data_8ZLW
# 
_entry.id   8ZLW 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   8ZLW         pdb_00008zlw 10.2210/pdb8zlw/pdb 
WWPDB D_1300046947 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-02 ? 
2 'Structure model' 1 1 2025-04-09 ? 
# 
_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                        8ZLW 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-21 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              liuwei@sphmc.org 
_pdbx_contact_author.name_first         Wei 
_pdbx_contact_author.name_last          Liu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8250-2562 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Liu, J.'    1 ? 
'Ding, Y.Z.' 2 ? 
'Li, J.C.'   3 ? 
'Liu, W.'    4 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                3120 
_citation.page_last                 3120 
_citation.title                     
'Structural insights into the dual Ca 2+ -sensor-mediated activation of the PPEF phosphatase family.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-58261-z 
_citation.pdbx_database_id_PubMed   40169586 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Liu, J.'  1  ?                   
primary 'Wu, C.'   2  0000-0002-6218-8569 
primary 'Liu, Y.'  3  ?                   
primary 'Chen, Q.' 4  ?                   
primary 'Ding, Y.' 5  ?                   
primary 'Lin, Z.'  6  ?                   
primary 'Pan, L.'  7  0000-0002-9229-6288 
primary 'Xiao, K.' 8  0000-0002-7666-2460 
primary 'Li, J.'   9  0000-0002-8921-1626 
primary 'Liu, Z.'  10 0000-0002-3280-3890 
primary 'Liu, W.'  11 0000-0001-8250-2562 
# 
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 'Maltodextrin-binding protein'              40807.242 1  ?        ? ? ? 
2 polymer     man Calmodulin                                  17123.816 1  ?        ? ? ? 
3 polymer     man 'Serine/threonine-protein phosphatase rdgC' 4268.873  1  3.1.3.16 ? ? ? 
4 non-polymer syn 'CALCIUM ION'                               40.078    4  ?        ? ? ? 
5 water       nat water                                       18.015    58 ?        ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
2 CaM                              
3 'Retinal degeneration C 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 
;MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEI
TPAAAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWP
LIAADGGYAFKYAAGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSA
VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAA
TMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALAAAQTNAARAFAAA
;
;MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEI
TPAAAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWP
LIAADGGYAFKYAAGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSA
VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAA
TMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALAAAQTNAARAFAAA
;
A ? 
2 'polypeptide(L)' no no 
;GPGSMADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARK
MKDTDSEEEIREAFRVFDKDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVTMMTSK
;
;GPGSMADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARK
MKDTDSEEEIREAFRVFDKDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVTMMTSK
;
N ? 
3 'polypeptide(L)' no no MDENAIRAAIFIQKWYRRHQARREMLEHHHHHH MDENAIRAAIFIQKWYRRHQARREMLEHHHHHH R ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 'CALCIUM ION' CA  
5 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   LYS n 
1 3   ILE n 
1 4   GLU n 
1 5   GLU n 
1 6   GLY n 
1 7   LYS n 
1 8   LEU n 
1 9   VAL n 
1 10  ILE n 
1 11  TRP n 
1 12  ILE n 
1 13  ASN n 
1 14  GLY n 
1 15  ASP n 
1 16  LYS n 
1 17  GLY n 
1 18  TYR n 
1 19  ASN n 
1 20  GLY n 
1 21  LEU n 
1 22  ALA n 
1 23  GLU n 
1 24  VAL n 
1 25  GLY n 
1 26  LYS n 
1 27  LYS n 
1 28  PHE n 
1 29  GLU n 
1 30  LYS n 
1 31  ASP n 
1 32  THR n 
1 33  GLY n 
1 34  ILE n 
1 35  LYS n 
1 36  VAL n 
1 37  THR n 
1 38  VAL n 
1 39  GLU n 
1 40  HIS n 
1 41  PRO n 
1 42  ASP n 
1 43  LYS n 
1 44  LEU n 
1 45  GLU n 
1 46  GLU n 
1 47  LYS n 
1 48  PHE n 
1 49  PRO n 
1 50  GLN n 
1 51  VAL n 
1 52  ALA n 
1 53  ALA n 
1 54  THR n 
1 55  GLY n 
1 56  ASP n 
1 57  GLY n 
1 58  PRO n 
1 59  ASP n 
1 60  ILE n 
1 61  ILE n 
1 62  PHE n 
1 63  TRP n 
1 64  ALA n 
1 65  HIS n 
1 66  ASP n 
1 67  ARG n 
1 68  PHE n 
1 69  GLY n 
1 70  GLY n 
1 71  TYR n 
1 72  ALA n 
1 73  GLN n 
1 74  SER n 
1 75  GLY n 
1 76  LEU n 
1 77  LEU n 
1 78  ALA n 
1 79  GLU n 
1 80  ILE n 
1 81  THR n 
1 82  PRO n 
1 83  ALA n 
1 84  ALA n 
1 85  ALA n 
1 86  PHE n 
1 87  GLN n 
1 88  ASP n 
1 89  LYS n 
1 90  LEU n 
1 91  TYR n 
1 92  PRO n 
1 93  PHE n 
1 94  THR n 
1 95  TRP n 
1 96  ASP n 
1 97  ALA n 
1 98  VAL n 
1 99  ARG n 
1 100 TYR n 
1 101 ASN n 
1 102 GLY n 
1 103 LYS n 
1 104 LEU n 
1 105 ILE n 
1 106 ALA n 
1 107 TYR n 
1 108 PRO n 
1 109 ILE n 
1 110 ALA n 
1 111 VAL n 
1 112 GLU n 
1 113 ALA n 
1 114 LEU n 
1 115 SER n 
1 116 LEU n 
1 117 ILE n 
1 118 TYR n 
1 119 ASN n 
1 120 LYS n 
1 121 ASP n 
1 122 LEU n 
1 123 LEU n 
1 124 PRO n 
1 125 ASN n 
1 126 PRO n 
1 127 PRO n 
1 128 LYS n 
1 129 THR n 
1 130 TRP n 
1 131 GLU n 
1 132 GLU n 
1 133 ILE n 
1 134 PRO n 
1 135 ALA n 
1 136 LEU n 
1 137 ASP n 
1 138 LYS n 
1 139 GLU n 
1 140 LEU n 
1 141 LYS n 
1 142 ALA n 
1 143 LYS n 
1 144 GLY n 
1 145 LYS n 
1 146 SER n 
1 147 ALA n 
1 148 LEU n 
1 149 MET n 
1 150 PHE n 
1 151 ASN n 
1 152 LEU n 
1 153 GLN n 
1 154 GLU n 
1 155 PRO n 
1 156 TYR n 
1 157 PHE n 
1 158 THR n 
1 159 TRP n 
1 160 PRO n 
1 161 LEU n 
1 162 ILE n 
1 163 ALA n 
1 164 ALA n 
1 165 ASP n 
1 166 GLY n 
1 167 GLY n 
1 168 TYR n 
1 169 ALA n 
1 170 PHE n 
1 171 LYS n 
1 172 TYR n 
1 173 ALA n 
1 174 ALA n 
1 175 GLY n 
1 176 LYS n 
1 177 TYR n 
1 178 ASP n 
1 179 ILE n 
1 180 LYS n 
1 181 ASP n 
1 182 VAL n 
1 183 GLY n 
1 184 VAL n 
1 185 ASP n 
1 186 ASN n 
1 187 ALA n 
1 188 GLY n 
1 189 ALA n 
1 190 LYS n 
1 191 ALA n 
1 192 GLY n 
1 193 LEU n 
1 194 THR n 
1 195 PHE n 
1 196 LEU n 
1 197 VAL n 
1 198 ASP n 
1 199 LEU n 
1 200 ILE n 
1 201 LYS n 
1 202 ASN n 
1 203 LYS n 
1 204 HIS n 
1 205 MET n 
1 206 ASN n 
1 207 ALA n 
1 208 ASP n 
1 209 THR n 
1 210 ASP n 
1 211 TYR n 
1 212 SER n 
1 213 ILE n 
1 214 ALA n 
1 215 GLU n 
1 216 ALA n 
1 217 ALA n 
1 218 PHE n 
1 219 ASN n 
1 220 LYS n 
1 221 GLY n 
1 222 GLU n 
1 223 THR n 
1 224 ALA n 
1 225 MET n 
1 226 THR n 
1 227 ILE n 
1 228 ASN n 
1 229 GLY n 
1 230 PRO n 
1 231 TRP n 
1 232 ALA n 
1 233 TRP n 
1 234 SER n 
1 235 ASN n 
1 236 ILE n 
1 237 ASP n 
1 238 THR n 
1 239 SER n 
1 240 ALA n 
1 241 VAL n 
1 242 ASN n 
1 243 TYR n 
1 244 GLY n 
1 245 VAL n 
1 246 THR n 
1 247 VAL n 
1 248 LEU n 
1 249 PRO n 
1 250 THR n 
1 251 PHE n 
1 252 LYS n 
1 253 GLY n 
1 254 GLN n 
1 255 PRO n 
1 256 SER n 
1 257 LYS n 
1 258 PRO n 
1 259 PHE n 
1 260 VAL n 
1 261 GLY n 
1 262 VAL n 
1 263 LEU n 
1 264 SER n 
1 265 ALA n 
1 266 GLY n 
1 267 ILE n 
1 268 ASN n 
1 269 ALA n 
1 270 ALA n 
1 271 SER n 
1 272 PRO n 
1 273 ASN n 
1 274 LYS n 
1 275 GLU n 
1 276 LEU n 
1 277 ALA n 
1 278 LYS n 
1 279 GLU n 
1 280 PHE n 
1 281 LEU n 
1 282 GLU n 
1 283 ASN n 
1 284 TYR n 
1 285 LEU n 
1 286 LEU n 
1 287 THR n 
1 288 ASP n 
1 289 GLU n 
1 290 GLY n 
1 291 LEU n 
1 292 GLU n 
1 293 ALA n 
1 294 VAL n 
1 295 ASN n 
1 296 LYS n 
1 297 ASP n 
1 298 LYS n 
1 299 PRO n 
1 300 LEU n 
1 301 GLY n 
1 302 ALA n 
1 303 VAL n 
1 304 ALA n 
1 305 LEU n 
1 306 LYS n 
1 307 SER n 
1 308 TYR n 
1 309 GLU n 
1 310 GLU n 
1 311 GLU n 
1 312 LEU n 
1 313 ALA n 
1 314 LYS n 
1 315 ASP n 
1 316 PRO n 
1 317 ARG n 
1 318 ILE n 
1 319 ALA n 
1 320 ALA n 
1 321 THR n 
1 322 MET n 
1 323 GLU n 
1 324 ASN n 
1 325 ALA n 
1 326 GLN n 
1 327 LYS n 
1 328 GLY n 
1 329 GLU n 
1 330 ILE n 
1 331 MET n 
1 332 PRO n 
1 333 ASN n 
1 334 ILE n 
1 335 PRO n 
1 336 GLN n 
1 337 MET n 
1 338 SER n 
1 339 ALA n 
1 340 PHE n 
1 341 TRP n 
1 342 TYR n 
1 343 ALA n 
1 344 VAL n 
1 345 ARG n 
1 346 THR n 
1 347 ALA n 
1 348 VAL n 
1 349 ILE n 
1 350 ASN n 
1 351 ALA n 
1 352 ALA n 
1 353 SER n 
1 354 GLY n 
1 355 ARG n 
1 356 GLN n 
1 357 THR n 
1 358 VAL n 
1 359 ASP n 
1 360 ALA n 
1 361 ALA n 
1 362 LEU n 
1 363 ALA n 
1 364 ALA n 
1 365 ALA n 
1 366 GLN n 
1 367 THR n 
1 368 ASN n 
1 369 ALA n 
1 370 ALA n 
1 371 ARG n 
1 372 ALA n 
1 373 PHE n 
1 374 ALA n 
1 375 ALA n 
1 376 ALA n 
2 1   GLY n 
2 2   PRO n 
2 3   GLY n 
2 4   SER n 
2 5   MET n 
2 6   ALA n 
2 7   ASP n 
2 8   GLN n 
2 9   LEU n 
2 10  THR n 
2 11  GLU n 
2 12  GLU n 
2 13  GLN n 
2 14  ILE n 
2 15  ALA n 
2 16  GLU n 
2 17  PHE n 
2 18  LYS n 
2 19  GLU n 
2 20  ALA n 
2 21  PHE n 
2 22  SER n 
2 23  LEU n 
2 24  PHE n 
2 25  ASP n 
2 26  LYS n 
2 27  ASP n 
2 28  GLY n 
2 29  ASP n 
2 30  GLY n 
2 31  THR n 
2 32  ILE n 
2 33  THR n 
2 34  THR n 
2 35  LYS n 
2 36  GLU n 
2 37  LEU n 
2 38  GLY n 
2 39  THR n 
2 40  VAL n 
2 41  MET n 
2 42  ARG n 
2 43  SER n 
2 44  LEU n 
2 45  GLY n 
2 46  GLN n 
2 47  ASN n 
2 48  PRO n 
2 49  THR n 
2 50  GLU n 
2 51  ALA n 
2 52  GLU n 
2 53  LEU n 
2 54  GLN n 
2 55  ASP n 
2 56  MET n 
2 57  ILE n 
2 58  ASN n 
2 59  GLU n 
2 60  VAL n 
2 61  ASP n 
2 62  ALA n 
2 63  ASP n 
2 64  GLY n 
2 65  ASN n 
2 66  GLY n 
2 67  THR n 
2 68  ILE n 
2 69  ASP n 
2 70  PHE n 
2 71  PRO n 
2 72  GLU n 
2 73  PHE n 
2 74  LEU n 
2 75  THR n 
2 76  MET n 
2 77  MET n 
2 78  ALA n 
2 79  ARG n 
2 80  LYS n 
2 81  MET n 
2 82  LYS n 
2 83  ASP n 
2 84  THR n 
2 85  ASP n 
2 86  SER n 
2 87  GLU n 
2 88  GLU n 
2 89  GLU n 
2 90  ILE n 
2 91  ARG n 
2 92  GLU n 
2 93  ALA n 
2 94  PHE n 
2 95  ARG n 
2 96  VAL n 
2 97  PHE n 
2 98  ASP n 
2 99  LYS n 
2 100 ASP n 
2 101 GLY n 
2 102 ASN n 
2 103 GLY n 
2 104 PHE n 
2 105 ILE n 
2 106 SER n 
2 107 ALA n 
2 108 ALA n 
2 109 GLU n 
2 110 LEU n 
2 111 ARG n 
2 112 HIS n 
2 113 VAL n 
2 114 MET n 
2 115 THR n 
2 116 ASN n 
2 117 LEU n 
2 118 GLY n 
2 119 GLU n 
2 120 LYS n 
2 121 LEU n 
2 122 THR n 
2 123 ASP n 
2 124 GLU n 
2 125 GLU n 
2 126 VAL n 
2 127 ASP n 
2 128 GLU n 
2 129 MET n 
2 130 ILE n 
2 131 ARG n 
2 132 GLU n 
2 133 ALA n 
2 134 ASP n 
2 135 ILE n 
2 136 ASP n 
2 137 GLY n 
2 138 ASP n 
2 139 GLY n 
2 140 GLN n 
2 141 VAL n 
2 142 ASN n 
2 143 TYR n 
2 144 GLU n 
2 145 GLU n 
2 146 PHE n 
2 147 VAL n 
2 148 THR n 
2 149 MET n 
2 150 MET n 
2 151 THR n 
2 152 SER n 
2 153 LYS n 
3 1   MET n 
3 2   ASP n 
3 3   GLU n 
3 4   ASN n 
3 5   ALA n 
3 6   ILE n 
3 7   ARG n 
3 8   ALA n 
3 9   ALA n 
3 10  ILE n 
3 11  PHE n 
3 12  ILE n 
3 13  GLN n 
3 14  LYS n 
3 15  TRP n 
3 16  TYR n 
3 17  ARG n 
3 18  ARG n 
3 19  HIS n 
3 20  GLN n 
3 21  ALA n 
3 22  ARG n 
3 23  ARG n 
3 24  GLU n 
3 25  MET n 
3 26  LEU n 
3 27  GLU n 
3 28  HIS n 
3 29  HIS n 
3 30  HIS n 
3 31  HIS n 
3 32  HIS n 
3 33  HIS 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' 1 376 ?           ? 'malE, JW3994'  ? ? ? ? ? ? 'Escherichia coli #1/H766' 1354003 ? ? ? ? ? ? ? 
? 
;Escherichia coli 'BL21-Gold(DE3)pLysS AG'
;
866768 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 153 'Fruit fly' ? 'Cam, CG8472'   ? ? ? ? ? ? 'Drosophila melanogaster'  7227    ? ? ? ? ? ? ? 
? 
;Escherichia coli 'BL21-Gold(DE3)pLysS AG'
;
866768 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 33  'Fruit fly' ? 'rdgC, CG44746' ? ? ? ? ? ? 'Drosophila melanogaster'  7227    ? ? ? ? ? ? ? 
? 
;Escherichia coli 'BL21-Gold(DE3)pLysS AG'
;
866768 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CA  non-polymer         . 'CALCIUM ION'   ? 'Ca 2'           40.078  
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   1   1   MET MET A . n 
A 1 2   LYS 2   2   2   LYS LYS A . n 
A 1 3   ILE 3   3   3   ILE ILE A . n 
A 1 4   GLU 4   4   4   GLU GLU A . n 
A 1 5   GLU 5   5   5   GLU GLU A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   LYS 7   7   7   LYS LYS A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   VAL 9   9   9   VAL VAL A . n 
A 1 10  ILE 10  10  10  ILE ILE A . n 
A 1 11  TRP 11  11  11  TRP TRP A . n 
A 1 12  ILE 12  12  12  ILE ILE A . n 
A 1 13  ASN 13  13  13  ASN ASN A . n 
A 1 14  GLY 14  14  14  GLY GLY A . n 
A 1 15  ASP 15  15  15  ASP ASP A . n 
A 1 16  LYS 16  16  16  LYS LYS A . n 
A 1 17  GLY 17  17  17  GLY GLY A . n 
A 1 18  TYR 18  18  18  TYR TYR A . n 
A 1 19  ASN 19  19  19  ASN ASN A . n 
A 1 20  GLY 20  20  20  GLY GLY A . n 
A 1 21  LEU 21  21  21  LEU LEU A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  GLU 23  23  23  GLU GLU A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  LYS 26  26  26  LYS LYS A . n 
A 1 27  LYS 27  27  27  LYS LYS A . n 
A 1 28  PHE 28  28  28  PHE PHE A . n 
A 1 29  GLU 29  29  29  GLU GLU A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  ASP 31  31  31  ASP ASP A . n 
A 1 32  THR 32  32  32  THR THR A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  ILE 34  34  34  ILE ILE A . n 
A 1 35  LYS 35  35  35  LYS LYS A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  VAL 38  38  38  VAL VAL A . n 
A 1 39  GLU 39  39  39  GLU GLU A . n 
A 1 40  HIS 40  40  40  HIS HIS A . n 
A 1 41  PRO 41  41  41  PRO PRO A . n 
A 1 42  ASP 42  42  42  ASP ASP A . n 
A 1 43  LYS 43  43  43  LYS LYS A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  GLU 45  45  45  GLU GLU A . n 
A 1 46  GLU 46  46  46  GLU GLU A . n 
A 1 47  LYS 47  47  47  LYS LYS A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  PRO 49  49  49  PRO PRO A . n 
A 1 50  GLN 50  50  50  GLN GLN A . n 
A 1 51  VAL 51  51  51  VAL VAL A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  ALA 53  53  53  ALA ALA A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  GLY 55  55  55  GLY GLY A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  GLY 57  57  57  GLY GLY A . n 
A 1 58  PRO 58  58  58  PRO PRO A . n 
A 1 59  ASP 59  59  59  ASP ASP A . n 
A 1 60  ILE 60  60  60  ILE ILE A . n 
A 1 61  ILE 61  61  61  ILE ILE A . n 
A 1 62  PHE 62  62  62  PHE PHE A . n 
A 1 63  TRP 63  63  63  TRP TRP A . n 
A 1 64  ALA 64  64  64  ALA ALA A . n 
A 1 65  HIS 65  65  65  HIS HIS A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ARG 67  67  67  ARG ARG A . n 
A 1 68  PHE 68  68  68  PHE PHE A . n 
A 1 69  GLY 69  69  69  GLY GLY A . n 
A 1 70  GLY 70  70  70  GLY GLY A . n 
A 1 71  TYR 71  71  71  TYR TYR A . n 
A 1 72  ALA 72  72  72  ALA ALA A . n 
A 1 73  GLN 73  73  73  GLN GLN A . n 
A 1 74  SER 74  74  74  SER SER A . n 
A 1 75  GLY 75  75  75  GLY GLY A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  ALA 78  78  78  ALA ALA A . n 
A 1 79  GLU 79  79  79  GLU GLU A . n 
A 1 80  ILE 80  80  80  ILE ILE A . n 
A 1 81  THR 81  81  81  THR THR A . n 
A 1 82  PRO 82  82  82  PRO PRO A . n 
A 1 83  ALA 83  83  83  ALA ALA A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  ALA 85  85  85  ALA ALA A . n 
A 1 86  PHE 86  86  86  PHE PHE A . n 
A 1 87  GLN 87  87  87  GLN GLN A . n 
A 1 88  ASP 88  88  88  ASP ASP A . n 
A 1 89  LYS 89  89  89  LYS LYS A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  TYR 91  91  91  TYR TYR A . n 
A 1 92  PRO 92  92  92  PRO PRO A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  THR 94  94  94  THR THR A . n 
A 1 95  TRP 95  95  95  TRP TRP A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  VAL 98  98  98  VAL VAL A . n 
A 1 99  ARG 99  99  99  ARG ARG A . n 
A 1 100 TYR 100 100 100 TYR TYR A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 LYS 103 103 103 LYS LYS A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 ILE 105 105 105 ILE ILE A . n 
A 1 106 ALA 106 106 106 ALA ALA A . n 
A 1 107 TYR 107 107 107 TYR TYR A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 ILE 109 109 109 ILE ILE A . n 
A 1 110 ALA 110 110 110 ALA ALA A . n 
A 1 111 VAL 111 111 111 VAL VAL A . n 
A 1 112 GLU 112 112 112 GLU GLU A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 LEU 114 114 114 LEU LEU A . n 
A 1 115 SER 115 115 115 SER SER A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 ILE 117 117 117 ILE ILE A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 ASN 119 119 119 ASN ASN A . n 
A 1 120 LYS 120 120 120 LYS LYS A . n 
A 1 121 ASP 121 121 121 ASP ASP A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 PRO 124 124 124 PRO PRO A . n 
A 1 125 ASN 125 125 125 ASN ASN A . n 
A 1 126 PRO 126 126 126 PRO PRO A . n 
A 1 127 PRO 127 127 127 PRO PRO A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 THR 129 129 129 THR THR A . n 
A 1 130 TRP 130 130 130 TRP TRP A . n 
A 1 131 GLU 131 131 131 GLU GLU A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 ILE 133 133 133 ILE ILE A . n 
A 1 134 PRO 134 134 134 PRO PRO A . n 
A 1 135 ALA 135 135 135 ALA ALA A . n 
A 1 136 LEU 136 136 136 LEU LEU A . n 
A 1 137 ASP 137 137 137 ASP ASP A . n 
A 1 138 LYS 138 138 138 LYS LYS A . n 
A 1 139 GLU 139 139 139 GLU GLU A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 LYS 141 141 141 LYS LYS A . n 
A 1 142 ALA 142 142 142 ALA ALA A . n 
A 1 143 LYS 143 143 143 LYS LYS A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 LYS 145 145 145 LYS LYS A . n 
A 1 146 SER 146 146 146 SER SER A . n 
A 1 147 ALA 147 147 147 ALA ALA A . n 
A 1 148 LEU 148 148 148 LEU LEU A . n 
A 1 149 MET 149 149 149 MET MET A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 ASN 151 151 151 ASN ASN A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 GLN 153 153 153 GLN GLN A . n 
A 1 154 GLU 154 154 154 GLU GLU A . n 
A 1 155 PRO 155 155 155 PRO PRO A . n 
A 1 156 TYR 156 156 156 TYR TYR A . n 
A 1 157 PHE 157 157 157 PHE PHE A . n 
A 1 158 THR 158 158 158 THR THR A . n 
A 1 159 TRP 159 159 159 TRP TRP A . n 
A 1 160 PRO 160 160 160 PRO PRO A . n 
A 1 161 LEU 161 161 161 LEU LEU A . n 
A 1 162 ILE 162 162 162 ILE ILE A . n 
A 1 163 ALA 163 163 163 ALA ALA A . n 
A 1 164 ALA 164 164 164 ALA ALA A . n 
A 1 165 ASP 165 165 165 ASP ASP A . n 
A 1 166 GLY 166 166 166 GLY GLY A . n 
A 1 167 GLY 167 167 167 GLY GLY A . n 
A 1 168 TYR 168 168 168 TYR TYR A . n 
A 1 169 ALA 169 169 169 ALA ALA A . n 
A 1 170 PHE 170 170 170 PHE PHE A . n 
A 1 171 LYS 171 171 171 LYS LYS A . n 
A 1 172 TYR 172 172 172 TYR TYR A . n 
A 1 173 ALA 173 173 ?   ?   ?   A . n 
A 1 174 ALA 174 174 174 ALA ALA A . n 
A 1 175 GLY 175 175 175 GLY GLY A . n 
A 1 176 LYS 176 176 176 LYS LYS A . n 
A 1 177 TYR 177 177 177 TYR TYR A . n 
A 1 178 ASP 178 178 178 ASP ASP A . n 
A 1 179 ILE 179 179 179 ILE ILE A . n 
A 1 180 LYS 180 180 180 LYS LYS A . n 
A 1 181 ASP 181 181 181 ASP ASP A . n 
A 1 182 VAL 182 182 182 VAL VAL A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 VAL 184 184 184 VAL VAL A . n 
A 1 185 ASP 185 185 185 ASP ASP A . n 
A 1 186 ASN 186 186 186 ASN ASN A . n 
A 1 187 ALA 187 187 187 ALA ALA A . n 
A 1 188 GLY 188 188 188 GLY GLY A . n 
A 1 189 ALA 189 189 189 ALA ALA A . n 
A 1 190 LYS 190 190 190 LYS LYS A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 GLY 192 192 192 GLY GLY A . n 
A 1 193 LEU 193 193 193 LEU LEU A . n 
A 1 194 THR 194 194 194 THR THR A . n 
A 1 195 PHE 195 195 195 PHE PHE A . n 
A 1 196 LEU 196 196 196 LEU LEU A . n 
A 1 197 VAL 197 197 197 VAL VAL A . n 
A 1 198 ASP 198 198 198 ASP ASP A . n 
A 1 199 LEU 199 199 199 LEU LEU A . n 
A 1 200 ILE 200 200 200 ILE ILE A . n 
A 1 201 LYS 201 201 201 LYS LYS A . n 
A 1 202 ASN 202 202 202 ASN ASN A . n 
A 1 203 LYS 203 203 203 LYS LYS A . n 
A 1 204 HIS 204 204 204 HIS HIS A . n 
A 1 205 MET 205 205 205 MET MET A . n 
A 1 206 ASN 206 206 206 ASN ASN A . n 
A 1 207 ALA 207 207 207 ALA ALA A . n 
A 1 208 ASP 208 208 208 ASP ASP A . n 
A 1 209 THR 209 209 209 THR THR A . n 
A 1 210 ASP 210 210 210 ASP ASP A . n 
A 1 211 TYR 211 211 211 TYR TYR A . n 
A 1 212 SER 212 212 212 SER SER A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 ALA 214 214 214 ALA ALA A . n 
A 1 215 GLU 215 215 215 GLU GLU A . n 
A 1 216 ALA 216 216 216 ALA ALA A . n 
A 1 217 ALA 217 217 217 ALA ALA A . n 
A 1 218 PHE 218 218 218 PHE PHE A . n 
A 1 219 ASN 219 219 219 ASN ASN A . n 
A 1 220 LYS 220 220 220 LYS LYS A . n 
A 1 221 GLY 221 221 221 GLY GLY A . n 
A 1 222 GLU 222 222 222 GLU GLU A . n 
A 1 223 THR 223 223 223 THR THR A . n 
A 1 224 ALA 224 224 224 ALA ALA A . n 
A 1 225 MET 225 225 225 MET MET A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 ILE 227 227 227 ILE ILE A . n 
A 1 228 ASN 228 228 228 ASN ASN A . n 
A 1 229 GLY 229 229 229 GLY GLY A . n 
A 1 230 PRO 230 230 230 PRO PRO A . n 
A 1 231 TRP 231 231 231 TRP TRP A . n 
A 1 232 ALA 232 232 232 ALA ALA A . n 
A 1 233 TRP 233 233 233 TRP TRP A . n 
A 1 234 SER 234 234 234 SER SER A . n 
A 1 235 ASN 235 235 235 ASN ASN A . n 
A 1 236 ILE 236 236 236 ILE ILE A . n 
A 1 237 ASP 237 237 237 ASP ASP A . n 
A 1 238 THR 238 238 238 THR THR A . n 
A 1 239 SER 239 239 239 SER SER A . n 
A 1 240 ALA 240 240 240 ALA ALA A . n 
A 1 241 VAL 241 241 241 VAL VAL A . n 
A 1 242 ASN 242 242 242 ASN ASN A . n 
A 1 243 TYR 243 243 243 TYR TYR A . n 
A 1 244 GLY 244 244 244 GLY GLY A . n 
A 1 245 VAL 245 245 245 VAL VAL A . n 
A 1 246 THR 246 246 246 THR THR A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 LEU 248 248 248 LEU LEU A . n 
A 1 249 PRO 249 249 249 PRO PRO A . n 
A 1 250 THR 250 250 250 THR THR A . n 
A 1 251 PHE 251 251 251 PHE PHE A . n 
A 1 252 LYS 252 252 252 LYS LYS A . n 
A 1 253 GLY 253 253 253 GLY GLY A . n 
A 1 254 GLN 254 254 254 GLN GLN A . n 
A 1 255 PRO 255 255 255 PRO PRO A . n 
A 1 256 SER 256 256 256 SER SER A . n 
A 1 257 LYS 257 257 257 LYS LYS A . n 
A 1 258 PRO 258 258 258 PRO PRO A . n 
A 1 259 PHE 259 259 259 PHE PHE A . n 
A 1 260 VAL 260 260 260 VAL VAL A . n 
A 1 261 GLY 261 261 261 GLY GLY A . n 
A 1 262 VAL 262 262 262 VAL VAL A . n 
A 1 263 LEU 263 263 263 LEU LEU A . n 
A 1 264 SER 264 264 264 SER SER A . n 
A 1 265 ALA 265 265 265 ALA ALA A . n 
A 1 266 GLY 266 266 266 GLY GLY A . n 
A 1 267 ILE 267 267 267 ILE ILE A . n 
A 1 268 ASN 268 268 268 ASN ASN A . n 
A 1 269 ALA 269 269 269 ALA ALA A . n 
A 1 270 ALA 270 270 270 ALA ALA A . n 
A 1 271 SER 271 271 271 SER SER A . n 
A 1 272 PRO 272 272 272 PRO PRO A . n 
A 1 273 ASN 273 273 273 ASN ASN A . n 
A 1 274 LYS 274 274 274 LYS LYS A . n 
A 1 275 GLU 275 275 275 GLU GLU A . n 
A 1 276 LEU 276 276 276 LEU LEU A . n 
A 1 277 ALA 277 277 277 ALA ALA A . n 
A 1 278 LYS 278 278 278 LYS LYS A . n 
A 1 279 GLU 279 279 279 GLU GLU A . n 
A 1 280 PHE 280 280 280 PHE PHE A . n 
A 1 281 LEU 281 281 281 LEU LEU A . n 
A 1 282 GLU 282 282 282 GLU GLU A . n 
A 1 283 ASN 283 283 283 ASN ASN A . n 
A 1 284 TYR 284 284 284 TYR TYR A . n 
A 1 285 LEU 285 285 285 LEU LEU A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 THR 287 287 287 THR THR A . n 
A 1 288 ASP 288 288 288 ASP ASP A . n 
A 1 289 GLU 289 289 289 GLU GLU A . n 
A 1 290 GLY 290 290 290 GLY GLY A . n 
A 1 291 LEU 291 291 291 LEU LEU A . n 
A 1 292 GLU 292 292 292 GLU GLU A . n 
A 1 293 ALA 293 293 293 ALA ALA A . n 
A 1 294 VAL 294 294 294 VAL VAL A . n 
A 1 295 ASN 295 295 295 ASN ASN A . n 
A 1 296 LYS 296 296 296 LYS LYS A . n 
A 1 297 ASP 297 297 297 ASP ASP A . n 
A 1 298 LYS 298 298 298 LYS LYS A . n 
A 1 299 PRO 299 299 299 PRO PRO A . n 
A 1 300 LEU 300 300 300 LEU LEU A . n 
A 1 301 GLY 301 301 301 GLY GLY A . n 
A 1 302 ALA 302 302 302 ALA ALA A . n 
A 1 303 VAL 303 303 303 VAL VAL A . n 
A 1 304 ALA 304 304 304 ALA ALA A . n 
A 1 305 LEU 305 305 305 LEU LEU A . n 
A 1 306 LYS 306 306 306 LYS LYS A . n 
A 1 307 SER 307 307 307 SER SER A . n 
A 1 308 TYR 308 308 308 TYR TYR A . n 
A 1 309 GLU 309 309 309 GLU GLU A . n 
A 1 310 GLU 310 310 310 GLU GLU A . n 
A 1 311 GLU 311 311 311 GLU GLU A . n 
A 1 312 LEU 312 312 312 LEU LEU A . n 
A 1 313 ALA 313 313 313 ALA ALA A . n 
A 1 314 LYS 314 314 314 LYS LYS A . n 
A 1 315 ASP 315 315 315 ASP ASP A . n 
A 1 316 PRO 316 316 316 PRO PRO A . n 
A 1 317 ARG 317 317 317 ARG ARG A . n 
A 1 318 ILE 318 318 318 ILE ILE A . n 
A 1 319 ALA 319 319 319 ALA ALA A . n 
A 1 320 ALA 320 320 320 ALA ALA A . n 
A 1 321 THR 321 321 321 THR THR A . n 
A 1 322 MET 322 322 322 MET MET A . n 
A 1 323 GLU 323 323 323 GLU GLU A . n 
A 1 324 ASN 324 324 324 ASN ASN A . n 
A 1 325 ALA 325 325 325 ALA ALA A . n 
A 1 326 GLN 326 326 326 GLN GLN A . n 
A 1 327 LYS 327 327 327 LYS LYS A . n 
A 1 328 GLY 328 328 328 GLY GLY A . n 
A 1 329 GLU 329 329 329 GLU GLU A . n 
A 1 330 ILE 330 330 330 ILE ILE A . n 
A 1 331 MET 331 331 331 MET MET A . n 
A 1 332 PRO 332 332 332 PRO PRO A . n 
A 1 333 ASN 333 333 333 ASN ASN A . n 
A 1 334 ILE 334 334 334 ILE ILE A . n 
A 1 335 PRO 335 335 335 PRO PRO A . n 
A 1 336 GLN 336 336 336 GLN GLN A . n 
A 1 337 MET 337 337 337 MET MET A . n 
A 1 338 SER 338 338 338 SER SER A . n 
A 1 339 ALA 339 339 339 ALA ALA A . n 
A 1 340 PHE 340 340 340 PHE PHE A . n 
A 1 341 TRP 341 341 341 TRP TRP A . n 
A 1 342 TYR 342 342 342 TYR TYR A . n 
A 1 343 ALA 343 343 343 ALA ALA A . n 
A 1 344 VAL 344 344 344 VAL VAL A . n 
A 1 345 ARG 345 345 345 ARG ARG A . n 
A 1 346 THR 346 346 346 THR THR A . n 
A 1 347 ALA 347 347 347 ALA ALA A . n 
A 1 348 VAL 348 348 348 VAL VAL A . n 
A 1 349 ILE 349 349 349 ILE ILE A . n 
A 1 350 ASN 350 350 350 ASN ASN A . n 
A 1 351 ALA 351 351 351 ALA ALA A . n 
A 1 352 ALA 352 352 352 ALA ALA A . n 
A 1 353 SER 353 353 353 SER SER A . n 
A 1 354 GLY 354 354 354 GLY GLY A . n 
A 1 355 ARG 355 355 355 ARG ARG A . n 
A 1 356 GLN 356 356 356 GLN GLN A . n 
A 1 357 THR 357 357 357 THR THR A . n 
A 1 358 VAL 358 358 358 VAL VAL A . n 
A 1 359 ASP 359 359 359 ASP ASP A . n 
A 1 360 ALA 360 360 360 ALA ALA A . n 
A 1 361 ALA 361 361 361 ALA ALA A . n 
A 1 362 LEU 362 362 362 LEU LEU A . n 
A 1 363 ALA 363 363 363 ALA ALA A . n 
A 1 364 ALA 364 364 364 ALA ALA A . n 
A 1 365 ALA 365 365 365 ALA ALA A . n 
A 1 366 GLN 366 366 366 GLN GLN A . n 
A 1 367 THR 367 367 367 THR THR A . n 
A 1 368 ASN 368 368 368 ASN ASN A . n 
A 1 369 ALA 369 369 369 ALA ALA A . n 
A 1 370 ALA 370 370 370 ALA ALA A . n 
A 1 371 ARG 371 371 ?   ?   ?   A . n 
A 1 372 ALA 372 372 ?   ?   ?   A . n 
A 1 373 PHE 373 373 ?   ?   ?   A . n 
A 1 374 ALA 374 374 ?   ?   ?   A . n 
A 1 375 ALA 375 375 ?   ?   ?   A . n 
A 1 376 ALA 376 376 ?   ?   ?   A . n 
B 2 1   GLY 1   -6  ?   ?   ?   N . n 
B 2 2   PRO 2   -5  ?   ?   ?   N . n 
B 2 3   GLY 3   -4  ?   ?   ?   N . n 
B 2 4   SER 4   -3  ?   ?   ?   N . n 
B 2 5   MET 5   -2  ?   ?   ?   N . n 
B 2 6   ALA 6   -1  ?   ?   ?   N . n 
B 2 7   ASP 7   0   ?   ?   ?   N . n 
B 2 8   GLN 8   1   ?   ?   ?   N . n 
B 2 9   LEU 9   2   ?   ?   ?   N . n 
B 2 10  THR 10  3   3   THR THR N . n 
B 2 11  GLU 11  4   4   GLU GLU N . n 
B 2 12  GLU 12  5   5   GLU GLU N . n 
B 2 13  GLN 13  6   6   GLN GLN N . n 
B 2 14  ILE 14  7   7   ILE ILE N . n 
B 2 15  ALA 15  8   8   ALA ALA N . n 
B 2 16  GLU 16  9   9   GLU GLU N . n 
B 2 17  PHE 17  10  10  PHE PHE N . n 
B 2 18  LYS 18  11  11  LYS LYS N . n 
B 2 19  GLU 19  12  12  GLU GLU N . n 
B 2 20  ALA 20  13  13  ALA ALA N . n 
B 2 21  PHE 21  14  14  PHE PHE N . n 
B 2 22  SER 22  15  15  SER SER N . n 
B 2 23  LEU 23  16  16  LEU LEU N . n 
B 2 24  PHE 24  17  17  PHE PHE N . n 
B 2 25  ASP 25  18  18  ASP ASP N . n 
B 2 26  LYS 26  19  19  LYS LYS N . n 
B 2 27  ASP 27  20  20  ASP ASP N . n 
B 2 28  GLY 28  21  21  GLY GLY N . n 
B 2 29  ASP 29  22  22  ASP ASP N . n 
B 2 30  GLY 30  23  23  GLY GLY N . n 
B 2 31  THR 31  24  24  THR THR N . n 
B 2 32  ILE 32  25  25  ILE ILE N . n 
B 2 33  THR 33  26  26  THR THR N . n 
B 2 34  THR 34  27  27  THR THR N . n 
B 2 35  LYS 35  28  28  LYS LYS N . n 
B 2 36  GLU 36  29  29  GLU GLU N . n 
B 2 37  LEU 37  30  30  LEU LEU N . n 
B 2 38  GLY 38  31  31  GLY GLY N . n 
B 2 39  THR 39  32  32  THR THR N . n 
B 2 40  VAL 40  33  33  VAL VAL N . n 
B 2 41  MET 41  34  34  MET MET N . n 
B 2 42  ARG 42  35  35  ARG ARG N . n 
B 2 43  SER 43  36  36  SER SER N . n 
B 2 44  LEU 44  37  37  LEU LEU N . n 
B 2 45  GLY 45  38  38  GLY GLY N . n 
B 2 46  GLN 46  39  39  GLN GLN N . n 
B 2 47  ASN 47  40  40  ASN ASN N . n 
B 2 48  PRO 48  41  41  PRO PRO N . n 
B 2 49  THR 49  42  42  THR THR N . n 
B 2 50  GLU 50  43  43  GLU GLU N . n 
B 2 51  ALA 51  44  44  ALA ALA N . n 
B 2 52  GLU 52  45  45  GLU GLU N . n 
B 2 53  LEU 53  46  46  LEU LEU N . n 
B 2 54  GLN 54  47  47  GLN GLN N . n 
B 2 55  ASP 55  48  48  ASP ASP N . n 
B 2 56  MET 56  49  49  MET MET N . n 
B 2 57  ILE 57  50  50  ILE ILE N . n 
B 2 58  ASN 58  51  51  ASN ASN N . n 
B 2 59  GLU 59  52  52  GLU GLU N . n 
B 2 60  VAL 60  53  53  VAL VAL N . n 
B 2 61  ASP 61  54  54  ASP ASP N . n 
B 2 62  ALA 62  55  55  ALA ALA N . n 
B 2 63  ASP 63  56  56  ASP ASP N . n 
B 2 64  GLY 64  57  57  GLY GLY N . n 
B 2 65  ASN 65  58  58  ASN ASN N . n 
B 2 66  GLY 66  59  59  GLY GLY N . n 
B 2 67  THR 67  60  60  THR THR N . n 
B 2 68  ILE 68  61  61  ILE ILE N . n 
B 2 69  ASP 69  62  62  ASP ASP N . n 
B 2 70  PHE 70  63  63  PHE PHE N . n 
B 2 71  PRO 71  64  64  PRO PRO N . n 
B 2 72  GLU 72  65  65  GLU GLU N . n 
B 2 73  PHE 73  66  66  PHE PHE N . n 
B 2 74  LEU 74  67  67  LEU LEU N . n 
B 2 75  THR 75  68  68  THR THR N . n 
B 2 76  MET 76  69  69  MET MET N . n 
B 2 77  MET 77  70  70  MET MET N . n 
B 2 78  ALA 78  71  71  ALA ALA N . n 
B 2 79  ARG 79  72  72  ARG ARG N . n 
B 2 80  LYS 80  73  ?   ?   ?   N . n 
B 2 81  MET 81  74  ?   ?   ?   N . n 
B 2 82  LYS 82  75  ?   ?   ?   N . n 
B 2 83  ASP 83  76  76  ASP ASP N . n 
B 2 84  THR 84  77  77  THR THR N . n 
B 2 85  ASP 85  78  78  ASP ASP N . n 
B 2 86  SER 86  79  79  SER SER N . n 
B 2 87  GLU 87  80  80  GLU GLU N . n 
B 2 88  GLU 88  81  81  GLU GLU N . n 
B 2 89  GLU 89  82  82  GLU GLU N . n 
B 2 90  ILE 90  83  83  ILE ILE N . n 
B 2 91  ARG 91  84  84  ARG ARG N . n 
B 2 92  GLU 92  85  85  GLU GLU N . n 
B 2 93  ALA 93  86  86  ALA ALA N . n 
B 2 94  PHE 94  87  87  PHE PHE N . n 
B 2 95  ARG 95  88  88  ARG ARG N . n 
B 2 96  VAL 96  89  89  VAL VAL N . n 
B 2 97  PHE 97  90  90  PHE PHE N . n 
B 2 98  ASP 98  91  91  ASP ASP N . n 
B 2 99  LYS 99  92  92  LYS LYS N . n 
B 2 100 ASP 100 93  93  ASP ASP N . n 
B 2 101 GLY 101 94  94  GLY GLY N . n 
B 2 102 ASN 102 95  95  ASN ASN N . n 
B 2 103 GLY 103 96  96  GLY GLY N . n 
B 2 104 PHE 104 97  97  PHE PHE N . n 
B 2 105 ILE 105 98  98  ILE ILE N . n 
B 2 106 SER 106 99  99  SER SER N . n 
B 2 107 ALA 107 100 100 ALA ALA N . n 
B 2 108 ALA 108 101 101 ALA ALA N . n 
B 2 109 GLU 109 102 102 GLU GLU N . n 
B 2 110 LEU 110 103 103 LEU LEU N . n 
B 2 111 ARG 111 104 104 ARG ARG N . n 
B 2 112 HIS 112 105 105 HIS HIS N . n 
B 2 113 VAL 113 106 106 VAL VAL N . n 
B 2 114 MET 114 107 107 MET MET N . n 
B 2 115 THR 115 108 108 THR THR N . n 
B 2 116 ASN 116 109 109 ASN ASN N . n 
B 2 117 LEU 117 110 110 LEU LEU N . n 
B 2 118 GLY 118 111 111 GLY GLY N . n 
B 2 119 GLU 119 112 112 GLU GLU N . n 
B 2 120 LYS 120 113 113 LYS LYS N . n 
B 2 121 LEU 121 114 114 LEU LEU N . n 
B 2 122 THR 122 115 115 THR THR N . n 
B 2 123 ASP 123 116 116 ASP ASP N . n 
B 2 124 GLU 124 117 117 GLU GLU N . n 
B 2 125 GLU 125 118 118 GLU GLU N . n 
B 2 126 VAL 126 119 119 VAL VAL N . n 
B 2 127 ASP 127 120 120 ASP ASP N . n 
B 2 128 GLU 128 121 121 GLU GLU N . n 
B 2 129 MET 129 122 122 MET MET N . n 
B 2 130 ILE 130 123 123 ILE ILE N . n 
B 2 131 ARG 131 124 124 ARG ARG N . n 
B 2 132 GLU 132 125 125 GLU GLU N . n 
B 2 133 ALA 133 126 126 ALA ALA N . n 
B 2 134 ASP 134 127 127 ASP ASP N . n 
B 2 135 ILE 135 128 128 ILE ILE N . n 
B 2 136 ASP 136 129 129 ASP ASP N . n 
B 2 137 GLY 137 130 130 GLY GLY N . n 
B 2 138 ASP 138 131 131 ASP ASP N . n 
B 2 139 GLY 139 132 132 GLY GLY N . n 
B 2 140 GLN 140 133 133 GLN GLN N . n 
B 2 141 VAL 141 134 134 VAL VAL N . n 
B 2 142 ASN 142 135 135 ASN ASN N . n 
B 2 143 TYR 143 136 136 TYR TYR N . n 
B 2 144 GLU 144 137 137 GLU GLU N . n 
B 2 145 GLU 145 138 138 GLU GLU N . n 
B 2 146 PHE 146 139 139 PHE PHE N . n 
B 2 147 VAL 147 140 140 VAL VAL N . n 
B 2 148 THR 148 141 141 THR THR N . n 
B 2 149 MET 149 142 142 MET MET N . n 
B 2 150 MET 150 143 143 MET MET N . n 
B 2 151 THR 151 144 144 THR THR N . n 
B 2 152 SER 152 145 145 SER SER N . n 
B 2 153 LYS 153 146 146 LYS LYS N . n 
C 3 1   MET 1   1   ?   ?   ?   R . n 
C 3 2   ASP 2   2   2   ASP ASP R . n 
C 3 3   GLU 3   2   2   GLU GLU R A n 
C 3 4   ASN 4   2   2   ASN ASN R B n 
C 3 5   ALA 5   2   2   ALA ALA R C n 
C 3 6   ILE 6   2   2   ILE ILE R D n 
C 3 7   ARG 7   2   2   ARG ARG R E n 
C 3 8   ALA 8   2   2   ALA ALA R F n 
C 3 9   ALA 9   2   2   ALA ALA R G n 
C 3 10  ILE 10  2   2   ILE ILE R H n 
C 3 11  PHE 11  2   2   PHE PHE R I n 
C 3 12  ILE 12  2   2   ILE ILE R J n 
C 3 13  GLN 13  3   3   GLN GLN R . n 
C 3 14  LYS 14  4   4   LYS LYS R . n 
C 3 15  TRP 15  5   5   TRP TRP R . n 
C 3 16  TYR 16  6   6   TYR TYR R . n 
C 3 17  ARG 17  7   7   ARG ARG R . n 
C 3 18  ARG 18  8   8   ARG ARG R . n 
C 3 19  HIS 19  9   9   HIS HIS R . n 
C 3 20  GLN 20  10  10  GLN GLN R . n 
C 3 21  ALA 21  11  11  ALA ALA R . n 
C 3 22  ARG 22  12  12  ARG ARG R . n 
C 3 23  ARG 23  13  13  ARG ARG R . n 
C 3 24  GLU 24  14  14  GLU GLU R . n 
C 3 25  MET 25  15  15  MET MET R . n 
C 3 26  LEU 26  16  16  LEU LEU R . n 
C 3 27  GLU 27  17  17  GLU GLU R . n 
C 3 28  HIS 28  18  18  HIS HIS R . n 
C 3 29  HIS 29  19  19  HIS HIS R . n 
C 3 30  HIS 30  20  20  HIS HIS R . n 
C 3 31  HIS 31  21  ?   ?   ?   R . n 
C 3 32  HIS 32  22  ?   ?   ?   R . n 
C 3 33  HIS 33  23  ?   ?   ?   R . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        CA 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   CA 
_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 
D 4 CA  1  201 1  CA  CA  N . 
E 4 CA  1  202 4  CA  CA  N . 
F 4 CA  1  203 5  CA  CA  N . 
G 4 CA  1  204 6  CA  CA  N . 
H 5 HOH 1  401 36 HOH HOH A . 
H 5 HOH 2  402 31 HOH HOH A . 
H 5 HOH 3  403 55 HOH HOH A . 
H 5 HOH 4  404 35 HOH HOH A . 
H 5 HOH 5  405 2  HOH HOH A . 
H 5 HOH 6  406 10 HOH HOH A . 
H 5 HOH 7  407 15 HOH HOH A . 
H 5 HOH 8  408 3  HOH HOH A . 
H 5 HOH 9  409 51 HOH HOH A . 
H 5 HOH 10 410 32 HOH HOH A . 
H 5 HOH 11 411 4  HOH HOH A . 
H 5 HOH 12 412 57 HOH HOH A . 
H 5 HOH 13 413 37 HOH HOH A . 
H 5 HOH 14 414 9  HOH HOH A . 
H 5 HOH 15 415 12 HOH HOH A . 
H 5 HOH 16 416 17 HOH HOH A . 
H 5 HOH 17 417 30 HOH HOH A . 
H 5 HOH 18 418 1  HOH HOH A . 
H 5 HOH 19 419 21 HOH HOH A . 
H 5 HOH 20 420 20 HOH HOH A . 
H 5 HOH 21 421 28 HOH HOH A . 
H 5 HOH 22 422 22 HOH HOH A . 
H 5 HOH 23 423 33 HOH HOH A . 
H 5 HOH 24 424 19 HOH HOH A . 
H 5 HOH 25 425 6  HOH HOH A . 
H 5 HOH 26 426 38 HOH HOH A . 
H 5 HOH 27 427 53 HOH HOH A . 
H 5 HOH 28 428 54 HOH HOH A . 
H 5 HOH 29 429 5  HOH HOH A . 
H 5 HOH 30 430 41 HOH HOH A . 
H 5 HOH 31 431 48 HOH HOH A . 
H 5 HOH 32 432 34 HOH HOH A . 
H 5 HOH 33 433 25 HOH HOH A . 
H 5 HOH 34 434 27 HOH HOH A . 
H 5 HOH 35 435 40 HOH HOH A . 
H 5 HOH 36 436 45 HOH HOH A . 
H 5 HOH 37 437 18 HOH HOH A . 
H 5 HOH 38 438 52 HOH HOH A . 
H 5 HOH 39 439 63 HOH HOH A . 
H 5 HOH 40 440 24 HOH HOH A . 
H 5 HOH 41 441 42 HOH HOH A . 
H 5 HOH 42 442 60 HOH HOH A . 
I 5 HOH 1  301 13 HOH HOH N . 
I 5 HOH 2  302 23 HOH HOH N . 
I 5 HOH 3  303 47 HOH HOH N . 
I 5 HOH 4  304 29 HOH HOH N . 
I 5 HOH 5  305 49 HOH HOH N . 
I 5 HOH 6  306 62 HOH HOH N . 
I 5 HOH 7  307 26 HOH HOH N . 
I 5 HOH 8  308 56 HOH HOH N . 
I 5 HOH 9  309 8  HOH HOH N . 
I 5 HOH 10 310 61 HOH HOH N . 
I 5 HOH 11 311 7  HOH HOH N . 
I 5 HOH 12 312 64 HOH HOH N . 
J 5 HOH 1  101 16 HOH HOH R . 
J 5 HOH 2  102 50 HOH HOH R . 
J 5 HOH 3  103 14 HOH HOH R . 
J 5 HOH 4  104 58 HOH HOH R . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A MET 1   ? CG  ? A MET 1   CG  
2  1 Y 1 A MET 1   ? SD  ? A MET 1   SD  
3  1 Y 1 A MET 1   ? CE  ? A MET 1   CE  
4  1 Y 1 A LYS 2   ? CG  ? A LYS 2   CG  
5  1 Y 1 A LYS 2   ? CD  ? A LYS 2   CD  
6  1 Y 1 A LYS 2   ? CE  ? A LYS 2   CE  
7  1 Y 1 A LYS 2   ? NZ  ? A LYS 2   NZ  
8  1 Y 1 A LYS 176 ? CG  ? A LYS 176 CG  
9  1 Y 1 A LYS 176 ? CD  ? A LYS 176 CD  
10 1 Y 1 A LYS 176 ? CE  ? A LYS 176 CE  
11 1 Y 1 A LYS 176 ? NZ  ? A LYS 176 NZ  
12 1 Y 1 A LYS 180 ? CG  ? A LYS 180 CG  
13 1 Y 1 A LYS 180 ? CD  ? A LYS 180 CD  
14 1 Y 1 A LYS 180 ? CE  ? A LYS 180 CE  
15 1 Y 1 A LYS 180 ? NZ  ? A LYS 180 NZ  
16 1 Y 1 A LYS 296 ? CG  ? A LYS 296 CG  
17 1 Y 1 A LYS 296 ? CD  ? A LYS 296 CD  
18 1 Y 1 A LYS 296 ? CE  ? A LYS 296 CE  
19 1 Y 1 A LYS 296 ? NZ  ? A LYS 296 NZ  
20 1 Y 1 A GLN 336 ? CG  ? A GLN 336 CG  
21 1 Y 1 A GLN 336 ? CD  ? A GLN 336 CD  
22 1 Y 1 A GLN 336 ? OE1 ? A GLN 336 OE1 
23 1 Y 1 A GLN 336 ? NE2 ? A GLN 336 NE2 
24 1 Y 1 A ARG 355 ? CG  ? A ARG 355 CG  
25 1 Y 1 A ARG 355 ? CD  ? A ARG 355 CD  
26 1 Y 1 A ARG 355 ? NE  ? A ARG 355 NE  
27 1 Y 1 A ARG 355 ? CZ  ? A ARG 355 CZ  
28 1 Y 1 A ARG 355 ? NH1 ? A ARG 355 NH1 
29 1 Y 1 A ARG 355 ? NH2 ? A ARG 355 NH2 
30 1 Y 1 A ASN 368 ? CG  ? A ASN 368 CG  
31 1 Y 1 A ASN 368 ? OD1 ? A ASN 368 OD1 
32 1 Y 1 A ASN 368 ? ND2 ? A ASN 368 ND2 
33 1 Y 1 N LYS 11  ? CG  ? B LYS 18  CG  
34 1 Y 1 N LYS 11  ? CD  ? B LYS 18  CD  
35 1 Y 1 N LYS 11  ? CE  ? B LYS 18  CE  
36 1 Y 1 N LYS 11  ? NZ  ? B LYS 18  NZ  
37 1 Y 1 N ARG 72  ? CG  ? B ARG 79  CG  
38 1 Y 1 N ARG 72  ? CD  ? B ARG 79  CD  
39 1 Y 1 N ARG 72  ? NE  ? B ARG 79  NE  
40 1 Y 1 N ARG 72  ? CZ  ? B ARG 79  CZ  
41 1 Y 1 N ARG 72  ? NH1 ? B ARG 79  NH1 
42 1 Y 1 N ARG 72  ? NH2 ? B ARG 79  NH2 
43 1 Y 1 N SER 79  ? OG  ? B SER 86  OG  
44 1 Y 1 R ASP 2   ? CG  ? C ASP 2   CG  
45 1 Y 1 R ASP 2   ? OD1 ? C ASP 2   OD1 
46 1 Y 1 R ASP 2   ? OD2 ? C ASP 2   OD2 
# 
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   ? ? ? '(1.19.2_4158: ???)' 1 
? 'data scaling' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .                    2 
? phasing        ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .                    3 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   94.17 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8ZLW 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     52.664 
_cell.length_a_esd                 ? 
_cell.length_b                     61.590 
_cell.length_b_esd                 ? 
_cell.length_c                     88.002 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_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                         8ZLW 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8ZLW 
_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             2.38 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.37 
_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    '2 % v/v Tacsimate pH 4.0, 0.1 M Sodium acetate trihydrate pH 4.6, 16 % w/v PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_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 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         2022-01-08 
_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   0.97853 
_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                        'SSRF BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97853 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8ZLW 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.200 
_reflns.d_resolution_low                               29.26 
_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                                     28328 
_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                           98.68 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.10 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.163 
_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                                    2.200 
_reflns_shell.d_res_low                                     2.279 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             28328 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_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                                  0.554 
_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                               ? 
_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                                 8ZLW 
_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                            2.20 
_refine.ls_d_res_low                             29.26 
_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                     28328 
_refine.ls_number_reflns_R_free                  1389 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.68 
_refine.ls_percent_reflns_R_free                 4.90 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2180 
_refine.ls_R_factor_R_free                       0.2536 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2162 
_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                          1.38 
_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               NONE 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_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             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 29.60 
_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                            0.34 
_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                       2.20 
_refine_hist.d_res_low                        29.26 
_refine_hist.number_atoms_solvent             58 
_refine_hist.number_atoms_total               4219 
_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        4157 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         4 
_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' ? 0.008 ? 4243 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.949 ? 5752 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 6.088 ? 565  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.056 ? 630  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007 ? 758  ? f_plane_restr      ? ? 
# 
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' 2.20 2.28  . . 140 2652 99.00  . . . . 0.3321 . . . . . . . . . . . 0.3429 
'X-RAY DIFFRACTION' 2.28 2.37  . . 134 2683 99.00  . . . . 0.2977 . . . . . . . . . . . 0.3727 
'X-RAY DIFFRACTION' 2.37 2.48  . . 134 2721 100.00 . . . . 0.2616 . . . . . . . . . . . 0.2926 
'X-RAY DIFFRACTION' 2.48 2.61  . . 152 2686 99.00  . . . . 0.2480 . . . . . . . . . . . 0.3197 
'X-RAY DIFFRACTION' 2.61 2.77  . . 143 2677 98.00  . . . . 0.2400 . . . . . . . . . . . 0.2934 
'X-RAY DIFFRACTION' 2.77 2.99  . . 135 2650 98.00  . . . . 0.2485 . . . . . . . . . . . 0.3012 
'X-RAY DIFFRACTION' 2.99 3.29  . . 144 2715 99.00  . . . . 0.2389 . . . . . . . . . . . 0.2728 
'X-RAY DIFFRACTION' 3.29 3.76  . . 129 2723 99.00  . . . . 0.2155 . . . . . . . . . . . 0.2561 
'X-RAY DIFFRACTION' 3.76 4.73  . . 140 2684 97.00  . . . . 0.1750 . . . . . . . . . . . 0.1795 
'X-RAY DIFFRACTION' 4.73 29.26 . . 138 2748 98.00  . . . . 0.1741 . . . . . . . . . . . 0.2225 
# 
_struct.entry_id                     8ZLW 
_struct.title                        'Crystal Structure of RDGC IQ motif/dCaM Complex' 
_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        8ZLW 
_struct_keywords.text            'complex serine-threonine phosphatase, 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 ? 
F N N 4 ? 
G N N 4 ? 
H N N 5 ? 
I N N 5 ? 
J N N 5 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP A0A4P1LXE0_SERSF A0A4P1LXE0 ? 1 
;KIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEIT
PDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPL
IAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKV
NYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAAT
MENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTNAA
;
3 
2 UNP CALM_DROME       P62152     ? 2 
;MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDT
DSEEEIREAFRVFDKDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVTMMTSK
;
1 
3 UNP RDGC_DROME       P40421     ? 3 MDENAIRAAIFIQKWYRRHQARREM 1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8ZLW A 2 ? 370 ? A0A4P1LXE0 3 ? 371 ? 2  370 
2 2 8ZLW N 5 ? 153 ? P62152     1 ? 149 ? -2 146 
3 3 8ZLW R 1 ? 25  ? P40421     1 ? 25  ? 1  15  
# 
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 8ZLW MET A 1   ? UNP A0A4P1LXE0 ?   ?   'initiating methionine' 1   1  
1 8ZLW ALA A 83  ? UNP A0A4P1LXE0 ASP 84  conflict                83  2  
1 8ZLW ALA A 84  ? UNP A0A4P1LXE0 LYS 85  conflict                84  3  
1 8ZLW ALA A 173 ? UNP A0A4P1LXE0 GLU 174 conflict                173 4  
1 8ZLW ALA A 174 ? UNP A0A4P1LXE0 ASN 175 conflict                174 5  
1 8ZLW ALA A 240 ? UNP A0A4P1LXE0 LYS 241 conflict                240 6  
1 8ZLW ALA A 360 ? UNP A0A4P1LXE0 GLU 361 conflict                360 7  
1 8ZLW ALA A 363 ? UNP A0A4P1LXE0 LYS 364 conflict                363 8  
1 8ZLW ALA A 364 ? UNP A0A4P1LXE0 ASP 365 conflict                364 9  
1 8ZLW ARG A 371 ? UNP A0A4P1LXE0 ?   ?   'expression tag'        371 10 
1 8ZLW ALA A 372 ? UNP A0A4P1LXE0 ?   ?   'expression tag'        372 11 
1 8ZLW PHE A 373 ? UNP A0A4P1LXE0 ?   ?   'expression tag'        373 12 
1 8ZLW ALA A 374 ? UNP A0A4P1LXE0 ?   ?   'expression tag'        374 13 
1 8ZLW ALA A 375 ? UNP A0A4P1LXE0 ?   ?   'expression tag'        375 14 
1 8ZLW ALA A 376 ? UNP A0A4P1LXE0 ?   ?   'expression tag'        376 15 
2 8ZLW GLY N 1   ? UNP P62152     ?   ?   'expression tag'        -6  16 
2 8ZLW PRO N 2   ? UNP P62152     ?   ?   'expression tag'        -5  17 
2 8ZLW GLY N 3   ? UNP P62152     ?   ?   'expression tag'        -4  18 
2 8ZLW SER N 4   ? UNP P62152     ?   ?   'expression tag'        -3  19 
3 8ZLW LEU R 26  ? UNP P40421     ?   ?   'expression tag'        16  20 
3 8ZLW GLU R 27  ? UNP P40421     ?   ?   'expression tag'        17  21 
3 8ZLW HIS R 28  ? UNP P40421     ?   ?   'expression tag'        18  22 
3 8ZLW HIS R 29  ? UNP P40421     ?   ?   'expression tag'        19  23 
3 8ZLW HIS R 30  ? UNP P40421     ?   ?   'expression tag'        20  24 
3 8ZLW HIS R 31  ? UNP P40421     ?   ?   'expression tag'        21  25 
3 8ZLW HIS R 32  ? UNP P40421     ?   ?   'expression tag'        22  26 
3 8ZLW HIS R 33  ? UNP P40421     ?   ?   'expression tag'        23  27 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 17  ? THR A 32  ? GLY A 17  THR A 32  1 ? 16 
HELX_P HELX_P2  AA2 LYS A 43  ? ALA A 52  ? LYS A 43  ALA A 52  1 ? 10 
HELX_P HELX_P3  AA3 ALA A 53  ? GLY A 55  ? ALA A 53  GLY A 55  5 ? 3  
HELX_P HELX_P4  AA4 ARG A 67  ? SER A 74  ? ARG A 67  SER A 74  1 ? 8  
HELX_P HELX_P5  AA5 ALA A 83  ? LYS A 89  ? ALA A 83  LYS A 89  1 ? 7  
HELX_P HELX_P6  AA6 TYR A 91  ? ASP A 96  ? TYR A 91  ASP A 96  1 ? 6  
HELX_P HELX_P7  AA7 GLU A 132 ? ALA A 142 ? GLU A 132 ALA A 142 1 ? 11 
HELX_P HELX_P8  AA8 GLU A 154 ? ASP A 165 ? GLU A 154 ASP A 165 1 ? 12 
HELX_P HELX_P9  AA9 ASN A 186 ? ASN A 202 ? ASN A 186 ASN A 202 1 ? 17 
HELX_P HELX_P10 AB1 ASP A 210 ? LYS A 220 ? ASP A 210 LYS A 220 1 ? 11 
HELX_P HELX_P11 AB2 GLY A 229 ? TRP A 231 ? GLY A 229 TRP A 231 5 ? 3  
HELX_P HELX_P12 AB3 ALA A 232 ? ALA A 240 ? ALA A 232 ALA A 240 1 ? 9  
HELX_P HELX_P13 AB4 ASN A 273 ? GLU A 282 ? ASN A 273 GLU A 282 1 ? 10 
HELX_P HELX_P14 AB5 THR A 287 ? LYS A 298 ? THR A 287 LYS A 298 1 ? 12 
HELX_P HELX_P15 AB6 LEU A 305 ? ALA A 313 ? LEU A 305 ALA A 313 1 ? 9  
HELX_P HELX_P16 AB7 ASP A 315 ? LYS A 327 ? ASP A 315 LYS A 327 1 ? 13 
HELX_P HELX_P17 AB8 GLN A 336 ? SER A 353 ? GLN A 336 SER A 353 1 ? 18 
HELX_P HELX_P18 AB9 THR A 357 ? ASN A 368 ? THR A 357 ASN A 368 1 ? 12 
HELX_P HELX_P19 AC1 GLU B 11  ? ASP B 25  ? GLU N 4   ASP N 18  1 ? 15 
HELX_P HELX_P20 AC2 THR B 33  ? LEU B 44  ? THR N 26  LEU N 37  1 ? 12 
HELX_P HELX_P21 AC3 THR B 49  ? GLU B 59  ? THR N 42  GLU N 52  1 ? 11 
HELX_P HELX_P22 AC4 PHE B 70  ? ARG B 79  ? PHE N 63  ARG N 72  1 ? 10 
HELX_P HELX_P23 AC5 ASP B 85  ? ASP B 98  ? ASP N 78  ASP N 91  1 ? 14 
HELX_P HELX_P24 AC6 SER B 106 ? GLY B 118 ? SER N 99  GLY N 111 1 ? 13 
HELX_P HELX_P25 AC7 THR B 122 ? ASP B 134 ? THR N 115 ASP N 127 1 ? 13 
HELX_P HELX_P26 AC8 ASN B 142 ? SER B 152 ? ASN N 135 SER N 145 1 ? 11 
HELX_P HELX_P27 AC9 GLU C 3   A GLU C 27  ? GLU R 2   GLU R 17  1 ? 25 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? B ASP 25  OD1 ? ? ? 1_555 F CA . CA ? ? N ASP 18  N CA 203 1_555 ? ? ? ? ? ? ? 2.438 ? ? 
metalc2  metalc ? ? B ASP 27  OD1 ? ? ? 1_555 F CA . CA ? ? N ASP 20  N CA 203 1_555 ? ? ? ? ? ? ? 2.490 ? ? 
metalc3  metalc ? ? B ASP 29  OD1 ? ? ? 1_555 F CA . CA ? ? N ASP 22  N CA 203 1_555 ? ? ? ? ? ? ? 2.439 ? ? 
metalc4  metalc ? ? B THR 31  O   ? ? ? 1_555 F CA . CA ? ? N THR 24  N CA 203 1_555 ? ? ? ? ? ? ? 2.319 ? ? 
metalc5  metalc ? ? B GLU 36  OE1 ? ? ? 1_555 F CA . CA ? ? N GLU 29  N CA 203 1_555 ? ? ? ? ? ? ? 2.436 ? ? 
metalc6  metalc ? ? B GLU 36  OE2 ? ? ? 1_555 F CA . CA ? ? N GLU 29  N CA 203 1_555 ? ? ? ? ? ? ? 2.508 ? ? 
metalc7  metalc ? ? B ASP 61  OD1 ? ? ? 1_555 E CA . CA ? ? N ASP 54  N CA 202 1_555 ? ? ? ? ? ? ? 2.397 ? ? 
metalc8  metalc ? ? B ASN 65  OD1 ? ? ? 1_555 E CA . CA ? ? N ASN 58  N CA 202 1_555 ? ? ? ? ? ? ? 2.419 ? ? 
metalc9  metalc ? ? B THR 67  O   ? ? ? 1_555 E CA . CA ? ? N THR 60  N CA 202 1_555 ? ? ? ? ? ? ? 2.348 ? ? 
metalc10 metalc ? ? B GLU 72  OE1 ? ? ? 1_555 E CA . CA ? ? N GLU 65  N CA 202 1_555 ? ? ? ? ? ? ? 2.554 ? ? 
metalc11 metalc ? ? B GLU 72  OE2 ? ? ? 1_555 E CA . CA ? ? N GLU 65  N CA 202 1_555 ? ? ? ? ? ? ? 2.641 ? ? 
metalc12 metalc ? ? B ASP 100 OD2 ? ? ? 1_555 G CA . CA ? ? N ASP 93  N CA 204 1_555 ? ? ? ? ? ? ? 3.003 ? ? 
metalc13 metalc ? ? B ASN 102 OD1 ? ? ? 1_555 G CA . CA ? ? N ASN 95  N CA 204 1_555 ? ? ? ? ? ? ? 3.164 ? ? 
metalc14 metalc ? ? B ASP 134 OD1 ? ? ? 1_555 D CA . CA ? ? N ASP 127 N CA 201 1_555 ? ? ? ? ? ? ? 2.291 ? ? 
metalc15 metalc ? ? B ASP 136 OD1 ? ? ? 1_555 D CA . CA ? ? N ASP 129 N CA 201 1_555 ? ? ? ? ? ? ? 2.367 ? ? 
metalc16 metalc ? ? B ASP 138 OD1 ? ? ? 1_555 D CA . CA ? ? N ASP 131 N CA 201 1_555 ? ? ? ? ? ? ? 2.370 ? ? 
metalc17 metalc ? ? B GLN 140 O   ? ? ? 1_555 D CA . CA ? ? N GLN 133 N CA 201 1_555 ? ? ? ? ? ? ? 2.280 ? ? 
metalc18 metalc ? ? B GLU 145 OE1 ? ? ? 1_555 D CA . CA ? ? N GLU 138 N CA 201 1_555 ? ? ? ? ? ? ? 2.573 ? ? 
metalc19 metalc ? ? B GLU 145 OE2 ? ? ? 1_555 D CA . CA ? ? N GLU 138 N CA 201 1_555 ? ? ? ? ? ? ? 2.429 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD1 ? B ASP 25  ? N ASP 18  ? 1_555 CA ? F CA . ? N CA 203 ? 1_555 OD1 ? B ASP 27  ? N ASP 20  ? 1_555 67.9  ? 
2  OD1 ? B ASP 25  ? N ASP 18  ? 1_555 CA ? F CA . ? N CA 203 ? 1_555 OD1 ? B ASP 29  ? N ASP 22  ? 1_555 72.9  ? 
3  OD1 ? B ASP 27  ? N ASP 20  ? 1_555 CA ? F CA . ? N CA 203 ? 1_555 OD1 ? B ASP 29  ? N ASP 22  ? 1_555 76.6  ? 
4  OD1 ? B ASP 25  ? N ASP 18  ? 1_555 CA ? F CA . ? N CA 203 ? 1_555 O   ? B THR 31  ? N THR 24  ? 1_555 77.0  ? 
5  OD1 ? B ASP 27  ? N ASP 20  ? 1_555 CA ? F CA . ? N CA 203 ? 1_555 O   ? B THR 31  ? N THR 24  ? 1_555 142.5 ? 
6  OD1 ? B ASP 29  ? N ASP 22  ? 1_555 CA ? F CA . ? N CA 203 ? 1_555 O   ? B THR 31  ? N THR 24  ? 1_555 80.8  ? 
7  OD1 ? B ASP 25  ? N ASP 18  ? 1_555 CA ? F CA . ? N CA 203 ? 1_555 OE1 ? B GLU 36  ? N GLU 29  ? 1_555 114.4 ? 
8  OD1 ? B ASP 27  ? N ASP 20  ? 1_555 CA ? F CA . ? N CA 203 ? 1_555 OE1 ? B GLU 36  ? N GLU 29  ? 1_555 128.3 ? 
9  OD1 ? B ASP 29  ? N ASP 22  ? 1_555 CA ? F CA . ? N CA 203 ? 1_555 OE1 ? B GLU 36  ? N GLU 29  ? 1_555 155.1 ? 
10 O   ? B THR 31  ? N THR 24  ? 1_555 CA ? F CA . ? N CA 203 ? 1_555 OE1 ? B GLU 36  ? N GLU 29  ? 1_555 78.0  ? 
11 OD1 ? B ASP 25  ? N ASP 18  ? 1_555 CA ? F CA . ? N CA 203 ? 1_555 OE2 ? B GLU 36  ? N GLU 29  ? 1_555 91.0  ? 
12 OD1 ? B ASP 27  ? N ASP 20  ? 1_555 CA ? F CA . ? N CA 203 ? 1_555 OE2 ? B GLU 36  ? N GLU 29  ? 1_555 75.3  ? 
13 OD1 ? B ASP 29  ? N ASP 22  ? 1_555 CA ? F CA . ? N CA 203 ? 1_555 OE2 ? B GLU 36  ? N GLU 29  ? 1_555 151.2 ? 
14 O   ? B THR 31  ? N THR 24  ? 1_555 CA ? F CA . ? N CA 203 ? 1_555 OE2 ? B GLU 36  ? N GLU 29  ? 1_555 119.5 ? 
15 OE1 ? B GLU 36  ? N GLU 29  ? 1_555 CA ? F CA . ? N CA 203 ? 1_555 OE2 ? B GLU 36  ? N GLU 29  ? 1_555 53.5  ? 
16 OD1 ? B ASP 61  ? N ASP 54  ? 1_555 CA ? E CA . ? N CA 202 ? 1_555 OD1 ? B ASN 65  ? N ASN 58  ? 1_555 71.8  ? 
17 OD1 ? B ASP 61  ? N ASP 54  ? 1_555 CA ? E CA . ? N CA 202 ? 1_555 O   ? B THR 67  ? N THR 60  ? 1_555 72.1  ? 
18 OD1 ? B ASN 65  ? N ASN 58  ? 1_555 CA ? E CA . ? N CA 202 ? 1_555 O   ? B THR 67  ? N THR 60  ? 1_555 81.6  ? 
19 OD1 ? B ASP 61  ? N ASP 54  ? 1_555 CA ? E CA . ? N CA 202 ? 1_555 OE1 ? B GLU 72  ? N GLU 65  ? 1_555 110.4 ? 
20 OD1 ? B ASN 65  ? N ASN 58  ? 1_555 CA ? E CA . ? N CA 202 ? 1_555 OE1 ? B GLU 72  ? N GLU 65  ? 1_555 163.8 ? 
21 O   ? B THR 67  ? N THR 60  ? 1_555 CA ? E CA . ? N CA 202 ? 1_555 OE1 ? B GLU 72  ? N GLU 65  ? 1_555 83.9  ? 
22 OD1 ? B ASP 61  ? N ASP 54  ? 1_555 CA ? E CA . ? N CA 202 ? 1_555 OE2 ? B GLU 72  ? N GLU 65  ? 1_555 85.1  ? 
23 OD1 ? B ASN 65  ? N ASN 58  ? 1_555 CA ? E CA . ? N CA 202 ? 1_555 OE2 ? B GLU 72  ? N GLU 65  ? 1_555 145.0 ? 
24 O   ? B THR 67  ? N THR 60  ? 1_555 CA ? E CA . ? N CA 202 ? 1_555 OE2 ? B GLU 72  ? N GLU 65  ? 1_555 116.5 ? 
25 OE1 ? B GLU 72  ? N GLU 65  ? 1_555 CA ? E CA . ? N CA 202 ? 1_555 OE2 ? B GLU 72  ? N GLU 65  ? 1_555 49.8  ? 
26 OD2 ? B ASP 100 ? N ASP 93  ? 1_555 CA ? G CA . ? N CA 204 ? 1_555 OD1 ? B ASN 102 ? N ASN 95  ? 1_555 80.6  ? 
27 OD1 ? B ASP 134 ? N ASP 127 ? 1_555 CA ? D CA . ? N CA 201 ? 1_555 OD1 ? B ASP 136 ? N ASP 129 ? 1_555 77.9  ? 
28 OD1 ? B ASP 134 ? N ASP 127 ? 1_555 CA ? D CA . ? N CA 201 ? 1_555 OD1 ? B ASP 138 ? N ASP 131 ? 1_555 87.2  ? 
29 OD1 ? B ASP 136 ? N ASP 129 ? 1_555 CA ? D CA . ? N CA 201 ? 1_555 OD1 ? B ASP 138 ? N ASP 131 ? 1_555 79.4  ? 
30 OD1 ? B ASP 134 ? N ASP 127 ? 1_555 CA ? D CA . ? N CA 201 ? 1_555 O   ? B GLN 140 ? N GLN 133 ? 1_555 92.4  ? 
31 OD1 ? B ASP 136 ? N ASP 129 ? 1_555 CA ? D CA . ? N CA 201 ? 1_555 O   ? B GLN 140 ? N GLN 133 ? 1_555 154.8 ? 
32 OD1 ? B ASP 138 ? N ASP 131 ? 1_555 CA ? D CA . ? N CA 201 ? 1_555 O   ? B GLN 140 ? N GLN 133 ? 1_555 76.9  ? 
33 OD1 ? B ASP 134 ? N ASP 127 ? 1_555 CA ? D CA . ? N CA 201 ? 1_555 OE1 ? B GLU 145 ? N GLU 138 ? 1_555 116.9 ? 
34 OD1 ? B ASP 136 ? N ASP 129 ? 1_555 CA ? D CA . ? N CA 201 ? 1_555 OE1 ? B GLU 145 ? N GLU 138 ? 1_555 124.4 ? 
35 OD1 ? B ASP 138 ? N ASP 131 ? 1_555 CA ? D CA . ? N CA 201 ? 1_555 OE1 ? B GLU 145 ? N GLU 138 ? 1_555 147.7 ? 
36 O   ? B GLN 140 ? N GLN 133 ? 1_555 CA ? D CA . ? N CA 201 ? 1_555 OE1 ? B GLU 145 ? N GLU 138 ? 1_555 80.8  ? 
37 OD1 ? B ASP 134 ? N ASP 127 ? 1_555 CA ? D CA . ? N CA 201 ? 1_555 OE2 ? B GLU 145 ? N GLU 138 ? 1_555 86.6  ? 
38 OD1 ? B ASP 136 ? N ASP 129 ? 1_555 CA ? D CA . ? N CA 201 ? 1_555 OE2 ? B GLU 145 ? N GLU 138 ? 1_555 78.1  ? 
39 OD1 ? B ASP 138 ? N ASP 131 ? 1_555 CA ? D CA . ? N CA 201 ? 1_555 OE2 ? B GLU 145 ? N GLU 138 ? 1_555 157.4 ? 
40 O   ? B GLN 140 ? N GLN 133 ? 1_555 CA ? D CA . ? N CA 201 ? 1_555 OE2 ? B GLU 145 ? N GLU 138 ? 1_555 125.1 ? 
41 OE1 ? B GLU 145 ? N GLU 138 ? 1_555 CA ? D CA . ? N CA 201 ? 1_555 OE2 ? B GLU 145 ? N GLU 138 ? 1_555 52.2  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 5 ? 
AA3 ? 2 ? 
AA4 ? 4 ? 
AA5 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? parallel      
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? 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 VAL A 36  ? GLU A 39  ? VAL A 36  GLU A 39  
AA1 2 LEU A 8   ? TRP A 11  ? LEU A 8   TRP A 11  
AA1 3 ILE A 60  ? ALA A 64  ? ILE A 60  ALA A 64  
AA1 4 PHE A 259 ? ILE A 267 ? PHE A 259 ILE A 267 
AA1 5 TYR A 107 ? GLU A 112 ? TYR A 107 GLU A 112 
AA1 6 ALA A 302 ? VAL A 303 ? ALA A 302 VAL A 303 
AA2 1 VAL A 36  ? GLU A 39  ? VAL A 36  GLU A 39  
AA2 2 LEU A 8   ? TRP A 11  ? LEU A 8   TRP A 11  
AA2 3 ILE A 60  ? ALA A 64  ? ILE A 60  ALA A 64  
AA2 4 PHE A 259 ? ILE A 267 ? PHE A 259 ILE A 267 
AA2 5 GLU A 329 ? ILE A 330 ? GLU A 329 ILE A 330 
AA3 1 ARG A 99  ? TYR A 100 ? ARG A 99  TYR A 100 
AA3 2 LYS A 103 ? LEU A 104 ? LYS A 103 LEU A 104 
AA4 1 SER A 146 ? LEU A 148 ? SER A 146 LEU A 148 
AA4 2 THR A 223 ? ASN A 228 ? THR A 223 ASN A 228 
AA4 3 SER A 115 ? ASN A 119 ? SER A 115 ASN A 119 
AA4 4 TYR A 243 ? THR A 246 ? TYR A 243 THR A 246 
AA5 1 THR B 31  ? ILE B 32  ? THR N 24  ILE N 25  
AA5 2 ILE B 68  ? ASP B 69  ? ILE N 61  ASP N 62  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O GLU A 39  ? O GLU A 39  N ILE A 10  ? N ILE A 10  
AA1 2 3 N TRP A 11  ? N TRP A 11  O PHE A 62  ? O PHE A 62  
AA1 3 4 N ILE A 61  ? N ILE A 61  O GLY A 266 ? O GLY A 266 
AA1 4 5 O ALA A 265 ? O ALA A 265 N TYR A 107 ? N TYR A 107 
AA1 5 6 N VAL A 111 ? N VAL A 111 O ALA A 302 ? O ALA A 302 
AA2 1 2 O GLU A 39  ? O GLU A 39  N ILE A 10  ? N ILE A 10  
AA2 2 3 N TRP A 11  ? N TRP A 11  O PHE A 62  ? O PHE A 62  
AA2 3 4 N ILE A 61  ? N ILE A 61  O GLY A 266 ? O GLY A 266 
AA2 4 5 N VAL A 260 ? N VAL A 260 O GLU A 329 ? O GLU A 329 
AA3 1 2 N TYR A 100 ? N TYR A 100 O LYS A 103 ? O LYS A 103 
AA4 1 2 N SER A 146 ? N SER A 146 O ALA A 224 ? O ALA A 224 
AA4 2 3 O ALA A 224 ? O ALA A 224 N ASN A 119 ? N ASN A 119 
AA4 3 4 N TYR A 118 ? N TYR A 118 O GLY A 244 ? O GLY A 244 
AA5 1 2 N ILE B 32  ? N ILE N 25  O ILE B 68  ? O ILE N 61  
# 
_pdbx_entry_details.entry_id                   8ZLW 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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 ALA A 53  ? ? -106.62 52.95   
2 1 ILE A 109 ? ? -121.19 -61.68  
3 1 LEU A 123 ? ? -155.07 79.27   
4 1 LYS A 145 ? ? -114.78 -166.99 
5 1 ASP A 210 ? ? -120.66 -161.15 
6 1 LYS A 257 ? ? -117.47 79.27   
7 1 ASN A 368 ? ? -63.85  0.55    
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A ALA 173 ? A ALA 173 
2  1 Y 1 A ARG 371 ? A ARG 371 
3  1 Y 1 A ALA 372 ? A ALA 372 
4  1 Y 1 A PHE 373 ? A PHE 373 
5  1 Y 1 A ALA 374 ? A ALA 374 
6  1 Y 1 A ALA 375 ? A ALA 375 
7  1 Y 1 A ALA 376 ? A ALA 376 
8  1 Y 1 N GLY -6  ? B GLY 1   
9  1 Y 1 N PRO -5  ? B PRO 2   
10 1 Y 1 N GLY -4  ? B GLY 3   
11 1 Y 1 N SER -3  ? B SER 4   
12 1 Y 1 N MET -2  ? B MET 5   
13 1 Y 1 N ALA -1  ? B ALA 6   
14 1 Y 1 N ASP 0   ? B ASP 7   
15 1 Y 1 N GLN 1   ? B GLN 8   
16 1 Y 1 N LEU 2   ? B LEU 9   
17 1 Y 1 N LYS 73  ? B LYS 80  
18 1 Y 1 N MET 74  ? B MET 81  
19 1 Y 1 N LYS 75  ? B LYS 82  
20 1 Y 1 R MET 1   ? C MET 1   
21 1 Y 1 R HIS 21  ? C HIS 31  
22 1 Y 1 R HIS 22  ? C HIS 32  
23 1 Y 1 R HIS 23  ? C HIS 33  
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CA  CA   CA N N 74  
GLN N    N  N N 75  
GLN CA   C  N S 76  
GLN C    C  N N 77  
GLN O    O  N N 78  
GLN CB   C  N N 79  
GLN CG   C  N N 80  
GLN CD   C  N N 81  
GLN OE1  O  N N 82  
GLN NE2  N  N N 83  
GLN OXT  O  N N 84  
GLN H    H  N N 85  
GLN H2   H  N N 86  
GLN HA   H  N N 87  
GLN HB2  H  N N 88  
GLN HB3  H  N N 89  
GLN HG2  H  N N 90  
GLN HG3  H  N N 91  
GLN HE21 H  N N 92  
GLN HE22 H  N N 93  
GLN HXT  H  N N 94  
GLU N    N  N N 95  
GLU CA   C  N S 96  
GLU C    C  N N 97  
GLU O    O  N N 98  
GLU CB   C  N N 99  
GLU CG   C  N N 100 
GLU CD   C  N N 101 
GLU OE1  O  N N 102 
GLU OE2  O  N N 103 
GLU OXT  O  N N 104 
GLU H    H  N N 105 
GLU H2   H  N N 106 
GLU HA   H  N N 107 
GLU HB2  H  N N 108 
GLU HB3  H  N N 109 
GLU HG2  H  N N 110 
GLU HG3  H  N N 111 
GLU HE2  H  N N 112 
GLU HXT  H  N N 113 
GLY N    N  N N 114 
GLY CA   C  N N 115 
GLY C    C  N N 116 
GLY O    O  N N 117 
GLY OXT  O  N N 118 
GLY H    H  N N 119 
GLY H2   H  N N 120 
GLY HA2  H  N N 121 
GLY HA3  H  N N 122 
GLY HXT  H  N N 123 
HIS N    N  N N 124 
HIS CA   C  N S 125 
HIS C    C  N N 126 
HIS O    O  N N 127 
HIS CB   C  N N 128 
HIS CG   C  Y N 129 
HIS ND1  N  Y N 130 
HIS CD2  C  Y N 131 
HIS CE1  C  Y N 132 
HIS NE2  N  Y N 133 
HIS OXT  O  N N 134 
HIS H    H  N N 135 
HIS H2   H  N N 136 
HIS HA   H  N N 137 
HIS HB2  H  N N 138 
HIS HB3  H  N N 139 
HIS HD1  H  N N 140 
HIS HD2  H  N N 141 
HIS HE1  H  N N 142 
HIS HE2  H  N N 143 
HIS HXT  H  N N 144 
HOH O    O  N N 145 
HOH H1   H  N N 146 
HOH H2   H  N N 147 
ILE N    N  N N 148 
ILE CA   C  N S 149 
ILE C    C  N N 150 
ILE O    O  N N 151 
ILE CB   C  N S 152 
ILE CG1  C  N N 153 
ILE CG2  C  N N 154 
ILE CD1  C  N N 155 
ILE OXT  O  N N 156 
ILE H    H  N N 157 
ILE H2   H  N N 158 
ILE HA   H  N N 159 
ILE HB   H  N N 160 
ILE HG12 H  N N 161 
ILE HG13 H  N N 162 
ILE HG21 H  N N 163 
ILE HG22 H  N N 164 
ILE HG23 H  N N 165 
ILE HD11 H  N N 166 
ILE HD12 H  N N 167 
ILE HD13 H  N N 168 
ILE HXT  H  N N 169 
LEU N    N  N N 170 
LEU CA   C  N S 171 
LEU C    C  N N 172 
LEU O    O  N N 173 
LEU CB   C  N N 174 
LEU CG   C  N N 175 
LEU CD1  C  N N 176 
LEU CD2  C  N N 177 
LEU OXT  O  N N 178 
LEU H    H  N N 179 
LEU H2   H  N N 180 
LEU HA   H  N N 181 
LEU HB2  H  N N 182 
LEU HB3  H  N N 183 
LEU HG   H  N N 184 
LEU HD11 H  N N 185 
LEU HD12 H  N N 186 
LEU HD13 H  N N 187 
LEU HD21 H  N N 188 
LEU HD22 H  N N 189 
LEU HD23 H  N N 190 
LEU HXT  H  N N 191 
LYS N    N  N N 192 
LYS CA   C  N S 193 
LYS C    C  N N 194 
LYS O    O  N N 195 
LYS CB   C  N N 196 
LYS CG   C  N N 197 
LYS CD   C  N N 198 
LYS CE   C  N N 199 
LYS NZ   N  N N 200 
LYS OXT  O  N N 201 
LYS H    H  N N 202 
LYS H2   H  N N 203 
LYS HA   H  N N 204 
LYS HB2  H  N N 205 
LYS HB3  H  N N 206 
LYS HG2  H  N N 207 
LYS HG3  H  N N 208 
LYS HD2  H  N N 209 
LYS HD3  H  N N 210 
LYS HE2  H  N N 211 
LYS HE3  H  N N 212 
LYS HZ1  H  N N 213 
LYS HZ2  H  N N 214 
LYS HZ3  H  N N 215 
LYS HXT  H  N N 216 
MET N    N  N N 217 
MET CA   C  N S 218 
MET C    C  N N 219 
MET O    O  N N 220 
MET CB   C  N N 221 
MET CG   C  N N 222 
MET SD   S  N N 223 
MET CE   C  N N 224 
MET OXT  O  N N 225 
MET H    H  N N 226 
MET H2   H  N N 227 
MET HA   H  N N 228 
MET HB2  H  N N 229 
MET HB3  H  N N 230 
MET HG2  H  N N 231 
MET HG3  H  N N 232 
MET HE1  H  N N 233 
MET HE2  H  N N 234 
MET HE3  H  N N 235 
MET HXT  H  N N 236 
PHE N    N  N N 237 
PHE CA   C  N S 238 
PHE C    C  N N 239 
PHE O    O  N N 240 
PHE CB   C  N N 241 
PHE CG   C  Y N 242 
PHE CD1  C  Y N 243 
PHE CD2  C  Y N 244 
PHE CE1  C  Y N 245 
PHE CE2  C  Y N 246 
PHE CZ   C  Y N 247 
PHE OXT  O  N N 248 
PHE H    H  N N 249 
PHE H2   H  N N 250 
PHE HA   H  N N 251 
PHE HB2  H  N N 252 
PHE HB3  H  N N 253 
PHE HD1  H  N N 254 
PHE HD2  H  N N 255 
PHE HE1  H  N N 256 
PHE HE2  H  N N 257 
PHE HZ   H  N N 258 
PHE HXT  H  N N 259 
PRO N    N  N N 260 
PRO CA   C  N S 261 
PRO C    C  N N 262 
PRO O    O  N N 263 
PRO CB   C  N N 264 
PRO CG   C  N N 265 
PRO CD   C  N N 266 
PRO OXT  O  N N 267 
PRO H    H  N N 268 
PRO HA   H  N N 269 
PRO HB2  H  N N 270 
PRO HB3  H  N N 271 
PRO HG2  H  N N 272 
PRO HG3  H  N N 273 
PRO HD2  H  N N 274 
PRO HD3  H  N N 275 
PRO HXT  H  N N 276 
SER N    N  N N 277 
SER CA   C  N S 278 
SER C    C  N N 279 
SER O    O  N N 280 
SER CB   C  N N 281 
SER OG   O  N N 282 
SER OXT  O  N N 283 
SER H    H  N N 284 
SER H2   H  N N 285 
SER HA   H  N N 286 
SER HB2  H  N N 287 
SER HB3  H  N N 288 
SER HG   H  N N 289 
SER HXT  H  N N 290 
THR N    N  N N 291 
THR CA   C  N S 292 
THR C    C  N N 293 
THR O    O  N N 294 
THR CB   C  N R 295 
THR OG1  O  N N 296 
THR CG2  C  N N 297 
THR OXT  O  N N 298 
THR H    H  N N 299 
THR H2   H  N N 300 
THR HA   H  N N 301 
THR HB   H  N N 302 
THR HG1  H  N N 303 
THR HG21 H  N N 304 
THR HG22 H  N N 305 
THR HG23 H  N N 306 
THR HXT  H  N N 307 
TRP N    N  N N 308 
TRP CA   C  N S 309 
TRP C    C  N N 310 
TRP O    O  N N 311 
TRP CB   C  N N 312 
TRP CG   C  Y N 313 
TRP CD1  C  Y N 314 
TRP CD2  C  Y N 315 
TRP NE1  N  Y N 316 
TRP CE2  C  Y N 317 
TRP CE3  C  Y N 318 
TRP CZ2  C  Y N 319 
TRP CZ3  C  Y N 320 
TRP CH2  C  Y N 321 
TRP OXT  O  N N 322 
TRP H    H  N N 323 
TRP H2   H  N N 324 
TRP HA   H  N N 325 
TRP HB2  H  N N 326 
TRP HB3  H  N N 327 
TRP HD1  H  N N 328 
TRP HE1  H  N N 329 
TRP HE3  H  N N 330 
TRP HZ2  H  N N 331 
TRP HZ3  H  N N 332 
TRP HH2  H  N N 333 
TRP HXT  H  N N 334 
TYR N    N  N N 335 
TYR CA   C  N S 336 
TYR C    C  N N 337 
TYR O    O  N N 338 
TYR CB   C  N N 339 
TYR CG   C  Y N 340 
TYR CD1  C  Y N 341 
TYR CD2  C  Y N 342 
TYR CE1  C  Y N 343 
TYR CE2  C  Y N 344 
TYR CZ   C  Y N 345 
TYR OH   O  N N 346 
TYR OXT  O  N N 347 
TYR H    H  N N 348 
TYR H2   H  N N 349 
TYR HA   H  N N 350 
TYR HB2  H  N N 351 
TYR HB3  H  N N 352 
TYR HD1  H  N N 353 
TYR HD2  H  N N 354 
TYR HE1  H  N N 355 
TYR HE2  H  N N 356 
TYR HH   H  N N 357 
TYR HXT  H  N N 358 
VAL N    N  N N 359 
VAL CA   C  N S 360 
VAL C    C  N N 361 
VAL O    O  N N 362 
VAL CB   C  N N 363 
VAL CG1  C  N N 364 
VAL CG2  C  N N 365 
VAL OXT  O  N N 366 
VAL H    H  N N 367 
VAL H2   H  N N 368 
VAL HA   H  N N 369 
VAL HB   H  N N 370 
VAL HG11 H  N N 371 
VAL HG12 H  N N 372 
VAL HG13 H  N N 373 
VAL HG21 H  N N 374 
VAL HG22 H  N N 375 
VAL HG23 H  N N 376 
VAL HXT  H  N N 377 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
HIS N   CA   sing N N 116 
HIS N   H    sing N N 117 
HIS N   H2   sing N N 118 
HIS CA  C    sing N N 119 
HIS CA  CB   sing N N 120 
HIS CA  HA   sing N N 121 
HIS C   O    doub N N 122 
HIS C   OXT  sing N N 123 
HIS CB  CG   sing N N 124 
HIS CB  HB2  sing N N 125 
HIS CB  HB3  sing N N 126 
HIS CG  ND1  sing Y N 127 
HIS CG  CD2  doub Y N 128 
HIS ND1 CE1  doub Y N 129 
HIS ND1 HD1  sing N N 130 
HIS CD2 NE2  sing Y N 131 
HIS CD2 HD2  sing N N 132 
HIS CE1 NE2  sing Y N 133 
HIS CE1 HE1  sing N N 134 
HIS NE2 HE2  sing N N 135 
HIS OXT HXT  sing N N 136 
HOH O   H1   sing N N 137 
HOH O   H2   sing N N 138 
ILE N   CA   sing N N 139 
ILE N   H    sing N N 140 
ILE N   H2   sing N N 141 
ILE CA  C    sing N N 142 
ILE CA  CB   sing N N 143 
ILE CA  HA   sing N N 144 
ILE C   O    doub N N 145 
ILE C   OXT  sing N N 146 
ILE CB  CG1  sing N N 147 
ILE CB  CG2  sing N N 148 
ILE CB  HB   sing N N 149 
ILE CG1 CD1  sing N N 150 
ILE CG1 HG12 sing N N 151 
ILE CG1 HG13 sing N N 152 
ILE CG2 HG21 sing N N 153 
ILE CG2 HG22 sing N N 154 
ILE CG2 HG23 sing N N 155 
ILE CD1 HD11 sing N N 156 
ILE CD1 HD12 sing N N 157 
ILE CD1 HD13 sing N N 158 
ILE OXT HXT  sing N N 159 
LEU N   CA   sing N N 160 
LEU N   H    sing N N 161 
LEU N   H2   sing N N 162 
LEU CA  C    sing N N 163 
LEU CA  CB   sing N N 164 
LEU CA  HA   sing N N 165 
LEU C   O    doub N N 166 
LEU C   OXT  sing N N 167 
LEU CB  CG   sing N N 168 
LEU CB  HB2  sing N N 169 
LEU CB  HB3  sing N N 170 
LEU CG  CD1  sing N N 171 
LEU CG  CD2  sing N N 172 
LEU CG  HG   sing N N 173 
LEU CD1 HD11 sing N N 174 
LEU CD1 HD12 sing N N 175 
LEU CD1 HD13 sing N N 176 
LEU CD2 HD21 sing N N 177 
LEU CD2 HD22 sing N N 178 
LEU CD2 HD23 sing N N 179 
LEU OXT HXT  sing N N 180 
LYS N   CA   sing N N 181 
LYS N   H    sing N N 182 
LYS N   H2   sing N N 183 
LYS CA  C    sing N N 184 
LYS CA  CB   sing N N 185 
LYS CA  HA   sing N N 186 
LYS C   O    doub N N 187 
LYS C   OXT  sing N N 188 
LYS CB  CG   sing N N 189 
LYS CB  HB2  sing N N 190 
LYS CB  HB3  sing N N 191 
LYS CG  CD   sing N N 192 
LYS CG  HG2  sing N N 193 
LYS CG  HG3  sing N N 194 
LYS CD  CE   sing N N 195 
LYS CD  HD2  sing N N 196 
LYS CD  HD3  sing N N 197 
LYS CE  NZ   sing N N 198 
LYS CE  HE2  sing N N 199 
LYS CE  HE3  sing N N 200 
LYS NZ  HZ1  sing N N 201 
LYS NZ  HZ2  sing N N 202 
LYS NZ  HZ3  sing N N 203 
LYS OXT HXT  sing N N 204 
MET N   CA   sing N N 205 
MET N   H    sing N N 206 
MET N   H2   sing N N 207 
MET CA  C    sing N N 208 
MET CA  CB   sing N N 209 
MET CA  HA   sing N N 210 
MET C   O    doub N N 211 
MET C   OXT  sing N N 212 
MET CB  CG   sing N N 213 
MET CB  HB2  sing N N 214 
MET CB  HB3  sing N N 215 
MET CG  SD   sing N N 216 
MET CG  HG2  sing N N 217 
MET CG  HG3  sing N N 218 
MET SD  CE   sing N N 219 
MET CE  HE1  sing N N 220 
MET CE  HE2  sing N N 221 
MET CE  HE3  sing N N 222 
MET OXT HXT  sing N N 223 
PHE N   CA   sing N N 224 
PHE N   H    sing N N 225 
PHE N   H2   sing N N 226 
PHE CA  C    sing N N 227 
PHE CA  CB   sing N N 228 
PHE CA  HA   sing N N 229 
PHE C   O    doub N N 230 
PHE C   OXT  sing N N 231 
PHE CB  CG   sing N N 232 
PHE CB  HB2  sing N N 233 
PHE CB  HB3  sing N N 234 
PHE CG  CD1  doub Y N 235 
PHE CG  CD2  sing Y N 236 
PHE CD1 CE1  sing Y N 237 
PHE CD1 HD1  sing N N 238 
PHE CD2 CE2  doub Y N 239 
PHE CD2 HD2  sing N N 240 
PHE CE1 CZ   doub Y N 241 
PHE CE1 HE1  sing N N 242 
PHE CE2 CZ   sing Y N 243 
PHE CE2 HE2  sing N N 244 
PHE CZ  HZ   sing N N 245 
PHE OXT HXT  sing N N 246 
PRO N   CA   sing N N 247 
PRO N   CD   sing N N 248 
PRO N   H    sing N N 249 
PRO CA  C    sing N N 250 
PRO CA  CB   sing N N 251 
PRO CA  HA   sing N N 252 
PRO C   O    doub N N 253 
PRO C   OXT  sing N N 254 
PRO CB  CG   sing N N 255 
PRO CB  HB2  sing N N 256 
PRO CB  HB3  sing N N 257 
PRO CG  CD   sing N N 258 
PRO CG  HG2  sing N N 259 
PRO CG  HG3  sing N N 260 
PRO CD  HD2  sing N N 261 
PRO CD  HD3  sing N N 262 
PRO OXT HXT  sing N N 263 
SER N   CA   sing N N 264 
SER N   H    sing N N 265 
SER N   H2   sing N N 266 
SER CA  C    sing N N 267 
SER CA  CB   sing N N 268 
SER CA  HA   sing N N 269 
SER C   O    doub N N 270 
SER C   OXT  sing N N 271 
SER CB  OG   sing N N 272 
SER CB  HB2  sing N N 273 
SER CB  HB3  sing N N 274 
SER OG  HG   sing N N 275 
SER OXT HXT  sing N N 276 
THR N   CA   sing N N 277 
THR N   H    sing N N 278 
THR N   H2   sing N N 279 
THR CA  C    sing N N 280 
THR CA  CB   sing N N 281 
THR CA  HA   sing N N 282 
THR C   O    doub N N 283 
THR C   OXT  sing N N 284 
THR CB  OG1  sing N N 285 
THR CB  CG2  sing N N 286 
THR CB  HB   sing N N 287 
THR OG1 HG1  sing N N 288 
THR CG2 HG21 sing N N 289 
THR CG2 HG22 sing N N 290 
THR CG2 HG23 sing N N 291 
THR OXT HXT  sing N N 292 
TRP N   CA   sing N N 293 
TRP N   H    sing N N 294 
TRP N   H2   sing N N 295 
TRP CA  C    sing N N 296 
TRP CA  CB   sing N N 297 
TRP CA  HA   sing N N 298 
TRP C   O    doub N N 299 
TRP C   OXT  sing N N 300 
TRP CB  CG   sing N N 301 
TRP CB  HB2  sing N N 302 
TRP CB  HB3  sing N N 303 
TRP CG  CD1  doub Y N 304 
TRP CG  CD2  sing Y N 305 
TRP CD1 NE1  sing Y N 306 
TRP CD1 HD1  sing N N 307 
TRP CD2 CE2  doub Y N 308 
TRP CD2 CE3  sing Y N 309 
TRP NE1 CE2  sing Y N 310 
TRP NE1 HE1  sing N N 311 
TRP CE2 CZ2  sing Y N 312 
TRP CE3 CZ3  doub Y N 313 
TRP CE3 HE3  sing N N 314 
TRP CZ2 CH2  doub Y N 315 
TRP CZ2 HZ2  sing N N 316 
TRP CZ3 CH2  sing Y N 317 
TRP CZ3 HZ3  sing N N 318 
TRP CH2 HH2  sing N N 319 
TRP OXT HXT  sing N N 320 
TYR N   CA   sing N N 321 
TYR N   H    sing N N 322 
TYR N   H2   sing N N 323 
TYR CA  C    sing N N 324 
TYR CA  CB   sing N N 325 
TYR CA  HA   sing N N 326 
TYR C   O    doub N N 327 
TYR C   OXT  sing N N 328 
TYR CB  CG   sing N N 329 
TYR CB  HB2  sing N N 330 
TYR CB  HB3  sing N N 331 
TYR CG  CD1  doub Y N 332 
TYR CG  CD2  sing Y N 333 
TYR CD1 CE1  sing Y N 334 
TYR CD1 HD1  sing N N 335 
TYR CD2 CE2  doub Y N 336 
TYR CD2 HD2  sing N N 337 
TYR CE1 CZ   doub Y N 338 
TYR CE1 HE1  sing N N 339 
TYR CE2 CZ   sing Y N 340 
TYR CE2 HE2  sing N N 341 
TYR CZ  OH   sing N N 342 
TYR OH  HH   sing N N 343 
TYR OXT HXT  sing N N 344 
VAL N   CA   sing N N 345 
VAL N   H    sing N N 346 
VAL N   H2   sing N N 347 
VAL CA  C    sing N N 348 
VAL CA  CB   sing N N 349 
VAL CA  HA   sing N N 350 
VAL C   O    doub N N 351 
VAL C   OXT  sing N N 352 
VAL CB  CG1  sing N N 353 
VAL CB  CG2  sing N N 354 
VAL CB  HB   sing N N 355 
VAL CG1 HG11 sing N N 356 
VAL CG1 HG12 sing N N 357 
VAL CG1 HG13 sing N N 358 
VAL CG2 HG21 sing N N 359 
VAL CG2 HG22 sing N N 360 
VAL CG2 HG23 sing N N 361 
VAL OXT HXT  sing N N 362 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           31870746 
_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 2vgq ? 
2 ? 'experimental model' PDB 2be6 ? 
# 
_atom_sites.entry_id                    8ZLW 
_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]   0.018988 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001384 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016236 
_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]   0.011394 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CA 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . MET A 1 1   ? 43.585 34.885  55.045 1.00 64.23  ? 1   MET A N   1 
ATOM   2    C  CA  . MET A 1 1   ? 43.514 34.809  53.591 1.00 78.04  ? 1   MET A CA  1 
ATOM   3    C  C   . MET A 1 1   ? 44.084 33.479  53.088 1.00 74.74  ? 1   MET A C   1 
ATOM   4    O  O   . MET A 1 1   ? 43.693 32.411  53.576 1.00 70.46  ? 1   MET A O   1 
ATOM   5    C  CB  . MET A 1 1   ? 44.270 35.984  52.967 1.00 83.34  ? 1   MET A CB  1 
ATOM   6    N  N   . LYS A 1 2   ? 44.974 33.554  52.090 1.00 64.72  ? 2   LYS A N   1 
ATOM   7    C  CA  . LYS A 1 2   ? 45.947 32.502  51.813 1.00 58.78  ? 2   LYS A CA  1 
ATOM   8    C  C   . LYS A 1 2   ? 47.156 32.678  52.726 1.00 48.55  ? 2   LYS A C   1 
ATOM   9    O  O   . LYS A 1 2   ? 47.369 33.748  53.307 1.00 51.53  ? 2   LYS A O   1 
ATOM   10   C  CB  . LYS A 1 2   ? 46.410 32.526  50.351 1.00 54.14  ? 2   LYS A CB  1 
ATOM   11   N  N   . ILE A 1 3   ? 47.949 31.608  52.863 1.00 45.41  ? 3   ILE A N   1 
ATOM   12   C  CA  . ILE A 1 3   ? 49.124 31.664  53.734 1.00 45.10  ? 3   ILE A CA  1 
ATOM   13   C  C   . ILE A 1 3   ? 50.103 32.700  53.192 1.00 44.21  ? 3   ILE A C   1 
ATOM   14   O  O   . ILE A 1 3   ? 50.359 32.775  51.981 1.00 44.35  ? 3   ILE A O   1 
ATOM   15   C  CB  . ILE A 1 3   ? 49.780 30.279  53.853 1.00 50.26  ? 3   ILE A CB  1 
ATOM   16   C  CG1 . ILE A 1 3   ? 49.054 29.428  54.895 1.00 53.97  ? 3   ILE A CG1 1 
ATOM   17   C  CG2 . ILE A 1 3   ? 51.264 30.385  54.231 1.00 48.80  ? 3   ILE A CG2 1 
ATOM   18   C  CD1 . ILE A 1 3   ? 49.363 27.951  54.810 1.00 57.07  ? 3   ILE A CD1 1 
ATOM   19   N  N   . GLU A 1 4   ? 50.636 33.523  54.083 1.00 40.08  ? 4   GLU A N   1 
ATOM   20   C  CA  . GLU A 1 4   ? 51.674 34.477  53.750 1.00 43.72  ? 4   GLU A CA  1 
ATOM   21   C  C   . GLU A 1 4   ? 52.772 34.388  54.794 1.00 41.51  ? 4   GLU A C   1 
ATOM   22   O  O   . GLU A 1 4   ? 52.490 34.253  55.991 1.00 41.96  ? 4   GLU A O   1 
ATOM   23   C  CB  . GLU A 1 4   ? 51.120 35.886  53.705 1.00 47.26  ? 4   GLU A CB  1 
ATOM   24   C  CG  . GLU A 1 4   ? 51.359 36.586  52.394 1.00 60.19  ? 4   GLU A CG  1 
ATOM   25   C  CD  . GLU A 1 4   ? 50.636 37.909  52.319 1.00 63.06  ? 4   GLU A CD  1 
ATOM   26   O  OE1 . GLU A 1 4   ? 49.416 37.920  52.599 1.00 63.26  ? 4   GLU A OE1 1 
ATOM   27   O  OE2 . GLU A 1 4   ? 51.291 38.927  51.996 1.00 66.81  ? 4   GLU A OE2 1 
ATOM   28   N  N   . GLU A 1 5   ? 54.018 34.477  54.351 1.00 39.91  ? 5   GLU A N   1 
ATOM   29   C  CA  . GLU A 1 5   ? 55.126 34.423  55.295 1.00 39.60  ? 5   GLU A CA  1 
ATOM   30   C  C   . GLU A 1 5   ? 55.162 35.708  56.110 1.00 38.04  ? 5   GLU A C   1 
ATOM   31   O  O   . GLU A 1 5   ? 55.289 36.803  55.550 1.00 34.95  ? 5   GLU A O   1 
ATOM   32   C  CB  . GLU A 1 5   ? 56.445 34.206  54.558 1.00 40.98  ? 5   GLU A CB  1 
ATOM   33   C  CG  . GLU A 1 5   ? 57.627 33.809  55.460 1.00 37.66  ? 5   GLU A CG  1 
ATOM   34   C  CD  . GLU A 1 5   ? 58.872 33.549  54.636 1.00 40.08  ? 5   GLU A CD  1 
ATOM   35   O  OE1 . GLU A 1 5   ? 58.855 33.903  53.428 1.00 38.04  ? 5   GLU A OE1 1 
ATOM   36   O  OE2 . GLU A 1 5   ? 59.854 33.001  55.181 1.00 40.93  ? 5   GLU A OE2 1 
ATOM   37   N  N   . GLY A 1 6   ? 55.078 35.576  57.438 1.00 39.85  ? 6   GLY A N   1 
ATOM   38   C  CA  . GLY A 1 6   ? 54.992 36.717  58.327 1.00 38.79  ? 6   GLY A CA  1 
ATOM   39   C  C   . GLY A 1 6   ? 53.622 36.920  58.946 1.00 42.59  ? 6   GLY A C   1 
ATOM   40   O  O   . GLY A 1 6   ? 53.447 37.852  59.736 1.00 45.43  ? 6   GLY A O   1 
ATOM   41   N  N   . LYS A 1 7   ? 52.645 36.086  58.610 1.00 46.60  ? 7   LYS A N   1 
ATOM   42   C  CA  . LYS A 1 7   ? 51.334 36.091  59.247 1.00 44.91  ? 7   LYS A CA  1 
ATOM   43   C  C   . LYS A 1 7   ? 50.957 34.655  59.589 1.00 44.15  ? 7   LYS A C   1 
ATOM   44   O  O   . LYS A 1 7   ? 51.574 33.699  59.112 1.00 38.84  ? 7   LYS A O   1 
ATOM   45   C  CB  . LYS A 1 7   ? 50.260 36.701  58.337 1.00 44.41  ? 7   LYS A CB  1 
ATOM   46   C  CG  . LYS A 1 7   ? 50.392 38.177  58.065 1.00 51.07  ? 7   LYS A CG  1 
ATOM   47   C  CD  . LYS A 1 7   ? 49.564 38.539  56.840 1.00 53.50  ? 7   LYS A CD  1 
ATOM   48   C  CE  . LYS A 1 7   ? 49.618 40.024  56.532 1.00 58.45  ? 7   LYS A CE  1 
ATOM   49   N  NZ  . LYS A 1 7   ? 48.623 40.381  55.469 1.00 61.26  ? 7   LYS A NZ  1 
ATOM   50   N  N   . LEU A 1 8   ? 49.911 34.503  60.395 1.00 38.94  ? 8   LEU A N   1 
ATOM   51   C  CA  . LEU A 1 8   ? 49.389 33.197  60.759 1.00 37.16  ? 8   LEU A CA  1 
ATOM   52   C  C   . LEU A 1 8   ? 47.941 33.077  60.306 1.00 35.06  ? 8   LEU A C   1 
ATOM   53   O  O   . LEU A 1 8   ? 47.150 34.007  60.481 1.00 34.86  ? 8   LEU A O   1 
ATOM   54   C  CB  . LEU A 1 8   ? 49.476 32.984  62.268 1.00 37.45  ? 8   LEU A CB  1 
ATOM   55   C  CG  . LEU A 1 8   ? 50.872 32.798  62.853 1.00 39.26  ? 8   LEU A CG  1 
ATOM   56   C  CD1 . LEU A 1 8   ? 50.839 32.673  64.412 1.00 38.16  ? 8   LEU A CD1 1 
ATOM   57   C  CD2 . LEU A 1 8   ? 51.481 31.571  62.227 1.00 36.65  ? 8   LEU A CD2 1 
ATOM   58   N  N   . VAL A 1 9   ? 47.585 31.935  59.736 1.00 31.67  ? 9   VAL A N   1 
ATOM   59   C  CA  . VAL A 1 9   ? 46.189 31.619  59.441 1.00 30.87  ? 9   VAL A CA  1 
ATOM   60   C  C   . VAL A 1 9   ? 45.828 30.369  60.223 1.00 30.46  ? 9   VAL A C   1 
ATOM   61   O  O   . VAL A 1 9   ? 46.579 29.393  60.211 1.00 32.69  ? 9   VAL A O   1 
ATOM   62   C  CB  . VAL A 1 9   ? 45.949 31.416  57.934 1.00 33.12  ? 9   VAL A CB  1 
ATOM   63   C  CG1 . VAL A 1 9   ? 44.488 31.013  57.683 1.00 32.26  ? 9   VAL A CG1 1 
ATOM   64   C  CG2 . VAL A 1 9   ? 46.330 32.682  57.161 1.00 33.08  ? 9   VAL A CG2 1 
ATOM   65   N  N   . ILE A 1 10  ? 44.696 30.393  60.903 1.00 31.84  ? 10  ILE A N   1 
ATOM   66   C  CA  . ILE A 1 10  ? 44.315 29.297  61.790 1.00 30.13  ? 10  ILE A CA  1 
ATOM   67   C  C   . ILE A 1 10  ? 42.933 28.783  61.417 1.00 31.84  ? 10  ILE A C   1 
ATOM   68   O  O   . ILE A 1 10  ? 42.007 29.572  61.208 1.00 35.15  ? 10  ILE A O   1 
ATOM   69   C  CB  . ILE A 1 10  ? 44.311 29.743  63.269 1.00 27.84  ? 10  ILE A CB  1 
ATOM   70   C  CG1 . ILE A 1 10  ? 45.674 30.266  63.712 1.00 30.02  ? 10  ILE A CG1 1 
ATOM   71   C  CG2 . ILE A 1 10  ? 43.794 28.627  64.149 1.00 31.87  ? 10  ILE A CG2 1 
ATOM   72   C  CD1 . ILE A 1 10  ? 45.708 30.640  65.219 1.00 31.21  ? 10  ILE A CD1 1 
ATOM   73   N  N   . TRP A 1 11  ? 42.782 27.462  61.407 1.00 32.75  ? 11  TRP A N   1 
ATOM   74   C  CA  . TRP A 1 11  ? 41.508 26.797  61.190 1.00 28.75  ? 11  TRP A CA  1 
ATOM   75   C  C   . TRP A 1 11  ? 41.079 26.097  62.475 1.00 32.56  ? 11  TRP A C   1 
ATOM   76   O  O   . TRP A 1 11  ? 41.881 25.385  63.116 1.00 27.45  ? 11  TRP A O   1 
ATOM   77   C  CB  . TRP A 1 11  ? 41.601 25.772  60.053 1.00 28.57  ? 11  TRP A CB  1 
ATOM   78   C  CG  . TRP A 1 11  ? 41.651 26.377  58.679 1.00 31.77  ? 11  TRP A CG  1 
ATOM   79   C  CD1 . TRP A 1 11  ? 41.816 27.703  58.363 1.00 33.43  ? 11  TRP A CD1 1 
ATOM   80   C  CD2 . TRP A 1 11  ? 41.542 25.676  57.426 1.00 32.11  ? 11  TRP A CD2 1 
ATOM   81   N  NE1 . TRP A 1 11  ? 41.829 27.866  56.983 1.00 31.37  ? 11  TRP A NE1 1 
ATOM   82   C  CE2 . TRP A 1 11  ? 41.669 26.637  56.392 1.00 33.11  ? 11  TRP A CE2 1 
ATOM   83   C  CE3 . TRP A 1 11  ? 41.371 24.327  57.079 1.00 35.39  ? 11  TRP A CE3 1 
ATOM   84   C  CZ2 . TRP A 1 11  ? 41.607 26.297  55.036 1.00 32.39  ? 11  TRP A CZ2 1 
ATOM   85   C  CZ3 . TRP A 1 11  ? 41.314 23.985  55.705 1.00 32.13  ? 11  TRP A CZ3 1 
ATOM   86   C  CH2 . TRP A 1 11  ? 41.427 24.973  54.714 1.00 32.81  ? 11  TRP A CH2 1 
ATOM   87   N  N   . ILE A 1 12  ? 39.808 26.278  62.832 1.00 28.28  ? 12  ILE A N   1 
ATOM   88   C  CA  . ILE A 1 12  ? 39.236 25.647  64.014 1.00 30.07  ? 12  ILE A CA  1 
ATOM   89   C  C   . ILE A 1 12  ? 37.734 25.531  63.773 1.00 30.05  ? 12  ILE A C   1 
ATOM   90   O  O   . ILE A 1 12  ? 37.141 26.370  63.102 1.00 28.97  ? 12  ILE A O   1 
ATOM   91   C  CB  . ILE A 1 12  ? 39.585 26.473  65.284 1.00 28.88  ? 12  ILE A CB  1 
ATOM   92   C  CG1 . ILE A 1 12  ? 39.144 25.770  66.573 1.00 27.92  ? 12  ILE A CG1 1 
ATOM   93   C  CG2 . ILE A 1 12  ? 39.026 27.915  65.182 1.00 29.91  ? 12  ILE A CG2 1 
ATOM   94   C  CD1 . ILE A 1 12  ? 39.602 26.541  67.850 1.00 26.35  ? 12  ILE A CD1 1 
ATOM   95   N  N   . ASN A 1 13  ? 37.127 24.470  64.293 1.00 33.38  ? 13  ASN A N   1 
ATOM   96   C  CA  . ASN A 1 13  ? 35.738 24.182  63.949 1.00 33.51  ? 13  ASN A CA  1 
ATOM   97   C  C   . ASN A 1 13  ? 34.769 25.239  64.478 1.00 32.82  ? 13  ASN A C   1 
ATOM   98   O  O   . ASN A 1 13  ? 34.984 25.847  65.532 1.00 32.16  ? 13  ASN A O   1 
ATOM   99   C  CB  . ASN A 1 13  ? 35.321 22.821  64.481 1.00 33.23  ? 13  ASN A CB  1 
ATOM   100  C  CG  . ASN A 1 13  ? 34.064 22.326  63.813 1.00 35.52  ? 13  ASN A CG  1 
ATOM   101  O  OD1 . ASN A 1 13  ? 33.961 22.351  62.572 1.00 30.99  ? 13  ASN A OD1 1 
ATOM   102  N  ND2 . ASN A 1 13  ? 33.090 21.889  64.615 1.00 31.60  ? 13  ASN A ND2 1 
ATOM   103  N  N   . GLY A 1 14  ? 33.650 25.401  63.755 1.00 29.72  ? 14  GLY A N   1 
ATOM   104  C  CA  . GLY A 1 14  ? 32.664 26.420  64.077 1.00 30.16  ? 14  GLY A CA  1 
ATOM   105  C  C   . GLY A 1 14  ? 32.081 26.354  65.483 1.00 28.21  ? 14  GLY A C   1 
ATOM   106  O  O   . GLY A 1 14  ? 31.568 27.365  65.982 1.00 29.56  ? 14  GLY A O   1 
ATOM   107  N  N   . ASP A 1 15  ? 32.135 25.201  66.129 1.00 29.98  ? 15  ASP A N   1 
ATOM   108  C  CA  . ASP A 1 15  ? 31.521 25.037  67.438 1.00 33.02  ? 15  ASP A CA  1 
ATOM   109  C  C   . ASP A 1 15  ? 32.427 25.476  68.578 1.00 33.01  ? 15  ASP A C   1 
ATOM   110  O  O   . ASP A 1 15  ? 31.952 25.594  69.712 1.00 32.01  ? 15  ASP A O   1 
ATOM   111  C  CB  . ASP A 1 15  ? 31.101 23.569  67.646 1.00 33.28  ? 15  ASP A CB  1 
ATOM   112  C  CG  . ASP A 1 15  ? 32.297 22.619  67.851 1.00 37.43  ? 15  ASP A CG  1 
ATOM   113  O  OD1 . ASP A 1 15  ? 33.127 22.465  66.915 1.00 35.75  ? 15  ASP A OD1 1 
ATOM   114  O  OD2 . ASP A 1 15  ? 32.380 21.977  68.936 1.00 36.24  ? 15  ASP A OD2 1 
ATOM   115  N  N   . LYS A 1 16  ? 33.710 25.715  68.308 1.00 35.91  ? 16  LYS A N   1 
ATOM   116  C  CA  . LYS A 1 16  ? 34.639 26.106  69.350 1.00 34.82  ? 16  LYS A CA  1 
ATOM   117  C  C   . LYS A 1 16  ? 34.622 27.620  69.533 1.00 37.64  ? 16  LYS A C   1 
ATOM   118  O  O   . LYS A 1 16  ? 33.987 28.368  68.780 1.00 35.55  ? 16  LYS A O   1 
ATOM   119  C  CB  . LYS A 1 16  ? 36.037 25.589  69.024 1.00 39.14  ? 16  LYS A CB  1 
ATOM   120  C  CG  . LYS A 1 16  ? 36.049 24.090  68.705 1.00 39.31  ? 16  LYS A CG  1 
ATOM   121  C  CD  . LYS A 1 16  ? 36.120 23.252  69.978 1.00 42.79  ? 16  LYS A CD  1 
ATOM   122  C  CE  . LYS A 1 16  ? 35.189 22.044  69.995 1.00 46.82  ? 16  LYS A CE  1 
ATOM   123  N  NZ  . LYS A 1 16  ? 35.359 21.148  68.836 1.00 44.13  ? 16  LYS A NZ  1 
ATOM   124  N  N   . GLY A 1 17  ? 35.314 28.066  70.573 1.00 37.27  ? 17  GLY A N   1 
ATOM   125  C  CA  . GLY A 1 17  ? 35.419 29.473  70.883 1.00 34.99  ? 17  GLY A CA  1 
ATOM   126  C  C   . GLY A 1 17  ? 36.355 30.222  69.961 1.00 30.55  ? 17  GLY A C   1 
ATOM   127  O  O   . GLY A 1 17  ? 37.333 30.812  70.420 1.00 28.29  ? 17  GLY A O   1 
ATOM   128  N  N   . TYR A 1 18  ? 36.043 30.258  68.660 1.00 31.12  ? 18  TYR A N   1 
ATOM   129  C  CA  . TYR A 1 18  ? 36.967 30.885  67.722 1.00 31.34  ? 18  TYR A CA  1 
ATOM   130  C  C   . TYR A 1 18  ? 37.052 32.404  67.899 1.00 31.56  ? 18  TYR A C   1 
ATOM   131  O  O   . TYR A 1 18  ? 38.107 32.988  67.638 1.00 29.31  ? 18  TYR A O   1 
ATOM   132  C  CB  . TYR A 1 18  ? 36.589 30.511  66.293 1.00 31.89  ? 18  TYR A CB  1 
ATOM   133  C  CG  . TYR A 1 18  ? 35.181 30.882  65.880 1.00 37.25  ? 18  TYR A CG  1 
ATOM   134  C  CD1 . TYR A 1 18  ? 34.861 32.191  65.514 1.00 38.23  ? 18  TYR A CD1 1 
ATOM   135  C  CD2 . TYR A 1 18  ? 34.176 29.910  65.800 1.00 36.35  ? 18  TYR A CD2 1 
ATOM   136  C  CE1 . TYR A 1 18  ? 33.571 32.526  65.098 1.00 37.06  ? 18  TYR A CE1 1 
ATOM   137  C  CE2 . TYR A 1 18  ? 32.883 30.240  65.376 1.00 34.24  ? 18  TYR A CE2 1 
ATOM   138  C  CZ  . TYR A 1 18  ? 32.584 31.537  65.039 1.00 37.33  ? 18  TYR A CZ  1 
ATOM   139  O  OH  . TYR A 1 18  ? 31.303 31.860  64.636 1.00 38.21  ? 18  TYR A OH  1 
ATOM   140  N  N   . ASN A 1 19  ? 35.985 33.078  68.333 1.00 33.79  ? 19  ASN A N   1 
ATOM   141  C  CA  . ASN A 1 19  ? 36.176 34.492  68.644 1.00 35.70  ? 19  ASN A CA  1 
ATOM   142  C  C   . ASN A 1 19  ? 37.025 34.666  69.899 1.00 36.66  ? 19  ASN A C   1 
ATOM   143  O  O   . ASN A 1 19  ? 37.725 35.678  70.029 1.00 37.84  ? 19  ASN A O   1 
ATOM   144  C  CB  . ASN A 1 19  ? 34.842 35.225  68.795 1.00 33.56  ? 19  ASN A CB  1 
ATOM   145  C  CG  . ASN A 1 19  ? 34.083 35.325  67.477 1.00 39.97  ? 19  ASN A CG  1 
ATOM   146  O  OD1 . ASN A 1 19  ? 34.679 35.605  66.433 1.00 36.79  ? 19  ASN A OD1 1 
ATOM   147  N  ND2 . ASN A 1 19  ? 32.766 35.062  67.513 1.00 40.22  ? 19  ASN A ND2 1 
ATOM   148  N  N   . GLY A 1 20  ? 36.971 33.703  70.826 1.00 39.29  ? 20  GLY A N   1 
ATOM   149  C  CA  . GLY A 1 20  ? 37.902 33.708  71.946 1.00 37.46  ? 20  GLY A CA  1 
ATOM   150  C  C   . GLY A 1 20  ? 39.326 33.491  71.474 1.00 39.49  ? 20  GLY A C   1 
ATOM   151  O  O   . GLY A 1 20  ? 40.246 34.187  71.910 1.00 36.47  ? 20  GLY A O   1 
ATOM   152  N  N   . LEU A 1 21  ? 39.513 32.564  70.519 1.00 40.25  ? 21  LEU A N   1 
ATOM   153  C  CA  . LEU A 1 21  ? 40.837 32.353  69.938 1.00 37.37  ? 21  LEU A CA  1 
ATOM   154  C  C   . LEU A 1 21  ? 41.286 33.579  69.162 1.00 38.14  ? 21  LEU A C   1 
ATOM   155  O  O   . LEU A 1 21  ? 42.476 33.912  69.162 1.00 34.69  ? 21  LEU A O   1 
ATOM   156  C  CB  . LEU A 1 21  ? 40.842 31.109  69.039 1.00 36.00  ? 21  LEU A CB  1 
ATOM   157  C  CG  . LEU A 1 21  ? 42.205 30.672  68.492 1.00 35.85  ? 21  LEU A CG  1 
ATOM   158  C  CD1 . LEU A 1 21  ? 43.198 30.384  69.638 1.00 36.74  ? 21  LEU A CD1 1 
ATOM   159  C  CD2 . LEU A 1 21  ? 42.057 29.467  67.590 1.00 39.92  ? 21  LEU A CD2 1 
ATOM   160  N  N   . ALA A 1 22  ? 40.350 34.289  68.530 1.00 36.11  ? 22  ALA A N   1 
ATOM   161  C  CA  . ALA A 1 22  ? 40.735 35.506  67.819 1.00 38.39  ? 22  ALA A CA  1 
ATOM   162  C  C   . ALA A 1 22  ? 41.220 36.594  68.780 1.00 34.87  ? 22  ALA A C   1 
ATOM   163  O  O   . ALA A 1 22  ? 42.115 37.368  68.425 1.00 33.51  ? 22  ALA A O   1 
ATOM   164  C  CB  . ALA A 1 22  ? 39.578 36.006  66.963 1.00 36.65  ? 22  ALA A CB  1 
ATOM   165  N  N   . GLU A 1 23  ? 40.671 36.648  70.002 1.00 33.82  ? 23  GLU A N   1 
ATOM   166  C  CA  . GLU A 1 23  ? 41.206 37.565  71.007 1.00 34.47  ? 23  GLU A CA  1 
ATOM   167  C  C   . GLU A 1 23  ? 42.666 37.258  71.309 1.00 38.34  ? 23  GLU A C   1 
ATOM   168  O  O   . GLU A 1 23  ? 43.465 38.175  71.538 1.00 34.92  ? 23  GLU A O   1 
ATOM   169  C  CB  . GLU A 1 23  ? 40.395 37.489  72.298 1.00 37.45  ? 23  GLU A CB  1 
ATOM   170  C  CG  . GLU A 1 23  ? 39.136 38.344  72.334 1.00 48.97  ? 23  GLU A CG  1 
ATOM   171  C  CD  . GLU A 1 23  ? 38.135 37.849  73.387 1.00 53.23  ? 23  GLU A CD  1 
ATOM   172  O  OE1 . GLU A 1 23  ? 38.466 37.831  74.599 1.00 63.55  ? 23  GLU A OE1 1 
ATOM   173  O  OE2 . GLU A 1 23  ? 37.026 37.446  72.992 1.00 59.28  ? 23  GLU A OE2 1 
ATOM   174  N  N   . VAL A 1 24  ? 43.025 35.967  71.357 1.00 36.27  ? 24  VAL A N   1 
ATOM   175  C  CA  . VAL A 1 24  ? 44.411 35.615  71.632 1.00 37.91  ? 24  VAL A CA  1 
ATOM   176  C  C   . VAL A 1 24  ? 45.291 36.018  70.455 1.00 36.20  ? 24  VAL A C   1 
ATOM   177  O  O   . VAL A 1 24  ? 46.417 36.477  70.647 1.00 38.48  ? 24  VAL A O   1 
ATOM   178  C  CB  . VAL A 1 24  ? 44.530 34.118  71.988 1.00 39.60  ? 24  VAL A CB  1 
ATOM   179  C  CG1 . VAL A 1 24  ? 45.935 33.783  72.417 1.00 38.80  ? 24  VAL A CG1 1 
ATOM   180  C  CG2 . VAL A 1 24  ? 43.567 33.772  73.115 1.00 45.51  ? 24  VAL A CG2 1 
ATOM   181  N  N   . GLY A 1 25  ? 44.774 35.925  69.228 1.00 35.00  ? 25  GLY A N   1 
ATOM   182  C  CA  . GLY A 1 25  ? 45.516 36.443  68.086 1.00 41.66  ? 25  GLY A CA  1 
ATOM   183  C  C   . GLY A 1 25  ? 45.716 37.949  68.147 1.00 44.32  ? 25  GLY A C   1 
ATOM   184  O  O   . GLY A 1 25  ? 46.784 38.455  67.803 1.00 37.24  ? 25  GLY A O   1 
ATOM   185  N  N   . LYS A 1 26  ? 44.690 38.683  68.590 1.00 45.73  ? 26  LYS A N   1 
ATOM   186  C  CA  . LYS A 1 26  ? 44.829 40.123  68.778 1.00 47.77  ? 26  LYS A CA  1 
ATOM   187  C  C   . LYS A 1 26  ? 45.953 40.448  69.759 1.00 43.42  ? 26  LYS A C   1 
ATOM   188  O  O   . LYS A 1 26  ? 46.843 41.245  69.449 1.00 44.95  ? 26  LYS A O   1 
ATOM   189  C  CB  . LYS A 1 26  ? 43.508 40.726  69.256 1.00 51.52  ? 26  LYS A CB  1 
ATOM   190  C  CG  . LYS A 1 26  ? 42.368 40.586  68.254 1.00 61.59  ? 26  LYS A CG  1 
ATOM   191  C  CD  . LYS A 1 26  ? 42.828 40.814  66.808 1.00 67.03  ? 26  LYS A CD  1 
ATOM   192  C  CE  . LYS A 1 26  ? 42.020 39.961  65.823 1.00 74.33  ? 26  LYS A CE  1 
ATOM   193  N  NZ  . LYS A 1 26  ? 40.551 40.310  65.806 1.00 76.78  ? 26  LYS A NZ  1 
ATOM   194  N  N   . LYS A 1 27  ? 45.930 39.847  70.954 1.00 40.91  ? 27  LYS A N   1 
ATOM   195  C  CA  . LYS A 1 27  ? 47.015 40.091  71.905 1.00 44.56  ? 27  LYS A CA  1 
ATOM   196  C  C   . LYS A 1 27  ? 48.364 39.746  71.287 1.00 41.48  ? 27  LYS A C   1 
ATOM   197  O  O   . LYS A 1 27  ? 49.320 40.517  71.397 1.00 40.63  ? 27  LYS A O   1 
ATOM   198  C  CB  . LYS A 1 27  ? 46.806 39.298  73.194 1.00 48.67  ? 27  LYS A CB  1 
ATOM   199  C  CG  . LYS A 1 27  ? 48.052 39.277  74.094 1.00 54.82  ? 27  LYS A CG  1 
ATOM   200  C  CD  . LYS A 1 27  ? 47.720 39.025  75.566 1.00 58.54  ? 27  LYS A CD  1 
ATOM   201  C  CE  . LYS A 1 27  ? 48.805 39.589  76.474 1.00 57.72  ? 27  LYS A CE  1 
ATOM   202  N  NZ  . LYS A 1 27  ? 49.038 41.033  76.196 1.00 62.98  ? 27  LYS A NZ  1 
ATOM   203  N  N   . PHE A 1 28  ? 48.448 38.609  70.598 1.00 42.14  ? 28  PHE A N   1 
ATOM   204  C  CA  . PHE A 1 28  ? 49.672 38.266  69.886 1.00 40.45  ? 28  PHE A CA  1 
ATOM   205  C  C   . PHE A 1 28  ? 50.052 39.366  68.906 1.00 43.38  ? 28  PHE A C   1 
ATOM   206  O  O   . PHE A 1 28  ? 51.230 39.747  68.804 1.00 44.92  ? 28  PHE A O   1 
ATOM   207  C  CB  . PHE A 1 28  ? 49.492 36.929  69.167 1.00 38.27  ? 28  PHE A CB  1 
ATOM   208  C  CG  . PHE A 1 28  ? 50.765 36.349  68.612 1.00 37.43  ? 28  PHE A CG  1 
ATOM   209  C  CD1 . PHE A 1 28  ? 51.720 35.788  69.459 1.00 37.71  ? 28  PHE A CD1 1 
ATOM   210  C  CD2 . PHE A 1 28  ? 51.001 36.345  67.234 1.00 35.88  ? 28  PHE A CD2 1 
ATOM   211  C  CE1 . PHE A 1 28  ? 52.885 35.234  68.952 1.00 37.23  ? 28  PHE A CE1 1 
ATOM   212  C  CE2 . PHE A 1 28  ? 52.170 35.792  66.719 1.00 35.09  ? 28  PHE A CE2 1 
ATOM   213  C  CZ  . PHE A 1 28  ? 53.110 35.231  67.576 1.00 37.33  ? 28  PHE A CZ  1 
ATOM   214  N  N   . GLU A 1 29  ? 49.064 39.909  68.193 1.00 38.45  ? 29  GLU A N   1 
ATOM   215  C  CA  . GLU A 1 29  ? 49.345 41.004  67.274 1.00 42.83  ? 29  GLU A CA  1 
ATOM   216  C  C   . GLU A 1 29  ? 49.785 42.267  68.018 1.00 47.91  ? 29  GLU A C   1 
ATOM   217  O  O   . GLU A 1 29  ? 50.642 43.004  67.524 1.00 49.40  ? 29  GLU A O   1 
ATOM   218  C  CB  . GLU A 1 29  ? 48.127 41.298  66.403 1.00 42.36  ? 29  GLU A CB  1 
ATOM   219  C  CG  . GLU A 1 29  ? 48.373 42.476  65.492 1.00 45.56  ? 29  GLU A CG  1 
ATOM   220  C  CD  . GLU A 1 29  ? 47.390 42.583  64.365 1.00 47.22  ? 29  GLU A CD  1 
ATOM   221  O  OE1 . GLU A 1 29  ? 46.209 42.208  64.559 1.00 62.38  ? 29  GLU A OE1 1 
ATOM   222  O  OE2 . GLU A 1 29  ? 47.804 43.058  63.286 1.00 55.31  ? 29  GLU A OE2 1 
ATOM   223  N  N   . LYS A 1 30  ? 49.203 42.544  69.195 1.00 47.92  ? 30  LYS A N   1 
ATOM   224  C  CA  . LYS A 1 30  ? 49.624 43.708  69.976 1.00 54.78  ? 30  LYS A CA  1 
ATOM   225  C  C   . LYS A 1 30  ? 51.084 43.592  70.406 1.00 55.23  ? 30  LYS A C   1 
ATOM   226  O  O   . LYS A 1 30  ? 51.851 44.557  70.290 1.00 49.31  ? 30  LYS A O   1 
ATOM   227  C  CB  . LYS A 1 30  ? 48.723 43.878  71.204 1.00 63.03  ? 30  LYS A CB  1 
ATOM   228  C  CG  . LYS A 1 30  ? 48.933 45.180  71.997 1.00 64.79  ? 30  LYS A CG  1 
ATOM   229  C  CD  . LYS A 1 30  ? 48.081 45.227  73.272 1.00 71.80  ? 30  LYS A CD  1 
ATOM   230  C  CE  . LYS A 1 30  ? 48.890 44.886  74.530 1.00 73.89  ? 30  LYS A CE  1 
ATOM   231  N  NZ  . LYS A 1 30  ? 48.045 44.462  75.697 1.00 69.97  ? 30  LYS A NZ  1 
ATOM   232  N  N   . ASP A 1 31  ? 51.489 42.411  70.883 1.00 52.70  ? 31  ASP A N   1 
ATOM   233  C  CA  . ASP A 1 31  ? 52.811 42.221  71.480 1.00 48.27  ? 31  ASP A CA  1 
ATOM   234  C  C   . ASP A 1 31  ? 53.903 42.121  70.433 1.00 46.94  ? 31  ASP A C   1 
ATOM   235  O  O   . ASP A 1 31  ? 54.976 42.711  70.591 1.00 45.03  ? 31  ASP A O   1 
ATOM   236  C  CB  . ASP A 1 31  ? 52.833 40.957  72.330 1.00 46.31  ? 31  ASP A CB  1 
ATOM   237  C  CG  . ASP A 1 31  ? 52.099 41.116  73.637 1.00 52.55  ? 31  ASP A CG  1 
ATOM   238  O  OD1 . ASP A 1 31  ? 51.611 42.236  73.921 1.00 45.85  ? 31  ASP A OD1 1 
ATOM   239  O  OD2 . ASP A 1 31  ? 52.031 40.111  74.383 1.00 50.55  ? 31  ASP A OD2 1 
ATOM   240  N  N   . THR A 1 32  ? 53.682 41.309  69.410 1.00 47.99  ? 32  THR A N   1 
ATOM   241  C  CA  . THR A 1 32  ? 54.586 41.159  68.284 1.00 46.12  ? 32  THR A CA  1 
ATOM   242  C  C   . THR A 1 32  ? 54.052 42.026  67.157 1.00 44.25  ? 32  THR A C   1 
ATOM   243  O  O   . THR A 1 32  ? 53.088 42.770  67.330 1.00 45.53  ? 32  THR A O   1 
ATOM   244  C  CB  . THR A 1 32  ? 54.679 39.689  67.869 1.00 46.60  ? 32  THR A CB  1 
ATOM   245  O  OG1 . THR A 1 32  ? 53.426 39.286  67.297 1.00 48.76  ? 32  THR A OG1 1 
ATOM   246  C  CG2 . THR A 1 32  ? 54.978 38.814  69.066 1.00 45.10  ? 32  THR A CG2 1 
ATOM   247  N  N   . GLY A 1 33  ? 54.654 41.944  65.984 1.00 42.87  ? 33  GLY A N   1 
ATOM   248  C  CA  . GLY A 1 33  ? 53.944 42.627  64.923 1.00 49.75  ? 33  GLY A CA  1 
ATOM   249  C  C   . GLY A 1 33  ? 52.972 41.753  64.162 1.00 46.73  ? 33  GLY A C   1 
ATOM   250  O  O   . GLY A 1 33  ? 52.360 42.217  63.196 1.00 53.10  ? 33  GLY A O   1 
ATOM   251  N  N   . ILE A 1 34  ? 52.779 40.512  64.590 1.00 47.52  ? 34  ILE A N   1 
ATOM   252  C  CA  . ILE A 1 34  ? 52.286 39.450  63.722 1.00 42.46  ? 34  ILE A CA  1 
ATOM   253  C  C   . ILE A 1 34  ? 50.759 39.419  63.720 1.00 39.85  ? 34  ILE A C   1 
ATOM   254  O  O   . ILE A 1 34  ? 50.130 39.292  64.779 1.00 41.57  ? 34  ILE A O   1 
ATOM   255  C  CB  . ILE A 1 34  ? 52.861 38.096  64.168 1.00 41.12  ? 34  ILE A CB  1 
ATOM   256  C  CG1 . ILE A 1 34  ? 54.388 38.191  64.353 1.00 40.71  ? 34  ILE A CG1 1 
ATOM   257  C  CG2 . ILE A 1 34  ? 52.448 36.996  63.197 1.00 38.31  ? 34  ILE A CG2 1 
ATOM   258  C  CD1 . ILE A 1 34  ? 55.141 38.661  63.118 1.00 37.61  ? 34  ILE A CD1 1 
ATOM   259  N  N   . LYS A 1 35  ? 50.157 39.490  62.529 1.00 38.79  ? 35  LYS A N   1 
ATOM   260  C  CA  . LYS A 1 35  ? 48.705 39.362  62.425 1.00 39.54  ? 35  LYS A CA  1 
ATOM   261  C  C   . LYS A 1 35  ? 48.290 37.887  62.466 1.00 40.89  ? 35  LYS A C   1 
ATOM   262  O  O   . LYS A 1 35  ? 49.012 36.998  61.996 1.00 43.10  ? 35  LYS A O   1 
ATOM   263  C  CB  . LYS A 1 35  ? 48.201 40.022  61.142 1.00 42.04  ? 35  LYS A CB  1 
ATOM   264  C  CG  . LYS A 1 35  ? 46.667 40.141  61.033 1.00 52.25  ? 35  LYS A CG  1 
ATOM   265  C  CD  . LYS A 1 35  ? 46.242 40.521  59.603 1.00 48.98  ? 35  LYS A CD  1 
ATOM   266  C  CE  . LYS A 1 35  ? 46.736 39.465  58.614 1.00 52.60  ? 35  LYS A CE  1 
ATOM   267  N  NZ  . LYS A 1 35  ? 46.238 39.585  57.199 1.00 57.65  ? 35  LYS A NZ  1 
ATOM   268  N  N   . VAL A 1 36  ? 47.121 37.636  63.053 1.00 33.99  ? 36  VAL A N   1 
ATOM   269  C  CA  . VAL A 1 36  ? 46.555 36.299  63.189 1.00 35.85  ? 36  VAL A CA  1 
ATOM   270  C  C   . VAL A 1 36  ? 45.116 36.337  62.678 1.00 38.10  ? 36  VAL A C   1 
ATOM   271  O  O   . VAL A 1 36  ? 44.303 37.137  63.152 1.00 34.19  ? 36  VAL A O   1 
ATOM   272  C  CB  . VAL A 1 36  ? 46.595 35.800  64.649 1.00 35.39  ? 36  VAL A CB  1 
ATOM   273  C  CG1 . VAL A 1 36  ? 46.255 34.322  64.718 1.00 33.94  ? 36  VAL A CG1 1 
ATOM   274  C  CG2 . VAL A 1 36  ? 47.987 36.073  65.298 1.00 34.60  ? 36  VAL A CG2 1 
ATOM   275  N  N   . THR A 1 37  ? 44.806 35.480  61.713 1.00 39.31  ? 37  THR A N   1 
ATOM   276  C  CA  . THR A 1 37  ? 43.462 35.349  61.176 1.00 34.26  ? 37  THR A CA  1 
ATOM   277  C  C   . THR A 1 37  ? 42.924 33.995  61.596 1.00 33.40  ? 37  THR A C   1 
ATOM   278  O  O   . THR A 1 37  ? 43.399 32.957  61.129 1.00 33.09  ? 37  THR A O   1 
ATOM   279  C  CB  . THR A 1 37  ? 43.441 35.477  59.656 1.00 40.13  ? 37  THR A CB  1 
ATOM   280  O  OG1 . THR A 1 37  ? 44.117 36.676  59.268 1.00 38.52  ? 37  THR A OG1 1 
ATOM   281  C  CG2 . THR A 1 37  ? 42.004 35.533  59.167 1.00 43.70  ? 37  THR A CG2 1 
ATOM   282  N  N   . VAL A 1 38  ? 41.933 34.006  62.469 1.00 32.69  ? 38  VAL A N   1 
ATOM   283  C  CA  . VAL A 1 38  ? 41.247 32.792  62.881 1.00 31.42  ? 38  VAL A CA  1 
ATOM   284  C  C   . VAL A 1 38  ? 40.055 32.590  61.959 1.00 30.54  ? 38  VAL A C   1 
ATOM   285  O  O   . VAL A 1 38  ? 39.184 33.460  61.866 1.00 32.45  ? 38  VAL A O   1 
ATOM   286  C  CB  . VAL A 1 38  ? 40.794 32.884  64.342 1.00 31.40  ? 38  VAL A CB  1 
ATOM   287  C  CG1 . VAL A 1 38  ? 40.020 31.651  64.711 1.00 32.48  ? 38  VAL A CG1 1 
ATOM   288  C  CG2 . VAL A 1 38  ? 42.006 33.126  65.281 1.00 31.19  ? 38  VAL A CG2 1 
ATOM   289  N  N   . GLU A 1 39  ? 40.012 31.445  61.297 1.00 30.97  ? 39  GLU A N   1 
ATOM   290  C  CA  . GLU A 1 39  ? 38.933 31.079  60.392 1.00 35.55  ? 39  GLU A CA  1 
ATOM   291  C  C   . GLU A 1 39  ? 38.285 29.792  60.880 1.00 34.44  ? 39  GLU A C   1 
ATOM   292  O  O   . GLU A 1 39  ? 38.929 28.976  61.551 1.00 30.61  ? 39  GLU A O   1 
ATOM   293  C  CB  . GLU A 1 39  ? 39.449 30.869  58.959 1.00 34.72  ? 39  GLU A CB  1 
ATOM   294  C  CG  . GLU A 1 39  ? 40.237 32.023  58.396 1.00 37.60  ? 39  GLU A CG  1 
ATOM   295  C  CD  . GLU A 1 39  ? 40.542 31.823  56.914 1.00 39.87  ? 39  GLU A CD  1 
ATOM   296  O  OE1 . GLU A 1 39  ? 40.888 30.694  56.503 1.00 40.40  ? 39  GLU A OE1 1 
ATOM   297  O  OE2 . GLU A 1 39  ? 40.415 32.800  56.155 1.00 45.81  ? 39  GLU A OE2 1 
ATOM   298  N  N   . HIS A 1 40  ? 37.005 29.607  60.546 1.00 33.75  ? 40  HIS A N   1 
ATOM   299  C  CA  . HIS A 1 40  ? 36.282 28.382  60.888 1.00 35.61  ? 40  HIS A CA  1 
ATOM   300  C  C   . HIS A 1 40  ? 35.518 27.883  59.671 1.00 35.53  ? 40  HIS A C   1 
ATOM   301  O  O   . HIS A 1 40  ? 34.277 27.835  59.667 1.00 33.87  ? 40  HIS A O   1 
ATOM   302  C  CB  . HIS A 1 40  ? 35.342 28.596  62.082 1.00 34.24  ? 40  HIS A CB  1 
ATOM   303  C  CG  . HIS A 1 40  ? 34.370 29.721  61.905 1.00 34.35  ? 40  HIS A CG  1 
ATOM   304  N  ND1 . HIS A 1 40  ? 34.726 31.044  62.061 1.00 33.54  ? 40  HIS A ND1 1 
ATOM   305  C  CD2 . HIS A 1 40  ? 33.053 29.724  61.582 1.00 33.59  ? 40  HIS A CD2 1 
ATOM   306  C  CE1 . HIS A 1 40  ? 33.671 31.813  61.844 1.00 33.99  ? 40  HIS A CE1 1 
ATOM   307  N  NE2 . HIS A 1 40  ? 32.640 31.038  61.562 1.00 32.22  ? 40  HIS A NE2 1 
ATOM   308  N  N   . PRO A 1 41  ? 36.224 27.463  58.629 1.00 37.22  ? 41  PRO A N   1 
ATOM   309  C  CA  . PRO A 1 41  ? 35.516 26.961  57.451 1.00 35.96  ? 41  PRO A CA  1 
ATOM   310  C  C   . PRO A 1 41  ? 34.809 25.653  57.751 1.00 41.45  ? 41  PRO A C   1 
ATOM   311  O  O   . PRO A 1 41  ? 35.194 24.866  58.625 1.00 37.74  ? 41  PRO A O   1 
ATOM   312  C  CB  . PRO A 1 41  ? 36.614 26.787  56.394 1.00 38.26  ? 41  PRO A CB  1 
ATOM   313  C  CG  . PRO A 1 41  ? 37.923 26.878  57.117 1.00 39.80  ? 41  PRO A CG  1 
ATOM   314  C  CD  . PRO A 1 41  ? 37.693 27.376  58.509 1.00 39.10  ? 41  PRO A CD  1 
ATOM   315  N  N   . ASP A 1 42  ? 33.720 25.466  57.032 1.00 43.34  ? 42  ASP A N   1 
ATOM   316  C  CA  . ASP A 1 42  ? 32.968 24.229  57.066 1.00 43.08  ? 42  ASP A CA  1 
ATOM   317  C  C   . ASP A 1 42  ? 33.803 23.113  56.444 1.00 41.31  ? 42  ASP A C   1 
ATOM   318  O  O   . ASP A 1 42  ? 34.515 23.328  55.459 1.00 43.09  ? 42  ASP A O   1 
ATOM   319  C  CB  . ASP A 1 42  ? 31.655 24.459  56.300 1.00 41.83  ? 42  ASP A CB  1 
ATOM   320  C  CG  . ASP A 1 42  ? 30.690 23.330  56.423 1.00 44.91  ? 42  ASP A CG  1 
ATOM   321  O  OD1 . ASP A 1 42  ? 30.776 22.560  57.403 1.00 40.11  ? 42  ASP A OD1 1 
ATOM   322  O  OD2 . ASP A 1 42  ? 29.812 23.234  55.534 1.00 49.56  ? 42  ASP A OD2 1 
ATOM   323  N  N   . LYS A 1 43  ? 33.730 21.920  57.027 1.00 41.71  ? 43  LYS A N   1 
ATOM   324  C  CA  . LYS A 1 43  ? 34.415 20.745  56.485 1.00 47.48  ? 43  LYS A CA  1 
ATOM   325  C  C   . LYS A 1 43  ? 35.933 20.939  56.455 1.00 43.19  ? 43  LYS A C   1 
ATOM   326  O  O   . LYS A 1 43  ? 36.621 20.410  55.580 1.00 38.47  ? 43  LYS A O   1 
ATOM   327  C  CB  . LYS A 1 43  ? 33.896 20.394  55.085 1.00 51.08  ? 43  LYS A CB  1 
ATOM   328  C  CG  . LYS A 1 43  ? 32.768 19.366  55.046 1.00 56.06  ? 43  LYS A CG  1 
ATOM   329  C  CD  . LYS A 1 43  ? 32.020 19.407  53.705 1.00 57.67  ? 43  LYS A CD  1 
ATOM   330  C  CE  . LYS A 1 43  ? 30.868 18.392  53.656 1.00 63.28  ? 43  LYS A CE  1 
ATOM   331  N  NZ  . LYS A 1 43  ? 30.171 18.319  52.322 1.00 62.12  ? 43  LYS A NZ  1 
ATOM   332  N  N   . LEU A 1 44  ? 36.469 21.697  57.414 1.00 37.76  ? 44  LEU A N   1 
ATOM   333  C  CA  . LEU A 1 44  ? 37.898 22.004  57.392 1.00 39.20  ? 44  LEU A CA  1 
ATOM   334  C  C   . LEU A 1 44  ? 38.732 20.730  57.497 1.00 36.20  ? 44  LEU A C   1 
ATOM   335  O  O   . LEU A 1 44  ? 39.754 20.597  56.821 1.00 40.17  ? 44  LEU A O   1 
ATOM   336  C  CB  . LEU A 1 44  ? 38.242 22.996  58.512 1.00 35.77  ? 44  LEU A CB  1 
ATOM   337  C  CG  . LEU A 1 44  ? 38.217 22.458  59.946 1.00 36.22  ? 44  LEU A CG  1 
ATOM   338  C  CD1 . LEU A 1 44  ? 39.607 21.953  60.352 1.00 39.57  ? 44  LEU A CD1 1 
ATOM   339  C  CD2 . LEU A 1 44  ? 37.735 23.534  60.891 1.00 37.66  ? 44  LEU A CD2 1 
ATOM   340  N  N   . GLU A 1 45  ? 38.287 19.760  58.302 1.00 39.95  ? 45  GLU A N   1 
ATOM   341  C  CA  . GLU A 1 45  ? 39.042 18.523  58.441 1.00 37.61  ? 45  GLU A CA  1 
ATOM   342  C  C   . GLU A 1 45  ? 39.065 17.716  57.146 1.00 41.13  ? 45  GLU A C   1 
ATOM   343  O  O   . GLU A 1 45  ? 39.942 16.867  56.971 1.00 42.53  ? 45  GLU A O   1 
ATOM   344  C  CB  . GLU A 1 45  ? 38.475 17.699  59.598 1.00 37.64  ? 45  GLU A CB  1 
ATOM   345  C  CG  . GLU A 1 45  ? 37.419 16.665  59.233 1.00 38.73  ? 45  GLU A CG  1 
ATOM   346  C  CD  . GLU A 1 45  ? 36.016 17.255  59.090 1.00 40.21  ? 45  GLU A CD  1 
ATOM   347  O  OE1 . GLU A 1 45  ? 35.877 18.481  58.861 1.00 41.88  ? 45  GLU A OE1 1 
ATOM   348  O  OE2 . GLU A 1 45  ? 35.052 16.487  59.201 1.00 37.34  ? 45  GLU A OE2 1 
ATOM   349  N  N   . GLU A 1 46  ? 38.139 17.973  56.231 1.00 45.06  ? 46  GLU A N   1 
ATOM   350  C  CA  . GLU A 1 46  ? 38.172 17.330  54.925 1.00 44.89  ? 46  GLU A CA  1 
ATOM   351  C  C   . GLU A 1 46  ? 38.959 18.151  53.933 1.00 40.45  ? 46  GLU A C   1 
ATOM   352  O  O   . GLU A 1 46  ? 39.634 17.585  53.064 1.00 36.02  ? 46  GLU A O   1 
ATOM   353  C  CB  . GLU A 1 46  ? 36.755 17.133  54.375 1.00 43.01  ? 46  GLU A CB  1 
ATOM   354  C  CG  . GLU A 1 46  ? 35.867 16.245  55.214 1.00 48.56  ? 46  GLU A CG  1 
ATOM   355  C  CD  . GLU A 1 46  ? 34.985 15.388  54.337 1.00 58.92  ? 46  GLU A CD  1 
ATOM   356  O  OE1 . GLU A 1 46  ? 34.031 15.947  53.753 1.00 71.73  ? 46  GLU A OE1 1 
ATOM   357  O  OE2 . GLU A 1 46  ? 35.270 14.172  54.197 1.00 55.35  ? 46  GLU A OE2 1 
ATOM   358  N  N   . LYS A 1 47  ? 38.873 19.475  54.058 1.00 37.19  ? 47  LYS A N   1 
ATOM   359  C  CA  . LYS A 1 47  ? 39.563 20.367  53.139 1.00 38.29  ? 47  LYS A CA  1 
ATOM   360  C  C   . LYS A 1 47  ? 41.062 20.393  53.393 1.00 36.57  ? 47  LYS A C   1 
ATOM   361  O  O   . LYS A 1 47  ? 41.836 20.584  52.449 1.00 33.88  ? 47  LYS A O   1 
ATOM   362  C  CB  . LYS A 1 47  ? 38.994 21.785  53.253 1.00 41.04  ? 47  LYS A CB  1 
ATOM   363  C  CG  . LYS A 1 47  ? 37.637 21.988  52.578 1.00 45.80  ? 47  LYS A CG  1 
ATOM   364  C  CD  . LYS A 1 47  ? 37.011 23.324  52.981 1.00 53.19  ? 47  LYS A CD  1 
ATOM   365  C  CE  . LYS A 1 47  ? 35.534 23.421  52.544 1.00 49.59  ? 47  LYS A CE  1 
ATOM   366  N  NZ  . LYS A 1 47  ? 34.937 24.665  53.095 1.00 51.60  ? 47  LYS A NZ  1 
ATOM   367  N  N   . PHE A 1 48  ? 41.491 20.244  54.651 1.00 31.54  ? 48  PHE A N   1 
ATOM   368  C  CA  . PHE A 1 48  ? 42.916 20.337  54.952 1.00 34.17  ? 48  PHE A CA  1 
ATOM   369  C  C   . PHE A 1 48  ? 43.770 19.461  54.042 1.00 33.32  ? 48  PHE A C   1 
ATOM   370  O  O   . PHE A 1 48  ? 44.686 20.000  53.409 1.00 34.00  ? 48  PHE A O   1 
ATOM   371  C  CB  . PHE A 1 48  ? 43.178 20.026  56.435 1.00 32.03  ? 48  PHE A CB  1 
ATOM   372  C  CG  . PHE A 1 48  ? 44.614 20.174  56.816 1.00 30.99  ? 48  PHE A CG  1 
ATOM   373  C  CD1 . PHE A 1 48  ? 45.266 21.380  56.622 1.00 33.94  ? 48  PHE A CD1 1 
ATOM   374  C  CD2 . PHE A 1 48  ? 45.327 19.106  57.361 1.00 31.18  ? 48  PHE A CD2 1 
ATOM   375  C  CE1 . PHE A 1 48  ? 46.615 21.535  56.982 1.00 33.22  ? 48  PHE A CE1 1 
ATOM   376  C  CE2 . PHE A 1 48  ? 46.665 19.246  57.724 1.00 29.84  ? 48  PHE A CE2 1 
ATOM   377  C  CZ  . PHE A 1 48  ? 47.308 20.460  57.531 1.00 32.00  ? 48  PHE A CZ  1 
ATOM   378  N  N   . PRO A 1 49  ? 43.520 18.153  53.891 1.00 37.36  ? 49  PRO A N   1 
ATOM   379  C  CA  . PRO A 1 49  ? 44.339 17.371  52.946 1.00 38.38  ? 49  PRO A CA  1 
ATOM   380  C  C   . PRO A 1 49  ? 44.247 17.827  51.501 1.00 41.46  ? 49  PRO A C   1 
ATOM   381  O  O   . PRO A 1 49  ? 45.238 17.713  50.772 1.00 45.21  ? 49  PRO A O   1 
ATOM   382  C  CB  . PRO A 1 49  ? 43.811 15.937  53.099 1.00 40.97  ? 49  PRO A CB  1 
ATOM   383  C  CG  . PRO A 1 49  ? 43.025 15.901  54.331 1.00 39.51  ? 49  PRO A CG  1 
ATOM   384  C  CD  . PRO A 1 49  ? 42.635 17.297  54.703 1.00 38.85  ? 49  PRO A CD  1 
ATOM   385  N  N   . GLN A 1 50  ? 43.092 18.315  51.046 1.00 48.09  ? 50  GLN A N   1 
ATOM   386  C  CA  . GLN A 1 50  ? 42.966 18.727  49.650 1.00 51.42  ? 50  GLN A CA  1 
ATOM   387  C  C   . GLN A 1 50  ? 43.847 19.917  49.304 1.00 51.62  ? 50  GLN A C   1 
ATOM   388  O  O   . GLN A 1 50  ? 44.168 20.112  48.128 1.00 51.47  ? 50  GLN A O   1 
ATOM   389  C  CB  . GLN A 1 50  ? 41.519 19.087  49.331 1.00 55.36  ? 50  GLN A CB  1 
ATOM   390  C  CG  . GLN A 1 50  ? 40.516 18.056  49.805 1.00 64.29  ? 50  GLN A CG  1 
ATOM   391  C  CD  . GLN A 1 50  ? 39.100 18.412  49.413 1.00 70.18  ? 50  GLN A CD  1 
ATOM   392  O  OE1 . GLN A 1 50  ? 38.582 19.462  49.805 1.00 71.77  ? 50  GLN A OE1 1 
ATOM   393  N  NE2 . GLN A 1 50  ? 38.465 17.544  48.632 1.00 73.24  ? 50  GLN A NE2 1 
ATOM   394  N  N   . VAL A 1 51  ? 44.262 20.700  50.297 1.00 45.90  ? 51  VAL A N   1 
ATOM   395  C  CA  . VAL A 1 51  ? 44.636 22.084  50.050 1.00 52.16  ? 51  VAL A CA  1 
ATOM   396  C  C   . VAL A 1 51  ? 45.907 22.421  50.825 1.00 57.02  ? 51  VAL A C   1 
ATOM   397  O  O   . VAL A 1 51  ? 46.396 23.557  50.770 1.00 54.09  ? 51  VAL A O   1 
ATOM   398  C  CB  . VAL A 1 51  ? 43.479 23.008  50.476 1.00 49.77  ? 51  VAL A CB  1 
ATOM   399  C  CG1 . VAL A 1 51  ? 43.396 23.125  52.025 1.00 49.10  ? 51  VAL A CG1 1 
ATOM   400  C  CG2 . VAL A 1 51  ? 43.557 24.323  49.808 1.00 56.24  ? 51  VAL A CG2 1 
ATOM   401  N  N   . ALA A 1 52  ? 46.448 21.428  51.548 1.00 62.43  ? 52  ALA A N   1 
ATOM   402  C  CA  . ALA A 1 52  ? 47.440 21.695  52.592 1.00 70.03  ? 52  ALA A CA  1 
ATOM   403  C  C   . ALA A 1 52  ? 48.723 22.290  52.019 1.00 74.22  ? 52  ALA A C   1 
ATOM   404  O  O   . ALA A 1 52  ? 49.197 23.337  52.485 1.00 74.55  ? 52  ALA A O   1 
ATOM   405  C  CB  . ALA A 1 52  ? 47.750 20.413  53.367 1.00 62.12  ? 52  ALA A CB  1 
ATOM   406  N  N   . ALA A 1 53  ? 49.313 21.625  51.021 1.00 72.18  ? 53  ALA A N   1 
ATOM   407  C  CA  . ALA A 1 53  ? 50.526 22.133  50.387 1.00 71.72  ? 53  ALA A CA  1 
ATOM   408  C  C   . ALA A 1 53  ? 50.228 22.685  48.996 1.00 77.67  ? 53  ALA A C   1 
ATOM   409  O  O   . ALA A 1 53  ? 50.848 22.278  48.006 1.00 88.68  ? 53  ALA A O   1 
ATOM   410  C  CB  . ALA A 1 53  ? 51.607 21.050  50.304 1.00 63.81  ? 53  ALA A CB  1 
ATOM   411  N  N   . THR A 1 54  ? 49.253 23.593  48.911 1.00 64.40  ? 54  THR A N   1 
ATOM   412  C  CA  . THR A 1 54  ? 49.110 24.478  47.764 1.00 61.44  ? 54  THR A CA  1 
ATOM   413  C  C   . THR A 1 54  ? 49.006 25.927  48.226 1.00 64.39  ? 54  THR A C   1 
ATOM   414  O  O   . THR A 1 54  ? 48.744 26.815  47.403 1.00 60.67  ? 54  THR A O   1 
ATOM   415  C  CB  . THR A 1 54  ? 47.898 24.100  46.903 1.00 61.66  ? 54  THR A CB  1 
ATOM   416  O  OG1 . THR A 1 54  ? 46.701 24.588  47.524 1.00 74.00  ? 54  THR A OG1 1 
ATOM   417  C  CG2 . THR A 1 54  ? 47.803 22.574  46.720 1.00 56.50  ? 54  THR A CG2 1 
ATOM   418  N  N   . GLY A 1 55  ? 49.222 26.185  49.523 1.00 56.37  ? 55  GLY A N   1 
ATOM   419  C  CA  . GLY A 1 55  ? 49.200 27.521  50.071 1.00 56.41  ? 55  GLY A CA  1 
ATOM   420  C  C   . GLY A 1 55  ? 47.846 27.996  50.550 1.00 69.23  ? 55  GLY A C   1 
ATOM   421  O  O   . GLY A 1 55  ? 47.761 29.077  51.151 1.00 72.17  ? 55  GLY A O   1 
ATOM   422  N  N   . ASP A 1 56  ? 46.783 27.231  50.311 1.00 65.36  ? 56  ASP A N   1 
ATOM   423  C  CA  . ASP A 1 56  ? 45.451 27.657  50.705 1.00 65.15  ? 56  ASP A CA  1 
ATOM   424  C  C   . ASP A 1 56  ? 44.962 26.962  51.968 1.00 56.44  ? 56  ASP A C   1 
ATOM   425  O  O   . ASP A 1 56  ? 43.788 27.106  52.320 1.00 58.73  ? 56  ASP A O   1 
ATOM   426  C  CB  . ASP A 1 56  ? 44.459 27.428  49.565 1.00 66.03  ? 56  ASP A CB  1 
ATOM   427  C  CG  . ASP A 1 56  ? 44.927 28.012  48.250 1.00 66.25  ? 56  ASP A CG  1 
ATOM   428  O  OD1 . ASP A 1 56  ? 44.816 29.248  48.072 1.00 63.65  ? 56  ASP A OD1 1 
ATOM   429  O  OD2 . ASP A 1 56  ? 45.397 27.221  47.394 1.00 62.00  ? 56  ASP A OD2 1 
ATOM   430  N  N   . GLY A 1 57  ? 45.822 26.208  52.651 1.00 44.05  ? 57  GLY A N   1 
ATOM   431  C  CA  . GLY A 1 57  ? 45.500 25.711  53.968 1.00 43.10  ? 57  GLY A CA  1 
ATOM   432  C  C   . GLY A 1 57  ? 45.762 26.769  55.024 1.00 37.96  ? 57  GLY A C   1 
ATOM   433  O  O   . GLY A 1 57  ? 45.976 27.949  54.721 1.00 42.65  ? 57  GLY A O   1 
ATOM   434  N  N   . PRO A 1 58  ? 45.744 26.369  56.297 1.00 29.72  ? 58  PRO A N   1 
ATOM   435  C  CA  . PRO A 1 58  ? 46.172 27.289  57.357 1.00 29.67  ? 58  PRO A CA  1 
ATOM   436  C  C   . PRO A 1 58  ? 47.603 26.990  57.815 1.00 30.19  ? 58  PRO A C   1 
ATOM   437  O  O   . PRO A 1 58  ? 48.152 25.941  57.464 1.00 31.45  ? 58  PRO A O   1 
ATOM   438  C  CB  . PRO A 1 58  ? 45.164 27.003  58.460 1.00 29.34  ? 58  PRO A CB  1 
ATOM   439  C  CG  . PRO A 1 58  ? 44.985 25.487  58.323 1.00 32.36  ? 58  PRO A CG  1 
ATOM   440  C  CD  . PRO A 1 58  ? 45.146 25.144  56.847 1.00 29.53  ? 58  PRO A CD  1 
ATOM   441  N  N   . ASP A 1 59  ? 48.235 27.880  58.584 1.00 28.48  ? 59  ASP A N   1 
ATOM   442  C  CA  . ASP A 1 59  ? 49.478 27.453  59.229 1.00 31.75  ? 59  ASP A CA  1 
ATOM   443  C  C   . ASP A 1 59  ? 49.172 26.485  60.352 1.00 31.09  ? 59  ASP A C   1 
ATOM   444  O  O   . ASP A 1 59  ? 49.981 25.598  60.662 1.00 30.96  ? 59  ASP A O   1 
ATOM   445  C  CB  . ASP A 1 59  ? 50.263 28.654  59.754 1.00 30.93  ? 59  ASP A CB  1 
ATOM   446  C  CG  . ASP A 1 59  ? 50.527 29.697  58.676 1.00 33.16  ? 59  ASP A CG  1 
ATOM   447  O  OD1 . ASP A 1 59  ? 51.571 29.588  57.978 1.00 33.72  ? 59  ASP A OD1 1 
ATOM   448  O  OD2 . ASP A 1 59  ? 49.692 30.634  58.531 1.00 33.15  ? 59  ASP A OD2 1 
ATOM   449  N  N   . ILE A 1 60  ? 47.986 26.614  60.931 1.00 28.29  ? 60  ILE A N   1 
ATOM   450  C  CA  . ILE A 1 60  ? 47.604 25.902  62.141 1.00 27.73  ? 60  ILE A CA  1 
ATOM   451  C  C   . ILE A 1 60  ? 46.201 25.357  61.962 1.00 29.15  ? 60  ILE A C   1 
ATOM   452  O  O   . ILE A 1 60  ? 45.312 26.057  61.461 1.00 28.70  ? 60  ILE A O   1 
ATOM   453  C  CB  . ILE A 1 60  ? 47.656 26.818  63.386 1.00 25.87  ? 60  ILE A CB  1 
ATOM   454  C  CG1 . ILE A 1 60  ? 49.047 27.467  63.512 1.00 30.63  ? 60  ILE A CG1 1 
ATOM   455  C  CG2 . ILE A 1 60  ? 47.205 26.004  64.614 1.00 28.49  ? 60  ILE A CG2 1 
ATOM   456  C  CD1 . ILE A 1 60  ? 49.283 28.275  64.855 1.00 30.03  ? 60  ILE A CD1 1 
ATOM   457  N  N   . ILE A 1 61  ? 46.001 24.113  62.369 1.00 25.92  ? 61  ILE A N   1 
ATOM   458  C  CA  . ILE A 1 61  ? 44.691 23.496  62.335 1.00 28.41  ? 61  ILE A CA  1 
ATOM   459  C  C   . ILE A 1 61  ? 44.411 22.875  63.701 1.00 29.80  ? 61  ILE A C   1 
ATOM   460  O  O   . ILE A 1 61  ? 45.240 22.124  64.234 1.00 29.53  ? 61  ILE A O   1 
ATOM   461  C  CB  . ILE A 1 61  ? 44.599 22.444  61.212 1.00 31.82  ? 61  ILE A CB  1 
ATOM   462  C  CG1 . ILE A 1 61  ? 43.280 21.682  61.284 1.00 33.73  ? 61  ILE A CG1 1 
ATOM   463  C  CG2 . ILE A 1 61  ? 45.753 21.471  61.290 1.00 30.44  ? 61  ILE A CG2 1 
ATOM   464  C  CD1 . ILE A 1 61  ? 43.020 20.838  60.022 1.00 34.94  ? 61  ILE A CD1 1 
ATOM   465  N  N   . PHE A 1 62  ? 43.247 23.194  64.260 1.00 30.48  ? 62  PHE A N   1 
ATOM   466  C  CA  . PHE A 1 62  ? 42.716 22.535  65.445 1.00 32.98  ? 62  PHE A CA  1 
ATOM   467  C  C   . PHE A 1 62  ? 41.702 21.480  65.021 1.00 33.50  ? 62  PHE A C   1 
ATOM   468  O  O   . PHE A 1 62  ? 40.781 21.772  64.249 1.00 33.24  ? 62  PHE A O   1 
ATOM   469  C  CB  . PHE A 1 62  ? 42.029 23.539  66.375 1.00 31.33  ? 62  PHE A CB  1 
ATOM   470  C  CG  . PHE A 1 62  ? 42.948 24.573  66.973 1.00 29.99  ? 62  PHE A CG  1 
ATOM   471  C  CD1 . PHE A 1 62  ? 43.503 25.578  66.184 1.00 28.91  ? 62  PHE A CD1 1 
ATOM   472  C  CD2 . PHE A 1 62  ? 43.209 24.577  68.356 1.00 28.98  ? 62  PHE A CD2 1 
ATOM   473  C  CE1 . PHE A 1 62  ? 44.333 26.552  66.739 1.00 27.41  ? 62  PHE A CE1 1 
ATOM   474  C  CE2 . PHE A 1 62  ? 44.047 25.550  68.930 1.00 28.54  ? 62  PHE A CE2 1 
ATOM   475  C  CZ  . PHE A 1 62  ? 44.613 26.542  68.128 1.00 26.37  ? 62  PHE A CZ  1 
ATOM   476  N  N   . TRP A 1 63  ? 41.851 20.272  65.550 1.00 35.99  ? 63  TRP A N   1 
ATOM   477  C  CA  . TRP A 1 63  ? 40.875 19.206  65.357 1.00 34.56  ? 63  TRP A CA  1 
ATOM   478  C  C   . TRP A 1 63  ? 41.088 18.163  66.437 1.00 31.45  ? 63  TRP A C   1 
ATOM   479  O  O   . TRP A 1 63  ? 42.079 18.201  67.172 1.00 34.66  ? 63  TRP A O   1 
ATOM   480  C  CB  . TRP A 1 63  ? 40.990 18.537  63.975 1.00 33.44  ? 63  TRP A CB  1 
ATOM   481  C  CG  . TRP A 1 63  ? 39.733 17.804  63.602 1.00 32.02  ? 63  TRP A CG  1 
ATOM   482  C  CD1 . TRP A 1 63  ? 39.510 16.447  63.679 1.00 34.52  ? 63  TRP A CD1 1 
ATOM   483  C  CD2 . TRP A 1 63  ? 38.507 18.382  63.125 1.00 30.58  ? 63  TRP A CD2 1 
ATOM   484  N  NE1 . TRP A 1 63  ? 38.230 16.151  63.254 1.00 33.35  ? 63  TRP A NE1 1 
ATOM   485  C  CE2 . TRP A 1 63  ? 37.592 17.318  62.914 1.00 33.24  ? 63  TRP A CE2 1 
ATOM   486  C  CE3 . TRP A 1 63  ? 38.090 19.694  62.855 1.00 34.25  ? 63  TRP A CE3 1 
ATOM   487  C  CZ2 . TRP A 1 63  ? 36.286 17.528  62.444 1.00 34.91  ? 63  TRP A CZ2 1 
ATOM   488  C  CZ3 . TRP A 1 63  ? 36.780 19.899  62.377 1.00 35.34  ? 63  TRP A CZ3 1 
ATOM   489  C  CH2 . TRP A 1 63  ? 35.904 18.821  62.177 1.00 33.90  ? 63  TRP A CH2 1 
ATOM   490  N  N   . ALA A 1 64  ? 40.152 17.212  66.500 1.00 29.07  ? 64  ALA A N   1 
ATOM   491  C  CA  . ALA A 1 64  ? 40.349 16.002  67.281 1.00 31.25  ? 64  ALA A CA  1 
ATOM   492  C  C   . ALA A 1 64  ? 41.622 15.286  66.835 1.00 32.88  ? 64  ALA A C   1 
ATOM   493  O  O   . ALA A 1 64  ? 41.890 15.147  65.636 1.00 31.70  ? 64  ALA A O   1 
ATOM   494  C  CB  . ALA A 1 64  ? 39.134 15.082  67.148 1.00 27.32  ? 64  ALA A CB  1 
ATOM   495  N  N   . HIS A 1 65  ? 42.402 14.810  67.815 1.00 31.43  ? 65  HIS A N   1 
ATOM   496  C  CA  . HIS A 1 65  ? 43.709 14.228  67.500 1.00 33.78  ? 65  HIS A CA  1 
ATOM   497  C  C   . HIS A 1 65  ? 43.616 13.050  66.540 1.00 32.40  ? 65  HIS A C   1 
ATOM   498  O  O   . HIS A 1 65  ? 44.582 12.765  65.819 1.00 30.69  ? 65  HIS A O   1 
ATOM   499  C  CB  . HIS A 1 65  ? 44.390 13.732  68.762 1.00 33.80  ? 65  HIS A CB  1 
ATOM   500  C  CG  . HIS A 1 65  ? 43.777 12.479  69.289 1.00 31.38  ? 65  HIS A CG  1 
ATOM   501  N  ND1 . HIS A 1 65  ? 42.592 12.476  69.993 1.00 30.26  ? 65  HIS A ND1 1 
ATOM   502  C  CD2 . HIS A 1 65  ? 44.151 11.184  69.172 1.00 31.11  ? 65  HIS A CD2 1 
ATOM   503  C  CE1 . HIS A 1 65  ? 42.276 11.232  70.310 1.00 33.08  ? 65  HIS A CE1 1 
ATOM   504  N  NE2 . HIS A 1 65  ? 43.209 10.431  69.829 1.00 29.24  ? 65  HIS A NE2 1 
ATOM   505  N  N   . ASP A 1 66  ? 42.504 12.313  66.557 1.00 32.99  ? 66  ASP A N   1 
ATOM   506  C  CA  . ASP A 1 66  ? 42.488 11.043  65.837 1.00 39.45  ? 66  ASP A CA  1 
ATOM   507  C  C   . ASP A 1 66  ? 42.569 11.234  64.324 1.00 36.34  ? 66  ASP A C   1 
ATOM   508  O  O   . ASP A 1 66  ? 43.004 10.318  63.620 1.00 35.40  ? 66  ASP A O   1 
ATOM   509  C  CB  . ASP A 1 66  ? 41.254 10.208  66.236 1.00 41.24  ? 66  ASP A CB  1 
ATOM   510  C  CG  . ASP A 1 66  ? 39.928 10.850  65.827 1.00 44.65  ? 66  ASP A CG  1 
ATOM   511  O  OD1 . ASP A 1 66  ? 39.644 12.004  66.214 1.00 45.34  ? 66  ASP A OD1 1 
ATOM   512  O  OD2 . ASP A 1 66  ? 39.141 10.176  65.135 1.00 49.88  ? 66  ASP A OD2 1 
ATOM   513  N  N   . ARG A 1 67  ? 42.214 12.410  63.816 1.00 35.08  ? 67  ARG A N   1 
ATOM   514  C  CA  . ARG A 1 67  ? 42.398 12.700  62.394 1.00 37.43  ? 67  ARG A CA  1 
ATOM   515  C  C   . ARG A 1 67  ? 43.846 13.005  62.052 1.00 36.23  ? 67  ARG A C   1 
ATOM   516  O  O   . ARG A 1 67  ? 44.224 12.903  60.882 1.00 36.35  ? 67  ARG A O   1 
ATOM   517  C  CB  . ARG A 1 67  ? 41.529 13.891  61.980 1.00 42.48  ? 67  ARG A CB  1 
ATOM   518  C  CG  . ARG A 1 67  ? 41.118 13.924  60.513 1.00 50.20  ? 67  ARG A CG  1 
ATOM   519  C  CD  . ARG A 1 67  ? 40.043 12.891  60.189 1.00 52.15  ? 67  ARG A CD  1 
ATOM   520  N  NE  . ARG A 1 67  ? 39.149 13.342  59.126 1.00 59.39  ? 67  ARG A NE  1 
ATOM   521  C  CZ  . ARG A 1 67  ? 39.489 13.499  57.850 1.00 60.43  ? 67  ARG A CZ  1 
ATOM   522  N  NH1 . ARG A 1 67  ? 40.726 13.279  57.428 1.00 59.31  ? 67  ARG A NH1 1 
ATOM   523  N  NH2 . ARG A 1 67  ? 38.559 13.880  56.970 1.00 60.51  ? 67  ARG A NH2 1 
ATOM   524  N  N   . PHE A 1 68  ? 44.662 13.380  63.048 1.00 32.94  ? 68  PHE A N   1 
ATOM   525  C  CA  . PHE A 1 68  ? 45.992 13.890  62.750 1.00 39.07  ? 68  PHE A CA  1 
ATOM   526  C  C   . PHE A 1 68  ? 46.933 12.773  62.326 1.00 36.92  ? 68  PHE A C   1 
ATOM   527  O  O   . PHE A 1 68  ? 47.902 13.033  61.608 1.00 36.90  ? 68  PHE A O   1 
ATOM   528  C  CB  . PHE A 1 68  ? 46.566 14.639  63.959 1.00 40.31  ? 68  PHE A CB  1 
ATOM   529  C  CG  . PHE A 1 68  ? 46.047 16.046  64.114 1.00 39.29  ? 68  PHE A CG  1 
ATOM   530  C  CD1 . PHE A 1 68  ? 45.137 16.575  63.216 1.00 43.75  ? 68  PHE A CD1 1 
ATOM   531  C  CD2 . PHE A 1 68  ? 46.458 16.834  65.171 1.00 38.91  ? 68  PHE A CD2 1 
ATOM   532  C  CE1 . PHE A 1 68  ? 44.661 17.877  63.357 1.00 38.67  ? 68  PHE A CE1 1 
ATOM   533  C  CE2 . PHE A 1 68  ? 45.984 18.132  65.320 1.00 42.30  ? 68  PHE A CE2 1 
ATOM   534  C  CZ  . PHE A 1 68  ? 45.076 18.653  64.410 1.00 37.11  ? 68  PHE A CZ  1 
ATOM   535  N  N   . GLY A 1 69  ? 46.679 11.538  62.778 1.00 38.09  ? 69  GLY A N   1 
ATOM   536  C  CA  . GLY A 1 69  ? 47.505 10.415  62.362 1.00 34.32  ? 69  GLY A CA  1 
ATOM   537  C  C   . GLY A 1 69  ? 47.475 10.209  60.855 1.00 35.24  ? 69  GLY A C   1 
ATOM   538  O  O   . GLY A 1 69  ? 48.520 10.028  60.216 1.00 39.40  ? 69  GLY A O   1 
ATOM   539  N  N   . GLY A 1 70  ? 46.280 10.250  60.261 1.00 33.43  ? 70  GLY A N   1 
ATOM   540  C  CA  . GLY A 1 70  ? 46.203 10.212  58.805 1.00 36.12  ? 70  GLY A CA  1 
ATOM   541  C  C   . GLY A 1 70  ? 46.928 11.377  58.150 1.00 38.75  ? 70  GLY A C   1 
ATOM   542  O  O   . GLY A 1 70  ? 47.627 11.202  57.142 1.00 35.72  ? 70  GLY A O   1 
ATOM   543  N  N   . TYR A 1 71  ? 46.792 12.579  58.732 1.00 32.46  ? 71  TYR A N   1 
ATOM   544  C  CA  . TYR A 1 71  ? 47.503 13.752  58.231 1.00 34.59  ? 71  TYR A CA  1 
ATOM   545  C  C   . TYR A 1 71  ? 49.012 13.532  58.261 1.00 31.87  ? 71  TYR A C   1 
ATOM   546  O  O   . TYR A 1 71  ? 49.724 13.833  57.294 1.00 34.89  ? 71  TYR A O   1 
ATOM   547  C  CB  . TYR A 1 71  ? 47.155 14.987  59.072 1.00 36.89  ? 71  TYR A CB  1 
ATOM   548  C  CG  . TYR A 1 71  ? 45.738 15.498  58.975 1.00 40.25  ? 71  TYR A CG  1 
ATOM   549  C  CD1 . TYR A 1 71  ? 44.868 15.057  57.984 1.00 38.48  ? 71  TYR A CD1 1 
ATOM   550  C  CD2 . TYR A 1 71  ? 45.272 16.437  59.886 1.00 42.61  ? 71  TYR A CD2 1 
ATOM   551  C  CE1 . TYR A 1 71  ? 43.571 15.549  57.910 1.00 37.61  ? 71  TYR A CE1 1 
ATOM   552  C  CE2 . TYR A 1 71  ? 43.993 16.921  59.824 1.00 39.99  ? 71  TYR A CE2 1 
ATOM   553  C  CZ  . TYR A 1 71  ? 43.139 16.480  58.832 1.00 40.39  ? 71  TYR A CZ  1 
ATOM   554  O  OH  . TYR A 1 71  ? 41.855 16.992  58.772 1.00 36.44  ? 71  TYR A OH  1 
ATOM   555  N  N   . ALA A 1 72  ? 49.516 13.043  59.389 1.00 30.71  ? 72  ALA A N   1 
ATOM   556  C  CA  . ALA A 1 72  ? 50.944 12.828  59.535 1.00 34.49  ? 72  ALA A CA  1 
ATOM   557  C  C   . ALA A 1 72  ? 51.433 11.808  58.525 1.00 38.78  ? 72  ALA A C   1 
ATOM   558  O  O   . ALA A 1 72  ? 52.502 11.979  57.928 1.00 39.00  ? 72  ALA A O   1 
ATOM   559  C  CB  . ALA A 1 72  ? 51.263 12.371  60.970 1.00 33.28  ? 72  ALA A CB  1 
ATOM   560  N  N   . GLN A 1 73  ? 50.653 10.742  58.317 1.00 40.36  ? 73  GLN A N   1 
ATOM   561  C  CA  . GLN A 1 73  ? 51.031 9.720   57.350 1.00 41.60  ? 73  GLN A CA  1 
ATOM   562  C  C   . GLN A 1 73  ? 51.103 10.282  55.937 1.00 36.43  ? 73  GLN A C   1 
ATOM   563  O  O   . GLN A 1 73  ? 51.877 9.791   55.113 1.00 33.29  ? 73  GLN A O   1 
ATOM   564  C  CB  . GLN A 1 73  ? 50.043 8.563   57.404 1.00 47.04  ? 73  GLN A CB  1 
ATOM   565  C  CG  . GLN A 1 73  ? 50.607 7.260   56.910 1.00 57.94  ? 73  GLN A CG  1 
ATOM   566  C  CD  . GLN A 1 73  ? 49.584 6.154   56.993 1.00 77.08  ? 73  GLN A CD  1 
ATOM   567  O  OE1 . GLN A 1 73  ? 49.819 5.125   57.633 1.00 85.13  ? 73  GLN A OE1 1 
ATOM   568  N  NE2 . GLN A 1 73  ? 48.442 6.354   56.344 1.00 82.91  ? 73  GLN A NE2 1 
ATOM   569  N  N   . SER A 1 74  ? 50.315 11.300  55.636 1.00 34.84  ? 74  SER A N   1 
ATOM   570  C  CA  . SER A 1 74  ? 50.387 11.954  54.340 1.00 35.22  ? 74  SER A CA  1 
ATOM   571  C  C   . SER A 1 74  ? 51.412 13.079  54.302 1.00 33.93  ? 74  SER A C   1 
ATOM   572  O  O   . SER A 1 74  ? 51.453 13.821  53.322 1.00 32.91  ? 74  SER A O   1 
ATOM   573  C  CB  . SER A 1 74  ? 49.012 12.484  53.969 1.00 34.18  ? 74  SER A CB  1 
ATOM   574  O  OG  . SER A 1 74  ? 48.052 11.481  54.237 1.00 33.58  ? 74  SER A OG  1 
ATOM   575  N  N   . GLY A 1 75  ? 52.225 13.241  55.351 1.00 34.43  ? 75  GLY A N   1 
ATOM   576  C  CA  . GLY A 1 75  ? 53.201 14.315  55.351 1.00 34.18  ? 75  GLY A CA  1 
ATOM   577  C  C   . GLY A 1 75  ? 52.639 15.715  55.479 1.00 31.12  ? 75  GLY A C   1 
ATOM   578  O  O   . GLY A 1 75  ? 53.308 16.671  55.106 1.00 36.61  ? 75  GLY A O   1 
ATOM   579  N  N   . LEU A 1 76  ? 51.446 15.883  56.020 1.00 33.00  ? 76  LEU A N   1 
ATOM   580  C  CA  . LEU A 1 76  ? 50.884 17.228  56.130 1.00 32.62  ? 76  LEU A CA  1 
ATOM   581  C  C   . LEU A 1 76  ? 51.239 17.970  57.420 1.00 29.02  ? 76  LEU A C   1 
ATOM   582  O  O   . LEU A 1 76  ? 50.931 19.162  57.510 1.00 29.76  ? 76  LEU A O   1 
ATOM   583  C  CB  . LEU A 1 76  ? 49.350 17.191  56.023 1.00 31.14  ? 76  LEU A CB  1 
ATOM   584  C  CG  . LEU A 1 76  ? 48.734 16.347  54.918 1.00 35.51  ? 76  LEU A CG  1 
ATOM   585  C  CD1 . LEU A 1 76  ? 47.219 16.322  55.087 1.00 35.48  ? 76  LEU A CD1 1 
ATOM   586  C  CD2 . LEU A 1 76  ? 49.145 16.903  53.539 1.00 34.40  ? 76  LEU A CD2 1 
ATOM   587  N  N   . LEU A 1 77  ? 51.838 17.326  58.426 1.00 25.81  ? 77  LEU A N   1 
ATOM   588  C  CA  . LEU A 1 77  ? 52.041 17.978  59.720 1.00 28.05  ? 77  LEU A CA  1 
ATOM   589  C  C   . LEU A 1 77  ? 53.529 18.133  60.035 1.00 31.84  ? 77  LEU A C   1 
ATOM   590  O  O   . LEU A 1 77  ? 54.297 17.178  59.914 1.00 37.72  ? 77  LEU A O   1 
ATOM   591  C  CB  . LEU A 1 77  ? 51.344 17.212  60.834 1.00 29.03  ? 77  LEU A CB  1 
ATOM   592  C  CG  . LEU A 1 77  ? 49.801 17.294  60.816 1.00 36.16  ? 77  LEU A CG  1 
ATOM   593  C  CD1 . LEU A 1 77  ? 49.162 16.404  61.908 1.00 39.83  ? 77  LEU A CD1 1 
ATOM   594  C  CD2 . LEU A 1 77  ? 49.273 18.732  60.912 1.00 34.50  ? 77  LEU A CD2 1 
ATOM   595  N  N   . ALA A 1 78  ? 53.934 19.343  60.423 1.00 30.13  ? 78  ALA A N   1 
ATOM   596  C  CA  . ALA A 1 78  ? 55.277 19.527  60.941 1.00 31.08  ? 78  ALA A CA  1 
ATOM   597  C  C   . ALA A 1 78  ? 55.432 18.771  62.255 1.00 35.80  ? 78  ALA A C   1 
ATOM   598  O  O   . ALA A 1 78  ? 54.450 18.485  62.943 1.00 31.22  ? 78  ALA A O   1 
ATOM   599  C  CB  . ALA A 1 78  ? 55.565 21.001  61.165 1.00 32.07  ? 78  ALA A CB  1 
ATOM   600  N  N   . GLU A 1 79  ? 56.678 18.419  62.583 1.00 36.35  ? 79  GLU A N   1 
ATOM   601  C  CA  . GLU A 1 79  ? 56.999 17.849  63.886 1.00 38.02  ? 79  GLU A CA  1 
ATOM   602  C  C   . GLU A 1 79  ? 57.215 18.971  64.889 1.00 36.12  ? 79  GLU A C   1 
ATOM   603  O  O   . GLU A 1 79  ? 57.782 20.013  64.570 1.00 37.78  ? 79  GLU A O   1 
ATOM   604  C  CB  . GLU A 1 79  ? 58.238 16.958  63.816 1.00 41.86  ? 79  GLU A CB  1 
ATOM   605  C  CG  . GLU A 1 79  ? 58.763 16.502  65.186 1.00 46.87  ? 79  GLU A CG  1 
ATOM   606  C  CD  . GLU A 1 79  ? 59.957 15.535  65.094 1.00 47.87  ? 79  GLU A CD  1 
ATOM   607  O  OE1 . GLU A 1 79  ? 60.492 15.323  63.988 1.00 44.83  ? 79  GLU A OE1 1 
ATOM   608  O  OE2 . GLU A 1 79  ? 60.355 14.978  66.135 1.00 43.07  ? 79  GLU A OE2 1 
ATOM   609  N  N   . ILE A 1 80  ? 56.748 18.762  66.078 1.00 37.71  ? 80  ILE A N   1 
ATOM   610  C  CA  . ILE A 1 80  ? 56.604 19.823  67.060 1.00 42.25  ? 80  ILE A CA  1 
ATOM   611  C  C   . ILE A 1 80  ? 57.777 19.739  68.033 1.00 33.82  ? 80  ILE A C   1 
ATOM   612  O  O   . ILE A 1 80  ? 58.281 18.651  68.281 1.00 36.55  ? 80  ILE A O   1 
ATOM   613  C  CB  . ILE A 1 80  ? 55.235 19.632  67.734 1.00 48.33  ? 80  ILE A CB  1 
ATOM   614  C  CG1 . ILE A 1 80  ? 54.239 20.393  66.894 1.00 52.08  ? 80  ILE A CG1 1 
ATOM   615  C  CG2 . ILE A 1 80  ? 55.225 20.215  69.080 1.00 61.85  ? 80  ILE A CG2 1 
ATOM   616  C  CD1 . ILE A 1 80  ? 54.340 21.819  67.127 1.00 52.16  ? 80  ILE A CD1 1 
ATOM   617  N  N   . THR A 1 81  ? 58.270 20.889  68.556 1.00 32.79  ? 81  THR A N   1 
ATOM   618  C  CA  . THR A 1 81  ? 59.503 20.793  69.347 1.00 33.94  ? 81  THR A CA  1 
ATOM   619  C  C   . THR A 1 81  ? 59.398 21.390  70.758 1.00 34.96  ? 81  THR A C   1 
ATOM   620  O  O   . THR A 1 81  ? 60.323 22.074  71.210 1.00 34.26  ? 81  THR A O   1 
ATOM   621  C  CB  . THR A 1 81  ? 60.661 21.467  68.611 1.00 32.30  ? 81  THR A CB  1 
ATOM   622  O  OG1 . THR A 1 81  ? 60.336 22.833  68.377 1.00 33.27  ? 81  THR A OG1 1 
ATOM   623  C  CG2 . THR A 1 81  ? 60.945 20.795  67.268 1.00 35.45  ? 81  THR A CG2 1 
ATOM   624  N  N   . PRO A 1 82  ? 58.316 21.154  71.497 1.00 38.07  ? 82  PRO A N   1 
ATOM   625  C  CA  . PRO A 1 82  ? 58.191 21.805  72.804 1.00 37.81  ? 82  PRO A CA  1 
ATOM   626  C  C   . PRO A 1 82  ? 59.239 21.259  73.765 1.00 36.22  ? 82  PRO A C   1 
ATOM   627  O  O   . PRO A 1 82  ? 59.530 20.062  73.777 1.00 40.73  ? 82  PRO A O   1 
ATOM   628  C  CB  . PRO A 1 82  ? 56.773 21.427  73.244 1.00 36.31  ? 82  PRO A CB  1 
ATOM   629  C  CG  . PRO A 1 82  ? 56.598 20.064  72.682 1.00 36.18  ? 82  PRO A CG  1 
ATOM   630  C  CD  . PRO A 1 82  ? 57.362 20.036  71.362 1.00 31.92  ? 82  PRO A CD  1 
ATOM   631  N  N   . ALA A 1 83  ? 59.812 22.148  74.569 1.00 37.88  ? 83  ALA A N   1 
ATOM   632  C  CA  . ALA A 1 83  ? 60.834 21.726  75.518 1.00 35.50  ? 83  ALA A CA  1 
ATOM   633  C  C   . ALA A 1 83  ? 60.225 20.834  76.598 1.00 34.64  ? 83  ALA A C   1 
ATOM   634  O  O   . ALA A 1 83  ? 59.027 20.869  76.869 1.00 35.98  ? 83  ALA A O   1 
ATOM   635  C  CB  . ALA A 1 83  ? 61.514 22.944  76.136 1.00 34.76  ? 83  ALA A CB  1 
ATOM   636  N  N   . ALA A 1 84  ? 61.077 20.024  77.225 1.00 42.60  ? 84  ALA A N   1 
ATOM   637  C  CA  . ALA A 1 84  ? 60.627 19.168  78.318 1.00 41.60  ? 84  ALA A CA  1 
ATOM   638  C  C   . ALA A 1 84  ? 59.846 19.942  79.373 1.00 40.12  ? 84  ALA A C   1 
ATOM   639  O  O   . ALA A 1 84  ? 58.913 19.404  79.978 1.00 42.80  ? 84  ALA A O   1 
ATOM   640  C  CB  . ALA A 1 84  ? 61.827 18.474  78.955 1.00 41.23  ? 84  ALA A CB  1 
ATOM   641  N  N   . ALA A 1 85  ? 60.193 21.205  79.599 1.00 36.63  ? 85  ALA A N   1 
ATOM   642  C  CA  . ALA A 1 85  ? 59.510 21.974  80.627 1.00 41.63  ? 85  ALA A CA  1 
ATOM   643  C  C   . ALA A 1 85  ? 58.166 22.486  80.136 1.00 41.57  ? 85  ALA A C   1 
ATOM   644  O  O   . ALA A 1 85  ? 57.247 22.682  80.934 1.00 45.25  ? 85  ALA A O   1 
ATOM   645  C  CB  . ALA A 1 85  ? 60.393 23.140  81.090 1.00 43.66  ? 85  ALA A CB  1 
ATOM   646  N  N   . PHE A 1 86  ? 58.024 22.723  78.837 1.00 38.92  ? 86  PHE A N   1 
ATOM   647  C  CA  . PHE A 1 86  ? 56.691 23.021  78.350 1.00 35.25  ? 86  PHE A CA  1 
ATOM   648  C  C   . PHE A 1 86  ? 55.794 21.793  78.469 1.00 40.92  ? 86  PHE A C   1 
ATOM   649  O  O   . PHE A 1 86  ? 54.623 21.906  78.866 1.00 40.79  ? 86  PHE A O   1 
ATOM   650  C  CB  . PHE A 1 86  ? 56.725 23.531  76.915 1.00 32.03  ? 86  PHE A CB  1 
ATOM   651  C  CG  . PHE A 1 86  ? 55.349 23.863  76.397 1.00 36.52  ? 86  PHE A CG  1 
ATOM   652  C  CD1 . PHE A 1 86  ? 54.803 25.121  76.622 1.00 33.65  ? 86  PHE A CD1 1 
ATOM   653  C  CD2 . PHE A 1 86  ? 54.566 22.886  75.779 1.00 32.53  ? 86  PHE A CD2 1 
ATOM   654  C  CE1 . PHE A 1 86  ? 53.533 25.418  76.216 1.00 34.66  ? 86  PHE A CE1 1 
ATOM   655  C  CE2 . PHE A 1 86  ? 53.286 23.185  75.327 1.00 35.64  ? 86  PHE A CE2 1 
ATOM   656  C  CZ  . PHE A 1 86  ? 52.764 24.451  75.554 1.00 36.12  ? 86  PHE A CZ  1 
ATOM   657  N  N   . GLN A 1 87  ? 56.335 20.608  78.157 1.00 37.98  ? 87  GLN A N   1 
ATOM   658  C  CA  . GLN A 1 87  ? 55.513 19.411  78.149 1.00 40.23  ? 87  GLN A CA  1 
ATOM   659  C  C   . GLN A 1 87  ? 54.980 19.091  79.538 1.00 46.05  ? 87  GLN A C   1 
ATOM   660  O  O   . GLN A 1 87  ? 53.847 18.603  79.670 1.00 48.61  ? 87  GLN A O   1 
ATOM   661  C  CB  . GLN A 1 87  ? 56.309 18.242  77.587 1.00 41.78  ? 87  GLN A CB  1 
ATOM   662  C  CG  . GLN A 1 87  ? 56.712 18.404  76.118 1.00 41.66  ? 87  GLN A CG  1 
ATOM   663  C  CD  . GLN A 1 87  ? 57.544 17.224  75.641 1.00 44.25  ? 87  GLN A CD  1 
ATOM   664  O  OE1 . GLN A 1 87  ? 57.304 16.091  76.049 1.00 42.29  ? 87  GLN A OE1 1 
ATOM   665  N  NE2 . GLN A 1 87  ? 58.531 17.486  74.784 1.00 45.59  ? 87  GLN A NE2 1 
ATOM   666  N  N   . ASP A 1 88  ? 55.760 19.403  80.584 1.00 47.43  ? 88  ASP A N   1 
ATOM   667  C  CA  . ASP A 1 88  ? 55.322 19.116  81.945 1.00 46.35  ? 88  ASP A CA  1 
ATOM   668  C  C   . ASP A 1 88  ? 54.057 19.880  82.310 1.00 45.94  ? 88  ASP A C   1 
ATOM   669  O  O   . ASP A 1 88  ? 53.291 19.422  83.163 1.00 47.59  ? 88  ASP A O   1 
ATOM   670  C  CB  . ASP A 1 88  ? 56.435 19.440  82.943 1.00 48.65  ? 88  ASP A CB  1 
ATOM   671  C  CG  . ASP A 1 88  ? 57.700 18.664  82.669 1.00 51.91  ? 88  ASP A CG  1 
ATOM   672  O  OD1 . ASP A 1 88  ? 57.598 17.562  82.083 1.00 50.33  ? 88  ASP A OD1 1 
ATOM   673  O  OD2 . ASP A 1 88  ? 58.798 19.166  83.018 1.00 57.20  ? 88  ASP A OD2 1 
ATOM   674  N  N   . LYS A 1 89  ? 53.820 21.040  81.685 1.00 46.97  ? 89  LYS A N   1 
ATOM   675  C  CA  . LYS A 1 89  ? 52.652 21.858  82.022 1.00 44.84  ? 89  LYS A CA  1 
ATOM   676  C  C   . LYS A 1 89  ? 51.330 21.186  81.651 1.00 41.48  ? 89  LYS A C   1 
ATOM   677  O  O   . LYS A 1 89  ? 50.271 21.614  82.123 1.00 36.13  ? 89  LYS A O   1 
ATOM   678  C  CB  . LYS A 1 89  ? 52.728 23.215  81.316 1.00 47.63  ? 89  LYS A CB  1 
ATOM   679  C  CG  . LYS A 1 89  ? 53.758 24.167  81.841 1.00 52.09  ? 89  LYS A CG  1 
ATOM   680  C  CD  . LYS A 1 89  ? 54.244 25.079  80.715 1.00 60.37  ? 89  LYS A CD  1 
ATOM   681  C  CE  . LYS A 1 89  ? 54.551 26.466  81.220 1.00 63.72  ? 89  LYS A CE  1 
ATOM   682  N  NZ  . LYS A 1 89  ? 56.006 26.697  81.370 1.00 70.47  ? 89  LYS A NZ  1 
ATOM   683  N  N   . LEU A 1 90  ? 51.368 20.156  80.818 1.00 38.57  ? 90  LEU A N   1 
ATOM   684  C  CA  . LEU A 1 90  ? 50.183 19.460  80.359 1.00 36.23  ? 90  LEU A CA  1 
ATOM   685  C  C   . LEU A 1 90  ? 50.190 18.059  80.952 1.00 39.94  ? 90  LEU A C   1 
ATOM   686  O  O   . LEU A 1 90  ? 51.258 17.483  81.196 1.00 36.95  ? 90  LEU A O   1 
ATOM   687  C  CB  . LEU A 1 90  ? 50.156 19.382  78.824 1.00 36.87  ? 90  LEU A CB  1 
ATOM   688  C  CG  . LEU A 1 90  ? 49.612 20.544  77.989 1.00 39.60  ? 90  LEU A CG  1 
ATOM   689  C  CD1 . LEU A 1 90  ? 50.286 21.836  78.324 1.00 43.67  ? 90  LEU A CD1 1 
ATOM   690  C  CD2 . LEU A 1 90  ? 49.729 20.264  76.476 1.00 40.02  ? 90  LEU A CD2 1 
ATOM   691  N  N   . TYR A 1 91  ? 48.994 17.510  81.174 1.00 41.04  ? 91  TYR A N   1 
ATOM   692  C  CA  . TYR A 1 91  ? 48.895 16.159  81.706 1.00 46.64  ? 91  TYR A CA  1 
ATOM   693  C  C   . TYR A 1 91  ? 49.639 15.200  80.780 1.00 44.80  ? 91  TYR A C   1 
ATOM   694  O  O   . TYR A 1 91  ? 49.486 15.296  79.554 1.00 48.66  ? 91  TYR A O   1 
ATOM   695  C  CB  . TYR A 1 91  ? 47.429 15.741  81.852 1.00 47.34  ? 91  TYR A CB  1 
ATOM   696  C  CG  . TYR A 1 91  ? 46.691 16.539  82.902 1.00 44.46  ? 91  TYR A CG  1 
ATOM   697  C  CD1 . TYR A 1 91  ? 46.811 16.225  84.259 1.00 42.60  ? 91  TYR A CD1 1 
ATOM   698  C  CD2 . TYR A 1 91  ? 45.900 17.625  82.544 1.00 41.43  ? 91  TYR A CD2 1 
ATOM   699  C  CE1 . TYR A 1 91  ? 46.157 16.963  85.219 1.00 45.23  ? 91  TYR A CE1 1 
ATOM   700  C  CE2 . TYR A 1 91  ? 45.240 18.377  83.501 1.00 43.87  ? 91  TYR A CE2 1 
ATOM   701  C  CZ  . TYR A 1 91  ? 45.370 18.035  84.840 1.00 45.32  ? 91  TYR A CZ  1 
ATOM   702  O  OH  . TYR A 1 91  ? 44.719 18.776  85.804 1.00 43.23  ? 91  TYR A OH  1 
ATOM   703  N  N   . PRO A 1 92  ? 50.456 14.283  81.318 1.00 42.11  ? 92  PRO A N   1 
ATOM   704  C  CA  . PRO A 1 92  ? 51.306 13.443  80.446 1.00 40.25  ? 92  PRO A CA  1 
ATOM   705  C  C   . PRO A 1 92  ? 50.529 12.632  79.421 1.00 42.78  ? 92  PRO A C   1 
ATOM   706  O  O   . PRO A 1 92  ? 50.954 12.503  78.258 1.00 42.04  ? 92  PRO A O   1 
ATOM   707  C  CB  . PRO A 1 92  ? 52.041 12.529  81.441 1.00 42.61  ? 92  PRO A CB  1 
ATOM   708  C  CG  . PRO A 1 92  ? 51.933 13.195  82.782 1.00 41.26  ? 92  PRO A CG  1 
ATOM   709  C  CD  . PRO A 1 92  ? 50.750 14.117  82.760 1.00 39.98  ? 92  PRO A CD  1 
ATOM   710  N  N   . PHE A 1 93  ? 49.381 12.088  79.826 1.00 38.64  ? 93  PHE A N   1 
ATOM   711  C  CA  . PHE A 1 93  ? 48.624 11.220  78.944 1.00 38.81  ? 93  PHE A CA  1 
ATOM   712  C  C   . PHE A 1 93  ? 48.137 11.942  77.684 1.00 35.81  ? 93  PHE A C   1 
ATOM   713  O  O   . PHE A 1 93  ? 47.959 11.287  76.650 1.00 32.48  ? 93  PHE A O   1 
ATOM   714  C  CB  . PHE A 1 93  ? 47.462 10.596  79.721 1.00 39.25  ? 93  PHE A CB  1 
ATOM   715  C  CG  . PHE A 1 93  ? 46.253 11.492  79.865 1.00 45.62  ? 93  PHE A CG  1 
ATOM   716  C  CD1 . PHE A 1 93  ? 46.222 12.496  80.824 1.00 42.84  ? 93  PHE A CD1 1 
ATOM   717  C  CD2 . PHE A 1 93  ? 45.128 11.298  79.068 1.00 47.31  ? 93  PHE A CD2 1 
ATOM   718  C  CE1 . PHE A 1 93  ? 45.115 13.301  80.976 1.00 42.74  ? 93  PHE A CE1 1 
ATOM   719  C  CE2 . PHE A 1 93  ? 44.013 12.106  79.213 1.00 49.74  ? 93  PHE A CE2 1 
ATOM   720  C  CZ  . PHE A 1 93  ? 44.013 13.116  80.165 1.00 49.75  ? 93  PHE A CZ  1 
ATOM   721  N  N   . THR A 1 94  ? 47.976 13.273  77.723 1.00 33.90  ? 94  THR A N   1 
ATOM   722  C  CA  . THR A 1 94  ? 47.557 13.966  76.509 1.00 35.87  ? 94  THR A CA  1 
ATOM   723  C  C   . THR A 1 94  ? 48.649 13.978  75.447 1.00 36.81  ? 94  THR A C   1 
ATOM   724  O  O   . THR A 1 94  ? 48.326 14.014  74.256 1.00 36.37  ? 94  THR A O   1 
ATOM   725  C  CB  . THR A 1 94  ? 47.084 15.399  76.796 1.00 37.86  ? 94  THR A CB  1 
ATOM   726  O  OG1 . THR A 1 94  ? 48.157 16.210  77.313 1.00 40.63  ? 94  THR A OG1 1 
ATOM   727  C  CG2 . THR A 1 94  ? 45.860 15.401  77.731 1.00 37.27  ? 94  THR A CG2 1 
ATOM   728  N  N   . TRP A 1 95  ? 49.935 13.924  75.838 1.00 39.90  ? 95  TRP A N   1 
ATOM   729  C  CA  . TRP A 1 95  ? 50.993 13.899  74.829 1.00 35.38  ? 95  TRP A CA  1 
ATOM   730  C  C   . TRP A 1 95  ? 50.996 12.585  74.064 1.00 36.08  ? 95  TRP A C   1 
ATOM   731  O  O   . TRP A 1 95  ? 51.363 12.559  72.881 1.00 40.31  ? 95  TRP A O   1 
ATOM   732  C  CB  . TRP A 1 95  ? 52.373 14.166  75.449 1.00 34.31  ? 95  TRP A CB  1 
ATOM   733  C  CG  . TRP A 1 95  ? 52.572 15.604  75.890 1.00 33.43  ? 95  TRP A CG  1 
ATOM   734  C  CD1 . TRP A 1 95  ? 52.627 16.067  77.185 1.00 38.64  ? 95  TRP A CD1 1 
ATOM   735  C  CD2 . TRP A 1 95  ? 52.710 16.758  75.056 1.00 34.32  ? 95  TRP A CD2 1 
ATOM   736  N  NE1 . TRP A 1 95  ? 52.795 17.431  77.205 1.00 36.81  ? 95  TRP A NE1 1 
ATOM   737  C  CE2 . TRP A 1 95  ? 52.857 17.883  75.915 1.00 34.84  ? 95  TRP A CE2 1 
ATOM   738  C  CE3 . TRP A 1 95  ? 52.730 16.958  73.668 1.00 32.46  ? 95  TRP A CE3 1 
ATOM   739  C  CZ2 . TRP A 1 95  ? 53.015 19.184  75.429 1.00 33.48  ? 95  TRP A CZ2 1 
ATOM   740  C  CZ3 . TRP A 1 95  ? 52.895 18.252  73.184 1.00 30.71  ? 95  TRP A CZ3 1 
ATOM   741  C  CH2 . TRP A 1 95  ? 53.034 19.349  74.063 1.00 34.02  ? 95  TRP A CH2 1 
ATOM   742  N  N   . ASP A 1 96  ? 50.561 11.496  74.697 1.00 36.43  ? 96  ASP A N   1 
ATOM   743  C  CA  . ASP A 1 96  ? 50.442 10.236  73.976 1.00 39.11  ? 96  ASP A CA  1 
ATOM   744  C  C   . ASP A 1 96  ? 49.362 10.268  72.899 1.00 38.36  ? 96  ASP A C   1 
ATOM   745  O  O   . ASP A 1 96  ? 49.352 9.383   72.037 1.00 36.63  ? 96  ASP A O   1 
ATOM   746  C  CB  . ASP A 1 96  ? 50.178 9.085   74.961 1.00 41.24  ? 96  ASP A CB  1 
ATOM   747  C  CG  . ASP A 1 96  ? 51.289 8.949   76.018 1.00 47.69  ? 96  ASP A CG  1 
ATOM   748  O  OD1 . ASP A 1 96  ? 52.466 9.299   75.717 1.00 46.03  ? 96  ASP A OD1 1 
ATOM   749  O  OD2 . ASP A 1 96  ? 50.980 8.503   77.152 1.00 49.38  ? 96  ASP A OD2 1 
ATOM   750  N  N   . ALA A 1 97  ? 48.473 11.268  72.900 1.00 34.73  ? 97  ALA A N   1 
ATOM   751  C  CA  . ALA A 1 97  ? 47.452 11.328  71.867 1.00 34.72  ? 97  ALA A CA  1 
ATOM   752  C  C   . ALA A 1 97  ? 47.943 11.980  70.579 1.00 36.79  ? 97  ALA A C   1 
ATOM   753  O  O   . ALA A 1 97  ? 47.274 11.840  69.546 1.00 33.04  ? 97  ALA A O   1 
ATOM   754  C  CB  . ALA A 1 97  ? 46.227 12.075  72.377 1.00 36.28  ? 97  ALA A CB  1 
ATOM   755  N  N   . VAL A 1 98  ? 49.086 12.674  70.613 1.00 34.29  ? 98  VAL A N   1 
ATOM   756  C  CA  . VAL A 1 98  ? 49.578 13.468  69.484 1.00 36.54  ? 98  VAL A CA  1 
ATOM   757  C  C   . VAL A 1 98  ? 50.944 12.985  69.005 1.00 37.26  ? 98  VAL A C   1 
ATOM   758  O  O   . VAL A 1 98  ? 51.757 13.785  68.528 1.00 36.75  ? 98  VAL A O   1 
ATOM   759  C  CB  . VAL A 1 98  ? 49.662 14.960  69.854 1.00 37.92  ? 98  VAL A CB  1 
ATOM   760  C  CG1 . VAL A 1 98  ? 48.279 15.560  70.020 1.00 35.98  ? 98  VAL A CG1 1 
ATOM   761  C  CG2 . VAL A 1 98  ? 50.494 15.149  71.139 1.00 36.94  ? 98  VAL A CG2 1 
ATOM   762  N  N   . ARG A 1 99  ? 51.219 11.689  69.150 1.00 38.55  ? 99  ARG A N   1 
ATOM   763  C  CA  . ARG A 1 99  ? 52.409 11.062  68.590 1.00 39.53  ? 99  ARG A CA  1 
ATOM   764  C  C   . ARG A 1 99  ? 52.067 10.297  67.320 1.00 37.65  ? 99  ARG A C   1 
ATOM   765  O  O   . ARG A 1 99  ? 51.012 9.656   67.224 1.00 40.31  ? 99  ARG A O   1 
ATOM   766  C  CB  . ARG A 1 99  ? 53.041 10.071  69.558 1.00 40.97  ? 99  ARG A CB  1 
ATOM   767  C  CG  . ARG A 1 99  ? 53.118 10.510  70.959 1.00 49.34  ? 99  ARG A CG  1 
ATOM   768  C  CD  . ARG A 1 99  ? 54.149 9.660   71.656 1.00 61.64  ? 99  ARG A CD  1 
ATOM   769  N  NE  . ARG A 1 99  ? 55.418 10.370  71.680 1.00 66.57  ? 99  ARG A NE  1 
ATOM   770  C  CZ  . ARG A 1 99  ? 55.775 11.204  72.644 1.00 58.31  ? 99  ARG A CZ  1 
ATOM   771  N  NH1 . ARG A 1 99  ? 55.023 11.368  73.724 1.00 57.73  ? 99  ARG A NH1 1 
ATOM   772  N  NH2 . ARG A 1 99  ? 56.912 11.885  72.522 1.00 60.57  ? 99  ARG A NH2 1 
ATOM   773  N  N   . TYR A 1 100 ? 52.978 10.341  66.359 1.00 36.95  ? 100 TYR A N   1 
ATOM   774  C  CA  . TYR A 1 100 ? 52.875 9.486   65.188 1.00 41.41  ? 100 TYR A CA  1 
ATOM   775  C  C   . TYR A 1 100 ? 54.270 9.061   64.769 1.00 42.73  ? 100 TYR A C   1 
ATOM   776  O  O   . TYR A 1 100 ? 55.145 9.910   64.581 1.00 44.74  ? 100 TYR A O   1 
ATOM   777  C  CB  . TYR A 1 100 ? 52.148 10.178  64.040 1.00 44.32  ? 100 TYR A CB  1 
ATOM   778  C  CG  . TYR A 1 100 ? 51.567 9.167   63.077 1.00 49.70  ? 100 TYR A CG  1 
ATOM   779  C  CD1 . TYR A 1 100 ? 50.306 8.617   63.302 1.00 49.56  ? 100 TYR A CD1 1 
ATOM   780  C  CD2 . TYR A 1 100 ? 52.260 8.774   61.942 1.00 51.25  ? 100 TYR A CD2 1 
ATOM   781  C  CE1 . TYR A 1 100 ? 49.758 7.697   62.435 1.00 53.69  ? 100 TYR A CE1 1 
ATOM   782  C  CE2 . TYR A 1 100 ? 51.711 7.853   61.058 1.00 56.48  ? 100 TYR A CE2 1 
ATOM   783  C  CZ  . TYR A 1 100 ? 50.461 7.320   61.314 1.00 54.07  ? 100 TYR A CZ  1 
ATOM   784  O  OH  . TYR A 1 100 ? 49.904 6.411   60.441 1.00 62.89  ? 100 TYR A OH  1 
ATOM   785  N  N   . ASN A 1 101 ? 54.465 7.742   64.642 1.00 48.03  ? 101 ASN A N   1 
ATOM   786  C  CA  . ASN A 1 101 ? 55.792 7.144   64.504 1.00 46.21  ? 101 ASN A CA  1 
ATOM   787  C  C   . ASN A 1 101 ? 56.757 7.699   65.547 1.00 45.44  ? 101 ASN A C   1 
ATOM   788  O  O   . ASN A 1 101 ? 57.891 8.053   65.241 1.00 50.18  ? 101 ASN A O   1 
ATOM   789  C  CB  . ASN A 1 101 ? 56.341 7.344   63.093 1.00 52.60  ? 101 ASN A CB  1 
ATOM   790  C  CG  . ASN A 1 101 ? 55.611 6.492   62.069 1.00 58.19  ? 101 ASN A CG  1 
ATOM   791  O  OD1 . ASN A 1 101 ? 55.254 5.343   62.348 1.00 59.87  ? 101 ASN A OD1 1 
ATOM   792  N  ND2 . ASN A 1 101 ? 55.373 7.053   60.881 1.00 62.14  ? 101 ASN A ND2 1 
ATOM   793  N  N   . GLY A 1 102 ? 56.289 7.812   66.793 1.00 47.58  ? 102 GLY A N   1 
ATOM   794  C  CA  . GLY A 1 102 ? 57.098 8.350   67.876 1.00 50.71  ? 102 GLY A CA  1 
ATOM   795  C  C   . GLY A 1 102 ? 57.255 9.866   67.937 1.00 58.34  ? 102 GLY A C   1 
ATOM   796  O  O   . GLY A 1 102 ? 57.652 10.388  68.992 1.00 56.36  ? 102 GLY A O   1 
ATOM   797  N  N   . LYS A 1 103 ? 56.956 10.604  66.862 1.00 51.39  ? 103 LYS A N   1 
ATOM   798  C  CA  . LYS A 1 103 ? 57.176 12.047  66.853 1.00 51.27  ? 103 LYS A CA  1 
ATOM   799  C  C   . LYS A 1 103 ? 55.931 12.806  67.310 1.00 43.15  ? 103 LYS A C   1 
ATOM   800  O  O   . LYS A 1 103 ? 54.806 12.441  66.960 1.00 38.35  ? 103 LYS A O   1 
ATOM   801  C  CB  . LYS A 1 103 ? 57.579 12.508  65.454 1.00 58.32  ? 103 LYS A CB  1 
ATOM   802  C  CG  . LYS A 1 103 ? 58.813 11.803  64.908 1.00 64.81  ? 103 LYS A CG  1 
ATOM   803  C  CD  . LYS A 1 103 ? 58.825 11.819  63.385 1.00 68.98  ? 103 LYS A CD  1 
ATOM   804  C  CE  . LYS A 1 103 ? 60.248 11.797  62.837 1.00 71.96  ? 103 LYS A CE  1 
ATOM   805  N  NZ  . LYS A 1 103 ? 60.269 11.810  61.340 1.00 71.69  ? 103 LYS A NZ  1 
ATOM   806  N  N   . LEU A 1 104 ? 56.146 13.867  68.095 1.00 36.21  ? 104 LEU A N   1 
ATOM   807  C  CA  . LEU A 1 104 ? 55.070 14.787  68.453 1.00 34.43  ? 104 LEU A CA  1 
ATOM   808  C  C   . LEU A 1 104 ? 54.620 15.553  67.217 1.00 35.47  ? 104 LEU A C   1 
ATOM   809  O  O   . LEU A 1 104 ? 55.461 16.046  66.459 1.00 33.71  ? 104 LEU A O   1 
ATOM   810  C  CB  . LEU A 1 104 ? 55.536 15.777  69.514 1.00 33.91  ? 104 LEU A CB  1 
ATOM   811  C  CG  . LEU A 1 104 ? 55.905 15.187  70.872 1.00 37.30  ? 104 LEU A CG  1 
ATOM   812  C  CD1 . LEU A 1 104 ? 56.231 16.306  71.834 1.00 41.37  ? 104 LEU A CD1 1 
ATOM   813  C  CD2 . LEU A 1 104 ? 54.741 14.359  71.392 1.00 37.08  ? 104 LEU A CD2 1 
ATOM   814  N  N   . ILE A 1 105 ? 53.297 15.672  67.018 1.00 33.03  ? 105 ILE A N   1 
ATOM   815  C  CA  . ILE A 1 105 ? 52.773 16.278  65.789 1.00 32.47  ? 105 ILE A CA  1 
ATOM   816  C  C   . ILE A 1 105 ? 51.578 17.202  66.039 1.00 32.39  ? 105 ILE A C   1 
ATOM   817  O  O   . ILE A 1 105 ? 50.938 17.663  65.084 1.00 26.72  ? 105 ILE A O   1 
ATOM   818  C  CB  . ILE A 1 105 ? 52.401 15.192  64.757 1.00 38.20  ? 105 ILE A CB  1 
ATOM   819  C  CG1 . ILE A 1 105 ? 51.691 14.009  65.434 1.00 42.19  ? 105 ILE A CG1 1 
ATOM   820  C  CG2 . ILE A 1 105 ? 53.617 14.733  63.973 1.00 36.60  ? 105 ILE A CG2 1 
ATOM   821  C  CD1 . ILE A 1 105 ? 50.165 14.188  65.557 1.00 40.52  ? 105 ILE A CD1 1 
ATOM   822  N  N   . ALA A 1 106 ? 51.277 17.504  67.305 1.00 28.02  ? 106 ALA A N   1 
ATOM   823  C  CA  . ALA A 1 106 ? 50.239 18.480  67.604 1.00 30.59  ? 106 ALA A CA  1 
ATOM   824  C  C   . ALA A 1 106 ? 50.351 18.873  69.070 1.00 32.04  ? 106 ALA A C   1 
ATOM   825  O  O   . ALA A 1 106 ? 50.928 18.137  69.869 1.00 31.07  ? 106 ALA A O   1 
ATOM   826  C  CB  . ALA A 1 106 ? 48.842 17.920  67.309 1.00 34.62  ? 106 ALA A CB  1 
ATOM   827  N  N   . TYR A 1 107 ? 49.776 20.039  69.415 1.00 33.56  ? 107 TYR A N   1 
ATOM   828  C  CA  . TYR A 1 107 ? 49.688 20.489  70.807 1.00 35.69  ? 107 TYR A CA  1 
ATOM   829  C  C   . TYR A 1 107 ? 48.329 20.123  71.389 1.00 37.11  ? 107 TYR A C   1 
ATOM   830  O  O   . TYR A 1 107 ? 47.298 20.571  70.857 1.00 29.40  ? 107 TYR A O   1 
ATOM   831  C  CB  . TYR A 1 107 ? 49.895 21.992  70.912 1.00 35.52  ? 107 TYR A CB  1 
ATOM   832  C  CG  . TYR A 1 107 ? 51.318 22.433  70.724 1.00 34.83  ? 107 TYR A CG  1 
ATOM   833  C  CD1 . TYR A 1 107 ? 51.808 22.687  69.465 1.00 32.05  ? 107 TYR A CD1 1 
ATOM   834  C  CD2 . TYR A 1 107 ? 52.188 22.581  71.817 1.00 31.47  ? 107 TYR A CD2 1 
ATOM   835  C  CE1 . TYR A 1 107 ? 53.094 23.121  69.283 1.00 29.86  ? 107 TYR A CE1 1 
ATOM   836  C  CE2 . TYR A 1 107 ? 53.505 22.998  71.638 1.00 31.56  ? 107 TYR A CE2 1 
ATOM   837  C  CZ  . TYR A 1 107 ? 53.956 23.247  70.358 1.00 29.27  ? 107 TYR A CZ  1 
ATOM   838  O  OH  . TYR A 1 107 ? 55.251 23.648  70.103 1.00 30.90  ? 107 TYR A OH  1 
ATOM   839  N  N   . PRO A 1 108 ? 48.274 19.345  72.477 1.00 35.48  ? 108 PRO A N   1 
ATOM   840  C  CA  . PRO A 1 108 ? 46.984 19.060  73.119 1.00 33.77  ? 108 PRO A CA  1 
ATOM   841  C  C   . PRO A 1 108 ? 46.358 20.336  73.662 1.00 33.27  ? 108 PRO A C   1 
ATOM   842  O  O   . PRO A 1 108 ? 47.056 21.218  74.164 1.00 30.06  ? 108 PRO A O   1 
ATOM   843  C  CB  . PRO A 1 108 ? 47.361 18.082  74.242 1.00 35.61  ? 108 PRO A CB  1 
ATOM   844  C  CG  . PRO A 1 108 ? 48.641 17.463  73.782 1.00 32.36  ? 108 PRO A CG  1 
ATOM   845  C  CD  . PRO A 1 108 ? 49.373 18.573  73.085 1.00 35.27  ? 108 PRO A CD  1 
ATOM   846  N  N   . ILE A 1 109 ? 45.029 20.444  73.528 1.00 32.63  ? 109 ILE A N   1 
ATOM   847  C  CA  . ILE A 1 109 ? 44.301 21.619  74.009 1.00 35.19  ? 109 ILE A CA  1 
ATOM   848  C  C   . ILE A 1 109 ? 43.249 21.203  75.033 1.00 35.18  ? 109 ILE A C   1 
ATOM   849  O  O   . ILE A 1 109 ? 43.288 21.639  76.191 1.00 38.64  ? 109 ILE A O   1 
ATOM   850  C  CB  . ILE A 1 109 ? 43.634 22.406  72.855 1.00 34.35  ? 109 ILE A CB  1 
ATOM   851  C  CG1 . ILE A 1 109 ? 44.642 22.790  71.748 1.00 35.33  ? 109 ILE A CG1 1 
ATOM   852  C  CG2 . ILE A 1 109 ? 42.869 23.631  73.405 1.00 29.66  ? 109 ILE A CG2 1 
ATOM   853  C  CD1 . ILE A 1 109 ? 45.807 23.707  72.188 1.00 35.56  ? 109 ILE A CD1 1 
ATOM   854  N  N   . ALA A 1 110 ? 42.286 20.378  74.610 1.00 37.32  ? 110 ALA A N   1 
ATOM   855  C  CA  . ALA A 1 110 ? 41.163 19.998  75.456 1.00 37.09  ? 110 ALA A CA  1 
ATOM   856  C  C   . ALA A 1 110 ? 40.924 18.501  75.362 1.00 34.85  ? 110 ALA A C   1 
ATOM   857  O  O   . ALA A 1 110 ? 41.353 17.839  74.410 1.00 33.03  ? 110 ALA A O   1 
ATOM   858  C  CB  . ALA A 1 110 ? 39.877 20.744  75.090 1.00 36.49  ? 110 ALA A CB  1 
ATOM   859  N  N   . VAL A 1 111 ? 40.228 17.982  76.376 1.00 33.96  ? 111 VAL A N   1 
ATOM   860  C  CA  . VAL A 1 111 ? 40.031 16.552  76.574 1.00 38.39  ? 111 VAL A CA  1 
ATOM   861  C  C   . VAL A 1 111 ? 38.553 16.307  76.830 1.00 33.35  ? 111 VAL A C   1 
ATOM   862  O  O   . VAL A 1 111 ? 37.942 17.006  77.647 1.00 34.89  ? 111 VAL A O   1 
ATOM   863  C  CB  . VAL A 1 111 ? 40.873 16.020  77.753 1.00 38.15  ? 111 VAL A CB  1 
ATOM   864  C  CG1 . VAL A 1 111 ? 40.673 14.543  77.926 1.00 37.10  ? 111 VAL A CG1 1 
ATOM   865  C  CG2 . VAL A 1 111 ? 42.344 16.356  77.567 1.00 40.41  ? 111 VAL A CG2 1 
ATOM   866  N  N   . GLU A 1 112 ? 37.984 15.313  76.137 1.00 31.50  ? 112 GLU A N   1 
ATOM   867  C  CA  . GLU A 1 112 ? 36.593 14.918  76.323 1.00 34.90  ? 112 GLU A CA  1 
ATOM   868  C  C   . GLU A 1 112 ? 36.509 13.401  76.432 1.00 34.13  ? 112 GLU A C   1 
ATOM   869  O  O   . GLU A 1 112 ? 37.357 12.672  75.904 1.00 32.63  ? 112 GLU A O   1 
ATOM   870  C  CB  . GLU A 1 112 ? 35.689 15.417  75.163 1.00 33.68  ? 112 GLU A CB  1 
ATOM   871  C  CG  . GLU A 1 112 ? 35.995 14.727  73.856 1.00 35.99  ? 112 GLU A CG  1 
ATOM   872  C  CD  . GLU A 1 112 ? 34.953 14.959  72.769 1.00 39.89  ? 112 GLU A CD  1 
ATOM   873  O  OE1 . GLU A 1 112 ? 34.074 15.852  72.912 1.00 42.80  ? 112 GLU A OE1 1 
ATOM   874  O  OE2 . GLU A 1 112 ? 35.018 14.214  71.772 1.00 38.19  ? 112 GLU A OE2 1 
ATOM   875  N  N   . ALA A 1 113 ? 35.464 12.940  77.121 1.00 37.39  ? 113 ALA A N   1 
ATOM   876  C  CA  . ALA A 1 113 ? 35.160 11.527  77.305 1.00 30.85  ? 113 ALA A CA  1 
ATOM   877  C  C   . ALA A 1 113 ? 33.741 11.410  77.830 1.00 34.61  ? 113 ALA A C   1 
ATOM   878  O  O   . ALA A 1 113 ? 33.176 12.372  78.369 1.00 37.36  ? 113 ALA A O   1 
ATOM   879  C  CB  . ALA A 1 113 ? 36.133 10.838  78.264 1.00 33.95  ? 113 ALA A CB  1 
ATOM   880  N  N   . LEU A 1 114 ? 33.169 10.217  77.664 1.00 31.14  ? 114 LEU A N   1 
ATOM   881  C  CA  . LEU A 1 114 ? 31.854 9.946   78.211 1.00 30.78  ? 114 LEU A CA  1 
ATOM   882  C  C   . LEU A 1 114 ? 31.932 9.856   79.738 1.00 32.17  ? 114 LEU A C   1 
ATOM   883  O  O   . LEU A 1 114 ? 32.976 9.519   80.316 1.00 30.53  ? 114 LEU A O   1 
ATOM   884  C  CB  . LEU A 1 114 ? 31.287 8.655   77.625 1.00 32.59  ? 114 LEU A CB  1 
ATOM   885  C  CG  . LEU A 1 114 ? 31.033 8.618   76.095 1.00 31.77  ? 114 LEU A CG  1 
ATOM   886  C  CD1 . LEU A 1 114 ? 30.955 7.191   75.635 1.00 30.74  ? 114 LEU A CD1 1 
ATOM   887  C  CD2 . LEU A 1 114 ? 29.750 9.345   75.735 1.00 33.40  ? 114 LEU A CD2 1 
ATOM   888  N  N   . SER A 1 115 ? 30.808 10.175  80.381 1.00 32.29  ? 115 SER A N   1 
ATOM   889  C  CA  . SER A 1 115 ? 30.643 10.100  81.818 1.00 34.31  ? 115 SER A CA  1 
ATOM   890  C  C   . SER A 1 115 ? 29.268 9.500   82.115 1.00 37.01  ? 115 SER A C   1 
ATOM   891  O  O   . SER A 1 115 ? 28.411 9.362   81.217 1.00 30.16  ? 115 SER A O   1 
ATOM   892  C  CB  . SER A 1 115 ? 30.785 11.484  82.451 1.00 38.05  ? 115 SER A CB  1 
ATOM   893  O  OG  . SER A 1 115 ? 32.098 11.989  82.267 1.00 41.65  ? 115 SER A OG  1 
ATOM   894  N  N   . LEU A 1 116 ? 29.064 9.147   83.395 1.00 33.04  ? 116 LEU A N   1 
ATOM   895  C  CA  . LEU A 1 116 ? 27.752 8.746   83.891 1.00 33.90  ? 116 LEU A CA  1 
ATOM   896  C  C   . LEU A 1 116 ? 26.969 9.997   84.246 1.00 31.52  ? 116 LEU A C   1 
ATOM   897  O  O   . LEU A 1 116 ? 27.440 10.805  85.046 1.00 35.19  ? 116 LEU A O   1 
ATOM   898  C  CB  . LEU A 1 116 ? 27.874 7.833   85.118 1.00 31.78  ? 116 LEU A CB  1 
ATOM   899  C  CG  . LEU A 1 116 ? 26.564 7.190   85.622 1.00 31.85  ? 116 LEU A CG  1 
ATOM   900  C  CD1 . LEU A 1 116 ? 25.930 6.246   84.591 1.00 32.14  ? 116 LEU A CD1 1 
ATOM   901  C  CD2 . LEU A 1 116 ? 26.718 6.484   87.004 1.00 32.10  ? 116 LEU A CD2 1 
ATOM   902  N  N   . ILE A 1 117 ? 25.774 10.147  83.670 1.00 30.57  ? 117 ILE A N   1 
ATOM   903  C  CA  . ILE A 1 117 ? 24.877 11.269  83.936 1.00 31.63  ? 117 ILE A CA  1 
ATOM   904  C  C   . ILE A 1 117 ? 23.645 10.719  84.642 1.00 35.91  ? 117 ILE A C   1 
ATOM   905  O  O   . ILE A 1 117 ? 23.046 9.749   84.165 1.00 39.69  ? 117 ILE A O   1 
ATOM   906  C  CB  . ILE A 1 117 ? 24.470 11.989  82.637 1.00 33.48  ? 117 ILE A CB  1 
ATOM   907  C  CG1 . ILE A 1 117 ? 25.706 12.340  81.785 1.00 36.01  ? 117 ILE A CG1 1 
ATOM   908  C  CG2 . ILE A 1 117 ? 23.596 13.207  82.964 1.00 35.79  ? 117 ILE A CG2 1 
ATOM   909  C  CD1 . ILE A 1 117 ? 25.413 13.228  80.576 1.00 36.45  ? 117 ILE A CD1 1 
ATOM   910  N  N   . TYR A 1 118 ? 23.259 11.326  85.772 1.00 35.15  ? 118 TYR A N   1 
ATOM   911  C  CA  . TYR A 1 118 ? 22.177 10.747  86.557 1.00 33.72  ? 118 TYR A CA  1 
ATOM   912  C  C   . TYR A 1 118 ? 21.228 11.805  87.107 1.00 35.62  ? 118 TYR A C   1 
ATOM   913  O  O   . TYR A 1 118 ? 21.615 12.943  87.410 1.00 34.37  ? 118 TYR A O   1 
ATOM   914  C  CB  . TYR A 1 118 ? 22.722 9.886   87.703 1.00 32.15  ? 118 TYR A CB  1 
ATOM   915  C  CG  . TYR A 1 118 ? 23.400 10.662  88.814 1.00 30.37  ? 118 TYR A CG  1 
ATOM   916  C  CD1 . TYR A 1 118 ? 24.676 11.176  88.646 1.00 33.27  ? 118 TYR A CD1 1 
ATOM   917  C  CD2 . TYR A 1 118 ? 22.772 10.844  90.042 1.00 33.05  ? 118 TYR A CD2 1 
ATOM   918  C  CE1 . TYR A 1 118 ? 25.316 11.866  89.670 1.00 34.60  ? 118 TYR A CE1 1 
ATOM   919  C  CE2 . TYR A 1 118 ? 23.401 11.534  91.081 1.00 31.74  ? 118 TYR A CE2 1 
ATOM   920  C  CZ  . TYR A 1 118 ? 24.668 12.050  90.883 1.00 31.36  ? 118 TYR A CZ  1 
ATOM   921  O  OH  . TYR A 1 118 ? 25.294 12.756  91.874 1.00 35.87  ? 118 TYR A OH  1 
ATOM   922  N  N   . ASN A 1 119 ? 19.974 11.387  87.240 1.00 32.03  ? 119 ASN A N   1 
ATOM   923  C  CA  . ASN A 1 119 ? 18.888 12.197  87.768 1.00 38.53  ? 119 ASN A CA  1 
ATOM   924  C  C   . ASN A 1 119 ? 18.895 12.094  89.288 1.00 39.74  ? 119 ASN A C   1 
ATOM   925  O  O   . ASN A 1 119 ? 18.553 11.046  89.845 1.00 44.44  ? 119 ASN A O   1 
ATOM   926  C  CB  . ASN A 1 119 ? 17.573 11.687  87.191 1.00 43.55  ? 119 ASN A CB  1 
ATOM   927  C  CG  . ASN A 1 119 ? 16.401 12.577  87.517 1.00 37.89  ? 119 ASN A CG  1 
ATOM   928  O  OD1 . ASN A 1 119 ? 16.286 13.102  88.621 1.00 34.82  ? 119 ASN A OD1 1 
ATOM   929  N  ND2 . ASN A 1 119 ? 15.515 12.745  86.548 1.00 36.08  ? 119 ASN A ND2 1 
ATOM   930  N  N   . LYS A 1 120 ? 19.290 13.178  89.959 1.00 39.89  ? 120 LYS A N   1 
ATOM   931  C  CA  . LYS A 1 120 ? 19.400 13.171  91.415 1.00 39.42  ? 120 LYS A CA  1 
ATOM   932  C  C   . LYS A 1 120 ? 18.051 13.080  92.104 1.00 40.06  ? 120 LYS A C   1 
ATOM   933  O  O   . LYS A 1 120 ? 18.002 12.656  93.262 1.00 41.84  ? 120 LYS A O   1 
ATOM   934  C  CB  . LYS A 1 120 ? 20.114 14.434  91.913 1.00 38.96  ? 120 LYS A CB  1 
ATOM   935  C  CG  . LYS A 1 120 ? 21.558 14.602  91.457 1.00 39.26  ? 120 LYS A CG  1 
ATOM   936  C  CD  . LYS A 1 120 ? 22.139 15.823  92.150 1.00 38.61  ? 120 LYS A CD  1 
ATOM   937  C  CE  . LYS A 1 120 ? 23.484 16.195  91.621 1.00 40.06  ? 120 LYS A CE  1 
ATOM   938  N  NZ  . LYS A 1 120 ? 23.748 17.650  91.841 1.00 50.26  ? 120 LYS A NZ  1 
ATOM   939  N  N   . ASP A 1 121 ? 16.970 13.512  91.439 1.00 38.15  ? 121 ASP A N   1 
ATOM   940  C  CA  . ASP A 1 121 ? 15.625 13.317  91.975 1.00 40.48  ? 121 ASP A CA  1 
ATOM   941  C  C   . ASP A 1 121 ? 15.232 11.840  91.969 1.00 46.25  ? 121 ASP A C   1 
ATOM   942  O  O   . ASP A 1 121 ? 14.548 11.372  92.884 1.00 46.56  ? 121 ASP A O   1 
ATOM   943  C  CB  . ASP A 1 121 ? 14.597 14.126  91.172 1.00 37.91  ? 121 ASP A CB  1 
ATOM   944  C  CG  . ASP A 1 121 ? 14.753 15.638  91.329 1.00 39.64  ? 121 ASP A CG  1 
ATOM   945  O  OD1 . ASP A 1 121 ? 15.576 16.134  92.134 1.00 37.76  ? 121 ASP A OD1 1 
ATOM   946  O  OD2 . ASP A 1 121 ? 14.010 16.351  90.632 1.00 42.48  ? 121 ASP A OD2 1 
ATOM   947  N  N   . LEU A 1 122 ? 15.631 11.092  90.940 1.00 44.32  ? 122 LEU A N   1 
ATOM   948  C  CA  . LEU A 1 122 ? 15.300 9.671   90.860 1.00 41.25  ? 122 LEU A CA  1 
ATOM   949  C  C   . LEU A 1 122 ? 16.323 8.776   91.543 1.00 42.48  ? 122 LEU A C   1 
ATOM   950  O  O   . LEU A 1 122 ? 15.999 7.642   91.912 1.00 43.57  ? 122 LEU A O   1 
ATOM   951  C  CB  . LEU A 1 122 ? 15.168 9.244   89.396 1.00 42.58  ? 122 LEU A CB  1 
ATOM   952  C  CG  . LEU A 1 122 ? 13.917 9.745   88.685 1.00 44.34  ? 122 LEU A CG  1 
ATOM   953  C  CD1 . LEU A 1 122 ? 13.913 9.301   87.227 1.00 46.09  ? 122 LEU A CD1 1 
ATOM   954  C  CD2 . LEU A 1 122 ? 12.671 9.228   89.404 1.00 42.76  ? 122 LEU A CD2 1 
ATOM   955  N  N   . LEU A 1 123 ? 17.538 9.264   91.726 1.00 40.02  ? 123 LEU A N   1 
ATOM   956  C  CA  . LEU A 1 123 ? 18.664 8.431   92.140 1.00 40.02  ? 123 LEU A CA  1 
ATOM   957  C  C   . LEU A 1 123 ? 19.662 9.346   92.832 1.00 40.30  ? 123 LEU A C   1 
ATOM   958  O  O   . LEU A 1 123 ? 20.642 9.796   92.234 1.00 50.26  ? 123 LEU A O   1 
ATOM   959  C  CB  . LEU A 1 123 ? 19.285 7.725   90.934 1.00 44.58  ? 123 LEU A CB  1 
ATOM   960  C  CG  . LEU A 1 123 ? 20.059 6.408   91.002 1.00 45.69  ? 123 LEU A CG  1 
ATOM   961  C  CD1 . LEU A 1 123 ? 19.398 5.388   91.896 1.00 42.41  ? 123 LEU A CD1 1 
ATOM   962  C  CD2 . LEU A 1 123 ? 20.184 5.878   89.571 1.00 45.15  ? 123 LEU A CD2 1 
ATOM   963  N  N   . PRO A 1 124 ? 19.408 9.687   94.097 1.00 41.42  ? 124 PRO A N   1 
ATOM   964  C  CA  . PRO A 1 124 ? 20.327 10.578  94.824 1.00 41.22  ? 124 PRO A CA  1 
ATOM   965  C  C   . PRO A 1 124 ? 21.752 10.075  94.876 1.00 42.36  ? 124 PRO A C   1 
ATOM   966  O  O   . PRO A 1 124 ? 22.682 10.889  94.872 1.00 45.57  ? 124 PRO A O   1 
ATOM   967  C  CB  . PRO A 1 124 ? 19.716 10.651  96.230 1.00 42.34  ? 124 PRO A CB  1 
ATOM   968  C  CG  . PRO A 1 124 ? 18.302 10.221  96.074 1.00 45.14  ? 124 PRO A CG  1 
ATOM   969  C  CD  . PRO A 1 124 ? 18.236 9.293   94.900 1.00 42.41  ? 124 PRO A CD  1 
ATOM   970  N  N   . ASN A 1 125 ? 21.962 8.764   94.947 1.00 43.56  ? 125 ASN A N   1 
ATOM   971  C  CA  . ASN A 1 125 ? 23.305 8.208   94.924 1.00 46.58  ? 125 ASN A CA  1 
ATOM   972  C  C   . ASN A 1 125 ? 23.490 7.383   93.658 1.00 44.26  ? 125 ASN A C   1 
ATOM   973  O  O   . ASN A 1 125 ? 22.754 6.402   93.448 1.00 45.14  ? 125 ASN A O   1 
ATOM   974  C  CB  . ASN A 1 125 ? 23.546 7.360   96.168 1.00 49.70  ? 125 ASN A CB  1 
ATOM   975  C  CG  . ASN A 1 125 ? 23.152 8.084   97.453 1.00 54.71  ? 125 ASN A CG  1 
ATOM   976  O  OD1 . ASN A 1 125 ? 23.043 9.309   97.480 1.00 59.22  ? 125 ASN A OD1 1 
ATOM   977  N  ND2 . ASN A 1 125 ? 22.915 7.321   98.516 1.00 62.69  ? 125 ASN A ND2 1 
ATOM   978  N  N   . PRO A 1 126 ? 24.427 7.736   92.778 1.00 41.83  ? 126 PRO A N   1 
ATOM   979  C  CA  . PRO A 1 126 ? 24.619 6.947   91.561 1.00 44.75  ? 126 PRO A CA  1 
ATOM   980  C  C   . PRO A 1 126 ? 25.307 5.631   91.874 1.00 41.90  ? 126 PRO A C   1 
ATOM   981  O  O   . PRO A 1 126 ? 26.142 5.553   92.797 1.00 42.12  ? 126 PRO A O   1 
ATOM   982  C  CB  . PRO A 1 126 ? 25.499 7.849   90.678 1.00 41.96  ? 126 PRO A CB  1 
ATOM   983  C  CG  . PRO A 1 126 ? 26.266 8.687   91.658 1.00 41.59  ? 126 PRO A CG  1 
ATOM   984  C  CD  . PRO A 1 126 ? 25.352 8.884   92.855 1.00 42.29  ? 126 PRO A CD  1 
ATOM   985  N  N   . PRO A 1 127 ? 25.011 4.568   91.124 1.00 42.66  ? 127 PRO A N   1 
ATOM   986  C  CA  . PRO A 1 127 ? 25.676 3.278   91.357 1.00 43.95  ? 127 PRO A CA  1 
ATOM   987  C  C   . PRO A 1 127 ? 27.141 3.332   90.956 1.00 36.57  ? 127 PRO A C   1 
ATOM   988  O  O   . PRO A 1 127 ? 27.477 3.801   89.866 1.00 39.54  ? 127 PRO A O   1 
ATOM   989  C  CB  . PRO A 1 127 ? 24.891 2.311   90.466 1.00 44.58  ? 127 PRO A CB  1 
ATOM   990  C  CG  . PRO A 1 127 ? 24.376 3.184   89.346 1.00 49.74  ? 127 PRO A CG  1 
ATOM   991  C  CD  . PRO A 1 127 ? 24.046 4.502   90.007 1.00 46.43  ? 127 PRO A CD  1 
ATOM   992  N  N   . LYS A 1 128 ? 28.011 2.836   91.844 1.00 37.32  ? 128 LYS A N   1 
ATOM   993  C  CA  . LYS A 1 128 ? 29.444 2.776   91.565 1.00 39.77  ? 128 LYS A CA  1 
ATOM   994  C  C   . LYS A 1 128 ? 29.791 1.684   90.562 1.00 37.22  ? 128 LYS A C   1 
ATOM   995  O  O   . LYS A 1 128 ? 30.864 1.726   89.945 1.00 37.72  ? 128 LYS A O   1 
ATOM   996  C  CB  . LYS A 1 128 ? 30.232 2.524   92.861 1.00 44.46  ? 128 LYS A CB  1 
ATOM   997  C  CG  . LYS A 1 128 ? 30.205 3.673   93.865 1.00 51.22  ? 128 LYS A CG  1 
ATOM   998  C  CD  . LYS A 1 128 ? 30.489 5.018   93.197 1.00 63.59  ? 128 LYS A CD  1 
ATOM   999  C  CE  . LYS A 1 128 ? 30.234 6.186   94.145 1.00 68.71  ? 128 LYS A CE  1 
ATOM   1000 N  NZ  . LYS A 1 128 ? 28.780 6.542   94.242 1.00 69.65  ? 128 LYS A NZ  1 
ATOM   1001 N  N   . THR A 1 129 ? 28.890 0.733   90.378 1.00 37.96  ? 129 THR A N   1 
ATOM   1002 C  CA  . THR A 1 129 ? 29.164 -0.576  89.822 1.00 37.30  ? 129 THR A CA  1 
ATOM   1003 C  C   . THR A 1 129 ? 28.132 -0.860  88.746 1.00 35.79  ? 129 THR A C   1 
ATOM   1004 O  O   . THR A 1 129 ? 26.953 -0.525  88.919 1.00 37.76  ? 129 THR A O   1 
ATOM   1005 C  CB  . THR A 1 129 ? 29.096 -1.616  90.965 1.00 38.92  ? 129 THR A CB  1 
ATOM   1006 O  OG1 . THR A 1 129 ? 30.417 -1.935  91.444 1.00 35.67  ? 129 THR A OG1 1 
ATOM   1007 C  CG2 . THR A 1 129 ? 28.358 -2.826  90.584 1.00 37.38  ? 129 THR A CG2 1 
ATOM   1008 N  N   . TRP A 1 130 ? 28.582 -1.443  87.622 1.00 34.45  ? 130 TRP A N   1 
ATOM   1009 C  CA  . TRP A 1 130 ? 27.636 -1.876  86.589 1.00 35.03  ? 130 TRP A CA  1 
ATOM   1010 C  C   . TRP A 1 130 ? 26.739 -2.990  87.109 1.00 34.00  ? 130 TRP A C   1 
ATOM   1011 O  O   . TRP A 1 130 ? 25.544 -3.051  86.779 1.00 30.21  ? 130 TRP A O   1 
ATOM   1012 C  CB  . TRP A 1 130 ? 28.376 -2.368  85.345 1.00 39.14  ? 130 TRP A CB  1 
ATOM   1013 C  CG  . TRP A 1 130 ? 28.753 -1.317  84.318 1.00 40.18  ? 130 TRP A CG  1 
ATOM   1014 C  CD1 . TRP A 1 130 ? 29.964 -0.700  84.198 1.00 36.85  ? 130 TRP A CD1 1 
ATOM   1015 C  CD2 . TRP A 1 130 ? 27.935 -0.808  83.241 1.00 35.68  ? 130 TRP A CD2 1 
ATOM   1016 N  NE1 . TRP A 1 130 ? 29.948 0.169   83.135 1.00 41.60  ? 130 TRP A NE1 1 
ATOM   1017 C  CE2 . TRP A 1 130 ? 28.717 0.130   82.533 1.00 37.77  ? 130 TRP A CE2 1 
ATOM   1018 C  CE3 . TRP A 1 130 ? 26.620 -1.041  82.824 1.00 37.25  ? 130 TRP A CE3 1 
ATOM   1019 C  CZ2 . TRP A 1 130 ? 28.232 0.838   81.413 1.00 37.72  ? 130 TRP A CZ2 1 
ATOM   1020 C  CZ3 . TRP A 1 130 ? 26.124 -0.330  81.708 1.00 36.96  ? 130 TRP A CZ3 1 
ATOM   1021 C  CH2 . TRP A 1 130 ? 26.938 0.595   81.016 1.00 37.73  ? 130 TRP A CH2 1 
ATOM   1022 N  N   . GLU A 1 131 ? 27.305 -3.891  87.920 1.00 33.71  ? 131 GLU A N   1 
ATOM   1023 C  CA  . GLU A 1 131 ? 26.569 -5.068  88.365 1.00 38.16  ? 131 GLU A CA  1 
ATOM   1024 C  C   . GLU A 1 131 ? 25.350 -4.718  89.206 1.00 43.07  ? 131 GLU A C   1 
ATOM   1025 O  O   . GLU A 1 131 ? 24.396 -5.505  89.256 1.00 40.17  ? 131 GLU A O   1 
ATOM   1026 C  CB  . GLU A 1 131 ? 27.499 -5.995  89.139 1.00 44.28  ? 131 GLU A CB  1 
ATOM   1027 C  CG  . GLU A 1 131 ? 28.537 -6.694  88.279 1.00 45.73  ? 131 GLU A CG  1 
ATOM   1028 C  CD  . GLU A 1 131 ? 29.824 -5.904  88.135 1.00 49.15  ? 131 GLU A CD  1 
ATOM   1029 O  OE1 . GLU A 1 131 ? 29.822 -4.681  88.422 1.00 46.56  ? 131 GLU A OE1 1 
ATOM   1030 O  OE2 . GLU A 1 131 ? 30.849 -6.517  87.749 1.00 49.57  ? 131 GLU A OE2 1 
ATOM   1031 N  N   . GLU A 1 132 ? 25.334 -3.562  89.852 1.00 41.91  ? 132 GLU A N   1 
ATOM   1032 C  CA  . GLU A 1 132 ? 24.195 -3.238  90.701 1.00 39.60  ? 132 GLU A CA  1 
ATOM   1033 C  C   . GLU A 1 132 ? 23.077 -2.559  89.933 1.00 37.68  ? 132 GLU A C   1 
ATOM   1034 O  O   . GLU A 1 132 ? 22.050 -2.228  90.525 1.00 46.50  ? 132 GLU A O   1 
ATOM   1035 C  CB  . GLU A 1 132 ? 24.631 -2.374  91.892 1.00 38.19  ? 132 GLU A CB  1 
ATOM   1036 C  CG  . GLU A 1 132 ? 25.036 -0.974  91.544 1.00 38.17  ? 132 GLU A CG  1 
ATOM   1037 C  CD  . GLU A 1 132 ? 25.850 -0.322  92.646 1.00 37.82  ? 132 GLU A CD  1 
ATOM   1038 O  OE1 . GLU A 1 132 ? 25.254 0.284   93.560 1.00 42.12  ? 132 GLU A OE1 1 
ATOM   1039 O  OE2 . GLU A 1 132 ? 27.085 -0.412  92.609 1.00 35.62  ? 132 GLU A OE2 1 
ATOM   1040 N  N   . ILE A 1 133 ? 23.226 -2.400  88.624 1.00 38.52  ? 133 ILE A N   1 
ATOM   1041 C  CA  . ILE A 1 133 ? 22.266 -1.649  87.822 1.00 38.60  ? 133 ILE A CA  1 
ATOM   1042 C  C   . ILE A 1 133 ? 20.980 -2.442  87.594 1.00 39.23  ? 133 ILE A C   1 
ATOM   1043 O  O   . ILE A 1 133 ? 19.888 -1.845  87.664 1.00 35.86  ? 133 ILE A O   1 
ATOM   1044 C  CB  . ILE A 1 133 ? 22.910 -1.205  86.499 1.00 38.27  ? 133 ILE A CB  1 
ATOM   1045 C  CG1 . ILE A 1 133 ? 23.865 -0.045  86.772 1.00 41.01  ? 133 ILE A CG1 1 
ATOM   1046 C  CG2 . ILE A 1 133 ? 21.850 -0.848  85.470 1.00 38.17  ? 133 ILE A CG2 1 
ATOM   1047 C  CD1 . ILE A 1 133 ? 24.070 0.874   85.606 1.00 41.42  ? 133 ILE A CD1 1 
ATOM   1048 N  N   . PRO A 1 134 ? 21.033 -3.762  87.306 1.00 38.75  ? 134 PRO A N   1 
ATOM   1049 C  CA  . PRO A 1 134 ? 19.769 -4.488  87.076 1.00 38.11  ? 134 PRO A CA  1 
ATOM   1050 C  C   . PRO A 1 134 ? 18.806 -4.389  88.245 1.00 37.30  ? 134 PRO A C   1 
ATOM   1051 O  O   . PRO A 1 134 ? 17.601 -4.158  88.036 1.00 42.12  ? 134 PRO A O   1 
ATOM   1052 C  CB  . PRO A 1 134 ? 20.234 -5.937  86.830 1.00 38.52  ? 134 PRO A CB  1 
ATOM   1053 C  CG  . PRO A 1 134 ? 21.598 -5.788  86.280 1.00 37.20  ? 134 PRO A CG  1 
ATOM   1054 C  CD  . PRO A 1 134 ? 22.191 -4.646  87.079 1.00 37.14  ? 134 PRO A CD  1 
ATOM   1055 N  N   . ALA A 1 135 ? 19.311 -4.547  89.474 1.00 34.58  ? 135 ALA A N   1 
ATOM   1056 C  CA  . ALA A 1 135 ? 18.468 -4.373  90.656 1.00 39.14  ? 135 ALA A CA  1 
ATOM   1057 C  C   . ALA A 1 135 ? 17.828 -2.992  90.673 1.00 42.66  ? 135 ALA A C   1 
ATOM   1058 O  O   . ALA A 1 135 ? 16.615 -2.860  90.897 1.00 50.25  ? 135 ALA A O   1 
ATOM   1059 C  CB  . ALA A 1 135 ? 19.281 -4.606  91.933 1.00 37.05  ? 135 ALA A CB  1 
ATOM   1060 N  N   . LEU A 1 136 ? 18.629 -1.946  90.418 1.00 42.67  ? 136 LEU A N   1 
ATOM   1061 C  CA  . LEU A 1 136 ? 18.095 -0.587  90.340 1.00 41.78  ? 136 LEU A CA  1 
ATOM   1062 C  C   . LEU A 1 136 ? 16.919 -0.509  89.372 1.00 40.14  ? 136 LEU A C   1 
ATOM   1063 O  O   . LEU A 1 136 ? 15.906 0.141   89.654 1.00 41.17  ? 136 LEU A O   1 
ATOM   1064 C  CB  . LEU A 1 136 ? 19.195 0.380   89.902 1.00 48.26  ? 136 LEU A CB  1 
ATOM   1065 C  CG  . LEU A 1 136 ? 20.104 1.020   90.945 1.00 49.57  ? 136 LEU A CG  1 
ATOM   1066 C  CD1 . LEU A 1 136 ? 20.922 2.133   90.312 1.00 51.79  ? 136 LEU A CD1 1 
ATOM   1067 C  CD2 . LEU A 1 136 ? 19.285 1.541   92.110 1.00 52.05  ? 136 LEU A CD2 1 
ATOM   1068 N  N   . ASP A 1 137 ? 17.034 -1.179  88.224 1.00 38.51  ? 137 ASP A N   1 
ATOM   1069 C  CA  . ASP A 1 137 ? 15.972 -1.109  87.223 1.00 41.00  ? 137 ASP A CA  1 
ATOM   1070 C  C   . ASP A 1 137 ? 14.703 -1.811  87.700 1.00 43.68  ? 137 ASP A C   1 
ATOM   1071 O  O   . ASP A 1 137 ? 13.593 -1.347  87.422 1.00 39.07  ? 137 ASP A O   1 
ATOM   1072 C  CB  . ASP A 1 137 ? 16.453 -1.713  85.909 1.00 39.57  ? 137 ASP A CB  1 
ATOM   1073 C  CG  . ASP A 1 137 ? 15.491 -1.453  84.783 1.00 37.72  ? 137 ASP A CG  1 
ATOM   1074 O  OD1 . ASP A 1 137 ? 15.320 -0.275  84.419 1.00 37.55  ? 137 ASP A OD1 1 
ATOM   1075 O  OD2 . ASP A 1 137 ? 14.885 -2.419  84.282 1.00 37.77  ? 137 ASP A OD2 1 
ATOM   1076 N  N   . LYS A 1 138 ? 14.840 -2.936  88.411 1.00 48.16  ? 138 LYS A N   1 
ATOM   1077 C  CA  . LYS A 1 138 ? 13.677 -3.532  89.070 1.00 49.29  ? 138 LYS A CA  1 
ATOM   1078 C  C   . LYS A 1 138 ? 12.986 -2.519  89.990 1.00 46.89  ? 138 LYS A C   1 
ATOM   1079 O  O   . LYS A 1 138 ? 11.759 -2.354  89.946 1.00 45.14  ? 138 LYS A O   1 
ATOM   1080 C  CB  . LYS A 1 138 ? 14.098 -4.772  89.867 1.00 49.78  ? 138 LYS A CB  1 
ATOM   1081 C  CG  . LYS A 1 138 ? 14.294 -6.056  89.064 1.00 49.77  ? 138 LYS A CG  1 
ATOM   1082 C  CD  . LYS A 1 138 ? 14.608 -7.221  90.015 1.00 52.72  ? 138 LYS A CD  1 
ATOM   1083 C  CE  . LYS A 1 138 ? 15.058 -8.501  89.278 1.00 56.76  ? 138 LYS A CE  1 
ATOM   1084 N  NZ  . LYS A 1 138 ? 16.407 -8.404  88.633 1.00 53.20  ? 138 LYS A NZ  1 
ATOM   1085 N  N   . GLU A 1 139 ? 13.764 -1.835  90.837 1.00 42.81  ? 139 GLU A N   1 
ATOM   1086 C  CA  . GLU A 1 139 ? 13.193 -0.848  91.748 1.00 50.22  ? 139 GLU A CA  1 
ATOM   1087 C  C   . GLU A 1 139 ? 12.533 0.302   90.982 1.00 53.16  ? 139 GLU A C   1 
ATOM   1088 O  O   . GLU A 1 139 ? 11.410 0.714   91.307 1.00 55.24  ? 139 GLU A O   1 
ATOM   1089 C  CB  . GLU A 1 139 ? 14.288 -0.347  92.697 1.00 56.65  ? 139 GLU A CB  1 
ATOM   1090 C  CG  . GLU A 1 139 ? 13.919 0.825   93.604 1.00 73.07  ? 139 GLU A CG  1 
ATOM   1091 C  CD  . GLU A 1 139 ? 14.435 2.180   93.105 1.00 81.31  ? 139 GLU A CD  1 
ATOM   1092 O  OE1 . GLU A 1 139 ? 15.661 2.445   93.196 1.00 77.81  ? 139 GLU A OE1 1 
ATOM   1093 O  OE2 . GLU A 1 139 ? 13.605 2.992   92.640 1.00 88.71  ? 139 GLU A OE2 1 
ATOM   1094 N  N   . LEU A 1 140 ? 13.188 0.805   89.935 1.00 46.28  ? 140 LEU A N   1 
ATOM   1095 C  CA  . LEU A 1 140 ? 12.644 1.965   89.239 1.00 47.17  ? 140 LEU A CA  1 
ATOM   1096 C  C   . LEU A 1 140 ? 11.471 1.591   88.346 1.00 43.35  ? 140 LEU A C   1 
ATOM   1097 O  O   . LEU A 1 140 ? 10.531 2.379   88.200 1.00 50.12  ? 140 LEU A O   1 
ATOM   1098 C  CB  . LEU A 1 140 ? 13.742 2.650   88.424 1.00 49.57  ? 140 LEU A CB  1 
ATOM   1099 C  CG  . LEU A 1 140 ? 14.652 3.546   89.260 1.00 46.71  ? 140 LEU A CG  1 
ATOM   1100 C  CD1 . LEU A 1 140 ? 15.877 3.882   88.485 1.00 49.58  ? 140 LEU A CD1 1 
ATOM   1101 C  CD2 . LEU A 1 140 ? 13.914 4.806   89.672 1.00 46.69  ? 140 LEU A CD2 1 
ATOM   1102 N  N   . LYS A 1 141 ? 11.522 0.413   87.719 1.00 43.89  ? 141 LYS A N   1 
ATOM   1103 C  CA  . LYS A 1 141 ? 10.402 -0.047  86.903 1.00 42.70  ? 141 LYS A CA  1 
ATOM   1104 C  C   . LYS A 1 141 ? 9.121  -0.104  87.719 1.00 40.75  ? 141 LYS A C   1 
ATOM   1105 O  O   . LYS A 1 141 ? 8.035  0.193   87.208 1.00 36.84  ? 141 LYS A O   1 
ATOM   1106 C  CB  . LYS A 1 141 ? 10.713 -1.420  86.308 1.00 45.78  ? 141 LYS A CB  1 
ATOM   1107 C  CG  . LYS A 1 141 ? 11.540 -1.370  85.032 1.00 49.24  ? 141 LYS A CG  1 
ATOM   1108 C  CD  . LYS A 1 141 ? 10.696 -0.962  83.839 1.00 45.14  ? 141 LYS A CD  1 
ATOM   1109 C  CE  . LYS A 1 141 ? 11.582 -0.519  82.687 1.00 46.64  ? 141 LYS A CE  1 
ATOM   1110 N  NZ  . LYS A 1 141 ? 12.879 -1.277  82.645 1.00 45.05  ? 141 LYS A NZ  1 
ATOM   1111 N  N   . ALA A 1 142 ? 9.233  -0.471  89.000 1.00 40.01  ? 142 ALA A N   1 
ATOM   1112 C  CA  . ALA A 1 142 ? 8.062  -0.525  89.863 1.00 46.07  ? 142 ALA A CA  1 
ATOM   1113 C  C   . ALA A 1 142 ? 7.517  0.858   90.180 1.00 50.38  ? 142 ALA A C   1 
ATOM   1114 O  O   . ALA A 1 142 ? 6.402  0.964   90.712 1.00 47.12  ? 142 ALA A O   1 
ATOM   1115 C  CB  . ALA A 1 142 ? 8.399  -1.272  91.148 1.00 45.10  ? 142 ALA A CB  1 
ATOM   1116 N  N   . LYS A 1 143 ? 8.268  1.913   89.858 1.00 49.75  ? 143 LYS A N   1 
ATOM   1117 C  CA  . LYS A 1 143 ? 7.791  3.283   89.968 1.00 49.07  ? 143 LYS A CA  1 
ATOM   1118 C  C   . LYS A 1 143 ? 7.504  3.907   88.611 1.00 43.95  ? 143 LYS A C   1 
ATOM   1119 O  O   . LYS A 1 143 ? 7.302  5.120   88.534 1.00 45.19  ? 143 LYS A O   1 
ATOM   1120 C  CB  . LYS A 1 143 ? 8.796  4.136   90.740 1.00 49.10  ? 143 LYS A CB  1 
ATOM   1121 C  CG  . LYS A 1 143 ? 9.143  3.561   92.099 1.00 53.50  ? 143 LYS A CG  1 
ATOM   1122 C  CD  . LYS A 1 143 ? 10.562 3.911   92.500 1.00 56.39  ? 143 LYS A CD  1 
ATOM   1123 C  CE  . LYS A 1 143 ? 10.601 4.685   93.806 1.00 60.59  ? 143 LYS A CE  1 
ATOM   1124 N  NZ  . LYS A 1 143 ? 11.797 4.309   94.619 1.00 65.76  ? 143 LYS A NZ  1 
ATOM   1125 N  N   . GLY A 1 144 ? 7.456  3.111   87.544 1.00 44.51  ? 144 GLY A N   1 
ATOM   1126 C  CA  . GLY A 1 144 ? 7.189  3.652   86.230 1.00 42.76  ? 144 GLY A CA  1 
ATOM   1127 C  C   . GLY A 1 144 ? 8.379  4.273   85.540 1.00 42.17  ? 144 GLY A C   1 
ATOM   1128 O  O   . GLY A 1 144 ? 8.208  4.917   84.500 1.00 43.53  ? 144 GLY A O   1 
ATOM   1129 N  N   . LYS A 1 145 ? 9.572  4.104   86.071 1.00 40.14  ? 145 LYS A N   1 
ATOM   1130 C  CA  . LYS A 1 145 ? 10.767 4.646   85.462 1.00 43.44  ? 145 LYS A CA  1 
ATOM   1131 C  C   . LYS A 1 145 ? 11.652 3.491   85.016 1.00 42.26  ? 145 LYS A C   1 
ATOM   1132 O  O   . LYS A 1 145 ? 11.222 2.337   84.971 1.00 49.71  ? 145 LYS A O   1 
ATOM   1133 C  CB  . LYS A 1 145 ? 11.489 5.573   86.448 1.00 47.50  ? 145 LYS A CB  1 
ATOM   1134 C  CG  . LYS A 1 145 ? 11.120 7.041   86.297 1.00 51.90  ? 145 LYS A CG  1 
ATOM   1135 C  CD  . LYS A 1 145 ? 9.626  7.275   86.497 1.00 56.30  ? 145 LYS A CD  1 
ATOM   1136 C  CE  . LYS A 1 145 ? 9.275  8.749   86.600 1.00 58.29  ? 145 LYS A CE  1 
ATOM   1137 N  NZ  . LYS A 1 145 ? 9.899  9.569   85.537 1.00 64.29  ? 145 LYS A NZ  1 
ATOM   1138 N  N   . SER A 1 146 ? 12.898 3.812   84.684 1.00 47.78  ? 146 SER A N   1 
ATOM   1139 C  CA  . SER A 1 146 ? 13.906 2.809   84.382 1.00 42.02  ? 146 SER A CA  1 
ATOM   1140 C  C   . SER A 1 146 ? 15.244 3.343   84.856 1.00 36.50  ? 146 SER A C   1 
ATOM   1141 O  O   . SER A 1 146 ? 15.395 4.532   85.146 1.00 37.04  ? 146 SER A O   1 
ATOM   1142 C  CB  . SER A 1 146 ? 13.957 2.480   82.893 1.00 41.65  ? 146 SER A CB  1 
ATOM   1143 O  OG  . SER A 1 146 ? 14.703 3.476   82.222 1.00 42.85  ? 146 SER A OG  1 
ATOM   1144 N  N   . ALA A 1 147 ? 16.223 2.446   84.925 1.00 35.29  ? 147 ALA A N   1 
ATOM   1145 C  CA  . ALA A 1 147 ? 17.511 2.787   85.521 1.00 31.17  ? 147 ALA A CA  1 
ATOM   1146 C  C   . ALA A 1 147 ? 18.405 3.525   84.541 1.00 34.69  ? 147 ALA A C   1 
ATOM   1147 O  O   . ALA A 1 147 ? 18.978 4.564   84.880 1.00 39.16  ? 147 ALA A O   1 
ATOM   1148 C  CB  . ALA A 1 147 ? 18.214 1.529   86.012 1.00 33.74  ? 147 ALA A CB  1 
ATOM   1149 N  N   . LEU A 1 148 ? 18.530 3.007   83.317 1.00 35.45  ? 148 LEU A N   1 
ATOM   1150 C  CA  . LEU A 1 148 ? 19.611 3.435   82.443 1.00 36.07  ? 148 LEU A CA  1 
ATOM   1151 C  C   . LEU A 1 148 ? 19.202 3.335   80.979 1.00 34.64  ? 148 LEU A C   1 
ATOM   1152 O  O   . LEU A 1 148 ? 18.749 2.276   80.527 1.00 31.61  ? 148 LEU A O   1 
ATOM   1153 C  CB  . LEU A 1 148 ? 20.866 2.586   82.697 1.00 35.05  ? 148 LEU A CB  1 
ATOM   1154 C  CG  . LEU A 1 148 ? 22.039 2.872   81.753 1.00 33.63  ? 148 LEU A CG  1 
ATOM   1155 C  CD1 . LEU A 1 148 ? 22.608 4.275   81.942 1.00 32.94  ? 148 LEU A CD1 1 
ATOM   1156 C  CD2 . LEU A 1 148 ? 23.134 1.834   81.974 1.00 36.05  ? 148 LEU A CD2 1 
ATOM   1157 N  N   . MET A 1 149 ? 19.406 4.424   80.240 1.00 33.22  ? 149 MET A N   1 
ATOM   1158 C  CA  . MET A 1 149 ? 19.225 4.421   78.791 1.00 37.83  ? 149 MET A CA  1 
ATOM   1159 C  C   . MET A 1 149 ? 20.334 5.243   78.168 1.00 44.42  ? 149 MET A C   1 
ATOM   1160 O  O   . MET A 1 149 ? 20.501 6.416   78.519 1.00 43.42  ? 149 MET A O   1 
ATOM   1161 C  CB  . MET A 1 149 ? 17.869 4.999   78.388 1.00 43.23  ? 149 MET A CB  1 
ATOM   1162 C  CG  . MET A 1 149 ? 16.706 4.049   78.552 1.00 43.06  ? 149 MET A CG  1 
ATOM   1163 S  SD  . MET A 1 149 ? 15.175 4.817   78.015 1.00 47.59  ? 149 MET A SD  1 
ATOM   1164 C  CE  . MET A 1 149 ? 15.291 4.601   76.240 1.00 42.67  ? 149 MET A CE  1 
ATOM   1165 N  N   . PHE A 1 150 ? 21.091 4.625   77.260 1.00 42.74  ? 150 PHE A N   1 
ATOM   1166 C  CA  . PHE A 1 150 ? 22.076 5.327   76.452 1.00 36.03  ? 150 PHE A CA  1 
ATOM   1167 C  C   . PHE A 1 150 ? 22.120 4.699   75.059 1.00 33.27  ? 150 PHE A C   1 
ATOM   1168 O  O   . PHE A 1 150 ? 21.542 3.632   74.819 1.00 34.76  ? 150 PHE A O   1 
ATOM   1169 C  CB  . PHE A 1 150 ? 23.439 5.308   77.114 1.00 35.52  ? 150 PHE A CB  1 
ATOM   1170 C  CG  . PHE A 1 150 ? 24.064 3.952   77.186 1.00 40.03  ? 150 PHE A CG  1 
ATOM   1171 C  CD1 . PHE A 1 150 ? 23.523 2.962   77.985 1.00 38.26  ? 150 PHE A CD1 1 
ATOM   1172 C  CD2 . PHE A 1 150 ? 25.229 3.681   76.494 1.00 44.56  ? 150 PHE A CD2 1 
ATOM   1173 C  CE1 . PHE A 1 150 ? 24.129 1.731   78.080 1.00 36.73  ? 150 PHE A CE1 1 
ATOM   1174 C  CE2 . PHE A 1 150 ? 25.827 2.444   76.575 1.00 45.94  ? 150 PHE A CE2 1 
ATOM   1175 C  CZ  . PHE A 1 150 ? 25.273 1.468   77.370 1.00 40.91  ? 150 PHE A CZ  1 
ATOM   1176 N  N   . ASN A 1 151 ? 22.819 5.371   74.142 1.00 32.53  ? 151 ASN A N   1 
ATOM   1177 C  CA  . ASN A 1 151 ? 22.842 4.960   72.736 1.00 31.49  ? 151 ASN A CA  1 
ATOM   1178 C  C   . ASN A 1 151 ? 23.515 3.593   72.570 1.00 34.49  ? 151 ASN A C   1 
ATOM   1179 O  O   . ASN A 1 151 ? 24.692 3.419   72.908 1.00 33.32  ? 151 ASN A O   1 
ATOM   1180 C  CB  . ASN A 1 151 ? 23.563 6.023   71.913 1.00 31.69  ? 151 ASN A CB  1 
ATOM   1181 C  CG  . ASN A 1 151 ? 23.629 5.688   70.424 1.00 35.35  ? 151 ASN A CG  1 
ATOM   1182 O  OD1 . ASN A 1 151 ? 22.962 4.769   69.927 1.00 33.51  ? 151 ASN A OD1 1 
ATOM   1183 N  ND2 . ASN A 1 151 ? 24.451 6.443   69.704 1.00 36.80  ? 151 ASN A ND2 1 
ATOM   1184 N  N   . LEU A 1 152 ? 22.762 2.614   72.068 1.00 34.39  ? 152 LEU A N   1 
ATOM   1185 C  CA  . LEU A 1 152 ? 23.277 1.257   71.895 1.00 39.68  ? 152 LEU A CA  1 
ATOM   1186 C  C   . LEU A 1 152 ? 23.716 0.960   70.464 1.00 43.08  ? 152 LEU A C   1 
ATOM   1187 O  O   . LEU A 1 152 ? 24.237 -0.129  70.206 1.00 50.71  ? 152 LEU A O   1 
ATOM   1188 C  CB  . LEU A 1 152 ? 22.219 0.228   72.323 1.00 36.91  ? 152 LEU A CB  1 
ATOM   1189 C  CG  . LEU A 1 152 ? 21.804 0.166   73.798 1.00 38.49  ? 152 LEU A CG  1 
ATOM   1190 C  CD1 . LEU A 1 152 ? 21.244 -1.228  74.120 1.00 38.24  ? 152 LEU A CD1 1 
ATOM   1191 C  CD2 . LEU A 1 152 ? 22.960 0.557   74.766 1.00 35.72  ? 152 LEU A CD2 1 
ATOM   1192 N  N   . GLN A 1 153 ? 23.531 1.900   69.534 1.00 44.00  ? 153 GLN A N   1 
ATOM   1193 C  CA  . GLN A 1 153 ? 23.859 1.687   68.129 1.00 43.83  ? 153 GLN A CA  1 
ATOM   1194 C  C   . GLN A 1 153 ? 25.306 2.010   67.765 1.00 45.65  ? 153 GLN A C   1 
ATOM   1195 O  O   . GLN A 1 153 ? 25.783 1.522   66.736 1.00 58.52  ? 153 GLN A O   1 
ATOM   1196 C  CB  . GLN A 1 153 ? 22.946 2.536   67.247 1.00 45.19  ? 153 GLN A CB  1 
ATOM   1197 C  CG  . GLN A 1 153 ? 21.492 2.504   67.651 1.00 46.90  ? 153 GLN A CG  1 
ATOM   1198 C  CD  . GLN A 1 153 ? 20.943 1.098   67.648 1.00 49.89  ? 153 GLN A CD  1 
ATOM   1199 O  OE1 . GLN A 1 153 ? 20.921 0.447   66.611 1.00 45.65  ? 153 GLN A OE1 1 
ATOM   1200 N  NE2 . GLN A 1 153 ? 20.499 0.618   68.807 1.00 53.18  ? 153 GLN A NE2 1 
ATOM   1201 N  N   . GLU A 1 154 ? 26.013 2.828   68.552 1.00 44.20  ? 154 GLU A N   1 
ATOM   1202 C  CA  . GLU A 1 154 ? 27.371 3.263   68.193 1.00 43.94  ? 154 GLU A CA  1 
ATOM   1203 C  C   . GLU A 1 154 ? 28.401 2.607   69.098 1.00 40.97  ? 154 GLU A C   1 
ATOM   1204 O  O   . GLU A 1 154 ? 28.339 2.766   70.329 1.00 43.28  ? 154 GLU A O   1 
ATOM   1205 C  CB  . GLU A 1 154 ? 27.526 4.786   68.277 1.00 46.59  ? 154 GLU A CB  1 
ATOM   1206 C  CG  . GLU A 1 154 ? 26.576 5.599   67.436 1.00 53.50  ? 154 GLU A CG  1 
ATOM   1207 C  CD  . GLU A 1 154 ? 26.892 5.544   65.958 1.00 60.12  ? 154 GLU A CD  1 
ATOM   1208 O  OE1 . GLU A 1 154 ? 28.085 5.370   65.605 1.00 62.53  ? 154 GLU A OE1 1 
ATOM   1209 O  OE2 . GLU A 1 154 ? 25.936 5.681   65.158 1.00 56.76  ? 154 GLU A OE2 1 
ATOM   1210 N  N   . PRO A 1 155 ? 29.391 1.919   68.542 1.00 38.92  ? 155 PRO A N   1 
ATOM   1211 C  CA  . PRO A 1 155 ? 30.418 1.304   69.403 1.00 40.46  ? 155 PRO A CA  1 
ATOM   1212 C  C   . PRO A 1 155 ? 31.135 2.300   70.303 1.00 41.76  ? 155 PRO A C   1 
ATOM   1213 O  O   . PRO A 1 155 ? 31.631 1.905   71.368 1.00 39.01  ? 155 PRO A O   1 
ATOM   1214 C  CB  . PRO A 1 155 ? 31.393 0.652   68.409 1.00 43.02  ? 155 PRO A CB  1 
ATOM   1215 C  CG  . PRO A 1 155 ? 30.868 0.898   67.057 1.00 41.52  ? 155 PRO A CG  1 
ATOM   1216 C  CD  . PRO A 1 155 ? 29.522 1.561   67.123 1.00 39.02  ? 155 PRO A CD  1 
ATOM   1217 N  N   . TYR A 1 156 ? 31.220 3.576   69.901 1.00 37.95  ? 156 TYR A N   1 
ATOM   1218 C  CA  . TYR A 1 156 ? 31.824 4.589   70.755 1.00 36.39  ? 156 TYR A CA  1 
ATOM   1219 C  C   . TYR A 1 156 ? 31.109 4.684   72.107 1.00 38.44  ? 156 TYR A C   1 
ATOM   1220 O  O   . TYR A 1 156 ? 31.753 4.950   73.133 1.00 29.55  ? 156 TYR A O   1 
ATOM   1221 C  CB  . TYR A 1 156 ? 31.813 5.942   70.042 1.00 38.05  ? 156 TYR A CB  1 
ATOM   1222 C  CG  . TYR A 1 156 ? 32.265 7.122   70.892 1.00 38.10  ? 156 TYR A CG  1 
ATOM   1223 C  CD1 . TYR A 1 156 ? 31.349 7.858   71.643 1.00 36.68  ? 156 TYR A CD1 1 
ATOM   1224 C  CD2 . TYR A 1 156 ? 33.602 7.509   70.924 1.00 40.59  ? 156 TYR A CD2 1 
ATOM   1225 C  CE1 . TYR A 1 156 ? 31.751 8.927   72.412 1.00 36.52  ? 156 TYR A CE1 1 
ATOM   1226 C  CE2 . TYR A 1 156 ? 34.015 8.584   71.677 1.00 37.26  ? 156 TYR A CE2 1 
ATOM   1227 C  CZ  . TYR A 1 156 ? 33.089 9.286   72.428 1.00 35.25  ? 156 TYR A CZ  1 
ATOM   1228 O  OH  . TYR A 1 156 ? 33.497 10.351  73.177 1.00 34.86  ? 156 TYR A OH  1 
ATOM   1229 N  N   . PHE A 1 157 ? 29.787 4.467   72.127 1.00 35.29  ? 157 PHE A N   1 
ATOM   1230 C  CA  . PHE A 1 157 ? 29.028 4.589   73.366 1.00 35.37  ? 157 PHE A CA  1 
ATOM   1231 C  C   . PHE A 1 157 ? 29.045 3.320   74.211 1.00 37.03  ? 157 PHE A C   1 
ATOM   1232 O  O   . PHE A 1 157 ? 28.981 3.418   75.437 1.00 37.36  ? 157 PHE A O   1 
ATOM   1233 C  CB  . PHE A 1 157 ? 27.591 5.000   73.052 1.00 37.01  ? 157 PHE A CB  1 
ATOM   1234 C  CG  . PHE A 1 157 ? 27.467 6.453   72.716 1.00 38.94  ? 157 PHE A CG  1 
ATOM   1235 C  CD1 . PHE A 1 157 ? 27.750 6.910   71.427 1.00 36.47  ? 157 PHE A CD1 1 
ATOM   1236 C  CD2 . PHE A 1 157 ? 27.121 7.373   73.697 1.00 35.20  ? 157 PHE A CD2 1 
ATOM   1237 C  CE1 . PHE A 1 157 ? 27.658 8.264   71.118 1.00 35.82  ? 157 PHE A CE1 1 
ATOM   1238 C  CE2 . PHE A 1 157 ? 27.019 8.723   73.402 1.00 38.26  ? 157 PHE A CE2 1 
ATOM   1239 C  CZ  . PHE A 1 157 ? 27.295 9.177   72.107 1.00 38.60  ? 157 PHE A CZ  1 
ATOM   1240 N  N   . THR A 1 158 ? 29.119 2.137   73.591 1.00 33.77  ? 158 THR A N   1 
ATOM   1241 C  CA  . THR A 1 158 ? 29.129 0.883   74.331 1.00 36.37  ? 158 THR A CA  1 
ATOM   1242 C  C   . THR A 1 158 ? 30.532 0.393   74.652 1.00 38.07  ? 158 THR A C   1 
ATOM   1243 O  O   . THR A 1 158 ? 30.696 -0.431  75.559 1.00 37.99  ? 158 THR A O   1 
ATOM   1244 C  CB  . THR A 1 158 ? 28.375 -0.195  73.545 1.00 34.99  ? 158 THR A CB  1 
ATOM   1245 O  OG1 . THR A 1 158 ? 28.897 -0.288  72.221 1.00 38.37  ? 158 THR A OG1 1 
ATOM   1246 C  CG2 . THR A 1 158 ? 26.917 0.165   73.442 1.00 36.05  ? 158 THR A CG2 1 
ATOM   1247 N  N   . TRP A 1 159 ? 31.547 0.918   73.971 1.00 41.73  ? 159 TRP A N   1 
ATOM   1248 C  CA  . TRP A 1 159 ? 32.922 0.509   74.243 1.00 41.32  ? 159 TRP A CA  1 
ATOM   1249 C  C   . TRP A 1 159 ? 33.391 0.705   75.684 1.00 41.42  ? 159 TRP A C   1 
ATOM   1250 O  O   . TRP A 1 159 ? 34.263 -0.075  76.110 1.00 42.13  ? 159 TRP A O   1 
ATOM   1251 C  CB  . TRP A 1 159 ? 33.892 1.250   73.312 1.00 39.31  ? 159 TRP A CB  1 
ATOM   1252 C  CG  . TRP A 1 159 ? 35.263 0.691   73.390 1.00 37.90  ? 159 TRP A CG  1 
ATOM   1253 C  CD1 . TRP A 1 159 ? 36.350 1.251   73.994 1.00 44.12  ? 159 TRP A CD1 1 
ATOM   1254 C  CD2 . TRP A 1 159 ? 35.698 -0.560  72.866 1.00 40.46  ? 159 TRP A CD2 1 
ATOM   1255 N  NE1 . TRP A 1 159 ? 37.446 0.430   73.865 1.00 41.16  ? 159 TRP A NE1 1 
ATOM   1256 C  CE2 . TRP A 1 159 ? 37.068 -0.694  73.182 1.00 42.35  ? 159 TRP A CE2 1 
ATOM   1257 C  CE3 . TRP A 1 159 ? 35.066 -1.578  72.147 1.00 41.25  ? 159 TRP A CE3 1 
ATOM   1258 C  CZ2 . TRP A 1 159 ? 37.811 -1.807  72.807 1.00 41.09  ? 159 TRP A CZ2 1 
ATOM   1259 C  CZ3 . TRP A 1 159 ? 35.796 -2.676  71.784 1.00 43.42  ? 159 TRP A CZ3 1 
ATOM   1260 C  CH2 . TRP A 1 159 ? 37.164 -2.783  72.106 1.00 44.98  ? 159 TRP A CH2 1 
ATOM   1261 N  N   . PRO A 1 160 ? 32.938 1.719   76.450 1.00 42.54  ? 160 PRO A N   1 
ATOM   1262 C  CA  . PRO A 1 160 ? 33.419 1.823   77.844 1.00 42.92  ? 160 PRO A CA  1 
ATOM   1263 C  C   . PRO A 1 160 ? 33.241 0.535   78.629 1.00 40.81  ? 160 PRO A C   1 
ATOM   1264 O  O   . PRO A 1 160 ? 34.119 0.157   79.415 1.00 38.09  ? 160 PRO A O   1 
ATOM   1265 C  CB  . PRO A 1 160 ? 32.568 2.954   78.435 1.00 42.75  ? 160 PRO A CB  1 
ATOM   1266 C  CG  . PRO A 1 160 ? 32.091 3.736   77.280 1.00 39.66  ? 160 PRO A CG  1 
ATOM   1267 C  CD  . PRO A 1 160 ? 32.058 2.852   76.085 1.00 40.71  ? 160 PRO A CD  1 
ATOM   1268 N  N   . LEU A 1 161 ? 32.126 -0.159  78.414 1.00 39.42  ? 161 LEU A N   1 
ATOM   1269 C  CA  . LEU A 1 161 ? 31.836 -1.364  79.179 1.00 39.80  ? 161 LEU A CA  1 
ATOM   1270 C  C   . LEU A 1 161 ? 32.537 -2.588  78.590 1.00 38.56  ? 161 LEU A C   1 
ATOM   1271 O  O   . LEU A 1 161 ? 33.048 -3.434  79.338 1.00 35.71  ? 161 LEU A O   1 
ATOM   1272 C  CB  . LEU A 1 161 ? 30.320 -1.564  79.246 1.00 37.08  ? 161 LEU A CB  1 
ATOM   1273 C  CG  . LEU A 1 161 ? 29.733 -2.884  79.728 1.00 35.10  ? 161 LEU A CG  1 
ATOM   1274 C  CD1 . LEU A 1 161 ? 30.002 -3.088  81.222 1.00 35.94  ? 161 LEU A CD1 1 
ATOM   1275 C  CD2 . LEU A 1 161 ? 28.256 -2.844  79.441 1.00 32.99  ? 161 LEU A CD2 1 
ATOM   1276 N  N   . ILE A 1 162 ? 32.576 -2.690  77.254 1.00 39.89  ? 162 ILE A N   1 
ATOM   1277 C  CA  . ILE A 1 162 ? 33.255 -3.808  76.606 1.00 38.75  ? 162 ILE A CA  1 
ATOM   1278 C  C   . ILE A 1 162 ? 34.741 -3.802  76.949 1.00 40.95  ? 162 ILE A C   1 
ATOM   1279 O  O   . ILE A 1 162 ? 35.358 -4.860  77.118 1.00 47.71  ? 162 ILE A O   1 
ATOM   1280 C  CB  . ILE A 1 162 ? 33.021 -3.761  75.083 1.00 37.56  ? 162 ILE A CB  1 
ATOM   1281 C  CG1 . ILE A 1 162 ? 31.538 -3.990  74.770 1.00 40.78  ? 162 ILE A CG1 1 
ATOM   1282 C  CG2 . ILE A 1 162 ? 33.854 -4.822  74.397 1.00 39.17  ? 162 ILE A CG2 1 
ATOM   1283 C  CD1 . ILE A 1 162 ? 31.009 -3.283  73.532 1.00 38.48  ? 162 ILE A CD1 1 
ATOM   1284 N  N   . ALA A 1 163 ? 35.335 -2.614  77.072 1.00 40.97  ? 163 ALA A N   1 
ATOM   1285 C  CA  . ALA A 1 163 ? 36.761 -2.503  77.346 1.00 39.78  ? 163 ALA A CA  1 
ATOM   1286 C  C   . ALA A 1 163 ? 37.106 -2.657  78.823 1.00 38.86  ? 163 ALA A C   1 
ATOM   1287 O  O   . ALA A 1 163 ? 38.281 -2.850  79.149 1.00 42.96  ? 163 ALA A O   1 
ATOM   1288 C  CB  . ALA A 1 163 ? 37.294 -1.155  76.848 1.00 37.26  ? 163 ALA A CB  1 
ATOM   1289 N  N   . ALA A 1 164 ? 36.129 -2.566  79.724 1.00 43.19  ? 164 ALA A N   1 
ATOM   1290 C  CA  . ALA A 1 164 ? 36.463 -2.381  81.135 1.00 43.33  ? 164 ALA A CA  1 
ATOM   1291 C  C   . ALA A 1 164 ? 37.294 -3.537  81.672 1.00 46.34  ? 164 ALA A C   1 
ATOM   1292 O  O   . ALA A 1 164 ? 38.287 -3.320  82.376 1.00 44.03  ? 164 ALA A O   1 
ATOM   1293 C  CB  . ALA A 1 164 ? 35.191 -2.208  81.966 1.00 41.83  ? 164 ALA A CB  1 
ATOM   1294 N  N   . ASP A 1 165 ? 36.917 -4.769  81.341 1.00 51.50  ? 165 ASP A N   1 
ATOM   1295 C  CA  . ASP A 1 165 ? 37.570 -5.952  81.883 1.00 54.24  ? 165 ASP A CA  1 
ATOM   1296 C  C   . ASP A 1 165 ? 38.732 -6.441  81.028 1.00 54.18  ? 165 ASP A C   1 
ATOM   1297 O  O   . ASP A 1 165 ? 39.215 -7.555  81.251 1.00 57.04  ? 165 ASP A O   1 
ATOM   1298 C  CB  . ASP A 1 165 ? 36.549 -7.081  82.065 1.00 59.93  ? 165 ASP A CB  1 
ATOM   1299 C  CG  . ASP A 1 165 ? 37.051 -8.186  82.989 1.00 59.26  ? 165 ASP A CG  1 
ATOM   1300 O  OD1 . ASP A 1 165 ? 37.873 -7.897  83.885 1.00 56.42  ? 165 ASP A OD1 1 
ATOM   1301 O  OD2 . ASP A 1 165 ? 36.631 -9.346  82.811 1.00 64.47  ? 165 ASP A OD2 1 
ATOM   1302 N  N   . GLY A 1 166 ? 39.193 -5.649  80.060 1.00 49.44  ? 166 GLY A N   1 
ATOM   1303 C  CA  . GLY A 1 166 ? 40.369 -6.053  79.314 1.00 56.79  ? 166 GLY A CA  1 
ATOM   1304 C  C   . GLY A 1 166 ? 40.345 -5.847  77.810 1.00 55.25  ? 166 GLY A C   1 
ATOM   1305 O  O   . GLY A 1 166 ? 41.324 -6.165  77.128 1.00 51.26  ? 166 GLY A O   1 
ATOM   1306 N  N   . GLY A 1 167 ? 39.251 -5.319  77.272 1.00 50.29  ? 167 GLY A N   1 
ATOM   1307 C  CA  . GLY A 1 167 ? 39.218 -5.004  75.859 1.00 51.98  ? 167 GLY A CA  1 
ATOM   1308 C  C   . GLY A 1 167 ? 40.034 -3.767  75.522 1.00 54.83  ? 167 GLY A C   1 
ATOM   1309 O  O   . GLY A 1 167 ? 40.346 -2.932  76.381 1.00 54.81  ? 167 GLY A O   1 
ATOM   1310 N  N   . TYR A 1 168 ? 40.385 -3.656  74.240 1.00 49.35  ? 168 TYR A N   1 
ATOM   1311 C  CA  . TYR A 1 168 ? 41.115 -2.505  73.713 1.00 51.05  ? 168 TYR A CA  1 
ATOM   1312 C  C   . TYR A 1 168 ? 41.072 -2.588  72.193 1.00 49.48  ? 168 TYR A C   1 
ATOM   1313 O  O   . TYR A 1 168 ? 40.678 -3.606  71.627 1.00 40.19  ? 168 TYR A O   1 
ATOM   1314 C  CB  . TYR A 1 168 ? 42.545 -2.470  74.247 1.00 53.03  ? 168 TYR A CB  1 
ATOM   1315 C  CG  . TYR A 1 168 ? 43.376 -3.639  73.790 1.00 58.86  ? 168 TYR A CG  1 
ATOM   1316 C  CD1 . TYR A 1 168 ? 43.838 -3.736  72.479 1.00 63.87  ? 168 TYR A CD1 1 
ATOM   1317 C  CD2 . TYR A 1 168 ? 43.751 -4.625  74.692 1.00 61.87  ? 168 TYR A CD2 1 
ATOM   1318 C  CE1 . TYR A 1 168 ? 44.609 -4.795  72.078 1.00 68.68  ? 168 TYR A CE1 1 
ATOM   1319 C  CE2 . TYR A 1 168 ? 44.511 -5.701  74.292 1.00 66.65  ? 168 TYR A CE2 1 
ATOM   1320 C  CZ  . TYR A 1 168 ? 44.938 -5.783  72.987 1.00 68.53  ? 168 TYR A CZ  1 
ATOM   1321 O  OH  . TYR A 1 168 ? 45.701 -6.857  72.605 1.00 62.59  ? 168 TYR A OH  1 
ATOM   1322 N  N   . ALA A 1 169 ? 41.487 -1.512  71.533 1.00 47.28  ? 169 ALA A N   1 
ATOM   1323 C  CA  . ALA A 1 169 ? 41.367 -1.436  70.069 1.00 50.00  ? 169 ALA A CA  1 
ATOM   1324 C  C   . ALA A 1 169 ? 42.616 -2.006  69.401 1.00 57.17  ? 169 ALA A C   1 
ATOM   1325 O  O   . ALA A 1 169 ? 42.563 -3.041  68.729 1.00 57.09  ? 169 ALA A O   1 
ATOM   1326 C  CB  . ALA A 1 169 ? 41.112 0.007   69.629 1.00 45.08  ? 169 ALA A CB  1 
ATOM   1327 N  N   . PHE A 1 170 ? 43.736 -1.317  69.557 1.00 56.35  ? 170 PHE A N   1 
ATOM   1328 C  CA  . PHE A 1 170 ? 45.038 -1.791  69.127 1.00 56.95  ? 170 PHE A CA  1 
ATOM   1329 C  C   . PHE A 1 170 ? 45.985 -1.507  70.280 1.00 57.78  ? 170 PHE A C   1 
ATOM   1330 O  O   . PHE A 1 170 ? 45.869 -0.460  70.924 1.00 55.23  ? 170 PHE A O   1 
ATOM   1331 C  CB  . PHE A 1 170 ? 45.511 -1.067  67.847 1.00 57.45  ? 170 PHE A CB  1 
ATOM   1332 C  CG  . PHE A 1 170 ? 44.575 -1.209  66.660 1.00 56.40  ? 170 PHE A CG  1 
ATOM   1333 C  CD1 . PHE A 1 170 ? 44.403 -2.428  66.018 1.00 61.98  ? 170 PHE A CD1 1 
ATOM   1334 C  CD2 . PHE A 1 170 ? 43.859 -0.118  66.198 1.00 55.67  ? 170 PHE A CD2 1 
ATOM   1335 C  CE1 . PHE A 1 170 ? 43.552 -2.554  64.922 1.00 62.68  ? 170 PHE A CE1 1 
ATOM   1336 C  CE2 . PHE A 1 170 ? 42.994 -0.237  65.106 1.00 61.31  ? 170 PHE A CE2 1 
ATOM   1337 C  CZ  . PHE A 1 170 ? 42.846 -1.461  64.468 1.00 67.46  ? 170 PHE A CZ  1 
ATOM   1338 N  N   . LYS A 1 171 ? 46.909 -2.427  70.555 1.00 63.62  ? 171 LYS A N   1 
ATOM   1339 C  CA  . LYS A 1 171 ? 47.811 -2.232  71.685 1.00 63.59  ? 171 LYS A CA  1 
ATOM   1340 C  C   . LYS A 1 171 ? 48.796 -1.098  71.411 1.00 69.25  ? 171 LYS A C   1 
ATOM   1341 O  O   . LYS A 1 171 ? 49.454 -1.063  70.369 1.00 71.08  ? 171 LYS A O   1 
ATOM   1342 C  CB  . LYS A 1 171 ? 48.566 -3.519  72.017 1.00 65.46  ? 171 LYS A CB  1 
ATOM   1343 C  CG  . LYS A 1 171 ? 48.444 -3.902  73.499 1.00 75.57  ? 171 LYS A CG  1 
ATOM   1344 C  CD  . LYS A 1 171 ? 49.698 -4.562  74.054 1.00 79.24  ? 171 LYS A CD  1 
ATOM   1345 C  CE  . LYS A 1 171 ? 49.701 -4.547  75.586 1.00 79.65  ? 171 LYS A CE  1 
ATOM   1346 N  NZ  . LYS A 1 171 ? 50.945 -5.123  76.190 1.00 75.13  ? 171 LYS A NZ  1 
ATOM   1347 N  N   . TYR A 1 172 ? 48.869 -0.155  72.346 1.00 77.14  ? 172 TYR A N   1 
ATOM   1348 C  CA  . TYR A 1 172 ? 49.914 0.856   72.324 1.00 85.25  ? 172 TYR A CA  1 
ATOM   1349 C  C   . TYR A 1 172 ? 51.267 0.180   72.505 1.00 98.32  ? 172 TYR A C   1 
ATOM   1350 O  O   . TYR A 1 172 ? 51.505 -0.480  73.521 1.00 93.43  ? 172 TYR A O   1 
ATOM   1351 C  CB  . TYR A 1 172 ? 49.661 1.875   73.438 1.00 82.88  ? 172 TYR A CB  1 
ATOM   1352 C  CG  . TYR A 1 172 ? 50.205 3.271   73.192 1.00 82.23  ? 172 TYR A CG  1 
ATOM   1353 C  CD1 . TYR A 1 172 ? 50.664 3.657   71.935 1.00 74.16  ? 172 TYR A CD1 1 
ATOM   1354 C  CD2 . TYR A 1 172 ? 50.247 4.207   74.224 1.00 77.56  ? 172 TYR A CD2 1 
ATOM   1355 C  CE1 . TYR A 1 172 ? 51.157 4.933   71.714 1.00 76.41  ? 172 TYR A CE1 1 
ATOM   1356 C  CE2 . TYR A 1 172 ? 50.741 5.487   74.015 1.00 77.44  ? 172 TYR A CE2 1 
ATOM   1357 C  CZ  . TYR A 1 172 ? 51.194 5.850   72.757 1.00 79.35  ? 172 TYR A CZ  1 
ATOM   1358 O  OH  . TYR A 1 172 ? 51.690 7.126   72.544 1.00 64.95  ? 172 TYR A OH  1 
ATOM   1359 N  N   . ALA A 1 174 ? 57.408 1.956   72.815 1.00 30.00  ? 174 ALA A N   1 
ATOM   1360 C  CA  . ALA A 1 174 ? 56.345 2.797   73.414 1.00 30.00  ? 174 ALA A CA  1 
ATOM   1361 C  C   . ALA A 1 174 ? 56.150 4.036   72.550 1.00 30.00  ? 174 ALA A C   1 
ATOM   1362 O  O   . ALA A 1 174 ? 57.149 4.718   72.285 1.00 30.00  ? 174 ALA A O   1 
ATOM   1363 C  CB  . ALA A 1 174 ? 56.722 3.197   74.814 1.00 30.00  ? 174 ALA A CB  1 
ATOM   1364 N  N   . GLY A 1 175 ? 54.912 4.328   72.156 1.00 93.30  ? 175 GLY A N   1 
ATOM   1365 C  CA  . GLY A 1 175 ? 54.655 5.556   71.382 1.00 88.19  ? 175 GLY A CA  1 
ATOM   1366 C  C   . GLY A 1 175 ? 54.199 5.220   69.982 1.00 86.77  ? 175 GLY A C   1 
ATOM   1367 O  O   . GLY A 1 175 ? 54.123 6.135   69.141 1.00 75.09  ? 175 GLY A O   1 
ATOM   1368 N  N   . LYS A 1 176 ? 53.934 3.941   69.738 1.00 84.77  ? 176 LYS A N   1 
ATOM   1369 C  CA  . LYS A 1 176 ? 53.393 3.540   68.420 1.00 85.52  ? 176 LYS A CA  1 
ATOM   1370 C  C   . LYS A 1 176 ? 52.325 2.464   68.646 1.00 93.15  ? 176 LYS A C   1 
ATOM   1371 O  O   . LYS A 1 176 ? 52.323 1.839   69.723 1.00 90.32  ? 176 LYS A O   1 
ATOM   1372 C  CB  . LYS A 1 176 ? 54.530 3.068   67.512 1.00 72.95  ? 176 LYS A CB  1 
ATOM   1373 N  N   . TYR A 1 177 ? 51.455 2.262   67.661 1.00 88.04  ? 177 TYR A N   1 
ATOM   1374 C  CA  . TYR A 1 177 ? 50.380 1.253   67.799 1.00 79.03  ? 177 TYR A CA  1 
ATOM   1375 C  C   . TYR A 1 177 ? 50.786 -0.048  67.111 1.00 75.21  ? 177 TYR A C   1 
ATOM   1376 O  O   . TYR A 1 177 ? 51.501 0.014   66.105 1.00 75.89  ? 177 TYR A O   1 
ATOM   1377 C  CB  . TYR A 1 177 ? 49.058 1.796   67.249 1.00 68.41  ? 177 TYR A CB  1 
ATOM   1378 C  CG  . TYR A 1 177 ? 48.309 2.686   68.206 1.00 67.94  ? 177 TYR A CG  1 
ATOM   1379 C  CD1 . TYR A 1 177 ? 47.814 2.194   69.402 1.00 64.21  ? 177 TYR A CD1 1 
ATOM   1380 C  CD2 . TYR A 1 177 ? 48.102 4.025   67.924 1.00 61.29  ? 177 TYR A CD2 1 
ATOM   1381 C  CE1 . TYR A 1 177 ? 47.132 3.005   70.290 1.00 59.00  ? 177 TYR A CE1 1 
ATOM   1382 C  CE2 . TYR A 1 177 ? 47.420 4.850   68.801 1.00 59.93  ? 177 TYR A CE2 1 
ATOM   1383 C  CZ  . TYR A 1 177 ? 46.935 4.339   69.989 1.00 55.87  ? 177 TYR A CZ  1 
ATOM   1384 O  OH  . TYR A 1 177 ? 46.263 5.146   70.857 1.00 52.58  ? 177 TYR A OH  1 
ATOM   1385 N  N   . ASP A 1 178 ? 50.313 -1.179  67.621 1.00 75.02  ? 178 ASP A N   1 
ATOM   1386 C  CA  . ASP A 1 178 ? 50.582 -2.510  67.073 1.00 73.21  ? 178 ASP A CA  1 
ATOM   1387 C  C   . ASP A 1 178 ? 49.316 -2.987  66.367 1.00 76.37  ? 178 ASP A C   1 
ATOM   1388 O  O   . ASP A 1 178 ? 48.409 -3.531  67.003 1.00 81.23  ? 178 ASP A O   1 
ATOM   1389 C  CB  . ASP A 1 178 ? 51.006 -3.459  68.193 1.00 76.20  ? 178 ASP A CB  1 
ATOM   1390 C  CG  . ASP A 1 178 ? 51.095 -4.924  67.752 1.00 77.57  ? 178 ASP A CG  1 
ATOM   1391 O  OD1 . ASP A 1 178 ? 50.759 -5.262  66.593 1.00 71.97  ? 178 ASP A OD1 1 
ATOM   1392 O  OD2 . ASP A 1 178 ? 51.507 -5.748  68.601 1.00 69.35  ? 178 ASP A OD2 1 
ATOM   1393 N  N   . ILE A 1 179 ? 49.262 -2.800  65.044 1.00 75.87  ? 179 ILE A N   1 
ATOM   1394 C  CA  . ILE A 1 179 ? 48.087 -3.193  64.270 1.00 79.38  ? 179 ILE A CA  1 
ATOM   1395 C  C   . ILE A 1 179 ? 47.891 -4.703  64.219 1.00 83.64  ? 179 ILE A C   1 
ATOM   1396 O  O   . ILE A 1 179 ? 46.853 -5.172  63.734 1.00 83.51  ? 179 ILE A O   1 
ATOM   1397 C  CB  . ILE A 1 179 ? 48.168 -2.613  62.840 1.00 90.74  ? 179 ILE A CB  1 
ATOM   1398 C  CG1 . ILE A 1 179 ? 46.785 -2.589  62.175 1.00 93.16  ? 179 ILE A CG1 1 
ATOM   1399 C  CG2 . ILE A 1 179 ? 49.174 -3.387  61.991 1.00 85.61  ? 179 ILE A CG2 1 
ATOM   1400 C  CD1 . ILE A 1 179 ? 46.747 -1.813  60.884 1.00 89.58  ? 179 ILE A CD1 1 
ATOM   1401 N  N   . LYS A 1 180 ? 48.857 -5.485  64.707 1.00 82.82  ? 180 LYS A N   1 
ATOM   1402 C  CA  . LYS A 1 180 ? 48.637 -6.920  64.834 1.00 87.20  ? 180 LYS A CA  1 
ATOM   1403 C  C   . LYS A 1 180 ? 47.782 -7.230  66.057 1.00 95.91  ? 180 LYS A C   1 
ATOM   1404 O  O   . LYS A 1 180 ? 46.800 -7.977  65.965 1.00 96.69  ? 180 LYS A O   1 
ATOM   1405 C  CB  . LYS A 1 180 ? 49.979 -7.656  64.910 1.00 80.35  ? 180 LYS A CB  1 
ATOM   1406 N  N   . ASP A 1 181 ? 48.132 -6.640  67.201 1.00 94.60  ? 181 ASP A N   1 
ATOM   1407 C  CA  . ASP A 1 181 ? 47.534 -6.967  68.496 1.00 84.65  ? 181 ASP A CA  1 
ATOM   1408 C  C   . ASP A 1 181 ? 46.187 -6.272  68.635 1.00 79.52  ? 181 ASP A C   1 
ATOM   1409 O  O   . ASP A 1 181 ? 46.111 -5.112  69.051 1.00 72.22  ? 181 ASP A O   1 
ATOM   1410 C  CB  . ASP A 1 181 ? 48.463 -6.560  69.632 1.00 79.07  ? 181 ASP A CB  1 
ATOM   1411 C  CG  . ASP A 1 181 ? 48.326 -7.458  70.838 1.00 80.42  ? 181 ASP A CG  1 
ATOM   1412 O  OD1 . ASP A 1 181 ? 47.515 -8.407  70.771 1.00 82.92  ? 181 ASP A OD1 1 
ATOM   1413 O  OD2 . ASP A 1 181 ? 49.034 -7.227  71.843 1.00 83.22  ? 181 ASP A OD2 1 
ATOM   1414 N  N   . VAL A 1 182 ? 45.116 -6.980  68.297 1.00 74.75  ? 182 VAL A N   1 
ATOM   1415 C  CA  . VAL A 1 182 ? 43.775 -6.333  68.311 1.00 77.47  ? 182 VAL A CA  1 
ATOM   1416 C  C   . VAL A 1 182 ? 42.915 -6.956  69.405 1.00 81.90  ? 182 VAL A C   1 
ATOM   1417 O  O   . VAL A 1 182 ? 42.634 -8.161  69.312 1.00 73.14  ? 182 VAL A O   1 
ATOM   1418 C  CB  . VAL A 1 182 ? 43.081 -6.460  66.944 1.00 79.68  ? 182 VAL A CB  1 
ATOM   1419 C  CG1 . VAL A 1 182 ? 41.618 -6.052  67.008 1.00 74.54  ? 182 VAL A CG1 1 
ATOM   1420 C  CG2 . VAL A 1 182 ? 43.813 -5.690  65.859 1.00 78.46  ? 182 VAL A CG2 1 
ATOM   1421 N  N   . GLY A 1 183 ? 42.525 -6.191  70.432 1.00 78.23  ? 183 GLY A N   1 
ATOM   1422 C  CA  . GLY A 1 183 ? 41.837 -6.788  71.596 1.00 70.66  ? 183 GLY A CA  1 
ATOM   1423 C  C   . GLY A 1 183 ? 40.329 -6.640  71.606 1.00 69.24  ? 183 GLY A C   1 
ATOM   1424 O  O   . GLY A 1 183 ? 39.825 -5.921  72.484 1.00 68.16  ? 183 GLY A O   1 
ATOM   1425 N  N   . VAL A 1 184 ? 39.633 -7.358  70.728 1.00 61.23  ? 184 VAL A N   1 
ATOM   1426 C  CA  . VAL A 1 184 ? 38.145 -7.325  70.708 1.00 59.41  ? 184 VAL A CA  1 
ATOM   1427 C  C   . VAL A 1 184 ? 37.599 -8.717  71.050 1.00 63.64  ? 184 VAL A C   1 
ATOM   1428 O  O   . VAL A 1 184 ? 36.383 -8.834  71.247 1.00 57.35  ? 184 VAL A O   1 
ATOM   1429 C  CB  . VAL A 1 184 ? 37.645 -6.823  69.341 1.00 57.47  ? 184 VAL A CB  1 
ATOM   1430 C  CG1 . VAL A 1 184 ? 37.525 -7.934  68.310 1.00 58.49  ? 184 VAL A CG1 1 
ATOM   1431 C  CG2 . VAL A 1 184 ? 36.349 -6.042  69.459 1.00 57.17  ? 184 VAL A CG2 1 
ATOM   1432 N  N   . ASP A 1 185 ? 38.468 -9.726  71.154 1.00 65.60  ? 185 ASP A N   1 
ATOM   1433 C  CA  . ASP A 1 185 ? 37.998 -11.121 71.382 1.00 63.63  ? 185 ASP A CA  1 
ATOM   1434 C  C   . ASP A 1 185 ? 38.558 -11.708 72.681 1.00 54.53  ? 185 ASP A C   1 
ATOM   1435 O  O   . ASP A 1 185 ? 38.258 -12.867 72.955 1.00 63.24  ? 185 ASP A O   1 
ATOM   1436 C  CB  . ASP A 1 185 ? 38.367 -12.019 70.203 1.00 67.53  ? 185 ASP A CB  1 
ATOM   1437 C  CG  . ASP A 1 185 ? 37.353 -13.115 69.941 1.00 74.34  ? 185 ASP A CG  1 
ATOM   1438 O  OD1 . ASP A 1 185 ? 36.456 -13.294 70.782 1.00 78.36  ? 185 ASP A OD1 1 
ATOM   1439 O  OD2 . ASP A 1 185 ? 37.473 -13.779 68.899 1.00 82.41  ? 185 ASP A OD2 1 
ATOM   1440 N  N   . ASN A 1 186 ? 39.340 -10.956 73.447 1.00 53.17  ? 186 ASN A N   1 
ATOM   1441 C  CA  . ASN A 1 186 ? 39.806 -11.487 74.720 1.00 54.52  ? 186 ASN A CA  1 
ATOM   1442 C  C   . ASN A 1 186 ? 38.633 -11.694 75.681 1.00 52.47  ? 186 ASN A C   1 
ATOM   1443 O  O   . ASN A 1 186 ? 37.479 -11.350 75.400 1.00 53.72  ? 186 ASN A O   1 
ATOM   1444 C  CB  . ASN A 1 186 ? 40.864 -10.571 75.345 1.00 56.57  ? 186 ASN A CB  1 
ATOM   1445 C  CG  . ASN A 1 186 ? 40.410 -9.121  75.469 1.00 55.83  ? 186 ASN A CG  1 
ATOM   1446 O  OD1 . ASN A 1 186 ? 39.239 -8.824  75.707 1.00 59.27  ? 186 ASN A OD1 1 
ATOM   1447 N  ND2 . ASN A 1 186 ? 41.354 -8.208  75.314 1.00 55.92  ? 186 ASN A ND2 1 
ATOM   1448 N  N   . ALA A 1 187 ? 38.943 -12.286 76.834 1.00 50.40  ? 187 ALA A N   1 
ATOM   1449 C  CA  . ALA A 1 187 ? 37.890 -12.607 77.789 1.00 56.10  ? 187 ALA A CA  1 
ATOM   1450 C  C   . ALA A 1 187 ? 37.208 -11.344 78.306 1.00 54.16  ? 187 ALA A C   1 
ATOM   1451 O  O   . ALA A 1 187 ? 35.991 -11.348 78.542 1.00 49.07  ? 187 ALA A O   1 
ATOM   1452 C  CB  . ALA A 1 187 ? 38.466 -13.435 78.941 1.00 49.75  ? 187 ALA A CB  1 
ATOM   1453 N  N   . GLY A 1 188 ? 37.967 -10.254 78.463 1.00 44.59  ? 188 GLY A N   1 
ATOM   1454 C  CA  . GLY A 1 188 ? 37.418 -8.996  78.933 1.00 46.68  ? 188 GLY A CA  1 
ATOM   1455 C  C   . GLY A 1 188 ? 36.310 -8.474  78.041 1.00 43.39  ? 188 GLY A C   1 
ATOM   1456 O  O   . GLY A 1 188 ? 35.196 -8.227  78.506 1.00 46.07  ? 188 GLY A O   1 
ATOM   1457 N  N   . ALA A 1 189 ? 36.603 -8.318  76.749 1.00 40.80  ? 189 ALA A N   1 
ATOM   1458 C  CA  . ALA A 1 189 ? 35.596 -7.834  75.807 1.00 41.03  ? 189 ALA A CA  1 
ATOM   1459 C  C   . ALA A 1 189 ? 34.355 -8.718  75.809 1.00 42.51  ? 189 ALA A C   1 
ATOM   1460 O  O   . ALA A 1 189 ? 33.225 -8.214  75.755 1.00 42.80  ? 189 ALA A O   1 
ATOM   1461 C  CB  . ALA A 1 189 ? 36.198 -7.755  74.405 1.00 43.70  ? 189 ALA A CB  1 
ATOM   1462 N  N   . LYS A 1 190 ? 34.544 -10.043 75.876 1.00 44.92  ? 190 LYS A N   1 
ATOM   1463 C  CA  . LYS A 1 190 ? 33.403 -10.953 75.860 1.00 44.93  ? 190 LYS A CA  1 
ATOM   1464 C  C   . LYS A 1 190 ? 32.560 -10.792 77.113 1.00 39.94  ? 190 LYS A C   1 
ATOM   1465 O  O   . LYS A 1 190 ? 31.328 -10.841 77.055 1.00 42.41  ? 190 LYS A O   1 
ATOM   1466 C  CB  . LYS A 1 190 ? 33.865 -12.413 75.738 1.00 52.36  ? 190 LYS A CB  1 
ATOM   1467 C  CG  . LYS A 1 190 ? 34.567 -12.791 74.454 1.00 53.82  ? 190 LYS A CG  1 
ATOM   1468 C  CD  . LYS A 1 190 ? 34.739 -14.297 74.356 1.00 65.95  ? 190 LYS A CD  1 
ATOM   1469 C  CE  . LYS A 1 190 ? 36.067 -14.674 73.717 1.00 77.58  ? 190 LYS A CE  1 
ATOM   1470 N  NZ  . LYS A 1 190 ? 37.141 -14.894 74.744 1.00 78.34  ? 190 LYS A NZ  1 
ATOM   1471 N  N   . ALA A 1 191 ? 33.206 -10.648 78.262 1.00 35.48  ? 191 ALA A N   1 
ATOM   1472 C  CA  . ALA A 1 191 ? 32.448 -10.510 79.495 1.00 38.08  ? 191 ALA A CA  1 
ATOM   1473 C  C   . ALA A 1 191 ? 31.706 -9.181  79.512 1.00 39.41  ? 191 ALA A C   1 
ATOM   1474 O  O   . ALA A 1 191 ? 30.534 -9.127  79.893 1.00 45.04  ? 191 ALA A O   1 
ATOM   1475 C  CB  . ALA A 1 191 ? 33.386 -10.647 80.694 1.00 36.96  ? 191 ALA A CB  1 
ATOM   1476 N  N   . GLY A 1 192 ? 32.361 -8.115  79.037 1.00 40.84  ? 192 GLY A N   1 
ATOM   1477 C  CA  . GLY A 1 192 ? 31.704 -6.820  78.954 1.00 37.70  ? 192 GLY A CA  1 
ATOM   1478 C  C   . GLY A 1 192 ? 30.496 -6.836  78.036 1.00 38.93  ? 192 GLY A C   1 
ATOM   1479 O  O   . GLY A 1 192 ? 29.428 -6.339  78.393 1.00 33.95  ? 192 GLY A O   1 
ATOM   1480 N  N   . LEU A 1 193 ? 30.648 -7.400  76.830 1.00 35.78  ? 193 LEU A N   1 
ATOM   1481 C  CA  . LEU A 1 193 ? 29.529 -7.386  75.897 1.00 34.09  ? 193 LEU A CA  1 
ATOM   1482 C  C   . LEU A 1 193 ? 28.430 -8.358  76.326 1.00 40.15  ? 193 LEU A C   1 
ATOM   1483 O  O   . LEU A 1 193 ? 27.237 -8.111  76.078 1.00 39.56  ? 193 LEU A O   1 
ATOM   1484 C  CB  . LEU A 1 193 ? 30.031 -7.712  74.489 1.00 33.44  ? 193 LEU A CB  1 
ATOM   1485 C  CG  . LEU A 1 193 ? 28.985 -7.740  73.373 1.00 37.73  ? 193 LEU A CG  1 
ATOM   1486 C  CD1 . LEU A 1 193 ? 28.254 -6.403  73.267 1.00 41.44  ? 193 LEU A CD1 1 
ATOM   1487 C  CD2 . LEU A 1 193 ? 29.630 -8.114  72.029 1.00 40.47  ? 193 LEU A CD2 1 
ATOM   1488 N  N   . THR A 1 194 ? 28.807 -9.462  76.976 1.00 40.13  ? 194 THR A N   1 
ATOM   1489 C  CA  . THR A 1 194 ? 27.809 -10.361 77.546 1.00 42.11  ? 194 THR A CA  1 
ATOM   1490 C  C   . THR A 1 194 ? 26.942 -9.643  78.576 1.00 42.05  ? 194 THR A C   1 
ATOM   1491 O  O   . THR A 1 194 ? 25.713 -9.821  78.600 1.00 41.23  ? 194 THR A O   1 
ATOM   1492 C  CB  . THR A 1 194 ? 28.496 -11.580 78.174 1.00 44.22  ? 194 THR A CB  1 
ATOM   1493 O  OG1 . THR A 1 194 ? 29.299 -12.239 77.185 1.00 48.06  ? 194 THR A OG1 1 
ATOM   1494 C  CG2 . THR A 1 194 ? 27.456 -12.572 78.729 1.00 40.93  ? 194 THR A CG2 1 
ATOM   1495 N  N   . PHE A 1 195 ? 27.552 -8.818  79.432 1.00 39.68  ? 195 PHE A N   1 
ATOM   1496 C  CA  . PHE A 1 195 ? 26.751 -8.106  80.429 1.00 40.75  ? 195 PHE A CA  1 
ATOM   1497 C  C   . PHE A 1 195 ? 25.787 -7.136  79.758 1.00 40.40  ? 195 PHE A C   1 
ATOM   1498 O  O   . PHE A 1 195 ? 24.585 -7.114  80.064 1.00 37.31  ? 195 PHE A O   1 
ATOM   1499 C  CB  . PHE A 1 195 ? 27.650 -7.371  81.419 1.00 42.86  ? 195 PHE A CB  1 
ATOM   1500 C  CG  . PHE A 1 195 ? 26.890 -6.756  82.562 1.00 42.83  ? 195 PHE A CG  1 
ATOM   1501 C  CD1 . PHE A 1 195 ? 26.658 -7.486  83.728 1.00 40.65  ? 195 PHE A CD1 1 
ATOM   1502 C  CD2 . PHE A 1 195 ? 26.386 -5.458  82.467 1.00 38.07  ? 195 PHE A CD2 1 
ATOM   1503 C  CE1 . PHE A 1 195 ? 25.952 -6.931  84.789 1.00 39.34  ? 195 PHE A CE1 1 
ATOM   1504 C  CE2 . PHE A 1 195 ? 25.668 -4.892  83.520 1.00 40.76  ? 195 PHE A CE2 1 
ATOM   1505 C  CZ  . PHE A 1 195 ? 25.447 -5.634  84.683 1.00 40.80  ? 195 PHE A CZ  1 
ATOM   1506 N  N   . LEU A 1 196 ? 26.304 -6.331  78.825 1.00 43.51  ? 196 LEU A N   1 
ATOM   1507 C  CA  . LEU A 1 196 ? 25.454 -5.493  77.987 1.00 43.67  ? 196 LEU A CA  1 
ATOM   1508 C  C   . LEU A 1 196 ? 24.309 -6.288  77.373 1.00 37.85  ? 196 LEU A C   1 
ATOM   1509 O  O   . LEU A 1 196 ? 23.173 -5.799  77.283 1.00 41.11  ? 196 LEU A O   1 
ATOM   1510 C  CB  . LEU A 1 196 ? 26.293 -4.858  76.882 1.00 44.57  ? 196 LEU A CB  1 
ATOM   1511 C  CG  . LEU A 1 196 ? 25.452 -4.099  75.874 1.00 44.88  ? 196 LEU A CG  1 
ATOM   1512 C  CD1 . LEU A 1 196 ? 24.832 -2.951  76.595 1.00 51.30  ? 196 LEU A CD1 1 
ATOM   1513 C  CD2 . LEU A 1 196 ? 26.282 -3.595  74.704 1.00 51.71  ? 196 LEU A CD2 1 
ATOM   1514 N  N   . VAL A 1 197 ? 24.589 -7.513  76.928 1.00 38.21  ? 197 VAL A N   1 
ATOM   1515 C  CA  . VAL A 1 197 ? 23.552 -8.280  76.246 1.00 38.58  ? 197 VAL A CA  1 
ATOM   1516 C  C   . VAL A 1 197 ? 22.580 -8.868  77.261 1.00 37.84  ? 197 VAL A C   1 
ATOM   1517 O  O   . VAL A 1 197 ? 21.365 -8.913  77.020 1.00 33.95  ? 197 VAL A O   1 
ATOM   1518 C  CB  . VAL A 1 197 ? 24.196 -9.351  75.342 1.00 45.89  ? 197 VAL A CB  1 
ATOM   1519 C  CG1 . VAL A 1 197 ? 23.216 -10.465 74.986 1.00 44.14  ? 197 VAL A CG1 1 
ATOM   1520 C  CG2 . VAL A 1 197 ? 24.748 -8.694  74.061 1.00 46.41  ? 197 VAL A CG2 1 
ATOM   1521 N  N   . ASP A 1 198 ? 23.064 -9.258  78.438 1.00 39.48  ? 198 ASP A N   1 
ATOM   1522 C  CA  . ASP A 1 198 ? 22.119 -9.711  79.449 1.00 41.16  ? 198 ASP A CA  1 
ATOM   1523 C  C   . ASP A 1 198 ? 21.245 -8.567  79.934 1.00 41.33  ? 198 ASP A C   1 
ATOM   1524 O  O   . ASP A 1 198 ? 20.075 -8.788  80.274 1.00 43.47  ? 198 ASP A O   1 
ATOM   1525 C  CB  . ASP A 1 198 ? 22.866 -10.389 80.585 1.00 47.29  ? 198 ASP A CB  1 
ATOM   1526 C  CG  . ASP A 1 198 ? 23.317 -11.786 80.197 1.00 45.94  ? 198 ASP A CG  1 
ATOM   1527 O  OD1 . ASP A 1 198 ? 22.553 -12.448 79.441 1.00 47.15  ? 198 ASP A OD1 1 
ATOM   1528 O  OD2 . ASP A 1 198 ? 24.420 -12.208 80.617 1.00 41.63  ? 198 ASP A OD2 1 
ATOM   1529 N  N   . LEU A 1 199 ? 21.755 -7.335  79.896 1.00 38.94  ? 199 LEU A N   1 
ATOM   1530 C  CA  . LEU A 1 199 ? 20.915 -6.187  80.233 1.00 34.20  ? 199 LEU A CA  1 
ATOM   1531 C  C   . LEU A 1 199 ? 19.698 -6.123  79.319 1.00 36.19  ? 199 LEU A C   1 
ATOM   1532 O  O   . LEU A 1 199 ? 18.561 -5.949  79.776 1.00 38.68  ? 199 LEU A O   1 
ATOM   1533 C  CB  . LEU A 1 199 ? 21.731 -4.894  80.142 1.00 35.39  ? 199 LEU A CB  1 
ATOM   1534 C  CG  . LEU A 1 199 ? 22.599 -4.594  81.373 1.00 37.71  ? 199 LEU A CG  1 
ATOM   1535 C  CD1 . LEU A 1 199 ? 23.491 -3.347  81.162 1.00 35.94  ? 199 LEU A CD1 1 
ATOM   1536 C  CD2 . LEU A 1 199 ? 21.710 -4.475  82.644 1.00 34.22  ? 199 LEU A CD2 1 
ATOM   1537 N  N   . ILE A 1 200 ? 19.926 -6.268  78.014 1.00 35.21  ? 200 ILE A N   1 
ATOM   1538 C  CA  . ILE A 1 200 ? 18.845 -6.242  77.031 1.00 34.32  ? 200 ILE A CA  1 
ATOM   1539 C  C   . ILE A 1 200 ? 17.961 -7.478  77.161 1.00 39.49  ? 200 ILE A C   1 
ATOM   1540 O  O   . ILE A 1 200 ? 16.729 -7.392  77.039 1.00 39.51  ? 200 ILE A O   1 
ATOM   1541 C  CB  . ILE A 1 200 ? 19.448 -6.149  75.618 1.00 38.57  ? 200 ILE A CB  1 
ATOM   1542 C  CG1 . ILE A 1 200 ? 20.309 -4.885  75.469 1.00 40.34  ? 200 ILE A CG1 1 
ATOM   1543 C  CG2 . ILE A 1 200 ? 18.363 -6.254  74.565 1.00 38.15  ? 200 ILE A CG2 1 
ATOM   1544 C  CD1 . ILE A 1 200 ? 21.252 -4.940  74.269 1.00 37.73  ? 200 ILE A CD1 1 
ATOM   1545 N  N   . LYS A 1 201 ? 18.581 -8.654  77.361 1.00 46.86  ? 201 LYS A N   1 
ATOM   1546 C  CA  . LYS A 1 201 ? 17.827 -9.903  77.469 1.00 46.20  ? 201 LYS A CA  1 
ATOM   1547 C  C   . LYS A 1 201 ? 16.885 -9.864  78.656 1.00 42.43  ? 201 LYS A C   1 
ATOM   1548 O  O   . LYS A 1 201 ? 15.725 -10.274 78.549 1.00 40.31  ? 201 LYS A O   1 
ATOM   1549 C  CB  . LYS A 1 201 ? 18.778 -11.092 77.609 1.00 49.37  ? 201 LYS A CB  1 
ATOM   1550 C  CG  . LYS A 1 201 ? 19.362 -11.607 76.312 1.00 56.18  ? 201 LYS A CG  1 
ATOM   1551 C  CD  . LYS A 1 201 ? 19.847 -13.037 76.455 1.00 59.90  ? 201 LYS A CD  1 
ATOM   1552 C  CE  . LYS A 1 201 ? 18.671 -14.007 76.371 1.00 67.77  ? 201 LYS A CE  1 
ATOM   1553 N  NZ  . LYS A 1 201 ? 19.085 -15.440 76.243 1.00 69.91  ? 201 LYS A NZ  1 
ATOM   1554 N  N   . ASN A 1 202 ? 17.376 -9.375  79.800 1.00 41.28  ? 202 ASN A N   1 
ATOM   1555 C  CA  . ASN A 1 202 ? 16.590 -9.177  81.010 1.00 39.12  ? 202 ASN A CA  1 
ATOM   1556 C  C   . ASN A 1 202 ? 15.722 -7.912  80.955 1.00 43.92  ? 202 ASN A C   1 
ATOM   1557 O  O   . ASN A 1 202 ? 15.148 -7.525  81.986 1.00 36.49  ? 202 ASN A O   1 
ATOM   1558 C  CB  . ASN A 1 202 ? 17.532 -9.155  82.223 1.00 33.83  ? 202 ASN A CB  1 
ATOM   1559 C  CG  . ASN A 1 202 ? 18.246 -10.479 82.403 1.00 33.00  ? 202 ASN A CG  1 
ATOM   1560 O  OD1 . ASN A 1 202 ? 17.693 -11.511 82.069 1.00 42.06  ? 202 ASN A OD1 1 
ATOM   1561 N  ND2 . ASN A 1 202 ? 19.469 -10.459 82.884 1.00 36.37  ? 202 ASN A ND2 1 
ATOM   1562 N  N   . LYS A 1 203 ? 15.621 -7.274  79.777 1.00 41.37  ? 203 LYS A N   1 
ATOM   1563 C  CA  . LYS A 1 203 ? 14.691 -6.163  79.515 1.00 44.14  ? 203 LYS A CA  1 
ATOM   1564 C  C   . LYS A 1 203 ? 14.991 -4.928  80.369 1.00 44.55  ? 203 LYS A C   1 
ATOM   1565 O  O   . LYS A 1 203 ? 14.104 -4.095  80.623 1.00 40.99  ? 203 LYS A O   1 
ATOM   1566 C  CB  . LYS A 1 203 ? 13.221 -6.577  79.690 1.00 52.28  ? 203 LYS A CB  1 
ATOM   1567 C  CG  . LYS A 1 203 ? 12.813 -7.884  79.028 1.00 58.79  ? 203 LYS A CG  1 
ATOM   1568 C  CD  . LYS A 1 203 ? 12.541 -7.733  77.548 1.00 69.36  ? 203 LYS A CD  1 
ATOM   1569 C  CE  . LYS A 1 203 ? 12.594 -9.089  76.849 1.00 73.12  ? 203 LYS A CE  1 
ATOM   1570 N  NZ  . LYS A 1 203 ? 13.724 -9.210  75.880 1.00 71.05  ? 203 LYS A NZ  1 
ATOM   1571 N  N   . HIS A 1 204 ? 16.242 -4.777  80.799 1.00 39.19  ? 204 HIS A N   1 
ATOM   1572 C  CA  . HIS A 1 204 ? 16.634 -3.520  81.416 1.00 39.01  ? 204 HIS A CA  1 
ATOM   1573 C  C   . HIS A 1 204 ? 17.031 -2.464  80.389 1.00 39.33  ? 204 HIS A C   1 
ATOM   1574 O  O   . HIS A 1 204 ? 16.954 -1.275  80.690 1.00 42.83  ? 204 HIS A O   1 
ATOM   1575 C  CB  . HIS A 1 204 ? 17.767 -3.757  82.400 1.00 37.09  ? 204 HIS A CB  1 
ATOM   1576 C  CG  . HIS A 1 204 ? 17.447 -4.783  83.437 1.00 41.26  ? 204 HIS A CG  1 
ATOM   1577 N  ND1 . HIS A 1 204 ? 16.373 -4.662  84.292 1.00 38.01  ? 204 HIS A ND1 1 
ATOM   1578 C  CD2 . HIS A 1 204 ? 18.056 -5.952  83.756 1.00 40.17  ? 204 HIS A CD2 1 
ATOM   1579 C  CE1 . HIS A 1 204 ? 16.334 -5.711  85.095 1.00 42.17  ? 204 HIS A CE1 1 
ATOM   1580 N  NE2 . HIS A 1 204 ? 17.345 -6.509  84.790 1.00 41.26  ? 204 HIS A NE2 1 
ATOM   1581 N  N   . MET A 1 205 ? 17.441 -2.864  79.190 1.00 43.80  ? 205 MET A N   1 
ATOM   1582 C  CA  . MET A 1 205 ? 17.642 -1.925  78.094 1.00 42.32  ? 205 MET A CA  1 
ATOM   1583 C  C   . MET A 1 205 ? 17.050 -2.529  76.839 1.00 41.83  ? 205 MET A C   1 
ATOM   1584 O  O   . MET A 1 205 ? 16.788 -3.731  76.782 1.00 42.83  ? 205 MET A O   1 
ATOM   1585 C  CB  . MET A 1 205 ? 19.119 -1.578  77.869 1.00 43.00  ? 205 MET A CB  1 
ATOM   1586 C  CG  . MET A 1 205 ? 19.830 -1.014  79.075 1.00 42.84  ? 205 MET A CG  1 
ATOM   1587 S  SD  . MET A 1 205 ? 21.521 -0.522  78.680 1.00 39.36  ? 205 MET A SD  1 
ATOM   1588 C  CE  . MET A 1 205 ? 21.964 -1.726  77.457 1.00 39.11  ? 205 MET A CE  1 
ATOM   1589 N  N   . ASN A 1 206 ? 16.837 -1.691  75.831 1.00 45.60  ? 206 ASN A N   1 
ATOM   1590 C  CA  . ASN A 1 206 ? 16.281 -2.152  74.566 1.00 49.38  ? 206 ASN A CA  1 
ATOM   1591 C  C   . ASN A 1 206 ? 17.290 -1.937  73.451 1.00 46.48  ? 206 ASN A C   1 
ATOM   1592 O  O   . ASN A 1 206 ? 17.835 -0.837  73.303 1.00 48.40  ? 206 ASN A O   1 
ATOM   1593 C  CB  . ASN A 1 206 ? 14.981 -1.439  74.195 1.00 58.47  ? 206 ASN A CB  1 
ATOM   1594 C  CG  . ASN A 1 206 ? 14.123 -2.266  73.248 1.00 67.12  ? 206 ASN A CG  1 
ATOM   1595 O  OD1 . ASN A 1 206 ? 14.531 -2.592  72.126 1.00 72.87  ? 206 ASN A OD1 1 
ATOM   1596 N  ND2 . ASN A 1 206 ? 12.907 -2.564  73.676 1.00 77.23  ? 206 ASN A ND2 1 
ATOM   1597 N  N   . ALA A 1 207 ? 17.493 -2.982  72.644 1.00 46.17  ? 207 ALA A N   1 
ATOM   1598 C  CA  . ALA A 1 207 ? 18.514 -2.979  71.608 1.00 49.80  ? 207 ALA A CA  1 
ATOM   1599 C  C   . ALA A 1 207 ? 18.359 -1.840  70.606 1.00 50.05  ? 207 ALA A C   1 
ATOM   1600 O  O   . ALA A 1 207 ? 19.350 -1.454  69.974 1.00 59.73  ? 207 ALA A O   1 
ATOM   1601 C  CB  . ALA A 1 207 ? 18.502 -4.320  70.878 1.00 46.89  ? 207 ALA A CB  1 
ATOM   1602 N  N   . ASP A 1 208 ? 17.164 -1.274  70.453 1.00 45.94  ? 208 ASP A N   1 
ATOM   1603 C  CA  . ASP A 1 208 ? 16.952 -0.288  69.400 1.00 46.77  ? 208 ASP A CA  1 
ATOM   1604 C  C   . ASP A 1 208 ? 17.193 1.138   69.873 1.00 45.02  ? 208 ASP A C   1 
ATOM   1605 O  O   . ASP A 1 208 ? 17.212 2.057   69.044 1.00 47.82  ? 208 ASP A O   1 
ATOM   1606 C  CB  . ASP A 1 208 ? 15.524 -0.412  68.825 1.00 47.62  ? 208 ASP A CB  1 
ATOM   1607 C  CG  . ASP A 1 208 ? 14.465 0.013   69.804 1.00 57.09  ? 208 ASP A CG  1 
ATOM   1608 O  OD1 . ASP A 1 208 ? 14.721 -0.091  71.019 1.00 68.59  ? 208 ASP A OD1 1 
ATOM   1609 O  OD2 . ASP A 1 208 ? 13.399 0.508   69.380 1.00 67.95  ? 208 ASP A OD2 1 
ATOM   1610 N  N   . THR A 1 209 ? 17.380 1.338   71.177 1.00 39.09  ? 209 THR A N   1 
ATOM   1611 C  CA  . THR A 1 209 ? 17.667 2.658   71.721 1.00 41.21  ? 209 THR A CA  1 
ATOM   1612 C  C   . THR A 1 209 ? 18.887 3.280   71.038 1.00 40.99  ? 209 THR A C   1 
ATOM   1613 O  O   . THR A 1 209 ? 19.948 2.656   70.943 1.00 43.79  ? 209 THR A O   1 
ATOM   1614 C  CB  . THR A 1 209 ? 17.902 2.558   73.238 1.00 42.15  ? 209 THR A CB  1 
ATOM   1615 O  OG1 . THR A 1 209 ? 16.721 2.063   73.884 1.00 36.82  ? 209 THR A OG1 1 
ATOM   1616 C  CG2 . THR A 1 209 ? 18.257 3.928   73.816 1.00 38.49  ? 209 THR A CG2 1 
ATOM   1617 N  N   . ASP A 1 210 ? 18.728 4.515   70.556 1.00 41.02  ? 210 ASP A N   1 
ATOM   1618 C  CA  . ASP A 1 210 ? 19.834 5.250   69.947 1.00 42.23  ? 210 ASP A CA  1 
ATOM   1619 C  C   . ASP A 1 210 ? 20.089 6.552   70.703 1.00 44.09  ? 210 ASP A C   1 
ATOM   1620 O  O   . ASP A 1 210 ? 19.643 6.703   71.848 1.00 40.76  ? 210 ASP A O   1 
ATOM   1621 C  CB  . ASP A 1 210 ? 19.552 5.528   68.473 1.00 38.24  ? 210 ASP A CB  1 
ATOM   1622 C  CG  . ASP A 1 210 ? 18.240 6.242   68.261 1.00 39.67  ? 210 ASP A CG  1 
ATOM   1623 O  OD1 . ASP A 1 210 ? 17.608 6.640   69.250 1.00 42.74  ? 210 ASP A OD1 1 
ATOM   1624 O  OD2 . ASP A 1 210 ? 17.823 6.419   67.105 1.00 42.48  ? 210 ASP A OD2 1 
ATOM   1625 N  N   . TYR A 1 211 ? 20.783 7.504   70.068 1.00 38.49  ? 211 TYR A N   1 
ATOM   1626 C  CA  . TYR A 1 211 ? 21.076 8.767   70.733 1.00 37.94  ? 211 TYR A CA  1 
ATOM   1627 C  C   . TYR A 1 211 ? 19.799 9.529   71.044 1.00 37.68  ? 211 TYR A C   1 
ATOM   1628 O  O   . TYR A 1 211 ? 19.546 9.902   72.198 1.00 41.84  ? 211 TYR A O   1 
ATOM   1629 C  CB  . TYR A 1 211 ? 22.003 9.623   69.868 1.00 36.72  ? 211 TYR A CB  1 
ATOM   1630 C  CG  . TYR A 1 211 ? 22.571 10.816  70.609 1.00 32.33  ? 211 TYR A CG  1 
ATOM   1631 C  CD1 . TYR A 1 211 ? 21.860 12.017  70.693 1.00 29.35  ? 211 TYR A CD1 1 
ATOM   1632 C  CD2 . TYR A 1 211 ? 23.804 10.731  71.245 1.00 30.62  ? 211 TYR A CD2 1 
ATOM   1633 C  CE1 . TYR A 1 211 ? 22.373 13.107  71.377 1.00 32.89  ? 211 TYR A CE1 1 
ATOM   1634 C  CE2 . TYR A 1 211 ? 24.324 11.804  71.955 1.00 30.90  ? 211 TYR A CE2 1 
ATOM   1635 C  CZ  . TYR A 1 211 ? 23.612 12.992  72.014 1.00 34.47  ? 211 TYR A CZ  1 
ATOM   1636 O  OH  . TYR A 1 211 ? 24.147 14.063  72.697 1.00 35.09  ? 211 TYR A OH  1 
ATOM   1637 N  N   . SER A 1 212 ? 18.982 9.777   70.013 1.00 36.82  ? 212 SER A N   1 
ATOM   1638 C  CA  . SER A 1 212 ? 17.751 10.553  70.187 1.00 40.59  ? 212 SER A CA  1 
ATOM   1639 C  C   . SER A 1 212 ? 16.841 9.938   71.246 1.00 40.29  ? 212 SER A C   1 
ATOM   1640 O  O   . SER A 1 212 ? 16.291 10.654  72.094 1.00 46.02  ? 212 SER A O   1 
ATOM   1641 C  CB  . SER A 1 212 ? 16.992 10.671  68.854 1.00 38.99  ? 212 SER A CB  1 
ATOM   1642 O  OG  . SER A 1 212 ? 17.421 11.798  68.095 1.00 50.65  ? 212 SER A OG  1 
ATOM   1643 N  N   . ILE A 1 213 ? 16.637 8.619   71.189 1.00 40.94  ? 213 ILE A N   1 
ATOM   1644 C  CA  . ILE A 1 213 ? 15.731 7.954   72.131 1.00 39.94  ? 213 ILE A CA  1 
ATOM   1645 C  C   . ILE A 1 213 ? 16.236 8.113   73.564 1.00 39.52  ? 213 ILE A C   1 
ATOM   1646 O  O   . ILE A 1 213 ? 15.462 8.402   74.484 1.00 37.27  ? 213 ILE A O   1 
ATOM   1647 C  CB  . ILE A 1 213 ? 15.565 6.464   71.759 1.00 38.92  ? 213 ILE A CB  1 
ATOM   1648 C  CG1 . ILE A 1 213 ? 14.785 6.294   70.452 1.00 42.01  ? 213 ILE A CG1 1 
ATOM   1649 C  CG2 . ILE A 1 213 ? 14.910 5.669   72.898 1.00 36.69  ? 213 ILE A CG2 1 
ATOM   1650 C  CD1 . ILE A 1 213 ? 14.752 4.850   69.963 1.00 43.30  ? 213 ILE A CD1 1 
ATOM   1651 N  N   . ALA A 1 214 ? 17.543 7.928   73.773 1.00 37.60  ? 214 ALA A N   1 
ATOM   1652 C  CA  . ALA A 1 214 ? 18.084 8.003   75.130 1.00 38.00  ? 214 ALA A CA  1 
ATOM   1653 C  C   . ALA A 1 214 ? 18.115 9.447   75.642 1.00 38.09  ? 214 ALA A C   1 
ATOM   1654 O  O   . ALA A 1 214 ? 17.842 9.694   76.824 1.00 39.26  ? 214 ALA A O   1 
ATOM   1655 C  CB  . ALA A 1 214 ? 19.477 7.371   75.175 1.00 35.30  ? 214 ALA A CB  1 
ATOM   1656 N  N   . GLU A 1 215 ? 18.438 10.414  74.772 1.00 36.22  ? 215 GLU A N   1 
ATOM   1657 C  CA  . GLU A 1 215 ? 18.452 11.814  75.198 1.00 39.72  ? 215 GLU A CA  1 
ATOM   1658 C  C   . GLU A 1 215 ? 17.055 12.286  75.603 1.00 42.05  ? 215 GLU A C   1 
ATOM   1659 O  O   . GLU A 1 215 ? 16.878 12.933  76.648 1.00 41.83  ? 215 GLU A O   1 
ATOM   1660 C  CB  . GLU A 1 215 ? 19.012 12.702  74.090 1.00 38.08  ? 215 GLU A CB  1 
ATOM   1661 C  CG  . GLU A 1 215 ? 19.216 14.177  74.490 1.00 39.11  ? 215 GLU A CG  1 
ATOM   1662 C  CD  . GLU A 1 215 ? 19.850 14.978  73.356 1.00 39.15  ? 215 GLU A CD  1 
ATOM   1663 O  OE1 . GLU A 1 215 ? 19.495 14.666  72.202 1.00 38.47  ? 215 GLU A OE1 1 
ATOM   1664 O  OE2 . GLU A 1 215 ? 20.701 15.880  73.599 1.00 36.69  ? 215 GLU A OE2 1 
ATOM   1665 N  N   . ALA A 1 216 ? 16.049 11.969  74.783 1.00 36.56  ? 216 ALA A N   1 
ATOM   1666 C  CA  . ALA A 1 216 ? 14.672 12.351  75.092 1.00 38.00  ? 216 ALA A CA  1 
ATOM   1667 C  C   . ALA A 1 216 ? 14.218 11.770  76.424 1.00 38.40  ? 216 ALA A C   1 
ATOM   1668 O  O   . ALA A 1 216 ? 13.622 12.474  77.251 1.00 42.36  ? 216 ALA A O   1 
ATOM   1669 C  CB  . ALA A 1 216 ? 13.742 11.888  73.971 1.00 38.35  ? 216 ALA A CB  1 
ATOM   1670 N  N   . ALA A 1 217 ? 14.521 10.495  76.659 1.00 38.97  ? 217 ALA A N   1 
ATOM   1671 C  CA  . ALA A 1 217 ? 14.100 9.829   77.887 1.00 41.00  ? 217 ALA A CA  1 
ATOM   1672 C  C   . ALA A 1 217 ? 14.711 10.486  79.122 1.00 38.48  ? 217 ALA A C   1 
ATOM   1673 O  O   . ALA A 1 217 ? 13.996 10.810  80.078 1.00 44.16  ? 217 ALA A O   1 
ATOM   1674 C  CB  . ALA A 1 217 ? 14.473 8.349   77.825 1.00 42.21  ? 217 ALA A CB  1 
ATOM   1675 N  N   . PHE A 1 218 ? 16.039 10.674  79.134 1.00 34.04  ? 218 PHE A N   1 
ATOM   1676 C  CA  . PHE A 1 218 ? 16.665 11.261  80.323 1.00 32.86  ? 218 PHE A CA  1 
ATOM   1677 C  C   . PHE A 1 218 ? 16.210 12.698  80.522 1.00 35.04  ? 218 PHE A C   1 
ATOM   1678 O  O   . PHE A 1 218 ? 15.896 13.109  81.644 1.00 36.61  ? 218 PHE A O   1 
ATOM   1679 C  CB  . PHE A 1 218 ? 18.197 11.199  80.244 1.00 33.81  ? 218 PHE A CB  1 
ATOM   1680 C  CG  . PHE A 1 218 ? 18.868 11.583  81.539 1.00 35.47  ? 218 PHE A CG  1 
ATOM   1681 C  CD1 . PHE A 1 218 ? 18.992 10.664  82.570 1.00 32.14  ? 218 PHE A CD1 1 
ATOM   1682 C  CD2 . PHE A 1 218 ? 19.320 12.877  81.742 1.00 39.33  ? 218 PHE A CD2 1 
ATOM   1683 C  CE1 . PHE A 1 218 ? 19.580 11.012  83.766 1.00 38.34  ? 218 PHE A CE1 1 
ATOM   1684 C  CE2 . PHE A 1 218 ? 19.920 13.238  82.936 1.00 41.52  ? 218 PHE A CE2 1 
ATOM   1685 C  CZ  . PHE A 1 218 ? 20.047 12.305  83.963 1.00 41.65  ? 218 PHE A CZ  1 
ATOM   1686 N  N   . ASN A 1 219 ? 16.126 13.471  79.435 1.00 35.58  ? 219 ASN A N   1 
ATOM   1687 C  CA  . ASN A 1 219 ? 15.741 14.867  79.550 1.00 35.52  ? 219 ASN A CA  1 
ATOM   1688 C  C   . ASN A 1 219 ? 14.253 15.065  79.842 1.00 42.69  ? 219 ASN A C   1 
ATOM   1689 O  O   . ASN A 1 219 ? 13.853 16.185  80.174 1.00 45.07  ? 219 ASN A O   1 
ATOM   1690 C  CB  . ASN A 1 219 ? 16.194 15.593  78.287 1.00 36.21  ? 219 ASN A CB  1 
ATOM   1691 C  CG  . ASN A 1 219 ? 17.719 15.623  78.171 1.00 36.65  ? 219 ASN A CG  1 
ATOM   1692 O  OD1 . ASN A 1 219 ? 18.417 15.047  79.015 1.00 36.29  ? 219 ASN A OD1 1 
ATOM   1693 N  ND2 . ASN A 1 219 ? 18.241 16.277  77.133 1.00 37.17  ? 219 ASN A ND2 1 
ATOM   1694 N  N   . LYS A 1 220 ? 13.431 14.017  79.775 1.00 46.85  ? 220 LYS A N   1 
ATOM   1695 C  CA  . LYS A 1 220 ? 12.062 14.067  80.281 1.00 45.36  ? 220 LYS A CA  1 
ATOM   1696 C  C   . LYS A 1 220 ? 11.909 13.427  81.661 1.00 42.38  ? 220 LYS A C   1 
ATOM   1697 O  O   . LYS A 1 220 ? 10.795 13.365  82.182 1.00 37.48  ? 220 LYS A O   1 
ATOM   1698 C  CB  . LYS A 1 220 ? 11.104 13.394  79.297 1.00 46.52  ? 220 LYS A CB  1 
ATOM   1699 C  CG  . LYS A 1 220 ? 11.083 14.053  77.937 1.00 51.55  ? 220 LYS A CG  1 
ATOM   1700 C  CD  . LYS A 1 220 ? 9.876  13.628  77.107 1.00 60.04  ? 220 LYS A CD  1 
ATOM   1701 C  CE  . LYS A 1 220 ? 10.254 12.633  76.010 1.00 65.38  ? 220 LYS A CE  1 
ATOM   1702 N  NZ  . LYS A 1 220 ? 9.068  11.896  75.480 1.00 62.38  ? 220 LYS A NZ  1 
ATOM   1703 N  N   . GLY A 1 221 ? 12.988 12.952  82.269 1.00 43.26  ? 221 GLY A N   1 
ATOM   1704 C  CA  . GLY A 1 221 ? 12.857 12.352  83.580 1.00 44.83  ? 221 GLY A CA  1 
ATOM   1705 C  C   . GLY A 1 221 ? 12.282 10.952  83.594 1.00 46.13  ? 221 GLY A C   1 
ATOM   1706 O  O   . GLY A 1 221 ? 11.712 10.537  84.603 1.00 40.76  ? 221 GLY A O   1 
ATOM   1707 N  N   . GLU A 1 222 ? 12.430 10.195  82.508 1.00 45.42  ? 222 GLU A N   1 
ATOM   1708 C  CA  . GLU A 1 222 ? 11.858 8.859   82.454 1.00 43.43  ? 222 GLU A CA  1 
ATOM   1709 C  C   . GLU A 1 222 ? 12.837 7.757   82.859 1.00 37.99  ? 222 GLU A C   1 
ATOM   1710 O  O   . GLU A 1 222 ? 12.393 6.664   83.248 1.00 36.84  ? 222 GLU A O   1 
ATOM   1711 C  CB  . GLU A 1 222 ? 11.317 8.597   81.053 1.00 42.70  ? 222 GLU A CB  1 
ATOM   1712 C  CG  . GLU A 1 222 ? 10.083 9.417   80.738 1.00 44.46  ? 222 GLU A CG  1 
ATOM   1713 C  CD  . GLU A 1 222 ? 9.791  9.461   79.249 1.00 49.85  ? 222 GLU A CD  1 
ATOM   1714 O  OE1 . GLU A 1 222 ? 10.610 8.960   78.457 1.00 48.53  ? 222 GLU A OE1 1 
ATOM   1715 O  OE2 . GLU A 1 222 ? 8.731  9.988   78.861 1.00 60.48  ? 222 GLU A OE2 1 
ATOM   1716 N  N   . THR A 1 223 ? 14.144 8.009   82.778 1.00 38.84  ? 223 THR A N   1 
ATOM   1717 C  CA  . THR A 1 223 ? 15.168 7.057   83.192 1.00 38.83  ? 223 THR A CA  1 
ATOM   1718 C  C   . THR A 1 223 ? 16.157 7.769   84.101 1.00 34.66  ? 223 THR A C   1 
ATOM   1719 O  O   . THR A 1 223 ? 16.373 8.975   83.978 1.00 39.06  ? 223 THR A O   1 
ATOM   1720 C  CB  . THR A 1 223 ? 15.951 6.434   81.992 1.00 44.52  ? 223 THR A CB  1 
ATOM   1721 O  OG1 . THR A 1 223 ? 16.871 5.441   82.478 1.00 43.88  ? 223 THR A OG1 1 
ATOM   1722 C  CG2 . THR A 1 223 ? 16.743 7.526   81.216 1.00 41.13  ? 223 THR A CG2 1 
ATOM   1723 N  N   . ALA A 1 224 ? 16.775 7.017   84.995 1.00 31.25  ? 224 ALA A N   1 
ATOM   1724 C  CA  . ALA A 1 224 ? 17.568 7.650   86.032 1.00 33.25  ? 224 ALA A CA  1 
ATOM   1725 C  C   . ALA A 1 224 ? 18.992 7.945   85.591 1.00 34.97  ? 224 ALA A C   1 
ATOM   1726 O  O   . ALA A 1 224 ? 19.658 8.768   86.213 1.00 37.93  ? 224 ALA A O   1 
ATOM   1727 C  CB  . ALA A 1 224 ? 17.572 6.778   87.283 1.00 33.95  ? 224 ALA A CB  1 
ATOM   1728 N  N   . MET A 1 225 ? 19.467 7.324   84.517 1.00 39.02  ? 225 MET A N   1 
ATOM   1729 C  CA  . MET A 1 225 ? 20.828 7.535   84.071 1.00 34.32  ? 225 MET A CA  1 
ATOM   1730 C  C   . MET A 1 225 ? 20.888 7.539   82.548 1.00 38.45  ? 225 MET A C   1 
ATOM   1731 O  O   . MET A 1 225 ? 20.097 6.884   81.868 1.00 32.79  ? 225 MET A O   1 
ATOM   1732 C  CB  . MET A 1 225 ? 21.754 6.445   84.601 1.00 36.17  ? 225 MET A CB  1 
ATOM   1733 C  CG  . MET A 1 225 ? 22.060 6.537   86.074 1.00 36.28  ? 225 MET A CG  1 
ATOM   1734 S  SD  . MET A 1 225 ? 22.788 5.011   86.690 1.00 38.24  ? 225 MET A SD  1 
ATOM   1735 C  CE  . MET A 1 225 ? 21.408 3.878   86.694 1.00 42.79  ? 225 MET A CE  1 
ATOM   1736 N  N   . THR A 1 226 ? 21.863 8.268   82.017 1.00 36.40  ? 226 THR A N   1 
ATOM   1737 C  CA  . THR A 1 226 ? 22.346 8.004   80.682 1.00 31.41  ? 226 THR A CA  1 
ATOM   1738 C  C   . THR A 1 226 ? 23.872 8.055   80.722 1.00 30.97  ? 226 THR A C   1 
ATOM   1739 O  O   . THR A 1 226 ? 24.479 8.294   81.770 1.00 28.17  ? 226 THR A O   1 
ATOM   1740 C  CB  . THR A 1 226 ? 21.743 8.985   79.668 1.00 31.03  ? 226 THR A CB  1 
ATOM   1741 O  OG1 . THR A 1 226 ? 22.248 8.665   78.369 1.00 29.46  ? 226 THR A OG1 1 
ATOM   1742 C  CG2 . THR A 1 226 ? 22.107 10.426  80.032 1.00 31.66  ? 226 THR A CG2 1 
ATOM   1743 N  N   . ILE A 1 227 ? 24.496 7.770   79.586 1.00 32.48  ? 227 ILE A N   1 
ATOM   1744 C  CA  . ILE A 1 227 ? 25.936 7.917   79.412 1.00 36.14  ? 227 ILE A CA  1 
ATOM   1745 C  C   . ILE A 1 227 ? 26.145 8.854   78.234 1.00 33.01  ? 227 ILE A C   1 
ATOM   1746 O  O   . ILE A 1 227 ? 25.634 8.596   77.131 1.00 33.03  ? 227 ILE A O   1 
ATOM   1747 C  CB  . ILE A 1 227 ? 26.626 6.562   79.178 1.00 34.53  ? 227 ILE A CB  1 
ATOM   1748 C  CG1 . ILE A 1 227 ? 26.604 5.728   80.472 1.00 36.60  ? 227 ILE A CG1 1 
ATOM   1749 C  CG2 . ILE A 1 227 ? 28.040 6.770   78.699 1.00 37.57  ? 227 ILE A CG2 1 
ATOM   1750 C  CD1 . ILE A 1 227 ? 27.032 4.288   80.294 1.00 35.91  ? 227 ILE A CD1 1 
ATOM   1751 N  N   . ASN A 1 228 ? 26.852 9.959   78.461 1.00 36.27  ? 228 ASN A N   1 
ATOM   1752 C  CA  . ASN A 1 228 ? 27.038 10.918  77.374 1.00 33.73  ? 228 ASN A CA  1 
ATOM   1753 C  C   . ASN A 1 228 ? 28.222 11.825  77.684 1.00 32.75  ? 228 ASN A C   1 
ATOM   1754 O  O   . ASN A 1 228 ? 28.845 11.740  78.750 1.00 32.14  ? 228 ASN A O   1 
ATOM   1755 C  CB  . ASN A 1 228 ? 25.757 11.726  77.106 1.00 33.08  ? 228 ASN A CB  1 
ATOM   1756 C  CG  . ASN A 1 228 ? 25.496 11.906  75.623 1.00 36.13  ? 228 ASN A CG  1 
ATOM   1757 O  OD1 . ASN A 1 228 ? 26.410 12.271  74.884 1.00 33.27  ? 228 ASN A OD1 1 
ATOM   1758 N  ND2 . ASN A 1 228 ? 24.259 11.642  75.174 1.00 33.75  ? 228 ASN A ND2 1 
ATOM   1759 N  N   . GLY A 1 229 ? 28.556 12.667  76.704 1.00 34.21  ? 229 GLY A N   1 
ATOM   1760 C  CA  . GLY A 1 229 ? 29.672 13.570  76.806 1.00 35.67  ? 229 GLY A CA  1 
ATOM   1761 C  C   . GLY A 1 229 ? 29.262 14.979  77.187 1.00 33.59  ? 229 GLY A C   1 
ATOM   1762 O  O   . GLY A 1 229 ? 28.077 15.295  77.339 1.00 31.75  ? 229 GLY A O   1 
ATOM   1763 N  N   . PRO A 1 230 ? 30.261 15.850  77.364 1.00 33.71  ? 230 PRO A N   1 
ATOM   1764 C  CA  . PRO A 1 230 ? 29.975 17.269  77.651 1.00 32.48  ? 230 PRO A CA  1 
ATOM   1765 C  C   . PRO A 1 230 ? 29.098 17.950  76.600 1.00 32.61  ? 230 PRO A C   1 
ATOM   1766 O  O   . PRO A 1 230 ? 28.278 18.805  76.955 1.00 35.49  ? 230 PRO A O   1 
ATOM   1767 C  CB  . PRO A 1 230 ? 31.380 17.888  77.703 1.00 31.17  ? 230 PRO A CB  1 
ATOM   1768 C  CG  . PRO A 1 230 ? 32.280 16.746  78.057 1.00 30.64  ? 230 PRO A CG  1 
ATOM   1769 C  CD  . PRO A 1 230 ? 31.708 15.578  77.320 1.00 32.62  ? 230 PRO A CD  1 
ATOM   1770 N  N   . TRP A 1 231 ? 29.231 17.587  75.322 1.00 29.36  ? 231 TRP A N   1 
ATOM   1771 C  CA  . TRP A 1 231 ? 28.392 18.174  74.279 1.00 32.38  ? 231 TRP A CA  1 
ATOM   1772 C  C   . TRP A 1 231 ? 26.902 18.094  74.607 1.00 34.84  ? 231 TRP A C   1 
ATOM   1773 O  O   . TRP A 1 231 ? 26.098 18.871  74.068 1.00 37.55  ? 231 TRP A O   1 
ATOM   1774 C  CB  . TRP A 1 231 ? 28.673 17.461  72.945 1.00 35.12  ? 231 TRP A CB  1 
ATOM   1775 C  CG  . TRP A 1 231 ? 28.429 15.965  73.039 1.00 37.98  ? 231 TRP A CG  1 
ATOM   1776 C  CD1 . TRP A 1 231 ? 27.217 15.320  72.951 1.00 36.20  ? 231 TRP A CD1 1 
ATOM   1777 C  CD2 . TRP A 1 231 ? 29.411 14.933  73.263 1.00 33.72  ? 231 TRP A CD2 1 
ATOM   1778 N  NE1 . TRP A 1 231 ? 27.389 13.968  73.104 1.00 35.25  ? 231 TRP A NE1 1 
ATOM   1779 C  CE2 . TRP A 1 231 ? 28.723 13.704  73.301 1.00 34.99  ? 231 TRP A CE2 1 
ATOM   1780 C  CE3 . TRP A 1 231 ? 30.798 14.930  73.418 1.00 34.40  ? 231 TRP A CE3 1 
ATOM   1781 C  CZ2 . TRP A 1 231 ? 29.384 12.478  73.492 1.00 37.24  ? 231 TRP A CZ2 1 
ATOM   1782 C  CZ3 . TRP A 1 231 ? 31.454 13.705  73.617 1.00 37.50  ? 231 TRP A CZ3 1 
ATOM   1783 C  CH2 . TRP A 1 231 ? 30.743 12.504  73.655 1.00 33.91  ? 231 TRP A CH2 1 
ATOM   1784 N  N   . ALA A 1 232 ? 26.507 17.169  75.464 1.00 35.52  ? 232 ALA A N   1 
ATOM   1785 C  CA  . ALA A 1 232 ? 25.095 16.954  75.753 1.00 34.80  ? 232 ALA A CA  1 
ATOM   1786 C  C   . ALA A 1 232 ? 24.580 17.768  76.940 1.00 34.36  ? 232 ALA A C   1 
ATOM   1787 O  O   . ALA A 1 232 ? 23.362 17.822  77.135 1.00 29.43  ? 232 ALA A O   1 
ATOM   1788 C  CB  . ALA A 1 232 ? 24.842 15.465  76.010 1.00 36.41  ? 232 ALA A CB  1 
ATOM   1789 N  N   . TRP A 1 233 ? 25.465 18.378  77.747 1.00 32.87  ? 233 TRP A N   1 
ATOM   1790 C  CA  . TRP A 1 233 ? 25.006 19.067  78.956 1.00 36.10  ? 233 TRP A CA  1 
ATOM   1791 C  C   . TRP A 1 233 ? 24.033 20.185  78.622 1.00 40.27  ? 233 TRP A C   1 
ATOM   1792 O  O   . TRP A 1 233 ? 23.077 20.437  79.369 1.00 42.51  ? 233 TRP A O   1 
ATOM   1793 C  CB  . TRP A 1 233 ? 26.191 19.636  79.733 1.00 33.92  ? 233 TRP A CB  1 
ATOM   1794 C  CG  . TRP A 1 233 ? 27.155 18.590  80.195 1.00 31.07  ? 233 TRP A CG  1 
ATOM   1795 C  CD1 . TRP A 1 233 ? 26.944 17.237  80.253 1.00 28.96  ? 233 TRP A CD1 1 
ATOM   1796 C  CD2 . TRP A 1 233 ? 28.482 18.811  80.659 1.00 31.47  ? 233 TRP A CD2 1 
ATOM   1797 N  NE1 . TRP A 1 233 ? 28.066 16.603  80.694 1.00 33.37  ? 233 TRP A NE1 1 
ATOM   1798 C  CE2 . TRP A 1 233 ? 29.027 17.550  80.970 1.00 31.80  ? 233 TRP A CE2 1 
ATOM   1799 C  CE3 . TRP A 1 233 ? 29.265 19.960  80.861 1.00 37.20  ? 233 TRP A CE3 1 
ATOM   1800 C  CZ2 . TRP A 1 233 ? 30.319 17.399  81.469 1.00 29.80  ? 233 TRP A CZ2 1 
ATOM   1801 C  CZ3 . TRP A 1 233 ? 30.560 19.804  81.338 1.00 33.21  ? 233 TRP A CZ3 1 
ATOM   1802 C  CH2 . TRP A 1 233 ? 31.071 18.530  81.638 1.00 31.74  ? 233 TRP A CH2 1 
ATOM   1803 N  N   . SER A 1 234 ? 24.252 20.852  77.492 1.00 39.29  ? 234 SER A N   1 
ATOM   1804 C  CA  . SER A 1 234 ? 23.463 22.030  77.151 1.00 43.58  ? 234 SER A CA  1 
ATOM   1805 C  C   . SER A 1 234 ? 21.975 21.692  77.027 1.00 43.31  ? 234 SER A C   1 
ATOM   1806 O  O   . SER A 1 234 ? 21.125 22.415  77.561 1.00 41.04  ? 234 SER A O   1 
ATOM   1807 C  CB  . SER A 1 234 ? 24.036 22.651  75.871 1.00 40.10  ? 234 SER A CB  1 
ATOM   1808 O  OG  . SER A 1 234 ? 23.073 23.400  75.189 1.00 45.90  ? 234 SER A OG  1 
ATOM   1809 N  N   . ASN A 1 235 ? 21.635 20.571  76.372 1.00 42.33  ? 235 ASN A N   1 
ATOM   1810 C  CA  . ASN A 1 235 ? 20.229 20.168  76.301 1.00 37.81  ? 235 ASN A CA  1 
ATOM   1811 C  C   . ASN A 1 235 ? 19.699 19.720  77.656 1.00 34.78  ? 235 ASN A C   1 
ATOM   1812 O  O   . ASN A 1 235 ? 18.500 19.848  77.920 1.00 36.27  ? 235 ASN A O   1 
ATOM   1813 C  CB  . ASN A 1 235 ? 20.033 19.041  75.291 1.00 36.34  ? 235 ASN A CB  1 
ATOM   1814 C  CG  . ASN A 1 235 ? 19.977 19.543  73.842 1.00 44.36  ? 235 ASN A CG  1 
ATOM   1815 O  OD1 . ASN A 1 235 ? 19.899 20.754  73.584 1.00 38.14  ? 235 ASN A OD1 1 
ATOM   1816 N  ND2 . ASN A 1 235 ? 20.016 18.605  72.890 1.00 39.84  ? 235 ASN A ND2 1 
ATOM   1817 N  N   . ILE A 1 236 ? 20.554 19.174  78.522 1.00 36.19  ? 236 ILE A N   1 
ATOM   1818 C  CA  . ILE A 1 236 ? 20.056 18.741  79.826 1.00 41.00  ? 236 ILE A CA  1 
ATOM   1819 C  C   . ILE A 1 236 ? 19.713 19.954  80.681 1.00 39.25  ? 236 ILE A C   1 
ATOM   1820 O  O   . ILE A 1 236 ? 18.694 19.958  81.387 1.00 39.68  ? 236 ILE A O   1 
ATOM   1821 C  CB  . ILE A 1 236 ? 21.063 17.813  80.540 1.00 41.00  ? 236 ILE A CB  1 
ATOM   1822 C  CG1 . ILE A 1 236 ? 21.301 16.523  79.760 1.00 35.71  ? 236 ILE A CG1 1 
ATOM   1823 C  CG2 . ILE A 1 236 ? 20.557 17.428  81.925 1.00 43.35  ? 236 ILE A CG2 1 
ATOM   1824 C  CD1 . ILE A 1 236 ? 22.467 15.735  80.344 1.00 35.72  ? 236 ILE A CD1 1 
ATOM   1825 N  N   . ASP A 1 237 ? 20.564 20.993  80.636 1.00 42.22  ? 237 ASP A N   1 
ATOM   1826 C  CA  . ASP A 1 237 ? 20.269 22.255  81.319 1.00 38.55  ? 237 ASP A CA  1 
ATOM   1827 C  C   . ASP A 1 237 ? 18.869 22.750  80.962 1.00 37.62  ? 237 ASP A C   1 
ATOM   1828 O  O   . ASP A 1 237 ? 18.038 22.999  81.847 1.00 34.24  ? 237 ASP A O   1 
ATOM   1829 C  CB  . ASP A 1 237 ? 21.308 23.321  80.955 1.00 36.08  ? 237 ASP A CB  1 
ATOM   1830 C  CG  . ASP A 1 237 ? 22.702 22.994  81.469 1.00 38.79  ? 237 ASP A CG  1 
ATOM   1831 O  OD1 . ASP A 1 237 ? 22.824 22.320  82.513 1.00 35.70  ? 237 ASP A OD1 1 
ATOM   1832 O  OD2 . ASP A 1 237 ? 23.688 23.410  80.818 1.00 41.51  ? 237 ASP A OD2 1 
ATOM   1833 N  N   . THR A 1 238 ? 18.589 22.861  79.657 1.00 32.24  ? 238 THR A N   1 
ATOM   1834 C  CA  . THR A 1 238 ? 17.294 23.339  79.192 1.00 36.78  ? 238 THR A CA  1 
ATOM   1835 C  C   . THR A 1 238 ? 16.154 22.499  79.743 1.00 35.80  ? 238 THR A C   1 
ATOM   1836 O  O   . THR A 1 238 ? 15.108 23.031  80.124 1.00 42.20  ? 238 THR A O   1 
ATOM   1837 C  CB  . THR A 1 238 ? 17.279 23.324  77.665 1.00 34.39  ? 238 THR A CB  1 
ATOM   1838 O  OG1 . THR A 1 238 ? 18.324 24.177  77.221 1.00 35.62  ? 238 THR A OG1 1 
ATOM   1839 C  CG2 . THR A 1 238 ? 15.955 23.812  77.122 1.00 31.49  ? 238 THR A CG2 1 
ATOM   1840 N  N   . SER A 1 239 ? 16.328 21.182  79.755 1.00 34.64  ? 239 SER A N   1 
ATOM   1841 C  CA  . SER A 1 239 ? 15.329 20.280  80.311 1.00 38.00  ? 239 SER A CA  1 
ATOM   1842 C  C   . SER A 1 239 ? 15.004 20.610  81.763 1.00 39.56  ? 239 SER A C   1 
ATOM   1843 O  O   . SER A 1 239 ? 13.892 20.333  82.224 1.00 40.96  ? 239 SER A O   1 
ATOM   1844 C  CB  . SER A 1 239 ? 15.842 18.845  80.227 1.00 40.79  ? 239 SER A CB  1 
ATOM   1845 O  OG  . SER A 1 239 ? 16.798 18.629  81.266 1.00 33.72  ? 239 SER A OG  1 
ATOM   1846 N  N   . ALA A 1 240 ? 15.964 21.174  82.495 1.00 44.20  ? 240 ALA A N   1 
ATOM   1847 C  CA  . ALA A 1 240 ? 15.899 21.480  83.928 1.00 47.99  ? 240 ALA A CA  1 
ATOM   1848 C  C   . ALA A 1 240 ? 15.892 20.232  84.798 1.00 43.05  ? 240 ALA A C   1 
ATOM   1849 O  O   . ALA A 1 240 ? 15.579 20.322  85.978 1.00 43.78  ? 240 ALA A O   1 
ATOM   1850 C  CB  . ALA A 1 240 ? 14.698 22.365  84.298 1.00 43.99  ? 240 ALA A CB  1 
ATOM   1851 N  N   . VAL A 1 241 ? 16.247 19.067  84.253 1.00 45.92  ? 241 VAL A N   1 
ATOM   1852 C  CA  . VAL A 1 241 ? 16.408 17.884  85.088 1.00 40.46  ? 241 VAL A CA  1 
ATOM   1853 C  C   . VAL A 1 241 ? 17.493 18.148  86.132 1.00 40.21  ? 241 VAL A C   1 
ATOM   1854 O  O   . VAL A 1 241 ? 18.512 18.798  85.857 1.00 38.45  ? 241 VAL A O   1 
ATOM   1855 C  CB  . VAL A 1 241 ? 16.724 16.653  84.216 1.00 42.76  ? 241 VAL A CB  1 
ATOM   1856 C  CG1 . VAL A 1 241 ? 17.231 15.495  85.056 1.00 41.58  ? 241 VAL A CG1 1 
ATOM   1857 C  CG2 . VAL A 1 241 ? 15.477 16.215  83.432 1.00 42.48  ? 241 VAL A CG2 1 
ATOM   1858 N  N   . ASN A 1 242 ? 17.252 17.683  87.357 1.00 35.99  ? 242 ASN A N   1 
ATOM   1859 C  CA  . ASN A 1 242 ? 18.171 17.865  88.484 1.00 32.76  ? 242 ASN A CA  1 
ATOM   1860 C  C   . ASN A 1 242 ? 19.254 16.788  88.388 1.00 35.16  ? 242 ASN A C   1 
ATOM   1861 O  O   . ASN A 1 242 ? 19.133 15.707  88.961 1.00 37.97  ? 242 ASN A O   1 
ATOM   1862 C  CB  . ASN A 1 242 ? 17.378 17.794  89.789 1.00 31.12  ? 242 ASN A CB  1 
ATOM   1863 C  CG  . ASN A 1 242 ? 18.263 17.878  91.031 1.00 34.83  ? 242 ASN A CG  1 
ATOM   1864 O  OD1 . ASN A 1 242 ? 19.389 18.395  90.975 1.00 32.68  ? 242 ASN A OD1 1 
ATOM   1865 N  ND2 . ASN A 1 242 ? 17.745 17.389  92.165 1.00 35.09  ? 242 ASN A ND2 1 
ATOM   1866 N  N   . TYR A 1 243 ? 20.337 17.073  87.661 1.00 38.85  ? 243 TYR A N   1 
ATOM   1867 C  CA  . TYR A 1 243 ? 21.257 16.032  87.210 1.00 38.32  ? 243 TYR A CA  1 
ATOM   1868 C  C   . TYR A 1 243 ? 22.685 16.192  87.731 1.00 39.44  ? 243 TYR A C   1 
ATOM   1869 O  O   . TYR A 1 243 ? 23.172 17.305  87.945 1.00 33.87  ? 243 TYR A O   1 
ATOM   1870 C  CB  . TYR A 1 243 ? 21.312 15.977  85.678 1.00 43.04  ? 243 TYR A CB  1 
ATOM   1871 C  CG  . TYR A 1 243 ? 22.157 17.071  85.027 1.00 44.09  ? 243 TYR A CG  1 
ATOM   1872 C  CD1 . TYR A 1 243 ? 21.697 18.379  84.953 1.00 43.34  ? 243 TYR A CD1 1 
ATOM   1873 C  CD2 . TYR A 1 243 ? 23.398 16.777  84.455 1.00 38.51  ? 243 TYR A CD2 1 
ATOM   1874 C  CE1 . TYR A 1 243 ? 22.447 19.372  84.340 1.00 41.84  ? 243 TYR A CE1 1 
ATOM   1875 C  CE2 . TYR A 1 243 ? 24.166 17.767  83.836 1.00 41.44  ? 243 TYR A CE2 1 
ATOM   1876 C  CZ  . TYR A 1 243 ? 23.682 19.068  83.785 1.00 43.98  ? 243 TYR A CZ  1 
ATOM   1877 O  OH  . TYR A 1 243 ? 24.422 20.068  83.170 1.00 41.46  ? 243 TYR A OH  1 
ATOM   1878 N  N   . GLY A 1 244 ? 23.366 15.046  87.881 1.00 38.53  ? 244 GLY A N   1 
ATOM   1879 C  CA  . GLY A 1 244 ? 24.781 15.006  88.177 1.00 35.09  ? 244 GLY A CA  1 
ATOM   1880 C  C   . GLY A 1 244 ? 25.554 14.311  87.061 1.00 37.18  ? 244 GLY A C   1 
ATOM   1881 O  O   . GLY A 1 244 ? 24.976 13.681  86.154 1.00 32.20  ? 244 GLY A O   1 
ATOM   1882 N  N   . VAL A 1 245 ? 26.879 14.463  87.122 1.00 35.31  ? 245 VAL A N   1 
ATOM   1883 C  CA  . VAL A 1 245 ? 27.829 13.882  86.173 1.00 35.73  ? 245 VAL A CA  1 
ATOM   1884 C  C   . VAL A 1 245 ? 28.983 13.309  86.975 1.00 35.09  ? 245 VAL A C   1 
ATOM   1885 O  O   . VAL A 1 245 ? 29.567 14.014  87.804 1.00 30.25  ? 245 VAL A O   1 
ATOM   1886 C  CB  . VAL A 1 245 ? 28.376 14.925  85.178 1.00 36.50  ? 245 VAL A CB  1 
ATOM   1887 C  CG1 . VAL A 1 245 ? 29.481 14.310  84.309 1.00 31.90  ? 245 VAL A CG1 1 
ATOM   1888 C  CG2 . VAL A 1 245 ? 27.234 15.558  84.353 1.00 34.89  ? 245 VAL A CG2 1 
ATOM   1889 N  N   . THR A 1 246 ? 29.318 12.040  86.742 1.00 34.84  ? 246 THR A N   1 
ATOM   1890 C  CA  . THR A 1 246 ? 30.229 11.367  87.654 1.00 38.72  ? 246 THR A CA  1 
ATOM   1891 C  C   . THR A 1 246 ? 31.025 10.304  86.907 1.00 35.70  ? 246 THR A C   1 
ATOM   1892 O  O   . THR A 1 246 ? 30.829 10.072  85.702 1.00 32.04  ? 246 THR A O   1 
ATOM   1893 C  CB  . THR A 1 246 ? 29.451 10.785  88.844 1.00 39.91  ? 246 THR A CB  1 
ATOM   1894 O  OG1 . THR A 1 246 ? 30.375 10.327  89.825 1.00 39.73  ? 246 THR A OG1 1 
ATOM   1895 C  CG2 . THR A 1 246 ? 28.567 9.633   88.408 1.00 37.59  ? 246 THR A CG2 1 
ATOM   1896 N  N   . VAL A 1 247 ? 31.959 9.686   87.642 1.00 36.00  ? 247 VAL A N   1 
ATOM   1897 C  CA  . VAL A 1 247 ? 32.754 8.583   87.117 1.00 39.47  ? 247 VAL A CA  1 
ATOM   1898 C  C   . VAL A 1 247 ? 31.842 7.460   86.652 1.00 37.84  ? 247 VAL A C   1 
ATOM   1899 O  O   . VAL A 1 247 ? 30.812 7.164   87.272 1.00 35.78  ? 247 VAL A O   1 
ATOM   1900 C  CB  . VAL A 1 247 ? 33.742 8.075   88.185 1.00 44.70  ? 247 VAL A CB  1 
ATOM   1901 C  CG1 . VAL A 1 247 ? 32.990 7.470   89.375 1.00 41.85  ? 247 VAL A CG1 1 
ATOM   1902 C  CG2 . VAL A 1 247 ? 34.743 7.065   87.587 1.00 42.93  ? 247 VAL A CG2 1 
ATOM   1903 N  N   . LEU A 1 248 ? 32.220 6.831   85.546 1.00 37.88  ? 248 LEU A N   1 
ATOM   1904 C  CA  . LEU A 1 248 ? 31.492 5.685   85.027 1.00 36.55  ? 248 LEU A CA  1 
ATOM   1905 C  C   . LEU A 1 248 ? 31.460 4.535   86.039 1.00 34.72  ? 248 LEU A C   1 
ATOM   1906 O  O   . LEU A 1 248 ? 32.345 4.418   86.905 1.00 32.84  ? 248 LEU A O   1 
ATOM   1907 C  CB  . LEU A 1 248 ? 32.146 5.222   83.732 1.00 37.13  ? 248 LEU A CB  1 
ATOM   1908 C  CG  . LEU A 1 248 ? 31.876 6.233   82.619 1.00 35.51  ? 248 LEU A CG  1 
ATOM   1909 C  CD1 . LEU A 1 248 ? 32.872 6.071   81.517 1.00 35.93  ? 248 LEU A CD1 1 
ATOM   1910 C  CD2 . LEU A 1 248 ? 30.440 6.050   82.120 1.00 36.03  ? 248 LEU A CD2 1 
ATOM   1911 N  N   . PRO A 1 249 ? 30.437 3.678   85.977 1.00 35.82  ? 249 PRO A N   1 
ATOM   1912 C  CA  . PRO A 1 249 ? 30.418 2.513   86.876 1.00 37.83  ? 249 PRO A CA  1 
ATOM   1913 C  C   . PRO A 1 249 ? 31.561 1.568   86.535 1.00 35.88  ? 249 PRO A C   1 
ATOM   1914 O  O   . PRO A 1 249 ? 31.936 1.428   85.364 1.00 32.32  ? 249 PRO A O   1 
ATOM   1915 C  CB  . PRO A 1 249 ? 29.055 1.862   86.608 1.00 37.81  ? 249 PRO A CB  1 
ATOM   1916 C  CG  . PRO A 1 249 ? 28.257 2.865   85.792 1.00 37.98  ? 249 PRO A CG  1 
ATOM   1917 C  CD  . PRO A 1 249 ? 29.261 3.719   85.083 1.00 36.37  ? 249 PRO A CD  1 
ATOM   1918 N  N   . THR A 1 250 ? 32.136 0.939   87.570 1.00 34.97  ? 250 THR A N   1 
ATOM   1919 C  CA  . THR A 1 250 ? 33.087 -0.140  87.312 1.00 39.43  ? 250 THR A CA  1 
ATOM   1920 C  C   . THR A 1 250 ? 32.354 -1.396  86.823 1.00 38.23  ? 250 THR A C   1 
ATOM   1921 O  O   . THR A 1 250 ? 31.120 -1.493  86.865 1.00 40.12  ? 250 THR A O   1 
ATOM   1922 C  CB  . THR A 1 250 ? 33.918 -0.475  88.559 1.00 39.36  ? 250 THR A CB  1 
ATOM   1923 O  OG1 . THR A 1 250 ? 33.055 -0.981  89.592 1.00 42.03  ? 250 THR A OG1 1 
ATOM   1924 C  CG2 . THR A 1 250 ? 34.668 0.756   89.055 1.00 35.34  ? 250 THR A CG2 1 
ATOM   1925 N  N   . PHE A 1 251 ? 33.143 -2.346  86.310 1.00 40.30  ? 251 PHE A N   1 
ATOM   1926 C  CA  . PHE A 1 251 ? 32.675 -3.651  85.853 1.00 38.52  ? 251 PHE A CA  1 
ATOM   1927 C  C   . PHE A 1 251 ? 33.704 -4.658  86.306 1.00 44.16  ? 251 PHE A C   1 
ATOM   1928 O  O   . PHE A 1 251 ? 34.883 -4.529  85.949 1.00 42.03  ? 251 PHE A O   1 
ATOM   1929 C  CB  . PHE A 1 251 ? 32.535 -3.733  84.332 1.00 39.27  ? 251 PHE A CB  1 
ATOM   1930 C  CG  . PHE A 1 251 ? 32.121 -5.108  83.824 1.00 45.69  ? 251 PHE A CG  1 
ATOM   1931 C  CD1 . PHE A 1 251 ? 30.983 -5.742  84.318 1.00 45.47  ? 251 PHE A CD1 1 
ATOM   1932 C  CD2 . PHE A 1 251 ? 32.851 -5.756  82.824 1.00 42.09  ? 251 PHE A CD2 1 
ATOM   1933 C  CE1 . PHE A 1 251 ? 30.595 -6.996  83.831 1.00 45.85  ? 251 PHE A CE1 1 
ATOM   1934 C  CE2 . PHE A 1 251 ? 32.456 -6.996  82.337 1.00 39.65  ? 251 PHE A CE2 1 
ATOM   1935 C  CZ  . PHE A 1 251 ? 31.333 -7.621  82.842 1.00 42.31  ? 251 PHE A CZ  1 
ATOM   1936 N  N   . LYS A 1 252 ? 33.261 -5.660  87.066 1.00 46.00  ? 252 LYS A N   1 
ATOM   1937 C  CA  . LYS A 1 252 ? 34.173 -6.612  87.692 1.00 44.99  ? 252 LYS A CA  1 
ATOM   1938 C  C   . LYS A 1 252 ? 35.287 -5.866  88.428 1.00 40.85  ? 252 LYS A C   1 
ATOM   1939 O  O   . LYS A 1 252 ? 36.471 -6.170  88.288 1.00 36.09  ? 252 LYS A O   1 
ATOM   1940 C  CB  . LYS A 1 252 ? 34.746 -7.591  86.656 1.00 47.90  ? 252 LYS A CB  1 
ATOM   1941 C  CG  . LYS A 1 252 ? 33.681 -8.361  85.860 1.00 51.70  ? 252 LYS A CG  1 
ATOM   1942 C  CD  . LYS A 1 252 ? 34.098 -9.801  85.575 1.00 53.42  ? 252 LYS A CD  1 
ATOM   1943 C  CE  . LYS A 1 252 ? 33.037 -10.543 84.765 1.00 56.11  ? 252 LYS A CE  1 
ATOM   1944 N  NZ  . LYS A 1 252 ? 31.771 -10.832 85.525 1.00 57.54  ? 252 LYS A NZ  1 
ATOM   1945 N  N   . GLY A 1 253 ? 34.896 -4.845  89.192 1.00 38.96  ? 253 GLY A N   1 
ATOM   1946 C  CA  . GLY A 1 253 ? 35.848 -4.060  89.961 1.00 39.91  ? 253 GLY A CA  1 
ATOM   1947 C  C   . GLY A 1 253 ? 36.750 -3.141  89.157 1.00 39.89  ? 253 GLY A C   1 
ATOM   1948 O  O   . GLY A 1 253 ? 37.543 -2.409  89.756 1.00 39.91  ? 253 GLY A O   1 
ATOM   1949 N  N   . GLN A 1 254 ? 36.647 -3.140  87.788 1.00 41.24  ? 254 GLN A N   1 
ATOM   1950 C  CA  . GLN A 1 254 ? 37.566 -2.385  86.941 1.00 43.52  ? 254 GLN A CA  1 
ATOM   1951 C  C   . GLN A 1 254 ? 36.884 -1.155  86.352 1.00 44.56  ? 254 GLN A C   1 
ATOM   1952 O  O   . GLN A 1 254 ? 35.691 -1.206  86.018 1.00 43.22  ? 254 GLN A O   1 
ATOM   1953 C  CB  . GLN A 1 254 ? 38.118 -3.258  85.803 1.00 48.43  ? 254 GLN A CB  1 
ATOM   1954 C  CG  . GLN A 1 254 ? 38.831 -4.529  86.291 1.00 51.60  ? 254 GLN A CG  1 
ATOM   1955 C  CD  . GLN A 1 254 ? 40.069 -4.211  87.123 1.00 58.51  ? 254 GLN A CD  1 
ATOM   1956 O  OE1 . GLN A 1 254 ? 40.190 -4.631  88.274 1.00 55.22  ? 254 GLN A OE1 1 
ATOM   1957 N  NE2 . GLN A 1 254 ? 40.984 -3.446  86.548 1.00 66.97  ? 254 GLN A NE2 1 
ATOM   1958 N  N   . PRO A 1 255 ? 37.606 -0.044  86.213 1.00 37.60  ? 255 PRO A N   1 
ATOM   1959 C  CA  . PRO A 1 255 ? 36.972 1.181   85.712 1.00 40.35  ? 255 PRO A CA  1 
ATOM   1960 C  C   . PRO A 1 255 ? 36.478 0.986   84.291 1.00 40.48  ? 255 PRO A C   1 
ATOM   1961 O  O   . PRO A 1 255 ? 37.080 0.247   83.501 1.00 36.61  ? 255 PRO A O   1 
ATOM   1962 C  CB  . PRO A 1 255 ? 38.098 2.216   85.777 1.00 43.59  ? 255 PRO A CB  1 
ATOM   1963 C  CG  . PRO A 1 255 ? 39.343 1.385   85.662 1.00 42.58  ? 255 PRO A CG  1 
ATOM   1964 C  CD  . PRO A 1 255 ? 39.047 0.145   86.450 1.00 40.87  ? 255 PRO A CD  1 
ATOM   1965 N  N   . SER A 1 256 ? 35.348 1.625   83.981 1.00 36.75  ? 256 SER A N   1 
ATOM   1966 C  CA  . SER A 1 256 ? 34.940 1.722   82.587 1.00 38.60  ? 256 SER A CA  1 
ATOM   1967 C  C   . SER A 1 256 ? 35.975 2.545   81.831 1.00 40.07  ? 256 SER A C   1 
ATOM   1968 O  O   . SER A 1 256 ? 36.534 3.506   82.365 1.00 36.36  ? 256 SER A O   1 
ATOM   1969 C  CB  . SER A 1 256 ? 33.555 2.351   82.466 1.00 42.32  ? 256 SER A CB  1 
ATOM   1970 O  OG  . SER A 1 256 ? 32.535 1.403   82.705 1.00 41.44  ? 256 SER A OG  1 
ATOM   1971 N  N   . LYS A 1 257 ? 36.252 2.135   80.590 1.00 38.52  ? 257 LYS A N   1 
ATOM   1972 C  CA  . LYS A 1 257 ? 37.364 2.644   79.792 1.00 38.99  ? 257 LYS A CA  1 
ATOM   1973 C  C   . LYS A 1 257 ? 36.804 3.329   78.552 1.00 35.36  ? 257 LYS A C   1 
ATOM   1974 O  O   . LYS A 1 257 ? 36.818 2.749   77.455 1.00 30.70  ? 257 LYS A O   1 
ATOM   1975 C  CB  . LYS A 1 257 ? 38.318 1.522   79.380 1.00 44.48  ? 257 LYS A CB  1 
ATOM   1976 C  CG  . LYS A 1 257 ? 39.442 1.249   80.324 1.00 49.19  ? 257 LYS A CG  1 
ATOM   1977 C  CD  . LYS A 1 257 ? 40.398 0.214   79.736 1.00 55.74  ? 257 LYS A CD  1 
ATOM   1978 C  CE  . LYS A 1 257 ? 41.634 0.877   79.137 1.00 63.16  ? 257 LYS A CE  1 
ATOM   1979 N  NZ  . LYS A 1 257 ? 42.631 -0.131  78.653 1.00 63.59  ? 257 LYS A NZ  1 
ATOM   1980 N  N   . PRO A 1 258 ? 36.325 4.562   78.681 1.00 38.92  ? 258 PRO A N   1 
ATOM   1981 C  CA  . PRO A 1 258 ? 35.788 5.269   77.516 1.00 37.29  ? 258 PRO A CA  1 
ATOM   1982 C  C   . PRO A 1 258 ? 36.906 5.742   76.600 1.00 36.89  ? 258 PRO A C   1 
ATOM   1983 O  O   . PRO A 1 258 ? 38.063 5.897   77.005 1.00 31.69  ? 258 PRO A O   1 
ATOM   1984 C  CB  . PRO A 1 258 ? 35.042 6.451   78.141 1.00 38.90  ? 258 PRO A CB  1 
ATOM   1985 C  CG  . PRO A 1 258 ? 35.838 6.739   79.393 1.00 36.97  ? 258 PRO A CG  1 
ATOM   1986 C  CD  . PRO A 1 258 ? 36.327 5.408   79.889 1.00 38.07  ? 258 PRO A CD  1 
ATOM   1987 N  N   . PHE A 1 259 ? 36.542 5.947   75.334 1.00 37.23  ? 259 PHE A N   1 
ATOM   1988 C  CA  . PHE A 1 259 ? 37.482 6.545   74.390 1.00 39.92  ? 259 PHE A CA  1 
ATOM   1989 C  C   . PHE A 1 259 ? 37.718 8.006   74.732 1.00 36.37  ? 259 PHE A C   1 
ATOM   1990 O  O   . PHE A 1 259 ? 36.787 8.732   75.111 1.00 33.45  ? 259 PHE A O   1 
ATOM   1991 C  CB  . PHE A 1 259 ? 36.965 6.424   72.956 1.00 43.22  ? 259 PHE A CB  1 
ATOM   1992 C  CG  . PHE A 1 259 ? 37.293 5.114   72.330 1.00 42.78  ? 259 PHE A CG  1 
ATOM   1993 C  CD1 . PHE A 1 259 ? 38.606 4.694   72.250 1.00 41.34  ? 259 PHE A CD1 1 
ATOM   1994 C  CD2 . PHE A 1 259 ? 36.291 4.279   71.866 1.00 47.20  ? 259 PHE A CD2 1 
ATOM   1995 C  CE1 . PHE A 1 259 ? 38.917 3.470   71.688 1.00 45.43  ? 259 PHE A CE1 1 
ATOM   1996 C  CE2 . PHE A 1 259 ? 36.596 3.054   71.300 1.00 40.50  ? 259 PHE A CE2 1 
ATOM   1997 C  CZ  . PHE A 1 259 ? 37.905 2.651   71.215 1.00 42.81  ? 259 PHE A CZ  1 
ATOM   1998 N  N   . VAL A 1 260 ? 38.976 8.428   74.604 1.00 34.41  ? 260 VAL A N   1 
ATOM   1999 C  CA  . VAL A 1 260 ? 39.401 9.794   74.887 1.00 36.27  ? 260 VAL A CA  1 
ATOM   2000 C  C   . VAL A 1 260 ? 39.667 10.530  73.578 1.00 32.98  ? 260 VAL A C   1 
ATOM   2001 O  O   . VAL A 1 260 ? 40.314 9.991   72.674 1.00 38.70  ? 260 VAL A O   1 
ATOM   2002 C  CB  . VAL A 1 260 ? 40.662 9.819   75.772 1.00 35.61  ? 260 VAL A CB  1 
ATOM   2003 C  CG1 . VAL A 1 260 ? 41.080 11.247  76.036 1.00 39.82  ? 260 VAL A CG1 1 
ATOM   2004 C  CG2 . VAL A 1 260 ? 40.425 9.062   77.085 1.00 37.49  ? 260 VAL A CG2 1 
ATOM   2005 N  N   . GLY A 1 261 ? 39.186 11.768  73.493 1.00 32.27  ? 261 GLY A N   1 
ATOM   2006 C  CA  . GLY A 1 261 ? 39.352 12.606  72.325 1.00 31.98  ? 261 GLY A CA  1 
ATOM   2007 C  C   . GLY A 1 261 ? 40.033 13.891  72.739 1.00 37.00  ? 261 GLY A C   1 
ATOM   2008 O  O   . GLY A 1 261 ? 39.603 14.531  73.700 1.00 35.99  ? 261 GLY A O   1 
ATOM   2009 N  N   . VAL A 1 262 ? 41.116 14.263  72.065 1.00 35.06  ? 262 VAL A N   1 
ATOM   2010 C  CA  . VAL A 1 262 ? 41.937 15.392  72.480 1.00 31.99  ? 262 VAL A CA  1 
ATOM   2011 C  C   . VAL A 1 262 ? 41.902 16.411  71.360 1.00 29.85  ? 262 VAL A C   1 
ATOM   2012 O  O   . VAL A 1 262 ? 42.446 16.166  70.274 1.00 35.65  ? 262 VAL A O   1 
ATOM   2013 C  CB  . VAL A 1 262 ? 43.381 14.979  72.802 1.00 32.12  ? 262 VAL A CB  1 
ATOM   2014 C  CG1 . VAL A 1 262 ? 44.180 16.182  73.271 1.00 33.34  ? 262 VAL A CG1 1 
ATOM   2015 C  CG2 . VAL A 1 262 ? 43.402 13.880  73.862 1.00 34.53  ? 262 VAL A CG2 1 
ATOM   2016 N  N   . LEU A 1 263 ? 41.247 17.543  71.604 1.00 27.79  ? 263 LEU A N   1 
ATOM   2017 C  CA  . LEU A 1 263 ? 41.349 18.663  70.683 1.00 30.50  ? 263 LEU A CA  1 
ATOM   2018 C  C   . LEU A 1 263 ? 42.794 19.163  70.666 1.00 33.65  ? 263 LEU A C   1 
ATOM   2019 O  O   . LEU A 1 263 ? 43.349 19.508  71.722 1.00 29.24  ? 263 LEU A O   1 
ATOM   2020 C  CB  . LEU A 1 263 ? 40.377 19.775  71.098 1.00 29.58  ? 263 LEU A CB  1 
ATOM   2021 C  CG  . LEU A 1 263 ? 40.370 21.039  70.223 1.00 28.43  ? 263 LEU A CG  1 
ATOM   2022 C  CD1 . LEU A 1 263 ? 39.897 20.766  68.787 1.00 29.96  ? 263 LEU A CD1 1 
ATOM   2023 C  CD2 . LEU A 1 263 ? 39.537 22.100  70.876 1.00 32.06  ? 263 LEU A CD2 1 
ATOM   2024 N  N   . SER A 1 264 ? 43.403 19.190  69.467 1.00 31.48  ? 264 SER A N   1 
ATOM   2025 C  CA  . SER A 1 264 ? 44.837 19.422  69.310 1.00 28.90  ? 264 SER A CA  1 
ATOM   2026 C  C   . SER A 1 264 ? 45.105 20.416  68.187 1.00 31.32  ? 264 SER A C   1 
ATOM   2027 O  O   . SER A 1 264 ? 44.354 20.482  67.201 1.00 32.88  ? 264 SER A O   1 
ATOM   2028 C  CB  . SER A 1 264 ? 45.604 18.119  68.990 1.00 26.93  ? 264 SER A CB  1 
ATOM   2029 O  OG  . SER A 1 264 ? 45.263 17.066  69.872 1.00 25.92  ? 264 SER A OG  1 
ATOM   2030 N  N   . ALA A 1 265 ? 46.223 21.138  68.306 1.00 28.93  ? 265 ALA A N   1 
ATOM   2031 C  CA  . ALA A 1 265 ? 46.638 22.112  67.300 1.00 33.12  ? 265 ALA A CA  1 
ATOM   2032 C  C   . ALA A 1 265 ? 47.861 21.571  66.571 1.00 32.33  ? 265 ALA A C   1 
ATOM   2033 O  O   . ALA A 1 265 ? 48.896 21.315  67.198 1.00 38.30  ? 265 ALA A O   1 
ATOM   2034 C  CB  . ALA A 1 265 ? 46.931 23.480  67.925 1.00 33.66  ? 265 ALA A CB  1 
ATOM   2035 N  N   . GLY A 1 266 ? 47.732 21.366  65.247 1.00 30.13  ? 266 GLY A N   1 
ATOM   2036 C  CA  . GLY A 1 266 ? 48.843 20.933  64.425 1.00 31.96  ? 266 GLY A CA  1 
ATOM   2037 C  C   . GLY A 1 266 ? 49.409 22.080  63.590 1.00 34.54  ? 266 GLY A C   1 
ATOM   2038 O  O   . GLY A 1 266 ? 48.745 23.083  63.361 1.00 32.16  ? 266 GLY A O   1 
ATOM   2039 N  N   . ILE A 1 267 ? 50.659 21.932  63.143 1.00 32.68  ? 267 ILE A N   1 
ATOM   2040 C  CA  . ILE A 1 267 ? 51.316 22.937  62.313 1.00 31.51  ? 267 ILE A CA  1 
ATOM   2041 C  C   . ILE A 1 267 ? 51.467 22.390  60.890 1.00 29.78  ? 267 ILE A C   1 
ATOM   2042 O  O   . ILE A 1 267 ? 52.025 21.309  60.683 1.00 27.08  ? 267 ILE A O   1 
ATOM   2043 C  CB  . ILE A 1 267 ? 52.676 23.366  62.904 1.00 32.40  ? 267 ILE A CB  1 
ATOM   2044 C  CG1 . ILE A 1 267 ? 52.462 23.964  64.303 1.00 30.39  ? 267 ILE A CG1 1 
ATOM   2045 C  CG2 . ILE A 1 267 ? 53.359 24.416  62.013 1.00 30.36  ? 267 ILE A CG2 1 
ATOM   2046 C  CD1 . ILE A 1 267 ? 53.688 24.480  64.964 1.00 28.91  ? 267 ILE A CD1 1 
ATOM   2047 N  N   . ASN A 1 268 ? 50.957 23.137  59.916 1.00 28.86  ? 268 ASN A N   1 
ATOM   2048 C  CA  . ASN A 1 268 ? 51.052 22.733  58.513 1.00 28.54  ? 268 ASN A CA  1 
ATOM   2049 C  C   . ASN A 1 268 ? 52.515 22.504  58.108 1.00 29.61  ? 268 ASN A C   1 
ATOM   2050 O  O   . ASN A 1 268 ? 53.353 23.414  58.208 1.00 29.22  ? 268 ASN A O   1 
ATOM   2051 C  CB  . ASN A 1 268 ? 50.406 23.815  57.650 1.00 27.76  ? 268 ASN A CB  1 
ATOM   2052 C  CG  . ASN A 1 268 ? 50.284 23.412  56.197 1.00 30.67  ? 268 ASN A CG  1 
ATOM   2053 O  OD1 . ASN A 1 268 ? 51.082 22.636  55.695 1.00 30.92  ? 268 ASN A OD1 1 
ATOM   2054 N  ND2 . ASN A 1 268 ? 49.299 23.983  55.500 1.00 34.73  ? 268 ASN A ND2 1 
ATOM   2055 N  N   . ALA A 1 269 ? 52.820 21.284  57.649 1.00 28.59  ? 269 ALA A N   1 
ATOM   2056 C  CA  . ALA A 1 269 ? 54.172 20.978  57.182 1.00 31.63  ? 269 ALA A CA  1 
ATOM   2057 C  C   . ALA A 1 269 ? 54.650 21.910  56.064 1.00 36.32  ? 269 ALA A C   1 
ATOM   2058 O  O   . ALA A 1 269 ? 55.868 22.065  55.891 1.00 32.03  ? 269 ALA A O   1 
ATOM   2059 C  CB  . ALA A 1 269 ? 54.259 19.529  56.704 1.00 31.52  ? 269 ALA A CB  1 
ATOM   2060 N  N   . ALA A 1 270 ? 53.742 22.541  55.300 1.00 34.74  ? 270 ALA A N   1 
ATOM   2061 C  CA  . ALA A 1 270 ? 54.161 23.436  54.222 1.00 31.94  ? 270 ALA A CA  1 
ATOM   2062 C  C   . ALA A 1 270 ? 54.231 24.899  54.661 1.00 29.56  ? 270 ALA A C   1 
ATOM   2063 O  O   . ALA A 1 270 ? 54.364 25.794  53.816 1.00 28.23  ? 270 ALA A O   1 
ATOM   2064 C  CB  . ALA A 1 270 ? 53.227 23.285  53.012 1.00 33.60  ? 270 ALA A CB  1 
ATOM   2065 N  N   . SER A 1 271 ? 54.156 25.163  55.960 1.00 30.65  ? 271 SER A N   1 
ATOM   2066 C  CA  . SER A 1 271 ? 54.076 26.540  56.445 1.00 28.80  ? 271 SER A CA  1 
ATOM   2067 C  C   . SER A 1 271 ? 55.463 27.180  56.469 1.00 32.13  ? 271 SER A C   1 
ATOM   2068 O  O   . SER A 1 271 ? 56.417 26.578  56.966 1.00 30.05  ? 271 SER A O   1 
ATOM   2069 C  CB  . SER A 1 271 ? 53.470 26.541  57.856 1.00 28.73  ? 271 SER A CB  1 
ATOM   2070 O  OG  . SER A 1 271 ? 53.530 27.823  58.467 1.00 29.26  ? 271 SER A OG  1 
ATOM   2071 N  N   . PRO A 1 272 ? 55.607 28.429  55.987 1.00 31.78  ? 272 PRO A N   1 
ATOM   2072 C  CA  . PRO A 1 272 ? 56.800 29.226  56.284 1.00 30.74  ? 272 PRO A CA  1 
ATOM   2073 C  C   . PRO A 1 272 ? 56.714 29.993  57.593 1.00 29.67  ? 272 PRO A C   1 
ATOM   2074 O  O   . PRO A 1 272 ? 57.541 30.886  57.815 1.00 25.37  ? 272 PRO A O   1 
ATOM   2075 C  CB  . PRO A 1 272 ? 56.823 30.218  55.110 1.00 31.46  ? 272 PRO A CB  1 
ATOM   2076 C  CG  . PRO A 1 272 ? 55.327 30.490  54.875 1.00 32.83  ? 272 PRO A CG  1 
ATOM   2077 C  CD  . PRO A 1 272 ? 54.549 29.272  55.413 1.00 32.38  ? 272 PRO A CD  1 
ATOM   2078 N  N   . ASN A 1 273 ? 55.714 29.693  58.438 1.00 30.07  ? 273 ASN A N   1 
ATOM   2079 C  CA  . ASN A 1 273 ? 55.559 30.376  59.708 1.00 30.07  ? 273 ASN A CA  1 
ATOM   2080 C  C   . ASN A 1 273 ? 55.622 29.415  60.887 1.00 29.44  ? 273 ASN A C   1 
ATOM   2081 O  O   . ASN A 1 273 ? 54.936 29.626  61.900 1.00 26.67  ? 273 ASN A O   1 
ATOM   2082 C  CB  . ASN A 1 273 ? 54.253 31.163  59.714 1.00 35.11  ? 273 ASN A CB  1 
ATOM   2083 C  CG  . ASN A 1 273 ? 54.144 32.079  58.535 1.00 33.35  ? 273 ASN A CG  1 
ATOM   2084 O  OD1 . ASN A 1 273 ? 54.855 33.076  58.466 1.00 35.29  ? 273 ASN A OD1 1 
ATOM   2085 N  ND2 . ASN A 1 273 ? 53.256 31.747  57.579 1.00 31.72  ? 273 ASN A ND2 1 
ATOM   2086 N  N   . LYS A 1 274 ? 56.449 28.365  60.778 1.00 30.68  ? 274 LYS A N   1 
ATOM   2087 C  CA  . LYS A 1 274 ? 56.445 27.323  61.804 1.00 30.35  ? 274 LYS A CA  1 
ATOM   2088 C  C   . LYS A 1 274 ? 56.943 27.836  63.155 1.00 30.76  ? 274 LYS A C   1 
ATOM   2089 O  O   . LYS A 1 274 ? 56.433 27.400  64.197 1.00 25.50  ? 274 LYS A O   1 
ATOM   2090 C  CB  . LYS A 1 274 ? 57.273 26.123  61.350 1.00 33.85  ? 274 LYS A CB  1 
ATOM   2091 C  CG  . LYS A 1 274 ? 56.669 25.349  60.184 1.00 34.94  ? 274 LYS A CG  1 
ATOM   2092 C  CD  . LYS A 1 274 ? 57.276 23.957  60.069 1.00 33.62  ? 274 LYS A CD  1 
ATOM   2093 C  CE  . LYS A 1 274 ? 56.866 23.270  58.766 1.00 37.01  ? 274 LYS A CE  1 
ATOM   2094 N  NZ  . LYS A 1 274 ? 57.232 24.107  57.558 1.00 39.53  ? 274 LYS A NZ  1 
ATOM   2095 N  N   . GLU A 1 275 ? 57.914 28.766  63.166 1.00 34.21  ? 275 GLU A N   1 
ATOM   2096 C  CA  . GLU A 1 275 ? 58.450 29.272  64.436 1.00 34.10  ? 275 GLU A CA  1 
ATOM   2097 C  C   . GLU A 1 275 ? 57.445 30.200  65.127 1.00 34.23  ? 275 GLU A C   1 
ATOM   2098 O  O   . GLU A 1 275 ? 57.192 30.078  66.332 1.00 38.04  ? 275 GLU A O   1 
ATOM   2099 C  CB  . GLU A 1 275 ? 59.785 29.988  64.200 1.00 34.34  ? 275 GLU A CB  1 
ATOM   2100 C  CG  . GLU A 1 275 ? 60.410 30.562  65.475 1.00 37.67  ? 275 GLU A CG  1 
ATOM   2101 C  CD  . GLU A 1 275 ? 60.818 29.487  66.478 1.00 41.65  ? 275 GLU A CD  1 
ATOM   2102 O  OE1 . GLU A 1 275 ? 61.365 28.441  66.053 1.00 40.62  ? 275 GLU A OE1 1 
ATOM   2103 O  OE2 . GLU A 1 275 ? 60.600 29.689  67.694 1.00 40.81  ? 275 GLU A OE2 1 
ATOM   2104 N  N   . LEU A 1 276 ? 56.840 31.116  64.362 1.00 33.42  ? 276 LEU A N   1 
ATOM   2105 C  CA  . LEU A 1 276 ? 55.763 31.949  64.894 1.00 37.62  ? 276 LEU A CA  1 
ATOM   2106 C  C   . LEU A 1 276 ? 54.588 31.113  65.393 1.00 35.00  ? 276 LEU A C   1 
ATOM   2107 O  O   . LEU A 1 276 ? 53.961 31.457  66.403 1.00 35.60  ? 276 LEU A O   1 
ATOM   2108 C  CB  . LEU A 1 276 ? 55.293 32.940  63.831 1.00 39.75  ? 276 LEU A CB  1 
ATOM   2109 C  CG  . LEU A 1 276 ? 56.252 34.138  63.719 1.00 47.01  ? 276 LEU A CG  1 
ATOM   2110 C  CD1 . LEU A 1 276 ? 55.976 34.970  62.473 1.00 46.13  ? 276 LEU A CD1 1 
ATOM   2111 C  CD2 . LEU A 1 276 ? 56.234 34.994  64.999 1.00 42.30  ? 276 LEU A CD2 1 
ATOM   2112 N  N   . ALA A 1 277 ? 54.259 30.021  64.695 1.00 35.87  ? 277 ALA A N   1 
ATOM   2113 C  CA  . ALA A 1 277 ? 53.145 29.179  65.136 1.00 34.45  ? 277 ALA A CA  1 
ATOM   2114 C  C   . ALA A 1 277 ? 53.456 28.548  66.487 1.00 35.66  ? 277 ALA A C   1 
ATOM   2115 O  O   . ALA A 1 277 ? 52.613 28.528  67.392 1.00 31.93  ? 277 ALA A O   1 
ATOM   2116 C  CB  . ALA A 1 277 ? 52.843 28.091  64.097 1.00 30.03  ? 277 ALA A CB  1 
ATOM   2117 N  N   . LYS A 1 278 ? 54.672 28.010  66.628 1.00 40.12  ? 278 LYS A N   1 
ATOM   2118 C  CA  . LYS A 1 278 ? 55.109 27.478  67.909 1.00 37.58  ? 278 LYS A CA  1 
ATOM   2119 C  C   . LYS A 1 278 ? 55.004 28.542  68.996 1.00 36.38  ? 278 LYS A C   1 
ATOM   2120 O  O   . LYS A 1 278 ? 54.467 28.290  70.081 1.00 36.89  ? 278 LYS A O   1 
ATOM   2121 C  CB  . LYS A 1 278 ? 56.539 26.949  67.771 1.00 43.33  ? 278 LYS A CB  1 
ATOM   2122 C  CG  . LYS A 1 278 ? 57.166 26.470  69.080 1.00 45.79  ? 278 LYS A CG  1 
ATOM   2123 C  CD  . LYS A 1 278 ? 58.612 26.031  68.895 1.00 47.05  ? 278 LYS A CD  1 
ATOM   2124 C  CE  . LYS A 1 278 ? 59.341 26.044  70.238 1.00 45.08  ? 278 LYS A CE  1 
ATOM   2125 N  NZ  . LYS A 1 278 ? 60.584 25.241  70.218 1.00 47.44  ? 278 LYS A NZ  1 
ATOM   2126 N  N   . GLU A 1 279 ? 55.482 29.755  68.701 1.00 38.05  ? 279 GLU A N   1 
ATOM   2127 C  CA  . GLU A 1 279 ? 55.442 30.839  69.679 1.00 39.54  ? 279 GLU A CA  1 
ATOM   2128 C  C   . GLU A 1 279 ? 54.008 31.200  70.037 1.00 37.49  ? 279 GLU A C   1 
ATOM   2129 O  O   . GLU A 1 279 ? 53.688 31.434  71.208 1.00 33.71  ? 279 GLU A O   1 
ATOM   2130 C  CB  . GLU A 1 279 ? 56.166 32.069  69.133 1.00 42.48  ? 279 GLU A CB  1 
ATOM   2131 C  CG  . GLU A 1 279 ? 57.546 32.276  69.735 1.00 50.09  ? 279 GLU A CG  1 
ATOM   2132 C  CD  . GLU A 1 279 ? 58.527 32.930  68.766 1.00 52.09  ? 279 GLU A CD  1 
ATOM   2133 O  OE1 . GLU A 1 279 ? 58.121 33.861  68.036 1.00 54.22  ? 279 GLU A OE1 1 
ATOM   2134 O  OE2 . GLU A 1 279 ? 59.703 32.507  68.740 1.00 52.84  ? 279 GLU A OE2 1 
ATOM   2135 N  N   . PHE A 1 280 ? 53.127 31.265  69.052 1.00 29.55  ? 280 PHE A N   1 
ATOM   2136 C  CA  . PHE A 1 280 ? 51.748 31.601  69.381 1.00 32.68  ? 280 PHE A CA  1 
ATOM   2137 C  C   . PHE A 1 280 ? 51.104 30.524  70.257 1.00 34.97  ? 280 PHE A C   1 
ATOM   2138 O  O   . PHE A 1 280 ? 50.439 30.834  71.249 1.00 42.51  ? 280 PHE A O   1 
ATOM   2139 C  CB  . PHE A 1 280 ? 50.927 31.822  68.116 1.00 29.72  ? 280 PHE A CB  1 
ATOM   2140 C  CG  . PHE A 1 280 ? 49.476 31.967  68.402 1.00 36.10  ? 280 PHE A CG  1 
ATOM   2141 C  CD1 . PHE A 1 280 ? 48.973 33.186  68.822 1.00 36.91  ? 280 PHE A CD1 1 
ATOM   2142 C  CD2 . PHE A 1 280 ? 48.619 30.867  68.327 1.00 34.72  ? 280 PHE A CD2 1 
ATOM   2143 C  CE1 . PHE A 1 280 ? 47.627 33.322  69.118 1.00 41.95  ? 280 PHE A CE1 1 
ATOM   2144 C  CE2 . PHE A 1 280 ? 47.288 30.996  68.626 1.00 37.35  ? 280 PHE A CE2 1 
ATOM   2145 C  CZ  . PHE A 1 280 ? 46.781 32.222  69.021 1.00 37.12  ? 280 PHE A CZ  1 
ATOM   2146 N  N   . LEU A 1 281 ? 51.284 29.253  69.895 1.00 34.30  ? 281 LEU A N   1 
ATOM   2147 C  CA  . LEU A 1 281 ? 50.618 28.161  70.597 1.00 31.57  ? 281 LEU A CA  1 
ATOM   2148 C  C   . LEU A 1 281 ? 51.161 27.991  72.018 1.00 34.63  ? 281 LEU A C   1 
ATOM   2149 O  O   . LEU A 1 281 ? 50.389 27.840  72.970 1.00 38.82  ? 281 LEU A O   1 
ATOM   2150 C  CB  . LEU A 1 281 ? 50.784 26.868  69.794 1.00 30.21  ? 281 LEU A CB  1 
ATOM   2151 C  CG  . LEU A 1 281 ? 49.961 26.789  68.487 1.00 30.42  ? 281 LEU A CG  1 
ATOM   2152 C  CD1 . LEU A 1 281 ? 50.193 25.435  67.786 1.00 34.13  ? 281 LEU A CD1 1 
ATOM   2153 C  CD2 . LEU A 1 281 ? 48.461 27.005  68.782 1.00 30.65  ? 281 LEU A CD2 1 
ATOM   2154 N  N   . GLU A 1 282 ? 52.488 27.921  72.167 1.00 34.84  ? 282 GLU A N   1 
ATOM   2155 C  CA  . GLU A 1 282 ? 53.109 27.912  73.488 1.00 36.50  ? 282 GLU A CA  1 
ATOM   2156 C  C   . GLU A 1 282 ? 53.144 29.338  73.991 1.00 39.07  ? 282 GLU A C   1 
ATOM   2157 O  O   . GLU A 1 282 ? 53.395 30.258  73.228 1.00 46.27  ? 282 GLU A O   1 
ATOM   2158 C  CB  . GLU A 1 282 ? 54.535 27.354  73.435 1.00 31.89  ? 282 GLU A CB  1 
ATOM   2159 C  CG  . GLU A 1 282 ? 54.639 25.947  72.943 1.00 32.20  ? 282 GLU A CG  1 
ATOM   2160 C  CD  . GLU A 1 282 ? 56.046 25.528  72.562 1.00 34.38  ? 282 GLU A CD  1 
ATOM   2161 O  OE1 . GLU A 1 282 ? 56.975 26.335  72.668 1.00 38.05  ? 282 GLU A OE1 1 
ATOM   2162 O  OE2 . GLU A 1 282 ? 56.244 24.373  72.144 1.00 38.19  ? 282 GLU A OE2 1 
ATOM   2163 N  N   . ASN A 1 283 ? 52.818 29.537  75.242 1.00 49.01  ? 283 ASN A N   1 
ATOM   2164 C  CA  . ASN A 1 283 ? 52.942 30.833  75.919 1.00 53.63  ? 283 ASN A CA  1 
ATOM   2165 C  C   . ASN A 1 283 ? 52.090 31.984  75.323 1.00 46.08  ? 283 ASN A C   1 
ATOM   2166 O  O   . ASN A 1 283 ? 52.166 33.108  75.831 1.00 43.71  ? 283 ASN A O   1 
ATOM   2167 C  CB  . ASN A 1 283 ? 54.423 31.256  76.066 1.00 55.59  ? 283 ASN A CB  1 
ATOM   2168 C  CG  . ASN A 1 283 ? 55.079 31.640  74.757 1.00 51.37  ? 283 ASN A CG  1 
ATOM   2169 O  OD1 . ASN A 1 283 ? 54.551 32.459  74.012 1.00 55.26  ? 283 ASN A OD1 1 
ATOM   2170 N  ND2 . ASN A 1 283 ? 56.234 31.033  74.463 1.00 43.01  ? 283 ASN A ND2 1 
ATOM   2171 N  N   . TYR A 1 284 ? 51.221 31.747  74.323 1.00 43.35  ? 284 TYR A N   1 
ATOM   2172 C  CA  . TYR A 1 284 ? 50.013 32.574  74.187 1.00 42.39  ? 284 TYR A CA  1 
ATOM   2173 C  C   . TYR A 1 284 ? 48.743 31.752  74.373 1.00 42.71  ? 284 TYR A C   1 
ATOM   2174 O  O   . TYR A 1 284 ? 47.999 31.983  75.336 1.00 39.92  ? 284 TYR A O   1 
ATOM   2175 C  CB  . TYR A 1 284 ? 49.973 33.342  72.858 1.00 44.48  ? 284 TYR A CB  1 
ATOM   2176 C  CG  . TYR A 1 284 ? 50.751 34.628  72.958 1.00 46.29  ? 284 TYR A CG  1 
ATOM   2177 C  CD1 . TYR A 1 284 ? 52.127 34.632  72.777 1.00 50.59  ? 284 TYR A CD1 1 
ATOM   2178 C  CD2 . TYR A 1 284 ? 50.126 35.822  73.305 1.00 45.55  ? 284 TYR A CD2 1 
ATOM   2179 C  CE1 . TYR A 1 284 ? 52.858 35.789  72.898 1.00 48.29  ? 284 TYR A CE1 1 
ATOM   2180 C  CE2 . TYR A 1 284 ? 50.844 36.991  73.437 1.00 48.92  ? 284 TYR A CE2 1 
ATOM   2181 C  CZ  . TYR A 1 284 ? 52.220 36.969  73.230 1.00 53.29  ? 284 TYR A CZ  1 
ATOM   2182 O  OH  . TYR A 1 284 ? 52.974 38.118  73.360 1.00 45.18  ? 284 TYR A OH  1 
ATOM   2183 N  N   . LEU A 1 285 ? 48.479 30.773  73.503 1.00 44.28  ? 285 LEU A N   1 
ATOM   2184 C  CA  . LEU A 1 285 ? 47.290 29.943  73.673 1.00 41.47  ? 285 LEU A CA  1 
ATOM   2185 C  C   . LEU A 1 285 ? 47.389 29.065  74.915 1.00 38.46  ? 285 LEU A C   1 
ATOM   2186 O  O   . LEU A 1 285 ? 46.520 29.114  75.789 1.00 32.89  ? 285 LEU A O   1 
ATOM   2187 C  CB  . LEU A 1 285 ? 47.067 29.074  72.444 1.00 40.96  ? 285 LEU A CB  1 
ATOM   2188 C  CG  . LEU A 1 285 ? 45.784 28.274  72.617 1.00 40.80  ? 285 LEU A CG  1 
ATOM   2189 C  CD1 . LEU A 1 285 ? 44.606 29.226  72.869 1.00 42.53  ? 285 LEU A CD1 1 
ATOM   2190 C  CD2 . LEU A 1 285 ? 45.555 27.451  71.371 1.00 42.18  ? 285 LEU A CD2 1 
ATOM   2191 N  N   . LEU A 1 286 ? 48.417 28.213  74.986 1.00 33.47  ? 286 LEU A N   1 
ATOM   2192 C  CA  . LEU A 1 286 ? 48.506 27.216  76.054 1.00 39.79  ? 286 LEU A CA  1 
ATOM   2193 C  C   . LEU A 1 286 ? 49.017 27.892  77.328 1.00 42.85  ? 286 LEU A C   1 
ATOM   2194 O  O   . LEU A 1 286 ? 50.124 27.651  77.822 1.00 39.89  ? 286 LEU A O   1 
ATOM   2195 C  CB  . LEU A 1 286 ? 49.374 26.045  75.632 1.00 40.96  ? 286 LEU A CB  1 
ATOM   2196 C  CG  . LEU A 1 286 ? 48.574 25.048  74.794 1.00 40.43  ? 286 LEU A CG  1 
ATOM   2197 C  CD1 . LEU A 1 286 ? 49.482 24.033  74.107 1.00 37.43  ? 286 LEU A CD1 1 
ATOM   2198 C  CD2 . LEU A 1 286 ? 47.524 24.361  75.654 1.00 40.24  ? 286 LEU A CD2 1 
ATOM   2199 N  N   . THR A 1 287 ? 48.168 28.785  77.830 1.00 40.02  ? 287 THR A N   1 
ATOM   2200 C  CA  . THR A 1 287 ? 48.346 29.531  79.067 1.00 41.44  ? 287 THR A CA  1 
ATOM   2201 C  C   . THR A 1 287 ? 46.976 29.688  79.696 1.00 39.76  ? 287 THR A C   1 
ATOM   2202 O  O   . THR A 1 287 ? 45.945 29.535  79.030 1.00 39.86  ? 287 THR A O   1 
ATOM   2203 C  CB  . THR A 1 287 ? 48.958 30.937  78.870 1.00 38.43  ? 287 THR A CB  1 
ATOM   2204 O  OG1 . THR A 1 287 ? 48.045 31.772  78.150 1.00 39.64  ? 287 THR A OG1 1 
ATOM   2205 C  CG2 . THR A 1 287 ? 50.264 30.885  78.124 1.00 42.31  ? 287 THR A CG2 1 
ATOM   2206 N  N   . ASP A 1 288 ? 46.986 29.996  80.992 1.00 37.07  ? 288 ASP A N   1 
ATOM   2207 C  CA  . ASP A 1 288 ? 45.751 30.243  81.726 1.00 41.52  ? 288 ASP A CA  1 
ATOM   2208 C  C   . ASP A 1 288 ? 44.899 31.314  81.046 1.00 43.34  ? 288 ASP A C   1 
ATOM   2209 O  O   . ASP A 1 288 ? 43.686 31.140  80.859 1.00 38.56  ? 288 ASP A O   1 
ATOM   2210 C  CB  . ASP A 1 288 ? 46.085 30.656  83.160 1.00 38.14  ? 288 ASP A CB  1 
ATOM   2211 C  CG  . ASP A 1 288 ? 46.489 29.488  84.017 1.00 36.80  ? 288 ASP A CG  1 
ATOM   2212 O  OD1 . ASP A 1 288 ? 46.665 28.374  83.490 1.00 37.34  ? 288 ASP A OD1 1 
ATOM   2213 O  OD2 . ASP A 1 288 ? 46.634 29.677  85.240 1.00 53.28  ? 288 ASP A OD2 1 
ATOM   2214 N  N   . GLU A 1 289 ? 45.522 32.435  80.667 1.00 38.76  ? 289 GLU A N   1 
ATOM   2215 C  CA  . GLU A 1 289 ? 44.743 33.534  80.113 1.00 39.60  ? 289 GLU A CA  1 
ATOM   2216 C  C   . GLU A 1 289 ? 44.326 33.264  78.670 1.00 37.20  ? 289 GLU A C   1 
ATOM   2217 O  O   . GLU A 1 289 ? 43.255 33.717  78.254 1.00 39.56  ? 289 GLU A O   1 
ATOM   2218 C  CB  . GLU A 1 289 ? 45.522 34.849  80.230 1.00 40.53  ? 289 GLU A CB  1 
ATOM   2219 C  CG  . GLU A 1 289 ? 46.753 34.940  79.362 1.00 52.13  ? 289 GLU A CG  1 
ATOM   2220 C  CD  . GLU A 1 289 ? 48.045 34.633  80.131 1.00 56.40  ? 289 GLU A CD  1 
ATOM   2221 O  OE1 . GLU A 1 289 ? 47.955 34.045  81.238 1.00 55.72  ? 289 GLU A OE1 1 
ATOM   2222 O  OE2 . GLU A 1 289 ? 49.143 34.966  79.614 1.00 60.27  ? 289 GLU A OE2 1 
ATOM   2223 N  N   . GLY A 1 290 ? 45.139 32.529  77.903 1.00 37.59  ? 290 GLY A N   1 
ATOM   2224 C  CA  . GLY A 1 290 ? 44.752 32.193  76.540 1.00 33.20  ? 290 GLY A CA  1 
ATOM   2225 C  C   . GLY A 1 290 ? 43.619 31.181  76.494 1.00 33.34  ? 290 GLY A C   1 
ATOM   2226 O  O   . GLY A 1 290 ? 42.630 31.364  75.772 1.00 33.26  ? 290 GLY A O   1 
ATOM   2227 N  N   . LEU A 1 291 ? 43.732 30.105  77.275 1.00 34.87  ? 291 LEU A N   1 
ATOM   2228 C  CA  . LEU A 1 291 ? 42.648 29.125  77.280 1.00 39.56  ? 291 LEU A CA  1 
ATOM   2229 C  C   . LEU A 1 291 ? 41.382 29.721  77.886 1.00 41.30  ? 291 LEU A C   1 
ATOM   2230 O  O   . LEU A 1 291 ? 40.268 29.331  77.508 1.00 41.37  ? 291 LEU A O   1 
ATOM   2231 C  CB  . LEU A 1 291 ? 43.064 27.848  78.026 1.00 35.88  ? 291 LEU A CB  1 
ATOM   2232 C  CG  . LEU A 1 291 ? 44.130 26.924  77.409 1.00 38.81  ? 291 LEU A CG  1 
ATOM   2233 C  CD1 . LEU A 1 291 ? 44.415 25.754  78.356 1.00 40.03  ? 291 LEU A CD1 1 
ATOM   2234 C  CD2 . LEU A 1 291 ? 43.775 26.402  76.011 1.00 36.22  ? 291 LEU A CD2 1 
ATOM   2235 N  N   . GLU A 1 292 ? 41.535 30.697  78.784 1.00 41.66  ? 292 GLU A N   1 
ATOM   2236 C  CA  . GLU A 1 292 ? 40.372 31.365  79.346 1.00 44.17  ? 292 GLU A CA  1 
ATOM   2237 C  C   . GLU A 1 292 ? 39.638 32.178  78.288 1.00 35.98  ? 292 GLU A C   1 
ATOM   2238 O  O   . GLU A 1 292 ? 38.412 32.151  78.240 1.00 33.37  ? 292 GLU A O   1 
ATOM   2239 C  CB  . GLU A 1 292 ? 40.778 32.250  80.528 1.00 48.16  ? 292 GLU A CB  1 
ATOM   2240 C  CG  . GLU A 1 292 ? 39.625 33.078  81.106 1.00 58.79  ? 292 GLU A CG  1 
ATOM   2241 C  CD  . GLU A 1 292 ? 39.998 33.820  82.394 1.00 64.99  ? 292 GLU A CD  1 
ATOM   2242 O  OE1 . GLU A 1 292 ? 40.613 34.913  82.323 1.00 68.06  ? 292 GLU A OE1 1 
ATOM   2243 O  OE2 . GLU A 1 292 ? 39.685 33.290  83.482 1.00 73.06  ? 292 GLU A OE2 1 
ATOM   2244 N  N   . ALA A 1 293 ? 40.360 32.922  77.443 1.00 40.41  ? 293 ALA A N   1 
ATOM   2245 C  CA  . ALA A 1 293 ? 39.677 33.718  76.422 1.00 39.50  ? 293 ALA A CA  1 
ATOM   2246 C  C   . ALA A 1 293 ? 38.872 32.826  75.486 1.00 35.13  ? 293 ALA A C   1 
ATOM   2247 O  O   . ALA A 1 293 ? 37.744 33.163  75.117 1.00 38.25  ? 293 ALA A O   1 
ATOM   2248 C  CB  . ALA A 1 293 ? 40.678 34.562  75.637 1.00 41.57  ? 293 ALA A CB  1 
ATOM   2249 N  N   . VAL A 1 294 ? 39.416 31.656  75.142 1.00 34.79  ? 294 VAL A N   1 
ATOM   2250 C  CA  . VAL A 1 294 ? 38.689 30.676  74.334 1.00 38.16  ? 294 VAL A CA  1 
ATOM   2251 C  C   . VAL A 1 294 ? 37.486 30.121  75.095 1.00 36.81  ? 294 VAL A C   1 
ATOM   2252 O  O   . VAL A 1 294 ? 36.361 30.085  74.581 1.00 36.55  ? 294 VAL A O   1 
ATOM   2253 C  CB  . VAL A 1 294 ? 39.645 29.552  73.893 1.00 40.65  ? 294 VAL A CB  1 
ATOM   2254 C  CG1 . VAL A 1 294 ? 38.907 28.545  73.016 1.00 40.55  ? 294 VAL A CG1 1 
ATOM   2255 C  CG2 . VAL A 1 294 ? 40.879 30.150  73.175 1.00 39.37  ? 294 VAL A CG2 1 
ATOM   2256 N  N   . ASN A 1 295 ? 37.708 29.678  76.330 1.00 36.28  ? 295 ASN A N   1 
ATOM   2257 C  CA  . ASN A 1 295 ? 36.641 29.115  77.145 1.00 37.68  ? 295 ASN A CA  1 
ATOM   2258 C  C   . ASN A 1 295 ? 35.504 30.105  77.366 1.00 34.02  ? 295 ASN A C   1 
ATOM   2259 O  O   . ASN A 1 295 ? 34.342 29.696  77.462 1.00 39.61  ? 295 ASN A O   1 
ATOM   2260 C  CB  . ASN A 1 295 ? 37.226 28.661  78.485 1.00 37.78  ? 295 ASN A CB  1 
ATOM   2261 C  CG  . ASN A 1 295 ? 36.301 27.775  79.243 1.00 35.28  ? 295 ASN A CG  1 
ATOM   2262 O  OD1 . ASN A 1 295 ? 36.110 26.609  78.906 1.00 35.93  ? 295 ASN A OD1 1 
ATOM   2263 N  ND2 . ASN A 1 295 ? 35.725 28.312  80.287 1.00 35.12  ? 295 ASN A ND2 1 
ATOM   2264 N  N   . LYS A 1 296 ? 35.807 31.404  77.455 1.00 29.84  ? 296 LYS A N   1 
ATOM   2265 C  CA  . LYS A 1 296 ? 34.747 32.374  77.689 1.00 33.09  ? 296 LYS A CA  1 
ATOM   2266 C  C   . LYS A 1 296 ? 33.873 32.551  76.451 1.00 33.35  ? 296 LYS A C   1 
ATOM   2267 O  O   . LYS A 1 296 ? 32.705 32.939  76.569 1.00 34.05  ? 296 LYS A O   1 
ATOM   2268 C  CB  . LYS A 1 296 ? 35.340 33.716  78.133 1.00 37.13  ? 296 LYS A CB  1 
ATOM   2269 N  N   . ASP A 1 297 ? 34.414 32.285  75.263 1.00 34.34  ? 297 ASP A N   1 
ATOM   2270 C  CA  . ASP A 1 297 ? 33.594 32.328  74.050 1.00 32.32  ? 297 ASP A CA  1 
ATOM   2271 C  C   . ASP A 1 297 ? 32.702 31.085  73.948 1.00 38.66  ? 297 ASP A C   1 
ATOM   2272 O  O   . ASP A 1 297 ? 31.474 31.192  73.869 1.00 34.07  ? 297 ASP A O   1 
ATOM   2273 C  CB  . ASP A 1 297 ? 34.506 32.485  72.832 1.00 34.64  ? 297 ASP A CB  1 
ATOM   2274 C  CG  . ASP A 1 297 ? 33.736 32.632  71.520 1.00 36.43  ? 297 ASP A CG  1 
ATOM   2275 O  OD1 . ASP A 1 297 ? 32.559 33.054  71.527 1.00 41.81  ? 297 ASP A OD1 1 
ATOM   2276 O  OD2 . ASP A 1 297 ? 34.324 32.320  70.470 1.00 35.98  ? 297 ASP A OD2 1 
ATOM   2277 N  N   . LYS A 1 298 ? 33.299 29.887  73.967 1.00 40.21  ? 298 LYS A N   1 
ATOM   2278 C  CA  . LYS A 1 298 ? 32.533 28.641  74.100 1.00 43.04  ? 298 LYS A CA  1 
ATOM   2279 C  C   . LYS A 1 298 ? 33.359 27.698  74.969 1.00 41.63  ? 298 LYS A C   1 
ATOM   2280 O  O   . LYS A 1 298 ? 34.582 27.590  74.773 1.00 41.72  ? 298 LYS A O   1 
ATOM   2281 C  CB  . LYS A 1 298 ? 32.204 27.969  72.748 1.00 43.92  ? 298 LYS A CB  1 
ATOM   2282 C  CG  . LYS A 1 298 ? 31.208 28.739  71.844 1.00 47.25  ? 298 LYS A CG  1 
ATOM   2283 C  CD  . LYS A 1 298 ? 29.752 28.344  72.118 1.00 50.41  ? 298 LYS A CD  1 
ATOM   2284 C  CE  . LYS A 1 298 ? 28.753 29.333  71.524 1.00 53.37  ? 298 LYS A CE  1 
ATOM   2285 N  NZ  . LYS A 1 298 ? 27.548 29.624  72.389 1.00 55.16  ? 298 LYS A NZ  1 
ATOM   2286 N  N   . PRO A 1 299 ? 32.729 27.018  75.936 1.00 42.59  ? 299 PRO A N   1 
ATOM   2287 C  CA  . PRO A 1 299 ? 33.494 26.214  76.911 1.00 43.58  ? 299 PRO A CA  1 
ATOM   2288 C  C   . PRO A 1 299 ? 34.253 25.060  76.265 1.00 38.57  ? 299 PRO A C   1 
ATOM   2289 O  O   . PRO A 1 299 ? 33.730 24.358  75.397 1.00 36.15  ? 299 PRO A O   1 
ATOM   2290 C  CB  . PRO A 1 299 ? 32.422 25.693  77.876 1.00 41.88  ? 299 PRO A CB  1 
ATOM   2291 C  CG  . PRO A 1 299 ? 31.083 26.090  77.289 1.00 43.67  ? 299 PRO A CG  1 
ATOM   2292 C  CD  . PRO A 1 299 ? 31.307 27.163  76.292 1.00 42.41  ? 299 PRO A CD  1 
ATOM   2293 N  N   . LEU A 1 300 ? 35.501 24.864  76.713 1.00 34.46  ? 300 LEU A N   1 
ATOM   2294 C  CA  . LEU A 1 300 ? 36.385 23.809  76.217 1.00 39.06  ? 300 LEU A CA  1 
ATOM   2295 C  C   . LEU A 1 300 ? 36.144 22.448  76.863 1.00 38.21  ? 300 LEU A C   1 
ATOM   2296 O  O   . LEU A 1 300 ? 36.700 21.449  76.375 1.00 33.62  ? 300 LEU A O   1 
ATOM   2297 C  CB  . LEU A 1 300 ? 37.853 24.187  76.453 1.00 40.81  ? 300 LEU A CB  1 
ATOM   2298 C  CG  . LEU A 1 300 ? 38.444 25.266  75.543 1.00 38.90  ? 300 LEU A CG  1 
ATOM   2299 C  CD1 . LEU A 1 300 ? 39.652 25.939  76.188 1.00 41.86  ? 300 LEU A CD1 1 
ATOM   2300 C  CD2 . LEU A 1 300 ? 38.802 24.682  74.169 1.00 36.67  ? 300 LEU A CD2 1 
ATOM   2301 N  N   . GLY A 1 301 ? 35.358 22.380  77.944 1.00 33.60  ? 301 GLY A N   1 
ATOM   2302 C  CA  . GLY A 1 301 ? 35.289 21.170  78.734 1.00 31.28  ? 301 GLY A CA  1 
ATOM   2303 C  C   . GLY A 1 301 ? 36.507 21.082  79.633 1.00 33.79  ? 301 GLY A C   1 
ATOM   2304 O  O   . GLY A 1 301 ? 36.904 22.080  80.241 1.00 38.21  ? 301 GLY A O   1 
ATOM   2305 N  N   . ALA A 1 302 ? 37.108 19.899  79.734 1.00 31.26  ? 302 ALA A N   1 
ATOM   2306 C  CA  . ALA A 1 302 ? 38.379 19.734  80.426 1.00 33.13  ? 302 ALA A CA  1 
ATOM   2307 C  C   . ALA A 1 302 ? 39.540 20.065  79.489 1.00 31.39  ? 302 ALA A C   1 
ATOM   2308 O  O   . ALA A 1 302 ? 39.475 19.819  78.275 1.00 31.23  ? 302 ALA A O   1 
ATOM   2309 C  CB  . ALA A 1 302 ? 38.515 18.298  80.949 1.00 36.91  ? 302 ALA A CB  1 
ATOM   2310 N  N   . VAL A 1 303 ? 40.607 20.622  80.053 1.00 33.05  ? 303 VAL A N   1 
ATOM   2311 C  CA  . VAL A 1 303 ? 41.752 21.072  79.270 1.00 36.17  ? 303 VAL A CA  1 
ATOM   2312 C  C   . VAL A 1 303 ? 42.995 20.250  79.587 1.00 34.55  ? 303 VAL A C   1 
ATOM   2313 O  O   . VAL A 1 303 ? 43.132 19.652  80.662 1.00 34.32  ? 303 VAL A O   1 
ATOM   2314 C  CB  . VAL A 1 303 ? 42.041 22.565  79.497 1.00 37.76  ? 303 VAL A CB  1 
ATOM   2315 C  CG1 . VAL A 1 303 ? 40.856 23.406  79.042 1.00 38.36  ? 303 VAL A CG1 1 
ATOM   2316 C  CG2 . VAL A 1 303 ? 42.380 22.813  80.960 1.00 37.06  ? 303 VAL A CG2 1 
ATOM   2317 N  N   . ALA A 1 304 ? 43.936 20.259  78.635 1.00 34.73  ? 304 ALA A N   1 
ATOM   2318 C  CA  . ALA A 1 304 ? 45.192 19.534  78.819 1.00 39.42  ? 304 ALA A CA  1 
ATOM   2319 C  C   . ALA A 1 304 ? 46.139 20.244  79.793 1.00 39.18  ? 304 ALA A C   1 
ATOM   2320 O  O   . ALA A 1 304 ? 46.933 19.583  80.467 1.00 45.30  ? 304 ALA A O   1 
ATOM   2321 C  CB  . ALA A 1 304 ? 45.882 19.332  77.468 1.00 42.29  ? 304 ALA A CB  1 
ATOM   2322 N  N   . LEU A 1 305 ? 46.072 21.573  79.871 1.00 36.56  ? 305 LEU A N   1 
ATOM   2323 C  CA  . LEU A 1 305 ? 46.940 22.377  80.724 1.00 36.25  ? 305 LEU A CA  1 
ATOM   2324 C  C   . LEU A 1 305 ? 46.550 22.208  82.194 1.00 37.71  ? 305 LEU A C   1 
ATOM   2325 O  O   . LEU A 1 305 ? 45.471 22.647  82.612 1.00 36.02  ? 305 LEU A O   1 
ATOM   2326 C  CB  . LEU A 1 305 ? 46.838 23.835  80.300 1.00 36.15  ? 305 LEU A CB  1 
ATOM   2327 C  CG  . LEU A 1 305 ? 47.792 24.790  81.003 1.00 36.17  ? 305 LEU A CG  1 
ATOM   2328 C  CD1 . LEU A 1 305 ? 49.218 24.500  80.571 1.00 35.72  ? 305 LEU A CD1 1 
ATOM   2329 C  CD2 . LEU A 1 305 ? 47.386 26.249  80.750 1.00 35.53  ? 305 LEU A CD2 1 
ATOM   2330 N  N   . LYS A 1 306 ? 47.441 21.590  82.976 1.00 37.37  ? 306 LYS A N   1 
ATOM   2331 C  CA  . LYS A 1 306 ? 47.160 21.275  84.381 1.00 40.64  ? 306 LYS A CA  1 
ATOM   2332 C  C   . LYS A 1 306 ? 46.595 22.466  85.125 1.00 41.34  ? 306 LYS A C   1 
ATOM   2333 O  O   . LYS A 1 306 ? 45.545 22.375  85.764 1.00 43.43  ? 306 LYS A O   1 
ATOM   2334 C  CB  . LYS A 1 306 ? 48.435 20.811  85.091 1.00 42.09  ? 306 LYS A CB  1 
ATOM   2335 C  CG  . LYS A 1 306 ? 49.006 19.483  84.631 1.00 51.84  ? 306 LYS A CG  1 
ATOM   2336 C  CD  . LYS A 1 306 ? 49.838 18.866  85.745 1.00 56.37  ? 306 LYS A CD  1 
ATOM   2337 C  CE  . LYS A 1 306 ? 51.318 18.907  85.457 1.00 57.69  ? 306 LYS A CE  1 
ATOM   2338 N  NZ  . LYS A 1 306 ? 51.807 17.616  84.900 1.00 62.45  ? 306 LYS A NZ  1 
ATOM   2339 N  N   . SER A 1 307 ? 47.293 23.598  85.046 1.00 48.69  ? 307 SER A N   1 
ATOM   2340 C  CA  . SER A 1 307 ? 46.997 24.724  85.915 1.00 45.77  ? 307 SER A CA  1 
ATOM   2341 C  C   . SER A 1 307 ? 45.570 25.204  85.722 1.00 49.25  ? 307 SER A C   1 
ATOM   2342 O  O   . SER A 1 307 ? 44.881 25.538  86.697 1.00 43.05  ? 307 SER A O   1 
ATOM   2343 C  CB  . SER A 1 307 ? 48.002 25.845  85.652 1.00 47.73  ? 307 SER A CB  1 
ATOM   2344 O  OG  . SER A 1 307 ? 47.853 26.346  84.337 1.00 61.81  ? 307 SER A OG  1 
ATOM   2345 N  N   . TYR A 1 308 ? 45.095 25.225  84.471 1.00 40.00  ? 308 TYR A N   1 
ATOM   2346 C  CA  . TYR A 1 308 ? 43.766 25.751  84.222 1.00 39.40  ? 308 TYR A CA  1 
ATOM   2347 C  C   . TYR A 1 308 ? 42.696 24.681  84.408 1.00 37.44  ? 308 TYR A C   1 
ATOM   2348 O  O   . TYR A 1 308 ? 41.582 24.996  84.843 1.00 39.89  ? 308 TYR A O   1 
ATOM   2349 C  CB  . TYR A 1 308 ? 43.717 26.380  82.824 1.00 38.94  ? 308 TYR A CB  1 
ATOM   2350 C  CG  . TYR A 1 308 ? 42.429 27.099  82.485 1.00 38.62  ? 308 TYR A CG  1 
ATOM   2351 C  CD1 . TYR A 1 308 ? 41.820 27.981  83.390 1.00 41.83  ? 308 TYR A CD1 1 
ATOM   2352 C  CD2 . TYR A 1 308 ? 41.814 26.896  81.249 1.00 38.55  ? 308 TYR A CD2 1 
ATOM   2353 C  CE1 . TYR A 1 308 ? 40.615 28.653  83.059 1.00 36.03  ? 308 TYR A CE1 1 
ATOM   2354 C  CE2 . TYR A 1 308 ? 40.621 27.544  80.915 1.00 39.51  ? 308 TYR A CE2 1 
ATOM   2355 C  CZ  . TYR A 1 308 ? 40.026 28.425  81.813 1.00 36.85  ? 308 TYR A CZ  1 
ATOM   2356 O  OH  . TYR A 1 308 ? 38.842 29.053  81.436 1.00 34.11  ? 308 TYR A OH  1 
ATOM   2357 N  N   . GLU A 1 309 ? 43.024 23.420  84.140 1.00 36.41  ? 309 GLU A N   1 
ATOM   2358 C  CA  . GLU A 1 309 ? 42.103 22.331  84.459 1.00 36.19  ? 309 GLU A CA  1 
ATOM   2359 C  C   . GLU A 1 309 ? 41.740 22.331  85.939 1.00 38.65  ? 309 GLU A C   1 
ATOM   2360 O  O   . GLU A 1 309 ? 40.568 22.166  86.301 1.00 42.25  ? 309 GLU A O   1 
ATOM   2361 C  CB  . GLU A 1 309 ? 42.720 20.990  84.059 1.00 34.00  ? 309 GLU A CB  1 
ATOM   2362 C  CG  . GLU A 1 309 ? 41.966 19.751  84.542 1.00 35.21  ? 309 GLU A CG  1 
ATOM   2363 C  CD  . GLU A 1 309 ? 40.565 19.621  83.936 1.00 35.95  ? 309 GLU A CD  1 
ATOM   2364 O  OE1 . GLU A 1 309 ? 40.175 20.477  83.085 1.00 37.25  ? 309 GLU A OE1 1 
ATOM   2365 O  OE2 . GLU A 1 309 ? 39.853 18.657  84.300 1.00 34.16  ? 309 GLU A OE2 1 
ATOM   2366 N  N   . GLU A 1 310 ? 42.734 22.526  86.809 1.00 41.83  ? 310 GLU A N   1 
ATOM   2367 C  CA  . GLU A 1 310 ? 42.468 22.504  88.244 1.00 46.62  ? 310 GLU A CA  1 
ATOM   2368 C  C   . GLU A 1 310 ? 41.497 23.597  88.645 1.00 41.99  ? 310 GLU A C   1 
ATOM   2369 O  O   . GLU A 1 310 ? 40.694 23.399  89.557 1.00 45.13  ? 310 GLU A O   1 
ATOM   2370 C  CB  . GLU A 1 310 ? 43.774 22.631  89.016 1.00 53.58  ? 310 GLU A CB  1 
ATOM   2371 C  CG  . GLU A 1 310 ? 44.723 21.482  88.745 1.00 56.93  ? 310 GLU A CG  1 
ATOM   2372 C  CD  . GLU A 1 310 ? 46.088 21.750  89.289 1.00 53.97  ? 310 GLU A CD  1 
ATOM   2373 O  OE1 . GLU A 1 310 ? 46.211 22.678  90.108 1.00 67.27  ? 310 GLU A OE1 1 
ATOM   2374 O  OE2 . GLU A 1 310 ? 47.036 21.050  88.891 1.00 56.66  ? 310 GLU A OE2 1 
ATOM   2375 N  N   . GLU A 1 311 ? 41.546 24.742  87.963 1.00 38.73  ? 311 GLU A N   1 
ATOM   2376 C  CA  . GLU A 1 311 ? 40.530 25.771  88.137 1.00 40.87  ? 311 GLU A CA  1 
ATOM   2377 C  C   . GLU A 1 311 ? 39.177 25.311  87.599 1.00 41.54  ? 311 GLU A C   1 
ATOM   2378 O  O   . GLU A 1 311 ? 38.155 25.402  88.292 1.00 40.00  ? 311 GLU A O   1 
ATOM   2379 C  CB  . GLU A 1 311 ? 40.989 27.059  87.448 1.00 44.37  ? 311 GLU A CB  1 
ATOM   2380 C  CG  . GLU A 1 311 ? 40.020 28.233  87.522 1.00 53.34  ? 311 GLU A CG  1 
ATOM   2381 C  CD  . GLU A 1 311 ? 39.722 28.698  88.960 1.00 62.45  ? 311 GLU A CD  1 
ATOM   2382 O  OE1 . GLU A 1 311 ? 40.452 28.293  89.908 1.00 51.85  ? 311 GLU A OE1 1 
ATOM   2383 O  OE2 . GLU A 1 311 ? 38.749 29.480  89.128 1.00 55.28  ? 311 GLU A OE2 1 
ATOM   2384 N  N   . LEU A 1 312 ? 39.145 24.804  86.363 1.00 35.56  ? 312 LEU A N   1 
ATOM   2385 C  CA  . LEU A 1 312 ? 37.871 24.404  85.770 1.00 35.07  ? 312 LEU A CA  1 
ATOM   2386 C  C   . LEU A 1 312 ? 37.252 23.229  86.515 1.00 37.33  ? 312 LEU A C   1 
ATOM   2387 O  O   . LEU A 1 312 ? 36.025 23.142  86.645 1.00 40.58  ? 312 LEU A O   1 
ATOM   2388 C  CB  . LEU A 1 312 ? 38.068 24.048  84.305 1.00 37.16  ? 312 LEU A CB  1 
ATOM   2389 C  CG  . LEU A 1 312 ? 38.430 25.203  83.368 1.00 35.86  ? 312 LEU A CG  1 
ATOM   2390 C  CD1 . LEU A 1 312 ? 38.666 24.628  81.975 1.00 35.98  ? 312 LEU A CD1 1 
ATOM   2391 C  CD2 . LEU A 1 312 ? 37.321 26.265  83.353 1.00 37.85  ? 312 LEU A CD2 1 
ATOM   2392 N  N   . ALA A 1 313 ? 38.085 22.309  87.009 1.00 38.16  ? 313 ALA A N   1 
ATOM   2393 C  CA  . ALA A 1 313 ? 37.552 21.128  87.663 1.00 40.32  ? 313 ALA A CA  1 
ATOM   2394 C  C   . ALA A 1 313 ? 36.820 21.454  88.966 1.00 43.96  ? 313 ALA A C   1 
ATOM   2395 O  O   . ALA A 1 313 ? 36.306 20.531  89.607 1.00 51.33  ? 313 ALA A O   1 
ATOM   2396 C  CB  . ALA A 1 313 ? 38.680 20.124  87.915 1.00 42.10  ? 313 ALA A CB  1 
ATOM   2397 N  N   . LYS A 1 314 ? 36.775 22.725  89.391 1.00 41.42  ? 314 LYS A N   1 
ATOM   2398 C  CA  . LYS A 1 314 ? 35.869 23.091  90.475 1.00 45.03  ? 314 LYS A CA  1 
ATOM   2399 C  C   . LYS A 1 314 ? 34.437 22.736  90.109 1.00 42.14  ? 314 LYS A C   1 
ATOM   2400 O  O   . LYS A 1 314 ? 33.645 22.379  90.986 1.00 40.19  ? 314 LYS A O   1 
ATOM   2401 C  CB  . LYS A 1 314 ? 35.969 24.587  90.818 1.00 52.02  ? 314 LYS A CB  1 
ATOM   2402 C  CG  . LYS A 1 314 ? 37.275 25.064  91.498 1.00 56.60  ? 314 LYS A CG  1 
ATOM   2403 C  CD  . LYS A 1 314 ? 38.168 23.920  91.930 1.00 64.14  ? 314 LYS A CD  1 
ATOM   2404 C  CE  . LYS A 1 314 ? 39.437 24.392  92.624 1.00 69.04  ? 314 LYS A CE  1 
ATOM   2405 N  NZ  . LYS A 1 314 ? 40.340 23.223  92.897 1.00 72.41  ? 314 LYS A NZ  1 
ATOM   2406 N  N   . ASP A 1 315 ? 34.092 22.831  88.823 1.00 36.64  ? 315 ASP A N   1 
ATOM   2407 C  CA  . ASP A 1 315 ? 32.854 22.256  88.324 1.00 43.04  ? 315 ASP A CA  1 
ATOM   2408 C  C   . ASP A 1 315 ? 33.005 20.744  88.359 1.00 40.72  ? 315 ASP A C   1 
ATOM   2409 O  O   . ASP A 1 315 ? 33.869 20.203  87.659 1.00 45.00  ? 315 ASP A O   1 
ATOM   2410 C  CB  . ASP A 1 315 ? 32.561 22.746  86.901 1.00 43.72  ? 315 ASP A CB  1 
ATOM   2411 C  CG  . ASP A 1 315 ? 31.265 22.180  86.329 1.00 41.87  ? 315 ASP A CG  1 
ATOM   2412 O  OD1 . ASP A 1 315 ? 30.796 21.107  86.763 1.00 44.94  ? 315 ASP A OD1 1 
ATOM   2413 O  OD2 . ASP A 1 315 ? 30.711 22.811  85.410 1.00 40.60  ? 315 ASP A OD2 1 
ATOM   2414 N  N   . PRO A 1 316 ? 32.203 20.024  89.147 1.00 43.01  ? 316 PRO A N   1 
ATOM   2415 C  CA  . PRO A 1 316 ? 32.413 18.571  89.255 1.00 43.80  ? 316 PRO A CA  1 
ATOM   2416 C  C   . PRO A 1 316 ? 32.064 17.812  87.976 1.00 37.85  ? 316 PRO A C   1 
ATOM   2417 O  O   . PRO A 1 316 ? 32.549 16.690  87.792 1.00 36.01  ? 316 PRO A O   1 
ATOM   2418 C  CB  . PRO A 1 316 ? 31.511 18.174  90.432 1.00 41.53  ? 316 PRO A CB  1 
ATOM   2419 C  CG  . PRO A 1 316 ? 30.460 19.215  90.446 1.00 44.48  ? 316 PRO A CG  1 
ATOM   2420 C  CD  . PRO A 1 316 ? 31.111 20.496  90.014 1.00 43.32  ? 316 PRO A CD  1 
ATOM   2421 N  N   . ARG A 1 317 ? 31.270 18.395  87.076 1.00 35.33  ? 317 ARG A N   1 
ATOM   2422 C  CA  . ARG A 1 317 ? 31.059 17.743  85.790 1.00 34.36  ? 317 ARG A CA  1 
ATOM   2423 C  C   . ARG A 1 317 ? 32.347 17.713  84.977 1.00 35.34  ? 317 ARG A C   1 
ATOM   2424 O  O   . ARG A 1 317 ? 32.595 16.738  84.260 1.00 36.08  ? 317 ARG A O   1 
ATOM   2425 C  CB  . ARG A 1 317 ? 29.937 18.440  85.015 1.00 35.32  ? 317 ARG A CB  1 
ATOM   2426 C  CG  . ARG A 1 317 ? 28.667 18.670  85.812 1.00 33.58  ? 317 ARG A CG  1 
ATOM   2427 C  CD  . ARG A 1 317 ? 27.692 19.610  85.081 1.00 36.19  ? 317 ARG A CD  1 
ATOM   2428 N  NE  . ARG A 1 317 ? 28.298 20.893  84.726 1.00 37.74  ? 317 ARG A NE  1 
ATOM   2429 C  CZ  . ARG A 1 317 ? 27.919 21.640  83.700 1.00 35.54  ? 317 ARG A CZ  1 
ATOM   2430 N  NH1 . ARG A 1 317 ? 26.912 21.280  82.918 1.00 38.14  ? 317 ARG A NH1 1 
ATOM   2431 N  NH2 . ARG A 1 317 ? 28.569 22.771  83.445 1.00 33.70  ? 317 ARG A NH2 1 
ATOM   2432 N  N   . ILE A 1 318 ? 33.182 18.757  85.112 1.00 37.28  ? 318 ILE A N   1 
ATOM   2433 C  CA  . ILE A 1 318 ? 34.484 18.824  84.449 1.00 34.76  ? 318 ILE A CA  1 
ATOM   2434 C  C   . ILE A 1 318 ? 35.454 17.838  85.085 1.00 33.83  ? 318 ILE A C   1 
ATOM   2435 O  O   . ILE A 1 318 ? 36.153 17.084  84.392 1.00 31.20  ? 318 ILE A O   1 
ATOM   2436 C  CB  . ILE A 1 318 ? 35.022 20.269  84.512 1.00 35.98  ? 318 ILE A CB  1 
ATOM   2437 C  CG1 . ILE A 1 318 ? 34.040 21.245  83.860 1.00 41.14  ? 318 ILE A CG1 1 
ATOM   2438 C  CG2 . ILE A 1 318 ? 36.401 20.409  83.887 1.00 36.92  ? 318 ILE A CG2 1 
ATOM   2439 C  CD1 . ILE A 1 318 ? 33.875 21.050  82.400 1.00 46.04  ? 318 ILE A CD1 1 
ATOM   2440 N  N   . ALA A 1 319 ? 35.535 17.859  86.423 1.00 36.46  ? 319 ALA A N   1 
ATOM   2441 C  CA  . ALA A 1 319 ? 36.278 16.846  87.164 1.00 30.94  ? 319 ALA A CA  1 
ATOM   2442 C  C   . ALA A 1 319 ? 35.918 15.442  86.700 1.00 30.68  ? 319 ALA A C   1 
ATOM   2443 O  O   . ALA A 1 319 ? 36.796 14.592  86.523 1.00 41.40  ? 319 ALA A O   1 
ATOM   2444 C  CB  . ALA A 1 319 ? 36.000 17.006  88.664 1.00 32.18  ? 319 ALA A CB  1 
ATOM   2445 N  N   . ALA A 1 320 ? 34.628 15.182  86.487 1.00 29.82  ? 320 ALA A N   1 
ATOM   2446 C  CA  . ALA A 1 320 ? 34.199 13.841  86.116 1.00 32.07  ? 320 ALA A CA  1 
ATOM   2447 C  C   . ALA A 1 320 ? 34.655 13.490  84.700 1.00 31.53  ? 320 ALA A C   1 
ATOM   2448 O  O   . ALA A 1 320 ? 35.108 12.366  84.448 1.00 35.32  ? 320 ALA A O   1 
ATOM   2449 C  CB  . ALA A 1 320 ? 32.671 13.722  86.249 1.00 32.74  ? 320 ALA A CB  1 
ATOM   2450 N  N   . THR A 1 321 ? 34.564 14.446  83.770 1.00 30.49  ? 321 THR A N   1 
ATOM   2451 C  CA  . THR A 1 321 ? 35.076 14.218  82.419 1.00 29.30  ? 321 THR A CA  1 
ATOM   2452 C  C   . THR A 1 321 ? 36.567 13.882  82.439 1.00 31.63  ? 321 THR A C   1 
ATOM   2453 O  O   . THR A 1 321 ? 37.002 12.907  81.806 1.00 33.08  ? 321 THR A O   1 
ATOM   2454 C  CB  . THR A 1 321 ? 34.799 15.445  81.539 1.00 30.40  ? 321 THR A CB  1 
ATOM   2455 O  OG1 . THR A 1 321 ? 33.387 15.704  81.528 1.00 32.63  ? 321 THR A OG1 1 
ATOM   2456 C  CG2 . THR A 1 321 ? 35.309 15.233  80.096 1.00 32.51  ? 321 THR A CG2 1 
ATOM   2457 N  N   . MET A 1 322 ? 37.370 14.677  83.157 1.00 32.52  ? 322 MET A N   1 
ATOM   2458 C  CA  . MET A 1 322 ? 38.794 14.363  83.264 1.00 35.38  ? 322 MET A CA  1 
ATOM   2459 C  C   . MET A 1 322 ? 38.997 12.992  83.888 1.00 41.75  ? 322 MET A C   1 
ATOM   2460 O  O   . MET A 1 322 ? 39.706 12.143  83.325 1.00 38.00  ? 322 MET A O   1 
ATOM   2461 C  CB  . MET A 1 322 ? 39.526 15.424  84.083 1.00 36.51  ? 322 MET A CB  1 
ATOM   2462 C  CG  . MET A 1 322 ? 41.058 15.338  84.029 1.00 35.67  ? 322 MET A CG  1 
ATOM   2463 S  SD  . MET A 1 322 ? 41.701 14.919  82.383 1.00 36.85  ? 322 MET A SD  1 
ATOM   2464 C  CE  . MET A 1 322 ? 42.303 16.524  81.879 1.00 36.51  ? 322 MET A CE  1 
ATOM   2465 N  N   . GLU A 1 323 ? 38.348 12.740  85.039 1.00 40.35  ? 323 GLU A N   1 
ATOM   2466 C  CA  . GLU A 1 323 ? 38.542 11.458  85.718 1.00 37.17  ? 323 GLU A CA  1 
ATOM   2467 C  C   . GLU A 1 323 ? 38.179 10.284  84.810 1.00 34.74  ? 323 GLU A C   1 
ATOM   2468 O  O   . GLU A 1 323 ? 38.849 9.249   84.807 1.00 38.91  ? 323 GLU A O   1 
ATOM   2469 C  CB  . GLU A 1 323 ? 37.718 11.389  87.003 1.00 41.75  ? 323 GLU A CB  1 
ATOM   2470 C  CG  . GLU A 1 323 ? 37.894 10.047  87.714 1.00 42.34  ? 323 GLU A CG  1 
ATOM   2471 C  CD  . GLU A 1 323 ? 36.912 9.808   88.856 1.00 51.78  ? 323 GLU A CD  1 
ATOM   2472 O  OE1 . GLU A 1 323 ? 35.924 10.565  88.993 1.00 50.58  ? 323 GLU A OE1 1 
ATOM   2473 O  OE2 . GLU A 1 323 ? 37.129 8.844   89.621 1.00 57.22  ? 323 GLU A OE2 1 
ATOM   2474 N  N   . ASN A 1 324 ? 37.123 10.423  84.027 1.00 32.91  ? 324 ASN A N   1 
ATOM   2475 C  CA  . ASN A 1 324 ? 36.830 9.355   83.094 1.00 34.43  ? 324 ASN A CA  1 
ATOM   2476 C  C   . ASN A 1 324 ? 37.875 9.288   81.991 1.00 34.88  ? 324 ASN A C   1 
ATOM   2477 O  O   . ASN A 1 324 ? 38.325 8.200   81.633 1.00 32.86  ? 324 ASN A O   1 
ATOM   2478 C  CB  . ASN A 1 324 ? 35.422 9.535   82.551 1.00 35.10  ? 324 ASN A CB  1 
ATOM   2479 C  CG  . ASN A 1 324 ? 34.400 9.068   83.536 1.00 39.80  ? 324 ASN A CG  1 
ATOM   2480 O  OD1 . ASN A 1 324 ? 34.573 7.991   84.136 1.00 36.68  ? 324 ASN A OD1 1 
ATOM   2481 N  ND2 . ASN A 1 324 ? 33.357 9.883   83.770 1.00 35.35  ? 324 ASN A ND2 1 
ATOM   2482 N  N   . ALA A 1 325 ? 38.289 10.439  81.455 1.00 35.14  ? 325 ALA A N   1 
ATOM   2483 C  CA  . ALA A 1 325 ? 39.356 10.449  80.458 1.00 34.22  ? 325 ALA A CA  1 
ATOM   2484 C  C   . ALA A 1 325 ? 40.598 9.728   80.975 1.00 36.62  ? 325 ALA A C   1 
ATOM   2485 O  O   . ALA A 1 325 ? 41.146 8.841   80.303 1.00 35.81  ? 325 ALA A O   1 
ATOM   2486 C  CB  . ALA A 1 325 ? 39.696 11.887  80.065 1.00 30.71  ? 325 ALA A CB  1 
ATOM   2487 N  N   . GLN A 1 326 ? 41.056 10.090  82.178 1.00 36.62  ? 326 GLN A N   1 
ATOM   2488 C  CA  . GLN A 1 326 ? 42.291 9.497   82.680 1.00 43.03  ? 326 GLN A CA  1 
ATOM   2489 C  C   . GLN A 1 326 ? 42.147 7.990   82.871 1.00 38.62  ? 326 GLN A C   1 
ATOM   2490 O  O   . GLN A 1 326 ? 43.131 7.250   82.744 1.00 34.02  ? 326 GLN A O   1 
ATOM   2491 C  CB  . GLN A 1 326 ? 42.719 10.191  83.979 1.00 43.65  ? 326 GLN A CB  1 
ATOM   2492 C  CG  . GLN A 1 326 ? 43.217 11.608  83.749 1.00 48.01  ? 326 GLN A CG  1 
ATOM   2493 C  CD  . GLN A 1 326 ? 43.935 12.225  84.945 1.00 51.22  ? 326 GLN A CD  1 
ATOM   2494 O  OE1 . GLN A 1 326 ? 44.096 11.595  85.988 1.00 66.81  ? 326 GLN A OE1 1 
ATOM   2495 N  NE2 . GLN A 1 326 ? 44.376 13.466  84.788 1.00 49.68  ? 326 GLN A NE2 1 
ATOM   2496 N  N   . LYS A 1 327 ? 40.939 7.507   83.141 1.00 37.04  ? 327 LYS A N   1 
ATOM   2497 C  CA  . LYS A 1 327 ? 40.709 6.070   83.251 1.00 39.26  ? 327 LYS A CA  1 
ATOM   2498 C  C   . LYS A 1 327 ? 40.457 5.392   81.902 1.00 39.60  ? 327 LYS A C   1 
ATOM   2499 O  O   . LYS A 1 327 ? 40.222 4.176   81.863 1.00 41.58  ? 327 LYS A O   1 
ATOM   2500 C  CB  . LYS A 1 327 ? 39.532 5.801   84.188 1.00 39.10  ? 327 LYS A CB  1 
ATOM   2501 C  CG  . LYS A 1 327 ? 39.940 5.661   85.651 1.00 45.86  ? 327 LYS A CG  1 
ATOM   2502 C  CD  . LYS A 1 327 ? 38.894 6.263   86.583 1.00 49.80  ? 327 LYS A CD  1 
ATOM   2503 C  CE  . LYS A 1 327 ? 39.192 5.913   88.027 1.00 57.31  ? 327 LYS A CE  1 
ATOM   2504 N  NZ  . LYS A 1 327 ? 37.950 5.568   88.765 1.00 62.70  ? 327 LYS A NZ  1 
ATOM   2505 N  N   . GLY A 1 328 ? 40.516 6.132   80.799 1.00 41.01  ? 328 GLY A N   1 
ATOM   2506 C  CA  . GLY A 1 328 ? 40.017 5.658   79.525 1.00 43.17  ? 328 GLY A CA  1 
ATOM   2507 C  C   . GLY A 1 328 ? 41.104 5.243   78.557 1.00 37.70  ? 328 GLY A C   1 
ATOM   2508 O  O   . GLY A 1 328 ? 42.270 5.043   78.920 1.00 34.09  ? 328 GLY A O   1 
ATOM   2509 N  N   . GLU A 1 329 ? 40.715 5.110   77.299 1.00 39.67  ? 329 GLU A N   1 
ATOM   2510 C  CA  . GLU A 1 329 ? 41.596 4.642   76.238 1.00 43.54  ? 329 GLU A CA  1 
ATOM   2511 C  C   . GLU A 1 329 ? 41.736 5.772   75.223 1.00 38.52  ? 329 GLU A C   1 
ATOM   2512 O  O   . GLU A 1 329 ? 40.729 6.290   74.732 1.00 41.53  ? 329 GLU A O   1 
ATOM   2513 C  CB  . GLU A 1 329 ? 41.010 3.366   75.603 1.00 46.30  ? 329 GLU A CB  1 
ATOM   2514 C  CG  . GLU A 1 329 ? 41.934 2.575   74.658 1.00 52.75  ? 329 GLU A CG  1 
ATOM   2515 C  CD  . GLU A 1 329 ? 41.172 1.542   73.798 1.00 58.36  ? 329 GLU A CD  1 
ATOM   2516 O  OE1 . GLU A 1 329 ? 40.062 1.093   74.198 1.00 52.76  ? 329 GLU A OE1 1 
ATOM   2517 O  OE2 . GLU A 1 329 ? 41.687 1.177   72.716 1.00 52.73  ? 329 GLU A OE2 1 
ATOM   2518 N  N   . ILE A 1 330 ? 42.969 6.176   74.922 1.00 40.63  ? 330 ILE A N   1 
ATOM   2519 C  CA  . ILE A 1 330 ? 43.165 7.190   73.887 1.00 41.21  ? 330 ILE A CA  1 
ATOM   2520 C  C   . ILE A 1 330 ? 42.707 6.615   72.555 1.00 37.29  ? 330 ILE A C   1 
ATOM   2521 O  O   . ILE A 1 330 ? 43.106 5.509   72.170 1.00 33.59  ? 330 ILE A O   1 
ATOM   2522 C  CB  . ILE A 1 330 ? 44.636 7.634   73.834 1.00 42.96  ? 330 ILE A CB  1 
ATOM   2523 C  CG1 . ILE A 1 330 ? 45.052 8.204   75.192 1.00 40.33  ? 330 ILE A CG1 1 
ATOM   2524 C  CG2 . ILE A 1 330 ? 44.884 8.631   72.668 1.00 40.24  ? 330 ILE A CG2 1 
ATOM   2525 C  CD1 . ILE A 1 330 ? 46.127 9.220   75.122 1.00 45.29  ? 330 ILE A CD1 1 
ATOM   2526 N  N   . MET A 1 331 ? 41.834 7.330   71.866 1.00 39.56  ? 331 MET A N   1 
ATOM   2527 C  CA  . MET A 1 331 ? 41.372 6.805   70.590 1.00 40.59  ? 331 MET A CA  1 
ATOM   2528 C  C   . MET A 1 331 ? 42.583 6.682   69.673 1.00 39.81  ? 331 MET A C   1 
ATOM   2529 O  O   . MET A 1 331 ? 43.326 7.662   69.523 1.00 35.22  ? 331 MET A O   1 
ATOM   2530 C  CB  . MET A 1 331 ? 40.306 7.702   69.971 1.00 42.57  ? 331 MET A CB  1 
ATOM   2531 C  CG  . MET A 1 331 ? 39.606 7.052   68.782 1.00 52.50  ? 331 MET A CG  1 
ATOM   2532 S  SD  . MET A 1 331 ? 38.348 8.104   68.033 1.00 60.97  ? 331 MET A SD  1 
ATOM   2533 C  CE  . MET A 1 331 ? 37.478 8.721   69.491 1.00 60.08  ? 331 MET A CE  1 
ATOM   2534 N  N   . PRO A 1 332 ? 42.875 5.500   69.128 1.00 42.48  ? 332 PRO A N   1 
ATOM   2535 C  CA  . PRO A 1 332 ? 43.985 5.384   68.176 1.00 41.96  ? 332 PRO A CA  1 
ATOM   2536 C  C   . PRO A 1 332 ? 43.832 6.381   67.038 1.00 37.25  ? 332 PRO A C   1 
ATOM   2537 O  O   . PRO A 1 332 ? 42.719 6.647   66.568 1.00 36.33  ? 332 PRO A O   1 
ATOM   2538 C  CB  . PRO A 1 332 ? 43.865 3.941   67.679 1.00 40.21  ? 332 PRO A CB  1 
ATOM   2539 C  CG  . PRO A 1 332 ? 43.231 3.221   68.788 1.00 41.70  ? 332 PRO A CG  1 
ATOM   2540 C  CD  . PRO A 1 332 ? 42.230 4.197   69.364 1.00 42.70  ? 332 PRO A CD  1 
ATOM   2541 N  N   . ASN A 1 333 ? 44.951 6.961   66.612 1.00 38.15  ? 333 ASN A N   1 
ATOM   2542 C  CA  . ASN A 1 333 ? 44.931 7.900   65.498 1.00 41.25  ? 333 ASN A CA  1 
ATOM   2543 C  C   . ASN A 1 333 ? 45.371 7.255   64.181 1.00 40.94  ? 333 ASN A C   1 
ATOM   2544 O  O   . ASN A 1 333 ? 45.712 7.966   63.237 1.00 45.64  ? 333 ASN A O   1 
ATOM   2545 C  CB  . ASN A 1 333 ? 45.798 9.117   65.814 1.00 39.31  ? 333 ASN A CB  1 
ATOM   2546 C  CG  . ASN A 1 333 ? 47.271 8.762   65.986 1.00 34.80  ? 333 ASN A CG  1 
ATOM   2547 O  OD1 . ASN A 1 333 ? 47.631 7.594   65.992 1.00 35.33  ? 333 ASN A OD1 1 
ATOM   2548 N  ND2 . ASN A 1 333 ? 48.126 9.776   66.120 1.00 34.88  ? 333 ASN A ND2 1 
ATOM   2549 N  N   . ILE A 1 334 ? 45.380 5.931   64.102 1.00 47.28  ? 334 ILE A N   1 
ATOM   2550 C  CA  . ILE A 1 334 ? 45.819 5.231   62.895 1.00 54.85  ? 334 ILE A CA  1 
ATOM   2551 C  C   . ILE A 1 334 ? 44.603 4.985   62.009 1.00 60.50  ? 334 ILE A C   1 
ATOM   2552 O  O   . ILE A 1 334 ? 43.467 5.010   62.506 1.00 60.94  ? 334 ILE A O   1 
ATOM   2553 C  CB  . ILE A 1 334 ? 46.543 3.924   63.246 1.00 56.68  ? 334 ILE A CB  1 
ATOM   2554 C  CG1 . ILE A 1 334 ? 45.584 2.940   63.919 1.00 61.77  ? 334 ILE A CG1 1 
ATOM   2555 C  CG2 . ILE A 1 334 ? 47.748 4.216   64.137 1.00 58.98  ? 334 ILE A CG2 1 
ATOM   2556 C  CD1 . ILE A 1 334 ? 46.275 1.716   64.468 1.00 58.23  ? 334 ILE A CD1 1 
ATOM   2557 N  N   . PRO A 1 335 ? 44.771 4.760   60.701 1.00 67.21  ? 335 PRO A N   1 
ATOM   2558 C  CA  . PRO A 1 335 ? 43.594 4.662   59.829 1.00 63.31  ? 335 PRO A CA  1 
ATOM   2559 C  C   . PRO A 1 335 ? 42.906 3.308   59.878 1.00 60.74  ? 335 PRO A C   1 
ATOM   2560 O  O   . PRO A 1 335 ? 41.757 3.200   59.418 1.00 55.20  ? 335 PRO A O   1 
ATOM   2561 C  CB  . PRO A 1 335 ? 44.167 4.948   58.433 1.00 68.35  ? 335 PRO A CB  1 
ATOM   2562 C  CG  . PRO A 1 335 ? 45.655 4.639   58.533 1.00 75.25  ? 335 PRO A CG  1 
ATOM   2563 C  CD  . PRO A 1 335 ? 46.017 4.436   59.977 1.00 71.60  ? 335 PRO A CD  1 
ATOM   2564 N  N   . GLN A 1 336 ? 43.551 2.277   60.431 1.00 55.71  ? 336 GLN A N   1 
ATOM   2565 C  CA  . GLN A 1 336 ? 42.848 1.021   60.649 1.00 58.08  ? 336 GLN A CA  1 
ATOM   2566 C  C   . GLN A 1 336 ? 41.683 1.166   61.623 1.00 56.89  ? 336 GLN A C   1 
ATOM   2567 O  O   . GLN A 1 336 ? 40.907 0.219   61.779 1.00 59.32  ? 336 GLN A O   1 
ATOM   2568 C  CB  . GLN A 1 336 ? 43.818 -0.043  61.154 1.00 54.17  ? 336 GLN A CB  1 
ATOM   2569 N  N   . MET A 1 337 ? 41.552 2.319   62.288 1.00 50.40  ? 337 MET A N   1 
ATOM   2570 C  CA  . MET A 1 337 ? 40.420 2.553   63.173 1.00 50.05  ? 337 MET A CA  1 
ATOM   2571 C  C   . MET A 1 337 ? 39.109 2.474   62.406 1.00 54.19  ? 337 MET A C   1 
ATOM   2572 O  O   . MET A 1 337 ? 38.067 2.129   62.979 1.00 58.24  ? 337 MET A O   1 
ATOM   2573 C  CB  . MET A 1 337 ? 40.571 3.915   63.855 1.00 48.48  ? 337 MET A CB  1 
ATOM   2574 C  CG  . MET A 1 337 ? 41.250 3.886   65.233 1.00 49.35  ? 337 MET A CG  1 
ATOM   2575 S  SD  . MET A 1 337 ? 40.706 2.588   66.384 1.00 51.19  ? 337 MET A SD  1 
ATOM   2576 C  CE  . MET A 1 337 ? 39.013 3.117   66.678 1.00 54.97  ? 337 MET A CE  1 
ATOM   2577 N  N   . SER A 1 338 ? 39.145 2.774   61.108 1.00 51.36  ? 338 SER A N   1 
ATOM   2578 C  CA  . SER A 1 338 ? 37.941 2.678   60.288 1.00 52.20  ? 338 SER A CA  1 
ATOM   2579 C  C   . SER A 1 338 ? 37.430 1.241   60.229 1.00 49.21  ? 338 SER A C   1 
ATOM   2580 O  O   . SER A 1 338 ? 36.228 0.985   60.382 1.00 49.52  ? 338 SER A O   1 
ATOM   2581 C  CB  . SER A 1 338 ? 38.236 3.210   58.890 1.00 54.00  ? 338 SER A CB  1 
ATOM   2582 O  OG  . SER A 1 338 ? 37.040 3.595   58.254 1.00 60.22  ? 338 SER A OG  1 
ATOM   2583 N  N   . ALA A 1 339 ? 38.338 0.288   60.009 1.00 48.89  ? 339 ALA A N   1 
ATOM   2584 C  CA  . ALA A 1 339 ? 37.967 -1.117  60.033 1.00 48.29  ? 339 ALA A CA  1 
ATOM   2585 C  C   . ALA A 1 339 ? 37.475 -1.532  61.418 1.00 51.64  ? 339 ALA A C   1 
ATOM   2586 O  O   . ALA A 1 339 ? 36.474 -2.248  61.540 1.00 55.84  ? 339 ALA A O   1 
ATOM   2587 C  CB  . ALA A 1 339 ? 39.158 -1.965  59.598 1.00 49.81  ? 339 ALA A CB  1 
ATOM   2588 N  N   . PHE A 1 340 ? 38.161 -1.086  62.474 1.00 48.55  ? 340 PHE A N   1 
ATOM   2589 C  CA  . PHE A 1 340 ? 37.704 -1.379  63.832 1.00 53.36  ? 340 PHE A CA  1 
ATOM   2590 C  C   . PHE A 1 340 ? 36.282 -0.870  64.069 1.00 53.20  ? 340 PHE A C   1 
ATOM   2591 O  O   . PHE A 1 340 ? 35.428 -1.605  64.586 1.00 45.37  ? 340 PHE A O   1 
ATOM   2592 C  CB  . PHE A 1 340 ? 38.671 -0.773  64.846 1.00 51.89  ? 340 PHE A CB  1 
ATOM   2593 C  CG  . PHE A 1 340 ? 38.186 -0.821  66.272 1.00 53.26  ? 340 PHE A CG  1 
ATOM   2594 C  CD1 . PHE A 1 340 ? 38.469 -1.910  67.084 1.00 50.65  ? 340 PHE A CD1 1 
ATOM   2595 C  CD2 . PHE A 1 340 ? 37.481 0.246   66.819 1.00 52.60  ? 340 PHE A CD2 1 
ATOM   2596 C  CE1 . PHE A 1 340 ? 38.041 -1.946  68.413 1.00 48.74  ? 340 PHE A CE1 1 
ATOM   2597 C  CE2 . PHE A 1 340 ? 37.055 0.216   68.145 1.00 52.35  ? 340 PHE A CE2 1 
ATOM   2598 C  CZ  . PHE A 1 340 ? 37.335 -0.883  68.938 1.00 50.62  ? 340 PHE A CZ  1 
ATOM   2599 N  N   . TRP A 1 341 ? 36.009 0.389   63.701 1.00 54.87  ? 341 TRP A N   1 
ATOM   2600 C  CA  . TRP A 1 341 ? 34.679 0.963   63.918 1.00 55.41  ? 341 TRP A CA  1 
ATOM   2601 C  C   . TRP A 1 341 ? 33.592 0.119   63.261 1.00 57.05  ? 341 TRP A C   1 
ATOM   2602 O  O   . TRP A 1 341 ? 32.613 -0.269  63.912 1.00 61.71  ? 341 TRP A O   1 
ATOM   2603 C  CB  . TRP A 1 341 ? 34.605 2.393   63.374 1.00 56.96  ? 341 TRP A CB  1 
ATOM   2604 C  CG  . TRP A 1 341 ? 35.256 3.496   64.187 1.00 58.43  ? 341 TRP A CG  1 
ATOM   2605 C  CD1 . TRP A 1 341 ? 36.007 4.527   63.693 1.00 56.04  ? 341 TRP A CD1 1 
ATOM   2606 C  CD2 . TRP A 1 341 ? 35.185 3.702   65.611 1.00 58.82  ? 341 TRP A CD2 1 
ATOM   2607 N  NE1 . TRP A 1 341 ? 36.417 5.350   64.713 1.00 57.39  ? 341 TRP A NE1 1 
ATOM   2608 C  CE2 . TRP A 1 341 ? 35.928 4.870   65.900 1.00 56.69  ? 341 TRP A CE2 1 
ATOM   2609 C  CE3 . TRP A 1 341 ? 34.571 3.015   66.665 1.00 55.18  ? 341 TRP A CE3 1 
ATOM   2610 C  CZ2 . TRP A 1 341 ? 36.083 5.361   67.202 1.00 55.16  ? 341 TRP A CZ2 1 
ATOM   2611 C  CZ3 . TRP A 1 341 ? 34.720 3.510   67.955 1.00 54.40  ? 341 TRP A CZ3 1 
ATOM   2612 C  CH2 . TRP A 1 341 ? 35.471 4.671   68.212 1.00 53.62  ? 341 TRP A CH2 1 
ATOM   2613 N  N   . TYR A 1 342 ? 33.728 -0.142  61.955 1.00 59.61  ? 342 TYR A N   1 
ATOM   2614 C  CA  . TYR A 1 342 ? 32.720 -0.928  61.248 1.00 62.93  ? 342 TYR A CA  1 
ATOM   2615 C  C   . TYR A 1 342 ? 32.620 -2.335  61.827 1.00 61.24  ? 342 TYR A C   1 
ATOM   2616 O  O   . TYR A 1 342 ? 31.515 -2.873  61.986 1.00 58.32  ? 342 TYR A O   1 
ATOM   2617 C  CB  . TYR A 1 342 ? 33.042 -0.980  59.751 1.00 74.12  ? 342 TYR A CB  1 
ATOM   2618 C  CG  . TYR A 1 342 ? 32.012 -1.731  58.910 1.00 89.57  ? 342 TYR A CG  1 
ATOM   2619 C  CD1 . TYR A 1 342 ? 31.989 -3.126  58.873 1.00 91.46  ? 342 TYR A CD1 1 
ATOM   2620 C  CD2 . TYR A 1 342 ? 31.069 -1.046  58.149 1.00 95.02  ? 342 TYR A CD2 1 
ATOM   2621 C  CE1 . TYR A 1 342 ? 31.054 -3.812  58.119 1.00 94.31  ? 342 TYR A CE1 1 
ATOM   2622 C  CE2 . TYR A 1 342 ? 30.130 -1.728  57.382 1.00 96.30  ? 342 TYR A CE2 1 
ATOM   2623 C  CZ  . TYR A 1 342 ? 30.129 -3.111  57.374 1.00 102.05 ? 342 TYR A CZ  1 
ATOM   2624 O  OH  . TYR A 1 342 ? 29.203 -3.801  56.622 1.00 96.55  ? 342 TYR A OH  1 
ATOM   2625 N  N   . ALA A 1 343 ? 33.764 -2.953  62.135 1.00 54.35  ? 343 ALA A N   1 
ATOM   2626 C  CA  . ALA A 1 343 ? 33.753 -4.299  62.699 1.00 51.24  ? 343 ALA A CA  1 
ATOM   2627 C  C   . ALA A 1 343 ? 32.920 -4.352  63.973 1.00 54.37  ? 343 ALA A C   1 
ATOM   2628 O  O   . ALA A 1 343 ? 31.980 -5.149  64.088 1.00 60.61  ? 343 ALA A O   1 
ATOM   2629 C  CB  . ALA A 1 343 ? 35.186 -4.755  62.965 1.00 52.72  ? 343 ALA A CB  1 
ATOM   2630 N  N   . VAL A 1 344 ? 33.226 -3.471  64.928 1.00 56.85  ? 344 VAL A N   1 
ATOM   2631 C  CA  . VAL A 1 344 ? 32.580 -3.536  66.234 1.00 52.65  ? 344 VAL A CA  1 
ATOM   2632 C  C   . VAL A 1 344 ? 31.140 -3.018  66.194 1.00 46.63  ? 344 VAL A C   1 
ATOM   2633 O  O   . VAL A 1 344 ? 30.305 -3.471  66.981 1.00 51.25  ? 344 VAL A O   1 
ATOM   2634 C  CB  . VAL A 1 344 ? 33.436 -2.788  67.271 1.00 53.99  ? 344 VAL A CB  1 
ATOM   2635 C  CG1 . VAL A 1 344 ? 32.727 -2.745  68.623 1.00 55.63  ? 344 VAL A CG1 1 
ATOM   2636 C  CG2 . VAL A 1 344 ? 34.814 -3.449  67.393 1.00 49.78  ? 344 VAL A CG2 1 
ATOM   2637 N  N   . ARG A 1 345 ? 30.802 -2.089  65.292 1.00 43.73  ? 345 ARG A N   1 
ATOM   2638 C  CA  . ARG A 1 345 ? 29.404 -1.675  65.201 1.00 51.25  ? 345 ARG A CA  1 
ATOM   2639 C  C   . ARG A 1 345 ? 28.516 -2.861  64.845 1.00 52.31  ? 345 ARG A C   1 
ATOM   2640 O  O   . ARG A 1 345 ? 27.425 -3.023  65.406 1.00 58.32  ? 345 ARG A O   1 
ATOM   2641 C  CB  . ARG A 1 345 ? 29.237 -0.538  64.188 1.00 56.67  ? 345 ARG A CB  1 
ATOM   2642 C  CG  . ARG A 1 345 ? 27.774 -0.065  64.007 1.00 60.67  ? 345 ARG A CG  1 
ATOM   2643 C  CD  . ARG A 1 345 ? 27.643 1.399   63.544 1.00 64.68  ? 345 ARG A CD  1 
ATOM   2644 N  NE  . ARG A 1 345 ? 28.773 1.849   62.736 1.00 72.51  ? 345 ARG A NE  1 
ATOM   2645 C  CZ  . ARG A 1 345 ? 29.607 2.833   63.062 1.00 75.26  ? 345 ARG A CZ  1 
ATOM   2646 N  NH1 . ARG A 1 345 ? 29.478 3.514   64.193 1.00 72.62  ? 345 ARG A NH1 1 
ATOM   2647 N  NH2 . ARG A 1 345 ? 30.600 3.143   62.231 1.00 67.42  ? 345 ARG A NH2 1 
ATOM   2648 N  N   . THR A 1 346 ? 28.991 -3.721  63.938 1.00 58.11  ? 346 THR A N   1 
ATOM   2649 C  CA  . THR A 1 346 ? 28.224 -4.891  63.519 1.00 54.22  ? 346 THR A CA  1 
ATOM   2650 C  C   . THR A 1 346 ? 28.126 -5.919  64.649 1.00 48.50  ? 346 THR A C   1 
ATOM   2651 O  O   . THR A 1 346 ? 27.044 -6.435  64.943 1.00 55.03  ? 346 THR A O   1 
ATOM   2652 C  CB  . THR A 1 346 ? 28.871 -5.509  62.269 1.00 56.92  ? 346 THR A CB  1 
ATOM   2653 O  OG1 . THR A 1 346 ? 28.471 -4.784  61.098 1.00 62.37  ? 346 THR A OG1 1 
ATOM   2654 C  CG2 . THR A 1 346 ? 28.451 -6.963  62.113 1.00 54.79  ? 346 THR A CG2 1 
ATOM   2655 N  N   . ALA A 1 347 ? 29.253 -6.229  65.292 1.00 45.41  ? 347 ALA A N   1 
ATOM   2656 C  CA  . ALA A 1 347 ? 29.251 -7.193  66.390 1.00 45.29  ? 347 ALA A CA  1 
ATOM   2657 C  C   . ALA A 1 347 ? 28.208 -6.845  67.450 1.00 48.43  ? 347 ALA A C   1 
ATOM   2658 O  O   . ALA A 1 347 ? 27.431 -7.710  67.871 1.00 50.40  ? 347 ALA A O   1 
ATOM   2659 C  CB  . ALA A 1 347 ? 30.645 -7.276  67.011 1.00 48.15  ? 347 ALA A CB  1 
ATOM   2660 N  N   . VAL A 1 348 ? 28.160 -5.576  67.884 1.00 49.04  ? 348 VAL A N   1 
ATOM   2661 C  CA  . VAL A 1 348 ? 27.254 -5.204  68.970 1.00 46.08  ? 348 VAL A CA  1 
ATOM   2662 C  C   . VAL A 1 348 ? 25.810 -5.278  68.508 1.00 46.96  ? 348 VAL A C   1 
ATOM   2663 O  O   . VAL A 1 348 ? 24.948 -5.820  69.205 1.00 49.48  ? 348 VAL A O   1 
ATOM   2664 C  CB  . VAL A 1 348 ? 27.572 -3.804  69.520 1.00 49.39  ? 348 VAL A CB  1 
ATOM   2665 C  CG1 . VAL A 1 348 ? 26.546 -3.440  70.594 1.00 44.61  ? 348 VAL A CG1 1 
ATOM   2666 C  CG2 . VAL A 1 348 ? 28.987 -3.732  70.067 1.00 44.15  ? 348 VAL A CG2 1 
ATOM   2667 N  N   . ILE A 1 349 ? 25.519 -4.736  67.327 1.00 50.48  ? 349 ILE A N   1 
ATOM   2668 C  CA  . ILE A 1 349 ? 24.136 -4.735  66.861 1.00 54.32  ? 349 ILE A CA  1 
ATOM   2669 C  C   . ILE A 1 349 ? 23.640 -6.168  66.683 1.00 54.82  ? 349 ILE A C   1 
ATOM   2670 O  O   . ILE A 1 349 ? 22.518 -6.504  67.086 1.00 60.26  ? 349 ILE A O   1 
ATOM   2671 C  CB  . ILE A 1 349 ? 24.012 -3.901  65.570 1.00 58.40  ? 349 ILE A CB  1 
ATOM   2672 C  CG1 . ILE A 1 349 ? 23.977 -2.404  65.917 1.00 62.51  ? 349 ILE A CG1 1 
ATOM   2673 C  CG2 . ILE A 1 349 ? 22.770 -4.301  64.790 1.00 59.33  ? 349 ILE A CG2 1 
ATOM   2674 C  CD1 . ILE A 1 349 ? 23.890 -1.468  64.733 1.00 57.87  ? 349 ILE A CD1 1 
ATOM   2675 N  N   . ASN A 1 350 ? 24.490 -7.047  66.120 1.00 53.80  ? 350 ASN A N   1 
ATOM   2676 C  CA  . ASN A 1 350 ? 24.130 -8.454  65.918 1.00 48.78  ? 350 ASN A CA  1 
ATOM   2677 C  C   . ASN A 1 350 ? 24.000 -9.208  67.244 1.00 47.30  ? 350 ASN A C   1 
ATOM   2678 O  O   . ASN A 1 350 ? 23.065 -9.999  67.428 1.00 60.45  ? 350 ASN A O   1 
ATOM   2679 C  CB  . ASN A 1 350 ? 25.179 -9.138  65.039 1.00 46.89  ? 350 ASN A CB  1 
ATOM   2680 C  CG  . ASN A 1 350 ? 25.020 -8.818  63.545 1.00 52.73  ? 350 ASN A CG  1 
ATOM   2681 O  OD1 . ASN A 1 350 ? 24.059 -8.162  63.128 1.00 56.57  ? 350 ASN A OD1 1 
ATOM   2682 N  ND2 . ASN A 1 350 ? 25.978 -9.286  62.737 1.00 51.83  ? 350 ASN A ND2 1 
ATOM   2683 N  N   . ALA A 1 351 ? 24.955 -9.014  68.159 1.00 48.00  ? 351 ALA A N   1 
ATOM   2684 C  CA  . ALA A 1 351 ? 24.881 -9.660  69.469 1.00 47.71  ? 351 ALA A CA  1 
ATOM   2685 C  C   . ALA A 1 351 ? 23.687 -9.152  70.269 1.00 49.51  ? 351 ALA A C   1 
ATOM   2686 O  O   . ALA A 1 351 ? 22.930 -9.943  70.840 1.00 48.01  ? 351 ALA A O   1 
ATOM   2687 C  CB  . ALA A 1 351 ? 26.183 -9.437  70.237 1.00 48.09  ? 351 ALA A CB  1 
ATOM   2688 N  N   . ALA A 1 352 ? 23.492 -7.828  70.304 1.00 56.70  ? 352 ALA A N   1 
ATOM   2689 C  CA  . ALA A 1 352 ? 22.365 -7.247  71.038 1.00 57.16  ? 352 ALA A CA  1 
ATOM   2690 C  C   . ALA A 1 352 ? 21.019 -7.624  70.423 1.00 55.41  ? 352 ALA A C   1 
ATOM   2691 O  O   . ALA A 1 352 ? 20.013 -7.711  71.140 1.00 52.78  ? 352 ALA A O   1 
ATOM   2692 C  CB  . ALA A 1 352 ? 22.494 -5.722  71.097 1.00 56.41  ? 352 ALA A CB  1 
ATOM   2693 N  N   . SER A 1 353 ? 20.996 -7.808  69.100 1.00 55.91  ? 353 SER A N   1 
ATOM   2694 C  CA  . SER A 1 353 ? 19.726 -8.139  68.402 1.00 59.92  ? 353 SER A CA  1 
ATOM   2695 C  C   . SER A 1 353 ? 19.424 -9.632  68.560 1.00 58.48  ? 353 SER A C   1 
ATOM   2696 O  O   . SER A 1 353 ? 18.423 -10.096 67.980 1.00 57.19  ? 353 SER A O   1 
ATOM   2697 C  CB  . SER A 1 353 ? 19.785 -7.744  66.950 1.00 68.50  ? 353 SER A CB  1 
ATOM   2698 O  OG  . SER A 1 353 ? 19.922 -6.337  66.816 1.00 73.75  ? 353 SER A OG  1 
ATOM   2699 N  N   . GLY A 1 354 ? 20.264 -10.351 69.311 1.00 61.28  ? 354 GLY A N   1 
ATOM   2700 C  CA  . GLY A 1 354 ? 20.070 -11.802 69.490 1.00 60.51  ? 354 GLY A CA  1 
ATOM   2701 C  C   . GLY A 1 354 ? 20.362 -12.557 68.205 1.00 71.79  ? 354 GLY A C   1 
ATOM   2702 O  O   . GLY A 1 354 ? 20.886 -11.932 67.261 1.00 76.52  ? 354 GLY A O   1 
ATOM   2703 N  N   . ARG A 1 355 ? 20.048 -13.856 68.172 1.00 78.93  ? 355 ARG A N   1 
ATOM   2704 C  CA  . ARG A 1 355 ? 20.305 -14.688 66.965 1.00 79.54  ? 355 ARG A CA  1 
ATOM   2705 C  C   . ARG A 1 355 ? 21.786 -14.569 66.593 1.00 77.73  ? 355 ARG A C   1 
ATOM   2706 O  O   . ARG A 1 355 ? 22.121 -14.822 65.419 1.00 77.30  ? 355 ARG A O   1 
ATOM   2707 C  CB  . ARG A 1 355 ? 19.403 -14.247 65.808 1.00 30.00  ? 355 ARG A CB  1 
ATOM   2708 N  N   . GLN A 1 356 ? 22.632 -14.198 67.559 1.00 77.77  ? 356 GLN A N   1 
ATOM   2709 C  CA  . GLN A 1 356 ? 24.087 -14.034 67.299 1.00 71.52  ? 356 GLN A CA  1 
ATOM   2710 C  C   . GLN A 1 356 ? 24.845 -14.214 68.617 1.00 70.21  ? 356 GLN A C   1 
ATOM   2711 O  O   . GLN A 1 356 ? 24.594 -13.428 69.552 1.00 68.88  ? 356 GLN A O   1 
ATOM   2712 C  CB  . GLN A 1 356 ? 24.361 -12.662 66.683 1.00 78.79  ? 356 GLN A CB  1 
ATOM   2713 C  CG  . GLN A 1 356 ? 25.791 -12.183 66.878 1.00 83.03  ? 356 GLN A CG  1 
ATOM   2714 C  CD  . GLN A 1 356 ? 26.771 -13.006 66.080 1.00 90.36  ? 356 GLN A CD  1 
ATOM   2715 O  OE1 . GLN A 1 356 ? 27.329 -13.986 66.566 1.00 105.13 ? 356 GLN A OE1 1 
ATOM   2716 N  NE2 . GLN A 1 356 ? 26.990 -12.608 64.837 1.00 83.94  ? 356 GLN A NE2 1 
ATOM   2717 N  N   . THR A 1 357 ? 25.734 -15.209 68.683 1.00 75.38  ? 357 THR A N   1 
ATOM   2718 C  CA  . THR A 1 357 ? 26.483 -15.487 69.937 1.00 68.58  ? 357 THR A CA  1 
ATOM   2719 C  C   . THR A 1 357 ? 27.493 -14.365 70.191 1.00 63.53  ? 357 THR A C   1 
ATOM   2720 O  O   . THR A 1 357 ? 28.259 -14.045 69.261 1.00 58.99  ? 357 THR A O   1 
ATOM   2721 C  CB  . THR A 1 357 ? 27.180 -16.851 69.872 1.00 66.13  ? 357 THR A CB  1 
ATOM   2722 O  OG1 . THR A 1 357 ? 26.174 -17.854 69.729 1.00 64.08  ? 357 THR A OG1 1 
ATOM   2723 C  CG2 . THR A 1 357 ? 28.023 -17.141 71.094 1.00 63.62  ? 357 THR A CG2 1 
ATOM   2724 N  N   . VAL A 1 358 ? 27.491 -13.793 71.399 1.00 57.60  ? 358 VAL A N   1 
ATOM   2725 C  CA  . VAL A 1 358 ? 28.504 -12.752 71.744 1.00 56.06  ? 358 VAL A CA  1 
ATOM   2726 C  C   . VAL A 1 358 ? 29.880 -13.299 71.355 1.00 53.95  ? 358 VAL A C   1 
ATOM   2727 O  O   . VAL A 1 358 ? 30.691 -12.525 70.808 1.00 53.29  ? 358 VAL A O   1 
ATOM   2728 C  CB  . VAL A 1 358 ? 28.446 -12.370 73.236 1.00 52.67  ? 358 VAL A CB  1 
ATOM   2729 C  CG1 . VAL A 1 358 ? 29.772 -11.814 73.732 1.00 47.71  ? 358 VAL A CG1 1 
ATOM   2730 C  CG2 . VAL A 1 358 ? 27.315 -11.394 73.523 1.00 49.86  ? 358 VAL A CG2 1 
ATOM   2731 N  N   . ASP A 1 359 ? 30.119 -14.590 71.611 1.00 49.26  ? 359 ASP A N   1 
ATOM   2732 C  CA  . ASP A 1 359 ? 31.396 -15.197 71.243 1.00 56.85  ? 359 ASP A CA  1 
ATOM   2733 C  C   . ASP A 1 359 ? 31.606 -15.199 69.730 1.00 52.98  ? 359 ASP A C   1 
ATOM   2734 O  O   . ASP A 1 359 ? 32.716 -14.946 69.250 1.00 56.04  ? 359 ASP A O   1 
ATOM   2735 C  CB  . ASP A 1 359 ? 31.478 -16.621 71.798 1.00 60.08  ? 359 ASP A CB  1 
ATOM   2736 C  CG  . ASP A 1 359 ? 31.997 -16.668 73.231 1.00 64.10  ? 359 ASP A CG  1 
ATOM   2737 O  OD1 . ASP A 1 359 ? 31.909 -15.638 73.948 1.00 59.70  ? 359 ASP A OD1 1 
ATOM   2738 O  OD2 . ASP A 1 359 ? 32.489 -17.738 73.644 1.00 66.19  ? 359 ASP A OD2 1 
ATOM   2739 N  N   . ALA A 1 360 ? 30.548 -15.469 68.965 1.00 54.60  ? 360 ALA A N   1 
ATOM   2740 C  CA  . ALA A 1 360 ? 30.668 -15.522 67.512 1.00 57.30  ? 360 ALA A CA  1 
ATOM   2741 C  C   . ALA A 1 360 ? 30.903 -14.137 66.930 1.00 65.84  ? 360 ALA A C   1 
ATOM   2742 O  O   . ALA A 1 360 ? 31.849 -13.931 66.157 1.00 68.24  ? 360 ALA A O   1 
ATOM   2743 C  CB  . ALA A 1 360 ? 29.413 -16.155 66.902 1.00 58.23  ? 360 ALA A CB  1 
ATOM   2744 N  N   . ALA A 1 361 ? 30.047 -13.170 67.292 1.00 61.64  ? 361 ALA A N   1 
ATOM   2745 C  CA  . ALA A 1 361 ? 30.154 -11.826 66.728 1.00 56.44  ? 361 ALA A CA  1 
ATOM   2746 C  C   . ALA A 1 361 ? 31.512 -11.197 67.037 1.00 53.48  ? 361 ALA A C   1 
ATOM   2747 O  O   . ALA A 1 361 ? 32.110 -10.543 66.170 1.00 55.92  ? 361 ALA A O   1 
ATOM   2748 C  CB  . ALA A 1 361 ? 29.017 -10.941 67.243 1.00 61.72  ? 361 ALA A CB  1 
ATOM   2749 N  N   . LEU A 1 362 ? 32.024 -11.400 68.258 1.00 45.24  ? 362 LEU A N   1 
ATOM   2750 C  CA  . LEU A 1 362 ? 33.333 -10.849 68.613 1.00 47.81  ? 362 LEU A CA  1 
ATOM   2751 C  C   . LEU A 1 362 ? 34.461 -11.525 67.841 1.00 50.25  ? 362 LEU A C   1 
ATOM   2752 O  O   . LEU A 1 362 ? 35.443 -10.870 67.477 1.00 60.85  ? 362 LEU A O   1 
ATOM   2753 C  CB  . LEU A 1 362 ? 33.575 -10.962 70.122 1.00 49.93  ? 362 LEU A CB  1 
ATOM   2754 C  CG  . LEU A 1 362 ? 32.865 -9.937  71.025 1.00 51.43  ? 362 LEU A CG  1 
ATOM   2755 C  CD1 . LEU A 1 362 ? 33.369 -10.022 72.460 1.00 50.46  ? 362 LEU A CD1 1 
ATOM   2756 C  CD2 . LEU A 1 362 ? 33.032 -8.523  70.498 1.00 51.72  ? 362 LEU A CD2 1 
ATOM   2757 N  N   . ALA A 1 363 ? 34.352 -12.835 67.598 1.00 58.16  ? 363 ALA A N   1 
ATOM   2758 C  CA  . ALA A 1 363 ? 35.334 -13.521 66.756 1.00 56.77  ? 363 ALA A CA  1 
ATOM   2759 C  C   . ALA A 1 363 ? 35.370 -12.929 65.347 1.00 52.66  ? 363 ALA A C   1 
ATOM   2760 O  O   . ALA A 1 363 ? 36.451 -12.681 64.797 1.00 55.28  ? 363 ALA A O   1 
ATOM   2761 C  CB  . ALA A 1 363 ? 35.034 -15.019 66.708 1.00 59.22  ? 363 ALA A CB  1 
ATOM   2762 N  N   . ALA A 1 364 ? 34.192 -12.672 64.754 1.00 57.69  ? 364 ALA A N   1 
ATOM   2763 C  CA  . ALA A 1 364 ? 34.149 -12.083 63.417 1.00 56.97  ? 364 ALA A CA  1 
ATOM   2764 C  C   . ALA A 1 364 ? 34.629 -10.635 63.424 1.00 69.21  ? 364 ALA A C   1 
ATOM   2765 O  O   . ALA A 1 364 ? 35.256 -10.180 62.457 1.00 70.84  ? 364 ALA A O   1 
ATOM   2766 C  CB  . ALA A 1 364 ? 32.736 -12.172 62.841 1.00 54.41  ? 364 ALA A CB  1 
ATOM   2767 N  N   . ALA A 1 365 ? 34.334 -9.889  64.496 1.00 65.91  ? 365 ALA A N   1 
ATOM   2768 C  CA  . ALA A 1 365 ? 34.824 -8.515  64.588 1.00 60.99  ? 365 ALA A CA  1 
ATOM   2769 C  C   . ALA A 1 365 ? 36.337 -8.485  64.741 1.00 60.00  ? 365 ALA A C   1 
ATOM   2770 O  O   . ALA A 1 365 ? 37.010 -7.641  64.138 1.00 62.89  ? 365 ALA A O   1 
ATOM   2771 C  CB  . ALA A 1 365 ? 34.156 -7.785  65.752 1.00 60.08  ? 365 ALA A CB  1 
ATOM   2772 N  N   . GLN A 1 366 ? 36.877 -9.386  65.569 1.00 61.68  ? 366 GLN A N   1 
ATOM   2773 C  CA  . GLN A 1 366 ? 38.321 -9.595  65.659 1.00 62.69  ? 366 GLN A CA  1 
ATOM   2774 C  C   . GLN A 1 366 ? 38.947 -9.726  64.272 1.00 64.52  ? 366 GLN A C   1 
ATOM   2775 O  O   . GLN A 1 366 ? 39.966 -9.091  63.973 1.00 63.86  ? 366 GLN A O   1 
ATOM   2776 C  CB  . GLN A 1 366 ? 38.595 -10.842 66.510 1.00 58.94  ? 366 GLN A CB  1 
ATOM   2777 C  CG  . GLN A 1 366 ? 40.031 -11.321 66.553 1.00 59.09  ? 366 GLN A CG  1 
ATOM   2778 C  CD  . GLN A 1 366 ? 40.899 -10.496 67.475 1.00 60.15  ? 366 GLN A CD  1 
ATOM   2779 O  OE1 . GLN A 1 366 ? 40.429 -9.537  68.090 1.00 67.89  ? 366 GLN A OE1 1 
ATOM   2780 N  NE2 . GLN A 1 366 ? 42.174 -10.867 67.586 1.00 59.60  ? 366 GLN A NE2 1 
ATOM   2781 N  N   . THR A 1 367 ? 38.326 -10.523 63.398 1.00 60.52  ? 367 THR A N   1 
ATOM   2782 C  CA  . THR A 1 367 ? 38.848 -10.686 62.044 1.00 66.04  ? 367 THR A CA  1 
ATOM   2783 C  C   . THR A 1 367 ? 38.747 -9.390  61.245 1.00 63.48  ? 367 THR A C   1 
ATOM   2784 O  O   . THR A 1 367 ? 39.743 -8.918  60.683 1.00 53.50  ? 367 THR A O   1 
ATOM   2785 C  CB  . THR A 1 367 ? 38.099 -11.812 61.329 1.00 68.41  ? 367 THR A CB  1 
ATOM   2786 O  OG1 . THR A 1 367 ? 38.418 -13.062 61.947 1.00 58.88  ? 367 THR A OG1 1 
ATOM   2787 C  CG2 . THR A 1 367 ? 38.466 -11.857 59.843 1.00 72.20  ? 367 THR A CG2 1 
ATOM   2788 N  N   . ASN A 1 368 ? 37.554 -8.784  61.214 1.00 63.23  ? 368 ASN A N   1 
ATOM   2789 C  CA  . ASN A 1 368 ? 37.237 -7.683  60.309 1.00 61.65  ? 368 ASN A CA  1 
ATOM   2790 C  C   . ASN A 1 368 ? 38.058 -6.418  60.541 1.00 63.07  ? 368 ASN A C   1 
ATOM   2791 O  O   . ASN A 1 368 ? 37.863 -5.425  59.836 1.00 72.69  ? 368 ASN A O   1 
ATOM   2792 C  CB  . ASN A 1 368 ? 35.747 -7.350  60.401 1.00 64.69  ? 368 ASN A CB  1 
ATOM   2793 N  N   . ALA A 1 369 ? 38.973 -6.431  61.512 1.00 73.28  ? 369 ALA A N   1 
ATOM   2794 C  CA  . ALA A 1 369 ? 39.957 -5.357  61.663 1.00 71.23  ? 369 ALA A CA  1 
ATOM   2795 C  C   . ALA A 1 369 ? 41.179 -5.713  60.819 1.00 81.58  ? 369 ALA A C   1 
ATOM   2796 O  O   . ALA A 1 369 ? 42.214 -6.161  61.316 1.00 70.68  ? 369 ALA A O   1 
ATOM   2797 C  CB  . ALA A 1 369 ? 40.323 -5.159  63.124 1.00 71.71  ? 369 ALA A CB  1 
ATOM   2798 N  N   . ALA A 1 370 ? 41.034 -5.518  59.509 1.00 86.97  ? 370 ALA A N   1 
ATOM   2799 C  CA  . ALA A 1 370 ? 42.092 -5.760  58.532 1.00 80.21  ? 370 ALA A CA  1 
ATOM   2800 C  C   . ALA A 1 370 ? 41.609 -5.281  57.173 1.00 76.75  ? 370 ALA A C   1 
ATOM   2801 O  O   . ALA A 1 370 ? 40.542 -5.695  56.722 1.00 73.64  ? 370 ALA A O   1 
ATOM   2802 C  CB  . ALA A 1 370 ? 42.464 -7.237  58.475 1.00 79.86  ? 370 ALA A CB  1 
ATOM   2803 N  N   . THR B 2 10  ? 30.471 11.827  44.407 1.00 62.26  ? 3   THR N N   1 
ATOM   2804 C  CA  . THR B 2 10  ? 30.900 11.531  45.773 1.00 69.25  ? 3   THR N CA  1 
ATOM   2805 C  C   . THR B 2 10  ? 29.768 10.895  46.555 1.00 65.97  ? 3   THR N C   1 
ATOM   2806 O  O   . THR B 2 10  ? 28.618 11.275  46.390 1.00 61.89  ? 3   THR N O   1 
ATOM   2807 C  CB  . THR B 2 10  ? 31.371 12.798  46.507 1.00 75.12  ? 3   THR N CB  1 
ATOM   2808 O  OG1 . THR B 2 10  ? 32.596 13.253  45.924 1.00 88.10  ? 3   THR N OG1 1 
ATOM   2809 C  CG2 . THR B 2 10  ? 31.594 12.532  48.005 1.00 73.46  ? 3   THR N CG2 1 
ATOM   2810 N  N   . GLU B 2 11  ? 30.105 9.928   47.410 1.00 65.85  ? 4   GLU N N   1 
ATOM   2811 C  CA  . GLU B 2 11  ? 29.098 9.248   48.215 1.00 65.05  ? 4   GLU N CA  1 
ATOM   2812 C  C   . GLU B 2 11  ? 28.646 10.084  49.409 1.00 64.84  ? 4   GLU N C   1 
ATOM   2813 O  O   . GLU B 2 11  ? 27.491 9.970   49.834 1.00 70.85  ? 4   GLU N O   1 
ATOM   2814 C  CB  . GLU B 2 11  ? 29.643 7.897   48.679 1.00 65.20  ? 4   GLU N CB  1 
ATOM   2815 C  CG  . GLU B 2 11  ? 29.634 6.843   47.582 1.00 61.97  ? 4   GLU N CG  1 
ATOM   2816 C  CD  . GLU B 2 11  ? 28.257 6.224   47.397 1.00 64.91  ? 4   GLU N CD  1 
ATOM   2817 O  OE1 . GLU B 2 11  ? 27.757 5.634   48.376 1.00 68.78  ? 4   GLU N OE1 1 
ATOM   2818 O  OE2 . GLU B 2 11  ? 27.670 6.328   46.292 1.00 55.04  ? 4   GLU N OE2 1 
ATOM   2819 N  N   . GLU B 2 12  ? 29.534 10.915  49.965 1.00 65.46  ? 5   GLU N N   1 
ATOM   2820 C  CA  . GLU B 2 12  ? 29.128 11.847  51.014 1.00 69.57  ? 5   GLU N CA  1 
ATOM   2821 C  C   . GLU B 2 12  ? 28.053 12.800  50.506 1.00 60.50  ? 5   GLU N C   1 
ATOM   2822 O  O   . GLU B 2 12  ? 27.120 13.159  51.240 1.00 45.29  ? 5   GLU N O   1 
ATOM   2823 C  CB  . GLU B 2 12  ? 30.346 12.629  51.516 1.00 72.90  ? 5   GLU N CB  1 
ATOM   2824 C  CG  . GLU B 2 12  ? 30.202 13.221  52.915 1.00 79.42  ? 5   GLU N CG  1 
ATOM   2825 C  CD  . GLU B 2 12  ? 31.143 14.403  53.155 1.00 85.09  ? 5   GLU N CD  1 
ATOM   2826 O  OE1 . GLU B 2 12  ? 31.847 14.822  52.206 1.00 77.84  ? 5   GLU N OE1 1 
ATOM   2827 O  OE2 . GLU B 2 12  ? 31.175 14.921  54.293 1.00 78.10  ? 5   GLU N OE2 1 
ATOM   2828 N  N   . GLN B 2 13  ? 28.166 13.226  49.251 1.00 51.73  ? 6   GLN N N   1 
ATOM   2829 C  CA  . GLN B 2 13  ? 27.157 14.122  48.710 1.00 62.49  ? 6   GLN N CA  1 
ATOM   2830 C  C   . GLN B 2 13  ? 25.871 13.386  48.367 1.00 64.57  ? 6   GLN N C   1 
ATOM   2831 O  O   . GLN B 2 13  ? 24.789 13.973  48.464 1.00 61.12  ? 6   GLN N O   1 
ATOM   2832 C  CB  . GLN B 2 13  ? 27.702 14.852  47.484 1.00 64.91  ? 6   GLN N CB  1 
ATOM   2833 C  CG  . GLN B 2 13  ? 29.102 15.393  47.666 1.00 73.10  ? 6   GLN N CG  1 
ATOM   2834 C  CD  . GLN B 2 13  ? 29.525 16.263  46.509 1.00 73.68  ? 6   GLN N CD  1 
ATOM   2835 O  OE1 . GLN B 2 13  ? 30.131 15.788  45.546 1.00 66.12  ? 6   GLN N OE1 1 
ATOM   2836 N  NE2 . GLN B 2 13  ? 29.204 17.551  46.590 1.00 82.94  ? 6   GLN N NE2 1 
ATOM   2837 N  N   . ILE B 2 14  ? 25.974 12.119  47.951 1.00 60.71  ? 7   ILE N N   1 
ATOM   2838 C  CA  . ILE B 2 14  ? 24.785 11.296  47.744 1.00 51.84  ? 7   ILE N CA  1 
ATOM   2839 C  C   . ILE B 2 14  ? 23.926 11.306  49.001 1.00 45.72  ? 7   ILE N C   1 
ATOM   2840 O  O   . ILE B 2 14  ? 22.710 11.519  48.943 1.00 50.48  ? 7   ILE N O   1 
ATOM   2841 C  CB  . ILE B 2 14  ? 25.178 9.855   47.353 1.00 52.06  ? 7   ILE N CB  1 
ATOM   2842 C  CG1 . ILE B 2 14  ? 25.973 9.804   46.040 1.00 54.83  ? 7   ILE N CG1 1 
ATOM   2843 C  CG2 . ILE B 2 14  ? 23.958 8.974   47.277 1.00 48.90  ? 7   ILE N CG2 1 
ATOM   2844 C  CD1 . ILE B 2 14  ? 25.610 10.851  45.028 1.00 50.62  ? 7   ILE N CD1 1 
ATOM   2845 N  N   . ALA B 2 15  ? 24.554 11.078  50.161 1.00 39.99  ? 8   ALA N N   1 
ATOM   2846 C  CA  . ALA B 2 15  ? 23.798 11.057  51.411 1.00 41.14  ? 8   ALA N CA  1 
ATOM   2847 C  C   . ALA B 2 15  ? 23.164 12.417  51.696 1.00 50.66  ? 8   ALA N C   1 
ATOM   2848 O  O   . ALA B 2 15  ? 22.008 12.495  52.130 1.00 59.46  ? 8   ALA N O   1 
ATOM   2849 C  CB  . ALA B 2 15  ? 24.706 10.627  52.560 1.00 39.69  ? 8   ALA N CB  1 
ATOM   2850 N  N   . GLU B 2 16  ? 23.912 13.502  51.452 1.00 55.80  ? 9   GLU N N   1 
ATOM   2851 C  CA  . GLU B 2 16  ? 23.376 14.845  51.640 1.00 61.99  ? 9   GLU N CA  1 
ATOM   2852 C  C   . GLU B 2 16  ? 22.138 15.065  50.779 1.00 54.86  ? 9   GLU N C   1 
ATOM   2853 O  O   . GLU B 2 16  ? 21.153 15.669  51.222 1.00 46.54  ? 9   GLU N O   1 
ATOM   2854 C  CB  . GLU B 2 16  ? 24.455 15.880  51.315 1.00 69.15  ? 9   GLU N CB  1 
ATOM   2855 C  CG  . GLU B 2 16  ? 25.001 16.641  52.528 1.00 73.77  ? 9   GLU N CG  1 
ATOM   2856 C  CD  . GLU B 2 16  ? 25.494 18.048  52.169 1.00 81.30  ? 9   GLU N CD  1 
ATOM   2857 O  OE1 . GLU B 2 16  ? 26.616 18.169  51.603 1.00 58.88  ? 9   GLU N OE1 1 
ATOM   2858 O  OE2 . GLU B 2 16  ? 24.765 19.026  52.477 1.00 72.90  ? 9   GLU N OE2 1 
ATOM   2859 N  N   . PHE B 2 17  ? 22.172 14.567  49.549 1.00 46.36  ? 10  PHE N N   1 
ATOM   2860 C  CA  . PHE B 2 17  ? 21.010 14.615  48.674 1.00 45.15  ? 10  PHE N CA  1 
ATOM   2861 C  C   . PHE B 2 17  ? 19.892 13.684  49.138 1.00 45.93  ? 10  PHE N C   1 
ATOM   2862 O  O   . PHE B 2 17  ? 18.710 13.998  48.936 1.00 44.69  ? 10  PHE N O   1 
ATOM   2863 C  CB  . PHE B 2 17  ? 21.439 14.267  47.257 1.00 49.98  ? 10  PHE N CB  1 
ATOM   2864 C  CG  . PHE B 2 17  ? 22.101 15.391  46.550 1.00 55.11  ? 10  PHE N CG  1 
ATOM   2865 C  CD1 . PHE B 2 17  ? 23.012 15.140  45.537 1.00 60.14  ? 10  PHE N CD1 1 
ATOM   2866 C  CD2 . PHE B 2 17  ? 21.807 16.702  46.878 1.00 58.91  ? 10  PHE N CD2 1 
ATOM   2867 C  CE1 . PHE B 2 17  ? 23.629 16.176  44.875 1.00 62.40  ? 10  PHE N CE1 1 
ATOM   2868 C  CE2 . PHE B 2 17  ? 22.422 17.747  46.220 1.00 55.73  ? 10  PHE N CE2 1 
ATOM   2869 C  CZ  . PHE B 2 17  ? 23.335 17.483  45.216 1.00 57.62  ? 10  PHE N CZ  1 
ATOM   2870 N  N   . LYS B 2 18  ? 20.223 12.542  49.750 1.00 41.45  ? 11  LYS N N   1 
ATOM   2871 C  CA  . LYS B 2 18  ? 19.158 11.686  50.270 1.00 49.10  ? 11  LYS N CA  1 
ATOM   2872 C  C   . LYS B 2 18  ? 18.400 12.402  51.375 1.00 49.92  ? 11  LYS N C   1 
ATOM   2873 O  O   . LYS B 2 18  ? 17.164 12.325  51.445 1.00 40.08  ? 11  LYS N O   1 
ATOM   2874 C  CB  . LYS B 2 18  ? 19.719 10.352  50.771 1.00 46.23  ? 11  LYS N CB  1 
ATOM   2875 N  N   . GLU B 2 19  ? 19.127 13.134  52.229 1.00 49.05  ? 12  GLU N N   1 
ATOM   2876 C  CA  . GLU B 2 19  ? 18.477 13.985  53.221 1.00 53.40  ? 12  GLU N CA  1 
ATOM   2877 C  C   . GLU B 2 19  ? 17.609 15.046  52.546 1.00 47.01  ? 12  GLU N C   1 
ATOM   2878 O  O   . GLU B 2 19  ? 16.457 15.267  52.946 1.00 36.72  ? 12  GLU N O   1 
ATOM   2879 C  CB  . GLU B 2 19  ? 19.530 14.636  54.121 1.00 57.12  ? 12  GLU N CB  1 
ATOM   2880 C  CG  . GLU B 2 19  ? 19.065 14.814  55.544 1.00 63.30  ? 12  GLU N CG  1 
ATOM   2881 C  CD  . GLU B 2 19  ? 19.715 15.995  56.243 1.00 66.79  ? 12  GLU N CD  1 
ATOM   2882 O  OE1 . GLU B 2 19  ? 20.964 16.036  56.354 1.00 64.35  ? 12  GLU N OE1 1 
ATOM   2883 O  OE2 . GLU B 2 19  ? 18.961 16.884  56.688 1.00 72.31  ? 12  GLU N OE2 1 
ATOM   2884 N  N   . ALA B 2 20  ? 18.129 15.698  51.501 1.00 40.93  ? 13  ALA N N   1 
ATOM   2885 C  CA  . ALA B 2 20  ? 17.303 16.663  50.786 1.00 43.02  ? 13  ALA N CA  1 
ATOM   2886 C  C   . ALA B 2 20  ? 16.089 15.986  50.154 1.00 37.38  ? 13  ALA N C   1 
ATOM   2887 O  O   . ALA B 2 20  ? 14.992 16.554  50.145 1.00 34.24  ? 13  ALA N O   1 
ATOM   2888 C  CB  . ALA B 2 20  ? 18.134 17.393  49.740 1.00 45.63  ? 13  ALA N CB  1 
ATOM   2889 N  N   . PHE B 2 21  ? 16.255 14.759  49.649 1.00 40.56  ? 14  PHE N N   1 
ATOM   2890 C  CA  . PHE B 2 21  ? 15.104 14.010  49.142 1.00 40.37  ? 14  PHE N CA  1 
ATOM   2891 C  C   . PHE B 2 21  ? 14.031 13.850  50.217 1.00 41.62  ? 14  PHE N C   1 
ATOM   2892 O  O   . PHE B 2 21  ? 12.829 13.990  49.938 1.00 36.66  ? 14  PHE N O   1 
ATOM   2893 C  CB  . PHE B 2 21  ? 15.552 12.643  48.625 1.00 38.98  ? 14  PHE N CB  1 
ATOM   2894 C  CG  . PHE B 2 21  ? 14.469 11.873  47.908 1.00 38.43  ? 14  PHE N CG  1 
ATOM   2895 C  CD1 . PHE B 2 21  ? 14.228 12.081  46.545 1.00 39.83  ? 14  PHE N CD1 1 
ATOM   2896 C  CD2 . PHE B 2 21  ? 13.692 10.937  48.586 1.00 39.54  ? 14  PHE N CD2 1 
ATOM   2897 C  CE1 . PHE B 2 21  ? 13.226 11.368  45.874 1.00 36.93  ? 14  PHE N CE1 1 
ATOM   2898 C  CE2 . PHE B 2 21  ? 12.687 10.221  47.928 1.00 41.57  ? 14  PHE N CE2 1 
ATOM   2899 C  CZ  . PHE B 2 21  ? 12.454 10.434  46.562 1.00 38.01  ? 14  PHE N CZ  1 
ATOM   2900 N  N   . SER B 2 22  ? 14.462 13.604  51.463 1.00 41.90  ? 15  SER N N   1 
ATOM   2901 C  CA  . SER B 2 22  ? 13.550 13.288  52.556 1.00 44.78  ? 15  SER N CA  1 
ATOM   2902 C  C   . SER B 2 22  ? 12.678 14.470  52.949 1.00 44.36  ? 15  SER N C   1 
ATOM   2903 O  O   . SER B 2 22  ? 11.531 14.274  53.370 1.00 44.43  ? 15  SER N O   1 
ATOM   2904 C  CB  . SER B 2 22  ? 14.351 12.800  53.756 1.00 44.87  ? 15  SER N CB  1 
ATOM   2905 O  OG  . SER B 2 22  ? 14.439 11.390  53.713 1.00 48.22  ? 15  SER N OG  1 
ATOM   2906 N  N   . LEU B 2 23  ? 13.199 15.694  52.817 1.00 44.82  ? 16  LEU N N   1 
ATOM   2907 C  CA  . LEU B 2 23  ? 12.379 16.880  53.032 1.00 41.33  ? 16  LEU N CA  1 
ATOM   2908 C  C   . LEU B 2 23  ? 11.078 16.811  52.238 1.00 40.02  ? 16  LEU N C   1 
ATOM   2909 O  O   . LEU B 2 23  ? 10.002 17.133  52.757 1.00 40.96  ? 16  LEU N O   1 
ATOM   2910 C  CB  . LEU B 2 23  ? 13.171 18.130  52.650 1.00 40.96  ? 16  LEU N CB  1 
ATOM   2911 C  CG  . LEU B 2 23  ? 12.577 19.469  53.085 1.00 40.01  ? 16  LEU N CG  1 
ATOM   2912 C  CD1 . LEU B 2 23  ? 12.436 19.544  54.612 1.00 44.29  ? 16  LEU N CD1 1 
ATOM   2913 C  CD2 . LEU B 2 23  ? 13.398 20.614  52.557 1.00 41.20  ? 16  LEU N CD2 1 
ATOM   2914 N  N   . PHE B 2 24  ? 11.152 16.383  50.978 1.00 34.49  ? 17  PHE N N   1 
ATOM   2915 C  CA  . PHE B 2 24  ? 9.935  16.284  50.180 1.00 36.19  ? 17  PHE N CA  1 
ATOM   2916 C  C   . PHE B 2 24  ? 9.174  14.987  50.456 1.00 38.50  ? 17  PHE N C   1 
ATOM   2917 O  O   . PHE B 2 24  ? 7.939  14.986  50.501 1.00 42.02  ? 17  PHE N O   1 
ATOM   2918 C  CB  . PHE B 2 24  ? 10.273 16.388  48.691 1.00 35.28  ? 17  PHE N CB  1 
ATOM   2919 C  CG  . PHE B 2 24  ? 11.064 17.605  48.330 1.00 35.15  ? 17  PHE N CG  1 
ATOM   2920 C  CD1 . PHE B 2 24  ? 10.428 18.810  48.069 1.00 37.00  ? 17  PHE N CD1 1 
ATOM   2921 C  CD2 . PHE B 2 24  ? 12.444 17.549  48.248 1.00 35.78  ? 17  PHE N CD2 1 
ATOM   2922 C  CE1 . PHE B 2 24  ? 11.151 19.937  47.727 1.00 35.65  ? 17  PHE N CE1 1 
ATOM   2923 C  CE2 . PHE B 2 24  ? 13.179 18.672  47.918 1.00 37.91  ? 17  PHE N CE2 1 
ATOM   2924 C  CZ  . PHE B 2 24  ? 12.536 19.866  47.652 1.00 42.07  ? 17  PHE N CZ  1 
ATOM   2925 N  N   . ASP B 2 25  ? 9.890  13.873  50.615 1.00 41.45  ? 18  ASP N N   1 
ATOM   2926 C  CA  . ASP B 2 25  ? 9.274  12.551  50.779 1.00 45.93  ? 18  ASP N CA  1 
ATOM   2927 C  C   . ASP B 2 25  ? 8.906  12.367  52.248 1.00 42.93  ? 18  ASP N C   1 
ATOM   2928 O  O   . ASP B 2 25  ? 9.463  11.536  52.969 1.00 44.23  ? 18  ASP N O   1 
ATOM   2929 C  CB  . ASP B 2 25  ? 10.213 11.439  50.306 1.00 47.28  ? 18  ASP N CB  1 
ATOM   2930 C  CG  . ASP B 2 25  ? 9.548  10.040  50.310 1.00 47.04  ? 18  ASP N CG  1 
ATOM   2931 O  OD1 . ASP B 2 25  ? 8.307  9.955   50.392 1.00 47.15  ? 18  ASP N OD1 1 
ATOM   2932 O  OD2 . ASP B 2 25  ? 10.262 9.020   50.211 1.00 45.17  ? 18  ASP N OD2 1 
ATOM   2933 N  N   . LYS B 2 26  ? 7.934  13.164  52.687 1.00 44.03  ? 19  LYS N N   1 
ATOM   2934 C  CA  . LYS B 2 26  ? 7.676  13.248  54.119 1.00 50.04  ? 19  LYS N CA  1 
ATOM   2935 C  C   . LYS B 2 26  ? 7.113  11.945  54.672 1.00 49.87  ? 19  LYS N C   1 
ATOM   2936 O  O   . LYS B 2 26  ? 7.305  11.652  55.856 1.00 51.62  ? 19  LYS N O   1 
ATOM   2937 C  CB  . LYS B 2 26  ? 6.746  14.420  54.415 1.00 54.28  ? 19  LYS N CB  1 
ATOM   2938 C  CG  . LYS B 2 26  ? 7.361  15.766  54.101 1.00 53.20  ? 19  LYS N CG  1 
ATOM   2939 C  CD  . LYS B 2 26  ? 7.578  16.590  55.351 1.00 53.93  ? 19  LYS N CD  1 
ATOM   2940 C  CE  . LYS B 2 26  ? 7.634  18.067  55.002 1.00 56.28  ? 19  LYS N CE  1 
ATOM   2941 N  NZ  . LYS B 2 26  ? 9.014  18.626  55.131 1.00 62.16  ? 19  LYS N NZ  1 
ATOM   2942 N  N   . ASP B 2 27  ? 6.437  11.146  53.846 1.00 48.84  ? 20  ASP N N   1 
ATOM   2943 C  CA  . ASP B 2 27  ? 5.976  9.835   54.272 1.00 49.99  ? 20  ASP N CA  1 
ATOM   2944 C  C   . ASP B 2 27  ? 7.002  8.748   53.991 1.00 54.74  ? 20  ASP N C   1 
ATOM   2945 O  O   . ASP B 2 27  ? 6.718  7.568   54.224 1.00 56.44  ? 20  ASP N O   1 
ATOM   2946 C  CB  . ASP B 2 27  ? 4.639  9.492   53.600 1.00 47.70  ? 20  ASP N CB  1 
ATOM   2947 C  CG  . ASP B 2 27  ? 4.730  9.471   52.094 1.00 51.02  ? 20  ASP N CG  1 
ATOM   2948 O  OD1 . ASP B 2 27  ? 5.855  9.497   51.559 1.00 51.38  ? 20  ASP N OD1 1 
ATOM   2949 O  OD2 . ASP B 2 27  ? 3.667  9.436   51.434 1.00 50.51  ? 20  ASP N OD2 1 
ATOM   2950 N  N   . GLY B 2 28  ? 8.165  9.124   53.471 1.00 52.20  ? 21  GLY N N   1 
ATOM   2951 C  CA  . GLY B 2 28  ? 9.259  8.184   53.288 1.00 51.99  ? 21  GLY N CA  1 
ATOM   2952 C  C   . GLY B 2 28  ? 8.894  6.932   52.526 1.00 50.32  ? 21  GLY N C   1 
ATOM   2953 O  O   . GLY B 2 28  ? 9.312  5.832   52.910 1.00 53.81  ? 21  GLY N O   1 
ATOM   2954 N  N   . ASP B 2 29  ? 8.118  7.062   51.454 1.00 52.28  ? 22  ASP N N   1 
ATOM   2955 C  CA  . ASP B 2 29  ? 7.788  5.898   50.642 1.00 53.51  ? 22  ASP N CA  1 
ATOM   2956 C  C   . ASP B 2 29  ? 8.677  5.784   49.409 1.00 51.57  ? 22  ASP N C   1 
ATOM   2957 O  O   . ASP B 2 29  ? 8.374  4.995   48.506 1.00 50.59  ? 22  ASP N O   1 
ATOM   2958 C  CB  . ASP B 2 29  ? 6.299  5.911   50.258 1.00 56.05  ? 22  ASP N CB  1 
ATOM   2959 C  CG  . ASP B 2 29  ? 5.960  6.943   49.195 1.00 57.48  ? 22  ASP N CG  1 
ATOM   2960 O  OD1 . ASP B 2 29  ? 6.697  7.944   49.067 1.00 50.13  ? 22  ASP N OD1 1 
ATOM   2961 O  OD2 . ASP B 2 29  ? 4.943  6.752   48.482 1.00 48.62  ? 22  ASP N OD2 1 
ATOM   2962 N  N   . GLY B 2 30  ? 9.770  6.547   49.357 1.00 48.98  ? 23  GLY N N   1 
ATOM   2963 C  CA  . GLY B 2 30  ? 10.679 6.517   48.231 1.00 42.93  ? 23  GLY N CA  1 
ATOM   2964 C  C   . GLY B 2 30  ? 10.254 7.310   47.013 1.00 43.02  ? 23  GLY N C   1 
ATOM   2965 O  O   . GLY B 2 30  ? 10.939 7.242   45.990 1.00 39.11  ? 23  GLY N O   1 
ATOM   2966 N  N   . THR B 2 31  ? 9.151  8.056   47.077 1.00 47.30  ? 24  THR N N   1 
ATOM   2967 C  CA  . THR B 2 31  ? 8.670  8.834   45.942 1.00 52.05  ? 24  THR N CA  1 
ATOM   2968 C  C   . THR B 2 31  ? 8.247  10.224  46.399 1.00 50.00  ? 24  THR N C   1 
ATOM   2969 O  O   . THR B 2 31  ? 7.747  10.393  47.515 1.00 50.02  ? 24  THR N O   1 
ATOM   2970 C  CB  . THR B 2 31  ? 7.461  8.179   45.246 1.00 60.93  ? 24  THR N CB  1 
ATOM   2971 O  OG1 . THR B 2 31  ? 6.257  8.630   45.880 1.00 52.81  ? 24  THR N OG1 1 
ATOM   2972 C  CG2 . THR B 2 31  ? 7.533  6.657   45.321 1.00 62.25  ? 24  THR N CG2 1 
ATOM   2973 N  N   . ILE B 2 32  ? 8.422  11.215  45.516 1.00 44.19  ? 25  ILE N N   1 
ATOM   2974 C  CA  . ILE B 2 32  ? 7.947  12.581  45.746 1.00 41.47  ? 25  ILE N CA  1 
ATOM   2975 C  C   . ILE B 2 32  ? 6.722  12.812  44.862 1.00 44.00  ? 25  ILE N C   1 
ATOM   2976 O  O   . ILE B 2 32  ? 6.816  12.753  43.624 1.00 45.31  ? 25  ILE N O   1 
ATOM   2977 C  CB  . ILE B 2 32  ? 9.036  13.642  45.475 1.00 36.81  ? 25  ILE N CB  1 
ATOM   2978 C  CG1 . ILE B 2 32  ? 10.320 13.373  46.261 1.00 34.44  ? 25  ILE N CG1 1 
ATOM   2979 C  CG2 . ILE B 2 32  ? 8.530  15.034  45.864 1.00 41.66  ? 25  ILE N CG2 1 
ATOM   2980 C  CD1 . ILE B 2 32  ? 11.438 14.382  45.992 1.00 33.52  ? 25  ILE N CD1 1 
ATOM   2981 N  N   . THR B 2 33  ? 5.576  13.066  45.493 1.00 41.39  ? 26  THR N N   1 
ATOM   2982 C  CA  . THR B 2 33  ? 4.337  13.404  44.798 1.00 41.59  ? 26  THR N CA  1 
ATOM   2983 C  C   . THR B 2 33  ? 4.267  14.904  44.533 1.00 38.57  ? 26  THR N C   1 
ATOM   2984 O  O   . THR B 2 33  ? 5.030  15.698  45.093 1.00 37.33  ? 26  THR N O   1 
ATOM   2985 C  CB  . THR B 2 33  ? 3.120  13.007  45.632 1.00 44.63  ? 26  THR N CB  1 
ATOM   2986 O  OG1 . THR B 2 33  ? 3.140  13.743  46.870 1.00 41.76  ? 26  THR N OG1 1 
ATOM   2987 C  CG2 . THR B 2 33  ? 3.100  11.505  45.901 1.00 45.58  ? 26  THR N CG2 1 
ATOM   2988 N  N   . THR B 2 34  ? 3.301  15.313  43.711 1.00 38.03  ? 27  THR N N   1 
ATOM   2989 C  CA  . THR B 2 34  ? 3.101  16.755  43.581 1.00 38.84  ? 27  THR N CA  1 
ATOM   2990 C  C   . THR B 2 34  ? 2.522  17.337  44.855 1.00 36.90  ? 27  THR N C   1 
ATOM   2991 O  O   . THR B 2 34  ? 2.831  18.481  45.206 1.00 37.78  ? 27  THR N O   1 
ATOM   2992 C  CB  . THR B 2 34  ? 2.200  17.108  42.395 1.00 42.76  ? 27  THR N CB  1 
ATOM   2993 O  OG1 . THR B 2 34  ? 0.842  16.803  42.719 1.00 42.86  ? 27  THR N OG1 1 
ATOM   2994 C  CG2 . THR B 2 34  ? 2.621  16.344  41.151 1.00 47.23  ? 27  THR N CG2 1 
ATOM   2995 N  N   . LYS B 2 35  ? 1.686  16.569  45.559 1.00 42.35  ? 28  LYS N N   1 
ATOM   2996 C  CA  . LYS B 2 35  ? 1.182  17.038  46.842 1.00 44.35  ? 28  LYS N CA  1 
ATOM   2997 C  C   . LYS B 2 35  ? 2.332  17.286  47.813 1.00 33.09  ? 28  LYS N C   1 
ATOM   2998 O  O   . LYS B 2 35  ? 2.377  18.321  48.485 1.00 33.56  ? 28  LYS N O   1 
ATOM   2999 C  CB  . LYS B 2 35  ? 0.176  16.039  47.408 1.00 50.75  ? 28  LYS N CB  1 
ATOM   3000 C  CG  . LYS B 2 35  ? -0.729 16.598  48.489 1.00 63.80  ? 28  LYS N CG  1 
ATOM   3001 C  CD  . LYS B 2 35  ? -1.906 15.665  48.764 1.00 76.78  ? 28  LYS N CD  1 
ATOM   3002 C  CE  . LYS B 2 35  ? -1.448 14.214  48.874 1.00 81.84  ? 28  LYS N CE  1 
ATOM   3003 N  NZ  . LYS B 2 35  ? -2.393 13.266  48.215 1.00 82.70  ? 28  LYS N NZ  1 
ATOM   3004 N  N   . GLU B 2 36  ? 3.305  16.385  47.852 1.00 35.54  ? 29  GLU N N   1 
ATOM   3005 C  CA  . GLU B 2 36  ? 4.453  16.604  48.737 1.00 37.01  ? 29  GLU N CA  1 
ATOM   3006 C  C   . GLU B 2 36  ? 5.272  17.814  48.302 1.00 34.60  ? 29  GLU N C   1 
ATOM   3007 O  O   . GLU B 2 36  ? 5.777  18.569  49.145 1.00 36.99  ? 29  GLU N O   1 
ATOM   3008 C  CB  . GLU B 2 36  ? 5.315  15.351  48.779 1.00 34.25  ? 29  GLU N CB  1 
ATOM   3009 C  CG  . GLU B 2 36  ? 4.651  14.214  49.532 1.00 33.46  ? 29  GLU N CG  1 
ATOM   3010 C  CD  . GLU B 2 36  ? 5.492  12.968  49.503 1.00 35.88  ? 29  GLU N CD  1 
ATOM   3011 O  OE1 . GLU B 2 36  ? 5.897  12.585  48.378 1.00 30.62  ? 29  GLU N OE1 1 
ATOM   3012 O  OE2 . GLU B 2 36  ? 5.761  12.389  50.591 1.00 35.54  ? 29  GLU N OE2 1 
ATOM   3013 N  N   . LEU B 2 37  ? 5.396  18.019  46.986 1.00 32.80  ? 30  LEU N N   1 
ATOM   3014 C  CA  . LEU B 2 37  ? 6.088  19.186  46.457 1.00 36.05  ? 30  LEU N CA  1 
ATOM   3015 C  C   . LEU B 2 37  ? 5.384  20.468  46.858 1.00 35.18  ? 30  LEU N C   1 
ATOM   3016 O  O   . LEU B 2 37  ? 6.024  21.421  47.334 1.00 29.57  ? 30  LEU N O   1 
ATOM   3017 C  CB  . LEU B 2 37  ? 6.181  19.092  44.938 1.00 40.04  ? 30  LEU N CB  1 
ATOM   3018 C  CG  . LEU B 2 37  ? 7.143  20.113  44.357 1.00 47.47  ? 30  LEU N CG  1 
ATOM   3019 C  CD1 . LEU B 2 37  ? 8.502  20.020  45.072 1.00 50.94  ? 30  LEU N CD1 1 
ATOM   3020 C  CD2 . LEU B 2 37  ? 7.282  19.932  42.842 1.00 47.44  ? 30  LEU N CD2 1 
ATOM   3021 N  N   . GLY B 2 38  ? 4.057  20.515  46.658 1.00 33.89  ? 31  GLY N N   1 
ATOM   3022 C  CA  . GLY B 2 38  ? 3.314  21.706  47.004 1.00 31.94  ? 31  GLY N CA  1 
ATOM   3023 C  C   . GLY B 2 38  ? 3.295  21.983  48.495 1.00 31.21  ? 31  GLY N C   1 
ATOM   3024 O  O   . GLY B 2 38  ? 3.263  23.147  48.908 1.00 35.41  ? 31  GLY N O   1 
ATOM   3025 N  N   . THR B 2 39  ? 3.317  20.931  49.323 1.00 28.91  ? 32  THR N N   1 
ATOM   3026 C  CA  . THR B 2 39  ? 3.362  21.142  50.772 1.00 32.35  ? 32  THR N CA  1 
ATOM   3027 C  C   . THR B 2 39  ? 4.645  21.870  51.179 1.00 38.87  ? 32  THR N C   1 
ATOM   3028 O  O   . THR B 2 39  ? 4.610  22.787  52.012 1.00 39.72  ? 32  THR N O   1 
ATOM   3029 C  CB  . THR B 2 39  ? 3.234  19.805  51.513 1.00 33.01  ? 32  THR N CB  1 
ATOM   3030 O  OG1 . THR B 2 39  ? 1.949  19.233  51.259 1.00 32.66  ? 32  THR N OG1 1 
ATOM   3031 C  CG2 . THR B 2 39  ? 3.379  19.969  53.036 1.00 34.99  ? 32  THR N CG2 1 
ATOM   3032 N  N   . VAL B 2 40  ? 5.781  21.508  50.576 1.00 32.53  ? 33  VAL N N   1 
ATOM   3033 C  CA  . VAL B 2 40  ? 7.027  22.159  50.953 1.00 33.99  ? 33  VAL N CA  1 
ATOM   3034 C  C   . VAL B 2 40  ? 7.066  23.585  50.419 1.00 33.23  ? 33  VAL N C   1 
ATOM   3035 O  O   . VAL B 2 40  ? 7.364  24.526  51.161 1.00 28.77  ? 33  VAL N O   1 
ATOM   3036 C  CB  . VAL B 2 40  ? 8.229  21.316  50.489 1.00 36.39  ? 33  VAL N CB  1 
ATOM   3037 C  CG1 . VAL B 2 40  ? 9.459  22.178  50.253 1.00 37.32  ? 33  VAL N CG1 1 
ATOM   3038 C  CG2 . VAL B 2 40  ? 8.508  20.215  51.519 1.00 36.11  ? 33  VAL N CG2 1 
ATOM   3039 N  N   . MET B 2 41  ? 6.700  23.782  49.142 1.00 33.55  ? 34  MET N N   1 
ATOM   3040 C  CA  . MET B 2 41  ? 6.786  25.126  48.577 1.00 34.13  ? 34  MET N CA  1 
ATOM   3041 C  C   . MET B 2 41  ? 5.880  26.104  49.317 1.00 33.65  ? 34  MET N C   1 
ATOM   3042 O  O   . MET B 2 41  ? 6.279  27.248  49.575 1.00 41.76  ? 34  MET N O   1 
ATOM   3043 C  CB  . MET B 2 41  ? 6.436  25.118  47.085 1.00 40.10  ? 34  MET N CB  1 
ATOM   3044 C  CG  . MET B 2 41  ? 7.274  24.162  46.239 1.00 41.44  ? 34  MET N CG  1 
ATOM   3045 S  SD  . MET B 2 41  ? 9.034  24.532  46.043 1.00 56.51  ? 34  MET N SD  1 
ATOM   3046 C  CE  . MET B 2 41  ? 9.191  26.263  46.465 1.00 63.67  ? 34  MET N CE  1 
ATOM   3047 N  N   . ARG B 2 42  ? 4.651  25.688  49.655 1.00 30.91  ? 35  ARG N N   1 
ATOM   3048 C  CA  . ARG B 2 42  ? 3.767  26.600  50.373 1.00 35.51  ? 35  ARG N CA  1 
ATOM   3049 C  C   . ARG B 2 42  ? 4.289  26.851  51.793 1.00 30.71  ? 35  ARG N C   1 
ATOM   3050 O  O   . ARG B 2 42  ? 4.180  27.969  52.306 1.00 37.03  ? 35  ARG N O   1 
ATOM   3051 C  CB  . ARG B 2 42  ? 2.330  26.045  50.369 1.00 36.19  ? 35  ARG N CB  1 
ATOM   3052 C  CG  . ARG B 2 42  ? 1.717  25.985  48.952 1.00 38.92  ? 35  ARG N CG  1 
ATOM   3053 C  CD  . ARG B 2 42  ? 0.230  25.573  48.959 1.00 48.57  ? 35  ARG N CD  1 
ATOM   3054 N  NE  . ARG B 2 42  ? -0.064 24.555  47.957 1.00 51.77  ? 35  ARG N NE  1 
ATOM   3055 C  CZ  . ARG B 2 42  ? -0.366 24.831  46.697 1.00 53.18  ? 35  ARG N CZ  1 
ATOM   3056 N  NH1 . ARG B 2 42  ? -0.438 26.089  46.265 1.00 57.77  ? 35  ARG N NH1 1 
ATOM   3057 N  NH2 . ARG B 2 42  ? -0.561 23.826  45.845 1.00 51.83  ? 35  ARG N NH2 1 
ATOM   3058 N  N   . SER B 2 43  ? 4.920  25.844  52.410 1.00 30.29  ? 36  SER N N   1 
ATOM   3059 C  CA  . SER B 2 43  ? 5.622  26.059  53.676 1.00 34.71  ? 36  SER N CA  1 
ATOM   3060 C  C   . SER B 2 43  ? 6.668  27.168  53.558 1.00 32.72  ? 36  SER N C   1 
ATOM   3061 O  O   . SER B 2 43  ? 6.944  27.881  54.541 1.00 27.37  ? 36  SER N O   1 
ATOM   3062 C  CB  . SER B 2 43  ? 6.264  24.743  54.147 1.00 35.19  ? 36  SER N CB  1 
ATOM   3063 O  OG  . SER B 2 43  ? 5.252  23.793  54.500 1.00 36.86  ? 36  SER N OG  1 
ATOM   3064 N  N   . LEU B 2 44  ? 7.216  27.361  52.354 1.00 31.55  ? 37  LEU N N   1 
ATOM   3065 C  CA  . LEU B 2 44  ? 8.189  28.406  52.084 1.00 33.30  ? 37  LEU N CA  1 
ATOM   3066 C  C   . LEU B 2 44  ? 7.525  29.695  51.609 1.00 36.09  ? 37  LEU N C   1 
ATOM   3067 O  O   . LEU B 2 44  ? 8.207  30.586  51.091 1.00 31.93  ? 37  LEU N O   1 
ATOM   3068 C  CB  . LEU B 2 44  ? 9.227  27.906  51.066 1.00 34.26  ? 37  LEU N CB  1 
ATOM   3069 C  CG  . LEU B 2 44  ? 10.039 26.675  51.531 1.00 33.00  ? 37  LEU N CG  1 
ATOM   3070 C  CD1 . LEU B 2 44  ? 10.973 26.118  50.474 1.00 33.44  ? 37  LEU N CD1 1 
ATOM   3071 C  CD2 . LEU B 2 44  ? 10.836 26.963  52.827 1.00 32.38  ? 37  LEU N CD2 1 
ATOM   3072 N  N   . GLY B 2 45  ? 6.213  29.820  51.786 1.00 40.16  ? 38  GLY N N   1 
ATOM   3073 C  CA  . GLY B 2 45  ? 5.544  31.033  51.382 1.00 36.32  ? 38  GLY N CA  1 
ATOM   3074 C  C   . GLY B 2 45  ? 5.295  31.158  49.897 1.00 40.40  ? 38  GLY N C   1 
ATOM   3075 O  O   . GLY B 2 45  ? 4.879  32.227  49.447 1.00 44.33  ? 38  GLY N O   1 
ATOM   3076 N  N   . GLN B 2 46  ? 5.534  30.108  49.119 1.00 41.87  ? 39  GLN N N   1 
ATOM   3077 C  CA  . GLN B 2 46  ? 5.248  30.157  47.691 1.00 43.05  ? 39  GLN N CA  1 
ATOM   3078 C  C   . GLN B 2 46  ? 3.794  29.765  47.397 1.00 47.08  ? 39  GLN N C   1 
ATOM   3079 O  O   . GLN B 2 46  ? 3.081  29.183  48.224 1.00 41.00  ? 39  GLN N O   1 
ATOM   3080 C  CB  . GLN B 2 46  ? 6.208  29.253  46.916 1.00 44.42  ? 39  GLN N CB  1 
ATOM   3081 C  CG  . GLN B 2 46  ? 7.673  29.422  47.311 1.00 46.30  ? 39  GLN N CG  1 
ATOM   3082 C  CD  . GLN B 2 46  ? 8.119  30.866  47.259 1.00 46.22  ? 39  GLN N CD  1 
ATOM   3083 O  OE1 . GLN B 2 46  ? 8.070  31.509  46.207 1.00 46.22  ? 39  GLN N OE1 1 
ATOM   3084 N  NE2 . GLN B 2 46  ? 8.550  31.392  48.397 1.00 48.02  ? 39  GLN N NE2 1 
ATOM   3085 N  N   . ASN B 2 47  ? 3.373  30.063  46.168 1.00 50.63  ? 40  ASN N N   1 
ATOM   3086 C  CA  . ASN B 2 47  ? 1.976  29.944  45.752 1.00 48.75  ? 40  ASN N CA  1 
ATOM   3087 C  C   . ASN B 2 47  ? 1.872  29.249  44.390 1.00 50.01  ? 40  ASN N C   1 
ATOM   3088 O  O   . ASN B 2 47  ? 1.340  29.814  43.429 1.00 51.62  ? 40  ASN N O   1 
ATOM   3089 C  CB  . ASN B 2 47  ? 1.370  31.348  45.723 1.00 51.08  ? 40  ASN N CB  1 
ATOM   3090 C  CG  . ASN B 2 47  ? -0.097 31.366  45.341 1.00 59.72  ? 40  ASN N CG  1 
ATOM   3091 O  OD1 . ASN B 2 47  ? -0.821 30.379  45.523 1.00 51.18  ? 40  ASN N OD1 1 
ATOM   3092 N  ND2 . ASN B 2 47  ? -0.550 32.507  44.815 1.00 61.70  ? 40  ASN N ND2 1 
ATOM   3093 N  N   . PRO B 2 48  ? 2.377  28.019  44.263 1.00 46.15  ? 41  PRO N N   1 
ATOM   3094 C  CA  . PRO B 2 48  ? 2.269  27.317  42.975 1.00 42.94  ? 41  PRO N CA  1 
ATOM   3095 C  C   . PRO B 2 48  ? 0.881  26.759  42.698 1.00 47.04  ? 41  PRO N C   1 
ATOM   3096 O  O   . PRO B 2 48  ? 0.159  26.327  43.599 1.00 44.58  ? 41  PRO N O   1 
ATOM   3097 C  CB  . PRO B 2 48  ? 3.277  26.166  43.107 1.00 41.77  ? 41  PRO N CB  1 
ATOM   3098 C  CG  . PRO B 2 48  ? 3.308  25.879  44.573 1.00 41.50  ? 41  PRO N CG  1 
ATOM   3099 C  CD  . PRO B 2 48  ? 3.171  27.241  45.237 1.00 44.16  ? 41  PRO N CD  1 
ATOM   3100 N  N   . THR B 2 49  ? 0.538  26.729  41.405 1.00 46.26  ? 42  THR N N   1 
ATOM   3101 C  CA  . THR B 2 49  ? -0.646 26.024  40.939 1.00 43.98  ? 42  THR N CA  1 
ATOM   3102 C  C   . THR B 2 49  ? -0.359 24.529  40.798 1.00 47.95  ? 42  THR N C   1 
ATOM   3103 O  O   . THR B 2 49  ? 0.793  24.089  40.754 1.00 50.04  ? 42  THR N O   1 
ATOM   3104 C  CB  . THR B 2 49  ? -1.114 26.592  39.596 1.00 54.94  ? 42  THR N CB  1 
ATOM   3105 O  OG1 . THR B 2 49  ? -0.076 26.438  38.611 1.00 46.61  ? 42  THR N OG1 1 
ATOM   3106 C  CG2 . THR B 2 49  ? -1.477 28.072  39.726 1.00 51.62  ? 42  THR N CG2 1 
ATOM   3107 N  N   . GLU B 2 50  ? -1.433 23.739  40.737 1.00 44.59  ? 43  GLU N N   1 
ATOM   3108 C  CA  . GLU B 2 50  ? -1.288 22.314  40.458 1.00 46.98  ? 43  GLU N CA  1 
ATOM   3109 C  C   . GLU B 2 50  ? -0.604 22.079  39.114 1.00 51.40  ? 43  GLU N C   1 
ATOM   3110 O  O   . GLU B 2 50  ? 0.141  21.105  38.961 1.00 62.88  ? 43  GLU N O   1 
ATOM   3111 C  CB  . GLU B 2 50  ? -2.665 21.637  40.509 1.00 49.95  ? 43  GLU N CB  1 
ATOM   3112 C  CG  . GLU B 2 50  ? -2.706 20.130  40.243 1.00 57.39  ? 43  GLU N CG  1 
ATOM   3113 C  CD  . GLU B 2 50  ? -1.744 19.303  41.090 1.00 65.56  ? 43  GLU N CD  1 
ATOM   3114 O  OE1 . GLU B 2 50  ? -1.532 19.641  42.279 1.00 67.68  ? 43  GLU N OE1 1 
ATOM   3115 O  OE2 . GLU B 2 50  ? -1.220 18.287  40.567 1.00 70.13  ? 43  GLU N OE2 1 
ATOM   3116 N  N   . ALA B 2 51  ? -0.822 22.966  38.138 1.00 46.80  ? 44  ALA N N   1 
ATOM   3117 C  CA  . ALA B 2 51  ? -0.160 22.817  36.845 1.00 47.16  ? 44  ALA N CA  1 
ATOM   3118 C  C   . ALA B 2 51  ? 1.346  23.021  36.974 1.00 48.24  ? 44  ALA N C   1 
ATOM   3119 O  O   . ALA B 2 51  ? 2.137  22.244  36.423 1.00 48.29  ? 44  ALA N O   1 
ATOM   3120 C  CB  . ALA B 2 51  ? -0.743 23.803  35.839 1.00 43.11  ? 44  ALA N CB  1 
ATOM   3121 N  N   . GLU B 2 52  ? 1.758  24.071  37.693 1.00 44.15  ? 45  GLU N N   1 
ATOM   3122 C  CA  . GLU B 2 52  ? 3.181  24.310  37.894 1.00 45.31  ? 45  GLU N CA  1 
ATOM   3123 C  C   . GLU B 2 52  ? 3.797  23.201  38.731 1.00 47.54  ? 45  GLU N C   1 
ATOM   3124 O  O   . GLU B 2 52  ? 4.955  22.824  38.507 1.00 50.09  ? 45  GLU N O   1 
ATOM   3125 C  CB  . GLU B 2 52  ? 3.411  25.672  38.559 1.00 46.03  ? 45  GLU N CB  1 
ATOM   3126 C  CG  . GLU B 2 52  ? 2.831  26.868  37.808 1.00 50.02  ? 45  GLU N CG  1 
ATOM   3127 C  CD  . GLU B 2 52  ? 2.769  28.137  38.663 1.00 52.18  ? 45  GLU N CD  1 
ATOM   3128 O  OE1 . GLU B 2 52  ? 2.569  28.024  39.901 1.00 54.03  ? 45  GLU N OE1 1 
ATOM   3129 O  OE2 . GLU B 2 52  ? 2.938  29.253  38.099 1.00 52.65  ? 45  GLU N OE2 1 
ATOM   3130 N  N   . LEU B 2 53  ? 3.032  22.663  39.688 1.00 45.55  ? 46  LEU N N   1 
ATOM   3131 C  CA  . LEU B 2 53  ? 3.485  21.508  40.452 1.00 47.82  ? 46  LEU N CA  1 
ATOM   3132 C  C   . LEU B 2 53  ? 3.696  20.304  39.543 1.00 50.34  ? 46  LEU N C   1 
ATOM   3133 O  O   . LEU B 2 53  ? 4.740  19.641  39.608 1.00 46.65  ? 46  LEU N O   1 
ATOM   3134 C  CB  . LEU B 2 53  ? 2.477  21.177  41.553 1.00 43.51  ? 46  LEU N CB  1 
ATOM   3135 C  CG  . LEU B 2 53  ? 2.541  22.059  42.797 1.00 45.74  ? 46  LEU N CG  1 
ATOM   3136 C  CD1 . LEU B 2 53  ? 1.599  21.550  43.886 1.00 46.53  ? 46  LEU N CD1 1 
ATOM   3137 C  CD2 . LEU B 2 53  ? 3.971  22.148  43.303 1.00 43.94  ? 46  LEU N CD2 1 
ATOM   3138 N  N   . GLN B 2 54  ? 2.709  20.000  38.687 1.00 48.76  ? 47  GLN N N   1 
ATOM   3139 C  CA  . GLN B 2 54  ? 2.852  18.848  37.798 1.00 52.93  ? 47  GLN N CA  1 
ATOM   3140 C  C   . GLN B 2 54  ? 4.039  19.026  36.861 1.00 51.53  ? 47  GLN N C   1 
ATOM   3141 O  O   . GLN B 2 54  ? 4.839  18.100  36.690 1.00 51.35  ? 47  GLN N O   1 
ATOM   3142 C  CB  . GLN B 2 54  ? 1.566  18.602  37.006 1.00 55.61  ? 47  GLN N CB  1 
ATOM   3143 C  CG  . GLN B 2 54  ? 0.722  17.455  37.549 1.00 69.56  ? 47  GLN N CG  1 
ATOM   3144 C  CD  . GLN B 2 54  ? 1.221  16.083  37.087 1.00 80.12  ? 47  GLN N CD  1 
ATOM   3145 O  OE1 . GLN B 2 54  ? 2.346  15.672  37.406 1.00 79.31  ? 47  GLN N OE1 1 
ATOM   3146 N  NE2 . GLN B 2 54  ? 0.381  15.368  36.334 1.00 82.76  ? 47  GLN N NE2 1 
ATOM   3147 N  N   . ASP B 2 55  ? 4.194  20.225  36.286 1.00 48.92  ? 48  ASP N N   1 
ATOM   3148 C  CA  . ASP B 2 55  ? 5.320  20.497  35.393 1.00 52.03  ? 48  ASP N CA  1 
ATOM   3149 C  C   . ASP B 2 55  ? 6.659  20.264  36.094 1.00 53.32  ? 48  ASP N C   1 
ATOM   3150 O  O   . ASP B 2 55  ? 7.560  19.622  35.544 1.00 56.24  ? 48  ASP N O   1 
ATOM   3151 C  CB  . ASP B 2 55  ? 5.241  21.935  34.874 1.00 52.75  ? 48  ASP N CB  1 
ATOM   3152 C  CG  . ASP B 2 55  ? 4.090  22.153  33.900 1.00 58.17  ? 48  ASP N CG  1 
ATOM   3153 O  OD1 . ASP B 2 55  ? 3.510  21.153  33.413 1.00 61.83  ? 48  ASP N OD1 1 
ATOM   3154 O  OD2 . ASP B 2 55  ? 3.775  23.332  33.615 1.00 57.26  ? 48  ASP N OD2 1 
ATOM   3155 N  N   . MET B 2 56  ? 6.807  20.797  37.311 1.00 52.57  ? 49  MET N N   1 
ATOM   3156 C  CA  . MET B 2 56  ? 8.037  20.624  38.073 1.00 47.35  ? 49  MET N CA  1 
ATOM   3157 C  C   . MET B 2 56  ? 8.394  19.152  38.224 1.00 47.05  ? 49  MET N C   1 
ATOM   3158 O  O   . MET B 2 56  ? 9.576  18.786  38.183 1.00 49.87  ? 49  MET N O   1 
ATOM   3159 C  CB  . MET B 2 56  ? 7.885  21.278  39.446 1.00 44.99  ? 49  MET N CB  1 
ATOM   3160 C  CG  . MET B 2 56  ? 8.092  22.785  39.460 1.00 48.43  ? 49  MET N CG  1 
ATOM   3161 S  SD  . MET B 2 56  ? 7.961  23.476  41.136 1.00 54.58  ? 49  MET N SD  1 
ATOM   3162 C  CE  . MET B 2 56  ? 7.438  25.148  40.786 1.00 58.44  ? 49  MET N CE  1 
ATOM   3163 N  N   . ILE B 2 57  ? 7.394  18.290  38.368 1.00 48.54  ? 50  ILE N N   1 
ATOM   3164 C  CA  . ILE B 2 57  ? 7.671  16.873  38.560 1.00 46.20  ? 50  ILE N CA  1 
ATOM   3165 C  C   . ILE B 2 57  ? 7.873  16.149  37.232 1.00 51.95  ? 50  ILE N C   1 
ATOM   3166 O  O   . ILE B 2 57  ? 8.741  15.275  37.129 1.00 50.38  ? 50  ILE N O   1 
ATOM   3167 C  CB  . ILE B 2 57  ? 6.564  16.227  39.418 1.00 47.68  ? 50  ILE N CB  1 
ATOM   3168 C  CG1 . ILE B 2 57  ? 6.920  16.436  40.884 1.00 52.37  ? 50  ILE N CG1 1 
ATOM   3169 C  CG2 . ILE B 2 57  ? 6.411  14.739  39.138 1.00 48.10  ? 50  ILE N CG2 1 
ATOM   3170 C  CD1 . ILE B 2 57  ? 5.921  15.906  41.818 1.00 53.36  ? 50  ILE N CD1 1 
ATOM   3171 N  N   . ASN B 2 58  ? 7.095  16.477  36.194 1.00 53.36  ? 51  ASN N N   1 
ATOM   3172 C  CA  . ASN B 2 58  ? 7.317  15.835  34.898 1.00 55.80  ? 51  ASN N CA  1 
ATOM   3173 C  C   . ASN B 2 58  ? 8.744  16.078  34.406 1.00 60.10  ? 51  ASN N C   1 
ATOM   3174 O  O   . ASN B 2 58  ? 9.367  15.184  33.824 1.00 63.26  ? 51  ASN N O   1 
ATOM   3175 C  CB  . ASN B 2 58  ? 6.302  16.332  33.872 1.00 49.42  ? 51  ASN N CB  1 
ATOM   3176 C  CG  . ASN B 2 58  ? 4.870  16.234  34.366 1.00 55.75  ? 51  ASN N CG  1 
ATOM   3177 O  OD1 . ASN B 2 58  ? 4.536  15.402  35.219 1.00 57.22  ? 51  ASN N OD1 1 
ATOM   3178 N  ND2 . ASN B 2 58  ? 4.013  17.099  33.837 1.00 53.54  ? 51  ASN N ND2 1 
ATOM   3179 N  N   . GLU B 2 59  ? 9.286  17.270  34.677 1.00 53.66  ? 52  GLU N N   1 
ATOM   3180 C  CA  . GLU B 2 59  ? 10.647 17.609  34.270 1.00 60.20  ? 52  GLU N CA  1 
ATOM   3181 C  C   . GLU B 2 59  ? 11.679 16.617  34.799 1.00 62.06  ? 52  GLU N C   1 
ATOM   3182 O  O   . GLU B 2 59  ? 12.685 16.356  34.129 1.00 59.62  ? 52  GLU N O   1 
ATOM   3183 C  CB  . GLU B 2 59  ? 10.991 19.018  34.752 1.00 57.61  ? 52  GLU N CB  1 
ATOM   3184 C  CG  . GLU B 2 59  ? 12.157 19.646  34.038 1.00 68.60  ? 52  GLU N CG  1 
ATOM   3185 C  CD  . GLU B 2 59  ? 12.533 20.990  34.632 1.00 82.67  ? 52  GLU N CD  1 
ATOM   3186 O  OE1 . GLU B 2 59  ? 11.763 21.507  35.476 1.00 86.23  ? 52  GLU N OE1 1 
ATOM   3187 O  OE2 . GLU B 2 59  ? 13.592 21.537  34.247 1.00 86.04  ? 52  GLU N OE2 1 
ATOM   3188 N  N   . VAL B 2 60  ? 11.451 16.071  35.996 1.00 53.29  ? 53  VAL N N   1 
ATOM   3189 C  CA  . VAL B 2 60  ? 12.401 15.191  36.668 1.00 50.84  ? 53  VAL N CA  1 
ATOM   3190 C  C   . VAL B 2 60  ? 12.005 13.725  36.534 1.00 56.01  ? 53  VAL N C   1 
ATOM   3191 O  O   . VAL B 2 60  ? 12.877 12.846  36.617 1.00 60.63  ? 53  VAL N O   1 
ATOM   3192 C  CB  . VAL B 2 60  ? 12.519 15.580  38.163 1.00 51.12  ? 53  VAL N CB  1 
ATOM   3193 C  CG1 . VAL B 2 60  ? 13.759 14.969  38.810 1.00 50.09  ? 53  VAL N CG1 1 
ATOM   3194 C  CG2 . VAL B 2 60  ? 12.525 17.091  38.322 1.00 50.63  ? 53  VAL N CG2 1 
ATOM   3195 N  N   . ASP B 2 61  ? 10.727 13.440  36.319 1.00 57.69  ? 54  ASP N N   1 
ATOM   3196 C  CA  . ASP B 2 61  ? 10.177 12.088  36.363 1.00 62.73  ? 54  ASP N CA  1 
ATOM   3197 C  C   . ASP B 2 61  ? 10.378 11.437  35.000 1.00 64.98  ? 54  ASP N C   1 
ATOM   3198 O  O   . ASP B 2 61  ? 9.575  11.624  34.080 1.00 80.15  ? 54  ASP N O   1 
ATOM   3199 C  CB  . ASP B 2 61  ? 8.709  12.162  36.773 1.00 61.16  ? 54  ASP N CB  1 
ATOM   3200 C  CG  . ASP B 2 61  ? 7.902  10.968  36.334 1.00 58.40  ? 54  ASP N CG  1 
ATOM   3201 O  OD1 . ASP B 2 61  ? 8.097  9.856   36.872 1.00 59.66  ? 54  ASP N OD1 1 
ATOM   3202 O  OD2 . ASP B 2 61  ? 7.050  11.164  35.445 1.00 57.56  ? 54  ASP N OD2 1 
ATOM   3203 N  N   . ALA B 2 62  ? 11.469 10.682  34.863 1.00 60.72  ? 55  ALA N N   1 
ATOM   3204 C  CA  . ALA B 2 62  ? 11.777 10.005  33.608 1.00 61.55  ? 55  ALA N CA  1 
ATOM   3205 C  C   . ALA B 2 62  ? 10.921 8.764   33.387 1.00 55.96  ? 55  ALA N C   1 
ATOM   3206 O  O   . ALA B 2 62  ? 10.889 8.243   32.267 1.00 54.08  ? 55  ALA N O   1 
ATOM   3207 C  CB  . ALA B 2 62  ? 13.263 9.635   33.564 1.00 54.79  ? 55  ALA N CB  1 
ATOM   3208 N  N   . ASP B 2 63  ? 10.203 8.318   34.425 1.00 61.55  ? 56  ASP N N   1 
ATOM   3209 C  CA  . ASP B 2 63  ? 9.385  7.108   34.414 1.00 63.24  ? 56  ASP N CA  1 
ATOM   3210 C  C   . ASP B 2 63  ? 8.067  7.289   33.671 1.00 63.96  ? 56  ASP N C   1 
ATOM   3211 O  O   . ASP B 2 63  ? 7.607  6.369   32.989 1.00 61.03  ? 56  ASP N O   1 
ATOM   3212 C  CB  . ASP B 2 63  ? 9.073  6.691   35.852 1.00 62.59  ? 56  ASP N CB  1 
ATOM   3213 C  CG  . ASP B 2 63  ? 9.757  5.415   36.246 1.00 58.35  ? 56  ASP N CG  1 
ATOM   3214 O  OD1 . ASP B 2 63  ? 10.554 4.895   35.436 1.00 65.21  ? 56  ASP N OD1 1 
ATOM   3215 O  OD2 . ASP B 2 63  ? 9.496  4.930   37.366 1.00 66.33  ? 56  ASP N OD2 1 
ATOM   3216 N  N   . GLY B 2 64  ? 7.416  8.441   33.834 1.00 65.26  ? 57  GLY N N   1 
ATOM   3217 C  CA  . GLY B 2 64  ? 6.046  8.610   33.407 1.00 66.13  ? 57  GLY N CA  1 
ATOM   3218 C  C   . GLY B 2 64  ? 5.007  8.368   34.487 1.00 63.19  ? 57  GLY N C   1 
ATOM   3219 O  O   . GLY B 2 64  ? 3.878  8.867   34.364 1.00 66.81  ? 57  GLY N O   1 
ATOM   3220 N  N   . ASN B 2 65  ? 5.342  7.618   35.540 1.00 57.24  ? 58  ASN N N   1 
ATOM   3221 C  CA  . ASN B 2 65  ? 4.467  7.618   36.701 1.00 61.39  ? 58  ASN N CA  1 
ATOM   3222 C  C   . ASN B 2 65  ? 4.460  9.025   37.293 1.00 63.22  ? 58  ASN N C   1 
ATOM   3223 O  O   . ASN B 2 65  ? 5.288  9.867   36.961 1.00 76.18  ? 58  ASN N O   1 
ATOM   3224 C  CB  . ASN B 2 65  ? 4.891  6.547   37.712 1.00 63.20  ? 58  ASN N CB  1 
ATOM   3225 C  CG  . ASN B 2 65  ? 6.311  6.749   38.269 1.00 61.03  ? 58  ASN N CG  1 
ATOM   3226 O  OD1 . ASN B 2 65  ? 6.802  7.865   38.400 1.00 64.84  ? 58  ASN N OD1 1 
ATOM   3227 N  ND2 . ASN B 2 65  ? 6.954  5.652   38.629 1.00 56.71  ? 58  ASN N ND2 1 
ATOM   3228 N  N   . GLY B 2 66  ? 3.517  9.296   38.158 1.00 57.11  ? 59  GLY N N   1 
ATOM   3229 C  CA  . GLY B 2 66  ? 3.472  10.708  38.474 1.00 63.98  ? 59  GLY N CA  1 
ATOM   3230 C  C   . GLY B 2 66  ? 4.465  11.223  39.495 1.00 60.96  ? 59  GLY N C   1 
ATOM   3231 O  O   . GLY B 2 66  ? 4.276  12.335  39.993 1.00 55.01  ? 59  GLY N O   1 
ATOM   3232 N  N   . THR B 2 67  ? 5.528  10.483  39.814 1.00 58.38  ? 60  THR N N   1 
ATOM   3233 C  CA  . THR B 2 67  ? 6.335  10.779  40.989 1.00 57.64  ? 60  THR N CA  1 
ATOM   3234 C  C   . THR B 2 67  ? 7.830  10.813  40.659 1.00 56.18  ? 60  THR N C   1 
ATOM   3235 O  O   . THR B 2 67  ? 8.273  10.324  39.620 1.00 55.71  ? 60  THR N O   1 
ATOM   3236 C  CB  . THR B 2 67  ? 6.040  9.756   42.102 1.00 61.06  ? 60  THR N CB  1 
ATOM   3237 O  OG1 . THR B 2 67  ? 6.273  8.427   41.621 1.00 55.25  ? 60  THR N OG1 1 
ATOM   3238 C  CG2 . THR B 2 67  ? 4.580  9.869   42.555 1.00 67.81  ? 60  THR N CG2 1 
ATOM   3239 N  N   . ILE B 2 68  ? 8.607  11.432  41.551 1.00 51.03  ? 61  ILE N N   1 
ATOM   3240 C  CA  . ILE B 2 68  ? 10.071 11.449  41.469 1.00 46.81  ? 61  ILE N CA  1 
ATOM   3241 C  C   . ILE B 2 68  ? 10.605 10.409  42.450 1.00 44.37  ? 61  ILE N C   1 
ATOM   3242 O  O   . ILE B 2 68  ? 10.281 10.444  43.648 1.00 49.36  ? 61  ILE N O   1 
ATOM   3243 C  CB  . ILE B 2 68  ? 10.647 12.838  41.798 1.00 44.42  ? 61  ILE N CB  1 
ATOM   3244 C  CG1 . ILE B 2 68  ? 9.901  13.953  41.068 1.00 47.12  ? 61  ILE N CG1 1 
ATOM   3245 C  CG2 . ILE B 2 68  ? 12.144 12.894  41.514 1.00 49.27  ? 61  ILE N CG2 1 
ATOM   3246 C  CD1 . ILE B 2 68  ? 10.522 15.339  41.299 1.00 47.40  ? 61  ILE N CD1 1 
ATOM   3247 N  N   . ASP B 2 69  ? 11.415 9.481   41.963 1.00 44.32  ? 62  ASP N N   1 
ATOM   3248 C  CA  . ASP B 2 69  ? 12.163 8.613   42.861 1.00 47.64  ? 62  ASP N CA  1 
ATOM   3249 C  C   . ASP B 2 69  ? 13.586 9.157   43.035 1.00 42.40  ? 62  ASP N C   1 
ATOM   3250 O  O   . ASP B 2 69  ? 14.010 10.105  42.360 1.00 40.86  ? 62  ASP N O   1 
ATOM   3251 C  CB  . ASP B 2 69  ? 12.165 7.161   42.351 1.00 49.50  ? 62  ASP N CB  1 
ATOM   3252 C  CG  . ASP B 2 69  ? 12.733 7.020   40.941 1.00 51.62  ? 62  ASP N CG  1 
ATOM   3253 O  OD1 . ASP B 2 69  ? 13.823 7.575   40.648 1.00 45.29  ? 62  ASP N OD1 1 
ATOM   3254 O  OD2 . ASP B 2 69  ? 12.072 6.345   40.120 1.00 64.74  ? 62  ASP N OD2 1 
ATOM   3255 N  N   . PHE B 2 70  ? 14.330 8.547   43.965 1.00 41.80  ? 63  PHE N N   1 
ATOM   3256 C  CA  . PHE B 2 70  ? 15.655 9.082   44.303 1.00 38.94  ? 63  PHE N CA  1 
ATOM   3257 C  C   . PHE B 2 70  ? 16.645 8.997   43.139 1.00 37.98  ? 63  PHE N C   1 
ATOM   3258 O  O   . PHE B 2 70  ? 17.461 9.915   42.968 1.00 39.29  ? 63  PHE N O   1 
ATOM   3259 C  CB  . PHE B 2 70  ? 16.225 8.379   45.537 1.00 37.96  ? 63  PHE N CB  1 
ATOM   3260 C  CG  . PHE B 2 70  ? 17.531 8.962   46.017 1.00 45.44  ? 63  PHE N CG  1 
ATOM   3261 C  CD1 . PHE B 2 70  ? 17.577 10.243  46.555 1.00 40.98  ? 63  PHE N CD1 1 
ATOM   3262 C  CD2 . PHE B 2 70  ? 18.718 8.240   45.903 1.00 45.34  ? 63  PHE N CD2 1 
ATOM   3263 C  CE1 . PHE B 2 70  ? 18.789 10.793  46.988 1.00 43.77  ? 63  PHE N CE1 1 
ATOM   3264 C  CE2 . PHE B 2 70  ? 19.926 8.775   46.342 1.00 49.96  ? 63  PHE N CE2 1 
ATOM   3265 C  CZ  . PHE B 2 70  ? 19.962 10.052  46.891 1.00 48.84  ? 63  PHE N CZ  1 
ATOM   3266 N  N   . PRO B 2 71  ? 16.633 7.938   42.318 1.00 45.45  ? 64  PRO N N   1 
ATOM   3267 C  CA  . PRO B 2 71  ? 17.507 7.965   41.126 1.00 45.52  ? 64  PRO N CA  1 
ATOM   3268 C  C   . PRO B 2 71  ? 17.208 9.133   40.206 1.00 44.12  ? 64  PRO N C   1 
ATOM   3269 O  O   . PRO B 2 71  ? 18.140 9.834   39.776 1.00 43.51  ? 64  PRO N O   1 
ATOM   3270 C  CB  . PRO B 2 71  ? 17.231 6.615   40.458 1.00 47.83  ? 64  PRO N CB  1 
ATOM   3271 C  CG  . PRO B 2 71  ? 16.815 5.739   41.563 1.00 44.55  ? 64  PRO N CG  1 
ATOM   3272 C  CD  . PRO B 2 71  ? 16.070 6.592   42.540 1.00 46.18  ? 64  PRO N CD  1 
ATOM   3273 N  N   . GLU B 2 72  ? 15.920 9.374   39.914 1.00 44.03  ? 65  GLU N N   1 
ATOM   3274 C  CA  . GLU B 2 72  ? 15.512 10.561  39.155 1.00 40.15  ? 65  GLU N CA  1 
ATOM   3275 C  C   . GLU B 2 72  ? 15.973 11.842  39.845 1.00 35.23  ? 65  GLU N C   1 
ATOM   3276 O  O   . GLU B 2 72  ? 16.564 12.725  39.214 1.00 42.19  ? 65  GLU N O   1 
ATOM   3277 C  CB  . GLU B 2 72  ? 13.993 10.563  38.972 1.00 41.19  ? 65  GLU N CB  1 
ATOM   3278 C  CG  . GLU B 2 72  ? 13.481 9.476   38.008 1.00 44.04  ? 65  GLU N CG  1 
ATOM   3279 C  CD  . GLU B 2 72  ? 11.971 9.231   38.111 1.00 47.03  ? 65  GLU N CD  1 
ATOM   3280 O  OE1 . GLU B 2 72  ? 11.401 9.429   39.202 1.00 41.09  ? 65  GLU N OE1 1 
ATOM   3281 O  OE2 . GLU B 2 72  ? 11.347 8.837   37.096 1.00 47.08  ? 65  GLU N OE2 1 
ATOM   3282 N  N   . PHE B 2 73  ? 15.713 11.955  41.150 1.00 39.32  ? 66  PHE N N   1 
ATOM   3283 C  CA  . PHE B 2 73  ? 16.214 13.083  41.930 1.00 41.10  ? 66  PHE N CA  1 
ATOM   3284 C  C   . PHE B 2 73  ? 17.733 13.220  41.799 1.00 40.72  ? 66  PHE N C   1 
ATOM   3285 O  O   . PHE B 2 73  ? 18.252 14.313  41.552 1.00 40.92  ? 66  PHE N O   1 
ATOM   3286 C  CB  . PHE B 2 73  ? 15.797 12.891  43.393 1.00 39.55  ? 66  PHE N CB  1 
ATOM   3287 C  CG  . PHE B 2 73  ? 16.049 14.086  44.288 1.00 39.03  ? 66  PHE N CG  1 
ATOM   3288 C  CD1 . PHE B 2 73  ? 15.101 15.091  44.417 1.00 43.79  ? 66  PHE N CD1 1 
ATOM   3289 C  CD2 . PHE B 2 73  ? 17.204 14.167  45.047 1.00 42.27  ? 66  PHE N CD2 1 
ATOM   3290 C  CE1 . PHE B 2 73  ? 15.308 16.171  45.275 1.00 45.81  ? 66  PHE N CE1 1 
ATOM   3291 C  CE2 . PHE B 2 73  ? 17.427 15.243  45.913 1.00 46.00  ? 66  PHE N CE2 1 
ATOM   3292 C  CZ  . PHE B 2 73  ? 16.476 16.239  46.034 1.00 43.07  ? 66  PHE N CZ  1 
ATOM   3293 N  N   . LEU B 2 74  ? 18.463 12.110  41.960 1.00 44.38  ? 67  LEU N N   1 
ATOM   3294 C  CA  . LEU B 2 74  ? 19.922 12.170  41.915 1.00 43.25  ? 67  LEU N CA  1 
ATOM   3295 C  C   . LEU B 2 74  ? 20.421 12.559  40.528 1.00 41.94  ? 67  LEU N C   1 
ATOM   3296 O  O   . LEU B 2 74  ? 21.252 13.464  40.398 1.00 43.24  ? 67  LEU N O   1 
ATOM   3297 C  CB  . LEU B 2 74  ? 20.516 10.836  42.357 1.00 47.68  ? 67  LEU N CB  1 
ATOM   3298 C  CG  . LEU B 2 74  ? 21.960 10.904  42.868 1.00 56.68  ? 67  LEU N CG  1 
ATOM   3299 C  CD1 . LEU B 2 74  ? 22.009 11.434  44.284 1.00 60.68  ? 67  LEU N CD1 1 
ATOM   3300 C  CD2 . LEU B 2 74  ? 22.625 9.544   42.795 1.00 61.68  ? 67  LEU N CD2 1 
ATOM   3301 N  N   . THR B 2 75  ? 19.909 11.901  39.475 1.00 47.01  ? 68  THR N N   1 
ATOM   3302 C  CA  . THR B 2 75  ? 20.290 12.271  38.109 1.00 50.27  ? 68  THR N CA  1 
ATOM   3303 C  C   . THR B 2 75  ? 20.117 13.770  37.870 1.00 52.93  ? 68  THR N C   1 
ATOM   3304 O  O   . THR B 2 75  ? 20.975 14.410  37.252 1.00 58.08  ? 68  THR N O   1 
ATOM   3305 C  CB  . THR B 2 75  ? 19.463 11.481  37.075 1.00 48.87  ? 68  THR N CB  1 
ATOM   3306 O  OG1 . THR B 2 75  ? 19.538 10.081  37.344 1.00 40.51  ? 68  THR N OG1 1 
ATOM   3307 C  CG2 . THR B 2 75  ? 19.974 11.725  35.648 1.00 45.66  ? 68  THR N CG2 1 
ATOM   3308 N  N   . MET B 2 76  ? 19.014 14.347  38.366 1.00 58.45  ? 69  MET N N   1 
ATOM   3309 C  CA  . MET B 2 76  ? 18.732 15.760  38.120 1.00 58.19  ? 69  MET N CA  1 
ATOM   3310 C  C   . MET B 2 76  ? 19.676 16.666  38.907 1.00 55.26  ? 69  MET N C   1 
ATOM   3311 O  O   . MET B 2 76  ? 20.173 17.667  38.376 1.00 51.76  ? 69  MET N O   1 
ATOM   3312 C  CB  . MET B 2 76  ? 17.271 16.070  38.460 1.00 58.00  ? 69  MET N CB  1 
ATOM   3313 C  CG  . MET B 2 76  ? 16.920 17.566  38.444 1.00 56.22  ? 69  MET N CG  1 
ATOM   3314 S  SD  . MET B 2 76  ? 16.977 18.331  40.091 1.00 66.17  ? 69  MET N SD  1 
ATOM   3315 C  CE  . MET B 2 76  ? 15.284 18.115  40.655 1.00 60.00  ? 69  MET N CE  1 
ATOM   3316 N  N   . MET B 2 77  ? 19.940 16.334  40.173 1.00 57.93  ? 70  MET N N   1 
ATOM   3317 C  CA  . MET B 2 77  ? 20.870 17.136  40.961 1.00 60.88  ? 70  MET N CA  1 
ATOM   3318 C  C   . MET B 2 77  ? 22.227 17.238  40.273 1.00 65.12  ? 70  MET N C   1 
ATOM   3319 O  O   . MET B 2 77  ? 22.871 18.293  40.311 1.00 69.04  ? 70  MET N O   1 
ATOM   3320 C  CB  . MET B 2 77  ? 21.006 16.538  42.358 1.00 61.06  ? 70  MET N CB  1 
ATOM   3321 C  CG  . MET B 2 77  ? 19.889 16.924  43.332 1.00 62.46  ? 70  MET N CG  1 
ATOM   3322 S  SD  . MET B 2 77  ? 18.961 18.418  42.905 1.00 65.00  ? 70  MET N SD  1 
ATOM   3323 C  CE  . MET B 2 77  ? 19.886 19.644  43.840 1.00 65.52  ? 70  MET N CE  1 
ATOM   3324 N  N   . ALA B 2 78  ? 22.651 16.164  39.596 1.00 64.50  ? 71  ALA N N   1 
ATOM   3325 C  CA  . ALA B 2 78  ? 23.919 16.169  38.869 1.00 66.49  ? 71  ALA N CA  1 
ATOM   3326 C  C   . ALA B 2 78  ? 23.876 17.090  37.652 1.00 64.71  ? 71  ALA N C   1 
ATOM   3327 O  O   . ALA B 2 78  ? 24.842 17.821  37.389 1.00 66.44  ? 71  ALA N O   1 
ATOM   3328 C  CB  . ALA B 2 78  ? 24.277 14.746  38.444 1.00 68.15  ? 71  ALA N CB  1 
ATOM   3329 N  N   . ARG B 2 79  ? 22.772 17.068  36.898 1.00 65.08  ? 72  ARG N N   1 
ATOM   3330 C  CA  . ARG B 2 79  ? 22.631 17.854  35.664 1.00 67.69  ? 72  ARG N CA  1 
ATOM   3331 C  C   . ARG B 2 79  ? 22.830 19.350  35.902 1.00 68.97  ? 72  ARG N C   1 
ATOM   3332 O  O   . ARG B 2 79  ? 22.334 19.907  36.880 1.00 76.05  ? 72  ARG N O   1 
ATOM   3333 C  CB  . ARG B 2 79  ? 21.261 17.614  35.025 1.00 58.00  ? 72  ARG N CB  1 
ATOM   3334 N  N   . ASP B 2 83  ? 23.467 24.210  37.411 1.00 63.50  ? 76  ASP N N   1 
ATOM   3335 C  CA  . ASP B 2 83  ? 24.815 23.789  37.022 1.00 71.54  ? 76  ASP N CA  1 
ATOM   3336 C  C   . ASP B 2 83  ? 25.718 24.986  36.718 1.00 68.57  ? 76  ASP N C   1 
ATOM   3337 O  O   . ASP B 2 83  ? 26.844 25.069  37.223 1.00 61.17  ? 76  ASP N O   1 
ATOM   3338 C  CB  . ASP B 2 83  ? 24.761 22.856  35.807 1.00 71.34  ? 76  ASP N CB  1 
ATOM   3339 C  CG  . ASP B 2 83  ? 25.778 21.726  35.892 1.00 70.99  ? 76  ASP N CG  1 
ATOM   3340 O  OD1 . ASP B 2 83  ? 26.471 21.605  36.932 1.00 74.93  ? 76  ASP N OD1 1 
ATOM   3341 O  OD2 . ASP B 2 83  ? 25.880 20.955  34.916 1.00 71.26  ? 76  ASP N OD2 1 
ATOM   3342 N  N   . THR B 2 84  ? 25.217 25.910  35.892 1.00 70.41  ? 77  THR N N   1 
ATOM   3343 C  CA  . THR B 2 84  ? 25.964 27.115  35.551 1.00 71.17  ? 77  THR N CA  1 
ATOM   3344 C  C   . THR B 2 84  ? 25.710 28.276  36.518 1.00 73.58  ? 77  THR N C   1 
ATOM   3345 O  O   . THR B 2 84  ? 26.667 28.925  36.968 1.00 61.42  ? 77  THR N O   1 
ATOM   3346 C  CB  . THR B 2 84  ? 25.659 27.524  34.100 1.00 74.95  ? 77  THR N CB  1 
ATOM   3347 O  OG1 . THR B 2 84  ? 26.724 28.342  33.589 1.00 79.75  ? 77  THR N OG1 1 
ATOM   3348 C  CG2 . THR B 2 84  ? 24.313 28.234  33.953 1.00 79.86  ? 77  THR N CG2 1 
ATOM   3349 N  N   . ASP B 2 85  ? 24.451 28.542  36.887 1.00 86.24  ? 78  ASP N N   1 
ATOM   3350 C  CA  . ASP B 2 85  ? 24.118 29.692  37.730 1.00 94.08  ? 78  ASP N CA  1 
ATOM   3351 C  C   . ASP B 2 85  ? 23.190 29.253  38.862 1.00 89.27  ? 78  ASP N C   1 
ATOM   3352 O  O   . ASP B 2 85  ? 22.011 29.614  38.941 1.00 87.16  ? 78  ASP N O   1 
ATOM   3353 C  CB  . ASP B 2 85  ? 23.534 30.831  36.917 1.00 86.56  ? 78  ASP N CB  1 
ATOM   3354 C  CG  . ASP B 2 85  ? 24.588 31.841  36.541 1.00 86.04  ? 78  ASP N CG  1 
ATOM   3355 O  OD1 . ASP B 2 85  ? 25.563 31.963  37.317 1.00 83.76  ? 78  ASP N OD1 1 
ATOM   3356 O  OD2 . ASP B 2 85  ? 24.460 32.488  35.480 1.00 72.51  ? 78  ASP N OD2 1 
ATOM   3357 N  N   . SER B 2 86  ? 23.767 28.441  39.744 1.00 75.21  ? 79  SER N N   1 
ATOM   3358 C  CA  . SER B 2 86  ? 23.308 28.262  41.109 1.00 63.62  ? 79  SER N CA  1 
ATOM   3359 C  C   . SER B 2 86  ? 23.325 29.563  41.906 1.00 57.45  ? 79  SER N C   1 
ATOM   3360 O  O   . SER B 2 86  ? 22.776 29.607  43.015 1.00 52.14  ? 79  SER N O   1 
ATOM   3361 C  CB  . SER B 2 86  ? 24.220 27.236  41.751 1.00 63.01  ? 79  SER N CB  1 
ATOM   3362 N  N   . GLU B 2 87  ? 23.968 30.611  41.384 1.00 54.70  ? 80  GLU N N   1 
ATOM   3363 C  CA  . GLU B 2 87  ? 23.930 31.903  42.055 1.00 54.86  ? 80  GLU N CA  1 
ATOM   3364 C  C   . GLU B 2 87  ? 22.500 32.390  42.216 1.00 52.17  ? 80  GLU N C   1 
ATOM   3365 O  O   . GLU B 2 87  ? 22.121 32.877  43.288 1.00 49.92  ? 80  GLU N O   1 
ATOM   3366 C  CB  . GLU B 2 87  ? 24.756 32.928  41.288 1.00 53.83  ? 80  GLU N CB  1 
ATOM   3367 C  CG  . GLU B 2 87  ? 26.239 32.682  41.336 1.00 61.49  ? 80  GLU N CG  1 
ATOM   3368 C  CD  . GLU B 2 87  ? 26.954 33.338  40.169 1.00 61.29  ? 80  GLU N CD  1 
ATOM   3369 O  OE1 . GLU B 2 87  ? 26.859 34.580  40.024 1.00 64.39  ? 80  GLU N OE1 1 
ATOM   3370 O  OE2 . GLU B 2 87  ? 27.597 32.605  39.390 1.00 59.36  ? 80  GLU N OE2 1 
ATOM   3371 N  N   . GLU B 2 88  ? 21.688 32.265  41.160 1.00 47.72  ? 81  GLU N N   1 
ATOM   3372 C  CA  . GLU B 2 88  ? 20.291 32.676  41.257 1.00 44.36  ? 81  GLU N CA  1 
ATOM   3373 C  C   . GLU B 2 88  ? 19.575 31.890  42.345 1.00 44.52  ? 81  GLU N C   1 
ATOM   3374 O  O   . GLU B 2 88  ? 18.886 32.467  43.193 1.00 53.11  ? 81  GLU N O   1 
ATOM   3375 C  CB  . GLU B 2 88  ? 19.589 32.491  39.911 1.00 49.18  ? 81  GLU N CB  1 
ATOM   3376 C  CG  . GLU B 2 88  ? 18.275 33.238  39.796 1.00 56.07  ? 81  GLU N CG  1 
ATOM   3377 C  CD  . GLU B 2 88  ? 17.138 32.610  40.608 1.00 69.40  ? 81  GLU N CD  1 
ATOM   3378 O  OE1 . GLU B 2 88  ? 17.065 31.360  40.681 1.00 71.74  ? 81  GLU N OE1 1 
ATOM   3379 O  OE2 . GLU B 2 88  ? 16.314 33.372  41.169 1.00 82.62  ? 81  GLU N OE2 1 
ATOM   3380 N  N   . GLU B 2 89  ? 19.725 30.562  42.330 1.00 41.87  ? 82  GLU N N   1 
ATOM   3381 C  CA  . GLU B 2 89  ? 19.025 29.723  43.299 1.00 42.54  ? 82  GLU N CA  1 
ATOM   3382 C  C   . GLU B 2 89  ? 19.437 30.063  44.738 1.00 39.08  ? 82  GLU N C   1 
ATOM   3383 O  O   . GLU B 2 89  ? 18.591 30.120  45.638 1.00 35.83  ? 82  GLU N O   1 
ATOM   3384 C  CB  . GLU B 2 89  ? 19.283 28.251  42.970 1.00 44.50  ? 82  GLU N CB  1 
ATOM   3385 C  CG  . GLU B 2 89  ? 18.414 27.727  41.838 1.00 46.56  ? 82  GLU N CG  1 
ATOM   3386 C  CD  . GLU B 2 89  ? 19.201 27.037  40.730 1.00 53.54  ? 82  GLU N CD  1 
ATOM   3387 O  OE1 . GLU B 2 89  ? 20.095 26.208  41.036 1.00 58.10  ? 82  GLU N OE1 1 
ATOM   3388 O  OE2 . GLU B 2 89  ? 18.915 27.319  39.545 1.00 57.49  ? 82  GLU N OE2 1 
ATOM   3389 N  N   . ILE B 2 90  ? 20.727 30.323  44.964 1.00 36.36  ? 83  ILE N N   1 
ATOM   3390 C  CA  . ILE B 2 90  ? 21.191 30.713  46.292 1.00 34.74  ? 83  ILE N CA  1 
ATOM   3391 C  C   . ILE B 2 90  ? 20.629 32.078  46.671 1.00 36.29  ? 83  ILE N C   1 
ATOM   3392 O  O   . ILE B 2 90  ? 20.245 32.305  47.828 1.00 35.87  ? 83  ILE N O   1 
ATOM   3393 C  CB  . ILE B 2 90  ? 22.729 30.688  46.344 1.00 35.79  ? 83  ILE N CB  1 
ATOM   3394 C  CG1 . ILE B 2 90  ? 23.240 29.258  46.184 1.00 36.06  ? 83  ILE N CG1 1 
ATOM   3395 C  CG2 . ILE B 2 90  ? 23.255 31.299  47.655 1.00 34.11  ? 83  ILE N CG2 1 
ATOM   3396 C  CD1 . ILE B 2 90  ? 24.760 29.187  45.963 1.00 36.55  ? 83  ILE N CD1 1 
ATOM   3397 N  N   . ARG B 2 91  ? 20.555 33.004  45.701 1.00 37.97  ? 84  ARG N N   1 
ATOM   3398 C  CA  . ARG B 2 91  ? 19.928 34.301  45.956 1.00 40.07  ? 84  ARG N CA  1 
ATOM   3399 C  C   . ARG B 2 91  ? 18.455 34.131  46.287 1.00 43.73  ? 84  ARG N C   1 
ATOM   3400 O  O   . ARG B 2 91  ? 17.931 34.796  47.189 1.00 41.72  ? 84  ARG N O   1 
ATOM   3401 C  CB  . ARG B 2 91  ? 20.086 35.235  44.755 1.00 42.33  ? 84  ARG N CB  1 
ATOM   3402 C  CG  . ARG B 2 91  ? 21.246 36.220  44.866 1.00 46.22  ? 84  ARG N CG  1 
ATOM   3403 C  CD  . ARG B 2 91  ? 21.194 37.314  43.798 1.00 48.38  ? 84  ARG N CD  1 
ATOM   3404 N  NE  . ARG B 2 91  ? 21.045 36.817  42.430 1.00 45.71  ? 84  ARG N NE  1 
ATOM   3405 C  CZ  . ARG B 2 91  ? 22.032 36.345  41.678 1.00 43.86  ? 84  ARG N CZ  1 
ATOM   3406 N  NH1 . ARG B 2 91  ? 23.255 36.177  42.158 1.00 47.58  ? 84  ARG N NH1 1 
ATOM   3407 N  NH2 . ARG B 2 91  ? 21.789 36.045  40.407 1.00 39.93  ? 84  ARG N NH2 1 
ATOM   3408 N  N   . GLU B 2 92  ? 17.773 33.237  45.570 1.00 48.70  ? 85  GLU N N   1 
ATOM   3409 C  CA  . GLU B 2 92  ? 16.375 32.964  45.875 1.00 52.26  ? 85  GLU N CA  1 
ATOM   3410 C  C   . GLU B 2 92  ? 16.229 32.381  47.274 1.00 45.41  ? 85  GLU N C   1 
ATOM   3411 O  O   . GLU B 2 92  ? 15.262 32.689  47.984 1.00 45.79  ? 85  GLU N O   1 
ATOM   3412 C  CB  . GLU B 2 92  ? 15.792 32.028  44.813 1.00 57.00  ? 85  GLU N CB  1 
ATOM   3413 C  CG  . GLU B 2 92  ? 14.435 31.406  45.128 1.00 61.57  ? 85  GLU N CG  1 
ATOM   3414 C  CD  . GLU B 2 92  ? 13.359 32.407  45.499 1.00 60.80  ? 85  GLU N CD  1 
ATOM   3415 O  OE1 . GLU B 2 92  ? 13.508 33.608  45.190 1.00 69.36  ? 85  GLU N OE1 1 
ATOM   3416 O  OE2 . GLU B 2 92  ? 12.341 31.980  46.085 1.00 68.70  ? 85  GLU N OE2 1 
ATOM   3417 N  N   . ALA B 2 93  ? 17.202 31.567  47.702 1.00 39.03  ? 86  ALA N N   1 
ATOM   3418 C  CA  . ALA B 2 93  ? 17.150 30.995  49.046 1.00 36.68  ? 86  ALA N CA  1 
ATOM   3419 C  C   . ALA B 2 93  ? 17.371 32.068  50.097 1.00 34.53  ? 86  ALA N C   1 
ATOM   3420 O  O   . ALA B 2 93  ? 16.693 32.080  51.132 1.00 31.52  ? 86  ALA N O   1 
ATOM   3421 C  CB  . ALA B 2 93  ? 18.189 29.884  49.193 1.00 34.23  ? 86  ALA N CB  1 
ATOM   3422 N  N   . PHE B 2 94  ? 18.330 32.969  49.842 1.00 33.52  ? 87  PHE N N   1 
ATOM   3423 C  CA  . PHE B 2 94  ? 18.498 34.157  50.666 1.00 35.15  ? 87  PHE N CA  1 
ATOM   3424 C  C   . PHE B 2 94  ? 17.206 34.949  50.781 1.00 34.58  ? 87  PHE N C   1 
ATOM   3425 O  O   . PHE B 2 94  ? 16.813 35.355  51.881 1.00 35.06  ? 87  PHE N O   1 
ATOM   3426 C  CB  . PHE B 2 94  ? 19.594 35.056  50.108 1.00 33.69  ? 87  PHE N CB  1 
ATOM   3427 C  CG  . PHE B 2 94  ? 19.917 36.174  51.018 1.00 37.68  ? 87  PHE N CG  1 
ATOM   3428 C  CD1 . PHE B 2 94  ? 20.777 35.972  52.091 1.00 37.73  ? 87  PHE N CD1 1 
ATOM   3429 C  CD2 . PHE B 2 94  ? 19.305 37.414  50.866 1.00 35.71  ? 87  PHE N CD2 1 
ATOM   3430 C  CE1 . PHE B 2 94  ? 21.055 37.013  52.964 1.00 38.49  ? 87  PHE N CE1 1 
ATOM   3431 C  CE2 . PHE B 2 94  ? 19.574 38.447  51.754 1.00 34.51  ? 87  PHE N CE2 1 
ATOM   3432 C  CZ  . PHE B 2 94  ? 20.450 38.250  52.794 1.00 35.16  ? 87  PHE N CZ  1 
ATOM   3433 N  N   . ARG B 2 95  ? 16.528 35.187  49.654 1.00 35.32  ? 88  ARG N N   1 
ATOM   3434 C  CA  . ARG B 2 95  ? 15.330 36.025  49.710 1.00 39.69  ? 88  ARG N CA  1 
ATOM   3435 C  C   . ARG B 2 95  ? 14.219 35.378  50.529 1.00 39.38  ? 88  ARG N C   1 
ATOM   3436 O  O   . ARG B 2 95  ? 13.472 36.089  51.208 1.00 38.97  ? 88  ARG N O   1 
ATOM   3437 C  CB  . ARG B 2 95  ? 14.838 36.354  48.302 1.00 42.01  ? 88  ARG N CB  1 
ATOM   3438 C  CG  . ARG B 2 95  ? 15.442 37.630  47.744 1.00 47.47  ? 88  ARG N CG  1 
ATOM   3439 C  CD  . ARG B 2 95  ? 14.839 38.023  46.392 1.00 49.71  ? 88  ARG N CD  1 
ATOM   3440 N  NE  . ARG B 2 95  ? 14.904 36.949  45.410 1.00 56.01  ? 88  ARG N NE  1 
ATOM   3441 C  CZ  . ARG B 2 95  ? 15.757 36.904  44.392 1.00 58.26  ? 88  ARG N CZ  1 
ATOM   3442 N  NH1 . ARG B 2 95  ? 16.650 37.864  44.190 1.00 59.68  ? 88  ARG N NH1 1 
ATOM   3443 N  NH2 . ARG B 2 95  ? 15.718 35.866  43.558 1.00 55.33  ? 88  ARG N NH2 1 
ATOM   3444 N  N   . VAL B 2 96  ? 14.113 34.041  50.506 1.00 39.38  ? 89  VAL N N   1 
ATOM   3445 C  CA  . VAL B 2 96  ? 13.066 33.369  51.276 1.00 38.78  ? 89  VAL N CA  1 
ATOM   3446 C  C   . VAL B 2 96  ? 13.295 33.550  52.767 1.00 37.16  ? 89  VAL N C   1 
ATOM   3447 O  O   . VAL B 2 96  ? 12.352 33.790  53.524 1.00 37.23  ? 89  VAL N O   1 
ATOM   3448 C  CB  . VAL B 2 96  ? 12.980 31.878  50.901 1.00 37.64  ? 89  VAL N CB  1 
ATOM   3449 C  CG1 . VAL B 2 96  ? 12.036 31.133  51.881 1.00 36.10  ? 89  VAL N CG1 1 
ATOM   3450 C  CG2 . VAL B 2 96  ? 12.518 31.719  49.446 1.00 33.46  ? 89  VAL N CG2 1 
ATOM   3451 N  N   . PHE B 2 97  ? 14.552 33.443  53.214 1.00 37.97  ? 90  PHE N N   1 
ATOM   3452 C  CA  . PHE B 2 97  ? 14.874 33.670  54.622 1.00 37.09  ? 90  PHE N CA  1 
ATOM   3453 C  C   . PHE B 2 97  ? 14.628 35.116  55.024 1.00 33.69  ? 90  PHE N C   1 
ATOM   3454 O  O   . PHE B 2 97  ? 14.254 35.395  56.170 1.00 31.68  ? 90  PHE N O   1 
ATOM   3455 C  CB  . PHE B 2 97  ? 16.345 33.345  54.898 1.00 36.26  ? 90  PHE N CB  1 
ATOM   3456 C  CG  . PHE B 2 97  ? 16.645 31.889  55.058 1.00 30.60  ? 90  PHE N CG  1 
ATOM   3457 C  CD1 . PHE B 2 97  ? 16.236 31.201  56.199 1.00 29.16  ? 90  PHE N CD1 1 
ATOM   3458 C  CD2 . PHE B 2 97  ? 17.393 31.220  54.097 1.00 27.08  ? 90  PHE N CD2 1 
ATOM   3459 C  CE1 . PHE B 2 97  ? 16.531 29.864  56.364 1.00 28.05  ? 90  PHE N CE1 1 
ATOM   3460 C  CE2 . PHE B 2 97  ? 17.701 29.872  54.256 1.00 29.48  ? 90  PHE N CE2 1 
ATOM   3461 C  CZ  . PHE B 2 97  ? 17.272 29.192  55.394 1.00 27.47  ? 90  PHE N CZ  1 
ATOM   3462 N  N   . ASP B 2 98  ? 14.908 36.053  54.120 1.00 36.52  ? 91  ASP N N   1 
ATOM   3463 C  CA  . ASP B 2 98  ? 14.949 37.470  54.469 1.00 39.09  ? 91  ASP N CA  1 
ATOM   3464 C  C   . ASP B 2 98  ? 13.600 38.107  54.147 1.00 42.12  ? 91  ASP N C   1 
ATOM   3465 O  O   . ASP B 2 98  ? 13.476 38.991  53.300 1.00 41.69  ? 91  ASP N O   1 
ATOM   3466 C  CB  . ASP B 2 98  ? 16.094 38.171  53.729 1.00 34.79  ? 91  ASP N CB  1 
ATOM   3467 C  CG  . ASP B 2 98  ? 16.165 39.664  54.044 1.00 33.56  ? 91  ASP N CG  1 
ATOM   3468 O  OD1 . ASP B 2 98  ? 15.813 40.064  55.186 1.00 31.34  ? 91  ASP N OD1 1 
ATOM   3469 O  OD2 . ASP B 2 98  ? 16.559 40.436  53.153 1.00 33.21  ? 91  ASP N OD2 1 
ATOM   3470 N  N   . LYS B 2 99  ? 12.587 37.645  54.882 1.00 52.83  ? 92  LYS N N   1 
ATOM   3471 C  CA  . LYS B 2 99  ? 11.203 37.908  54.500 1.00 54.18  ? 92  LYS N CA  1 
ATOM   3472 C  C   . LYS B 2 99  ? 10.863 39.392  54.536 1.00 45.08  ? 92  LYS N C   1 
ATOM   3473 O  O   . LYS B 2 99  ? 9.983  39.834  53.787 1.00 45.26  ? 92  LYS N O   1 
ATOM   3474 C  CB  . LYS B 2 99  ? 10.249 37.121  55.397 1.00 53.09  ? 92  LYS N CB  1 
ATOM   3475 C  CG  . LYS B 2 99  ? 8.889  36.852  54.753 1.00 63.05  ? 92  LYS N CG  1 
ATOM   3476 C  CD  . LYS B 2 99  ? 9.023  35.993  53.494 1.00 69.49  ? 92  LYS N CD  1 
ATOM   3477 C  CE  . LYS B 2 99  ? 7.899  36.266  52.496 1.00 63.73  ? 92  LYS N CE  1 
ATOM   3478 N  NZ  . LYS B 2 99  ? 8.246  37.294  51.489 1.00 61.48  ? 92  LYS N NZ  1 
ATOM   3479 N  N   . ASP B 2 100 ? 11.538 40.174  55.388 1.00 40.19  ? 93  ASP N N   1 
ATOM   3480 C  CA  . ASP B 2 100 ? 11.348 41.623  55.426 1.00 41.72  ? 93  ASP N CA  1 
ATOM   3481 C  C   . ASP B 2 100 ? 12.311 42.384  54.508 1.00 44.23  ? 93  ASP N C   1 
ATOM   3482 O  O   . ASP B 2 100 ? 12.356 43.611  54.569 1.00 47.75  ? 93  ASP N O   1 
ATOM   3483 C  CB  . ASP B 2 100 ? 11.454 42.152  56.868 1.00 41.42  ? 93  ASP N CB  1 
ATOM   3484 C  CG  . ASP B 2 100 ? 12.843 42.020  57.459 1.00 43.87  ? 93  ASP N CG  1 
ATOM   3485 O  OD1 . ASP B 2 100 ? 13.764 41.605  56.745 1.00 43.08  ? 93  ASP N OD1 1 
ATOM   3486 O  OD2 . ASP B 2 100 ? 13.014 42.316  58.665 1.00 44.92  ? 93  ASP N OD2 1 
ATOM   3487 N  N   . GLY B 2 101 ? 13.078 41.691  53.669 1.00 42.23  ? 94  GLY N N   1 
ATOM   3488 C  CA  . GLY B 2 101 ? 13.869 42.341  52.637 1.00 41.74  ? 94  GLY N CA  1 
ATOM   3489 C  C   . GLY B 2 101 ? 14.903 43.339  53.117 1.00 43.88  ? 94  GLY N C   1 
ATOM   3490 O  O   . GLY B 2 101 ? 15.397 44.133  52.310 1.00 41.82  ? 94  GLY N O   1 
ATOM   3491 N  N   . ASN B 2 102 ? 15.261 43.320  54.405 1.00 46.34  ? 95  ASN N N   1 
ATOM   3492 C  CA  . ASN B 2 102 ? 16.193 44.307  54.947 1.00 44.97  ? 95  ASN N CA  1 
ATOM   3493 C  C   . ASN B 2 102 ? 17.652 43.933  54.728 1.00 44.25  ? 95  ASN N C   1 
ATOM   3494 O  O   . ASN B 2 102 ? 18.535 44.671  55.180 1.00 45.52  ? 95  ASN N O   1 
ATOM   3495 C  CB  . ASN B 2 102 ? 15.916 44.552  56.447 1.00 45.82  ? 95  ASN N CB  1 
ATOM   3496 C  CG  . ASN B 2 102 ? 16.469 43.446  57.373 1.00 45.26  ? 95  ASN N CG  1 
ATOM   3497 O  OD1 . ASN B 2 102 ? 16.631 42.284  56.975 1.00 41.40  ? 95  ASN N OD1 1 
ATOM   3498 N  ND2 . ASN B 2 102 ? 16.735 43.816  58.636 1.00 40.41  ? 95  ASN N ND2 1 
ATOM   3499 N  N   . GLY B 2 103 ? 17.930 42.816  54.061 1.00 46.02  ? 96  GLY N N   1 
ATOM   3500 C  CA  . GLY B 2 103 ? 19.288 42.449  53.697 1.00 42.98  ? 96  GLY N CA  1 
ATOM   3501 C  C   . GLY B 2 103 ? 20.014 41.553  54.676 1.00 38.17  ? 96  GLY N C   1 
ATOM   3502 O  O   . GLY B 2 103 ? 21.181 41.211  54.424 1.00 38.62  ? 96  GLY N O   1 
ATOM   3503 N  N   . PHE B 2 104 ? 19.370 41.171  55.783 1.00 36.90  ? 97  PHE N N   1 
ATOM   3504 C  CA  . PHE B 2 104 ? 19.996 40.414  56.862 1.00 38.47  ? 97  PHE N CA  1 
ATOM   3505 C  C   . PHE B 2 104 ? 19.053 39.326  57.358 1.00 37.57  ? 97  PHE N C   1 
ATOM   3506 O  O   . PHE B 2 104 ? 17.891 39.603  57.661 1.00 43.25  ? 97  PHE N O   1 
ATOM   3507 C  CB  . PHE B 2 104 ? 20.375 41.312  58.048 1.00 42.19  ? 97  PHE N CB  1 
ATOM   3508 C  CG  . PHE B 2 104 ? 21.162 42.543  57.677 1.00 45.77  ? 97  PHE N CG  1 
ATOM   3509 C  CD1 . PHE B 2 104 ? 20.515 43.681  57.214 1.00 46.71  ? 97  PHE N CD1 1 
ATOM   3510 C  CD2 . PHE B 2 104 ? 22.541 42.556  57.776 1.00 49.06  ? 97  PHE N CD2 1 
ATOM   3511 C  CE1 . PHE B 2 104 ? 21.230 44.813  56.858 1.00 50.13  ? 97  PHE N CE1 1 
ATOM   3512 C  CE2 . PHE B 2 104 ? 23.268 43.679  57.428 1.00 45.77  ? 97  PHE N CE2 1 
ATOM   3513 C  CZ  . PHE B 2 104 ? 22.612 44.814  56.966 1.00 51.80  ? 97  PHE N CZ  1 
ATOM   3514 N  N   . ILE B 2 105 ? 19.555 38.102  57.468 1.00 34.34  ? 98  ILE N N   1 
ATOM   3515 C  CA  . ILE B 2 105 ? 18.806 37.008  58.075 1.00 30.23  ? 98  ILE N CA  1 
ATOM   3516 C  C   . ILE B 2 105 ? 19.066 37.030  59.573 1.00 31.98  ? 98  ILE N C   1 
ATOM   3517 O  O   . ILE B 2 105 ? 20.218 36.898  60.003 1.00 32.93  ? 98  ILE N O   1 
ATOM   3518 C  CB  . ILE B 2 105 ? 19.212 35.648  57.482 1.00 33.50  ? 98  ILE N CB  1 
ATOM   3519 C  CG1 . ILE B 2 105 ? 19.130 35.676  55.950 1.00 33.67  ? 98  ILE N CG1 1 
ATOM   3520 C  CG2 . ILE B 2 105 ? 18.369 34.504  58.125 1.00 34.12  ? 98  ILE N CG2 1 
ATOM   3521 C  CD1 . ILE B 2 105 ? 19.669 34.399  55.286 1.00 30.75  ? 98  ILE N CD1 1 
ATOM   3522 N  N   . SER B 2 106 ? 17.997 37.168  60.363 1.00 34.17  ? 99  SER N N   1 
ATOM   3523 C  CA  . SER B 2 106 ? 18.077 37.168  61.821 1.00 31.80  ? 99  SER N CA  1 
ATOM   3524 C  C   . SER B 2 106 ? 17.835 35.758  62.363 1.00 32.56  ? 99  SER N C   1 
ATOM   3525 O  O   . SER B 2 106 ? 17.491 34.832  61.623 1.00 34.90  ? 99  SER N O   1 
ATOM   3526 C  CB  . SER B 2 106 ? 17.047 38.145  62.408 1.00 31.31  ? 99  SER N CB  1 
ATOM   3527 O  OG  . SER B 2 106 ? 15.732 37.819  61.928 1.00 34.47  ? 99  SER N OG  1 
ATOM   3528 N  N   . ALA B 2 107 ? 18.011 35.600  63.683 1.00 30.26  ? 100 ALA N N   1 
ATOM   3529 C  CA  . ALA B 2 107 ? 17.626 34.351  64.338 1.00 30.96  ? 100 ALA N CA  1 
ATOM   3530 C  C   . ALA B 2 107 ? 16.138 34.071  64.143 1.00 31.80  ? 100 ALA N C   1 
ATOM   3531 O  O   . ALA B 2 107 ? 15.741 32.934  63.865 1.00 39.49  ? 100 ALA N O   1 
ATOM   3532 C  CB  . ALA B 2 107 ? 17.968 34.407  65.833 1.00 29.00  ? 100 ALA N CB  1 
ATOM   3533 N  N   . ALA B 2 108 ? 15.299 35.099  64.284 1.00 29.92  ? 101 ALA N N   1 
ATOM   3534 C  CA  . ALA B 2 108 ? 13.865 34.915  64.094 1.00 30.42  ? 101 ALA N CA  1 
ATOM   3535 C  C   . ALA B 2 108 ? 13.543 34.399  62.688 1.00 29.44  ? 101 ALA N C   1 
ATOM   3536 O  O   . ALA B 2 108 ? 12.737 33.483  62.539 1.00 31.39  ? 101 ALA N O   1 
ATOM   3537 C  CB  . ALA B 2 108 ? 13.133 36.230  64.371 1.00 29.69  ? 101 ALA N CB  1 
ATOM   3538 N  N   . GLU B 2 109 ? 14.172 34.966  61.643 1.00 33.78  ? 102 GLU N N   1 
ATOM   3539 C  CA  . GLU B 2 109 ? 13.876 34.535  60.267 1.00 30.49  ? 102 GLU N CA  1 
ATOM   3540 C  C   . GLU B 2 109 ? 14.390 33.127  59.997 1.00 34.26  ? 102 GLU N C   1 
ATOM   3541 O  O   . GLU B 2 109 ? 13.706 32.333  59.334 1.00 35.43  ? 102 GLU N O   1 
ATOM   3542 C  CB  . GLU B 2 109 ? 14.463 35.522  59.257 1.00 30.98  ? 102 GLU N CB  1 
ATOM   3543 C  CG  . GLU B 2 109 ? 13.715 36.855  59.247 1.00 36.74  ? 102 GLU N CG  1 
ATOM   3544 C  CD  . GLU B 2 109 ? 14.425 37.933  58.451 1.00 40.52  ? 102 GLU N CD  1 
ATOM   3545 O  OE1 . GLU B 2 109 ? 15.674 37.934  58.467 1.00 39.20  ? 102 GLU N OE1 1 
ATOM   3546 O  OE2 . GLU B 2 109 ? 13.736 38.763  57.798 1.00 40.42  ? 102 GLU N OE2 1 
ATOM   3547 N  N   . LEU B 2 110 ? 15.592 32.794  60.508 1.00 32.82  ? 103 LEU N N   1 
ATOM   3548 C  CA  . LEU B 2 110 ? 16.068 31.413  60.462 1.00 33.55  ? 103 LEU N CA  1 
ATOM   3549 C  C   . LEU B 2 110 ? 15.078 30.464  61.130 1.00 30.53  ? 103 LEU N C   1 
ATOM   3550 O  O   . LEU B 2 110 ? 14.734 29.418  60.579 1.00 28.90  ? 103 LEU N O   1 
ATOM   3551 C  CB  . LEU B 2 110 ? 17.435 31.293  61.137 1.00 34.68  ? 103 LEU N CB  1 
ATOM   3552 C  CG  . LEU B 2 110 ? 17.950 29.858  61.327 1.00 35.60  ? 103 LEU N CG  1 
ATOM   3553 C  CD1 . LEU B 2 110 ? 17.924 29.075  59.994 1.00 34.68  ? 103 LEU N CD1 1 
ATOM   3554 C  CD2 . LEU B 2 110 ? 19.377 29.874  61.913 1.00 34.73  ? 103 LEU N CD2 1 
ATOM   3555 N  N   . ARG B 2 111 ? 14.650 30.795  62.342 1.00 32.50  ? 104 ARG N N   1 
ATOM   3556 C  CA  . ARG B 2 111 ? 13.703 29.949  63.053 1.00 35.61  ? 104 ARG N CA  1 
ATOM   3557 C  C   . ARG B 2 111 ? 12.398 29.833  62.279 1.00 31.38  ? 104 ARG N C   1 
ATOM   3558 O  O   . ARG B 2 111 ? 11.820 28.748  62.168 1.00 29.37  ? 104 ARG N O   1 
ATOM   3559 C  CB  . ARG B 2 111 ? 13.445 30.535  64.442 1.00 40.65  ? 104 ARG N CB  1 
ATOM   3560 C  CG  . ARG B 2 111 ? 12.079 30.196  65.017 1.00 42.04  ? 104 ARG N CG  1 
ATOM   3561 C  CD  . ARG B 2 111 ? 12.002 28.723  65.368 1.00 48.83  ? 104 ARG N CD  1 
ATOM   3562 N  NE  . ARG B 2 111 ? 12.782 28.418  66.567 1.00 57.17  ? 104 ARG N NE  1 
ATOM   3563 C  CZ  . ARG B 2 111 ? 13.317 27.234  66.842 1.00 53.96  ? 104 ARG N CZ  1 
ATOM   3564 N  NH1 . ARG B 2 111 ? 13.169 26.199  66.023 1.00 49.65  ? 104 ARG N NH1 1 
ATOM   3565 N  NH2 . ARG B 2 111 ? 14.031 27.089  67.959 1.00 56.07  ? 104 ARG N NH2 1 
ATOM   3566 N  N   . HIS B 2 112 ? 11.936 30.951  61.731 1.00 30.71  ? 105 HIS N N   1 
ATOM   3567 C  CA  . HIS B 2 112 ? 10.686 30.983  60.980 1.00 33.78  ? 105 HIS N CA  1 
ATOM   3568 C  C   . HIS B 2 112 ? 10.687 29.929  59.879 1.00 36.96  ? 105 HIS N C   1 
ATOM   3569 O  O   . HIS B 2 112 ? 9.757  29.121  59.774 1.00 37.28  ? 105 HIS N O   1 
ATOM   3570 C  CB  . HIS B 2 112 ? 10.484 32.392  60.415 1.00 30.05  ? 105 HIS N CB  1 
ATOM   3571 C  CG  . HIS B 2 112 ? 9.341  32.505  59.459 1.00 29.06  ? 105 HIS N CG  1 
ATOM   3572 N  ND1 . HIS B 2 112 ? 8.050  32.735  59.877 1.00 27.63  ? 105 HIS N ND1 1 
ATOM   3573 C  CD2 . HIS B 2 112 ? 9.293  32.414  58.107 1.00 27.33  ? 105 HIS N CD2 1 
ATOM   3574 C  CE1 . HIS B 2 112 ? 7.250  32.781  58.822 1.00 30.54  ? 105 HIS N CE1 1 
ATOM   3575 N  NE2 . HIS B 2 112 ? 7.981  32.608  57.734 1.00 28.70  ? 105 HIS N NE2 1 
ATOM   3576 N  N   . VAL B 2 113 ? 11.756 29.883  59.081 1.00 39.15  ? 106 VAL N N   1 
ATOM   3577 C  CA  . VAL B 2 113 ? 11.770 28.985  57.922 1.00 35.83  ? 106 VAL N CA  1 
ATOM   3578 C  C   . VAL B 2 113 ? 11.972 27.541  58.361 1.00 34.18  ? 106 VAL N C   1 
ATOM   3579 O  O   . VAL B 2 113 ? 11.318 26.623  57.849 1.00 32.26  ? 106 VAL N O   1 
ATOM   3580 C  CB  . VAL B 2 113 ? 12.857 29.427  56.928 1.00 36.17  ? 106 VAL N CB  1 
ATOM   3581 C  CG1 . VAL B 2 113 ? 13.042 28.376  55.837 1.00 37.89  ? 106 VAL N CG1 1 
ATOM   3582 C  CG2 . VAL B 2 113 ? 12.528 30.787  56.358 1.00 35.36  ? 106 VAL N CG2 1 
ATOM   3583 N  N   . MET B 2 114 ? 12.864 27.323  59.333 1.00 32.89  ? 107 MET N N   1 
ATOM   3584 C  CA  . MET B 2 114 ? 13.145 25.975  59.818 1.00 36.15  ? 107 MET N CA  1 
ATOM   3585 C  C   . MET B 2 114 ? 11.902 25.344  60.437 1.00 39.18  ? 107 MET N C   1 
ATOM   3586 O  O   . MET B 2 114 ? 11.601 24.167  60.193 1.00 35.36  ? 107 MET N O   1 
ATOM   3587 C  CB  . MET B 2 114 ? 14.293 26.039  60.825 1.00 39.73  ? 107 MET N CB  1 
ATOM   3588 C  CG  . MET B 2 114 ? 15.663 26.304  60.194 1.00 41.15  ? 107 MET N CG  1 
ATOM   3589 S  SD  . MET B 2 114 ? 16.064 25.142  58.883 1.00 41.55  ? 107 MET N SD  1 
ATOM   3590 C  CE  . MET B 2 114 ? 16.095 26.142  57.411 1.00 44.18  ? 107 MET N CE  1 
ATOM   3591 N  N   . THR B 2 115 ? 11.151 26.123  61.223 1.00 38.11  ? 108 THR N N   1 
ATOM   3592 C  CA  . THR B 2 115 ? 9.892  25.619  61.758 1.00 37.02  ? 108 THR N CA  1 
ATOM   3593 C  C   . THR B 2 115 ? 8.880  25.385  60.641 1.00 39.09  ? 108 THR N C   1 
ATOM   3594 O  O   . THR B 2 115 ? 8.118  24.413  60.673 1.00 33.87  ? 108 THR N O   1 
ATOM   3595 C  CB  . THR B 2 115 ? 9.351  26.592  62.795 1.00 38.30  ? 108 THR N CB  1 
ATOM   3596 O  OG1 . THR B 2 115 ? 10.199 26.532  63.947 1.00 39.80  ? 108 THR N OG1 1 
ATOM   3597 C  CG2 . THR B 2 115 ? 7.936  26.209  63.205 1.00 47.23  ? 108 THR N CG2 1 
ATOM   3598 N  N   . ASN B 2 116 ? 8.888  26.233  59.614 1.00 37.15  ? 109 ASN N N   1 
ATOM   3599 C  CA  . ASN B 2 116 ? 7.962  25.979  58.519 1.00 34.85  ? 109 ASN N CA  1 
ATOM   3600 C  C   . ASN B 2 116 ? 8.281  24.663  57.827 1.00 32.49  ? 109 ASN N C   1 
ATOM   3601 O  O   . ASN B 2 116 ? 7.365  23.930  57.454 1.00 34.08  ? 109 ASN N O   1 
ATOM   3602 C  CB  . ASN B 2 116 ? 7.961  27.155  57.547 1.00 35.84  ? 109 ASN N CB  1 
ATOM   3603 C  CG  . ASN B 2 116 ? 7.086  28.305  58.047 1.00 33.82  ? 109 ASN N CG  1 
ATOM   3604 O  OD1 . ASN B 2 116 ? 6.297  28.132  58.973 1.00 34.30  ? 109 ASN N OD1 1 
ATOM   3605 N  ND2 . ASN B 2 116 ? 7.246  29.481  57.458 1.00 32.22  ? 109 ASN N ND2 1 
ATOM   3606 N  N   . LEU B 2 117 ? 9.555  24.306  57.740 1.00 34.32  ? 110 LEU N N   1 
ATOM   3607 C  CA  . LEU B 2 117 ? 9.976  23.077  57.083 1.00 33.49  ? 110 LEU N CA  1 
ATOM   3608 C  C   . LEU B 2 117 ? 9.840  21.839  57.953 1.00 32.99  ? 110 LEU N C   1 
ATOM   3609 O  O   . LEU B 2 117 ? 9.994  20.736  57.428 1.00 38.40  ? 110 LEU N O   1 
ATOM   3610 C  CB  . LEU B 2 117 ? 11.430 23.199  56.611 1.00 35.92  ? 110 LEU N CB  1 
ATOM   3611 C  CG  . LEU B 2 117 ? 11.646 24.124  55.404 1.00 35.58  ? 110 LEU N CG  1 
ATOM   3612 C  CD1 . LEU B 2 117 ? 13.126 24.320  55.142 1.00 33.74  ? 110 LEU N CD1 1 
ATOM   3613 C  CD2 . LEU B 2 117 ? 10.924 23.603  54.167 1.00 34.14  ? 110 LEU N CD2 1 
ATOM   3614 N  N   . GLY B 2 118 ? 9.565  21.976  59.252 1.00 36.32  ? 111 GLY N N   1 
ATOM   3615 C  CA  . GLY B 2 118 ? 9.532  20.817  60.125 1.00 31.23  ? 111 GLY N CA  1 
ATOM   3616 C  C   . GLY B 2 118 ? 10.886 20.420  60.661 1.00 36.15  ? 111 GLY N C   1 
ATOM   3617 O  O   . GLY B 2 118 ? 11.045 19.305  61.173 1.00 37.10  ? 111 GLY N O   1 
ATOM   3618 N  N   . GLU B 2 119 ? 11.881 21.301  60.570 1.00 38.69  ? 112 GLU N N   1 
ATOM   3619 C  CA  . GLU B 2 119 ? 13.206 21.011  61.101 1.00 37.94  ? 112 GLU N CA  1 
ATOM   3620 C  C   . GLU B 2 119 ? 13.231 21.387  62.573 1.00 39.79  ? 112 GLU N C   1 
ATOM   3621 O  O   . GLU B 2 119 ? 12.975 22.543  62.931 1.00 54.83  ? 112 GLU N O   1 
ATOM   3622 C  CB  . GLU B 2 119 ? 14.288 21.754  60.312 1.00 34.73  ? 112 GLU N CB  1 
ATOM   3623 C  CG  . GLU B 2 119 ? 14.186 21.565  58.798 1.00 35.57  ? 112 GLU N CG  1 
ATOM   3624 C  CD  . GLU B 2 119 ? 14.428 20.121  58.352 1.00 38.42  ? 112 GLU N CD  1 
ATOM   3625 O  OE1 . GLU B 2 119 ? 14.420 19.199  59.191 1.00 37.84  ? 112 GLU N OE1 1 
ATOM   3626 O  OE2 . GLU B 2 119 ? 14.658 19.898  57.151 1.00 41.73  ? 112 GLU N OE2 1 
ATOM   3627 N  N   . LYS B 2 120 ? 13.505 20.416  63.428 1.00 41.76  ? 113 LYS N N   1 
ATOM   3628 C  CA  . LYS B 2 120 ? 13.500 20.669  64.860 1.00 48.28  ? 113 LYS N CA  1 
ATOM   3629 C  C   . LYS B 2 120 ? 14.862 21.215  65.245 1.00 51.09  ? 113 LYS N C   1 
ATOM   3630 O  O   . LYS B 2 120 ? 15.888 20.568  64.999 1.00 59.50  ? 113 LYS N O   1 
ATOM   3631 C  CB  . LYS B 2 120 ? 13.168 19.405  65.649 1.00 53.19  ? 113 LYS N CB  1 
ATOM   3632 C  CG  . LYS B 2 120 ? 11.721 19.354  66.093 1.00 57.38  ? 113 LYS N CG  1 
ATOM   3633 C  CD  . LYS B 2 120 ? 10.878 18.583  65.101 1.00 63.17  ? 113 LYS N CD  1 
ATOM   3634 C  CE  . LYS B 2 120 ? 10.813 17.113  65.471 1.00 72.30  ? 113 LYS N CE  1 
ATOM   3635 N  NZ  . LYS B 2 120 ? 10.043 16.319  64.467 1.00 74.72  ? 113 LYS N NZ  1 
ATOM   3636 N  N   . LEU B 2 121 ? 14.872 22.428  65.795 1.00 47.22  ? 114 LEU N N   1 
ATOM   3637 C  CA  . LEU B 2 121 ? 16.063 23.015  66.388 1.00 40.34  ? 114 LEU N CA  1 
ATOM   3638 C  C   . LEU B 2 121 ? 15.684 23.649  67.711 1.00 38.15  ? 114 LEU N C   1 
ATOM   3639 O  O   . LEU B 2 121 ? 14.633 24.290  67.814 1.00 36.97  ? 114 LEU N O   1 
ATOM   3640 C  CB  . LEU B 2 121 ? 16.695 24.086  65.499 1.00 42.58  ? 114 LEU N CB  1 
ATOM   3641 C  CG  . LEU B 2 121 ? 16.983 23.716  64.048 1.00 47.70  ? 114 LEU N CG  1 
ATOM   3642 C  CD1 . LEU B 2 121 ? 16.792 24.938  63.134 1.00 45.19  ? 114 LEU N CD1 1 
ATOM   3643 C  CD2 . LEU B 2 121 ? 18.383 23.069  63.908 1.00 46.09  ? 114 LEU N CD2 1 
ATOM   3644 N  N   . THR B 2 122 ? 16.538 23.480  68.716 1.00 34.58  ? 115 THR N N   1 
ATOM   3645 C  CA  . THR B 2 122 ? 16.394 24.299  69.905 1.00 36.36  ? 115 THR N CA  1 
ATOM   3646 C  C   . THR B 2 122 ? 16.758 25.746  69.586 1.00 37.72  ? 115 THR N C   1 
ATOM   3647 O  O   . THR B 2 122 ? 17.385 26.050  68.564 1.00 36.73  ? 115 THR N O   1 
ATOM   3648 C  CB  . THR B 2 122 ? 17.303 23.820  71.043 1.00 37.44  ? 115 THR N CB  1 
ATOM   3649 O  OG1 . THR B 2 122 ? 18.662 24.111  70.698 1.00 36.28  ? 115 THR N OG1 1 
ATOM   3650 C  CG2 . THR B 2 122 ? 17.143 22.336  71.308 1.00 36.60  ? 115 THR N CG2 1 
ATOM   3651 N  N   . ASP B 2 123 ? 16.390 26.643  70.511 1.00 39.31  ? 116 ASP N N   1 
ATOM   3652 C  CA  . ASP B 2 123 ? 16.790 28.045  70.399 1.00 42.29  ? 116 ASP N CA  1 
ATOM   3653 C  C   . ASP B 2 123 ? 18.307 28.191  70.336 1.00 44.02  ? 116 ASP N C   1 
ATOM   3654 O  O   . ASP B 2 123 ? 18.831 29.009  69.566 1.00 42.31  ? 116 ASP N O   1 
ATOM   3655 C  CB  . ASP B 2 123 ? 16.222 28.844  71.571 1.00 41.52  ? 116 ASP N CB  1 
ATOM   3656 C  CG  . ASP B 2 123 ? 14.704 28.831  71.593 1.00 43.87  ? 116 ASP N CG  1 
ATOM   3657 O  OD1 . ASP B 2 123 ? 14.093 28.647  70.513 1.00 45.94  ? 116 ASP N OD1 1 
ATOM   3658 O  OD2 . ASP B 2 123 ? 14.122 28.997  72.685 1.00 45.47  ? 116 ASP N OD2 1 
ATOM   3659 N  N   . GLU B 2 124 ? 19.031 27.387  71.122 1.00 42.52  ? 117 GLU N N   1 
ATOM   3660 C  CA  . GLU B 2 124 ? 20.490 27.461  71.121 1.00 39.29  ? 117 GLU N CA  1 
ATOM   3661 C  C   . GLU B 2 124 ? 21.064 27.048  69.767 1.00 36.74  ? 117 GLU N C   1 
ATOM   3662 O  O   . GLU B 2 124 ? 22.031 27.643  69.289 1.00 34.62  ? 117 GLU N O   1 
ATOM   3663 C  CB  . GLU B 2 124 ? 21.050 26.587  72.241 1.00 40.30  ? 117 GLU N CB  1 
ATOM   3664 C  CG  . GLU B 2 124 ? 20.285 26.744  73.543 1.00 51.81  ? 117 GLU N CG  1 
ATOM   3665 C  CD  . GLU B 2 124 ? 21.148 27.135  74.721 1.00 52.53  ? 117 GLU N CD  1 
ATOM   3666 O  OE1 . GLU B 2 124 ? 22.162 27.852  74.527 1.00 74.45  ? 117 GLU N OE1 1 
ATOM   3667 O  OE2 . GLU B 2 124 ? 20.816 26.700  75.845 1.00 53.74  ? 117 GLU N OE2 1 
ATOM   3668 N  N   . GLU B 2 125 ? 20.485 26.040  69.127 1.00 35.86  ? 118 GLU N N   1 
ATOM   3669 C  CA  . GLU B 2 125 ? 20.988 25.661  67.808 1.00 35.74  ? 118 GLU N CA  1 
ATOM   3670 C  C   . GLU B 2 125 ? 20.775 26.778  66.794 1.00 32.53  ? 118 GLU N C   1 
ATOM   3671 O  O   . GLU B 2 125 ? 21.667 27.076  66.001 1.00 33.20  ? 118 GLU N O   1 
ATOM   3672 C  CB  . GLU B 2 125 ? 20.314 24.377  67.342 1.00 34.97  ? 118 GLU N CB  1 
ATOM   3673 C  CG  . GLU B 2 125 ? 20.807 23.139  68.027 1.00 34.54  ? 118 GLU N CG  1 
ATOM   3674 C  CD  . GLU B 2 125 ? 20.026 21.935  67.597 1.00 39.21  ? 118 GLU N CD  1 
ATOM   3675 O  OE1 . GLU B 2 125 ? 18.873 21.808  68.054 1.00 41.07  ? 118 GLU N OE1 1 
ATOM   3676 O  OE2 . GLU B 2 125 ? 20.548 21.141  66.785 1.00 39.44  ? 118 GLU N OE2 1 
ATOM   3677 N  N   . VAL B 2 126 ? 19.600 27.423  66.825 1.00 35.08  ? 119 VAL N N   1 
ATOM   3678 C  CA  . VAL B 2 126 ? 19.341 28.562  65.947 1.00 36.71  ? 119 VAL N CA  1 
ATOM   3679 C  C   . VAL B 2 126 ? 20.370 29.652  66.190 1.00 39.38  ? 119 VAL N C   1 
ATOM   3680 O  O   . VAL B 2 126 ? 20.978 30.180  65.251 1.00 34.48  ? 119 VAL N O   1 
ATOM   3681 C  CB  . VAL B 2 126 ? 17.911 29.099  66.150 1.00 40.11  ? 119 VAL N CB  1 
ATOM   3682 C  CG1 . VAL B 2 126 ? 17.795 30.505  65.580 1.00 39.94  ? 119 VAL N CG1 1 
ATOM   3683 C  CG2 . VAL B 2 126 ? 16.892 28.200  65.463 1.00 39.35  ? 119 VAL N CG2 1 
ATOM   3684 N  N   . ASP B 2 127 ? 20.583 30.001  67.463 1.00 36.83  ? 120 ASP N N   1 
ATOM   3685 C  CA  . ASP B 2 127 ? 21.557 31.031  67.774 1.00 39.30  ? 120 ASP N CA  1 
ATOM   3686 C  C   . ASP B 2 127 ? 22.949 30.609  67.326 1.00 38.07  ? 120 ASP N C   1 
ATOM   3687 O  O   . ASP B 2 127 ? 23.697 31.420  66.767 1.00 35.64  ? 120 ASP N O   1 
ATOM   3688 C  CB  . ASP B 2 127 ? 21.513 31.360  69.269 1.00 42.60  ? 120 ASP N CB  1 
ATOM   3689 C  CG  . ASP B 2 127 ? 20.298 32.187  69.631 1.00 42.51  ? 120 ASP N CG  1 
ATOM   3690 O  OD1 . ASP B 2 127 ? 19.720 32.807  68.714 1.00 43.71  ? 120 ASP N OD1 1 
ATOM   3691 O  OD2 . ASP B 2 127 ? 19.920 32.232  70.815 1.00 42.65  ? 120 ASP N OD2 1 
ATOM   3692 N  N   . GLU B 2 128 ? 23.289 29.329  67.511 1.00 35.78  ? 121 GLU N N   1 
ATOM   3693 C  CA  . GLU B 2 128 ? 24.591 28.837  67.078 1.00 34.62  ? 121 GLU N CA  1 
ATOM   3694 C  C   . GLU B 2 128 ? 24.714 28.841  65.547 1.00 34.80  ? 121 GLU N C   1 
ATOM   3695 O  O   . GLU B 2 128 ? 25.782 29.136  65.003 1.00 32.74  ? 121 GLU N O   1 
ATOM   3696 C  CB  . GLU B 2 128 ? 24.824 27.442  67.656 1.00 35.29  ? 121 GLU N CB  1 
ATOM   3697 C  CG  . GLU B 2 128 ? 26.135 26.818  67.270 1.00 37.78  ? 121 GLU N CG  1 
ATOM   3698 C  CD  . GLU B 2 128 ? 27.344 27.572  67.834 1.00 41.40  ? 121 GLU N CD  1 
ATOM   3699 O  OE1 . GLU B 2 128 ? 27.244 28.176  68.924 1.00 37.73  ? 121 GLU N OE1 1 
ATOM   3700 O  OE2 . GLU B 2 128 ? 28.403 27.566  67.182 1.00 39.07  ? 121 GLU N OE2 1 
ATOM   3701 N  N   . MET B 2 129 ? 23.644 28.525  64.823 1.00 36.40  ? 122 MET N N   1 
ATOM   3702 C  CA  . MET B 2 129 ? 23.752 28.624  63.365 1.00 35.81  ? 122 MET N CA  1 
ATOM   3703 C  C   . MET B 2 129 ? 24.008 30.065  62.948 1.00 38.47  ? 122 MET N C   1 
ATOM   3704 O  O   . MET B 2 129 ? 24.762 30.318  62.001 1.00 41.15  ? 122 MET N O   1 
ATOM   3705 C  CB  . MET B 2 129 ? 22.491 28.081  62.685 1.00 35.98  ? 122 MET N CB  1 
ATOM   3706 C  CG  . MET B 2 129 ? 22.150 26.673  63.103 1.00 33.88  ? 122 MET N CG  1 
ATOM   3707 S  SD  . MET B 2 129 ? 20.694 25.875  62.388 1.00 34.03  ? 122 MET N SD  1 
ATOM   3708 C  CE  . MET B 2 129 ? 20.828 26.177  60.619 1.00 30.51  ? 122 MET N CE  1 
ATOM   3709 N  N   . ILE B 2 130 ? 23.401 31.029  63.660 1.00 40.46  ? 123 ILE N N   1 
ATOM   3710 C  CA  . ILE B 2 130 ? 23.601 32.441  63.337 1.00 33.20  ? 123 ILE N CA  1 
ATOM   3711 C  C   . ILE B 2 130 ? 25.042 32.844  63.606 1.00 35.53  ? 123 ILE N C   1 
ATOM   3712 O  O   . ILE B 2 130 ? 25.718 33.429  62.746 1.00 36.99  ? 123 ILE N O   1 
ATOM   3713 C  CB  . ILE B 2 130 ? 22.621 33.325  64.126 1.00 32.48  ? 123 ILE N CB  1 
ATOM   3714 C  CG1 . ILE B 2 130 ? 21.171 33.099  63.651 1.00 32.22  ? 123 ILE N CG1 1 
ATOM   3715 C  CG2 . ILE B 2 130 ? 23.002 34.796  63.949 1.00 34.52  ? 123 ILE N CG2 1 
ATOM   3716 C  CD1 . ILE B 2 130 ? 20.939 33.492  62.170 1.00 29.08  ? 123 ILE N CD1 1 
ATOM   3717 N  N   . ARG B 2 131 ? 25.528 32.534  64.813 1.00 32.79  ? 124 ARG N N   1 
ATOM   3718 C  CA  . ARG B 2 131 ? 26.876 32.902  65.226 1.00 36.62  ? 124 ARG N CA  1 
ATOM   3719 C  C   . ARG B 2 131 ? 27.922 32.455  64.210 1.00 35.32  ? 124 ARG N C   1 
ATOM   3720 O  O   . ARG B 2 131 ? 28.703 33.274  63.718 1.00 37.88  ? 124 ARG N O   1 
ATOM   3721 C  CB  . ARG B 2 131 ? 27.149 32.307  66.614 1.00 37.99  ? 124 ARG N CB  1 
ATOM   3722 C  CG  . ARG B 2 131 ? 28.591 32.119  66.932 1.00 37.76  ? 124 ARG N CG  1 
ATOM   3723 C  CD  . ARG B 2 131 ? 28.780 31.517  68.325 1.00 39.21  ? 124 ARG N CD  1 
ATOM   3724 N  NE  . ARG B 2 131 ? 30.188 31.568  68.694 1.00 39.51  ? 124 ARG N NE  1 
ATOM   3725 C  CZ  . ARG B 2 131 ? 31.066 30.603  68.452 1.00 42.33  ? 124 ARG N CZ  1 
ATOM   3726 N  NH1 . ARG B 2 131 ? 30.699 29.446  67.921 1.00 44.95  ? 124 ARG N NH1 1 
ATOM   3727 N  NH2 . ARG B 2 131 ? 32.343 30.798  68.764 1.00 45.86  ? 124 ARG N NH2 1 
ATOM   3728 N  N   . GLU B 2 132 ? 27.921 31.163  63.850 1.00 36.16  ? 125 GLU N N   1 
ATOM   3729 C  CA  . GLU B 2 132 ? 28.943 30.613  62.951 1.00 35.40  ? 125 GLU N CA  1 
ATOM   3730 C  C   . GLU B 2 132 ? 28.850 31.203  61.545 1.00 36.49  ? 125 GLU N C   1 
ATOM   3731 O  O   . GLU B 2 132 ? 29.872 31.404  60.876 1.00 33.45  ? 125 GLU N O   1 
ATOM   3732 C  CB  . GLU B 2 132 ? 28.806 29.098  62.875 1.00 31.95  ? 125 GLU N CB  1 
ATOM   3733 C  CG  . GLU B 2 132 ? 28.892 28.427  64.225 1.00 37.32  ? 125 GLU N CG  1 
ATOM   3734 C  CD  . GLU B 2 132 ? 28.942 26.917  64.106 1.00 36.45  ? 125 GLU N CD  1 
ATOM   3735 O  OE1 . GLU B 2 132 ? 29.206 26.417  62.991 1.00 32.71  ? 125 GLU N OE1 1 
ATOM   3736 O  OE2 . GLU B 2 132 ? 28.722 26.233  65.123 1.00 32.57  ? 125 GLU N OE2 1 
ATOM   3737 N  N   . ALA B 2 133 ? 27.639 31.464  61.074 1.00 31.68  ? 126 ALA N N   1 
ATOM   3738 C  CA  . ALA B 2 133 ? 27.477 32.091  59.771 1.00 35.62  ? 126 ALA N CA  1 
ATOM   3739 C  C   . ALA B 2 133 ? 27.911 33.552  59.790 1.00 34.72  ? 126 ALA N C   1 
ATOM   3740 O  O   . ALA B 2 133 ? 28.251 34.113  58.732 1.00 29.48  ? 126 ALA N O   1 
ATOM   3741 C  CB  . ALA B 2 133 ? 26.006 31.983  59.339 1.00 33.24  ? 126 ALA N CB  1 
ATOM   3742 N  N   . ASP B 2 134 ? 27.929 34.164  60.977 1.00 32.16  ? 127 ASP N N   1 
ATOM   3743 C  CA  . ASP B 2 134 ? 28.037 35.616  61.121 1.00 36.08  ? 127 ASP N CA  1 
ATOM   3744 C  C   . ASP B 2 134 ? 29.506 36.013  61.198 1.00 41.43  ? 127 ASP N C   1 
ATOM   3745 O  O   . ASP B 2 134 ? 30.070 36.228  62.274 1.00 43.05  ? 127 ASP N O   1 
ATOM   3746 C  CB  . ASP B 2 134 ? 27.269 36.067  62.358 1.00 35.86  ? 127 ASP N CB  1 
ATOM   3747 C  CG  . ASP B 2 134 ? 27.411 37.532  62.624 1.00 35.76  ? 127 ASP N CG  1 
ATOM   3748 O  OD1 . ASP B 2 134 ? 27.749 38.269  61.687 1.00 31.03  ? 127 ASP N OD1 1 
ATOM   3749 O  OD2 . ASP B 2 134 ? 27.198 37.951  63.780 1.00 34.73  ? 127 ASP N OD2 1 
ATOM   3750 N  N   . ILE B 2 135 ? 30.119 36.140  60.018 1.00 42.49  ? 128 ILE N N   1 
ATOM   3751 C  CA  . ILE B 2 135 ? 31.545 36.443  59.922 1.00 46.65  ? 128 ILE N CA  1 
ATOM   3752 C  C   . ILE B 2 135 ? 31.881 37.754  60.621 1.00 46.91  ? 128 ILE N C   1 
ATOM   3753 O  O   . ILE B 2 135 ? 32.826 37.818  61.415 1.00 46.73  ? 128 ILE N O   1 
ATOM   3754 C  CB  . ILE B 2 135 ? 31.988 36.472  58.448 1.00 49.86  ? 128 ILE N CB  1 
ATOM   3755 C  CG1 . ILE B 2 135 ? 31.345 35.315  57.690 1.00 45.47  ? 128 ILE N CG1 1 
ATOM   3756 C  CG2 . ILE B 2 135 ? 33.502 36.473  58.344 1.00 42.92  ? 128 ILE N CG2 1 
ATOM   3757 C  CD1 . ILE B 2 135 ? 31.991 33.992  57.986 1.00 48.96  ? 128 ILE N CD1 1 
ATOM   3758 N  N   . ASP B 2 136 ? 31.125 38.819  60.340 1.00 44.49  ? 129 ASP N N   1 
ATOM   3759 C  CA  . ASP B 2 136 ? 31.509 40.131  60.844 1.00 43.56  ? 129 ASP N CA  1 
ATOM   3760 C  C   . ASP B 2 136 ? 31.000 40.417  62.249 1.00 44.53  ? 129 ASP N C   1 
ATOM   3761 O  O   . ASP B 2 136 ? 31.237 41.518  62.754 1.00 53.33  ? 129 ASP N O   1 
ATOM   3762 C  CB  . ASP B 2 136 ? 31.057 41.254  59.889 1.00 44.23  ? 129 ASP N CB  1 
ATOM   3763 C  CG  . ASP B 2 136 ? 29.548 41.343  59.728 1.00 44.42  ? 129 ASP N CG  1 
ATOM   3764 O  OD1 . ASP B 2 136 ? 28.798 40.733  60.505 1.00 44.04  ? 129 ASP N OD1 1 
ATOM   3765 O  OD2 . ASP B 2 136 ? 29.108 42.044  58.801 1.00 46.36  ? 129 ASP N OD2 1 
ATOM   3766 N  N   . GLY B 2 137 ? 30.309 39.471  62.884 1.00 40.12  ? 130 GLY N N   1 
ATOM   3767 C  CA  . GLY B 2 137 ? 29.902 39.629  64.268 1.00 40.24  ? 130 GLY N CA  1 
ATOM   3768 C  C   . GLY B 2 137 ? 28.813 40.653  64.551 1.00 45.91  ? 130 GLY N C   1 
ATOM   3769 O  O   . GLY B 2 137 ? 28.626 41.025  65.710 1.00 46.31  ? 130 GLY N O   1 
ATOM   3770 N  N   . ASP B 2 138 ? 28.073 41.120  63.542 1.00 44.73  ? 131 ASP N N   1 
ATOM   3771 C  CA  . ASP B 2 138 ? 26.968 42.029  63.831 1.00 45.21  ? 131 ASP N CA  1 
ATOM   3772 C  C   . ASP B 2 138 ? 25.717 41.311  64.319 1.00 44.49  ? 131 ASP N C   1 
ATOM   3773 O  O   . ASP B 2 138 ? 24.749 41.979  64.686 1.00 52.01  ? 131 ASP N O   1 
ATOM   3774 C  CB  . ASP B 2 138 ? 26.630 42.922  62.607 1.00 42.91  ? 131 ASP N CB  1 
ATOM   3775 C  CG  . ASP B 2 138 ? 25.997 42.162  61.441 1.00 45.19  ? 131 ASP N CG  1 
ATOM   3776 O  OD1 . ASP B 2 138 ? 25.935 40.915  61.467 1.00 44.18  ? 131 ASP N OD1 1 
ATOM   3777 O  OD2 . ASP B 2 138 ? 25.578 42.831  60.465 1.00 42.52  ? 131 ASP N OD2 1 
ATOM   3778 N  N   . GLY B 2 139 ? 25.707 39.982  64.347 1.00 47.75  ? 132 GLY N N   1 
ATOM   3779 C  CA  . GLY B 2 139 ? 24.561 39.243  64.863 1.00 40.34  ? 132 GLY N CA  1 
ATOM   3780 C  C   . GLY B 2 139 ? 23.498 38.875  63.848 1.00 39.32  ? 132 GLY N C   1 
ATOM   3781 O  O   . GLY B 2 139 ? 22.405 38.450  64.248 1.00 37.87  ? 132 GLY N O   1 
ATOM   3782 N  N   . GLN B 2 140 ? 23.782 39.021  62.556 1.00 35.33  ? 133 GLN N N   1 
ATOM   3783 C  CA  . GLN B 2 140 ? 22.829 38.766  61.482 1.00 38.66  ? 133 GLN N CA  1 
ATOM   3784 C  C   . GLN B 2 140 ? 23.634 38.286  60.293 1.00 35.83  ? 133 GLN N C   1 
ATOM   3785 O  O   . GLN B 2 140 ? 24.825 38.570  60.190 1.00 37.02  ? 133 GLN N O   1 
ATOM   3786 C  CB  . GLN B 2 140 ? 22.045 40.018  61.065 1.00 43.96  ? 133 GLN N CB  1 
ATOM   3787 C  CG  . GLN B 2 140 ? 21.519 40.867  62.178 1.00 51.45  ? 133 GLN N CG  1 
ATOM   3788 C  CD  . GLN B 2 140 ? 20.013 40.770  62.296 1.00 53.93  ? 133 GLN N CD  1 
ATOM   3789 O  OE1 . GLN B 2 140 ? 19.282 40.982  61.319 1.00 48.12  ? 133 GLN N OE1 1 
ATOM   3790 N  NE2 . GLN B 2 140 ? 19.535 40.448  63.499 1.00 55.77  ? 133 GLN N NE2 1 
ATOM   3791 N  N   . VAL B 2 141 ? 22.987 37.582  59.381 1.00 33.63  ? 134 VAL N N   1 
ATOM   3792 C  CA  . VAL B 2 141 ? 23.702 36.990  58.257 1.00 33.29  ? 134 VAL N CA  1 
ATOM   3793 C  C   . VAL B 2 141 ? 23.344 37.780  57.010 1.00 31.02  ? 134 VAL N C   1 
ATOM   3794 O  O   . VAL B 2 141 ? 22.179 37.786  56.585 1.00 35.05  ? 134 VAL N O   1 
ATOM   3795 C  CB  . VAL B 2 141 ? 23.381 35.497  58.106 1.00 31.17  ? 134 VAL N CB  1 
ATOM   3796 C  CG1 . VAL B 2 141 ? 24.327 34.848  57.107 1.00 29.91  ? 134 VAL N CG1 1 
ATOM   3797 C  CG2 . VAL B 2 141 ? 23.493 34.830  59.441 1.00 30.29  ? 134 VAL N CG2 1 
ATOM   3798 N  N   . ASN B 2 142 ? 24.324 38.474  56.434 1.00 30.06  ? 135 ASN N N   1 
ATOM   3799 C  CA  . ASN B 2 142 ? 24.072 39.206  55.196 1.00 34.10  ? 135 ASN N CA  1 
ATOM   3800 C  C   . ASN B 2 142 ? 24.253 38.274  53.990 1.00 29.86  ? 135 ASN N C   1 
ATOM   3801 O  O   . ASN B 2 142 ? 24.426 37.056  54.127 1.00 34.44  ? 135 ASN N O   1 
ATOM   3802 C  CB  . ASN B 2 142 ? 24.948 40.469  55.109 1.00 32.97  ? 135 ASN N CB  1 
ATOM   3803 C  CG  . ASN B 2 142 ? 26.448 40.173  55.048 1.00 35.29  ? 135 ASN N CG  1 
ATOM   3804 O  OD1 . ASN B 2 142 ? 26.875 39.037  54.816 1.00 34.69  ? 135 ASN N OD1 1 
ATOM   3805 N  ND2 . ASN B 2 142 ? 27.255 41.214  55.239 1.00 34.24  ? 135 ASN N ND2 1 
ATOM   3806 N  N   . TYR B 2 143 ? 24.234 38.847  52.785 1.00 28.41  ? 136 TYR N N   1 
ATOM   3807 C  CA  . TYR B 2 143 ? 24.220 38.018  51.584 1.00 30.43  ? 136 TYR N CA  1 
ATOM   3808 C  C   . TYR B 2 143 ? 25.563 37.322  51.361 1.00 33.61  ? 136 TYR N C   1 
ATOM   3809 O  O   . TYR B 2 143 ? 25.604 36.135  51.014 1.00 35.61  ? 136 TYR N O   1 
ATOM   3810 C  CB  . TYR B 2 143 ? 23.837 38.876  50.376 1.00 31.88  ? 136 TYR N CB  1 
ATOM   3811 C  CG  . TYR B 2 143 ? 23.947 38.137  49.066 1.00 33.51  ? 136 TYR N CG  1 
ATOM   3812 C  CD1 . TYR B 2 143 ? 23.193 37.000  48.821 1.00 39.28  ? 136 TYR N CD1 1 
ATOM   3813 C  CD2 . TYR B 2 143 ? 24.817 38.561  48.084 1.00 33.15  ? 136 TYR N CD2 1 
ATOM   3814 C  CE1 . TYR B 2 143 ? 23.299 36.305  47.614 1.00 39.52  ? 136 TYR N CE1 1 
ATOM   3815 C  CE2 . TYR B 2 143 ? 24.937 37.868  46.887 1.00 38.05  ? 136 TYR N CE2 1 
ATOM   3816 C  CZ  . TYR B 2 143 ? 24.178 36.746  46.658 1.00 38.42  ? 136 TYR N CZ  1 
ATOM   3817 O  OH  . TYR B 2 143 ? 24.295 36.072  45.456 1.00 47.87  ? 136 TYR N OH  1 
ATOM   3818 N  N   . GLU B 2 144 ? 26.673 38.044  51.546 1.00 38.66  ? 137 GLU N N   1 
ATOM   3819 C  CA  . GLU B 2 144 ? 27.987 37.453  51.307 1.00 42.61  ? 137 GLU N CA  1 
ATOM   3820 C  C   . GLU B 2 144 ? 28.268 36.353  52.317 1.00 37.31  ? 137 GLU N C   1 
ATOM   3821 O  O   . GLU B 2 144 ? 28.791 35.286  51.962 1.00 39.38  ? 137 GLU N O   1 
ATOM   3822 C  CB  . GLU B 2 144 ? 29.071 38.544  51.353 1.00 54.63  ? 137 GLU N CB  1 
ATOM   3823 C  CG  . GLU B 2 144 ? 30.398 38.168  52.070 1.00 67.29  ? 137 GLU N CG  1 
ATOM   3824 C  CD  . GLU B 2 144 ? 31.360 37.320  51.208 1.00 84.90  ? 137 GLU N CD  1 
ATOM   3825 O  OE1 . GLU B 2 144 ? 31.028 37.017  50.037 1.00 93.45  ? 137 GLU N OE1 1 
ATOM   3826 O  OE2 . GLU B 2 144 ? 32.462 36.969  51.697 1.00 80.54  ? 137 GLU N OE2 1 
ATOM   3827 N  N   . GLU B 2 145 ? 27.906 36.593  53.578 1.00 35.41  ? 138 GLU N N   1 
ATOM   3828 C  CA  . GLU B 2 145 ? 27.994 35.550  54.593 1.00 35.66  ? 138 GLU N CA  1 
ATOM   3829 C  C   . GLU B 2 145 ? 27.160 34.326  54.198 1.00 34.47  ? 138 GLU N C   1 
ATOM   3830 O  O   . GLU B 2 145 ? 27.640 33.183  54.242 1.00 34.73  ? 138 GLU N O   1 
ATOM   3831 C  CB  . GLU B 2 145 ? 27.549 36.127  55.947 1.00 34.32  ? 138 GLU N CB  1 
ATOM   3832 C  CG  . GLU B 2 145 ? 28.520 37.147  56.529 1.00 33.30  ? 138 GLU N CG  1 
ATOM   3833 C  CD  . GLU B 2 145 ? 27.920 37.954  57.682 1.00 38.75  ? 138 GLU N CD  1 
ATOM   3834 O  OE1 . GLU B 2 145 ? 26.688 38.153  57.679 1.00 36.76  ? 138 GLU N OE1 1 
ATOM   3835 O  OE2 . GLU B 2 145 ? 28.681 38.401  58.589 1.00 41.99  ? 138 GLU N OE2 1 
ATOM   3836 N  N   . PHE B 2 146 ? 25.907 34.550  53.794 1.00 36.87  ? 139 PHE N N   1 
ATOM   3837 C  CA  . PHE B 2 146 ? 25.077 33.440  53.342 1.00 36.62  ? 139 PHE N CA  1 
ATOM   3838 C  C   . PHE B 2 146 ? 25.757 32.684  52.220 1.00 35.34  ? 139 PHE N C   1 
ATOM   3839 O  O   . PHE B 2 146 ? 25.770 31.447  52.212 1.00 34.95  ? 139 PHE N O   1 
ATOM   3840 C  CB  . PHE B 2 146 ? 23.712 33.958  52.886 1.00 35.07  ? 139 PHE N CB  1 
ATOM   3841 C  CG  . PHE B 2 146 ? 22.689 32.878  52.663 1.00 30.03  ? 139 PHE N CG  1 
ATOM   3842 C  CD1 . PHE B 2 146 ? 22.133 32.190  53.742 1.00 28.30  ? 139 PHE N CD1 1 
ATOM   3843 C  CD2 . PHE B 2 146 ? 22.249 32.577  51.374 1.00 28.72  ? 139 PHE N CD2 1 
ATOM   3844 C  CE1 . PHE B 2 146 ? 21.162 31.196  53.548 1.00 29.92  ? 139 PHE N CE1 1 
ATOM   3845 C  CE2 . PHE B 2 146 ? 21.262 31.594  51.158 1.00 30.20  ? 139 PHE N CE2 1 
ATOM   3846 C  CZ  . PHE B 2 146 ? 20.729 30.886  52.234 1.00 29.43  ? 139 PHE N CZ  1 
ATOM   3847 N  N   . VAL B 2 147 ? 26.345 33.414  51.274 1.00 35.03  ? 140 VAL N N   1 
ATOM   3848 C  CA  . VAL B 2 147 ? 26.961 32.780  50.117 1.00 40.03  ? 140 VAL N CA  1 
ATOM   3849 C  C   . VAL B 2 147 ? 28.189 31.988  50.535 1.00 38.45  ? 140 VAL N C   1 
ATOM   3850 O  O   . VAL B 2 147 ? 28.440 30.893  50.018 1.00 40.62  ? 140 VAL N O   1 
ATOM   3851 C  CB  . VAL B 2 147 ? 27.305 33.836  49.049 1.00 41.52  ? 140 VAL N CB  1 
ATOM   3852 C  CG1 . VAL B 2 147 ? 28.401 33.317  48.113 1.00 41.69  ? 140 VAL N CG1 1 
ATOM   3853 C  CG2 . VAL B 2 147 ? 26.039 34.252  48.282 1.00 38.01  ? 140 VAL N CG2 1 
ATOM   3854 N  N   . THR B 2 148 ? 28.966 32.517  51.480 1.00 37.23  ? 141 THR N N   1 
ATOM   3855 C  CA  . THR B 2 148 ? 30.127 31.778  51.979 1.00 45.54  ? 141 THR N CA  1 
ATOM   3856 C  C   . THR B 2 148 ? 29.722 30.387  52.457 1.00 46.67  ? 141 THR N C   1 
ATOM   3857 O  O   . THR B 2 148 ? 30.255 29.371  51.992 1.00 42.49  ? 141 THR N O   1 
ATOM   3858 C  CB  . THR B 2 148 ? 30.805 32.555  53.115 1.00 42.54  ? 141 THR N CB  1 
ATOM   3859 O  OG1 . THR B 2 148 ? 31.256 33.831  52.634 1.00 38.62  ? 141 THR N OG1 1 
ATOM   3860 C  CG2 . THR B 2 148 ? 31.992 31.772  53.662 1.00 42.61  ? 141 THR N CG2 1 
ATOM   3861 N  N   . MET B 2 149 ? 28.744 30.327  53.363 1.00 45.06  ? 142 MET N N   1 
ATOM   3862 C  CA  . MET B 2 149 ? 28.274 29.037  53.870 1.00 45.56  ? 142 MET N CA  1 
ATOM   3863 C  C   . MET B 2 149 ? 27.611 28.189  52.783 1.00 42.36  ? 142 MET N C   1 
ATOM   3864 O  O   . MET B 2 149 ? 27.773 26.964  52.761 1.00 48.62  ? 142 MET N O   1 
ATOM   3865 C  CB  . MET B 2 149 ? 27.301 29.262  55.011 1.00 46.48  ? 142 MET N CB  1 
ATOM   3866 C  CG  . MET B 2 149 ? 26.185 28.264  55.009 1.00 54.66  ? 142 MET N CG  1 
ATOM   3867 S  SD  . MET B 2 149 ? 24.982 28.776  56.197 1.00 69.72  ? 142 MET N SD  1 
ATOM   3868 C  CE  . MET B 2 149 ? 26.022 28.923  57.621 1.00 65.13  ? 142 MET N CE  1 
ATOM   3869 N  N   . MET B 2 150 ? 26.839 28.803  51.890 1.00 43.19  ? 143 MET N N   1 
ATOM   3870 C  CA  . MET B 2 150 ? 26.094 28.007  50.916 1.00 45.41  ? 143 MET N CA  1 
ATOM   3871 C  C   . MET B 2 150 ? 27.005 27.377  49.878 1.00 45.94  ? 143 MET N C   1 
ATOM   3872 O  O   . MET B 2 150 ? 26.610 26.421  49.202 1.00 45.26  ? 143 MET N O   1 
ATOM   3873 C  CB  . MET B 2 150 ? 25.050 28.883  50.217 1.00 44.18  ? 143 MET N CB  1 
ATOM   3874 C  CG  . MET B 2 150 ? 23.836 29.176  51.090 1.00 44.35  ? 143 MET N CG  1 
ATOM   3875 S  SD  . MET B 2 150 ? 22.976 27.650  51.490 1.00 43.36  ? 143 MET N SD  1 
ATOM   3876 C  CE  . MET B 2 150 ? 22.545 27.264  49.848 1.00 48.81  ? 143 MET N CE  1 
ATOM   3877 N  N   . THR B 2 151 ? 28.211 27.892  49.728 1.00 50.84  ? 144 THR N N   1 
ATOM   3878 C  CA  . THR B 2 151 ? 29.093 27.438  48.675 1.00 52.73  ? 144 THR N CA  1 
ATOM   3879 C  C   . THR B 2 151 ? 30.229 26.571  49.189 1.00 57.17  ? 144 THR N C   1 
ATOM   3880 O  O   . THR B 2 151 ? 31.031 26.094  48.386 1.00 58.65  ? 144 THR N O   1 
ATOM   3881 C  CB  . THR B 2 151 ? 29.647 28.641  47.913 1.00 48.37  ? 144 THR N CB  1 
ATOM   3882 O  OG1 . THR B 2 151 ? 30.283 28.176  46.717 1.00 53.97  ? 144 THR N OG1 1 
ATOM   3883 C  CG2 . THR B 2 151 ? 30.643 29.403  48.776 1.00 41.79  ? 144 THR N CG2 1 
ATOM   3884 N  N   . SER B 2 152 ? 30.312 26.342  50.502 1.00 67.41  ? 145 SER N N   1 
ATOM   3885 C  CA  . SER B 2 152 ? 31.327 25.440  51.034 1.00 83.25  ? 145 SER N CA  1 
ATOM   3886 C  C   . SER B 2 152 ? 31.206 24.048  50.418 1.00 98.14  ? 145 SER N C   1 
ATOM   3887 O  O   . SER B 2 152 ? 32.203 23.471  49.963 1.00 97.10  ? 145 SER N O   1 
ATOM   3888 C  CB  . SER B 2 152 ? 31.213 25.370  52.557 1.00 83.60  ? 145 SER N CB  1 
ATOM   3889 O  OG  . SER B 2 152 ? 31.777 24.169  53.055 1.00 81.69  ? 145 SER N OG  1 
ATOM   3890 N  N   . LYS B 2 153 ? 29.987 23.501  50.383 1.00 96.20  ? 146 LYS N N   1 
ATOM   3891 C  CA  . LYS B 2 153 ? 29.727 22.147  49.887 1.00 96.98  ? 146 LYS N CA  1 
ATOM   3892 C  C   . LYS B 2 153 ? 30.507 21.091  50.685 1.00 97.81  ? 146 LYS N C   1 
ATOM   3893 O  O   . LYS B 2 153 ? 31.634 20.719  50.339 1.00 77.21  ? 146 LYS N O   1 
ATOM   3894 C  CB  . LYS B 2 153 ? 30.064 22.040  48.394 1.00 102.70 ? 146 LYS N CB  1 
ATOM   3895 C  CG  . LYS B 2 153 ? 29.298 23.011  47.500 1.00 104.28 ? 146 LYS N CG  1 
ATOM   3896 C  CD  . LYS B 2 153 ? 29.365 22.585  46.033 1.00 95.95  ? 146 LYS N CD  1 
ATOM   3897 C  CE  . LYS B 2 153 ? 28.789 23.652  45.121 1.00 93.16  ? 146 LYS N CE  1 
ATOM   3898 N  NZ  . LYS B 2 153 ? 27.562 24.275  45.700 1.00 91.49  ? 146 LYS N NZ  1 
ATOM   3899 N  N   . ASP C 3 2   ? 14.673 24.037  34.045 1.00 68.41  ? 2   ASP R N   1 
ATOM   3900 C  CA  . ASP C 3 2   ? 14.994 24.952  35.136 1.00 75.91  ? 2   ASP R CA  1 
ATOM   3901 C  C   . ASP C 3 2   ? 15.098 24.214  36.470 1.00 77.22  ? 2   ASP R C   1 
ATOM   3902 O  O   . ASP C 3 2   ? 16.190 24.092  37.045 1.00 68.06  ? 2   ASP R O   1 
ATOM   3903 C  CB  . ASP C 3 2   ? 13.943 26.067  35.244 1.00 69.28  ? 2   ASP R CB  1 
ATOM   3904 N  N   . GLU C 3 3   A 13.953 23.717  36.951 1.00 67.37  ? 2   GLU R N   1 
ATOM   3905 C  CA  . GLU C 3 3   A 13.837 23.183  38.311 1.00 66.15  ? 2   GLU R CA  1 
ATOM   3906 C  C   . GLU C 3 3   A 14.343 24.201  39.329 1.00 53.80  ? 2   GLU R C   1 
ATOM   3907 O  O   . GLU C 3 3   A 15.030 23.857  40.293 1.00 45.61  ? 2   GLU R O   1 
ATOM   3908 C  CB  . GLU C 3 3   A 14.581 21.852  38.469 1.00 72.02  ? 2   GLU R CB  1 
ATOM   3909 C  CG  . GLU C 3 3   A 14.059 20.699  37.628 1.00 71.79  ? 2   GLU R CG  1 
ATOM   3910 C  CD  . GLU C 3 3   A 15.117 20.143  36.670 1.00 82.04  ? 2   GLU R CD  1 
ATOM   3911 O  OE1 . GLU C 3 3   A 16.272 20.644  36.666 1.00 70.99  ? 2   GLU R OE1 1 
ATOM   3912 O  OE2 . GLU C 3 3   A 14.791 19.190  35.926 1.00 85.04  ? 2   GLU R OE2 1 
ATOM   3913 N  N   . ASN C 3 4   B 14.010 25.474  39.093 1.00 53.96  ? 2   ASN R N   1 
ATOM   3914 C  CA  . ASN C 3 4   B 14.521 26.551  39.931 1.00 58.43  ? 2   ASN R CA  1 
ATOM   3915 C  C   . ASN C 3 4   B 14.013 26.440  41.363 1.00 54.47  ? 2   ASN R C   1 
ATOM   3916 O  O   . ASN C 3 4   B 14.775 26.654  42.313 1.00 51.51  ? 2   ASN R O   1 
ATOM   3917 C  CB  . ASN C 3 4   B 14.130 27.909  39.341 1.00 64.87  ? 2   ASN R CB  1 
ATOM   3918 C  CG  . ASN C 3 4   B 15.311 28.642  38.720 1.00 71.73  ? 2   ASN R CG  1 
ATOM   3919 O  OD1 . ASN C 3 4   B 16.336 28.868  39.374 1.00 76.08  ? 2   ASN R OD1 1 
ATOM   3920 N  ND2 . ASN C 3 4   B 15.174 29.012  37.443 1.00 66.41  ? 2   ASN R ND2 1 
ATOM   3921 N  N   . ALA C 3 5   C 12.731 26.110  41.540 1.00 47.14  ? 2   ALA R N   1 
ATOM   3922 C  CA  . ALA C 3 5   C 12.140 26.181  42.872 1.00 44.54  ? 2   ALA R CA  1 
ATOM   3923 C  C   . ALA C 3 5   C 12.601 25.021  43.747 1.00 41.26  ? 2   ALA R C   1 
ATOM   3924 O  O   . ALA C 3 5   C 12.839 25.197  44.949 1.00 43.99  ? 2   ALA R O   1 
ATOM   3925 C  CB  . ALA C 3 5   C 10.617 26.205  42.771 1.00 44.34  ? 2   ALA R CB  1 
ATOM   3926 N  N   . ILE C 3 6   D 12.712 23.824  43.168 1.00 43.32  ? 2   ILE R N   1 
ATOM   3927 C  CA  . ILE C 3 6   D 13.175 22.674  43.934 1.00 37.45  ? 2   ILE R CA  1 
ATOM   3928 C  C   . ILE C 3 6   D 14.615 22.895  44.381 1.00 34.59  ? 2   ILE R C   1 
ATOM   3929 O  O   . ILE C 3 6   D 14.950 22.744  45.564 1.00 32.13  ? 2   ILE R O   1 
ATOM   3930 C  CB  . ILE C 3 6   D 13.022 21.386  43.112 1.00 40.74  ? 2   ILE R CB  1 
ATOM   3931 C  CG1 . ILE C 3 6   D 11.542 21.125  42.806 1.00 38.62  ? 2   ILE R CG1 1 
ATOM   3932 C  CG2 . ILE C 3 6   D 13.631 20.211  43.864 1.00 43.10  ? 2   ILE R CG2 1 
ATOM   3933 C  CD1 . ILE C 3 6   D 11.256 19.735  42.257 1.00 39.26  ? 2   ILE R CD1 1 
ATOM   3934 N  N   . ARG C 3 7   E 15.470 23.324  43.453 1.00 34.67  ? 2   ARG R N   1 
ATOM   3935 C  CA  . ARG C 3 7   E 16.865 23.590  43.794 1.00 41.21  ? 2   ARG R CA  1 
ATOM   3936 C  C   . ARG C 3 7   E 16.985 24.671  44.870 1.00 44.44  ? 2   ARG R C   1 
ATOM   3937 O  O   . ARG C 3 7   E 17.769 24.523  45.821 1.00 40.13  ? 2   ARG R O   1 
ATOM   3938 C  CB  . ARG C 3 7   E 17.625 24.003  42.542 1.00 43.30  ? 2   ARG R CB  1 
ATOM   3939 C  CG  . ARG C 3 7   E 17.806 22.886  41.543 1.00 48.68  ? 2   ARG R CG  1 
ATOM   3940 C  CD  . ARG C 3 7   E 18.456 23.424  40.292 1.00 55.44  ? 2   ARG R CD  1 
ATOM   3941 N  NE  . ARG C 3 7   E 18.539 22.430  39.230 1.00 66.12  ? 2   ARG R NE  1 
ATOM   3942 C  CZ  . ARG C 3 7   E 19.495 21.513  39.145 1.00 76.22  ? 2   ARG R CZ  1 
ATOM   3943 N  NH1 . ARG C 3 7   E 20.401 21.364  40.102 1.00 68.34  ? 2   ARG R NH1 1 
ATOM   3944 N  NH2 . ARG C 3 7   E 19.548 20.726  38.069 1.00 74.54  ? 2   ARG R NH2 1 
ATOM   3945 N  N   . ALA C 3 8   F 16.225 25.774  44.726 1.00 38.67  ? 2   ALA R N   1 
ATOM   3946 C  CA  . ALA C 3 8   F 16.191 26.808  45.760 1.00 40.35  ? 2   ALA R CA  1 
ATOM   3947 C  C   . ALA C 3 8   F 15.800 26.231  47.118 1.00 38.57  ? 2   ALA R C   1 
ATOM   3948 O  O   . ALA C 3 8   F 16.342 26.647  48.154 1.00 35.93  ? 2   ALA R O   1 
ATOM   3949 C  CB  . ALA C 3 8   F 15.213 27.922  45.375 1.00 42.65  ? 2   ALA R CB  1 
ATOM   3950 N  N   . ALA C 3 9   G 14.840 25.290  47.137 1.00 35.98  ? 2   ALA R N   1 
ATOM   3951 C  CA  . ALA C 3 9   G 14.386 24.728  48.412 1.00 36.75  ? 2   ALA R CA  1 
ATOM   3952 C  C   . ALA C 3 9   G 15.443 23.816  49.003 1.00 34.34  ? 2   ALA R C   1 
ATOM   3953 O  O   . ALA C 3 9   G 15.662 23.816  50.218 1.00 40.71  ? 2   ALA R O   1 
ATOM   3954 C  CB  . ALA C 3 9   G 13.067 23.977  48.234 1.00 36.67  ? 2   ALA R CB  1 
ATOM   3955 N  N   . ILE C 3 10  H 16.131 23.055  48.149 1.00 37.62  ? 2   ILE R N   1 
ATOM   3956 C  CA  . ILE C 3 10  H 17.269 22.250  48.591 1.00 35.52  ? 2   ILE R CA  1 
ATOM   3957 C  C   . ILE C 3 10  H 18.355 23.150  49.151 1.00 36.85  ? 2   ILE R C   1 
ATOM   3958 O  O   . ILE C 3 10  H 19.012 22.822  50.147 1.00 33.40  ? 2   ILE R O   1 
ATOM   3959 C  CB  . ILE C 3 10  H 17.794 21.385  47.428 1.00 34.52  ? 2   ILE R CB  1 
ATOM   3960 C  CG1 . ILE C 3 10  H 16.760 20.309  47.067 1.00 37.51  ? 2   ILE R CG1 1 
ATOM   3961 C  CG2 . ILE C 3 10  H 19.152 20.741  47.771 1.00 35.85  ? 2   ILE R CG2 1 
ATOM   3962 C  CD1 . ILE C 3 10  H 16.887 19.747  45.658 1.00 36.86  ? 2   ILE R CD1 1 
ATOM   3963 N  N   . PHE C 3 11  I 18.576 24.294  48.507 1.00 43.08  ? 2   PHE R N   1 
ATOM   3964 C  CA  . PHE C 3 11  I 19.577 25.226  49.011 1.00 42.84  ? 2   PHE R CA  1 
ATOM   3965 C  C   . PHE C 3 11  I 19.140 25.816  50.348 1.00 41.64  ? 2   PHE R C   1 
ATOM   3966 O  O   . PHE C 3 11  I 19.961 25.950  51.267 1.00 36.68  ? 2   PHE R O   1 
ATOM   3967 C  CB  . PHE C 3 11  I 19.844 26.323  47.979 1.00 41.46  ? 2   PHE R CB  1 
ATOM   3968 C  CG  . PHE C 3 11  I 20.951 25.988  47.000 1.00 42.02  ? 2   PHE R CG  1 
ATOM   3969 C  CD1 . PHE C 3 11  I 22.196 25.577  47.441 1.00 39.61  ? 2   PHE R CD1 1 
ATOM   3970 C  CD2 . PHE C 3 11  I 20.729 26.065  45.633 1.00 43.81  ? 2   PHE R CD2 1 
ATOM   3971 C  CE1 . PHE C 3 11  I 23.197 25.290  46.555 1.00 39.34  ? 2   PHE R CE1 1 
ATOM   3972 C  CE2 . PHE C 3 11  I 21.733 25.765  44.743 1.00 42.22  ? 2   PHE R CE2 1 
ATOM   3973 C  CZ  . PHE C 3 11  I 22.961 25.382  45.202 1.00 42.70  ? 2   PHE R CZ  1 
ATOM   3974 N  N   . ILE C 3 12  J 17.844 26.123  50.491 1.00 31.59  ? 2   ILE R N   1 
ATOM   3975 C  CA  . ILE C 3 12  J 17.335 26.618  51.767 1.00 37.68  ? 2   ILE R CA  1 
ATOM   3976 C  C   . ILE C 3 12  J 17.581 25.599  52.872 1.00 36.25  ? 2   ILE R C   1 
ATOM   3977 O  O   . ILE C 3 12  J 17.865 25.959  54.021 1.00 38.39  ? 2   ILE R O   1 
ATOM   3978 C  CB  . ILE C 3 12  J 15.834 26.959  51.659 1.00 39.44  ? 2   ILE R CB  1 
ATOM   3979 C  CG1 . ILE C 3 12  J 15.589 28.157  50.746 1.00 38.98  ? 2   ILE R CG1 1 
ATOM   3980 C  CG2 . ILE C 3 12  J 15.237 27.230  53.048 1.00 42.73  ? 2   ILE R CG2 1 
ATOM   3981 C  CD1 . ILE C 3 12  J 14.150 28.318  50.339 1.00 42.48  ? 2   ILE R CD1 1 
ATOM   3982 N  N   . GLN C 3 13  ? 17.459 24.314  52.547 1.00 39.98  ? 3   GLN R N   1 
ATOM   3983 C  CA  . GLN C 3 13  ? 17.581 23.276  53.556 1.00 37.94  ? 3   GLN R CA  1 
ATOM   3984 C  C   . GLN C 3 13  ? 19.025 22.973  53.910 1.00 34.76  ? 3   GLN R C   1 
ATOM   3985 O  O   . GLN C 3 13  ? 19.274 22.439  55.000 1.00 37.91  ? 3   GLN R O   1 
ATOM   3986 C  CB  . GLN C 3 13  ? 16.891 21.993  53.084 1.00 40.97  ? 3   GLN R CB  1 
ATOM   3987 C  CG  . GLN C 3 13  ? 16.784 20.946  54.154 1.00 41.60  ? 3   GLN R CG  1 
ATOM   3988 C  CD  . GLN C 3 13  ? 17.082 19.562  53.635 1.00 43.75  ? 3   GLN R CD  1 
ATOM   3989 O  OE1 . GLN C 3 13  ? 17.836 19.399  52.677 1.00 41.66  ? 3   GLN R OE1 1 
ATOM   3990 N  NE2 . GLN C 3 13  ? 16.484 18.555  54.260 1.00 41.93  ? 3   GLN R NE2 1 
ATOM   3991 N  N   . LYS C 3 14  ? 19.971 23.326  53.035 1.00 32.64  ? 4   LYS R N   1 
ATOM   3992 C  CA  . LYS C 3 14  ? 21.389 23.045  53.283 1.00 31.63  ? 4   LYS R CA  1 
ATOM   3993 C  C   . LYS C 3 14  ? 21.853 23.576  54.635 1.00 29.46  ? 4   LYS R C   1 
ATOM   3994 O  O   . LYS C 3 14  ? 22.644 22.932  55.316 1.00 30.17  ? 4   LYS R O   1 
ATOM   3995 C  CB  . LYS C 3 14  ? 22.260 23.651  52.182 1.00 34.47  ? 4   LYS R CB  1 
ATOM   3996 C  CG  . LYS C 3 14  ? 23.740 23.318  52.295 1.00 35.69  ? 4   LYS R CG  1 
ATOM   3997 C  CD  . LYS C 3 14  ? 24.528 23.773  51.079 1.00 41.01  ? 4   LYS R CD  1 
ATOM   3998 C  CE  . LYS C 3 14  ? 26.021 23.518  51.278 1.00 38.74  ? 4   LYS R CE  1 
ATOM   3999 N  NZ  . LYS C 3 14  ? 26.786 23.603  50.016 1.00 42.94  ? 4   LYS R NZ  1 
ATOM   4000 N  N   . TRP C 3 15  ? 21.412 24.771  55.019 1.00 34.70  ? 5   TRP R N   1 
ATOM   4001 C  CA  . TRP C 3 15  ? 21.834 25.301  56.310 1.00 35.31  ? 5   TRP R CA  1 
ATOM   4002 C  C   . TRP C 3 15  ? 21.591 24.267  57.409 1.00 33.68  ? 5   TRP R C   1 
ATOM   4003 O  O   . TRP C 3 15  ? 22.505 23.934  58.171 1.00 29.50  ? 5   TRP R O   1 
ATOM   4004 C  CB  . TRP C 3 15  ? 21.107 26.618  56.593 1.00 34.26  ? 5   TRP R CB  1 
ATOM   4005 C  CG  . TRP C 3 15  ? 21.841 27.547  57.527 1.00 34.19  ? 5   TRP R CG  1 
ATOM   4006 C  CD1 . TRP C 3 15  ? 22.899 27.228  58.354 1.00 31.05  ? 5   TRP R CD1 1 
ATOM   4007 C  CD2 . TRP C 3 15  ? 21.556 28.932  57.762 1.00 33.04  ? 5   TRP R CD2 1 
ATOM   4008 N  NE1 . TRP C 3 15  ? 23.279 28.326  59.078 1.00 32.57  ? 5   TRP R NE1 1 
ATOM   4009 C  CE2 . TRP C 3 15  ? 22.488 29.392  58.728 1.00 33.48  ? 5   TRP R CE2 1 
ATOM   4010 C  CE3 . TRP C 3 15  ? 20.626 29.840  57.233 1.00 35.02  ? 5   TRP R CE3 1 
ATOM   4011 C  CZ2 . TRP C 3 15  ? 22.507 30.718  59.186 1.00 31.61  ? 5   TRP R CZ2 1 
ATOM   4012 C  CZ3 . TRP C 3 15  ? 20.652 31.170  57.690 1.00 33.64  ? 5   TRP R CZ3 1 
ATOM   4013 C  CH2 . TRP C 3 15  ? 21.581 31.589  58.664 1.00 29.92  ? 5   TRP R CH2 1 
ATOM   4014 N  N   . TYR C 3 16  ? 20.393 23.665  57.420 1.00 33.37  ? 6   TYR R N   1 
ATOM   4015 C  CA  . TYR C 3 16  ? 20.041 22.663  58.425 1.00 30.94  ? 6   TYR R CA  1 
ATOM   4016 C  C   . TYR C 3 16  ? 20.830 21.367  58.261 1.00 27.95  ? 6   TYR R C   1 
ATOM   4017 O  O   . TYR C 3 16  ? 21.164 20.703  59.265 1.00 25.73  ? 6   TYR R O   1 
ATOM   4018 C  CB  . TYR C 3 16  ? 18.539 22.376  58.364 1.00 33.29  ? 6   TYR R CB  1 
ATOM   4019 C  CG  . TYR C 3 16  ? 18.108 21.258  59.277 1.00 34.72  ? 6   TYR R CG  1 
ATOM   4020 C  CD1 . TYR C 3 16  ? 17.944 21.486  60.644 1.00 35.82  ? 6   TYR R CD1 1 
ATOM   4021 C  CD2 . TYR C 3 16  ? 17.898 19.972  58.791 1.00 35.17  ? 6   TYR R CD2 1 
ATOM   4022 C  CE1 . TYR C 3 16  ? 17.571 20.477  61.501 1.00 35.05  ? 6   TYR R CE1 1 
ATOM   4023 C  CE2 . TYR C 3 16  ? 17.514 18.945  59.648 1.00 39.14  ? 6   TYR R CE2 1 
ATOM   4024 C  CZ  . TYR C 3 16  ? 17.353 19.215  61.006 1.00 40.75  ? 6   TYR R CZ  1 
ATOM   4025 O  OH  . TYR C 3 16  ? 16.970 18.222  61.887 1.00 41.29  ? 6   TYR R OH  1 
ATOM   4026 N  N   . ARG C 3 17  ? 21.091 20.950  57.010 1.00 29.94  ? 7   ARG R N   1 
ATOM   4027 C  CA  . ARG C 3 17  ? 21.839 19.711  56.780 1.00 33.45  ? 7   ARG R CA  1 
ATOM   4028 C  C   . ARG C 3 17  ? 23.241 19.802  57.370 1.00 33.63  ? 7   ARG R C   1 
ATOM   4029 O  O   . ARG C 3 17  ? 23.704 18.880  58.047 1.00 36.86  ? 7   ARG R O   1 
ATOM   4030 C  CB  . ARG C 3 17  ? 21.947 19.401  55.289 1.00 39.65  ? 7   ARG R CB  1 
ATOM   4031 C  CG  . ARG C 3 17  ? 20.655 19.048  54.574 1.00 46.66  ? 7   ARG R CG  1 
ATOM   4032 C  CD  . ARG C 3 17  ? 20.954 18.291  53.247 1.00 47.18  ? 7   ARG R CD  1 
ATOM   4033 N  NE  . ARG C 3 17  ? 21.673 19.100  52.263 1.00 42.87  ? 7   ARG R NE  1 
ATOM   4034 C  CZ  . ARG C 3 17  ? 21.100 20.017  51.492 1.00 48.15  ? 7   ARG R CZ  1 
ATOM   4035 N  NH1 . ARG C 3 17  ? 19.797 20.267  51.564 1.00 47.35  ? 7   ARG R NH1 1 
ATOM   4036 N  NH2 . ARG C 3 17  ? 21.852 20.709  50.632 1.00 42.96  ? 7   ARG R NH2 1 
ATOM   4037 N  N   . ARG C 3 18  ? 23.945 20.899  57.081 1.00 35.47  ? 8   ARG R N   1 
ATOM   4038 C  CA  . ARG C 3 18  ? 25.294 21.091  57.593 1.00 34.26  ? 8   ARG R CA  1 
ATOM   4039 C  C   . ARG C 3 18  ? 25.296 21.152  59.119 1.00 35.91  ? 8   ARG R C   1 
ATOM   4040 O  O   . ARG C 3 18  ? 26.051 20.428  59.775 1.00 33.07  ? 8   ARG R O   1 
ATOM   4041 C  CB  . ARG C 3 18  ? 25.903 22.358  56.986 1.00 34.56  ? 8   ARG R CB  1 
ATOM   4042 C  CG  . ARG C 3 18  ? 26.177 22.259  55.479 1.00 37.00  ? 8   ARG R CG  1 
ATOM   4043 C  CD  . ARG C 3 18  ? 26.979 20.984  55.123 1.00 40.00  ? 8   ARG R CD  1 
ATOM   4044 N  NE  . ARG C 3 18  ? 28.216 20.902  55.897 1.00 43.07  ? 8   ARG R NE  1 
ATOM   4045 C  CZ  . ARG C 3 18  ? 28.666 19.816  56.519 1.00 42.34  ? 8   ARG R CZ  1 
ATOM   4046 N  NH1 . ARG C 3 18  ? 28.039 18.654  56.431 1.00 41.71  ? 8   ARG R NH1 1 
ATOM   4047 N  NH2 . ARG C 3 18  ? 29.779 19.900  57.249 1.00 45.55  ? 8   ARG R NH2 1 
ATOM   4048 N  N   . HIS C 3 19  ? 24.429 21.980  59.710 1.00 40.00  ? 9   HIS R N   1 
ATOM   4049 C  CA  . HIS C 3 19  ? 24.389 22.051  61.170 1.00 36.73  ? 9   HIS R CA  1 
ATOM   4050 C  C   . HIS C 3 19  ? 24.102 20.677  61.778 1.00 35.58  ? 9   HIS R C   1 
ATOM   4051 O  O   . HIS C 3 19  ? 24.753 20.274  62.755 1.00 33.03  ? 9   HIS R O   1 
ATOM   4052 C  CB  . HIS C 3 19  ? 23.355 23.081  61.632 1.00 36.19  ? 9   HIS R CB  1 
ATOM   4053 C  CG  . HIS C 3 19  ? 22.971 22.938  63.073 1.00 34.89  ? 9   HIS R CG  1 
ATOM   4054 N  ND1 . HIS C 3 19  ? 23.748 23.433  64.103 1.00 40.10  ? 9   HIS R ND1 1 
ATOM   4055 C  CD2 . HIS C 3 19  ? 21.917 22.323  63.662 1.00 39.71  ? 9   HIS R CD2 1 
ATOM   4056 C  CE1 . HIS C 3 19  ? 23.186 23.139  65.262 1.00 37.38  ? 9   HIS R CE1 1 
ATOM   4057 N  NE2 . HIS C 3 19  ? 22.076 22.465  65.025 1.00 42.81  ? 9   HIS R NE2 1 
ATOM   4058 N  N   . GLN C 3 20  ? 23.183 19.915  61.163 1.00 36.20  ? 10  GLN R N   1 
ATOM   4059 C  CA  . GLN C 3 20  ? 22.821 18.594  61.675 1.00 37.16  ? 10  GLN R CA  1 
ATOM   4060 C  C   . GLN C 3 20  ? 23.978 17.615  61.555 1.00 38.94  ? 10  GLN R C   1 
ATOM   4061 O  O   . GLN C 3 20  ? 24.309 16.908  62.520 1.00 31.94  ? 10  GLN R O   1 
ATOM   4062 C  CB  . GLN C 3 20  ? 21.599 18.041  60.940 1.00 45.24  ? 10  GLN R CB  1 
ATOM   4063 C  CG  . GLN C 3 20  ? 21.186 16.665  61.442 1.00 49.05  ? 10  GLN R CG  1 
ATOM   4064 C  CD  . GLN C 3 20  ? 19.850 16.195  60.883 1.00 55.26  ? 10  GLN R CD  1 
ATOM   4065 O  OE1 . GLN C 3 20  ? 18.901 15.932  61.637 1.00 50.45  ? 10  GLN R OE1 1 
ATOM   4066 N  NE2 . GLN C 3 20  ? 19.772 16.068  59.556 1.00 59.12  ? 10  GLN R NE2 1 
ATOM   4067 N  N   . ALA C 3 21  ? 24.593 17.547  60.370 1.00 33.46  ? 11  ALA R N   1 
ATOM   4068 C  CA  . ALA C 3 21  ? 25.776 16.714  60.202 1.00 36.02  ? 11  ALA R CA  1 
ATOM   4069 C  C   . ALA C 3 21  ? 26.874 17.105  61.189 1.00 36.11  ? 11  ALA R C   1 
ATOM   4070 O  O   . ALA C 3 21  ? 27.518 16.233  61.785 1.00 38.86  ? 11  ALA R O   1 
ATOM   4071 C  CB  . ALA C 3 21  ? 26.284 16.803  58.760 1.00 34.97  ? 11  ALA R CB  1 
ATOM   4072 N  N   . ARG C 3 22  ? 27.098 18.408  61.383 1.00 35.78  ? 12  ARG R N   1 
ATOM   4073 C  CA  . ARG C 3 22  ? 28.123 18.858  62.327 1.00 37.58  ? 12  ARG R CA  1 
ATOM   4074 C  C   . ARG C 3 22  ? 27.795 18.434  63.755 1.00 40.54  ? 12  ARG R C   1 
ATOM   4075 O  O   . ARG C 3 22  ? 28.686 18.048  64.513 1.00 38.34  ? 12  ARG R O   1 
ATOM   4076 C  CB  . ARG C 3 22  ? 28.266 20.379  62.262 1.00 35.50  ? 12  ARG R CB  1 
ATOM   4077 C  CG  . ARG C 3 22  ? 29.267 20.826  61.271 1.00 43.30  ? 12  ARG R CG  1 
ATOM   4078 C  CD  . ARG C 3 22  ? 30.509 19.983  61.476 1.00 52.95  ? 12  ARG R CD  1 
ATOM   4079 N  NE  . ARG C 3 22  ? 31.671 20.458  60.744 1.00 54.98  ? 12  ARG R NE  1 
ATOM   4080 C  CZ  . ARG C 3 22  ? 32.520 19.651  60.130 1.00 55.60  ? 12  ARG R CZ  1 
ATOM   4081 N  NH1 . ARG C 3 22  ? 32.362 18.338  60.154 1.00 56.59  ? 12  ARG R NH1 1 
ATOM   4082 N  NH2 . ARG C 3 22  ? 33.536 20.174  59.451 1.00 53.17  ? 12  ARG R NH2 1 
ATOM   4083 N  N   . ARG C 3 23  ? 26.522 18.542  64.145 1.00 40.99  ? 13  ARG R N   1 
ATOM   4084 C  CA  . ARG C 3 23  ? 26.113 18.183  65.496 1.00 44.98  ? 13  ARG R CA  1 
ATOM   4085 C  C   . ARG C 3 23  ? 26.276 16.687  65.727 1.00 40.51  ? 13  ARG R C   1 
ATOM   4086 O  O   . ARG C 3 23  ? 26.746 16.262  66.788 1.00 39.39  ? 13  ARG R O   1 
ATOM   4087 C  CB  . ARG C 3 23  ? 24.658 18.629  65.745 1.00 46.39  ? 13  ARG R CB  1 
ATOM   4088 C  CG  . ARG C 3 23  ? 24.198 18.524  67.220 1.00 55.35  ? 13  ARG R CG  1 
ATOM   4089 C  CD  . ARG C 3 23  ? 22.658 18.434  67.375 1.00 62.41  ? 13  ARG R CD  1 
ATOM   4090 N  NE  . ARG C 3 23  ? 22.115 17.163  66.904 1.00 70.60  ? 13  ARG R NE  1 
ATOM   4091 C  CZ  . ARG C 3 23  ? 21.296 17.026  65.868 1.00 67.04  ? 13  ARG R CZ  1 
ATOM   4092 N  NH1 . ARG C 3 23  ? 20.841 18.074  65.203 1.00 63.00  ? 13  ARG R NH1 1 
ATOM   4093 N  NH2 . ARG C 3 23  ? 20.928 15.805  65.489 1.00 65.51  ? 13  ARG R NH2 1 
ATOM   4094 N  N   . GLU C 3 24  ? 25.921 15.875  64.731 1.00 39.74  ? 14  GLU R N   1 
ATOM   4095 C  CA  . GLU C 3 24  ? 26.050 14.429  64.881 1.00 41.25  ? 14  GLU R CA  1 
ATOM   4096 C  C   . GLU C 3 24  ? 27.504 14.025  65.121 1.00 39.47  ? 14  GLU R C   1 
ATOM   4097 O  O   . GLU C 3 24  ? 27.794 13.182  65.975 1.00 38.64  ? 14  GLU R O   1 
ATOM   4098 C  CB  . GLU C 3 24  ? 25.463 13.737  63.652 1.00 41.71  ? 14  GLU R CB  1 
ATOM   4099 C  CG  . GLU C 3 24  ? 23.921 13.747  63.652 1.00 42.91  ? 14  GLU R CG  1 
ATOM   4100 C  CD  . GLU C 3 24  ? 23.321 13.291  62.331 1.00 45.87  ? 14  GLU R CD  1 
ATOM   4101 O  OE1 . GLU C 3 24  ? 24.089 13.040  61.371 1.00 45.97  ? 14  GLU R OE1 1 
ATOM   4102 O  OE2 . GLU C 3 24  ? 22.079 13.196  62.257 1.00 54.85  ? 14  GLU R OE2 1 
ATOM   4103 N  N   . MET C 3 25  ? 28.431 14.654  64.410 1.00 44.71  ? 15  MET R N   1 
ATOM   4104 C  CA  . MET C 3 25  ? 29.840 14.332  64.566 1.00 43.34  ? 15  MET R CA  1 
ATOM   4105 C  C   . MET C 3 25  ? 30.377 14.786  65.925 1.00 38.60  ? 15  MET R C   1 
ATOM   4106 O  O   . MET C 3 25  ? 31.225 14.111  66.500 1.00 39.99  ? 15  MET R O   1 
ATOM   4107 C  CB  . MET C 3 25  ? 30.605 14.950  63.402 1.00 42.47  ? 15  MET R CB  1 
ATOM   4108 C  CG  . MET C 3 25  ? 32.096 14.915  63.512 1.00 55.83  ? 15  MET R CG  1 
ATOM   4109 S  SD  . MET C 3 25  ? 32.816 15.850  62.144 1.00 67.96  ? 15  MET R SD  1 
ATOM   4110 C  CE  . MET C 3 25  ? 32.708 17.495  62.851 1.00 74.60  ? 15  MET R CE  1 
ATOM   4111 N  N   . LEU C 3 26  ? 29.882 15.898  66.471 1.00 40.67  ? 16  LEU R N   1 
ATOM   4112 C  CA  . LEU C 3 26  ? 30.326 16.323  67.800 1.00 41.08  ? 16  LEU R CA  1 
ATOM   4113 C  C   . LEU C 3 26  ? 29.726 15.441  68.889 1.00 40.71  ? 16  LEU R C   1 
ATOM   4114 O  O   . LEU C 3 26  ? 30.309 15.305  69.973 1.00 33.18  ? 16  LEU R O   1 
ATOM   4115 C  CB  . LEU C 3 26  ? 29.945 17.782  68.045 1.00 44.20  ? 16  LEU R CB  1 
ATOM   4116 C  CG  . LEU C 3 26  ? 30.792 18.929  67.477 1.00 52.72  ? 16  LEU R CG  1 
ATOM   4117 C  CD1 . LEU C 3 26  ? 31.406 18.638  66.111 1.00 52.39  ? 16  LEU R CD1 1 
ATOM   4118 C  CD2 . LEU C 3 26  ? 29.899 20.162  67.367 1.00 53.85  ? 16  LEU R CD2 1 
ATOM   4119 N  N   . GLU C 3 27  ? 28.557 14.849  68.618 1.00 39.62  ? 17  GLU R N   1 
ATOM   4120 C  CA  . GLU C 3 27  ? 27.898 13.909  69.511 1.00 41.46  ? 17  GLU R CA  1 
ATOM   4121 C  C   . GLU C 3 27  ? 28.226 12.458  69.148 1.00 39.05  ? 17  GLU R C   1 
ATOM   4122 O  O   . GLU C 3 27  ? 27.617 11.536  69.698 1.00 41.90  ? 17  GLU R O   1 
ATOM   4123 C  CB  . GLU C 3 27  ? 26.375 14.141  69.502 1.00 41.77  ? 17  GLU R CB  1 
ATOM   4124 C  CG  . GLU C 3 27  ? 25.944 15.579  69.799 1.00 41.26  ? 17  GLU R CG  1 
ATOM   4125 C  CD  . GLU C 3 27  ? 24.415 15.811  69.687 1.00 45.94  ? 17  GLU R CD  1 
ATOM   4126 O  OE1 . GLU C 3 27  ? 23.703 15.001  69.042 1.00 41.64  ? 17  GLU R OE1 1 
ATOM   4127 O  OE2 . GLU C 3 27  ? 23.925 16.810  70.254 1.00 50.94  ? 17  GLU R OE2 1 
ATOM   4128 N  N   . HIS C 3 28  ? 29.144 12.246  68.208 1.00 35.90  ? 18  HIS R N   1 
ATOM   4129 C  CA  . HIS C 3 28  ? 29.729 10.929  67.942 1.00 36.13  ? 18  HIS R CA  1 
ATOM   4130 C  C   . HIS C 3 28  ? 28.685 9.886   67.516 1.00 37.49  ? 18  HIS R C   1 
ATOM   4131 O  O   . HIS C 3 28  ? 28.710 8.744   67.975 1.00 37.56  ? 18  HIS R O   1 
ATOM   4132 C  CB  . HIS C 3 28  ? 30.504 10.434  69.172 1.00 38.21  ? 18  HIS R CB  1 
ATOM   4133 C  CG  . HIS C 3 28  ? 31.723 11.246  69.510 1.00 36.93  ? 18  HIS R CG  1 
ATOM   4134 N  ND1 . HIS C 3 28  ? 32.990 10.894  69.092 1.00 36.41  ? 18  HIS R ND1 1 
ATOM   4135 C  CD2 . HIS C 3 28  ? 31.875 12.363  70.264 1.00 38.77  ? 18  HIS R CD2 1 
ATOM   4136 C  CE1 . HIS C 3 28  ? 33.866 11.774  69.544 1.00 33.55  ? 18  HIS R CE1 1 
ATOM   4137 N  NE2 . HIS C 3 28  ? 33.215 12.678  70.257 1.00 40.59  ? 18  HIS R NE2 1 
ATOM   4138 N  N   . HIS C 3 29  ? 27.761 10.246  66.630 1.00 41.08  ? 19  HIS R N   1 
ATOM   4139 C  CA  . HIS C 3 29  ? 26.743 9.269   66.233 1.00 47.46  ? 19  HIS R CA  1 
ATOM   4140 C  C   . HIS C 3 29  ? 26.198 9.599   64.843 1.00 50.82  ? 19  HIS R C   1 
ATOM   4141 O  O   . HIS C 3 29  ? 26.677 10.513  64.167 1.00 50.62  ? 19  HIS R O   1 
ATOM   4142 C  CB  . HIS C 3 29  ? 25.613 9.190   67.269 1.00 42.45  ? 19  HIS R CB  1 
ATOM   4143 C  CG  . HIS C 3 29  ? 24.724 10.391  67.294 1.00 43.20  ? 19  HIS R CG  1 
ATOM   4144 N  ND1 . HIS C 3 29  ? 23.696 10.578  66.395 1.00 49.23  ? 19  HIS R ND1 1 
ATOM   4145 C  CD2 . HIS C 3 29  ? 24.707 11.464  68.116 1.00 42.92  ? 19  HIS R CD2 1 
ATOM   4146 C  CE1 . HIS C 3 29  ? 23.086 11.719  66.661 1.00 52.52  ? 19  HIS R CE1 1 
ATOM   4147 N  NE2 . HIS C 3 29  ? 23.680 12.277  67.702 1.00 47.17  ? 19  HIS R NE2 1 
ATOM   4148 N  N   . HIS C 3 30  ? 25.179 8.839   64.436 1.00 67.85  ? 20  HIS R N   1 
ATOM   4149 C  CA  . HIS C 3 30  ? 24.567 8.862   63.104 1.00 76.88  ? 20  HIS R CA  1 
ATOM   4150 C  C   . HIS C 3 30  ? 25.595 9.081   61.993 1.00 83.85  ? 20  HIS R C   1 
ATOM   4151 O  O   . HIS C 3 30  ? 25.240 9.325   60.839 1.00 90.85  ? 20  HIS R O   1 
ATOM   4152 C  CB  . HIS C 3 30  ? 23.472 9.930   63.044 1.00 81.78  ? 20  HIS R CB  1 
ATOM   4153 C  CG  . HIS C 3 30  ? 22.090 9.391   63.238 1.00 91.93  ? 20  HIS R CG  1 
ATOM   4154 N  ND1 . HIS C 3 30  ? 21.339 8.873   62.204 1.00 89.53  ? 20  HIS R ND1 1 
ATOM   4155 C  CD2 . HIS C 3 30  ? 21.325 9.285   64.350 1.00 95.82  ? 20  HIS R CD2 1 
ATOM   4156 C  CE1 . HIS C 3 30  ? 20.169 8.476   62.671 1.00 90.91  ? 20  HIS R CE1 1 
ATOM   4157 N  NE2 . HIS C 3 30  ? 20.136 8.712   63.970 1.00 91.17  ? 20  HIS R NE2 1 
HETATM 4158 CA CA  . CA  D 4 .   ? 26.915 39.433  59.899 1.00 39.73  ? 201 CA  N CA  1 
HETATM 4159 CA CA  . CA  E 4 .   ? 9.147  8.451   38.506 1.00 52.91  ? 202 CA  N CA  1 
HETATM 4160 CA CA  . CA  F 4 .   ? 6.193  10.324  49.235 1.00 46.06  ? 203 CA  N CA  1 
HETATM 4161 CA CA  . CA  G 4 .   ? 15.545 41.060  59.683 1.00 30.00  ? 204 CA  N CA  1 
HETATM 4162 O  O   . HOH H 5 .   ? 23.188 16.123  72.875 1.00 30.05  ? 401 HOH A O   1 
HETATM 4163 O  O   . HOH H 5 .   ? 52.850 19.538  70.409 1.00 54.28  ? 402 HOH A O   1 
HETATM 4164 O  O   . HOH H 5 .   ? 53.177 15.971  81.318 1.00 30.00  ? 403 HOH A O   1 
HETATM 4165 O  O   . HOH H 5 .   ? 32.012 13.922  80.442 1.00 31.05  ? 404 HOH A O   1 
HETATM 4166 O  O   . HOH H 5 .   ? 31.246 33.935  69.582 1.00 35.13  ? 405 HOH A O   1 
HETATM 4167 O  O   . HOH H 5 .   ? 18.887 20.441  83.994 1.00 34.88  ? 406 HOH A O   1 
HETATM 4168 O  O   . HOH H 5 .   ? 56.892 33.725  59.803 1.00 33.43  ? 407 HOH A O   1 
HETATM 4169 O  O   . HOH H 5 .   ? 29.228 13.893  80.007 1.00 29.68  ? 408 HOH A O   1 
HETATM 4170 O  O   . HOH H 5 .   ? 35.734 5.700   84.179 1.00 44.06  ? 409 HOH A O   1 
HETATM 4171 O  O   . HOH H 5 .   ? 52.086 19.766  63.439 1.00 28.10  ? 410 HOH A O   1 
HETATM 4172 O  O   . HOH H 5 .   ? 34.197 8.892   75.404 1.00 29.79  ? 411 HOH A O   1 
HETATM 4173 O  O   . HOH H 5 .   ? 45.876 7.984   69.044 1.00 30.00  ? 412 HOH A O   1 
HETATM 4174 O  O   . HOH H 5 .   ? 40.858 -0.190  76.373 1.00 46.03  ? 413 HOH A O   1 
HETATM 4175 O  O   . HOH H 5 .   ? 34.743 -5.403  79.888 1.00 35.47  ? 414 HOH A O   1 
HETATM 4176 O  O   . HOH H 5 .   ? 32.398 -3.539  89.297 1.00 35.05  ? 415 HOH A O   1 
HETATM 4177 O  O   . HOH H 5 .   ? 47.216 12.156  66.908 1.00 32.40  ? 416 HOH A O   1 
HETATM 4178 O  O   . HOH H 5 .   ? 33.795 6.043   74.498 1.00 36.89  ? 417 HOH A O   1 
HETATM 4179 O  O   . HOH H 5 .   ? 38.277 22.423  65.604 1.00 26.24  ? 418 HOH A O   1 
HETATM 4180 O  O   . HOH H 5 .   ? 62.471 32.482  54.827 1.00 38.98  ? 419 HOH A O   1 
HETATM 4181 O  O   . HOH H 5 .   ? 15.871 11.762  84.061 1.00 42.68  ? 420 HOH A O   1 
HETATM 4182 O  O   . HOH H 5 .   ? 17.653 1.294   76.302 1.00 29.98  ? 421 HOH A O   1 
HETATM 4183 O  O   . HOH H 5 .   ? 30.860 4.533   67.392 1.00 36.61  ? 422 HOH A O   1 
HETATM 4184 O  O   . HOH H 5 .   ? 36.742 32.758  62.816 1.00 30.59  ? 423 HOH A O   1 
HETATM 4185 O  O   . HOH H 5 .   ? 49.926 32.816  56.922 1.00 37.02  ? 424 HOH A O   1 
HETATM 4186 O  O   . HOH H 5 .   ? 56.722 23.444  67.816 1.00 30.92  ? 425 HOH A O   1 
HETATM 4187 O  O   . HOH H 5 .   ? 49.805 23.867  83.623 1.00 38.41  ? 426 HOH A O   1 
HETATM 4188 O  O   . HOH H 5 .   ? 32.621 3.850   89.951 1.00 35.30  ? 427 HOH A O   1 
HETATM 4189 O  O   . HOH H 5 .   ? 27.246 -0.458  70.016 1.00 48.99  ? 428 HOH A O   1 
HETATM 4190 O  O   . HOH H 5 .   ? 35.867 26.339  72.659 1.00 24.06  ? 429 HOH A O   1 
HETATM 4191 O  O   . HOH H 5 .   ? 58.046 31.367  61.873 1.00 30.90  ? 430 HOH A O   1 
HETATM 4192 O  O   . HOH H 5 .   ? 21.787 10.033  73.840 1.00 34.74  ? 431 HOH A O   1 
HETATM 4193 O  O   . HOH H 5 .   ? 21.148 15.752  76.378 1.00 31.92  ? 432 HOH A O   1 
HETATM 4194 O  O   . HOH H 5 .   ? 21.550 10.981  76.808 1.00 26.78  ? 433 HOH A O   1 
HETATM 4195 O  O   . HOH H 5 .   ? 35.156 3.931   86.198 1.00 35.47  ? 434 HOH A O   1 
HETATM 4196 O  O   . HOH H 5 .   ? 54.875 34.426  51.520 1.00 35.66  ? 435 HOH A O   1 
HETATM 4197 O  O   . HOH H 5 .   ? 20.267 1.622   76.583 1.00 35.07  ? 436 HOH A O   1 
HETATM 4198 O  O   . HOH H 5 .   ? 21.924 7.231   67.287 1.00 38.73  ? 437 HOH A O   1 
HETATM 4199 O  O   . HOH H 5 .   ? 20.786 13.510  77.725 1.00 38.69  ? 438 HOH A O   1 
HETATM 4200 O  O   . HOH H 5 .   ? 23.773 -7.527  83.034 1.00 30.00  ? 439 HOH A O   1 
HETATM 4201 O  O   . HOH H 5 .   ? 27.254 2.297   94.833 1.00 40.49  ? 440 HOH A O   1 
HETATM 4202 O  O   . HOH H 5 .   ? 19.979 8.929   67.156 1.00 36.53  ? 441 HOH A O   1 
HETATM 4203 O  O   . HOH H 5 .   ? 37.290 19.378  66.153 1.00 30.00  ? 442 HOH A O   1 
HETATM 4204 O  O   . HOH I 5 .   ? 21.247 23.163  37.160 1.00 44.68  ? 301 HOH N O   1 
HETATM 4205 O  O   . HOH I 5 .   ? 28.933 32.899  56.415 1.00 35.29  ? 302 HOH N O   1 
HETATM 4206 O  O   . HOH I 5 .   ? 7.022  29.508  61.099 1.00 38.52  ? 303 HOH N O   1 
HETATM 4207 O  O   . HOH I 5 .   ? 22.744 41.447  52.167 1.00 35.49  ? 304 HOH N O   1 
HETATM 4208 O  O   . HOH I 5 .   ? 8.980  29.787  55.291 1.00 42.78  ? 305 HOH N O   1 
HETATM 4209 O  O   . HOH I 5 .   ? 2.216  29.693  50.859 1.00 30.00  ? 306 HOH N O   1 
HETATM 4210 O  O   . HOH I 5 .   ? 11.374 29.040  46.245 1.00 45.52  ? 307 HOH N O   1 
HETATM 4211 O  O   . HOH I 5 .   ? 18.001 25.690  73.680 1.00 30.00  ? 308 HOH N O   1 
HETATM 4212 O  O   . HOH I 5 .   ? 34.833 20.283  51.042 1.00 55.33  ? 309 HOH N O   1 
HETATM 4213 O  O   . HOH I 5 .   ? 30.295 30.180  57.353 1.00 30.00  ? 310 HOH N O   1 
HETATM 4214 O  O   . HOH I 5 .   ? 28.545 28.320  58.889 1.00 32.97  ? 311 HOH N O   1 
HETATM 4215 O  O   . HOH I 5 .   ? 19.909 39.919  47.981 1.00 30.00  ? 312 HOH N O   1 
HETATM 4216 O  O   . HOH J 5 .   ? 34.516 22.540  59.884 1.00 40.34  ? 101 HOH R O   1 
HETATM 4217 O  O   . HOH J 5 .   ? 20.841 27.196  53.612 1.00 48.18  ? 102 HOH R O   1 
HETATM 4218 O  O   . HOH J 5 .   ? 33.414 8.425   67.305 1.00 38.95  ? 103 HOH R O   1 
HETATM 4219 O  O   . HOH J 5 .   ? 30.576 23.362  62.007 1.00 30.00  ? 104 HOH R O   1 
# 
