 89.60881  ? 334  CYS   A SG   1 
ATOM   4882 O  OXT  . CYS   B 2 329 ? -8.42143  41.05669  -18.64798 1.000 58.65409  ? 334  CYS   A OXT  1 
HETATM 4883 C  C01  . A1AM2 C 3 .   ? -8.38242  15.24376  -15.37975 1.000 38.37363  ? 1401 A1AM2 A C01  1 
HETATM 4884 C  C03  . A1AM2 C 3 .   ? -7.63859  13.37036  -16.26503 1.000 38.15199  ? 1401 A1AM2 A C03  1 
HETATM 4885 C  C04  . A1AM2 C 3 .   ? -6.51767  12.29427  -16.27263 1.000 34.13872  ? 1401 A1AM2 A C04  1 
HETATM 4886 C  C06  . A1AM2 C 3 .   ? -5.21576  10.61876  -14.77101 1.000 33.81220  ? 1401 A1AM2 A C06  1 
HETATM 4887 C  C07  . A1AM2 C 3 .   ? -4.24880  10.51229  -15.76800 1.000 37.84959  ? 1401 A1AM2 A C07  1 
HETATM 4888 C  C08  . A1AM2 C 3 .   ? -3.19987  9.59426   -15.64066 1.000 32.03562  ? 1401 A1AM2 A C08  1 
HETATM 4889 C  C09  . A1AM2 C 3 .   ? -3.11489  8.80870   -14.49535 1.000 38.04625  ? 1401 A1AM2 A C09  1 
HETATM 4890 C  C10  . A1AM2 C 3 .   ? -2.10196  7.86472   -14.26901 1.000 39.73574  ? 1401 A1AM2 A C10  1 
HETATM 4891 C  C11  . A1AM2 C 3 .   ? -1.50105  7.12027   -15.27973 1.000 38.33922  ? 1401 A1AM2 A C11  1 
HETATM 4892 C  C13  . A1AM2 C 3 .   ? -0.51611  6.18832   -14.95239 1.000 41.98791  ? 1401 A1AM2 A C13  1 
HETATM 4893 C  C14  . A1AM2 C 3 .   ? -0.13109  5.98481   -13.63332 1.000 37.09569  ? 1401 A1AM2 A C14  1 
HETATM 4894 C  C15  . A1AM2 C 3 .   ? -0.74300  6.73425   -12.63860 1.000 46.99510  ? 1401 A1AM2 A C15  1 
HETATM 4895 C  C16  . A1AM2 C 3 .   ? -0.37597  6.52881   -11.16353 1.000 37.84960  ? 1401 A1AM2 A C16  1 
HETATM 4896 C  C19  . A1AM2 C 3 .   ? 0.46596   4.97146   -9.34794  1.000 46.99958  ? 1401 A1AM2 A C19  1 
HETATM 4897 C  C20  . A1AM2 C 3 .   ? -0.71308  4.16579   -8.75559  1.000 43.54119  ? 1401 A1AM2 A C20  1 
HETATM 4898 C  C22  . A1AM2 C 3 .   ? -2.23523  2.75346   -9.87998  1.000 47.16499  ? 1401 A1AM2 A C22  1 
HETATM 4899 C  C23  . A1AM2 C 3 .   ? -2.83425  2.02399   -8.66368  1.000 49.49242  ? 1401 A1AM2 A C23  1 
HETATM 4900 C  C25  . A1AM2 C 3 .   ? -1.81831  0.68055   -7.04917  1.000 58.21118  ? 1401 A1AM2 A C25  1 
HETATM 4901 C  C26  . A1AM2 C 3 .   ? -1.16341  -0.69742  -6.84265  1.000 65.00909  ? 1401 A1AM2 A C26  1 
HETATM 4902 C  C28  . A1AM2 C 3 .   ? -1.35060  -2.82880  -7.82980  1.000 70.12452  ? 1401 A1AM2 A C28  1 
HETATM 4903 C  C29  . A1AM2 C 3 .   ? -1.25464  -3.78633  -6.62342  1.000 70.25835  ? 1401 A1AM2 A C29  1 
HETATM 4904 C  C31  . A1AM2 C 3 .   ? -2.54164  -4.44049  -4.77313  1.000 56.34856  ? 1401 A1AM2 A C31  1 
HETATM 4905 C  C32  . A1AM2 C 3 .   ? -1.58173  -5.64452  -4.65268  1.000 51.88657  ? 1401 A1AM2 A C32  1 
HETATM 4906 C  C34  . A1AM2 C 3 .   ? -2.64079  -7.16074  -2.88605  1.000 47.11150  ? 1401 A1AM2 A C34  1 
HETATM 4907 C  C36  . A1AM2 C 3 .   ? -2.59179  -7.68917  -1.43684  1.000 46.47731  ? 1401 A1AM2 A C36  1 
HETATM 4908 C  C37  . A1AM2 C 3 .   ? -3.09388  -8.89203  -1.17835  1.000 34.21612  ? 1401 A1AM2 A C37  1 
HETATM 4909 C  C38  . A1AM2 C 3 .   ? -3.37493  -9.98559  -0.12591  1.000 43.61876  ? 1401 A1AM2 A C38  1 
HETATM 4910 C  C39  . A1AM2 C 3 .   ? -2.42295  -10.52832 0.73828   1.000 38.51039  ? 1401 A1AM2 A C39  1 
HETATM 4911 C  C40  . A1AM2 C 3 .   ? -1.05692  -10.22240 0.79912   1.000 34.15452  ? 1401 A1AM2 A C40  1 
HETATM 4912 C  C41  . A1AM2 C 3 .   ? -0.53883  -9.50002  1.86582   1.000 32.86114  ? 1401 A1AM2 A C41  1 
HETATM 4913 C  C43  . A1AM2 C 3 .   ? 0.81819   -9.21611  1.92167   1.000 37.11769  ? 1401 A1AM2 A C43  1 
HETATM 4914 C  C44  . A1AM2 C 3 .   ? 1.66013   -9.65657  0.90781   1.000 35.68507  ? 1401 A1AM2 A C44  1 
HETATM 4915 C  C46  . A1AM2 C 3 .   ? 1.13704   -10.38495 -0.15388  1.000 30.52661  ? 1401 A1AM2 A C46  1 
HETATM 4916 C  C47  . A1AM2 C 3 .   ? -0.21699  -10.67287 -0.20673  1.000 32.27498  ? 1401 A1AM2 A C47  1 
HETATM 4917 C  C48  . A1AM2 C 3 .   ? -3.10000  -11.45696 1.52367   1.000 38.18566  ? 1401 A1AM2 A C48  1 
HETATM 4918 C  C49  . A1AM2 C 3 .   ? -2.51003  -12.36257 2.62201   1.000 42.07188  ? 1401 A1AM2 A C49  1 
HETATM 4919 C  C52  . A1AM2 C 3 .   ? -2.78613  -14.21490 4.24975   1.000 41.91342  ? 1401 A1AM2 A C52  1 
HETATM 4920 C  C53  . A1AM2 C 3 .   ? -2.66625  -15.60415 3.66430   1.000 34.12886  ? 1401 A1AM2 A C53  1 
HETATM 4921 C  C54  . A1AM2 C 3 .   ? -1.83431  -16.54898 4.24465   1.000 35.74885  ? 1401 A1AM2 A C54  1 
HETATM 4922 C  C55  . A1AM2 C 3 .   ? -1.75543  -17.81521 3.68814   1.000 30.27432  ? 1401 A1AM2 A C55  1 
HETATM 4923 C  C56  . A1AM2 C 3 .   ? -2.50448  -18.11959 2.56329   1.000 31.13425  ? 1401 A1AM2 A C56  1 
HETATM 4924 C  C58  . A1AM2 C 3 .   ? -3.33743  -17.16676 1.99093   1.000 29.18277  ? 1401 A1AM2 A C58  1 
HETATM 4925 C  C60  . A1AM2 C 3 .   ? -3.42031  -15.90753 2.54644   1.000 32.39495  ? 1401 A1AM2 A C60  1 
HETATM 4926 C  C61  . A1AM2 C 3 .   ? -3.74510  -14.30537 5.40881   1.000 39.98363  ? 1401 A1AM2 A C61  1 
HETATM 4927 C  C62  . A1AM2 C 3 .   ? -4.17998  -12.98908 6.05331   1.000 43.13164  ? 1401 A1AM2 A C62  1 
HETATM 4928 C  C65  . A1AM2 C 3 .   ? -4.42401  -11.43702 1.10870   1.000 37.57674  ? 1401 A1AM2 A C65  1 
HETATM 4929 C  C67  . A1AM2 C 3 .   ? -1.73194  7.65721   -12.94994 1.000 40.36232  ? 1401 A1AM2 A C67  1 
HETATM 4930 C  C68  . A1AM2 C 3 .   ? -4.08086  8.92317   -13.50537 1.000 38.54994  ? 1401 A1AM2 A C68  1 
HETATM 4931 C  C69  . A1AM2 C 3 .   ? -5.12379  9.82320   -13.62770 1.000 32.75868  ? 1401 A1AM2 A C69  1 
HETATM 4932 C  C71  . A1AM2 C 3 .   ? -5.83768  10.34322  -11.20888 1.000 33.89951  ? 1401 A1AM2 A C71  1 
HETATM 4933 C  C73  . A1AM2 C 3 .   ? -6.99566  10.21470  -10.20380 1.000 34.34503  ? 1401 A1AM2 A C73  1 
HETATM 4934 C  C74  . A1AM2 C 3 .   ? -7.45055  11.31909  -9.31022  1.000 35.54914  ? 1401 A1AM2 A C74  1 
HETATM 4935 C  C75  . A1AM2 C 3 .   ? -6.75644  12.67803  -9.32878  1.000 34.02652  ? 1401 A1AM2 A C75  1 
HETATM 4936 C  C79  . A1AM2 C 3 .   ? -8.58154  11.08855  -8.36809  1.000 35.47992  ? 1401 A1AM2 A C79  1 
HETATM 4937 C  C80  . A1AM2 C 3 .   ? -9.28064  9.73262   -8.32954  1.000 35.89958  ? 1401 A1AM2 A C80  1 
HETATM 4938 C  C83  . A1AM2 C 3 .   ? -7.70076  8.86378   -10.14324 1.000 34.21347  ? 1401 A1AM2 A C83  1 
HETATM 4939 C  C84  . A1AM2 C 3 .   ? -5.95657  12.86906  -14.14788 1.000 32.93227  ? 1401 A1AM2 A C84  1 
HETATM 4940 C  C85  . A1AM2 C 3 .   ? -7.01148  13.99815  -14.13329 1.000 40.10486  ? 1401 A1AM2 A C85  1 
HETATM 4941 C  C86  . A1AM2 C 3 .   ? -6.29537  15.11643  -13.27776 1.000 34.70299  ? 1401 A1AM2 A C86  1 
HETATM 4942 C  C87  . A1AM2 C 3 .   ? -7.72660  13.85477  -17.76322 1.000 34.45462  ? 1401 A1AM2 A C87  1 
HETATM 4943 F  F12  . A1AM2 C 3 .   ? -1.85207  7.29878   -16.57779 1.000 36.77469  ? 1401 A1AM2 A F12  1 
HETATM 4944 F  F42  . A1AM2 C 3 .   ? -1.35477  -9.06557  2.85867   1.000 40.34328  ? 1401 A1AM2 A F42  1 
HETATM 4945 F  F57  . A1AM2 C 3 .   ? -2.42759  -19.36181 2.02578   1.000 38.43208  ? 1401 A1AM2 A F57  1 
HETATM 4946 F  F76  . A1AM2 C 3 .   ? -6.72744  13.16853  -10.59197 1.000 35.64040  ? 1401 A1AM2 A F76  1 
HETATM 4947 F  F77  . A1AM2 C 3 .   ? -5.49044  12.50411  -8.87575  1.000 37.20079  ? 1401 A1AM2 A F77  1 
HETATM 4948 F  F78  . A1AM2 C 3 .   ? -7.41235  13.53141  -8.50210  1.000 34.80324  ? 1401 A1AM2 A F78  1 
HETATM 4949 N  N02  . A1AM2 C 3 .   ? -7.38348  14.42868  -15.40245 1.000 44.59878  ? 1401 A1AM2 A N02  1 
HETATM 4950 N  N05  . A1AM2 C 3 .   ? -6.25268  11.70376  -14.96941 1.000 35.25050  ? 1401 A1AM2 A N05  1 
HETATM 4951 N  N18  . A1AM2 C 3 .   ? 0.13894   5.22293   -10.75403 1.000 50.22344  ? 1401 A1AM2 A N18  1 
HETATM 4952 N  N33  . A1AM2 C 3 .   ? -1.60973  -6.20298  -3.29346  1.000 56.00610  ? 1401 A1AM2 A N33  1 
HETATM 4953 N  N51  . A1AM2 C 3 .   ? -3.37109  -13.36026 3.24543   1.000 40.29728  ? 1401 A1AM2 A N51  1 
HETATM 4954 N  N64  . A1AM2 C 3 .   ? -5.53995  -12.49705 5.87515   1.000 44.92667  ? 1401 A1AM2 A N64  1 
HETATM 4955 N  N66  . A1AM2 C 3 .   ? -4.54597  -10.54640 0.13335   1.000 43.68469  ? 1401 A1AM2 A N66  1 
HETATM 4956 N  N70  . A1AM2 C 3 .   ? -6.10576  9.83271   -12.54167 1.000 37.73268  ? 1401 A1AM2 A N70  1 
HETATM 4957 N  N82  . A1AM2 C 3 .   ? -8.83375  8.64224   -9.22112  1.000 35.18179  ? 1401 A1AM2 A N82  1 
HETATM 4958 O  O17  . A1AM2 C 3 .   ? -0.53288  7.39813   -10.38287 1.000 47.97045  ? 1401 A1AM2 A O17  1 
HETATM 4959 O  O21  . A1AM2 C 3 .   ? -0.89120  3.04347   -9.58914  1.000 46.23805  ? 1401 A1AM2 A O21  1 
HETATM 4960 O  O24  . A1AM2 C 3 .   ? -2.09933  0.84903   -8.41923  1.000 47.79288  ? 1401 A1AM2 A O24  1 
HETATM 4961 O  O27  . A1AM2 C 3 .   ? -2.02050  -1.66358  -7.40924  1.000 64.73671  ? 1401 A1AM2 A O27  1 
HETATM 4962 O  O30  . A1AM2 C 3 .   ? -2.55164  -4.02603  -6.12229  1.000 61.49405  ? 1401 A1AM2 A O30  1 
HETATM 4963 O  O35  . A1AM2 C 3 .   ? -3.48084  -7.49698  -3.64989  1.000 42.42374  ? 1401 A1AM2 A O35  1 
HETATM 4964 O  O50  . A1AM2 C 3 .   ? -1.38102  -12.29752 2.95695   1.000 39.42857  ? 1401 A1AM2 A O50  1 
HETATM 4965 O  O63  . A1AM2 C 3 .   ? -3.40391  -12.38388 6.70504   1.000 48.69485  ? 1401 A1AM2 A O63  1 
HETATM 4966 O  O72  . A1AM2 C 3 .   ? -4.78663  10.79824  -10.94109 1.000 40.07713  ? 1401 A1AM2 A O72  1 
HETATM 4967 O  O81  . A1AM2 C 3 .   ? -10.17963 9.53998   -7.59443  1.000 38.33760  ? 1401 A1AM2 A O81  1 
HETATM 4968 CL CL45 . A1AM2 C 3 .   ? 3.40716   -9.30069  0.95762   1.000 43.88423  ? 1401 A1AM2 A CL45 1 
HETATM 4969 CL CL59 . A1AM2 C 3 .   ? -4.30950  -17.53825 0.55111   1.000 42.00308  ? 1401 A1AM2 A CL59 1 
HETATM 4970 O  O    . HOH   D 4 .   ? -6.59800  -25.44000 10.65800  1.000 48.77311  ? 1401 HOH   B O    1 
HETATM 4971 O  O    . HOH   D 4 .   ? -23.89000 -6.21000  -0.68200  1.000 48.77146  ? 1402 HOH   B O    1 
HETATM 4972 O  O    . HOH   D 4 .   ? 13.38400  -5.00900  21.96900  1.000 60.52268  ? 1403 HOH   B O    1 
HETATM 4973 O  O    . HOH   D 4 .   ? -27.51200 -15.12400 13.87000  1.000 54.61500  ? 1404 HOH   B O    1 
HETATM 4974 O  O    . HOH   D 4 .   ? -6.94000  -23.39300 12.08200  1.000 57.87079  ? 1405 HOH   B O    1 
HETATM 4975 O  O    . HOH   D 4 .   ? -27.03100 -5.44300  -0.60100  1.000 50.58987  ? 1406 HOH   B O    1 
HETATM 4976 O  O    . HOH   D 4 .   ? -0.59700  -9.07100  14.47300  1.000 43.42033  ? 1407 HOH   B O    1 
HETATM 4977 O  O    . HOH   D 4 .   ? -20.35100 -30.57700 2.50000   1.000 47.23971  ? 1408 HOH   B O    1 
HETATM 4978 O  O    . HOH   D 4 .   ? -6.91200  -7.33200  21.03600  1.000 47.71186  ? 1409 HOH   B O    1 
HETATM 4979 O  O    . HOH   D 4 .   ? -21.93300 -5.94600  -9.06000  1.000 51.85462  ? 1410 HOH   B O    1 
HETATM 4980 O  O    . HOH   D 4 .   ? 10.18600  -18.03300 -7.67800  1.000 49.57041  ? 1411 HOH   B O    1 
HETATM 4981 O  O    . HOH   D 4 .   ? -0.20500  -20.40500 15.88600  1.000 58.14627  ? 1412 HOH   B O    1 
HETATM 4982 O  O    . HOH   D 4 .   ? -2.57100  -2.40900  0.36900   1.000 36.71368  ? 1413 HOH   B O    1 
HETATM 4983 O  O    . HOH   D 4 .   ? -25.09900 -11.46200 -5.67700  1.000 46.37146  ? 1414 HOH   B O    1 
HETATM 4984 O  O    . HOH   D 4 .   ? -18.77400 -3.77100  -2.15800  1.000 41.50058  ? 1415 HOH   B O    1 
HETATM 4985 O  O    . HOH   D 4 .   ? 5.54400   -12.93200 11.94800  1.000 43.41650  ? 1416 HOH   B O    1 
HETATM 4986 O  O    . HOH   D 4 .   ? 7.25800   -17.64000 1.70400   1.000 44.49200  ? 1417 HOH   B O    1 
HETATM 4987 O  O    . HOH   D 4 .   ? 10.28300  -2.86200  -0.85100  1.000 49.08618  ? 1418 HOH   B O    1 
HETATM 4988 O  O    . HOH   D 4 .   ? -10.51100 6.58400   0.63500   1.000 47.59381  ? 1419 HOH   B O    1 
HETATM 4989 O  O    . HOH   D 4 .   ? 7.00000   -10.43900 2.16000   1.000 37.14603  ? 1420 HOH   B O    1 
HETATM 4990 O  O    . HOH   D 4 .   ? -2.38500  -7.62900  9.57700   1.000 49.96332  ? 1421 HOH   B O    1 
HETATM 4991 O  O    . HOH   D 4 .   ? 5.66200   -22.11800 -3.81000  1.000 43.53963  ? 1422 HOH   B O    1 
HETATM 4992 O  O    . HOH   D 4 .   ? -25.14500 -13.37600 -0.09500  1.000 42.29966  ? 1423 HOH   B O    1 
HETATM 4993 O  O    . HOH   D 4 .   ? -20.04900 -2.16000  15.91500  1.000 72.82605  ? 1424 HOH   B O    1 
HETATM 4994 O  O    . HOH   D 4 .   ? 14.48800  -17.75600 -0.95500  1.000 35.71223  ? 1425 HOH   B O    1 
HETATM 4995 O  O    . HOH   D 4 .   ? -7.28300  -10.04200 5.05600   1.000 39.57202  ? 1426 HOH   B O    1 
HETATM 4996 O  O    . HOH   D 4 .   ? 17.31500  -23.18600 1.69700   1.000 36.28440  ? 1427 HOH   B O    1 
HETATM 4997 O  O    . HOH   D 4 .   ? -6.81500  -9.36700  -0.98200  1.000 34.69352  ? 1428 HOH   B O    1 
HETATM 4998 O  O    . HOH   D 4 .   ? 15.00400  -2.20500  4.49100   1.000 45.58792  ? 1429 HOH   B O    1 
HETATM 4999 O  O    . HOH   D 4 .   ? 3.20700   -8.08800  13.67800  1.000 40.38969  ? 1430 HOH   B O    1 
HETATM 5000 O  O    . HOH   D 4 .   ? 9.25900   -9.50400  6.91300   1.000 48.66726  ? 1431 HOH   B O    1 
HETATM 5001 O  O    . HOH   D 4 .   ? 3.48400   -10.74900 7.54900   1.000 43.81564  ? 1432 HOH   B O    1 
HETATM 5002 O  O    . HOH   D 4 .   ? 15.26300  -14.40100 0.73500   1.000 34.78328  ? 1433 HOH   B O    1 
HETATM 5003 O  O    . HOH   D 4 .   ? -5.09500  -9.62300  15.83900  1.000 44.55946  ? 1434 HOH   B O    1 
HETATM 5004 O  O    . HOH   D 4 .   ? -0.57800  -15.42900 -16.48400 1.000 56.83263  ? 1435 HOH   B O    1 
HETATM 5005 O  O    . HOH   D 4 .   ? 14.37000  -20.47200 -2.99500  1.000 51.30228  ? 1436 HOH   B O    1 
HETATM 5006 O  O    . HOH   D 4 .   ? -3.85500  -11.82200 13.06300  1.000 52.59326  ? 1437 HOH   B O    1 
HETATM 5007 O  O    . HOH   D 4 .   ? 6.72600   -3.06400  -1.53100  1.000 50.98525  ? 1438 HOH   B O    1 
HETATM 5008 O  O    . HOH   D 4 .   ? 15.26400  -16.59200 2.45400   1.000 36.54436  ? 1439 HOH   B O    1 
HETATM 5009 O  O    . HOH   D 4 .   ? 9.87700   -16.96100 15.82900  1.000 47.13255  ? 1440 HOH   B O    1 
HETATM 5010 O  O    . HOH   D 4 .   ? 23.002    -16.678   4.597     1.000 49.89952  ? 1441 HOH   B O    1 
HETATM 5011 O  O    . HOH   D 4 .   ? 16.48600  -12.08100 4.17900   1.000 39.62845  ? 1442 HOH   B O    1 
HETATM 5012 O  O    . HOH   D 4 .   ? 16.80900  -15.01200 4.10100   1.000 43.75532  ? 1443 HOH   B O    1 
HETATM 5013 O  O    . HOH   D 4 .   ? 13.97000  -7.30500  -4.57100  1.000 41.49402  ? 1444 HOH   B O    1 
HETATM 5014 O  O    . HOH   D 4 .   ? 15.96900  -20.53300 18.38700  1.000 57.91207  ? 1445 HOH   B O    1 
HETATM 5015 O  O    . HOH   D 4 .   ? -5.71500  -11.16200 8.57000   1.000 46.68322  ? 1446 HOH   B O    1 
HETATM 5016 O  O    . HOH   D 4 .   ? 15.09200  -3.33400  7.72200   1.000 43.85923  ? 1447 HOH   B O    1 
HETATM 5017 O  O    . HOH   D 4 .   ? 3.50800   -4.08200  8.37900   1.000 39.60040  ? 1448 HOH   B O    1 
HETATM 5018 O  O    . HOH   D 4 .   ? -9.86800  -17.49300 -10.98800 1.000 36.30566  ? 1449 HOH   B O    1 
HETATM 5019 O  O    . HOH   D 4 .   ? -10.05300 -10.41400 -11.18200 1.000 52.61602  ? 1450 HOH   B O    1 
HETATM 5020 O  O    . HOH   D 4 .   ? -1.59000  -20.18900 -5.15500  1.000 38.99513  ? 1451 HOH   B O    1 
HETATM 5021 O  O    . HOH   D 4 .   ? 6.05600   -13.83900 -6.57800  1.000 43.70756  ? 1452 HOH   B O    1 
HETATM 5022 O  O    . HOH   D 4 .   ? -17.273   -25.776   -1.841    1.000 51.90983  ? 1453 HOH   B O    1 
HETATM 5023 O  O    . HOH   D 4 .   ? -24.28800 -23.78400 4.37800   1.000 52.27303  ? 1454 HOH   B O    1 
HETATM 5024 O  O    . HOH   D 4 .   ? 16.83700  -1.69000  6.11100   1.000 50.24429  ? 1455 HOH   B O    1 
HETATM 5025 O  O    . HOH   D 4 .   ? 6.12400   -10.58400 6.38000   1.000 47.90554  ? 1456 HOH   B O    1 
HETATM 5026 O  O    . HOH   D 4 .   ? -17.31900 -21.04700 -7.38900  1.000 46.73208  ? 1457 HOH   B O    1 
HETATM 5027 O  O    . HOH   D 4 .   ? 3.22500   -14.79500 5.19200   1.000 37.63490  ? 1458 HOH   B O    1 
HETATM 5028 O  O    . HOH   D 4 .   ? -4.01600  13.81000  -3.30500  1.000 47.82502  ? 1459 HOH   B O    1 
HETATM 5029 O  O    . HOH   D 4 .   ? -11.86900 -6.87900  16.30400  1.000 51.58084  ? 1460 HOH   B O    1 
HETATM 5030 O  O    . HOH   D 4 .   ? -11.21900 -1.85600  -7.48600  1.000 42.64236  ? 1461 HOH   B O    1 
HETATM 5031 O  O    . HOH   D 4 .   ? -3.85500  -4.82600  6.77400   1.000 46.40676  ? 1462 HOH   B O    1 
HETATM 5032 O  O    . HOH   D 4 .   ? 11.04900  -23.61400 -5.09500  1.000 39.84193  ? 1463 HOH   B O    1 
HETATM 5033 O  O    . HOH   D 4 .   ? -2.39300  -21.26600 -9.59800  1.000 50.17442  ? 1464 HOH   B O    1 
HETATM 5034 O  O    . HOH   D 4 .   ? -27.72600 -10.44000 13.13000  1.000 56.53879  ? 1465 HOH   B O    1 
HETATM 5035 O  O    . HOH   D 4 .   ? 12.51200  -14.35200 -6.30100  1.000 49.69407  ? 1466 HOH   B O    1 
HETATM 5036 O  O    . HOH   D 4 .   ? -19.97600 -3.22600  -6.13000  1.000 60.06455  ? 1467 HOH   B O    1 
HETATM 5037 O  O    . HOH   D 4 .   ? 2.24100   -11.96000 11.11100  1.000 50.75489  ? 1468 HOH   B O    1 
HETATM 5038 O  O    . HOH   D 4 .   ? -6.81700  -30.34600 -4.75800  1.000 55.13014  ? 1469 HOH   B O    1 
HETATM 5039 O  O    . HOH   D 4 .   ? -16.40000 -15.11800 13.98400  1.000 57.65264  ? 1470 HOH   B O    1 
HETATM 5040 O  O    . HOH   D 4 .   ? 14.335    -29.943   1.107     1.000 43.27887  ? 1471 HOH   B O    1 
HETATM 5041 O  O    . HOH   D 4 .   ? 4.90300   -15.83600 -7.43500  1.000 40.45166  ? 1472 HOH   B O    1 
HETATM 5042 O  O    . HOH   D 4 .   ? 8.08100   -16.31700 4.28900   1.000 38.51396  ? 1473 HOH   B O    1 
HETATM 5043 O  O    . HOH   D 4 .   ? 3.48000   -24.57500 -3.12300  1.000 51.67901  ? 1474 HOH   B O    1 
HETATM 5044 O  O    . HOH   D 4 .   ? -12.80400 -16.57800 15.45200  1.000 44.72024  ? 1475 HOH   B O    1 
HETATM 5045 O  O    . HOH   D 4 .   ? 5.60300   -12.02300 3.92800   1.000 39.32692  ? 1476 HOH   B O    1 
HETATM 5046 O  O    . HOH   D 4 .   ? 9.08800   -29.62100 2.97300   1.000 47.54500  ? 1477 HOH   B O    1 
HETATM 5047 O  O    . HOH   D 4 .   ? 18.80200  -5.55400  -2.94400  1.000 57.96292  ? 1478 HOH   B O    1 
HETATM 5048 O  O    . HOH   D 4 .   ? -29.275   -19.627   4.073     1.000 54.53872  ? 1479 HOH   B O    1 
HETATM 5049 O  O    . HOH   D 4 .   ? -18.23700 -5.20000  -7.05600  1.000 55.72866  ? 1480 HOH   B O    1 
HETATM 5050 O  O    . HOH   D 4 .   ? -5.99200  -15.14700 7.94700   1.000 38.51876  ? 1481 HOH   B O    1 
HETATM 5051 O  O    . HOH   D 4 .   ? -9.90900  -14.88600 11.05400  1.000 39.04050  ? 1482 HOH   B O    1 
HETATM 5052 O  O    . HOH   D 4 .   ? 15.46300  -29.19300 4.67500   1.000 48.23897  ? 1483 HOH   B O    1 
HETATM 5053 O  O    . HOH   D 4 .   ? 5.78700   -15.01700 3.80700   1.000 35.27937  ? 1484 HOH   B O    1 
HETATM 5054 O  O    . HOH   D 4 .   ? 0.48300   -22.50200 -3.32500  1.000 46.46781  ? 1485 HOH   B O    1 
HETATM 5055 O  O    . HOH   D 4 .   ? -6.60900  -16.72900 10.00000  1.000 43.62104  ? 1486 HOH   B O    1 
HETATM 5056 O  O    . HOH   D 4 .   ? -1.87100  -3.08700  -17.11600 1.000 38.17594  ? 1487 HOH   B O    1 
HETATM 5057 O  O    . HOH   D 4 .   ? 3.31800   10.74800  14.91800  1.000 62.54944  ? 1488 HOH   B O    1 
HETATM 5058 O  O    . HOH   D 4 .   ? 9.08100   -28.33400 -0.11600  1.000 41.81103  ? 1489 HOH   B O    1 
HETATM 5059 O  O    . HOH   D 4 .   ? -17.95300 -4.88500  -4.67100  1.000 45.52119  ? 1490 HOH   B O    1 
HETATM 5060 O  O    . HOH   D 4 .   ? 6.96700   -3.36900  0.42200   1.000 47.16296  ? 1491 HOH   B O    1 
HETATM 5061 O  O    . HOH   D 4 .   ? 6.72300   -8.79900  -7.49900  1.000 49.07190  ? 1492 HOH   B O    1 
HETATM 5062 O  O    . HOH   D 4 .   ? -9.32800  -0.15600  -6.48700  1.000 44.78086  ? 1493 HOH   B O    1 
HETATM 5063 O  O    . HOH   D 4 .   ? -3.89600  -11.73500 16.68200  1.000 53.90350  ? 1494 HOH   B O    1 
HETATM 5064 O  O    . HOH   D 4 .   ? -0.29300  -16.82900 11.68300  1.000 49.68511  ? 1495 HOH   B O    1 
HETATM 5065 O  O    . HOH   D 4 .   ? -26.28000 -4.59800  5.10600   1.000 45.11735  ? 1496 HOH   B O    1 
HETATM 5066 O  O    . HOH   D 4 .   ? -28.47300 -11.24600 -3.68900  1.000 45.52079  ? 1497 HOH   B O    1 
HETATM 5067 O  O    . HOH   D 4 .   ? -0.22100  -21.64100 -7.24200  1.000 52.76277  ? 1498 HOH   B O    1 
HETATM 5068 O  O    . HOH   D 4 .   ? 21.97000  -16.25100 8.86500   1.000 50.68267  ? 1499 HOH   B O    1 
HETATM 5069 O  O    . HOH   D 4 .   ? -8.05900  8.95700   -2.44600  1.000 57.10544  ? 1500 HOH   B O    1 
HETATM 5070 O  O    . HOH   D 4 .   ? -16.80300 -2.90400  -16.08500 1.000 42.02001  ? 1501 HOH   B O    1 
HETATM 5071 O  O    . HOH   D 4 .   ? -8.47500  -28.77800 13.48000  1.000 66.15821  ? 1502 HOH   B O    1 
HETATM 5072 O  O    . HOH   D 4 .   ? -26.78900 -10.26400 -7.44900  1.000 51.11275  ? 1503 HOH   B O    1 
HETATM 5073 O  O    . HOH   D 4 .   ? 2.23400   -13.18000 7.17600   1.000 42.78915  ? 1504 HOH   B O    1 
HETATM 5074 O  O    . HOH   D 4 .   ? -9.25800  -9.74600  -15.98100 1.000 71.44372  ? 1505 HOH   B O    1 
HETATM 5075 O  O    . HOH   D 4 .   ? -19.56100 3.89800   7.10400   1.000 53.79756  ? 1506 HOH   B O    1 
HETATM 5076 O  O    . HOH   D 4 .   ? -7.99700  -5.96400  -3.79600  1.000 42.24355  ? 1507 HOH   B O    1 
HETATM 5077 O  O    . HOH   D 4 .   ? 24.38500  -8.41500  10.20500  1.000 62.16264  ? 1508 HOH   B O    1 
HETATM 5078 O  O    . HOH   D 4 .   ? 3.12800   -29.74700 14.92600  1.000 56.92699  ? 1509 HOH   B O    1 
HETATM 5079 O  O    . HOH   D 4 .   ? 20.093    5.103     16.725    1.000 63.02237  ? 1510 HOH   B O    1 
HETATM 5080 O  O    . HOH   D 4 .   ? 20.60400  -0.95800  -1.39000  1.000 69.48334  ? 1511 HOH   B O    1 
HETATM 5081 O  O    . HOH   D 4 .   ? -5.96900  -26.98400 12.04500  1.000 60.56965  ? 1512 HOH   B O    1 
HETATM 5082 O  O    . HOH   D 4 .   ? 10.00700  -11.30400 -9.36100  1.000 58.26353  ? 1513 HOH   B O    1 
HETATM 5083 O  O    . HOH   D 4 .   ? -18.77300 -4.92600  -16.37500 1.000 56.67390  ? 1514 HOH   B O    1 
HETATM 5084 O  O    . HOH   D 4 .   ? 26.09800  -19.36200 16.06100  1.000 56.67437  ? 1515 HOH   B O    1 
HETATM 5085 O  O    . HOH   D 4 .   ? -9.61300  -8.19400  -18.43100 1.000 56.91815  ? 1516 HOH   B O    1 
HETATM 5086 O  O    . HOH   D 4 .   ? 1.58100   -22.90900 -6.70500  1.000 57.42080  ? 1517 HOH   B O    1 
HETATM 5087 O  O    . HOH   D 4 .   ? -0.11000  -10.99000 12.42200  1.000 56.23349  ? 1518 HOH   B O    1 
HETATM 5088 O  O    . HOH   D 4 .   ? -17.30600 -19.23700 13.98000  1.000 58.24009  ? 1519 HOH   B O    1 
HETATM 5089 O  O    . HOH   D 4 .   ? -0.35900  8.18500   -5.57500  1.000 64.27548  ? 1520 HOH   B O    1 
HETATM 5090 O  O    . HOH   D 4 .   ? -16.81800 -13.67500 -15.24800 1.000 57.02953  ? 1521 HOH   B O    1 
HETATM 5091 O  O    . HOH   D 4 .   ? 7.48800   -25.96300 -5.29600  1.000 55.12734  ? 1522 HOH   B O    1 
HETATM 5092 O  O    . HOH   D 4 .   ? 1.09200   -20.98600 18.81800  1.000 53.42331  ? 1523 HOH   B O    1 
HETATM 5093 O  O    . HOH   D 4 .   ? -12.12300 -28.97500 -1.28600  1.000 56.60856  ? 1524 HOH   B O    1 
HETATM 5094 O  O    . HOH   D 4 .   ? -28.19600 -21.70700 7.99800   1.000 63.59222  ? 1525 HOH   B O    1 
HETATM 5095 O  O    . HOH   D 4 .   ? -5.46500  10.43900  14.37700  1.000 68.78255  ? 1526 HOH   B O    1 
HETATM 5096 O  O    . HOH   D 4 .   ? 3.04600   -14.17900 10.30400  1.000 55.32876  ? 1527 HOH   B O    1 
HETATM 5097 O  O    . HOH   D 4 .   ? 15.16700  5.96500   9.55700   1.000 56.65457  ? 1528 HOH   B O    1 
HETATM 5098 O  O    . HOH   D 4 .   ? -7.63200  -7.44000  -7.88100  1.000 49.17438  ? 1529 HOH   B O    1 
HETATM 5099 O  O    . HOH   D 4 .   ? 24.15700  -6.28800  11.77200  1.000 57.70857  ? 1530 HOH   B O    1 
HETATM 5100 O  O    . HOH   D 4 .   ? -6.39700  -8.84600  23.44800  1.000 49.48804  ? 1531 HOH   B O    1 
HETATM 5101 O  O    . HOH   D 4 .   ? 6.53000   -23.44500 -5.93600  1.000 50.85472  ? 1532 HOH   B O    1 
HETATM 5102 O  O    . HOH   D 4 .   ? 2.84600   -23.42100 -4.77100  1.000 52.53912  ? 1533 HOH   B O    1 
HETATM 5103 O  O    . HOH   D 4 .   ? -5.72400  -29.21600 10.79700  1.000 49.90717  ? 1534 HOH   B O    1 
HETATM 5104 O  O    . HOH   D 4 .   ? 13.07300  -18.46900 -8.71800  1.000 56.91403  ? 1535 HOH   B O    1 
HETATM 5105 O  O    . HOH   D 4 .   ? 21.94400  -2.61600  -3.99300  1.000 64.92414  ? 1536 HOH   B O    1 
HETATM 5106 O  O    . HOH   D 4 .   ? -22.58100 -27.03700 9.82300   1.000 59.78639  ? 1537 HOH   B O    1 
HETATM 5107 O  O    . HOH   D 4 .   ? -0.91300  -3.64200  -14.54100 1.000 61.15367  ? 1538 HOH   B O    1 
HETATM 5108 O  O    . HOH   D 4 .   ? 22.13500  -12.70500 18.04800  1.000 64.46413  ? 1539 HOH   B O    1 
HETATM 5109 O  O    . HOH   D 4 .   ? -9.04800  -6.07200  -6.33800  1.000 53.32604  ? 1540 HOH   B O    1 
HETATM 5110 O  O    . HOH   D 4 .   ? 1.20800   -1.50900  -14.16300 1.000 53.16431  ? 1541 HOH   B O    1 
HETATM 5111 O  O    . HOH   D 4 .   ? -31.07500 -0.13400  -1.38500  1.000 79.09220  ? 1542 HOH   B O    1 
HETATM 5112 O  O    . HOH   D 4 .   ? 23.29800  -4.27000  28.40800  1.000 65.53580  ? 1543 HOH   B O    1 
HETATM 5113 O  O    . HOH   E 4 .   ? -8.23300  23.20600  -21.44000 1.000 48.22139  ? 1501 HOH   A O    1 
HETATM 5114 O  O    . HOH   E 4 .   ? -19.92800 14.04600  -35.78800 1.000 49.41771  ? 1502 HOH   A O    1 
HETATM 5115 O  O    . HOH   E 4 .   ? 2.10000   20.75500  -3.23800  1.000 50.83288  ? 1503 HOH   A O    1 
HETATM 5116 O  O    . HOH   E 4 .   ? -10.85200 15.26800  -20.55100 1.000 51.10554  ? 1504 HOH   A O    1 
HETATM 5117 O  O    . HOH   E 4 .   ? 7.07600   41.35800  -18.15100 1.000 51.37117  ? 1505 HOH   A O    1 
HETATM 5118 O  O    . HOH   E 4 .   ? -9.52200  18.67300  -15.83400 1.000 41.58842  ? 1506 HOH   A O    1 
HETATM 5119 O  O    . HOH   E 4 .   ? -15.28300 36.76000  -24.58600 1.000 56.14644  ? 1507 HOH   A O    1 
HETATM 5120 O  O    . HOH   E 4 .   ? -7.71500  35.19700  -22.43400 1.000 37.38466  ? 1508 HOH   A O    1 
HETATM 5121 O  O    . HOH   E 4 .   ? 3.23200   9.63800   -12.39300 1.000 48.71371  ? 1509 HOH   A O    1 
HETATM 5122 O  O    . HOH   E 4 .   ? -4.23400  22.78600  -14.59300 1.000 44.53400  ? 1510 HOH   A O    1 
HETATM 5123 O  O    . HOH   E 4 .   ? -23.19200 31.95700  -19.54400 1.000 45.05524  ? 1511 HOH   A O    1 
HETATM 5124 O  O    . HOH   E 4 .   ? -9.74400  41.25400  -21.34000 1.000 49.85736  ? 1512 HOH   A O    1 
HETATM 5125 O  O    . HOH   E 4 .   ? -16.96100 38.25400  -9.72400  1.000 65.30510  ? 1513 HOH   A O    1 
HETATM 5126 O  O    . HOH   E 4 .   ? -7.29200  16.31800  -23.26300 1.000 43.52020  ? 1514 HOH   A O    1 
HETATM 5127 O  O    . HOH   E 4 .   ? 0.65100   1.41900   -10.63400 1.000 48.36901  ? 1515 HOH   A O    1 
HETATM 5128 O  O    . HOH   E 4 .   ? -15.66700 22.16100  -32.21400 1.000 45.56581  ? 1516 HOH   A O    1 
HETATM 5129 O  O    . HOH   E 4 .   ? -0.40800  20.13500  -37.42200 1.000 56.66963  ? 1517 HOH   A O    1 
HETATM 5130 O  O    . HOH   E 4 .   ? 2.74100   20.24700  -17.20000 1.000 42.32736  ? 1518 HOH   A O    1 
HETATM 5131 O  O    . HOH   E 4 .   ? -10.72700 7.49100   -12.94200 1.000 35.73966  ? 1519 HOH   A O    1 
HETATM 5132 O  O    . HOH   E 4 .   ? -15.68600 22.27500  -20.66700 1.000 39.41161  ? 1520 HOH   A O    1 
HETATM 5133 O  O    . HOH   E 4 .   ? -8.37600  -3.28600  -30.49300 1.000 50.83055  ? 1521 HOH   A O    1 
HETATM 5134 O  O    . HOH   E 4 .   ? -10.34200 -1.84200  -23.44700 1.000 38.04153  ? 1522 HOH   A O    1 
HETATM 5135 O  O    . HOH   E 4 .   ? -0.95000  -0.54700  -18.07900 1.000 37.93979  ? 1523 HOH   A O    1 
HETATM 5136 O  O    . HOH   E 4 .   ? 5.93600   1.39000   -22.53100 1.000 50.92733  ? 1524 HOH   A O    1 
HETATM 5137 O  O    . HOH   E 4 .   ? 0.54500   17.13900  -16.64000 1.000 29.86543  ? 1525 HOH   A O    1 
HETATM 5138 O  O    . HOH   E 4 .   ? -16.56200 12.63700  -34.72400 1.000 45.10187  ? 1526 HOH   A O    1 
HETATM 5139 O  O    . HOH   E 4 .   ? 11.98100  26.75100  -21.04400 1.000 52.80436  ? 1527 HOH   A O    1 
HETATM 5140 O  O    . HOH   E 4 .   ? -15.48500 -1.51000  -17.97200 1.000 36.68661  ? 1528 HOH   A O    1 
HETATM 5141 O  O    . HOH   E 4 .   ? -1.43700  -2.49900  -24.60500 1.000 43.91149  ? 1529 HOH   A O    1 
HETATM 5142 O  O    . HOH   E 4 .   ? -8.24300  -4.40400  -21.79000 1.000 49.74814  ? 1530 HOH   A O    1 
HETATM 5143 O  O    . HOH   E 4 .   ? -14.61100 21.27200  -3.33200  1.000 42.33184  ? 1531 HOH   A O    1 
HETATM 5144 O  O    . HOH   E 4 .   ? -26.28100 2.43700   -16.15500 1.000 47.68250  ? 1532 HOH   A O    1 
HETATM 5145 O  O    . HOH   E 4 .   ? -20.68300 8.05500   -6.57300  1.000 40.45089  ? 1533 HOH   A O    1 
HETATM 5146 O  O    . HOH   E 4 .   ? -10.11500 26.87500  -23.30300 1.000 54.18406  ? 1534 HOH   A O    1 
HETATM 5147 O  O    . HOH   E 4 .   ? -20.82900 32.13000  -21.92000 1.000 48.07409  ? 1535 HOH   A O    1 
HETATM 5148 O  O    . HOH   E 4 .   ? -1.93800  15.52200  -1.88900  1.000 52.82893  ? 1536 HOH   A O    1 
HETATM 5149 O  O    . HOH   E 4 .   ? -10.43400 21.15000  -16.98300 1.000 36.24130  ? 1537 HOH   A O    1 
HETATM 5150 O  O    . HOH   E 4 .   ? 10.02700  34.54200  -26.45000 1.000 47.36390  ? 1538 HOH   A O    1 
HETATM 5151 O  O    . HOH   E 4 .   ? -10.71100 5.78900   -6.55100  1.000 42.79803  ? 1539 HOH   A O    1 
HETATM 5152 O  O    . HOH   E 4 .   ? -34.15000 15.77900  -18.38800 1.000 57.95012  ? 1540 HOH   A O    1 
HETATM 5153 O  O    . HOH   E 4 .   ? -26.21300 27.09000  -8.64000  1.000 51.50520  ? 1541 HOH   A O    1 
HETATM 5154 O  O    . HOH   E 4 .   ? -21.57800 32.98400  -4.32400  1.000 45.60179  ? 1542 HOH   A O    1 
HETATM 5155 O  O    . HOH   E 4 .   ? -27.05200 11.65300  -9.11600  1.000 46.20680  ? 1543 HOH   A O    1 
HETATM 5156 O  O    . HOH   E 4 .   ? -7.12400  38.94500  -19.53600 1.000 43.83954  ? 1544 HOH   A O    1 
HETATM 5157 O  O    . HOH   E 4 .   ? -7.22500  30.93100  -1.17100  1.000 51.19567  ? 1545 HOH   A O    1 
HETATM 5158 O  O    . HOH   E 4 .   ? -9.41200  26.64300  -0.33500  1.000 50.56126  ? 1546 HOH   A O    1 
HETATM 5159 O  O    . HOH   E 4 .   ? -4.59200  30.75800  -25.88500 1.000 36.48935  ? 1547 HOH   A O    1 
HETATM 5160 O  O    . HOH   E 4 .   ? -8.11400  24.91200  -23.79400 1.000 36.20184  ? 1548 HOH   A O    1 
HETATM 5161 O  O    . HOH   E 4 .   ? 1.68700   -3.17600  -22.56200 1.000 49.66004  ? 1549 HOH   A O    1 
HETATM 5162 O  O    . HOH   E 4 .   ? 8.57900   29.25100  -20.57600 1.000 41.73386  ? 1550 HOH   A O    1 
HETATM 5163 O  O    . HOH   E 4 .   ? 0.04600   10.57600  -12.38600 1.000 44.20428  ? 1551 HOH   A O    1 
HETATM 5164 O  O    . HOH   E 4 .   ? -21.15400 23.90700  -27.67800 1.000 43.07418  ? 1552 HOH   A O    1 
HETATM 5165 O  O    . HOH   E 4 .   ? -3.01200  28.54500  -6.08000  1.000 43.75650  ? 1553 HOH   A O    1 
HETATM 5166 O  O    . HOH   E 4 .   ? -9.62800  21.45800  -32.34900 1.000 43.76441  ? 1554 HOH   A O    1 
HETATM 5167 O  O    . HOH   E 4 .   ? -14.24300 20.78100  -0.23400  1.000 45.62823  ? 1555 HOH   A O    1 
HETATM 5168 O  O    . HOH   E 4 .   ? -13.49000 18.31300  -21.55400 1.000 32.28820  ? 1556 HOH   A O    1 
HETATM 5169 O  O    . HOH   E 4 .   ? -9.15700  32.27900  -19.18200 1.000 37.26247  ? 1557 HOH   A O    1 
HETATM 5170 O  O    . HOH   E 4 .   ? -29.62000 18.04200  -18.70500 1.000 51.33166  ? 1558 HOH   A O    1 
HETATM 5171 O  O    . HOH   E 4 .   ? -22.97700 31.53400  -11.49800 1.000 44.16960  ? 1559 HOH   A O    1 
HETATM 5172 O  O    . HOH   E 4 .   ? 13.32300  18.67300  -10.89000 1.000 77.05993  ? 1560 HOH   A O    1 
HETATM 5173 O  O    . HOH   E 4 .   ? -2.62300  12.04200  -11.93900 1.000 37.60556  ? 1561 HOH   A O    1 
HETATM 5174 O  O    . HOH   E 4 .   ? -1.01700  28.68100  -3.71000  1.000 46.71813  ? 1562 HOH   A O    1 
HETATM 5175 O  O    . HOH   E 4 .   ? -4.31600  14.42700  -18.61100 1.000 37.54137  ? 1563 HOH   A O    1 
HETATM 5176 O  O    . HOH   E 4 .   ? 7.40300   12.13100  -24.48200 1.000 43.52643  ? 1564 HOH   A O    1 
HETATM 5177 O  O    . HOH   E 4 .   ? -23.89100 24.62700  -24.87100 1.000 40.68547  ? 1565 HOH   A O    1 
HETATM 5178 O  O    . HOH   E 4 .   ? -17.83400 19.68900  -24.88000 1.000 50.25419  ? 1566 HOH   A O    1 
HETATM 5179 O  O    . HOH   E 4 .   ? -26.39400 6.88500   -10.13600 1.000 49.25915  ? 1567 HOH   A O    1 
HETATM 5180 O  O    . HOH   E 4 .   ? -15.37900 3.46800   -2.90300  1.000 47.06714  ? 1568 HOH   A O    1 
HETATM 5181 O  O    . HOH   E 4 .   ? -11.49400 -0.96200  -10.24200 1.000 44.50687  ? 1569 HOH   A O    1 
HETATM 5182 O  O    . HOH   E 4 .   ? -5.13800  15.93000  -16.49900 1.000 33.29293  ? 1570 HOH   A O    1 
HETATM 5183 O  O    . HOH   E 4 .   ? -1.04900  40.04400  -24.77500 1.000 50.78532  ? 1571 HOH   A O    1 
HETATM 5184 O  O    . HOH   E 4 .   ? 5.71500   18.30200  -23.10500 1.000 42.46596  ? 1572 HOH   A O    1 
HETATM 5185 O  O    . HOH   E 4 .   ? -28.47200 16.24600  -25.03400 1.000 50.65255  ? 1573 HOH   A O    1 
HETATM 5186 O  O    . HOH   E 4 .   ? -11.34400 32.18100  -20.63700 1.000 38.74338  ? 1574 HOH   A O    1 
HETATM 5187 O  O    . HOH   E 4 .   ? 9.71700   23.83300  -15.56300 1.000 43.29624  ? 1575 HOH   A O    1 
HETATM 5188 O  O    . HOH   E 4 .   ? 3.81100   9.28000   -37.34100 1.000 44.64352  ? 1576 HOH   A O    1 
HETATM 5189 O  O    . HOH   E 4 .   ? 2.73300   -1.56100  -19.76700 1.000 52.14208  ? 1577 HOH   A O    1 
HETATM 5190 O  O    . HOH   E 4 .   ? -3.17900  10.40900  -8.72200  1.000 41.33457  ? 1578 HOH   A O    1 
HETATM 5191 O  O    . HOH   E 4 .   ? -4.49700  -3.04400  -16.46900 1.000 42.35904  ? 1579 HOH   A O    1 
HETATM 5192 O  O    . HOH   E 4 .   ? -2.47500  43.72200  -26.76000 1.000 44.48009  ? 1580 HOH   A O    1 
HETATM 5193 O  O    . HOH   E 4 .   ? -28.60100 7.67100   -11.48700 1.000 47.01249  ? 1581 HOH   A O    1 
HETATM 5194 O  O    . HOH   E 4 .   ? 8.00900   6.85700   -20.73100 1.000 47.55673  ? 1582 HOH   A O    1 
HETATM 5195 O  O    . HOH   E 4 .   ? -16.60800 16.89600  -24.14500 1.000 42.71287  ? 1583 HOH   A O    1 
HETATM 5196 O  O    . HOH   E 4 .   ? 5.71100   38.23700  -18.63800 1.000 51.20767  ? 1584 HOH   A O    1 
HETATM 5197 O  O    . HOH   E 4 .   ? -12.40900 10.79600  -39.23900 1.000 42.20792  ? 1585 HOH   A O    1 
HETATM 5198 O  O    . HOH   E 4 .   ? -18.56300 27.26000  -25.77900 1.000 46.55456  ? 1586 HOH   A O    1 
HETATM 5199 O  O    . HOH   E 4 .   ? -20.53600 30.27600  -23.92800 1.000 46.06905  ? 1587 HOH   A O    1 
HETATM 5200 O  O    . HOH   E 4 .   ? -5.59200  1.30300   -35.41100 1.000 51.25342  ? 1588 HOH   A O    1 
HETATM 5201 O  O    . HOH   E 4 .   ? -13.51200 37.58700  -25.78600 1.000 48.48409  ? 1589 HOH   A O    1 
HETATM 5202 O  O    . HOH   E 4 .   ? -24.80200 18.20200  -27.29300 1.000 45.28900  ? 1590 HOH   A O    1 
HETATM 5203 O  O    . HOH   E 4 .   ? -22.11600 1.29300   -11.85800 1.000 46.82602  ? 1591 HOH   A O    1 
HETATM 5204 O  O    . HOH   E 4 .   ? -8.71400  14.27800  -21.75400 1.000 36.36516  ? 1592 HOH   A O    1 
HETATM 5205 O  O    . HOH   E 4 .   ? -27.46000 8.45300   -23.76000 1.000 57.56080  ? 1593 HOH   A O    1 
HETATM 5206 O  O    . HOH   E 4 .   ? 10.19400  33.39700  -23.05600 1.000 50.59809  ? 1594 HOH   A O    1 
HETATM 5207 O  O    . HOH   E 4 .   ? -6.19200  -4.64700  -17.50500 1.000 50.62766  ? 1595 HOH   A O    1 
HETATM 5208 O  O    . HOH   E 4 .   ? -4.05000  2.02400   -37.00600 1.000 50.01731  ? 1596 HOH   A O    1 
HETATM 5209 O  O    . HOH   E 4 .   ? 2.78000   39.06700  -22.21400 1.000 45.67345  ? 1597 HOH   A O    1 
HETATM 5210 O  O    . HOH   E 4 .   ? 5.18700   16.52500  -25.77900 1.000 49.12576  ? 1598 HOH   A O    1 
HETATM 5211 O  O    . HOH   E 4 .   ? -18.15300 15.94400  -34.08200 1.000 44.66002  ? 1599 HOH   A O    1 
HETATM 5212 O  O    . HOH   E 4 .   ? -7.74400  36.20700  -19.90800 1.000 44.39924  ? 1600 HOH   A O    1 
HETATM 5213 O  O    . HOH   E 4 .   ? -14.73400 -2.49400  -29.82000 1.000 50.34582  ? 1601 HOH   A O    1 
HETATM 5214 O  O    . HOH   E 4 .   ? -15.26000 1.22900   -19.70200 1.000 41.40056  ? 1602 HOH   A O    1 
HETATM 5215 O  O    . HOH   E 4 .   ? -0.55400  10.24700  -9.88800  1.000 60.55637  ? 1603 HOH   A O    1 
HETATM 5216 O  O    . HOH   E 4 .   ? 7.91500   25.42800  -9.44800  1.000 57.17047  ? 1604 HOH   A O    1 
HETATM 5217 O  O    . HOH   E 4 .   ? -19.76300 1.29700   -11.42100 1.000 47.99618  ? 1605 HOH   A O    1 
HETATM 5218 O  O    . HOH   E 4 .   ? 5.18900   39.20700  -21.09900 1.000 46.56682  ? 1606 HOH   A O    1 
HETATM 5219 O  O    . HOH   E 4 .   ? -18.94900 -3.45800  -8.60800  1.000 60.19971  ? 1607 HOH   A O    1 
HETATM 5220 O  O    . HOH   E 4 .   ? -22.27200 35.61400  -19.80700 1.000 57.90341  ? 1608 HOH   A O    1 
HETATM 5221 O  O    . HOH   E 4 .   ? 3.83600   2.26000   -27.35200 1.000 42.47289  ? 1609 HOH   A O    1 
HETATM 5222 O  O    . HOH   E 4 .   ? -20.57000 9.67600   -9.40400  1.000 38.95326  ? 1610 HOH   A O    1 
HETATM 5223 O  O    . HOH   E 4 .   ? -24.84100 4.86500   -11.60900 1.000 45.85009  ? 1611 HOH   A O    1 
HETATM 5224 O  O    . HOH   E 4 .   ? 0.18900   34.92400  -27.12100 1.000 47.69792  ? 1612 HOH   A O    1 
HETATM 5225 O  O    . HOH   E 4 .   ? 1.22600   21.62400  -40.63300 1.000 58.83512  ? 1613 HOH   A O    1 
HETATM 5226 O  O    . HOH   E 4 .   ? 9.81400   30.07300  -29.89600 1.000 59.45108  ? 1614 HOH   A O    1 
HETATM 5227 O  O    . HOH   E 4 .   ? -3.29100  -1.13100  -26.28800 1.000 43.37143  ? 1615 HOH   A O    1 
HETATM 5228 O  O    . HOH   E 4 .   ? -13.08300 16.75600  -27.47200 1.000 44.02153  ? 1616 HOH   A O    1 
HETATM 5229 O  O    . HOH   E 4 .   ? -16.00500 19.45900  -21.08000 1.000 37.82569  ? 1617 HOH   A O    1 
HETATM 5230 O  O    . HOH   E 4 .   ? -6.42600  -8.04700  -3.68900  1.000 41.48381  ? 1618 HOH   A O    1 
HETATM 5231 O  O    . HOH   E 4 .   ? -21.73100 -0.47800  -22.47300 1.000 50.02672  ? 1619 HOH   A O    1 
HETATM 5232 O  O    . HOH   E 4 .   ? -8.40200  -1.84000  -10.59600 1.000 47.75274  ? 1620 HOH   A O    1 
HETATM 5233 O  O    . HOH   E 4 .   ? -10.59700 31.06200  -22.57400 1.000 43.00105  ? 1621 HOH   A O    1 
HETATM 5234 O  O    . HOH   E 4 .   ? -9.89300  18.10500  -23.30600 1.000 45.68316  ? 1622 HOH   A O    1 
HETATM 5235 O  O    . HOH   E 4 .   ? -10.57000 25.24300  -20.64700 1.000 42.25887  ? 1623 HOH   A O    1 
HETATM 5236 O  O    . HOH   E 4 .   ? 2.090     38.404    -27.370   1.000 46.83189  ? 1624 HOH   A O    1 
HETATM 5237 O  O    . HOH   E 4 .   ? -7.45400  -13.09700 8.13400   1.000 41.70545  ? 1625 HOH   A O    1 
HETATM 5238 O  O    . HOH   E 4 .   ? -13.78800 23.36800  -19.32700 1.000 41.55570  ? 1626 HOH   A O    1 
HETATM 5239 O  O    . HOH   E 4 .   ? 0.01100   20.63900  -17.81300 1.000 39.04589  ? 1627 HOH   A O    1 
HETATM 5240 O  O    . HOH   E 4 .   ? -15.92500 6.11500   -34.93600 1.000 53.85120  ? 1628 HOH   A O    1 
HETATM 5241 O  O    . HOH   E 4 .   ? -11.19100 20.68300  -30.26800 1.000 41.85505  ? 1629 HOH   A O    1 
HETATM 5242 O  O    . HOH   E 4 .   ? -29.13800 20.94500  -18.61100 1.000 56.15062  ? 1630 HOH   A O    1 
HETATM 5243 O  O    . HOH   E 4 .   ? 1.40400   3.21900   -12.75700 1.000 44.97429  ? 1631 HOH   A O    1 
HETATM 5244 O  O    . HOH   E 4 .   ? 2.15500   36.58800  -10.49500 1.000 44.09343  ? 1632 HOH   A O    1 
HETATM 5245 O  O    . HOH   E 4 .   ? -13.82400 22.84300  -38.15200 1.000 52.09731  ? 1633 HOH   A O    1 
HETATM 5246 O  O    . HOH   E 4 .   ? -1.11200  9.03200   -7.71400  1.000 60.33123  ? 1634 HOH   A O    1 
HETATM 5247 O  O    . HOH   E 4 .   ? 10.66200  22.83900  -11.69300 1.000 51.70249  ? 1635 HOH   A O    1 
HETATM 5248 O  O    . HOH   E 4 .   ? -11.02600 22.50500  -19.41200 1.000 35.54933  ? 1636 HOH   A O    1 
HETATM 5249 O  O    . HOH   E 4 .   ? -9.24100  3.72200   -6.78500  1.000 45.13729  ? 1637 HOH   A O    1 
HETATM 5250 O  O    . HOH   E 4 .   ? -6.48400  45.37600  -28.36500 1.000 57.00696  ? 1638 HOH   A O    1 
HETATM 5251 O  O    . HOH   E 4 .   ? 3.44800   3.25800   -16.62400 1.000 52.19541  ? 1639 HOH   A O    1 
HETATM 5252 O  O    . HOH   E 4 .   ? 3.37200   5.05000   -11.79100 1.000 51.50301  ? 1640 HOH   A O    1 
HETATM 5253 O  O    . HOH   E 4 .   ? -24.93600 7.00800   -5.38900  1.000 58.86795  ? 1641 HOH   A O    1 
HETATM 5254 O  O    . HOH   E 4 .   ? 12.63800  22.05100  -18.63200 1.000 54.24241  ? 1642 HOH   A O    1 
HETATM 5255 O  O    . HOH   E 4 .   ? -13.70600 -3.93700  -8.87200  1.000 53.08086  ? 1643 HOH   A O    1 
HETATM 5256 O  O    . HOH   E 4 .   ? -23.63200 27.01600  -25.74800 1.000 51.64097  ? 1644 HOH   A O    1 
HETATM 5257 O  O    . HOH   E 4 .   ? -3.66500  -11.46300 10.11200  1.000 52.66665  ? 1645 HOH   A O    1 
HETATM 5258 O  O    . HOH   E 4 .   ? -29.24700 22.10300  -13.84900 1.000 53.74746  ? 1646 HOH   A O    1 
HETATM 5259 O  O    . HOH   E 4 .   ? 9.86900   30.54000  -18.26000 1.000 45.54902  ? 1647 HOH   A O    1 
HETATM 5260 O  O    . HOH   E 4 .   ? -30.48400 16.41400  -23.82300 1.000 61.36872  ? 1648 HOH   A O    1 
HETATM 5261 O  O    . HOH   E 4 .   ? -15.39400 39.46300  -22.94600 1.000 58.23647  ? 1649 HOH   A O    1 
HETATM 5262 O  O    . HOH   E 4 .   ? -18.58300 37.67600  -14.56300 1.000 51.32944  ? 1650 HOH   A O    1 
HETATM 5263 O  O    . HOH   E 4 .   ? 6.74700   41.62700  -20.90500 1.000 44.51807  ? 1651 HOH   A O    1 
HETATM 5264 O  O    . HOH   E 4 .   ? 0.96800   -0.01200  -16.36900 1.000 43.43113  ? 1652 HOH   A O    1 
HETATM 5265 O  O    . HOH   E 4 .   ? 1.04500   9.89000   -7.65500  1.000 58.02368  ? 1653 HOH   A O    1 
HETATM 5266 O  O    . HOH   E 4 .   ? -2.63900  -3.49800  -11.97100 1.000 60.08927  ? 1654 HOH   A O    1 
HETATM 5267 O  O    . HOH   E 4 .   ? 6.74800   14.48000  -26.00200 1.000 48.52425  ? 1655 HOH   A O    1 
HETATM 5268 O  O    . HOH   E 4 .   ? -23.80500 35.77400  -10.92500 1.000 60.60562  ? 1656 HOH   A O    1 
HETATM 5269 O  O    . HOH   E 4 .   ? -17.34000 7.37500   -36.83500 1.000 52.47513  ? 1657 HOH   A O    1 
HETATM 5270 O  O    . HOH   E 4 .   ? -28.53100 10.29000  -24.85300 1.000 49.22297  ? 1658 HOH   A O    1 
HETATM 5271 O  O    . HOH   E 4 .   ? -9.64400  -5.06500  -28.98900 1.000 44.73463  ? 1659 HOH   A O    1 
HETATM 5272 O  O    . HOH   E 4 .   ? -21.70200 7.88700   -3.52000  1.000 44.75990  ? 1660 HOH   A O    1 
HETATM 5273 O  O    . HOH   E 4 .   ? 4.99800   36.24000  -12.59000 1.000 51.46489  ? 1661 HOH   A O    1 
HETATM 5274 O  O    . HOH   E 4 .   ? 1.87000   2.79200   -15.13700 1.000 49.13339  ? 1662 HOH   A O    1 
HETATM 5275 O  O    . HOH   E 4 .   ? -4.35600  -3.71400  -26.84400 1.000 47.57358  ? 1663 HOH   A O    1 
HETATM 5276 O  O    . HOH   E 4 .   ? -14.36600 21.96800  -27.31100 1.000 56.89293  ? 1664 HOH   A O    1 
HETATM 5277 O  O    . HOH   E 4 .   ? -15.61300 44.46300  -25.76900 1.000 68.16740  ? 1665 HOH   A O    1 
HETATM 5278 O  O    . HOH   E 4 .   ? -25.48200 22.57000  0.38700   1.000 54.57861  ? 1666 HOH   A O    1 
HETATM 5279 O  O    . HOH   E 4 .   ? -16.18000 25.62700  -29.07500 1.000 60.90280  ? 1667 HOH   A O    1 
# 
