data_5J72
# 
_entry.id   5J72 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.383 
_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   5J72         pdb_00005j72 10.2210/pdb5j72/pdb 
WWPDB D_1000218902 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2017-02-08 
2 'Structure model' 1 1 2017-03-08 
3 'Structure model' 1 2 2017-03-22 
4 'Structure model' 1 3 2018-10-24 
5 'Structure model' 1 4 2024-01-10 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1  2 'Structure model' 'Refinement description' 
2  3 'Structure model' 'Data collection'        
3  3 'Structure model' 'Database references'    
4  4 'Structure model' Advisory                 
5  4 'Structure model' 'Data collection'        
6  4 'Structure model' 'Derived calculations'   
7  5 'Structure model' Advisory                 
8  5 'Structure model' 'Data collection'        
9  5 'Structure model' 'Database references'    
10 5 'Structure model' 'Derived calculations'   
11 5 'Structure model' 'Refinement description' 
# 
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  4 'Structure model' pdbx_unobs_or_zero_occ_atoms    
2  4 'Structure model' pdbx_unobs_or_zero_occ_residues 
3  4 'Structure model' pdbx_validate_symm_contact      
4  4 'Structure model' struct_conn                     
5  4 'Structure model' struct_conn_type                
6  5 'Structure model' chem_comp_atom                  
7  5 'Structure model' chem_comp_bond                  
8  5 'Structure model' database_2                      
9  5 'Structure model' pdbx_initial_refinement_model   
10 5 'Structure model' pdbx_struct_conn_angle          
11 5 'Structure model' pdbx_unobs_or_zero_occ_atoms    
12 5 'Structure model' pdbx_unobs_or_zero_occ_residues 
13 5 'Structure model' struct_conn                     
# 
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  5 'Structure model' '_database_2.pdbx_DOI'                        
2  5 'Structure model' '_database_2.pdbx_database_accession'         
3  5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
4  5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
5  5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
6  5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
7  5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
8  5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
9  5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
10 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
11 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
12 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
13 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
14 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
15 5 'Structure model' '_pdbx_struct_conn_angle.value'               
16 5 'Structure model' '_struct_conn.pdbx_dist_value'                
17 5 'Structure model' '_struct_conn.pdbx_ptnr1_label_alt_id'        
18 5 'Structure model' '_struct_conn.ptnr1_auth_asym_id'             
19 5 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
20 5 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
21 5 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
22 5 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
23 5 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
24 5 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
25 5 'Structure model' '_struct_conn.ptnr1_symmetry'                 
26 5 'Structure model' '_struct_conn.ptnr2_auth_asym_id'             
27 5 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
28 5 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
29 5 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
30 5 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
31 5 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
32 5 'Structure model' '_struct_conn.ptnr2_label_seq_id'             
33 5 'Structure model' '_struct_conn.ptnr2_symmetry'                 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        5J72 
_pdbx_database_status.recvd_initial_deposition_date   2016-04-05 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Renko, M.'  1 
'Usenik, A.' 2 
'Turk, D.'   3 
# 
_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            Structure 
_citation.journal_id_ASTM           STRUE6 
_citation.journal_id_CSD            2005 
_citation.journal_id_ISSN           1878-4186 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            25 
_citation.language                  ? 
_citation.page_first                514 
_citation.page_last                 521 
_citation.title                     
;The CWB2 Cell Wall-Anchoring Module Is Revealed by the Crystal Structures of the Clostridium difficile Cell Wall Proteins Cwp8 and Cwp6.
;
_citation.year                      2017 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.str.2016.12.018 
_citation.pdbx_database_id_PubMed   28132783 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Usenik, A.'  1 ? 
primary 'Renko, M.'   2 ? 
primary 'Mihelic, M.' 3 ? 
primary 'Lindic, N.'  4 ? 
primary 'Borisek, J.' 5 ? 
primary 'Perdih, A.'  6 ? 
primary 'Pretnar, G.' 7 ? 
primary 'Muller, U.'  8 ? 
primary 'Turk, D.'    9 ? 
# 
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 'Putative N-acetylmuramoyl-L-alanine amidase,autolysin cwp6' 69319.742 2    3.5.1.28 ? ? ? 
2 non-polymer syn 'CALCIUM ION'                                                40.078    5    ?        ? ? ? 
3 non-polymer syn 'SODIUM ION'                                                 22.990    3    ?        ? ? ? 
4 non-polymer syn 'CHLORIDE ION'                                               35.453    5    ?        ? ? ? 
5 non-polymer man 'ZINC ION'                                                   65.409    2    3.5.1.28 ? ? ? 
6 non-polymer syn 'CITRIC ACID'                                                192.124   2    ?        ? ? ? 
7 water       nat water                                                        18.015    1329 ?        ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SDININLQRKSVVLGSKSNASVKFKEKLNADSITLNFMCYDMPLEATLNYNEKTDSYEGVINYNKDPEYLNVWELQSIKI
NGKDEQKVLNKEDLESMGLNLKDYDVTQEFIISDANSTKAVNEYMRKTSAPVKKLAGATRFETAVEISKQGWKDGSSKVV
IVNGELAADGITATPLASTYDAPILLANKDDIPESTKAELKRLNPSDVIIIGDDGSVSQKAVSQIKSAVNVNVTRIGGVD
RHETSLLIAKEIDKYHDVNKIYIANGYAGEYDALNISSKAGEDQQPIILANKDSVPQGTYNWLSSQGLEEAYYIGGSQSL
SSKIIDQISKIAKNGTSKNRVSGADRHETNANVIKTFYPDKELSAMLVAKSDIIVDSITAGPLAAKLKAPILITPKTYVS
AYHSTNLSEKTAETVYQIGDGMKDSVINSIASSLSKHNAPTEPDNSGSAAGKTVVIDPGHGGSDSGATSGLNGGAQEKKY
TLNTALATTEYLRSKGINVVMTRDTDKTMALGERTALSNTIKPDLFTSIHYNASNGSGNGVEIYYKVKDKNGGTTKTAAS
NILKRILEKFNMKNRGIKTRTLDNGKDYLYVLRNNNYPAILVECAFIDNKSDMDKLNTAEKVKTMGTQIGIGIEDTVK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SDININLQRKSVVLGSKSNASVKFKEKLNADSITLNFMCYDMPLEATLNYNEKTDSYEGVINYNKDPEYLNVWELQSIKI
NGKDEQKVLNKEDLESMGLNLKDYDVTQEFIISDANSTKAVNEYMRKTSAPVKKLAGATRFETAVEISKQGWKDGSSKVV
IVNGELAADGITATPLASTYDAPILLANKDDIPESTKAELKRLNPSDVIIIGDDGSVSQKAVSQIKSAVNVNVTRIGGVD
RHETSLLIAKEIDKYHDVNKIYIANGYAGEYDALNISSKAGEDQQPIILANKDSVPQGTYNWLSSQGLEEAYYIGGSQSL
SSKIIDQISKIAKNGTSKNRVSGADRHETNANVIKTFYPDKELSAMLVAKSDIIVDSITAGPLAAKLKAPILITPKTYVS
AYHSTNLSEKTAETVYQIGDGMKDSVINSIASSLSKHNAPTEPDNSGSAAGKTVVIDPGHGGSDSGATSGLNGGAQEKKY
TLNTALATTEYLRSKGINVVMTRDTDKTMALGERTALSNTIKPDLFTSIHYNASNGSGNGVEIYYKVKDKNGGTTKTAAS
NILKRILEKFNMKNRGIKTRTLDNGKDYLYVLRNNNYPAILVECAFIDNKSDMDKLNTAEKVKTMGTQIGIGIEDTVK
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CALCIUM ION'  CA  
3 'SODIUM ION'   NA  
4 'CHLORIDE ION' CL  
5 'ZINC ION'     ZN  
6 'CITRIC ACID'  CIT 
7 water          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   ASP n 
1 3   ILE n 
1 4   ASN n 
1 5   ILE n 
1 6   ASN n 
1 7   LEU n 
1 8   GLN n 
1 9   ARG n 
1 10  LYS n 
1 11  SER n 
1 12  VAL n 
1 13  VAL n 
1 14  LEU n 
1 15  GLY n 
1 16  SER n 
1 17  LYS n 
1 18  SER n 
1 19  ASN n 
1 20  ALA n 
1 21  SER n 
1 22  VAL n 
1 23  LYS n 
1 24  PHE n 
1 25  LYS n 
1 26  GLU n 
1 27  LYS n 
1 28  LEU n 
1 29  ASN n 
1 30  ALA n 
1 31  ASP n 
1 32  SER n 
1 33  ILE n 
1 34  THR n 
1 35  LEU n 
1 36  ASN n 
1 37  PHE n 
1 38  MET n 
1 39  CYS n 
1 40  TYR n 
1 41  ASP n 
1 42  MET n 
1 43  PRO n 
1 44  LEU n 
1 45  GLU n 
1 46  ALA n 
1 47  THR n 
1 48  LEU n 
1 49  ASN n 
1 50  TYR n 
1 51  ASN n 
1 52  GLU n 
1 53  LYS n 
1 54  THR n 
1 55  ASP n 
1 56  SER n 
1 57  TYR n 
1 58  GLU n 
1 59  GLY n 
1 60  VAL n 
1 61  ILE n 
1 62  ASN n 
1 63  TYR n 
1 64  ASN n 
1 65  LYS n 
1 66  ASP n 
1 67  PRO n 
1 68  GLU n 
1 69  TYR n 
1 70  LEU n 
1 71  ASN n 
1 72  VAL n 
1 73  TRP n 
1 74  GLU n 
1 75  LEU n 
1 76  GLN n 
1 77  SER n 
1 78  ILE n 
1 79  LYS n 
1 80  ILE n 
1 81  ASN n 
1 82  GLY n 
1 83  LYS n 
1 84  ASP n 
1 85  GLU n 
1 86  GLN n 
1 87  LYS n 
1 88  VAL n 
1 89  LEU n 
1 90  ASN n 
1 91  LYS n 
1 92  GLU n 
1 93  ASP n 
1 94  LEU n 
1 95  GLU n 
1 96  SER n 
1 97  MET n 
1 98  GLY n 
1 99  LEU n 
1 100 ASN n 
1 101 LEU n 
1 102 LYS n 
1 103 ASP n 
1 104 TYR n 
1 105 ASP n 
1 106 VAL n 
1 107 THR n 
1 108 GLN n 
1 109 GLU n 
1 110 PHE n 
1 111 ILE n 
1 112 ILE n 
1 113 SER n 
1 114 ASP n 
1 115 ALA n 
1 116 ASN n 
1 117 SER n 
1 118 THR n 
1 119 LYS n 
1 120 ALA n 
1 121 VAL n 
1 122 ASN n 
1 123 GLU n 
1 124 TYR n 
1 125 MET n 
1 126 ARG n 
1 127 LYS n 
1 128 THR n 
1 129 SER n 
1 130 ALA n 
1 131 PRO n 
1 132 VAL n 
1 133 LYS n 
1 134 LYS n 
1 135 LEU n 
1 136 ALA n 
1 137 GLY n 
1 138 ALA n 
1 139 THR n 
1 140 ARG n 
1 141 PHE n 
1 142 GLU n 
1 143 THR n 
1 144 ALA n 
1 145 VAL n 
1 146 GLU n 
1 147 ILE n 
1 148 SER n 
1 149 LYS n 
1 150 GLN n 
1 151 GLY n 
1 152 TRP n 
1 153 LYS n 
1 154 ASP n 
1 155 GLY n 
1 156 SER n 
1 157 SER n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ILE n 
1 162 VAL n 
1 163 ASN n 
1 164 GLY n 
1 165 GLU n 
1 166 LEU n 
1 167 ALA n 
1 168 ALA n 
1 169 ASP n 
1 170 GLY n 
1 171 ILE n 
1 172 THR n 
1 173 ALA n 
1 174 THR n 
1 175 PRO n 
1 176 LEU n 
1 177 ALA n 
1 178 SER n 
1 179 THR n 
1 180 TYR n 
1 181 ASP n 
1 182 ALA n 
1 183 PRO n 
1 184 ILE n 
1 185 LEU n 
1 186 LEU n 
1 187 ALA n 
1 188 ASN n 
1 189 LYS n 
1 190 ASP n 
1 191 ASP n 
1 192 ILE n 
1 193 PRO n 
1 194 GLU n 
1 195 SER n 
1 196 THR n 
1 197 LYS n 
1 198 ALA n 
1 199 GLU n 
1 200 LEU n 
1 201 LYS n 
1 202 ARG n 
1 203 LEU n 
1 204 ASN n 
1 205 PRO n 
1 206 SER n 
1 207 ASP n 
1 208 VAL n 
1 209 ILE n 
1 210 ILE n 
1 211 ILE n 
1 212 GLY n 
1 213 ASP n 
1 214 ASP n 
1 215 GLY n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 GLN n 
1 220 LYS n 
1 221 ALA n 
1 222 VAL n 
1 223 SER n 
1 224 GLN n 
1 225 ILE n 
1 226 LYS n 
1 227 SER n 
1 228 ALA n 
1 229 VAL n 
1 230 ASN n 
1 231 VAL n 
1 232 ASN n 
1 233 VAL n 
1 234 THR n 
1 235 ARG n 
1 236 ILE n 
1 237 GLY n 
1 238 GLY n 
1 239 VAL n 
1 240 ASP n 
1 241 ARG n 
1 242 HIS n 
1 243 GLU n 
1 244 THR n 
1 245 SER n 
1 246 LEU n 
1 247 LEU n 
1 248 ILE n 
1 249 ALA n 
1 250 LYS n 
1 251 GLU n 
1 252 ILE n 
1 253 ASP n 
1 254 LYS n 
1 255 TYR n 
1 256 HIS n 
1 257 ASP n 
1 258 VAL n 
1 259 ASN n 
1 260 LYS n 
1 261 ILE n 
1 262 TYR n 
1 263 ILE n 
1 264 ALA n 
1 265 ASN n 
1 266 GLY n 
1 267 TYR n 
1 268 ALA n 
1 269 GLY n 
1 270 GLU n 
1 271 TYR n 
1 272 ASP n 
1 273 ALA n 
1 274 LEU n 
1 275 ASN n 
1 276 ILE n 
1 277 SER n 
1 278 SER n 
1 279 LYS n 
1 280 ALA n 
1 281 GLY n 
1 282 GLU n 
1 283 ASP n 
1 284 GLN n 
1 285 GLN n 
1 286 PRO n 
1 287 ILE n 
1 288 ILE n 
1 289 LEU n 
1 290 ALA n 
1 291 ASN n 
1 292 LYS n 
1 293 ASP n 
1 294 SER n 
1 295 VAL n 
1 296 PRO n 
1 297 GLN n 
1 298 GLY n 
1 299 THR n 
1 300 TYR n 
1 301 ASN n 
1 302 TRP n 
1 303 LEU n 
1 304 SER n 
1 305 SER n 
1 306 GLN n 
1 307 GLY n 
1 308 LEU n 
1 309 GLU n 
1 310 GLU n 
1 311 ALA n 
1 312 TYR n 
1 313 TYR n 
1 314 ILE n 
1 315 GLY n 
1 316 GLY n 
1 317 SER n 
1 318 GLN n 
1 319 SER n 
1 320 LEU n 
1 321 SER n 
1 322 SER n 
1 323 LYS n 
1 324 ILE n 
1 325 ILE n 
1 326 ASP n 
1 327 GLN n 
1 328 ILE n 
1 329 SER n 
1 330 LYS n 
1 331 ILE n 
1 332 ALA n 
1 333 LYS n 
1 334 ASN n 
1 335 GLY n 
1 336 THR n 
1 337 SER n 
1 338 LYS n 
1 339 ASN n 
1 340 ARG n 
1 341 VAL n 
1 342 SER n 
1 343 GLY n 
1 344 ALA n 
1 345 ASP n 
1 346 ARG n 
1 347 HIS n 
1 348 GLU n 
1 349 THR n 
1 350 ASN n 
1 351 ALA n 
1 352 ASN n 
1 353 VAL n 
1 354 ILE n 
1 355 LYS n 
1 356 THR n 
1 357 PHE n 
1 358 TYR n 
1 359 PRO n 
1 360 ASP n 
1 361 LYS n 
1 362 GLU n 
1 363 LEU n 
1 364 SER n 
1 365 ALA n 
1 366 MET n 
1 367 LEU n 
1 368 VAL n 
1 369 ALA n 
1 370 LYS n 
1 371 SER n 
1 372 ASP n 
1 373 ILE n 
1 374 ILE n 
1 375 VAL n 
1 376 ASP n 
1 377 SER n 
1 378 ILE n 
1 379 THR n 
1 380 ALA n 
1 381 GLY n 
1 382 PRO n 
1 383 LEU n 
1 384 ALA n 
1 385 ALA n 
1 386 LYS n 
1 387 LEU n 
1 388 LYS n 
1 389 ALA n 
1 390 PRO n 
1 391 ILE n 
1 392 LEU n 
1 393 ILE n 
1 394 THR n 
1 395 PRO n 
1 396 LYS n 
1 397 THR n 
1 398 TYR n 
1 399 VAL n 
1 400 SER n 
1 401 ALA n 
1 402 TYR n 
1 403 HIS n 
1 404 SER n 
1 405 THR n 
1 406 ASN n 
1 407 LEU n 
1 408 SER n 
1 409 GLU n 
1 410 LYS n 
1 411 THR n 
1 412 ALA n 
1 413 GLU n 
1 414 THR n 
1 415 VAL n 
1 416 TYR n 
1 417 GLN n 
1 418 ILE n 
1 419 GLY n 
1 420 ASP n 
1 421 GLY n 
1 422 MET n 
1 423 LYS n 
1 424 ASP n 
1 425 SER n 
1 426 VAL n 
1 427 ILE n 
1 428 ASN n 
1 429 SER n 
1 430 ILE n 
1 431 ALA n 
1 432 SER n 
1 433 SER n 
1 434 LEU n 
1 435 SER n 
1 436 LYS n 
1 437 HIS n 
1 438 ASN n 
1 439 ALA n 
1 440 PRO n 
1 441 THR n 
1 442 GLU n 
1 443 PRO n 
1 444 ASP n 
1 445 ASN n 
1 446 SER n 
1 447 GLY n 
1 448 SER n 
1 449 ALA n 
1 450 ALA n 
1 451 GLY n 
1 452 LYS n 
1 453 THR n 
1 454 VAL n 
1 455 VAL n 
1 456 ILE n 
1 457 ASP n 
1 458 PRO n 
1 459 GLY n 
1 460 HIS n 
1 461 GLY n 
1 462 GLY n 
1 463 SER n 
1 464 ASP n 
1 465 SER n 
1 466 GLY n 
1 467 ALA n 
1 468 THR n 
1 469 SER n 
1 470 GLY n 
1 471 LEU n 
1 472 ASN n 
1 473 GLY n 
1 474 GLY n 
1 475 ALA n 
1 476 GLN n 
1 477 GLU n 
1 478 LYS n 
1 479 LYS n 
1 480 TYR n 
1 481 THR n 
1 482 LEU n 
1 483 ASN n 
1 484 THR n 
1 485 ALA n 
1 486 LEU n 
1 487 ALA n 
1 488 THR n 
1 489 THR n 
1 490 GLU n 
1 491 TYR n 
1 492 LEU n 
1 493 ARG n 
1 494 SER n 
1 495 LYS n 
1 496 GLY n 
1 497 ILE n 
1 498 ASN n 
1 499 VAL n 
1 500 VAL n 
1 501 MET n 
1 502 THR n 
1 503 ARG n 
1 504 ASP n 
1 505 THR n 
1 506 ASP n 
1 507 LYS n 
1 508 THR n 
1 509 MET n 
1 510 ALA n 
1 511 LEU n 
1 512 GLY n 
1 513 GLU n 
1 514 ARG n 
1 515 THR n 
1 516 ALA n 
1 517 LEU n 
1 518 SER n 
1 519 ASN n 
1 520 THR n 
1 521 ILE n 
1 522 LYS n 
1 523 PRO n 
1 524 ASP n 
1 525 LEU n 
1 526 PHE n 
1 527 THR n 
1 528 SER n 
1 529 ILE n 
1 530 HIS n 
1 531 TYR n 
1 532 ASN n 
1 533 ALA n 
1 534 SER n 
1 535 ASN n 
1 536 GLY n 
1 537 SER n 
1 538 GLY n 
1 539 ASN n 
1 540 GLY n 
1 541 VAL n 
1 542 GLU n 
1 543 ILE n 
1 544 TYR n 
1 545 TYR n 
1 546 LYS n 
1 547 VAL n 
1 548 LYS n 
1 549 ASP n 
1 550 LYS n 
1 551 ASN n 
1 552 GLY n 
1 553 GLY n 
1 554 THR n 
1 555 THR n 
1 556 LYS n 
1 557 THR n 
1 558 ALA n 
1 559 ALA n 
1 560 SER n 
1 561 ASN n 
1 562 ILE n 
1 563 LEU n 
1 564 LYS n 
1 565 ARG n 
1 566 ILE n 
1 567 LEU n 
1 568 GLU n 
1 569 LYS n 
1 570 PHE n 
1 571 ASN n 
1 572 MET n 
1 573 LYS n 
1 574 ASN n 
1 575 ARG n 
1 576 GLY n 
1 577 ILE n 
1 578 LYS n 
1 579 THR n 
1 580 ARG n 
1 581 THR n 
1 582 LEU n 
1 583 ASP n 
1 584 ASN n 
1 585 GLY n 
1 586 LYS n 
1 587 ASP n 
1 588 TYR n 
1 589 LEU n 
1 590 TYR n 
1 591 VAL n 
1 592 LEU n 
1 593 ARG n 
1 594 ASN n 
1 595 ASN n 
1 596 ASN n 
1 597 TYR n 
1 598 PRO n 
1 599 ALA n 
1 600 ILE n 
1 601 LEU n 
1 602 VAL n 
1 603 GLU n 
1 604 CYS n 
1 605 ALA n 
1 606 PHE n 
1 607 ILE n 
1 608 ASP n 
1 609 ASN n 
1 610 LYS n 
1 611 SER n 
1 612 ASP n 
1 613 MET n 
1 614 ASP n 
1 615 LYS n 
1 616 LEU n 
1 617 ASN n 
1 618 THR n 
1 619 ALA n 
1 620 GLU n 
1 621 LYS n 
1 622 VAL n 
1 623 LYS n 
1 624 THR n 
1 625 MET n 
1 626 GLY n 
1 627 THR n 
1 628 GLN n 
1 629 ILE n 
1 630 GLY n 
1 631 ILE n 
1 632 GLY n 
1 633 ILE n 
1 634 GLU n 
1 635 ASP n 
1 636 THR n 
1 637 VAL n 
1 638 LYS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 639 ? ? 'cwp6, CD630_27840' ? 630 ? ? 'genomic DNA from C. difficile' ? 
'Peptoclostridium difficile (strain 630)' 272563 ? ? BAA-1382 ? ? ? ? ? 'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? ? 
? ? ? plasmid ? ? ? pMCSG9 ? ? 
5 1 sample 'Biological sequence' 1 639 ? ? 'cwp6, CD630_27840' ? 630 ? ? 'genomic DNA from C. difficile' ? 
'Peptoclostridium difficile (strain 630)' 272563 ? ? BAA-1382 ? ? ? ? ? 'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? ? 
? ? ? plasmid ? ? ? pMCSG9 ? ? 
# 
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  
CIT non-polymer         . 'CITRIC ACID'   ? 'C6 H8 O7'       192.124 
CL  non-polymer         . 'CHLORIDE ION'  ? 'Cl -1'          35.453  
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
NA  non-polymer         . 'SODIUM ION'    ? 'Na 1'           22.990  
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 
ZN  non-polymer         . 'ZINC ION'      ? 'Zn 2'           65.409  
# 
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   SER 1   10  10  SER SER A . n 
A 1 2   ASP 2   11  11  ASP ASP A . n 
A 1 3   ILE 3   12  12  ILE ILE A . n 
A 1 4   ASN 4   13  13  ASN ASN A . n 
A 1 5   ILE 5   14  14  ILE ILE A . n 
A 1 6   ASN 6   15  15  ASN ASN A . n 
A 1 7   LEU 7   16  16  LEU LEU A . n 
A 1 8   GLN 8   17  17  GLN GLN A . n 
A 1 9   ARG 9   18  18  ARG ARG A . n 
A 1 10  LYS 10  19  19  LYS LYS A . n 
A 1 11  SER 11  20  20  SER SER A . n 
A 1 12  VAL 12  21  21  VAL VAL A . n 
A 1 13  VAL 13  22  22  VAL VAL A . n 
A 1 14  LEU 14  23  23  LEU LEU A . n 
A 1 15  GLY 15  24  24  GLY GLY A . n 
A 1 16  SER 16  25  25  SER SER A . n 
A 1 17  LYS 17  26  26  LYS LYS A . n 
A 1 18  SER 18  27  27  SER SER A . n 
A 1 19  ASN 19  28  28  ASN ASN A . n 
A 1 20  ALA 20  29  29  ALA ALA A . n 
A 1 21  SER 21  30  30  SER SER A . n 
A 1 22  VAL 22  31  31  VAL VAL A . n 
A 1 23  LYS 23  32  32  LYS LYS A . n 
A 1 24  PHE 24  33  33  PHE PHE A . n 
A 1 25  LYS 25  34  34  LYS LYS A . n 
A 1 26  GLU 26  35  35  GLU GLU A . n 
A 1 27  LYS 27  36  36  LYS LYS A . n 
A 1 28  LEU 28  37  37  LEU LEU A . n 
A 1 29  ASN 29  38  38  ASN ASN A . n 
A 1 30  ALA 30  39  39  ALA ALA A . n 
A 1 31  ASP 31  40  40  ASP ASP A . n 
A 1 32  SER 32  41  41  SER SER A . n 
A 1 33  ILE 33  42  42  ILE ILE A . n 
A 1 34  THR 34  43  43  THR THR A . n 
A 1 35  LEU 35  44  44  LEU LEU A . n 
A 1 36  ASN 36  45  45  ASN ASN A . n 
A 1 37  PHE 37  46  46  PHE PHE A . n 
A 1 38  MET 38  47  47  MET MET A . n 
A 1 39  CYS 39  48  48  CYS CYS A . n 
A 1 40  TYR 40  49  49  TYR TYR A . n 
A 1 41  ASP 41  50  50  ASP ASP A . n 
A 1 42  MET 42  51  51  MET MET A . n 
A 1 43  PRO 43  52  52  PRO PRO A . n 
A 1 44  LEU 44  53  53  LEU LEU A . n 
A 1 45  GLU 45  54  54  GLU GLU A . n 
A 1 46  ALA 46  55  55  ALA ALA A . n 
A 1 47  THR 47  56  56  THR THR A . n 
A 1 48  LEU 48  57  57  LEU LEU A . n 
A 1 49  ASN 49  58  58  ASN ASN A . n 
A 1 50  TYR 50  59  59  TYR TYR A . n 
A 1 51  ASN 51  60  60  ASN ASN A . n 
A 1 52  GLU 52  61  61  GLU GLU A . n 
A 1 53  LYS 53  62  62  LYS LYS A . n 
A 1 54  THR 54  63  63  THR THR A . n 
A 1 55  ASP 55  64  64  ASP ASP A . n 
A 1 56  SER 56  65  65  SER SER A . n 
A 1 57  TYR 57  66  66  TYR TYR A . n 
A 1 58  GLU 58  67  67  GLU GLU A . n 
A 1 59  GLY 59  68  68  GLY GLY A . n 
A 1 60  VAL 60  69  69  VAL VAL A . n 
A 1 61  ILE 61  70  70  ILE ILE A . n 
A 1 62  ASN 62  71  71  ASN ASN A . n 
A 1 63  TYR 63  72  72  TYR TYR A . n 
A 1 64  ASN 64  73  73  ASN ASN A . n 
A 1 65  LYS 65  74  74  LYS LYS A . n 
A 1 66  ASP 66  75  75  ASP ASP A . n 
A 1 67  PRO 67  76  76  PRO PRO A . n 
A 1 68  GLU 68  77  77  GLU GLU A . n 
A 1 69  TYR 69  78  78  TYR TYR A . n 
A 1 70  LEU 70  79  79  LEU LEU A . n 
A 1 71  ASN 71  80  80  ASN ASN A . n 
A 1 72  VAL 72  81  81  VAL VAL A . n 
A 1 73  TRP 73  82  82  TRP TRP A . n 
A 1 74  GLU 74  83  83  GLU GLU A . n 
A 1 75  LEU 75  84  84  LEU LEU A . n 
A 1 76  GLN 76  85  85  GLN GLN A . n 
A 1 77  SER 77  86  86  SER SER A . n 
A 1 78  ILE 78  87  87  ILE ILE A . n 
A 1 79  LYS 79  88  88  LYS LYS A . n 
A 1 80  ILE 80  89  89  ILE ILE A . n 
A 1 81  ASN 81  90  90  ASN ASN A . n 
A 1 82  GLY 82  91  91  GLY GLY A . n 
A 1 83  LYS 83  92  92  LYS LYS A . n 
A 1 84  ASP 84  93  93  ASP ASP A . n 
A 1 85  GLU 85  94  94  GLU GLU A . n 
A 1 86  GLN 86  95  95  GLN GLN A . n 
A 1 87  LYS 87  96  96  LYS LYS A . n 
A 1 88  VAL 88  97  97  VAL VAL A . n 
A 1 89  LEU 89  98  98  LEU LEU A . n 
A 1 90  ASN 90  99  99  ASN ASN A . n 
A 1 91  LYS 91  100 100 LYS LYS A . n 
A 1 92  GLU 92  101 101 GLU GLU A . n 
A 1 93  ASP 93  102 102 ASP ASP A . n 
A 1 94  LEU 94  103 103 LEU LEU A . n 
A 1 95  GLU 95  104 104 GLU GLU A . n 
A 1 96  SER 96  105 105 SER SER A . n 
A 1 97  MET 97  106 106 MET MET A . n 
A 1 98  GLY 98  107 107 GLY GLY A . n 
A 1 99  LEU 99  108 108 LEU LEU A . n 
A 1 100 ASN 100 109 109 ASN ASN A . n 
A 1 101 LEU 101 110 110 LEU LEU A . n 
A 1 102 LYS 102 111 111 LYS LYS A . n 
A 1 103 ASP 103 112 112 ASP ASP A . n 
A 1 104 TYR 104 113 113 TYR TYR A . n 
A 1 105 ASP 105 114 114 ASP ASP A . n 
A 1 106 VAL 106 115 115 VAL VAL A . n 
A 1 107 THR 107 116 116 THR THR A . n 
A 1 108 GLN 108 117 117 GLN GLN A . n 
A 1 109 GLU 109 118 118 GLU GLU A . n 
A 1 110 PHE 110 119 119 PHE PHE A . n 
A 1 111 ILE 111 120 120 ILE ILE A . n 
A 1 112 ILE 112 121 121 ILE ILE A . n 
A 1 113 SER 113 122 122 SER SER A . n 
A 1 114 ASP 114 123 123 ASP ASP A . n 
A 1 115 ALA 115 124 124 ALA ALA A . n 
A 1 116 ASN 116 125 125 ASN ASN A . n 
A 1 117 SER 117 126 126 SER SER A . n 
A 1 118 THR 118 127 127 THR THR A . n 
A 1 119 LYS 119 128 128 LYS LYS A . n 
A 1 120 ALA 120 129 129 ALA ALA A . n 
A 1 121 VAL 121 130 130 VAL VAL A . n 
A 1 122 ASN 122 131 131 ASN ASN A . n 
A 1 123 GLU 123 132 132 GLU GLU A . n 
A 1 124 TYR 124 133 133 TYR TYR A . n 
A 1 125 MET 125 134 134 MET MET A . n 
A 1 126 ARG 126 135 135 ARG ARG A . n 
A 1 127 LYS 127 136 136 LYS LYS A . n 
A 1 128 THR 128 137 137 THR THR A . n 
A 1 129 SER 129 138 138 SER SER A . n 
A 1 130 ALA 130 139 139 ALA ALA A . n 
A 1 131 PRO 131 140 140 PRO PRO A . n 
A 1 132 VAL 132 141 141 VAL VAL A . n 
A 1 133 LYS 133 142 142 LYS LYS A . n 
A 1 134 LYS 134 143 143 LYS LYS A . n 
A 1 135 LEU 135 144 144 LEU LEU A . n 
A 1 136 ALA 136 145 145 ALA ALA A . n 
A 1 137 GLY 137 146 146 GLY GLY A . n 
A 1 138 ALA 138 147 147 ALA ALA A . n 
A 1 139 THR 139 148 148 THR THR A . n 
A 1 140 ARG 140 149 149 ARG ARG A . n 
A 1 141 PHE 141 150 150 PHE PHE A . n 
A 1 142 GLU 142 151 151 GLU GLU A . n 
A 1 143 THR 143 152 152 THR THR A . n 
A 1 144 ALA 144 153 153 ALA ALA A . n 
A 1 145 VAL 145 154 154 VAL VAL A . n 
A 1 146 GLU 146 155 155 GLU GLU A . n 
A 1 147 ILE 147 156 156 ILE ILE A . n 
A 1 148 SER 148 157 157 SER SER A . n 
A 1 149 LYS 149 158 158 LYS LYS A . n 
A 1 150 GLN 150 159 159 GLN GLN A . n 
A 1 151 GLY 151 160 160 GLY GLY A . n 
A 1 152 TRP 152 161 161 TRP TRP A . n 
A 1 153 LYS 153 162 162 LYS LYS A . n 
A 1 154 ASP 154 163 163 ASP ASP A . n 
A 1 155 GLY 155 164 164 GLY GLY A . n 
A 1 156 SER 156 165 165 SER SER A . n 
A 1 157 SER 157 166 166 SER SER A . n 
A 1 158 LYS 158 167 167 LYS LYS A . n 
A 1 159 VAL 159 168 168 VAL VAL A . n 
A 1 160 VAL 160 169 169 VAL VAL A . n 
A 1 161 ILE 161 170 170 ILE ILE A . n 
A 1 162 VAL 162 171 171 VAL VAL A . n 
A 1 163 ASN 163 172 172 ASN ASN A . n 
A 1 164 GLY 164 173 173 GLY GLY A . n 
A 1 165 GLU 165 174 174 GLU GLU A . n 
A 1 166 LEU 166 175 175 LEU LEU A . n 
A 1 167 ALA 167 176 176 ALA ALA A . n 
A 1 168 ALA 168 177 177 ALA ALA A . n 
A 1 169 ASP 169 178 178 ASP ASP A . n 
A 1 170 GLY 170 179 179 GLY GLY A . n 
A 1 171 ILE 171 180 180 ILE ILE A . n 
A 1 172 THR 172 181 181 THR THR A . n 
A 1 173 ALA 173 182 182 ALA ALA A . n 
A 1 174 THR 174 183 183 THR THR A . n 
A 1 175 PRO 175 184 184 PRO PRO A . n 
A 1 176 LEU 176 185 185 LEU LEU A . n 
A 1 177 ALA 177 186 186 ALA ALA A . n 
A 1 178 SER 178 187 187 SER SER A . n 
A 1 179 THR 179 188 188 THR THR A . n 
A 1 180 TYR 180 189 189 TYR TYR A . n 
A 1 181 ASP 181 190 190 ASP ASP A . n 
A 1 182 ALA 182 191 191 ALA ALA A . n 
A 1 183 PRO 183 192 192 PRO PRO A . n 
A 1 184 ILE 184 193 193 ILE ILE A . n 
A 1 185 LEU 185 194 194 LEU LEU A . n 
A 1 186 LEU 186 195 195 LEU LEU A . n 
A 1 187 ALA 187 196 196 ALA ALA A . n 
A 1 188 ASN 188 197 197 ASN ASN A . n 
A 1 189 LYS 189 198 198 LYS LYS A . n 
A 1 190 ASP 190 199 199 ASP ASP A . n 
A 1 191 ASP 191 200 200 ASP ASP A . n 
A 1 192 ILE 192 201 201 ILE ILE A . n 
A 1 193 PRO 193 202 202 PRO PRO A . n 
A 1 194 GLU 194 203 203 GLU GLU A . n 
A 1 195 SER 195 204 204 SER SER A . n 
A 1 196 THR 196 205 205 THR THR A . n 
A 1 197 LYS 197 206 206 LYS LYS A . n 
A 1 198 ALA 198 207 207 ALA ALA A . n 
A 1 199 GLU 199 208 208 GLU GLU A . n 
A 1 200 LEU 200 209 209 LEU LEU A . n 
A 1 201 LYS 201 210 210 LYS LYS A . n 
A 1 202 ARG 202 211 211 ARG ARG A . n 
A 1 203 LEU 203 212 212 LEU LEU A . n 
A 1 204 ASN 204 213 213 ASN ASN A . n 
A 1 205 PRO 205 214 214 PRO PRO A . n 
A 1 206 SER 206 215 215 SER SER A . n 
A 1 207 ASP 207 216 216 ASP ASP A . n 
A 1 208 VAL 208 217 217 VAL VAL A . n 
A 1 209 ILE 209 218 218 ILE ILE A . n 
A 1 210 ILE 210 219 219 ILE ILE A . n 
A 1 211 ILE 211 220 220 ILE ILE A . n 
A 1 212 GLY 212 221 221 GLY GLY A . n 
A 1 213 ASP 213 222 222 ASP ASP A . n 
A 1 214 ASP 214 223 223 ASP ASP A . n 
A 1 215 GLY 215 224 224 GLY GLY A . n 
A 1 216 SER 216 225 225 SER SER A . n 
A 1 217 VAL 217 226 226 VAL VAL A . n 
A 1 218 SER 218 227 227 SER SER A . n 
A 1 219 GLN 219 228 228 GLN GLN A . n 
A 1 220 LYS 220 229 229 LYS LYS A . n 
A 1 221 ALA 221 230 230 ALA ALA A . n 
A 1 222 VAL 222 231 231 VAL VAL A . n 
A 1 223 SER 223 232 232 SER SER A . n 
A 1 224 GLN 224 233 233 GLN GLN A . n 
A 1 225 ILE 225 234 234 ILE ILE A . n 
A 1 226 LYS 226 235 235 LYS LYS A . n 
A 1 227 SER 227 236 236 SER SER A . n 
A 1 228 ALA 228 237 237 ALA ALA A . n 
A 1 229 VAL 229 238 238 VAL VAL A . n 
A 1 230 ASN 230 239 239 ASN ASN A . n 
A 1 231 VAL 231 240 240 VAL VAL A . n 
A 1 232 ASN 232 241 241 ASN ASN A . n 
A 1 233 VAL 233 242 242 VAL VAL A . n 
A 1 234 THR 234 243 243 THR THR A . n 
A 1 235 ARG 235 244 244 ARG ARG A . n 
A 1 236 ILE 236 245 245 ILE ILE A . n 
A 1 237 GLY 237 246 246 GLY GLY A . n 
A 1 238 GLY 238 247 247 GLY GLY A . n 
A 1 239 VAL 239 248 248 VAL VAL A . n 
A 1 240 ASP 240 249 249 ASP ASP A . n 
A 1 241 ARG 241 250 250 ARG ARG A . n 
A 1 242 HIS 242 251 251 HIS HIS A . n 
A 1 243 GLU 243 252 252 GLU GLU A . n 
A 1 244 THR 244 253 253 THR THR A . n 
A 1 245 SER 245 254 254 SER SER A . n 
A 1 246 LEU 246 255 255 LEU LEU A . n 
A 1 247 LEU 247 256 256 LEU LEU A . n 
A 1 248 ILE 248 257 257 ILE ILE A . n 
A 1 249 ALA 249 258 258 ALA ALA A . n 
A 1 250 LYS 250 259 259 LYS LYS A . n 
A 1 251 GLU 251 260 260 GLU GLU A . n 
A 1 252 ILE 252 261 261 ILE ILE A . n 
A 1 253 ASP 253 262 262 ASP ASP A . n 
A 1 254 LYS 254 263 263 LYS LYS A . n 
A 1 255 TYR 255 264 264 TYR TYR A . n 
A 1 256 HIS 256 265 265 HIS HIS A . n 
A 1 257 ASP 257 266 266 ASP ASP A . n 
A 1 258 VAL 258 267 267 VAL VAL A . n 
A 1 259 ASN 259 268 268 ASN ASN A . n 
A 1 260 LYS 260 269 269 LYS LYS A . n 
A 1 261 ILE 261 270 270 ILE ILE A . n 
A 1 262 TYR 262 271 271 TYR TYR A . n 
A 1 263 ILE 263 272 272 ILE ILE A . n 
A 1 264 ALA 264 273 273 ALA ALA A . n 
A 1 265 ASN 265 274 274 ASN ASN A . n 
A 1 266 GLY 266 275 275 GLY GLY A . n 
A 1 267 TYR 267 276 276 TYR TYR A . n 
A 1 268 ALA 268 277 277 ALA ALA A . n 
A 1 269 GLY 269 278 278 GLY GLY A . n 
A 1 270 GLU 270 279 279 GLU GLU A . n 
A 1 271 TYR 271 280 280 TYR TYR A . n 
A 1 272 ASP 272 281 281 ASP ASP A . n 
A 1 273 ALA 273 282 282 ALA ALA A . n 
A 1 274 LEU 274 283 283 LEU LEU A . n 
A 1 275 ASN 275 284 284 ASN ASN A . n 
A 1 276 ILE 276 285 285 ILE ILE A . n 
A 1 277 SER 277 286 286 SER SER A . n 
A 1 278 SER 278 287 287 SER SER A . n 
A 1 279 LYS 279 288 288 LYS LYS A . n 
A 1 280 ALA 280 289 289 ALA ALA A . n 
A 1 281 GLY 281 290 290 GLY GLY A . n 
A 1 282 GLU 282 291 291 GLU GLU A . n 
A 1 283 ASP 283 292 292 ASP ASP A . n 
A 1 284 GLN 284 293 293 GLN GLN A . n 
A 1 285 GLN 285 294 294 GLN GLN A . n 
A 1 286 PRO 286 295 295 PRO PRO A . n 
A 1 287 ILE 287 296 296 ILE ILE A . n 
A 1 288 ILE 288 297 297 ILE ILE A . n 
A 1 289 LEU 289 298 298 LEU LEU A . n 
A 1 290 ALA 290 299 299 ALA ALA A . n 
A 1 291 ASN 291 300 300 ASN ASN A . n 
A 1 292 LYS 292 301 301 LYS LYS A . n 
A 1 293 ASP 293 302 302 ASP ASP A . n 
A 1 294 SER 294 303 303 SER SER A . n 
A 1 295 VAL 295 304 304 VAL VAL A . n 
A 1 296 PRO 296 305 305 PRO PRO A . n 
A 1 297 GLN 297 306 306 GLN GLN A . n 
A 1 298 GLY 298 307 307 GLY GLY A . n 
A 1 299 THR 299 308 308 THR THR A . n 
A 1 300 TYR 300 309 309 TYR TYR A . n 
A 1 301 ASN 301 310 310 ASN ASN A . n 
A 1 302 TRP 302 311 311 TRP TRP A . n 
A 1 303 LEU 303 312 312 LEU LEU A . n 
A 1 304 SER 304 313 313 SER SER A . n 
A 1 305 SER 305 314 314 SER SER A . n 
A 1 306 GLN 306 315 315 GLN GLN A . n 
A 1 307 GLY 307 316 316 GLY GLY A . n 
A 1 308 LEU 308 317 317 LEU LEU A . n 
A 1 309 GLU 309 318 318 GLU GLU A . n 
A 1 310 GLU 310 319 319 GLU GLU A . n 
A 1 311 ALA 311 320 320 ALA ALA A . n 
A 1 312 TYR 312 321 321 TYR TYR A . n 
A 1 313 TYR 313 322 322 TYR TYR A . n 
A 1 314 ILE 314 323 323 ILE ILE A . n 
A 1 315 GLY 315 324 324 GLY GLY A . n 
A 1 316 GLY 316 325 325 GLY GLY A . n 
A 1 317 SER 317 326 326 SER SER A . n 
A 1 318 GLN 318 327 327 GLN GLN A . n 
A 1 319 SER 319 328 328 SER SER A . n 
A 1 320 LEU 320 329 329 LEU LEU A . n 
A 1 321 SER 321 330 330 SER SER A . n 
A 1 322 SER 322 331 331 SER SER A . n 
A 1 323 LYS 323 332 332 LYS LYS A . n 
A 1 324 ILE 324 333 333 ILE ILE A . n 
A 1 325 ILE 325 334 334 ILE ILE A . n 
A 1 326 ASP 326 335 335 ASP ASP A . n 
A 1 327 GLN 327 336 336 GLN GLN A . n 
A 1 328 ILE 328 337 337 ILE ILE A . n 
A 1 329 SER 329 338 338 SER SER A . n 
A 1 330 LYS 330 339 339 LYS LYS A . n 
A 1 331 ILE 331 340 340 ILE ILE A . n 
A 1 332 ALA 332 341 341 ALA ALA A . n 
A 1 333 LYS 333 342 342 LYS LYS A . n 
A 1 334 ASN 334 343 343 ASN ASN A . n 
A 1 335 GLY 335 344 344 GLY GLY A . n 
A 1 336 THR 336 345 345 THR THR A . n 
A 1 337 SER 337 346 346 SER SER A . n 
A 1 338 LYS 338 347 347 LYS LYS A . n 
A 1 339 ASN 339 348 348 ASN ASN A . n 
A 1 340 ARG 340 349 349 ARG ARG A . n 
A 1 341 VAL 341 350 350 VAL VAL A . n 
A 1 342 SER 342 351 351 SER SER A . n 
A 1 343 GLY 343 352 352 GLY GLY A . n 
A 1 344 ALA 344 353 353 ALA ALA A . n 
A 1 345 ASP 345 354 354 ASP ASP A . n 
A 1 346 ARG 346 355 355 ARG ARG A . n 
A 1 347 HIS 347 356 356 HIS HIS A . n 
A 1 348 GLU 348 357 357 GLU GLU A . n 
A 1 349 THR 349 358 358 THR THR A . n 
A 1 350 ASN 350 359 359 ASN ASN A . n 
A 1 351 ALA 351 360 360 ALA ALA A . n 
A 1 352 ASN 352 361 361 ASN ASN A . n 
A 1 353 VAL 353 362 362 VAL VAL A . n 
A 1 354 ILE 354 363 363 ILE ILE A . n 
A 1 355 LYS 355 364 364 LYS LYS A . n 
A 1 356 THR 356 365 365 THR THR A . n 
A 1 357 PHE 357 366 366 PHE PHE A . n 
A 1 358 TYR 358 367 367 TYR TYR A . n 
A 1 359 PRO 359 368 368 PRO PRO A . n 
A 1 360 ASP 360 369 369 ASP ASP A . n 
A 1 361 LYS 361 370 370 LYS LYS A . n 
A 1 362 GLU 362 371 371 GLU GLU A . n 
A 1 363 LEU 363 372 372 LEU LEU A . n 
A 1 364 SER 364 373 373 SER SER A . n 
A 1 365 ALA 365 374 374 ALA ALA A . n 
A 1 366 MET 366 375 375 MET MET A . n 
A 1 367 LEU 367 376 376 LEU LEU A . n 
A 1 368 VAL 368 377 377 VAL VAL A . n 
A 1 369 ALA 369 378 378 ALA ALA A . n 
A 1 370 LYS 370 379 379 LYS LYS A . n 
A 1 371 SER 371 380 380 SER SER A . n 
A 1 372 ASP 372 381 381 ASP ASP A . n 
A 1 373 ILE 373 382 382 ILE ILE A . n 
A 1 374 ILE 374 383 383 ILE ILE A . n 
A 1 375 VAL 375 384 384 VAL VAL A . n 
A 1 376 ASP 376 385 385 ASP ASP A . n 
A 1 377 SER 377 386 386 SER SER A . n 
A 1 378 ILE 378 387 387 ILE ILE A . n 
A 1 379 THR 379 388 388 THR THR A . n 
A 1 380 ALA 380 389 389 ALA ALA A . n 
A 1 381 GLY 381 390 390 GLY GLY A . n 
A 1 382 PRO 382 391 391 PRO PRO A . n 
A 1 383 LEU 383 392 392 LEU LEU A . n 
A 1 384 ALA 384 393 393 ALA ALA A . n 
A 1 385 ALA 385 394 394 ALA ALA A . n 
A 1 386 LYS 386 395 395 LYS LYS A . n 
A 1 387 LEU 387 396 396 LEU LEU A . n 
A 1 388 LYS 388 397 397 LYS LYS A . n 
A 1 389 ALA 389 398 398 ALA ALA A . n 
A 1 390 PRO 390 399 399 PRO PRO A . n 
A 1 391 ILE 391 400 400 ILE ILE A . n 
A 1 392 LEU 392 401 401 LEU LEU A . n 
A 1 393 ILE 393 402 402 ILE ILE A . n 
A 1 394 THR 394 403 403 THR THR A . n 
A 1 395 PRO 395 404 404 PRO PRO A . n 
A 1 396 LYS 396 405 405 LYS LYS A . n 
A 1 397 THR 397 406 406 THR THR A . n 
A 1 398 TYR 398 407 407 TYR TYR A . n 
A 1 399 VAL 399 408 408 VAL VAL A . n 
A 1 400 SER 400 409 409 SER SER A . n 
A 1 401 ALA 401 410 410 ALA ALA A . n 
A 1 402 TYR 402 411 411 TYR TYR A . n 
A 1 403 HIS 403 412 412 HIS HIS A . n 
A 1 404 SER 404 413 413 SER SER A . n 
A 1 405 THR 405 414 414 THR THR A . n 
A 1 406 ASN 406 415 415 ASN ASN A . n 
A 1 407 LEU 407 416 416 LEU LEU A . n 
A 1 408 SER 408 417 417 SER SER A . n 
A 1 409 GLU 409 418 418 GLU GLU A . n 
A 1 410 LYS 410 419 419 LYS LYS A . n 
A 1 411 THR 411 420 420 THR THR A . n 
A 1 412 ALA 412 421 421 ALA ALA A . n 
A 1 413 GLU 413 422 422 GLU GLU A . n 
A 1 414 THR 414 423 423 THR THR A . n 
A 1 415 VAL 415 424 424 VAL VAL A . n 
A 1 416 TYR 416 425 425 TYR TYR A . n 
A 1 417 GLN 417 426 426 GLN GLN A . n 
A 1 418 ILE 418 427 427 ILE ILE A . n 
A 1 419 GLY 419 428 428 GLY GLY A . n 
A 1 420 ASP 420 429 429 ASP ASP A . n 
A 1 421 GLY 421 430 430 GLY GLY A . n 
A 1 422 MET 422 431 431 MET MET A . n 
A 1 423 LYS 423 432 432 LYS LYS A . n 
A 1 424 ASP 424 433 433 ASP ASP A . n 
A 1 425 SER 425 434 434 SER SER A . n 
A 1 426 VAL 426 435 435 VAL VAL A . n 
A 1 427 ILE 427 436 436 ILE ILE A . n 
A 1 428 ASN 428 437 437 ASN ASN A . n 
A 1 429 SER 429 438 438 SER SER A . n 
A 1 430 ILE 430 439 439 ILE ILE A . n 
A 1 431 ALA 431 440 440 ALA ALA A . n 
A 1 432 SER 432 441 441 SER SER A . n 
A 1 433 SER 433 442 442 SER SER A . n 
A 1 434 LEU 434 443 443 LEU LEU A . n 
A 1 435 SER 435 444 444 SER SER A . n 
A 1 436 LYS 436 445 445 LYS LYS A . n 
A 1 437 HIS 437 446 446 HIS HIS A . n 
A 1 438 ASN 438 447 447 ASN ASN A . n 
A 1 439 ALA 439 448 448 ALA ALA A . n 
A 1 440 PRO 440 449 449 PRO PRO A . n 
A 1 441 THR 441 450 450 THR THR A . n 
A 1 442 GLU 442 451 451 GLU GLU A . n 
A 1 443 PRO 443 452 452 PRO PRO A . n 
A 1 444 ASP 444 453 453 ASP ASP A . n 
A 1 445 ASN 445 454 454 ASN ASN A . n 
A 1 446 SER 446 455 455 SER SER A . n 
A 1 447 GLY 447 456 456 GLY GLY A . n 
A 1 448 SER 448 457 457 SER SER A . n 
A 1 449 ALA 449 458 458 ALA ALA A . n 
A 1 450 ALA 450 459 459 ALA ALA A . n 
A 1 451 GLY 451 460 460 GLY GLY A . n 
A 1 452 LYS 452 461 461 LYS LYS A . n 
A 1 453 THR 453 462 462 THR THR A . n 
A 1 454 VAL 454 463 463 VAL VAL A . n 
A 1 455 VAL 455 464 464 VAL VAL A . n 
A 1 456 ILE 456 465 465 ILE ILE A . n 
A 1 457 ASP 457 466 466 ASP ASP A . n 
A 1 458 PRO 458 467 467 PRO PRO A . n 
A 1 459 GLY 459 468 468 GLY GLY A . n 
A 1 460 HIS 460 469 469 HIS HIS A . n 
A 1 461 GLY 461 470 470 GLY GLY A . n 
A 1 462 GLY 462 471 471 GLY GLY A . n 
A 1 463 SER 463 472 472 SER SER A . n 
A 1 464 ASP 464 473 473 ASP ASP A . n 
A 1 465 SER 465 474 474 SER SER A . n 
A 1 466 GLY 466 475 475 GLY GLY A . n 
A 1 467 ALA 467 476 476 ALA ALA A . n 
A 1 468 THR 468 477 477 THR THR A . n 
A 1 469 SER 469 478 478 SER SER A . n 
A 1 470 GLY 470 479 479 GLY GLY A . n 
A 1 471 LEU 471 480 480 LEU LEU A . n 
A 1 472 ASN 472 481 481 ASN ASN A . n 
A 1 473 GLY 473 482 482 GLY GLY A . n 
A 1 474 GLY 474 483 483 GLY GLY A . n 
A 1 475 ALA 475 484 484 ALA ALA A . n 
A 1 476 GLN 476 485 485 GLN GLN A . n 
A 1 477 GLU 477 486 486 GLU GLU A . n 
A 1 478 LYS 478 487 487 LYS LYS A . n 
A 1 479 LYS 479 488 488 LYS LYS A . n 
A 1 480 TYR 480 489 489 TYR TYR A . n 
A 1 481 THR 481 490 490 THR THR A . n 
A 1 482 LEU 482 491 491 LEU LEU A . n 
A 1 483 ASN 483 492 492 ASN ASN A . n 
A 1 484 THR 484 493 493 THR THR A . n 
A 1 485 ALA 485 494 494 ALA ALA A . n 
A 1 486 LEU 486 495 495 LEU LEU A . n 
A 1 487 ALA 487 496 496 ALA ALA A . n 
A 1 488 THR 488 497 497 THR THR A . n 
A 1 489 THR 489 498 498 THR THR A . n 
A 1 490 GLU 490 499 499 GLU GLU A . n 
A 1 491 TYR 491 500 500 TYR TYR A . n 
A 1 492 LEU 492 501 501 LEU LEU A . n 
A 1 493 ARG 493 502 502 ARG ARG A . n 
A 1 494 SER 494 503 503 SER SER A . n 
A 1 495 LYS 495 504 504 LYS LYS A . n 
A 1 496 GLY 496 505 505 GLY GLY A . n 
A 1 497 ILE 497 506 506 ILE ILE A . n 
A 1 498 ASN 498 507 507 ASN ASN A . n 
A 1 499 VAL 499 508 508 VAL VAL A . n 
A 1 500 VAL 500 509 509 VAL VAL A . n 
A 1 501 MET 501 510 510 MET MET A . n 
A 1 502 THR 502 511 511 THR THR A . n 
A 1 503 ARG 503 512 512 ARG ARG A . n 
A 1 504 ASP 504 513 513 ASP ASP A . n 
A 1 505 THR 505 514 514 THR THR A . n 
A 1 506 ASP 506 515 515 ASP ASP A . n 
A 1 507 LYS 507 516 516 LYS LYS A . n 
A 1 508 THR 508 517 517 THR THR A . n 
A 1 509 MET 509 518 518 MET MET A . n 
A 1 510 ALA 510 519 519 ALA ALA A . n 
A 1 511 LEU 511 520 520 LEU LEU A . n 
A 1 512 GLY 512 521 521 GLY GLY A . n 
A 1 513 GLU 513 522 522 GLU GLU A . n 
A 1 514 ARG 514 523 523 ARG ARG A . n 
A 1 515 THR 515 524 524 THR THR A . n 
A 1 516 ALA 516 525 525 ALA ALA A . n 
A 1 517 LEU 517 526 526 LEU LEU A . n 
A 1 518 SER 518 527 527 SER SER A . n 
A 1 519 ASN 519 528 528 ASN ASN A . n 
A 1 520 THR 520 529 529 THR THR A . n 
A 1 521 ILE 521 530 530 ILE ILE A . n 
A 1 522 LYS 522 531 531 LYS LYS A . n 
A 1 523 PRO 523 532 532 PRO PRO A . n 
A 1 524 ASP 524 533 533 ASP ASP A . n 
A 1 525 LEU 525 534 534 LEU LEU A . n 
A 1 526 PHE 526 535 535 PHE PHE A . n 
A 1 527 THR 527 536 536 THR THR A . n 
A 1 528 SER 528 537 537 SER SER A . n 
A 1 529 ILE 529 538 538 ILE ILE A . n 
A 1 530 HIS 530 539 539 HIS HIS A . n 
A 1 531 TYR 531 540 540 TYR TYR A . n 
A 1 532 ASN 532 541 541 ASN ASN A . n 
A 1 533 ALA 533 542 542 ALA ALA A . n 
A 1 534 SER 534 543 543 SER SER A . n 
A 1 535 ASN 535 544 544 ASN ASN A . n 
A 1 536 GLY 536 545 545 GLY GLY A . n 
A 1 537 SER 537 546 546 SER SER A . n 
A 1 538 GLY 538 547 547 GLY GLY A . n 
A 1 539 ASN 539 548 548 ASN ASN A . n 
A 1 540 GLY 540 549 549 GLY GLY A . n 
A 1 541 VAL 541 550 550 VAL VAL A . n 
A 1 542 GLU 542 551 551 GLU GLU A . n 
A 1 543 ILE 543 552 552 ILE ILE A . n 
A 1 544 TYR 544 553 553 TYR TYR A . n 
A 1 545 TYR 545 554 554 TYR TYR A . n 
A 1 546 LYS 546 555 555 LYS LYS A . n 
A 1 547 VAL 547 556 556 VAL VAL A . n 
A 1 548 LYS 548 557 557 LYS LYS A . n 
A 1 549 ASP 549 558 558 ASP ASP A . n 
A 1 550 LYS 550 559 559 LYS LYS A . n 
A 1 551 ASN 551 560 560 ASN ASN A . n 
A 1 552 GLY 552 561 561 GLY GLY A . n 
A 1 553 GLY 553 562 562 GLY GLY A . n 
A 1 554 THR 554 563 563 THR THR A . n 
A 1 555 THR 555 564 564 THR THR A . n 
A 1 556 LYS 556 565 565 LYS LYS A . n 
A 1 557 THR 557 566 566 THR THR A . n 
A 1 558 ALA 558 567 567 ALA ALA A . n 
A 1 559 ALA 559 568 568 ALA ALA A . n 
A 1 560 SER 560 569 569 SER SER A . n 
A 1 561 ASN 561 570 570 ASN ASN A . n 
A 1 562 ILE 562 571 571 ILE ILE A . n 
A 1 563 LEU 563 572 572 LEU LEU A . n 
A 1 564 LYS 564 573 573 LYS LYS A . n 
A 1 565 ARG 565 574 574 ARG ARG A . n 
A 1 566 ILE 566 575 575 ILE ILE A . n 
A 1 567 LEU 567 576 576 LEU LEU A . n 
A 1 568 GLU 568 577 577 GLU GLU A . n 
A 1 569 LYS 569 578 578 LYS LYS A . n 
A 1 570 PHE 570 579 579 PHE PHE A . n 
A 1 571 ASN 571 580 580 ASN ASN A . n 
A 1 572 MET 572 581 581 MET MET A . n 
A 1 573 LYS 573 582 582 LYS LYS A . n 
A 1 574 ASN 574 583 583 ASN ASN A . n 
A 1 575 ARG 575 584 584 ARG ARG A . n 
A 1 576 GLY 576 585 585 GLY GLY A . n 
A 1 577 ILE 577 586 586 ILE ILE A . n 
A 1 578 LYS 578 587 587 LYS LYS A . n 
A 1 579 THR 579 588 588 THR THR A . n 
A 1 580 ARG 580 589 589 ARG ARG A . n 
A 1 581 THR 581 590 590 THR THR A . n 
A 1 582 LEU 582 591 591 LEU LEU A . n 
A 1 583 ASP 583 592 592 ASP ASP A . n 
A 1 584 ASN 584 593 593 ASN ASN A . n 
A 1 585 GLY 585 594 594 GLY GLY A . n 
A 1 586 LYS 586 595 595 LYS LYS A . n 
A 1 587 ASP 587 596 596 ASP ASP A . n 
A 1 588 TYR 588 597 597 TYR TYR A . n 
A 1 589 LEU 589 598 598 LEU LEU A . n 
A 1 590 TYR 590 599 599 TYR TYR A . n 
A 1 591 VAL 591 600 600 VAL VAL A . n 
A 1 592 LEU 592 601 601 LEU LEU A . n 
A 1 593 ARG 593 602 602 ARG ARG A . n 
A 1 594 ASN 594 603 603 ASN ASN A . n 
A 1 595 ASN 595 604 604 ASN ASN A . n 
A 1 596 ASN 596 605 605 ASN ASN A . n 
A 1 597 TYR 597 606 606 TYR TYR A . n 
A 1 598 PRO 598 607 607 PRO PRO A . n 
A 1 599 ALA 599 608 608 ALA ALA A . n 
A 1 600 ILE 600 609 609 ILE ILE A . n 
A 1 601 LEU 601 610 610 LEU LEU A . n 
A 1 602 VAL 602 611 611 VAL VAL A . n 
A 1 603 GLU 603 612 612 GLU GLU A . n 
A 1 604 CYS 604 613 613 CYS CYS A . n 
A 1 605 ALA 605 614 614 ALA ALA A . n 
A 1 606 PHE 606 615 615 PHE PHE A . n 
A 1 607 ILE 607 616 616 ILE ILE A . n 
A 1 608 ASP 608 617 617 ASP ASP A . n 
A 1 609 ASN 609 618 618 ASN ASN A . n 
A 1 610 LYS 610 619 619 LYS LYS A . n 
A 1 611 SER 611 620 620 SER SER A . n 
A 1 612 ASP 612 621 621 ASP ASP A . n 
A 1 613 MET 613 622 622 MET MET A . n 
A 1 614 ASP 614 623 623 ASP ASP A . n 
A 1 615 LYS 615 624 624 LYS LYS A . n 
A 1 616 LEU 616 625 625 LEU LEU A . n 
A 1 617 ASN 617 626 626 ASN ASN A . n 
A 1 618 THR 618 627 627 THR THR A . n 
A 1 619 ALA 619 628 628 ALA ALA A . n 
A 1 620 GLU 620 629 629 GLU GLU A . n 
A 1 621 LYS 621 630 630 LYS LYS A . n 
A 1 622 VAL 622 631 631 VAL VAL A . n 
A 1 623 LYS 623 632 632 LYS LYS A . n 
A 1 624 THR 624 633 633 THR THR A . n 
A 1 625 MET 625 634 634 MET MET A . n 
A 1 626 GLY 626 635 635 GLY GLY A . n 
A 1 627 THR 627 636 636 THR THR A . n 
A 1 628 GLN 628 637 637 GLN GLN A . n 
A 1 629 ILE 629 638 638 ILE ILE A . n 
A 1 630 GLY 630 639 639 GLY GLY A . n 
A 1 631 ILE 631 640 640 ILE ILE A . n 
A 1 632 GLY 632 641 641 GLY GLY A . n 
A 1 633 ILE 633 642 642 ILE ILE A . n 
A 1 634 GLU 634 643 643 GLU GLU A . n 
A 1 635 ASP 635 644 644 ASP ASP A . n 
A 1 636 THR 636 645 645 THR THR A . n 
A 1 637 VAL 637 646 646 VAL VAL A . n 
A 1 638 LYS 638 647 647 LYS LYS A . n 
B 1 1   SER 1   10  10  SER SER B . n 
B 1 2   ASP 2   11  11  ASP ASP B . n 
B 1 3   ILE 3   12  12  ILE ILE B . n 
B 1 4   ASN 4   13  13  ASN ASN B . n 
B 1 5   ILE 5   14  14  ILE ILE B . n 
B 1 6   ASN 6   15  15  ASN ASN B . n 
B 1 7   LEU 7   16  16  LEU LEU B . n 
B 1 8   GLN 8   17  17  GLN GLN B . n 
B 1 9   ARG 9   18  18  ARG ARG B . n 
B 1 10  LYS 10  19  19  LYS LYS B . n 
B 1 11  SER 11  20  20  SER SER B . n 
B 1 12  VAL 12  21  21  VAL VAL B . n 
B 1 13  VAL 13  22  22  VAL VAL B . n 
B 1 14  LEU 14  23  23  LEU LEU B . n 
B 1 15  GLY 15  24  24  GLY GLY B . n 
B 1 16  SER 16  25  25  SER SER B . n 
B 1 17  LYS 17  26  26  LYS LYS B . n 
B 1 18  SER 18  27  27  SER SER B . n 
B 1 19  ASN 19  28  28  ASN ASN B . n 
B 1 20  ALA 20  29  29  ALA ALA B . n 
B 1 21  SER 21  30  30  SER SER B . n 
B 1 22  VAL 22  31  31  VAL VAL B . n 
B 1 23  LYS 23  32  32  LYS LYS B . n 
B 1 24  PHE 24  33  33  PHE PHE B . n 
B 1 25  LYS 25  34  34  LYS LYS B . n 
B 1 26  GLU 26  35  35  GLU GLU B . n 
B 1 27  LYS 27  36  36  LYS LYS B . n 
B 1 28  LEU 28  37  37  LEU LEU B . n 
B 1 29  ASN 29  38  38  ASN ASN B . n 
B 1 30  ALA 30  39  39  ALA ALA B . n 
B 1 31  ASP 31  40  40  ASP ASP B . n 
B 1 32  SER 32  41  41  SER SER B . n 
B 1 33  ILE 33  42  42  ILE ILE B . n 
B 1 34  THR 34  43  43  THR THR B . n 
B 1 35  LEU 35  44  44  LEU LEU B . n 
B 1 36  ASN 36  45  45  ASN ASN B . n 
B 1 37  PHE 37  46  46  PHE PHE B . n 
B 1 38  MET 38  47  47  MET MET B . n 
B 1 39  CYS 39  48  48  CYS CYS B . n 
B 1 40  TYR 40  49  49  TYR TYR B . n 
B 1 41  ASP 41  50  50  ASP ASP B . n 
B 1 42  MET 42  51  51  MET MET B . n 
B 1 43  PRO 43  52  52  PRO PRO B . n 
B 1 44  LEU 44  53  53  LEU LEU B . n 
B 1 45  GLU 45  54  54  GLU GLU B . n 
B 1 46  ALA 46  55  55  ALA ALA B . n 
B 1 47  THR 47  56  56  THR THR B . n 
B 1 48  LEU 48  57  57  LEU LEU B . n 
B 1 49  ASN 49  58  58  ASN ASN B . n 
B 1 50  TYR 50  59  59  TYR TYR B . n 
B 1 51  ASN 51  60  60  ASN ASN B . n 
B 1 52  GLU 52  61  61  GLU GLU B . n 
B 1 53  LYS 53  62  62  LYS LYS B . n 
B 1 54  THR 54  63  63  THR THR B . n 
B 1 55  ASP 55  64  64  ASP ASP B . n 
B 1 56  SER 56  65  65  SER SER B . n 
B 1 57  TYR 57  66  66  TYR TYR B . n 
B 1 58  GLU 58  67  67  GLU GLU B . n 
B 1 59  GLY 59  68  68  GLY GLY B . n 
B 1 60  VAL 60  69  69  VAL VAL B . n 
B 1 61  ILE 61  70  70  ILE ILE B . n 
B 1 62  ASN 62  71  71  ASN ASN B . n 
B 1 63  TYR 63  72  72  TYR TYR B . n 
B 1 64  ASN 64  73  73  ASN ASN B . n 
B 1 65  LYS 65  74  74  LYS LYS B . n 
B 1 66  ASP 66  75  75  ASP ASP B . n 
B 1 67  PRO 67  76  76  PRO PRO B . n 
B 1 68  GLU 68  77  77  GLU GLU B . n 
B 1 69  TYR 69  78  78  TYR TYR B . n 
B 1 70  LEU 70  79  79  LEU LEU B . n 
B 1 71  ASN 71  80  80  ASN ASN B . n 
B 1 72  VAL 72  81  81  VAL VAL B . n 
B 1 73  TRP 73  82  82  TRP TRP B . n 
B 1 74  GLU 74  83  83  GLU GLU B . n 
B 1 75  LEU 75  84  84  LEU LEU B . n 
B 1 76  GLN 76  85  85  GLN GLN B . n 
B 1 77  SER 77  86  86  SER SER B . n 
B 1 78  ILE 78  87  87  ILE ILE B . n 
B 1 79  LYS 79  88  88  LYS LYS B . n 
B 1 80  ILE 80  89  89  ILE ILE B . n 
B 1 81  ASN 81  90  90  ASN ASN B . n 
B 1 82  GLY 82  91  91  GLY GLY B . n 
B 1 83  LYS 83  92  92  LYS LYS B . n 
B 1 84  ASP 84  93  93  ASP ASP B . n 
B 1 85  GLU 85  94  94  GLU GLU B . n 
B 1 86  GLN 86  95  95  GLN GLN B . n 
B 1 87  LYS 87  96  96  LYS LYS B . n 
B 1 88  VAL 88  97  97  VAL VAL B . n 
B 1 89  LEU 89  98  98  LEU LEU B . n 
B 1 90  ASN 90  99  99  ASN ASN B . n 
B 1 91  LYS 91  100 100 LYS LYS B . n 
B 1 92  GLU 92  101 101 GLU GLU B . n 
B 1 93  ASP 93  102 102 ASP ASP B . n 
B 1 94  LEU 94  103 103 LEU LEU B . n 
B 1 95  GLU 95  104 104 GLU GLU B . n 
B 1 96  SER 96  105 105 SER SER B . n 
B 1 97  MET 97  106 106 MET MET B . n 
B 1 98  GLY 98  107 107 GLY GLY B . n 
B 1 99  LEU 99  108 108 LEU LEU B . n 
B 1 100 ASN 100 109 109 ASN ASN B . n 
B 1 101 LEU 101 110 110 LEU LEU B . n 
B 1 102 LYS 102 111 111 LYS LYS B . n 
B 1 103 ASP 103 112 112 ASP ASP B . n 
B 1 104 TYR 104 113 113 TYR TYR B . n 
B 1 105 ASP 105 114 114 ASP ASP B . n 
B 1 106 VAL 106 115 115 VAL VAL B . n 
B 1 107 THR 107 116 116 THR THR B . n 
B 1 108 GLN 108 117 117 GLN GLN B . n 
B 1 109 GLU 109 118 118 GLU GLU B . n 
B 1 110 PHE 110 119 119 PHE PHE B . n 
B 1 111 ILE 111 120 120 ILE ILE B . n 
B 1 112 ILE 112 121 121 ILE ILE B . n 
B 1 113 SER 113 122 122 SER SER B . n 
B 1 114 ASP 114 123 123 ASP ASP B . n 
B 1 115 ALA 115 124 124 ALA ALA B . n 
B 1 116 ASN 116 125 125 ASN ASN B . n 
B 1 117 SER 117 126 126 SER SER B . n 
B 1 118 THR 118 127 127 THR THR B . n 
B 1 119 LYS 119 128 128 LYS LYS B . n 
B 1 120 ALA 120 129 129 ALA ALA B . n 
B 1 121 VAL 121 130 130 VAL VAL B . n 
B 1 122 ASN 122 131 131 ASN ASN B . n 
B 1 123 GLU 123 132 132 GLU GLU B . n 
B 1 124 TYR 124 133 133 TYR TYR B . n 
B 1 125 MET 125 134 134 MET MET B . n 
B 1 126 ARG 126 135 135 ARG ARG B . n 
B 1 127 LYS 127 136 136 LYS LYS B . n 
B 1 128 THR 128 137 137 THR THR B . n 
B 1 129 SER 129 138 138 SER SER B . n 
B 1 130 ALA 130 139 139 ALA ALA B . n 
B 1 131 PRO 131 140 140 PRO PRO B . n 
B 1 132 VAL 132 141 141 VAL VAL B . n 
B 1 133 LYS 133 142 142 LYS LYS B . n 
B 1 134 LYS 134 143 143 LYS LYS B . n 
B 1 135 LEU 135 144 144 LEU LEU B . n 
B 1 136 ALA 136 145 145 ALA ALA B . n 
B 1 137 GLY 137 146 146 GLY GLY B . n 
B 1 138 ALA 138 147 147 ALA ALA B . n 
B 1 139 THR 139 148 148 THR THR B . n 
B 1 140 ARG 140 149 149 ARG ARG B . n 
B 1 141 PHE 141 150 150 PHE PHE B . n 
B 1 142 GLU 142 151 151 GLU GLU B . n 
B 1 143 THR 143 152 152 THR THR B . n 
B 1 144 ALA 144 153 153 ALA ALA B . n 
B 1 145 VAL 145 154 154 VAL VAL B . n 
B 1 146 GLU 146 155 155 GLU GLU B . n 
B 1 147 ILE 147 156 156 ILE ILE B . n 
B 1 148 SER 148 157 157 SER SER B . n 
B 1 149 LYS 149 158 158 LYS LYS B . n 
B 1 150 GLN 150 159 159 GLN GLN B . n 
B 1 151 GLY 151 160 160 GLY GLY B . n 
B 1 152 TRP 152 161 161 TRP TRP B . n 
B 1 153 LYS 153 162 162 LYS LYS B . n 
B 1 154 ASP 154 163 163 ASP ASP B . n 
B 1 155 GLY 155 164 164 GLY GLY B . n 
B 1 156 SER 156 165 165 SER SER B . n 
B 1 157 SER 157 166 166 SER SER B . n 
B 1 158 LYS 158 167 167 LYS LYS B . n 
B 1 159 VAL 159 168 168 VAL VAL B . n 
B 1 160 VAL 160 169 169 VAL VAL B . n 
B 1 161 ILE 161 170 170 ILE ILE B . n 
B 1 162 VAL 162 171 171 VAL VAL B . n 
B 1 163 ASN 163 172 172 ASN ASN B . n 
B 1 164 GLY 164 173 173 GLY GLY B . n 
B 1 165 GLU 165 174 174 GLU GLU B . n 
B 1 166 LEU 166 175 175 LEU LEU B . n 
B 1 167 ALA 167 176 176 ALA ALA B . n 
B 1 168 ALA 168 177 177 ALA ALA B . n 
B 1 169 ASP 169 178 178 ASP ASP B . n 
B 1 170 GLY 170 179 179 GLY GLY B . n 
B 1 171 ILE 171 180 180 ILE ILE B . n 
B 1 172 THR 172 181 181 THR THR B . n 
B 1 173 ALA 173 182 182 ALA ALA B . n 
B 1 174 THR 174 183 183 THR THR B . n 
B 1 175 PRO 175 184 184 PRO PRO B . n 
B 1 176 LEU 176 185 185 LEU LEU B . n 
B 1 177 ALA 177 186 186 ALA ALA B . n 
B 1 178 SER 178 187 187 SER SER B . n 
B 1 179 THR 179 188 188 THR THR B . n 
B 1 180 TYR 180 189 189 TYR TYR B . n 
B 1 181 ASP 181 190 190 ASP ASP B . n 
B 1 182 ALA 182 191 191 ALA ALA B . n 
B 1 183 PRO 183 192 192 PRO PRO B . n 
B 1 184 ILE 184 193 193 ILE ILE B . n 
B 1 185 LEU 185 194 194 LEU LEU B . n 
B 1 186 LEU 186 195 195 LEU LEU B . n 
B 1 187 ALA 187 196 196 ALA ALA B . n 
B 1 188 ASN 188 197 197 ASN ASN B . n 
B 1 189 LYS 189 198 198 LYS LYS B . n 
B 1 190 ASP 190 199 199 ASP ASP B . n 
B 1 191 ASP 191 200 200 ASP ASP B . n 
B 1 192 ILE 192 201 201 ILE ILE B . n 
B 1 193 PRO 193 202 202 PRO PRO B . n 
B 1 194 GLU 194 203 203 GLU GLU B . n 
B 1 195 SER 195 204 204 SER SER B . n 
B 1 196 THR 196 205 205 THR THR B . n 
B 1 197 LYS 197 206 206 LYS LYS B . n 
B 1 198 ALA 198 207 207 ALA ALA B . n 
B 1 199 GLU 199 208 208 GLU GLU B . n 
B 1 200 LEU 200 209 209 LEU LEU B . n 
B 1 201 LYS 201 210 210 LYS LYS B . n 
B 1 202 ARG 202 211 211 ARG ARG B . n 
B 1 203 LEU 203 212 212 LEU LEU B . n 
B 1 204 ASN 204 213 213 ASN ASN B . n 
B 1 205 PRO 205 214 214 PRO PRO B . n 
B 1 206 SER 206 215 215 SER SER B . n 
B 1 207 ASP 207 216 216 ASP ASP B . n 
B 1 208 VAL 208 217 217 VAL VAL B . n 
B 1 209 ILE 209 218 218 ILE ILE B . n 
B 1 210 ILE 210 219 219 ILE ILE B . n 
B 1 211 ILE 211 220 220 ILE ILE B . n 
B 1 212 GLY 212 221 221 GLY GLY B . n 
B 1 213 ASP 213 222 222 ASP ASP B . n 
B 1 214 ASP 214 223 223 ASP ASP B . n 
B 1 215 GLY 215 224 224 GLY GLY B . n 
B 1 216 SER 216 225 225 SER SER B . n 
B 1 217 VAL 217 226 226 VAL VAL B . n 
B 1 218 SER 218 227 227 SER SER B . n 
B 1 219 GLN 219 228 228 GLN GLN B . n 
B 1 220 LYS 220 229 229 LYS LYS B . n 
B 1 221 ALA 221 230 230 ALA ALA B . n 
B 1 222 VAL 222 231 231 VAL VAL B . n 
B 1 223 SER 223 232 232 SER SER B . n 
B 1 224 GLN 224 233 233 GLN GLN B . n 
B 1 225 ILE 225 234 234 ILE ILE B . n 
B 1 226 LYS 226 235 235 LYS LYS B . n 
B 1 227 SER 227 236 236 SER SER B . n 
B 1 228 ALA 228 237 237 ALA ALA B . n 
B 1 229 VAL 229 238 238 VAL VAL B . n 
B 1 230 ASN 230 239 239 ASN ASN B . n 
B 1 231 VAL 231 240 240 VAL VAL B . n 
B 1 232 ASN 232 241 241 ASN ASN B . n 
B 1 233 VAL 233 242 242 VAL VAL B . n 
B 1 234 THR 234 243 243 THR THR B . n 
B 1 235 ARG 235 244 244 ARG ARG B . n 
B 1 236 ILE 236 245 245 ILE ILE B . n 
B 1 237 GLY 237 246 246 GLY GLY B . n 
B 1 238 GLY 238 247 247 GLY GLY B . n 
B 1 239 VAL 239 248 248 VAL VAL B . n 
B 1 240 ASP 240 249 249 ASP ASP B . n 
B 1 241 ARG 241 250 250 ARG ARG B . n 
B 1 242 HIS 242 251 251 HIS HIS B . n 
B 1 243 GLU 243 252 252 GLU GLU B . n 
B 1 244 THR 244 253 253 THR THR B . n 
B 1 245 SER 245 254 254 SER SER B . n 
B 1 246 LEU 246 255 255 LEU LEU B . n 
B 1 247 LEU 247 256 256 LEU LEU B . n 
B 1 248 ILE 248 257 257 ILE ILE B . n 
B 1 249 ALA 249 258 258 ALA ALA B . n 
B 1 250 LYS 250 259 259 LYS LYS B . n 
B 1 251 GLU 251 260 260 GLU GLU B . n 
B 1 252 ILE 252 261 261 ILE ILE B . n 
B 1 253 ASP 253 262 262 ASP ASP B . n 
B 1 254 LYS 254 263 263 LYS LYS B . n 
B 1 255 TYR 255 264 264 TYR TYR B . n 
B 1 256 HIS 256 265 265 HIS HIS B . n 
B 1 257 ASP 257 266 266 ASP ASP B . n 
B 1 258 VAL 258 267 267 VAL VAL B . n 
B 1 259 ASN 259 268 268 ASN ASN B . n 
B 1 260 LYS 260 269 269 LYS LYS B . n 
B 1 261 ILE 261 270 270 ILE ILE B . n 
B 1 262 TYR 262 271 271 TYR TYR B . n 
B 1 263 ILE 263 272 272 ILE ILE B . n 
B 1 264 ALA 264 273 273 ALA ALA B . n 
B 1 265 ASN 265 274 274 ASN ASN B . n 
B 1 266 GLY 266 275 275 GLY GLY B . n 
B 1 267 TYR 267 276 276 TYR TYR B . n 
B 1 268 ALA 268 277 277 ALA ALA B . n 
B 1 269 GLY 269 278 278 GLY GLY B . n 
B 1 270 GLU 270 279 279 GLU GLU B . n 
B 1 271 TYR 271 280 280 TYR TYR B . n 
B 1 272 ASP 272 281 281 ASP ASP B . n 
B 1 273 ALA 273 282 282 ALA ALA B . n 
B 1 274 LEU 274 283 283 LEU LEU B . n 
B 1 275 ASN 275 284 284 ASN ASN B . n 
B 1 276 ILE 276 285 285 ILE ILE B . n 
B 1 277 SER 277 286 286 SER SER B . n 
B 1 278 SER 278 287 287 SER SER B . n 
B 1 279 LYS 279 288 288 LYS LYS B . n 
B 1 280 ALA 280 289 289 ALA ALA B . n 
B 1 281 GLY 281 290 290 GLY GLY B . n 
B 1 282 GLU 282 291 291 GLU GLU B . n 
B 1 283 ASP 283 292 292 ASP ASP B . n 
B 1 284 GLN 284 293 293 GLN GLN B . n 
B 1 285 GLN 285 294 294 GLN GLN B . n 
B 1 286 PRO 286 295 295 PRO PRO B . n 
B 1 287 ILE 287 296 296 ILE ILE B . n 
B 1 288 ILE 288 297 297 ILE ILE B . n 
B 1 289 LEU 289 298 298 LEU LEU B . n 
B 1 290 ALA 290 299 299 ALA ALA B . n 
B 1 291 ASN 291 300 300 ASN ASN B . n 
B 1 292 LYS 292 301 301 LYS LYS B . n 
B 1 293 ASP 293 302 302 ASP ASP B . n 
B 1 294 SER 294 303 303 SER SER B . n 
B 1 295 VAL 295 304 304 VAL VAL B . n 
B 1 296 PRO 296 305 305 PRO PRO B . n 
B 1 297 GLN 297 306 306 GLN GLN B . n 
B 1 298 GLY 298 307 307 GLY GLY B . n 
B 1 299 THR 299 308 308 THR THR B . n 
B 1 300 TYR 300 309 309 TYR TYR B . n 
B 1 301 ASN 301 310 310 ASN ASN B . n 
B 1 302 TRP 302 311 311 TRP TRP B . n 
B 1 303 LEU 303 312 312 LEU LEU B . n 
B 1 304 SER 304 313 313 SER SER B . n 
B 1 305 SER 305 314 314 SER SER B . n 
B 1 306 GLN 306 315 315 GLN GLN B . n 
B 1 307 GLY 307 316 316 GLY GLY B . n 
B 1 308 LEU 308 317 317 LEU LEU B . n 
B 1 309 GLU 309 318 318 GLU GLU B . n 
B 1 310 GLU 310 319 319 GLU GLU B . n 
B 1 311 ALA 311 320 320 ALA ALA B . n 
B 1 312 TYR 312 321 321 TYR TYR B . n 
B 1 313 TYR 313 322 322 TYR TYR B . n 
B 1 314 ILE 314 323 323 ILE ILE B . n 
B 1 315 GLY 315 324 324 GLY GLY B . n 
B 1 316 GLY 316 325 325 GLY GLY B . n 
B 1 317 SER 317 326 326 SER SER B . n 
B 1 318 GLN 318 327 327 GLN GLN B . n 
B 1 319 SER 319 328 328 SER SER B . n 
B 1 320 LEU 320 329 329 LEU LEU B . n 
B 1 321 SER 321 330 330 SER SER B . n 
B 1 322 SER 322 331 331 SER SER B . n 
B 1 323 LYS 323 332 332 LYS LYS B . n 
B 1 324 ILE 324 333 333 ILE ILE B . n 
B 1 325 ILE 325 334 334 ILE ILE B . n 
B 1 326 ASP 326 335 335 ASP ASP B . n 
B 1 327 GLN 327 336 336 GLN GLN B . n 
B 1 328 ILE 328 337 337 ILE ILE B . n 
B 1 329 SER 329 338 338 SER SER B . n 
B 1 330 LYS 330 339 339 LYS LYS B . n 
B 1 331 ILE 331 340 340 ILE ILE B . n 
B 1 332 ALA 332 341 341 ALA ALA B . n 
B 1 333 LYS 333 342 342 LYS LYS B . n 
B 1 334 ASN 334 343 343 ASN ASN B . n 
B 1 335 GLY 335 344 344 GLY GLY B . n 
B 1 336 THR 336 345 345 THR THR B . n 
B 1 337 SER 337 346 346 SER SER B . n 
B 1 338 LYS 338 347 347 LYS LYS B . n 
B 1 339 ASN 339 348 348 ASN ASN B . n 
B 1 340 ARG 340 349 349 ARG ARG B . n 
B 1 341 VAL 341 350 350 VAL VAL B . n 
B 1 342 SER 342 351 351 SER SER B . n 
B 1 343 GLY 343 352 352 GLY GLY B . n 
B 1 344 ALA 344 353 353 ALA ALA B . n 
B 1 345 ASP 345 354 354 ASP ASP B . n 
B 1 346 ARG 346 355 355 ARG ARG B . n 
B 1 347 HIS 347 356 356 HIS HIS B . n 
B 1 348 GLU 348 357 357 GLU GLU B . n 
B 1 349 THR 349 358 358 THR THR B . n 
B 1 350 ASN 350 359 359 ASN ASN B . n 
B 1 351 ALA 351 360 360 ALA ALA B . n 
B 1 352 ASN 352 361 361 ASN ASN B . n 
B 1 353 VAL 353 362 362 VAL VAL B . n 
B 1 354 ILE 354 363 363 ILE ILE B . n 
B 1 355 LYS 355 364 364 LYS LYS B . n 
B 1 356 THR 356 365 365 THR THR B . n 
B 1 357 PHE 357 366 366 PHE PHE B . n 
B 1 358 TYR 358 367 367 TYR TYR B . n 
B 1 359 PRO 359 368 368 PRO PRO B . n 
B 1 360 ASP 360 369 369 ASP ASP B . n 
B 1 361 LYS 361 370 370 LYS LYS B . n 
B 1 362 GLU 362 371 371 GLU GLU B . n 
B 1 363 LEU 363 372 372 LEU LEU B . n 
B 1 364 SER 364 373 373 SER SER B . n 
B 1 365 ALA 365 374 374 ALA ALA B . n 
B 1 366 MET 366 375 375 MET MET B . n 
B 1 367 LEU 367 376 376 LEU LEU B . n 
B 1 368 VAL 368 377 377 VAL VAL B . n 
B 1 369 ALA 369 378 378 ALA ALA B . n 
B 1 370 LYS 370 379 379 LYS LYS B . n 
B 1 371 SER 371 380 380 SER SER B . n 
B 1 372 ASP 372 381 381 ASP ASP B . n 
B 1 373 ILE 373 382 382 ILE ILE B . n 
B 1 374 ILE 374 383 383 ILE ILE B . n 
B 1 375 VAL 375 384 384 VAL VAL B . n 
B 1 376 ASP 376 385 385 ASP ASP B . n 
B 1 377 SER 377 386 386 SER SER B . n 
B 1 378 ILE 378 387 387 ILE ILE B . n 
B 1 379 THR 379 388 388 THR THR B . n 
B 1 380 ALA 380 389 389 ALA ALA B . n 
B 1 381 GLY 381 390 390 GLY GLY B . n 
B 1 382 PRO 382 391 391 PRO PRO B . n 
B 1 383 LEU 383 392 392 LEU LEU B . n 
B 1 384 ALA 384 393 393 ALA ALA B . n 
B 1 385 ALA 385 394 394 ALA ALA B . n 
B 1 386 LYS 386 395 395 LYS LYS B . n 
B 1 387 LEU 387 396 396 LEU LEU B . n 
B 1 388 LYS 388 397 397 LYS LYS B . n 
B 1 389 ALA 389 398 398 ALA ALA B . n 
B 1 390 PRO 390 399 399 PRO PRO B . n 
B 1 391 ILE 391 400 400 ILE ILE B . n 
B 1 392 LEU 392 401 401 LEU LEU B . n 
B 1 393 ILE 393 402 402 ILE ILE B . n 
B 1 394 THR 394 403 403 THR THR B . n 
B 1 395 PRO 395 404 404 PRO PRO B . n 
B 1 396 LYS 396 405 405 LYS LYS B . n 
B 1 397 THR 397 406 406 THR THR B . n 
B 1 398 TYR 398 407 407 TYR TYR B . n 
B 1 399 VAL 399 408 408 VAL VAL B . n 
B 1 400 SER 400 409 409 SER SER B . n 
B 1 401 ALA 401 410 410 ALA ALA B . n 
B 1 402 TYR 402 411 411 TYR TYR B . n 
B 1 403 HIS 403 412 412 HIS HIS B . n 
B 1 404 SER 404 413 413 SER SER B . n 
B 1 405 THR 405 414 414 THR THR B . n 
B 1 406 ASN 406 415 415 ASN ASN B . n 
B 1 407 LEU 407 416 416 LEU LEU B . n 
B 1 408 SER 408 417 417 SER SER B . n 
B 1 409 GLU 409 418 418 GLU GLU B . n 
B 1 410 LYS 410 419 419 LYS LYS B . n 
B 1 411 THR 411 420 420 THR THR B . n 
B 1 412 ALA 412 421 421 ALA ALA B . n 
B 1 413 GLU 413 422 422 GLU GLU B . n 
B 1 414 THR 414 423 423 THR THR B . n 
B 1 415 VAL 415 424 424 VAL VAL B . n 
B 1 416 TYR 416 425 425 TYR TYR B . n 
B 1 417 GLN 417 426 426 GLN GLN B . n 
B 1 418 ILE 418 427 427 ILE ILE B . n 
B 1 419 GLY 419 428 428 GLY GLY B . n 
B 1 420 ASP 420 429 429 ASP ASP B . n 
B 1 421 GLY 421 430 430 GLY GLY B . n 
B 1 422 MET 422 431 431 MET MET B . n 
B 1 423 LYS 423 432 432 LYS LYS B . n 
B 1 424 ASP 424 433 433 ASP ASP B . n 
B 1 425 SER 425 434 434 SER SER B . n 
B 1 426 VAL 426 435 435 VAL VAL B . n 
B 1 427 ILE 427 436 436 ILE ILE B . n 
B 1 428 ASN 428 437 437 ASN ASN B . n 
B 1 429 SER 429 438 438 SER SER B . n 
B 1 430 ILE 430 439 439 ILE ILE B . n 
B 1 431 ALA 431 440 440 ALA ALA B . n 
B 1 432 SER 432 441 441 SER SER B . n 
B 1 433 SER 433 442 442 SER SER B . n 
B 1 434 LEU 434 443 443 LEU LEU B . n 
B 1 435 SER 435 444 444 SER SER B . n 
B 1 436 LYS 436 445 445 LYS LYS B . n 
B 1 437 HIS 437 446 446 HIS HIS B . n 
B 1 438 ASN 438 447 447 ASN ASN B . n 
B 1 439 ALA 439 448 448 ALA ALA B . n 
B 1 440 PRO 440 449 449 PRO PRO B . n 
B 1 441 THR 441 450 450 THR THR B . n 
B 1 442 GLU 442 451 451 GLU GLU B . n 
B 1 443 PRO 443 452 452 PRO PRO B . n 
B 1 444 ASP 444 453 453 ASP ASP B . n 
B 1 445 ASN 445 454 454 ASN ASN B . n 
B 1 446 SER 446 455 455 SER SER B . n 
B 1 447 GLY 447 456 456 GLY GLY B . n 
B 1 448 SER 448 457 457 SER SER B . n 
B 1 449 ALA 449 458 458 ALA ALA B . n 
B 1 450 ALA 450 459 459 ALA ALA B . n 
B 1 451 GLY 451 460 460 GLY GLY B . n 
B 1 452 LYS 452 461 461 LYS LYS B . n 
B 1 453 THR 453 462 462 THR THR B . n 
B 1 454 VAL 454 463 463 VAL VAL B . n 
B 1 455 VAL 455 464 464 VAL VAL B . n 
B 1 456 ILE 456 465 465 ILE ILE B . n 
B 1 457 ASP 457 466 466 ASP ASP B . n 
B 1 458 PRO 458 467 467 PRO PRO B . n 
B 1 459 GLY 459 468 468 GLY GLY B . n 
B 1 460 HIS 460 469 469 HIS HIS B . n 
B 1 461 GLY 461 470 470 GLY GLY B . n 
B 1 462 GLY 462 471 471 GLY GLY B . n 
B 1 463 SER 463 472 472 SER SER B . n 
B 1 464 ASP 464 473 473 ASP ASP B . n 
B 1 465 SER 465 474 474 SER SER B . n 
B 1 466 GLY 466 475 475 GLY GLY B . n 
B 1 467 ALA 467 476 476 ALA ALA B . n 
B 1 468 THR 468 477 477 THR THR B . n 
B 1 469 SER 469 478 478 SER SER B . n 
B 1 470 GLY 470 479 479 GLY GLY B . n 
B 1 471 LEU 471 480 480 LEU LEU B . n 
B 1 472 ASN 472 481 481 ASN ASN B . n 
B 1 473 GLY 473 482 482 GLY GLY B . n 
B 1 474 GLY 474 483 483 GLY GLY B . n 
B 1 475 ALA 475 484 484 ALA ALA B . n 
B 1 476 GLN 476 485 485 GLN GLN B . n 
B 1 477 GLU 477 486 486 GLU GLU B . n 
B 1 478 LYS 478 487 487 LYS LYS B . n 
B 1 479 LYS 479 488 488 LYS LYS B . n 
B 1 480 TYR 480 489 489 TYR TYR B . n 
B 1 481 THR 481 490 490 THR THR B . n 
B 1 482 LEU 482 491 491 LEU LEU B . n 
B 1 483 ASN 483 492 492 ASN ASN B . n 
B 1 484 THR 484 493 493 THR THR B . n 
B 1 485 ALA 485 494 494 ALA ALA B . n 
B 1 486 LEU 486 495 495 LEU LEU B . n 
B 1 487 ALA 487 496 496 ALA ALA B . n 
B 1 488 THR 488 497 497 THR THR B . n 
B 1 489 THR 489 498 498 THR THR B . n 
B 1 490 GLU 490 499 499 GLU GLU B . n 
B 1 491 TYR 491 500 500 TYR TYR B . n 
B 1 492 LEU 492 501 501 LEU LEU B . n 
B 1 493 ARG 493 502 502 ARG ARG B . n 
B 1 494 SER 494 503 503 SER SER B . n 
B 1 495 LYS 495 504 504 LYS LYS B . n 
B 1 496 GLY 496 505 505 GLY GLY B . n 
B 1 497 ILE 497 506 506 ILE ILE B . n 
B 1 498 ASN 498 507 507 ASN ASN B . n 
B 1 499 VAL 499 508 508 VAL VAL B . n 
B 1 500 VAL 500 509 509 VAL VAL B . n 
B 1 501 MET 501 510 510 MET MET B . n 
B 1 502 THR 502 511 511 THR THR B . n 
B 1 503 ARG 503 512 512 ARG ARG B . n 
B 1 504 ASP 504 513 513 ASP ASP B . n 
B 1 505 THR 505 514 514 THR THR B . n 
B 1 506 ASP 506 515 515 ASP ASP B . n 
B 1 507 LYS 507 516 516 LYS LYS B . n 
B 1 508 THR 508 517 517 THR THR B . n 
B 1 509 MET 509 518 518 MET MET B . n 
B 1 510 ALA 510 519 519 ALA ALA B . n 
B 1 511 LEU 511 520 520 LEU LEU B . n 
B 1 512 GLY 512 521 521 GLY GLY B . n 
B 1 513 GLU 513 522 522 GLU GLU B . n 
B 1 514 ARG 514 523 523 ARG ARG B . n 
B 1 515 THR 515 524 524 THR THR B . n 
B 1 516 ALA 516 525 525 ALA ALA B . n 
B 1 517 LEU 517 526 526 LEU LEU B . n 
B 1 518 SER 518 527 527 SER SER B . n 
B 1 519 ASN 519 528 528 ASN ASN B . n 
B 1 520 THR 520 529 529 THR THR B . n 
B 1 521 ILE 521 530 530 ILE ILE B . n 
B 1 522 LYS 522 531 531 LYS LYS B . n 
B 1 523 PRO 523 532 532 PRO PRO B . n 
B 1 524 ASP 524 533 533 ASP ASP B . n 
B 1 525 LEU 525 534 534 LEU LEU B . n 
B 1 526 PHE 526 535 535 PHE PHE B . n 
B 1 527 THR 527 536 536 THR THR B . n 
B 1 528 SER 528 537 537 SER SER B . n 
B 1 529 ILE 529 538 538 ILE ILE B . n 
B 1 530 HIS 530 539 539 HIS HIS B . n 
B 1 531 TYR 531 540 540 TYR TYR B . n 
B 1 532 ASN 532 541 541 ASN ASN B . n 
B 1 533 ALA 533 542 542 ALA ALA B . n 
B 1 534 SER 534 543 543 SER SER B . n 
B 1 535 ASN 535 544 544 ASN ASN B . n 
B 1 536 GLY 536 545 545 GLY GLY B . n 
B 1 537 SER 537 546 546 SER SER B . n 
B 1 538 GLY 538 547 547 GLY GLY B . n 
B 1 539 ASN 539 548 548 ASN ASN B . n 
B 1 540 GLY 540 549 549 GLY GLY B . n 
B 1 541 VAL 541 550 550 VAL VAL B . n 
B 1 542 GLU 542 551 551 GLU GLU B . n 
B 1 543 ILE 543 552 552 ILE ILE B . n 
B 1 544 TYR 544 553 553 TYR TYR B . n 
B 1 545 TYR 545 554 554 TYR TYR B . n 
B 1 546 LYS 546 555 555 LYS LYS B . n 
B 1 547 VAL 547 556 556 VAL VAL B . n 
B 1 548 LYS 548 557 557 LYS LYS B . n 
B 1 549 ASP 549 558 558 ASP ASP B . n 
B 1 550 LYS 550 559 559 LYS LYS B . n 
B 1 551 ASN 551 560 560 ASN ASN B . n 
B 1 552 GLY 552 561 561 GLY GLY B . n 
B 1 553 GLY 553 562 562 GLY GLY B . n 
B 1 554 THR 554 563 563 THR THR B . n 
B 1 555 THR 555 564 564 THR THR B . n 
B 1 556 LYS 556 565 565 LYS LYS B . n 
B 1 557 THR 557 566 566 THR THR B . n 
B 1 558 ALA 558 567 567 ALA ALA B . n 
B 1 559 ALA 559 568 568 ALA ALA B . n 
B 1 560 SER 560 569 569 SER SER B . n 
B 1 561 ASN 561 570 570 ASN ASN B . n 
B 1 562 ILE 562 571 571 ILE ILE B . n 
B 1 563 LEU 563 572 572 LEU LEU B . n 
B 1 564 LYS 564 573 573 LYS LYS B . n 
B 1 565 ARG 565 574 574 ARG ARG B . n 
B 1 566 ILE 566 575 575 ILE ILE B . n 
B 1 567 LEU 567 576 576 LEU LEU B . n 
B 1 568 GLU 568 577 577 GLU GLU B . n 
B 1 569 LYS 569 578 578 LYS LYS B . n 
B 1 570 PHE 570 579 579 PHE PHE B . n 
B 1 571 ASN 571 580 580 ASN ASN B . n 
B 1 572 MET 572 581 581 MET MET B . n 
B 1 573 LYS 573 582 582 LYS LYS B . n 
B 1 574 ASN 574 583 583 ASN ASN B . n 
B 1 575 ARG 575 584 584 ARG ARG B . n 
B 1 576 GLY 576 585 585 GLY GLY B . n 
B 1 577 ILE 577 586 586 ILE ILE B . n 
B 1 578 LYS 578 587 587 LYS LYS B . n 
B 1 579 THR 579 588 588 THR THR B . n 
B 1 580 ARG 580 589 589 ARG ARG B . n 
B 1 581 THR 581 590 590 THR THR B . n 
B 1 582 LEU 582 591 591 LEU LEU B . n 
B 1 583 ASP 583 592 592 ASP ASP B . n 
B 1 584 ASN 584 593 593 ASN ASN B . n 
B 1 585 GLY 585 594 594 GLY GLY B . n 
B 1 586 LYS 586 595 595 LYS LYS B . n 
B 1 587 ASP 587 596 596 ASP ASP B . n 
B 1 588 TYR 588 597 597 TYR TYR B . n 
B 1 589 LEU 589 598 598 LEU LEU B . n 
B 1 590 TYR 590 599 599 TYR TYR B . n 
B 1 591 VAL 591 600 600 VAL VAL B . n 
B 1 592 LEU 592 601 601 LEU LEU B . n 
B 1 593 ARG 593 602 602 ARG ARG B . n 
B 1 594 ASN 594 603 603 ASN ASN B . n 
B 1 595 ASN 595 604 604 ASN ASN B . n 
B 1 596 ASN 596 605 605 ASN ASN B . n 
B 1 597 TYR 597 606 606 TYR TYR B . n 
B 1 598 PRO 598 607 607 PRO PRO B . n 
B 1 599 ALA 599 608 608 ALA ALA B . n 
B 1 600 ILE 600 609 609 ILE ILE B . n 
B 1 601 LEU 601 610 610 LEU LEU B . n 
B 1 602 VAL 602 611 611 VAL VAL B . n 
B 1 603 GLU 603 612 612 GLU GLU B . n 
B 1 604 CYS 604 613 613 CYS CYS B . n 
B 1 605 ALA 605 614 614 ALA ALA B . n 
B 1 606 PHE 606 615 615 PHE PHE B . n 
B 1 607 ILE 607 616 616 ILE ILE B . n 
B 1 608 ASP 608 617 617 ASP ASP B . n 
B 1 609 ASN 609 618 618 ASN ASN B . n 
B 1 610 LYS 610 619 619 LYS LYS B . n 
B 1 611 SER 611 620 620 SER SER B . n 
B 1 612 ASP 612 621 621 ASP ASP B . n 
B 1 613 MET 613 622 622 MET MET B . n 
B 1 614 ASP 614 623 623 ASP ASP B . n 
B 1 615 LYS 615 624 624 LYS LYS B . n 
B 1 616 LEU 616 625 625 LEU LEU B . n 
B 1 617 ASN 617 626 626 ASN ASN B . n 
B 1 618 THR 618 627 627 THR THR B . n 
B 1 619 ALA 619 628 628 ALA ALA B . n 
B 1 620 GLU 620 629 629 GLU GLU B . n 
B 1 621 LYS 621 630 630 LYS LYS B . n 
B 1 622 VAL 622 631 631 VAL VAL B . n 
B 1 623 LYS 623 632 632 LYS LYS B . n 
B 1 624 THR 624 633 633 THR THR B . n 
B 1 625 MET 625 634 634 MET MET B . n 
B 1 626 GLY 626 635 635 GLY GLY B . n 
B 1 627 THR 627 636 636 THR THR B . n 
B 1 628 GLN 628 637 637 GLN GLN B . n 
B 1 629 ILE 629 638 638 ILE ILE B . n 
B 1 630 GLY 630 639 639 GLY GLY B . n 
B 1 631 ILE 631 640 640 ILE ILE B . n 
B 1 632 GLY 632 641 641 GLY GLY B . n 
B 1 633 ILE 633 642 642 ILE ILE B . n 
B 1 634 GLU 634 643 643 GLU GLU B . n 
B 1 635 ASP 635 644 644 ASP ASP B . n 
B 1 636 THR 636 645 645 THR THR B . n 
B 1 637 VAL 637 646 646 VAL VAL B . n 
B 1 638 LYS 638 647 647 LYS LYS B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 CA  1   701  650  CA  CA  A . 
D 2 CA  1   702  991  CA  CA  A . 
E 3 NA  1   703  995  NA  NA  A . 
F 4 CL  1   704  998  CL  CL  A . 
G 4 CL  1   705  1000 CL  CL  A . 
H 4 CL  1   706  1002 CL  CL  A . 
I 5 ZN  1   707  649  ZN  ZN  A . 
J 2 CA  1   701  992  CA  CA  B . 
K 2 CA  1   702  993  CA  CA  B . 
L 2 CA  1   703  994  CA  CA  B . 
M 3 NA  1   704  996  NA  NA  B . 
N 3 NA  1   705  997  NA  NA  B . 
O 4 CL  1   706  999  CL  CL  B . 
P 4 CL  1   707  1001 CL  CL  B . 
Q 6 CIT 1   708  1003 CIT CIT B . 
R 6 CIT 1   709  1004 CIT CIT B . 
S 5 ZN  1   710  649  ZN  ZN  B . 
T 7 HOH 1   801  1094 HOH HOH A . 
T 7 HOH 2   802  283  HOH HOH A . 
T 7 HOH 3   803  920  HOH HOH A . 
T 7 HOH 4   804  1080 HOH HOH A . 
T 7 HOH 5   805  1091 HOH HOH A . 
T 7 HOH 6   806  909  HOH HOH A . 
T 7 HOH 7   807  484  HOH HOH A . 
T 7 HOH 8   808  98   HOH HOH A . 
T 7 HOH 9   809  1316 HOH HOH A . 
T 7 HOH 10  810  213  HOH HOH A . 
T 7 HOH 11  811  308  HOH HOH A . 
T 7 HOH 12  812  337  HOH HOH A . 
T 7 HOH 13  813  966  HOH HOH A . 
T 7 HOH 14  814  888  HOH HOH A . 
T 7 HOH 15  815  542  HOH HOH A . 
T 7 HOH 16  816  623  HOH HOH A . 
T 7 HOH 17  817  533  HOH HOH A . 
T 7 HOH 18  818  1115 HOH HOH A . 
T 7 HOH 19  819  14   HOH HOH A . 
T 7 HOH 20  820  876  HOH HOH A . 
T 7 HOH 21  821  1072 HOH HOH A . 
T 7 HOH 22  822  895  HOH HOH A . 
T 7 HOH 23  823  1082 HOH HOH A . 
T 7 HOH 24  824  870  HOH HOH A . 
T 7 HOH 25  825  893  HOH HOH A . 
T 7 HOH 26  826  899  HOH HOH A . 
T 7 HOH 27  827  1208 HOH HOH A . 
T 7 HOH 28  828  312  HOH HOH A . 
T 7 HOH 29  829  268  HOH HOH A . 
T 7 HOH 30  830  944  HOH HOH A . 
T 7 HOH 31  831  1105 HOH HOH A . 
T 7 HOH 32  832  858  HOH HOH A . 
T 7 HOH 33  833  447  HOH HOH A . 
T 7 HOH 34  834  1030 HOH HOH A . 
T 7 HOH 35  835  1291 HOH HOH A . 
T 7 HOH 36  836  653  HOH HOH A . 
T 7 HOH 37  837  117  HOH HOH A . 
T 7 HOH 38  838  159  HOH HOH A . 
T 7 HOH 39  839  430  HOH HOH A . 
T 7 HOH 40  840  1181 HOH HOH A . 
T 7 HOH 41  841  1078 HOH HOH A . 
T 7 HOH 42  842  933  HOH HOH A . 
T 7 HOH 43  843  392  HOH HOH A . 
T 7 HOH 44  844  420  HOH HOH A . 
T 7 HOH 45  845  1169 HOH HOH A . 
T 7 HOH 46  846  276  HOH HOH A . 
T 7 HOH 47  847  1152 HOH HOH A . 
T 7 HOH 48  848  316  HOH HOH A . 
T 7 HOH 49  849  326  HOH HOH A . 
T 7 HOH 50  850  161  HOH HOH A . 
T 7 HOH 51  851  516  HOH HOH A . 
T 7 HOH 52  852  112  HOH HOH A . 
T 7 HOH 53  853  1231 HOH HOH A . 
T 7 HOH 54  854  220  HOH HOH A . 
T 7 HOH 55  855  1312 HOH HOH A . 
T 7 HOH 56  856  251  HOH HOH A . 
T 7 HOH 57  857  134  HOH HOH A . 
T 7 HOH 58  858  446  HOH HOH A . 
T 7 HOH 59  859  505  HOH HOH A . 
T 7 HOH 60  860  239  HOH HOH A . 
T 7 HOH 61  861  294  HOH HOH A . 
T 7 HOH 62  862  125  HOH HOH A . 
T 7 HOH 63  863  221  HOH HOH A . 
T 7 HOH 64  864  344  HOH HOH A . 
T 7 HOH 65  865  246  HOH HOH A . 
T 7 HOH 66  866  930  HOH HOH A . 
T 7 HOH 67  867  297  HOH HOH A . 
T 7 HOH 68  868  96   HOH HOH A . 
T 7 HOH 69  869  927  HOH HOH A . 
T 7 HOH 70  870  209  HOH HOH A . 
T 7 HOH 71  871  331  HOH HOH A . 
T 7 HOH 72  872  429  HOH HOH A . 
T 7 HOH 73  873  260  HOH HOH A . 
T 7 HOH 74  874  170  HOH HOH A . 
T 7 HOH 75  875  580  HOH HOH A . 
T 7 HOH 76  876  39   HOH HOH A . 
T 7 HOH 77  877  215  HOH HOH A . 
T 7 HOH 78  878  228  HOH HOH A . 
T 7 HOH 79  879  459  HOH HOH A . 
T 7 HOH 80  880  290  HOH HOH A . 
T 7 HOH 81  881  1025 HOH HOH A . 
T 7 HOH 82  882  118  HOH HOH A . 
T 7 HOH 83  883  1199 HOH HOH A . 
T 7 HOH 84  884  137  HOH HOH A . 
T 7 HOH 85  885  218  HOH HOH A . 
T 7 HOH 86  886  56   HOH HOH A . 
T 7 HOH 87  887  55   HOH HOH A . 
T 7 HOH 88  888  278  HOH HOH A . 
T 7 HOH 89  889  229  HOH HOH A . 
T 7 HOH 90  890  271  HOH HOH A . 
T 7 HOH 91  891  1182 HOH HOH A . 
T 7 HOH 92  892  262  HOH HOH A . 
T 7 HOH 93  893  885  HOH HOH A . 
T 7 HOH 94  894  678  HOH HOH A . 
T 7 HOH 95  895  511  HOH HOH A . 
T 7 HOH 96  896  163  HOH HOH A . 
T 7 HOH 97  897  1189 HOH HOH A . 
T 7 HOH 98  898  970  HOH HOH A . 
T 7 HOH 99  899  211  HOH HOH A . 
T 7 HOH 100 900  851  HOH HOH A . 
T 7 HOH 101 901  663  HOH HOH A . 
T 7 HOH 102 902  183  HOH HOH A . 
T 7 HOH 103 903  563  HOH HOH A . 
T 7 HOH 104 904  910  HOH HOH A . 
T 7 HOH 105 905  255  HOH HOH A . 
T 7 HOH 106 906  174  HOH HOH A . 
T 7 HOH 107 907  449  HOH HOH A . 
T 7 HOH 108 908  515  HOH HOH A . 
T 7 HOH 109 909  1127 HOH HOH A . 
T 7 HOH 110 910  256  HOH HOH A . 
T 7 HOH 111 911  317  HOH HOH A . 
T 7 HOH 112 912  1280 HOH HOH A . 
T 7 HOH 113 913  329  HOH HOH A . 
T 7 HOH 114 914  856  HOH HOH A . 
T 7 HOH 115 915  303  HOH HOH A . 
T 7 HOH 116 916  405  HOH HOH A . 
T 7 HOH 117 917  1070 HOH HOH A . 
T 7 HOH 118 918  38   HOH HOH A . 
T 7 HOH 119 919  152  HOH HOH A . 
T 7 HOH 120 920  358  HOH HOH A . 
T 7 HOH 121 921  382  HOH HOH A . 
T 7 HOH 122 922  889  HOH HOH A . 
T 7 HOH 123 923  295  HOH HOH A . 
T 7 HOH 124 924  359  HOH HOH A . 
T 7 HOH 125 925  367  HOH HOH A . 
T 7 HOH 126 926  293  HOH HOH A . 
T 7 HOH 127 927  231  HOH HOH A . 
T 7 HOH 128 928  17   HOH HOH A . 
T 7 HOH 129 929  931  HOH HOH A . 
T 7 HOH 130 930  1296 HOH HOH A . 
T 7 HOH 131 931  1292 HOH HOH A . 
T 7 HOH 132 932  1137 HOH HOH A . 
T 7 HOH 133 933  64   HOH HOH A . 
T 7 HOH 134 934  545  HOH HOH A . 
T 7 HOH 135 935  53   HOH HOH A . 
T 7 HOH 136 936  581  HOH HOH A . 
T 7 HOH 137 937  365  HOH HOH A . 
T 7 HOH 138 938  44   HOH HOH A . 
T 7 HOH 139 939  350  HOH HOH A . 
T 7 HOH 140 940  177  HOH HOH A . 
T 7 HOH 141 941  1315 HOH HOH A . 
T 7 HOH 142 942  206  HOH HOH A . 
T 7 HOH 143 943  140  HOH HOH A . 
T 7 HOH 144 944  261  HOH HOH A . 
T 7 HOH 145 945  233  HOH HOH A . 
T 7 HOH 146 946  552  HOH HOH A . 
T 7 HOH 147 947  78   HOH HOH A . 
T 7 HOH 148 948  1324 HOH HOH A . 
T 7 HOH 149 949  1113 HOH HOH A . 
T 7 HOH 150 950  612  HOH HOH A . 
T 7 HOH 151 951  346  HOH HOH A . 
T 7 HOH 152 952  915  HOH HOH A . 
T 7 HOH 153 953  41   HOH HOH A . 
T 7 HOH 154 954  376  HOH HOH A . 
T 7 HOH 155 955  442  HOH HOH A . 
T 7 HOH 156 956  463  HOH HOH A . 
T 7 HOH 157 957  274  HOH HOH A . 
T 7 HOH 158 958  1215 HOH HOH A . 
T 7 HOH 159 959  306  HOH HOH A . 
T 7 HOH 160 960  238  HOH HOH A . 
T 7 HOH 161 961  219  HOH HOH A . 
T 7 HOH 162 962  860  HOH HOH A . 
T 7 HOH 163 963  1314 HOH HOH A . 
T 7 HOH 164 964  494  HOH HOH A . 
T 7 HOH 165 965  450  HOH HOH A . 
T 7 HOH 166 966  391  HOH HOH A . 
T 7 HOH 167 967  1065 HOH HOH A . 
T 7 HOH 168 968  176  HOH HOH A . 
T 7 HOH 169 969  642  HOH HOH A . 
T 7 HOH 170 970  291  HOH HOH A . 
T 7 HOH 171 971  263  HOH HOH A . 
T 7 HOH 172 972  124  HOH HOH A . 
T 7 HOH 173 973  149  HOH HOH A . 
T 7 HOH 174 974  214  HOH HOH A . 
T 7 HOH 175 975  19   HOH HOH A . 
T 7 HOH 176 976  1028 HOH HOH A . 
T 7 HOH 177 977  131  HOH HOH A . 
T 7 HOH 178 978  1069 HOH HOH A . 
T 7 HOH 179 979  257  HOH HOH A . 
T 7 HOH 180 980  448  HOH HOH A . 
T 7 HOH 181 981  9    HOH HOH A . 
T 7 HOH 182 982  428  HOH HOH A . 
T 7 HOH 183 983  252  HOH HOH A . 
T 7 HOH 184 984  156  HOH HOH A . 
T 7 HOH 185 985  677  HOH HOH A . 
T 7 HOH 186 986  996  HOH HOH A . 
T 7 HOH 187 987  1144 HOH HOH A . 
T 7 HOH 188 988  634  HOH HOH A . 
T 7 HOH 189 989  968  HOH HOH A . 
T 7 HOH 190 990  54   HOH HOH A . 
T 7 HOH 191 991  107  HOH HOH A . 
T 7 HOH 192 992  281  HOH HOH A . 
T 7 HOH 193 993  57   HOH HOH A . 
T 7 HOH 194 994  402  HOH HOH A . 
T 7 HOH 195 995  97   HOH HOH A . 
T 7 HOH 196 996  613  HOH HOH A . 
T 7 HOH 197 997  1287 HOH HOH A . 
T 7 HOH 198 998  456  HOH HOH A . 
T 7 HOH 199 999  1111 HOH HOH A . 
T 7 HOH 200 1000 406  HOH HOH A . 
T 7 HOH 201 1001 342  HOH HOH A . 
T 7 HOH 202 1002 370  HOH HOH A . 
T 7 HOH 203 1003 1138 HOH HOH A . 
T 7 HOH 204 1004 602  HOH HOH A . 
T 7 HOH 205 1005 26   HOH HOH A . 
T 7 HOH 206 1006 982  HOH HOH A . 
T 7 HOH 207 1007 1285 HOH HOH A . 
T 7 HOH 208 1008 168  HOH HOH A . 
T 7 HOH 209 1009 423  HOH HOH A . 
T 7 HOH 210 1010 61   HOH HOH A . 
T 7 HOH 211 1011 1109 HOH HOH A . 
T 7 HOH 212 1012 190  HOH HOH A . 
T 7 HOH 213 1013 139  HOH HOH A . 
T 7 HOH 214 1014 984  HOH HOH A . 
T 7 HOH 215 1015 189  HOH HOH A . 
T 7 HOH 216 1016 1139 HOH HOH A . 
T 7 HOH 217 1017 227  HOH HOH A . 
T 7 HOH 218 1018 182  HOH HOH A . 
T 7 HOH 219 1019 898  HOH HOH A . 
T 7 HOH 220 1020 1227 HOH HOH A . 
T 7 HOH 221 1021 226  HOH HOH A . 
T 7 HOH 222 1022 166  HOH HOH A . 
T 7 HOH 223 1023 937  HOH HOH A . 
T 7 HOH 224 1024 253  HOH HOH A . 
T 7 HOH 225 1025 314  HOH HOH A . 
T 7 HOH 226 1026 330  HOH HOH A . 
T 7 HOH 227 1027 62   HOH HOH A . 
T 7 HOH 228 1028 223  HOH HOH A . 
T 7 HOH 229 1029 527  HOH HOH A . 
T 7 HOH 230 1030 647  HOH HOH A . 
T 7 HOH 231 1031 884  HOH HOH A . 
T 7 HOH 232 1032 674  HOH HOH A . 
T 7 HOH 233 1033 195  HOH HOH A . 
T 7 HOH 234 1034 46   HOH HOH A . 
T 7 HOH 235 1035 29   HOH HOH A . 
T 7 HOH 236 1036 849  HOH HOH A . 
T 7 HOH 237 1037 1045 HOH HOH A . 
T 7 HOH 238 1038 485  HOH HOH A . 
T 7 HOH 239 1039 269  HOH HOH A . 
T 7 HOH 240 1040 1090 HOH HOH A . 
T 7 HOH 241 1041 284  HOH HOH A . 
T 7 HOH 242 1042 242  HOH HOH A . 
T 7 HOH 243 1043 79   HOH HOH A . 
T 7 HOH 244 1044 1093 HOH HOH A . 
T 7 HOH 245 1045 416  HOH HOH A . 
T 7 HOH 246 1046 1136 HOH HOH A . 
T 7 HOH 247 1047 957  HOH HOH A . 
T 7 HOH 248 1048 1022 HOH HOH A . 
T 7 HOH 249 1049 381  HOH HOH A . 
T 7 HOH 250 1050 474  HOH HOH A . 
T 7 HOH 251 1051 1067 HOH HOH A . 
T 7 HOH 252 1052 222  HOH HOH A . 
T 7 HOH 253 1053 372  HOH HOH A . 
T 7 HOH 254 1054 88   HOH HOH A . 
T 7 HOH 255 1055 178  HOH HOH A . 
T 7 HOH 256 1056 173  HOH HOH A . 
T 7 HOH 257 1057 852  HOH HOH A . 
T 7 HOH 258 1058 393  HOH HOH A . 
T 7 HOH 259 1059 48   HOH HOH A . 
T 7 HOH 260 1060 85   HOH HOH A . 
T 7 HOH 261 1061 940  HOH HOH A . 
T 7 HOH 262 1062 192  HOH HOH A . 
T 7 HOH 263 1063 357  HOH HOH A . 
T 7 HOH 264 1064 532  HOH HOH A . 
T 7 HOH 265 1065 544  HOH HOH A . 
T 7 HOH 266 1066 458  HOH HOH A . 
T 7 HOH 267 1067 1176 HOH HOH A . 
T 7 HOH 268 1068 665  HOH HOH A . 
T 7 HOH 269 1069 232  HOH HOH A . 
T 7 HOH 270 1070 595  HOH HOH A . 
T 7 HOH 271 1071 180  HOH HOH A . 
T 7 HOH 272 1072 646  HOH HOH A . 
T 7 HOH 273 1073 1203 HOH HOH A . 
T 7 HOH 274 1074 203  HOH HOH A . 
T 7 HOH 275 1075 1193 HOH HOH A . 
T 7 HOH 276 1076 87   HOH HOH A . 
T 7 HOH 277 1077 27   HOH HOH A . 
T 7 HOH 278 1078 904  HOH HOH A . 
T 7 HOH 279 1079 439  HOH HOH A . 
T 7 HOH 280 1080 908  HOH HOH A . 
T 7 HOH 281 1081 1216 HOH HOH A . 
T 7 HOH 282 1082 267  HOH HOH A . 
T 7 HOH 283 1083 562  HOH HOH A . 
T 7 HOH 284 1084 325  HOH HOH A . 
T 7 HOH 285 1085 77   HOH HOH A . 
T 7 HOH 286 1086 110  HOH HOH A . 
T 7 HOH 287 1087 299  HOH HOH A . 
T 7 HOH 288 1088 1148 HOH HOH A . 
T 7 HOH 289 1089 907  HOH HOH A . 
T 7 HOH 290 1090 42   HOH HOH A . 
T 7 HOH 291 1091 564  HOH HOH A . 
T 7 HOH 292 1092 626  HOH HOH A . 
T 7 HOH 293 1093 1286 HOH HOH A . 
T 7 HOH 294 1094 859  HOH HOH A . 
T 7 HOH 295 1095 498  HOH HOH A . 
T 7 HOH 296 1096 886  HOH HOH A . 
T 7 HOH 297 1097 13   HOH HOH A . 
T 7 HOH 298 1098 36   HOH HOH A . 
T 7 HOH 299 1099 217  HOH HOH A . 
T 7 HOH 300 1100 1147 HOH HOH A . 
T 7 HOH 301 1101 480  HOH HOH A . 
T 7 HOH 302 1102 66   HOH HOH A . 
T 7 HOH 303 1103 481  HOH HOH A . 
T 7 HOH 304 1104 1168 HOH HOH A . 
T 7 HOH 305 1105 418  HOH HOH A . 
T 7 HOH 306 1106 1323 HOH HOH A . 
T 7 HOH 307 1107 80   HOH HOH A . 
T 7 HOH 308 1108 905  HOH HOH A . 
T 7 HOH 309 1109 194  HOH HOH A . 
T 7 HOH 310 1110 1073 HOH HOH A . 
T 7 HOH 311 1111 197  HOH HOH A . 
T 7 HOH 312 1112 897  HOH HOH A . 
T 7 HOH 313 1113 11   HOH HOH A . 
T 7 HOH 314 1114 914  HOH HOH A . 
T 7 HOH 315 1115 70   HOH HOH A . 
T 7 HOH 316 1116 398  HOH HOH A . 
T 7 HOH 317 1117 76   HOH HOH A . 
T 7 HOH 318 1118 35   HOH HOH A . 
T 7 HOH 319 1119 1191 HOH HOH A . 
T 7 HOH 320 1120 362  HOH HOH A . 
T 7 HOH 321 1121 584  HOH HOH A . 
T 7 HOH 322 1122 234  HOH HOH A . 
T 7 HOH 323 1123 33   HOH HOH A . 
T 7 HOH 324 1124 551  HOH HOH A . 
T 7 HOH 325 1125 407  HOH HOH A . 
T 7 HOH 326 1126 368  HOH HOH A . 
T 7 HOH 327 1127 343  HOH HOH A . 
T 7 HOH 328 1128 426  HOH HOH A . 
T 7 HOH 329 1129 417  HOH HOH A . 
T 7 HOH 330 1130 1156 HOH HOH A . 
T 7 HOH 331 1131 313  HOH HOH A . 
T 7 HOH 332 1132 10   HOH HOH A . 
T 7 HOH 333 1133 408  HOH HOH A . 
T 7 HOH 334 1134 208  HOH HOH A . 
T 7 HOH 335 1135 492  HOH HOH A . 
T 7 HOH 336 1136 903  HOH HOH A . 
T 7 HOH 337 1137 1034 HOH HOH A . 
T 7 HOH 338 1138 383  HOH HOH A . 
T 7 HOH 339 1139 181  HOH HOH A . 
T 7 HOH 340 1140 1142 HOH HOH A . 
T 7 HOH 341 1141 120  HOH HOH A . 
T 7 HOH 342 1142 419  HOH HOH A . 
T 7 HOH 343 1143 1151 HOH HOH A . 
T 7 HOH 344 1144 18   HOH HOH A . 
T 7 HOH 345 1145 1102 HOH HOH A . 
T 7 HOH 346 1146 45   HOH HOH A . 
T 7 HOH 347 1147 385  HOH HOH A . 
T 7 HOH 348 1148 243  HOH HOH A . 
T 7 HOH 349 1149 144  HOH HOH A . 
T 7 HOH 350 1150 148  HOH HOH A . 
T 7 HOH 351 1151 247  HOH HOH A . 
T 7 HOH 352 1152 977  HOH HOH A . 
T 7 HOH 353 1153 116  HOH HOH A . 
T 7 HOH 354 1154 99   HOH HOH A . 
T 7 HOH 355 1155 1313 HOH HOH A . 
T 7 HOH 356 1156 34   HOH HOH A . 
T 7 HOH 357 1157 171  HOH HOH A . 
T 7 HOH 358 1158 201  HOH HOH A . 
T 7 HOH 359 1159 1225 HOH HOH A . 
T 7 HOH 360 1160 497  HOH HOH A . 
T 7 HOH 361 1161 207  HOH HOH A . 
T 7 HOH 362 1162 1304 HOH HOH A . 
T 7 HOH 363 1163 388  HOH HOH A . 
T 7 HOH 364 1164 932  HOH HOH A . 
T 7 HOH 365 1165 151  HOH HOH A . 
T 7 HOH 366 1166 422  HOH HOH A . 
T 7 HOH 367 1167 509  HOH HOH A . 
T 7 HOH 368 1168 427  HOH HOH A . 
T 7 HOH 369 1169 553  HOH HOH A . 
T 7 HOH 370 1170 169  HOH HOH A . 
T 7 HOH 371 1171 973  HOH HOH A . 
T 7 HOH 372 1172 123  HOH HOH A . 
T 7 HOH 373 1173 265  HOH HOH A . 
T 7 HOH 374 1174 1083 HOH HOH A . 
T 7 HOH 375 1175 6    HOH HOH A . 
T 7 HOH 376 1176 862  HOH HOH A . 
T 7 HOH 377 1177 517  HOH HOH A . 
T 7 HOH 378 1178 995  HOH HOH A . 
T 7 HOH 379 1179 673  HOH HOH A . 
T 7 HOH 380 1180 878  HOH HOH A . 
T 7 HOH 381 1181 1201 HOH HOH A . 
T 7 HOH 382 1182 210  HOH HOH A . 
T 7 HOH 383 1183 273  HOH HOH A . 
T 7 HOH 384 1184 1141 HOH HOH A . 
T 7 HOH 385 1185 1293 HOH HOH A . 
T 7 HOH 386 1186 1116 HOH HOH A . 
T 7 HOH 387 1187 384  HOH HOH A . 
T 7 HOH 388 1188 340  HOH HOH A . 
T 7 HOH 389 1189 230  HOH HOH A . 
T 7 HOH 390 1190 336  HOH HOH A . 
T 7 HOH 391 1191 1114 HOH HOH A . 
T 7 HOH 392 1192 628  HOH HOH A . 
T 7 HOH 393 1193 1222 HOH HOH A . 
T 7 HOH 394 1194 133  HOH HOH A . 
T 7 HOH 395 1195 153  HOH HOH A . 
T 7 HOH 396 1196 615  HOH HOH A . 
T 7 HOH 397 1197 301  HOH HOH A . 
T 7 HOH 398 1198 514  HOH HOH A . 
T 7 HOH 399 1199 591  HOH HOH A . 
T 7 HOH 400 1200 684  HOH HOH A . 
T 7 HOH 401 1201 863  HOH HOH A . 
T 7 HOH 402 1202 1295 HOH HOH A . 
T 7 HOH 403 1203 412  HOH HOH A . 
T 7 HOH 404 1204 1284 HOH HOH A . 
T 7 HOH 405 1205 324  HOH HOH A . 
T 7 HOH 406 1206 919  HOH HOH A . 
T 7 HOH 407 1207 850  HOH HOH A . 
T 7 HOH 408 1208 264  HOH HOH A . 
T 7 HOH 409 1209 259  HOH HOH A . 
T 7 HOH 410 1210 546  HOH HOH A . 
T 7 HOH 411 1211 1233 HOH HOH A . 
T 7 HOH 412 1212 477  HOH HOH A . 
T 7 HOH 413 1213 901  HOH HOH A . 
T 7 HOH 414 1214 627  HOH HOH A . 
T 7 HOH 415 1215 861  HOH HOH A . 
T 7 HOH 416 1216 465  HOH HOH A . 
T 7 HOH 417 1217 311  HOH HOH A . 
T 7 HOH 418 1218 478  HOH HOH A . 
T 7 HOH 419 1219 289  HOH HOH A . 
T 7 HOH 420 1220 431  HOH HOH A . 
T 7 HOH 421 1221 354  HOH HOH A . 
T 7 HOH 422 1222 160  HOH HOH A . 
T 7 HOH 423 1223 537  HOH HOH A . 
T 7 HOH 424 1224 1220 HOH HOH A . 
T 7 HOH 425 1225 172  HOH HOH A . 
T 7 HOH 426 1226 364  HOH HOH A . 
T 7 HOH 427 1227 880  HOH HOH A . 
T 7 HOH 428 1228 890  HOH HOH A . 
T 7 HOH 429 1229 250  HOH HOH A . 
T 7 HOH 430 1230 887  HOH HOH A . 
T 7 HOH 431 1231 475  HOH HOH A . 
T 7 HOH 432 1232 881  HOH HOH A . 
T 7 HOH 433 1233 28   HOH HOH A . 
T 7 HOH 434 1234 1023 HOH HOH A . 
T 7 HOH 435 1235 437  HOH HOH A . 
T 7 HOH 436 1236 84   HOH HOH A . 
T 7 HOH 437 1237 58   HOH HOH A . 
T 7 HOH 438 1238 196  HOH HOH A . 
T 7 HOH 439 1239 565  HOH HOH A . 
T 7 HOH 440 1240 1279 HOH HOH A . 
T 7 HOH 441 1241 534  HOH HOH A . 
T 7 HOH 442 1242 1041 HOH HOH A . 
T 7 HOH 443 1243 500  HOH HOH A . 
T 7 HOH 444 1244 167  HOH HOH A . 
T 7 HOH 445 1245 296  HOH HOH A . 
T 7 HOH 446 1246 1101 HOH HOH A . 
T 7 HOH 447 1247 212  HOH HOH A . 
T 7 HOH 448 1248 1108 HOH HOH A . 
T 7 HOH 449 1249 0    HOH HOH A . 
T 7 HOH 450 1250 1197 HOH HOH A . 
T 7 HOH 451 1251 111  HOH HOH A . 
T 7 HOH 452 1252 63   HOH HOH A . 
T 7 HOH 453 1253 1047 HOH HOH A . 
T 7 HOH 454 1254 104  HOH HOH A . 
T 7 HOH 455 1255 335  HOH HOH A . 
T 7 HOH 456 1256 1149 HOH HOH A . 
T 7 HOH 457 1257 237  HOH HOH A . 
T 7 HOH 458 1258 543  HOH HOH A . 
T 7 HOH 459 1259 353  HOH HOH A . 
T 7 HOH 460 1260 1042 HOH HOH A . 
T 7 HOH 461 1261 52   HOH HOH A . 
T 7 HOH 462 1262 1305 HOH HOH A . 
T 7 HOH 463 1263 520  HOH HOH A . 
T 7 HOH 464 1264 333  HOH HOH A . 
T 7 HOH 465 1265 7    HOH HOH A . 
T 7 HOH 466 1266 8    HOH HOH A . 
T 7 HOH 467 1267 482  HOH HOH A . 
T 7 HOH 468 1268 258  HOH HOH A . 
T 7 HOH 469 1269 1317 HOH HOH A . 
T 7 HOH 470 1270 1237 HOH HOH A . 
T 7 HOH 471 1271 1179 HOH HOH A . 
T 7 HOH 472 1272 652  HOH HOH A . 
T 7 HOH 473 1273 91   HOH HOH A . 
T 7 HOH 474 1274 855  HOH HOH A . 
T 7 HOH 475 1275 854  HOH HOH A . 
T 7 HOH 476 1276 136  HOH HOH A . 
T 7 HOH 477 1277 387  HOH HOH A . 
T 7 HOH 478 1278 1188 HOH HOH A . 
T 7 HOH 479 1279 1299 HOH HOH A . 
T 7 HOH 480 1280 902  HOH HOH A . 
T 7 HOH 481 1281 883  HOH HOH A . 
T 7 HOH 482 1282 953  HOH HOH A . 
T 7 HOH 483 1283 926  HOH HOH A . 
T 7 HOH 484 1284 472  HOH HOH A . 
T 7 HOH 485 1285 67   HOH HOH A . 
T 7 HOH 486 1286 184  HOH HOH A . 
T 7 HOH 487 1287 5    HOH HOH A . 
T 7 HOH 488 1288 128  HOH HOH A . 
T 7 HOH 489 1289 526  HOH HOH A . 
T 7 HOH 490 1290 1310 HOH HOH A . 
T 7 HOH 491 1291 669  HOH HOH A . 
T 7 HOH 492 1292 1040 HOH HOH A . 
T 7 HOH 493 1293 371  HOH HOH A . 
T 7 HOH 494 1294 1024 HOH HOH A . 
T 7 HOH 495 1295 1150 HOH HOH A . 
T 7 HOH 496 1296 875  HOH HOH A . 
T 7 HOH 497 1297 1155 HOH HOH A . 
T 7 HOH 498 1298 949  HOH HOH A . 
T 7 HOH 499 1299 950  HOH HOH A . 
T 7 HOH 500 1300 467  HOH HOH A . 
T 7 HOH 501 1301 960  HOH HOH A . 
T 7 HOH 502 1302 1143 HOH HOH A . 
T 7 HOH 503 1303 857  HOH HOH A . 
T 7 HOH 504 1304 891  HOH HOH A . 
T 7 HOH 505 1305 1164 HOH HOH A . 
T 7 HOH 506 1306 129  HOH HOH A . 
T 7 HOH 507 1307 1230 HOH HOH A . 
T 7 HOH 508 1308 1229 HOH HOH A . 
T 7 HOH 509 1309 896  HOH HOH A . 
T 7 HOH 510 1310 961  HOH HOH A . 
T 7 HOH 511 1311 249  HOH HOH A . 
T 7 HOH 512 1312 352  HOH HOH A . 
T 7 HOH 513 1313 1180 HOH HOH A . 
T 7 HOH 514 1314 244  HOH HOH A . 
T 7 HOH 515 1315 529  HOH HOH A . 
T 7 HOH 516 1316 315  HOH HOH A . 
T 7 HOH 517 1317 60   HOH HOH A . 
T 7 HOH 518 1318 198  HOH HOH A . 
T 7 HOH 519 1319 16   HOH HOH A . 
T 7 HOH 520 1320 37   HOH HOH A . 
T 7 HOH 521 1321 528  HOH HOH A . 
T 7 HOH 522 1322 1177 HOH HOH A . 
T 7 HOH 523 1323 31   HOH HOH A . 
T 7 HOH 524 1324 1198 HOH HOH A . 
T 7 HOH 525 1325 1145 HOH HOH A . 
T 7 HOH 526 1326 900  HOH HOH A . 
T 7 HOH 527 1327 911  HOH HOH A . 
T 7 HOH 528 1328 1061 HOH HOH A . 
T 7 HOH 529 1329 300  HOH HOH A . 
T 7 HOH 530 1330 1234 HOH HOH A . 
T 7 HOH 531 1331 40   HOH HOH A . 
T 7 HOH 532 1332 913  HOH HOH A . 
T 7 HOH 533 1333 894  HOH HOH A . 
T 7 HOH 534 1334 320  HOH HOH A . 
T 7 HOH 535 1335 1103 HOH HOH A . 
T 7 HOH 536 1336 636  HOH HOH A . 
T 7 HOH 537 1337 536  HOH HOH A . 
T 7 HOH 538 1338 12   HOH HOH A . 
T 7 HOH 539 1339 1035 HOH HOH A . 
T 7 HOH 540 1340 1153 HOH HOH A . 
T 7 HOH 541 1341 126  HOH HOH A . 
T 7 HOH 542 1342 59   HOH HOH A . 
T 7 HOH 543 1343 225  HOH HOH A . 
T 7 HOH 544 1344 142  HOH HOH A . 
T 7 HOH 545 1345 4    HOH HOH A . 
T 7 HOH 546 1346 471  HOH HOH A . 
T 7 HOH 547 1347 521  HOH HOH A . 
T 7 HOH 548 1348 941  HOH HOH A . 
T 7 HOH 549 1349 32   HOH HOH A . 
T 7 HOH 550 1350 1214 HOH HOH A . 
T 7 HOH 551 1351 597  HOH HOH A . 
T 7 HOH 552 1352 1236 HOH HOH A . 
T 7 HOH 553 1353 43   HOH HOH A . 
T 7 HOH 554 1354 865  HOH HOH A . 
T 7 HOH 555 1355 1218 HOH HOH A . 
T 7 HOH 556 1356 1085 HOH HOH A . 
T 7 HOH 557 1357 1170 HOH HOH A . 
T 7 HOH 558 1358 266  HOH HOH A . 
T 7 HOH 559 1359 288  HOH HOH A . 
T 7 HOH 560 1360 24   HOH HOH A . 
T 7 HOH 561 1361 1326 HOH HOH A . 
T 7 HOH 562 1362 486  HOH HOH A . 
T 7 HOH 563 1363 323  HOH HOH A . 
T 7 HOH 564 1364 946  HOH HOH A . 
T 7 HOH 565 1365 1166 HOH HOH A . 
T 7 HOH 566 1366 86   HOH HOH A . 
T 7 HOH 567 1367 1212 HOH HOH A . 
T 7 HOH 568 1368 3    HOH HOH A . 
T 7 HOH 569 1369 683  HOH HOH A . 
T 7 HOH 570 1370 561  HOH HOH A . 
T 7 HOH 571 1371 1033 HOH HOH A . 
T 7 HOH 572 1372 147  HOH HOH A . 
T 7 HOH 573 1373 1027 HOH HOH A . 
T 7 HOH 574 1374 959  HOH HOH A . 
T 7 HOH 575 1375 1026 HOH HOH A . 
T 7 HOH 576 1376 1242 HOH HOH A . 
T 7 HOH 577 1377 877  HOH HOH A . 
T 7 HOH 578 1378 409  HOH HOH A . 
T 7 HOH 579 1379 892  HOH HOH A . 
T 7 HOH 580 1380 1036 HOH HOH A . 
T 7 HOH 581 1381 951  HOH HOH A . 
T 7 HOH 582 1382 1178 HOH HOH A . 
T 7 HOH 583 1383 1202 HOH HOH A . 
T 7 HOH 584 1384 1161 HOH HOH A . 
T 7 HOH 585 1385 204  HOH HOH A . 
T 7 HOH 586 1386 22   HOH HOH A . 
T 7 HOH 587 1387 483  HOH HOH A . 
T 7 HOH 588 1388 866  HOH HOH A . 
T 7 HOH 589 1389 965  HOH HOH A . 
T 7 HOH 590 1390 1311 HOH HOH A . 
T 7 HOH 591 1391 109  HOH HOH A . 
T 7 HOH 592 1392 583  HOH HOH A . 
T 7 HOH 593 1393 1209 HOH HOH A . 
T 7 HOH 594 1394 971  HOH HOH A . 
T 7 HOH 595 1395 1297 HOH HOH A . 
T 7 HOH 596 1396 1162 HOH HOH A . 
T 7 HOH 597 1397 506  HOH HOH A . 
T 7 HOH 598 1398 853  HOH HOH A . 
T 7 HOH 599 1399 275  HOH HOH A . 
T 7 HOH 600 1400 921  HOH HOH A . 
T 7 HOH 601 1401 332  HOH HOH A . 
T 7 HOH 602 1402 1185 HOH HOH A . 
T 7 HOH 603 1403 135  HOH HOH A . 
T 7 HOH 604 1404 879  HOH HOH A . 
T 7 HOH 605 1405 1172 HOH HOH A . 
T 7 HOH 606 1406 187  HOH HOH A . 
T 7 HOH 607 1407 872  HOH HOH A . 
T 7 HOH 608 1408 922  HOH HOH A . 
T 7 HOH 609 1409 952  HOH HOH A . 
T 7 HOH 610 1410 280  HOH HOH A . 
T 7 HOH 611 1411 936  HOH HOH A . 
T 7 HOH 612 1412 550  HOH HOH A . 
T 7 HOH 613 1413 30   HOH HOH A . 
T 7 HOH 614 1414 143  HOH HOH A . 
T 7 HOH 615 1415 956  HOH HOH A . 
T 7 HOH 616 1416 272  HOH HOH A . 
T 7 HOH 617 1417 186  HOH HOH A . 
T 7 HOH 618 1418 445  HOH HOH A . 
T 7 HOH 619 1419 150  HOH HOH A . 
T 7 HOH 620 1420 535  HOH HOH A . 
T 7 HOH 621 1421 103  HOH HOH A . 
T 7 HOH 622 1422 23   HOH HOH A . 
T 7 HOH 623 1423 918  HOH HOH A . 
T 7 HOH 624 1424 1217 HOH HOH A . 
T 7 HOH 625 1425 1146 HOH HOH A . 
T 7 HOH 626 1426 25   HOH HOH A . 
T 7 HOH 627 1427 1192 HOH HOH A . 
T 7 HOH 628 1428 400  HOH HOH A . 
T 7 HOH 629 1429 50   HOH HOH A . 
T 7 HOH 630 1430 1043 HOH HOH A . 
T 7 HOH 631 1431 1196 HOH HOH A . 
T 7 HOH 632 1432 882  HOH HOH A . 
T 7 HOH 633 1433 1194 HOH HOH A . 
T 7 HOH 634 1434 15   HOH HOH A . 
T 7 HOH 635 1435 1211 HOH HOH A . 
T 7 HOH 636 1436 871  HOH HOH A . 
T 7 HOH 637 1437 20   HOH HOH A . 
T 7 HOH 638 1438 869  HOH HOH A . 
T 7 HOH 639 1439 1173 HOH HOH A . 
T 7 HOH 640 1440 356  HOH HOH A . 
T 7 HOH 641 1441 1157 HOH HOH A . 
T 7 HOH 642 1442 1104 HOH HOH A . 
T 7 HOH 643 1443 917  HOH HOH A . 
U 7 HOH 1   801  721  HOH HOH B . 
U 7 HOH 2   802  1224 HOH HOH B . 
U 7 HOH 3   803  432  HOH HOH B . 
U 7 HOH 4   804  633  HOH HOH B . 
U 7 HOH 5   805  341  HOH HOH B . 
U 7 HOH 6   806  1081 HOH HOH B . 
U 7 HOH 7   807  1300 HOH HOH B . 
U 7 HOH 8   808  1134 HOH HOH B . 
U 7 HOH 9   809  286  HOH HOH B . 
U 7 HOH 10  810  138  HOH HOH B . 
U 7 HOH 11  811  1245 HOH HOH B . 
U 7 HOH 12  812  71   HOH HOH B . 
U 7 HOH 13  813  1124 HOH HOH B . 
U 7 HOH 14  814  975  HOH HOH B . 
U 7 HOH 15  815  1320 HOH HOH B . 
U 7 HOH 16  816  349  HOH HOH B . 
U 7 HOH 17  817  157  HOH HOH B . 
U 7 HOH 18  818  236  HOH HOH B . 
U 7 HOH 19  819  1056 HOH HOH B . 
U 7 HOH 20  820  758  HOH HOH B . 
U 7 HOH 21  821  925  HOH HOH B . 
U 7 HOH 22  822  1076 HOH HOH B . 
U 7 HOH 23  823  1171 HOH HOH B . 
U 7 HOH 24  824  1160 HOH HOH B . 
U 7 HOH 25  825  1122 HOH HOH B . 
U 7 HOH 26  826  983  HOH HOH B . 
U 7 HOH 27  827  1219 HOH HOH B . 
U 7 HOH 28  828  739  HOH HOH B . 
U 7 HOH 29  829  476  HOH HOH B . 
U 7 HOH 30  830  705  HOH HOH B . 
U 7 HOH 31  831  938  HOH HOH B . 
U 7 HOH 32  832  304  HOH HOH B . 
U 7 HOH 33  833  725  HOH HOH B . 
U 7 HOH 34  834  617  HOH HOH B . 
U 7 HOH 35  835  601  HOH HOH B . 
U 7 HOH 36  836  1253 HOH HOH B . 
U 7 HOH 37  837  105  HOH HOH B . 
U 7 HOH 38  838  523  HOH HOH B . 
U 7 HOH 39  839  832  HOH HOH B . 
U 7 HOH 40  840  707  HOH HOH B . 
U 7 HOH 41  841  1012 HOH HOH B . 
U 7 HOH 42  842  1301 HOH HOH B . 
U 7 HOH 43  843  912  HOH HOH B . 
U 7 HOH 44  844  307  HOH HOH B . 
U 7 HOH 45  845  666  HOH HOH B . 
U 7 HOH 46  846  761  HOH HOH B . 
U 7 HOH 47  847  154  HOH HOH B . 
U 7 HOH 48  848  549  HOH HOH B . 
U 7 HOH 49  849  538  HOH HOH B . 
U 7 HOH 50  850  495  HOH HOH B . 
U 7 HOH 51  851  820  HOH HOH B . 
U 7 HOH 52  852  574  HOH HOH B . 
U 7 HOH 53  853  731  HOH HOH B . 
U 7 HOH 54  854  692  HOH HOH B . 
U 7 HOH 55  855  720  HOH HOH B . 
U 7 HOH 56  856  648  HOH HOH B . 
U 7 HOH 57  857  810  HOH HOH B . 
U 7 HOH 58  858  979  HOH HOH B . 
U 7 HOH 59  859  829  HOH HOH B . 
U 7 HOH 60  860  1087 HOH HOH B . 
U 7 HOH 61  861  575  HOH HOH B . 
U 7 HOH 62  862  366  HOH HOH B . 
U 7 HOH 63  863  790  HOH HOH B . 
U 7 HOH 64  864  421  HOH HOH B . 
U 7 HOH 65  865  525  HOH HOH B . 
U 7 HOH 66  866  823  HOH HOH B . 
U 7 HOH 67  867  568  HOH HOH B . 
U 7 HOH 68  868  1063 HOH HOH B . 
U 7 HOH 69  869  560  HOH HOH B . 
U 7 HOH 70  870  981  HOH HOH B . 
U 7 HOH 71  871  1133 HOH HOH B . 
U 7 HOH 72  872  621  HOH HOH B . 
U 7 HOH 73  873  771  HOH HOH B . 
U 7 HOH 74  874  179  HOH HOH B . 
U 7 HOH 75  875  81   HOH HOH B . 
U 7 HOH 76  876  1106 HOH HOH B . 
U 7 HOH 77  877  740  HOH HOH B . 
U 7 HOH 78  878  659  HOH HOH B . 
U 7 HOH 79  879  1098 HOH HOH B . 
U 7 HOH 80  880  1084 HOH HOH B . 
U 7 HOH 81  881  624  HOH HOH B . 
U 7 HOH 82  882  778  HOH HOH B . 
U 7 HOH 83  883  582  HOH HOH B . 
U 7 HOH 84  884  188  HOH HOH B . 
U 7 HOH 85  885  629  HOH HOH B . 
U 7 HOH 86  886  1282 HOH HOH B . 
U 7 HOH 87  887  158  HOH HOH B . 
U 7 HOH 88  888  1005 HOH HOH B . 
U 7 HOH 89  889  1086 HOH HOH B . 
U 7 HOH 90  890  773  HOH HOH B . 
U 7 HOH 91  891  1290 HOH HOH B . 
U 7 HOH 92  892  782  HOH HOH B . 
U 7 HOH 93  893  1059 HOH HOH B . 
U 7 HOH 94  894  929  HOH HOH B . 
U 7 HOH 95  895  130  HOH HOH B . 
U 7 HOH 96  896  786  HOH HOH B . 
U 7 HOH 97  897  787  HOH HOH B . 
U 7 HOH 98  898  696  HOH HOH B . 
U 7 HOH 99  899  1110 HOH HOH B . 
U 7 HOH 100 900  822  HOH HOH B . 
U 7 HOH 101 901  1058 HOH HOH B . 
U 7 HOH 102 902  1265 HOH HOH B . 
U 7 HOH 103 903  808  HOH HOH B . 
U 7 HOH 104 904  461  HOH HOH B . 
U 7 HOH 105 905  1120 HOH HOH B . 
U 7 HOH 106 906  572  HOH HOH B . 
U 7 HOH 107 907  493  HOH HOH B . 
U 7 HOH 108 908  567  HOH HOH B . 
U 7 HOH 109 909  1283 HOH HOH B . 
U 7 HOH 110 910  1204 HOH HOH B . 
U 7 HOH 111 911  145  HOH HOH B . 
U 7 HOH 112 912  451  HOH HOH B . 
U 7 HOH 113 913  468  HOH HOH B . 
U 7 HOH 114 914  817  HOH HOH B . 
U 7 HOH 115 915  716  HOH HOH B . 
U 7 HOH 116 916  948  HOH HOH B . 
U 7 HOH 117 917  292  HOH HOH B . 
U 7 HOH 118 918  864  HOH HOH B . 
U 7 HOH 119 919  504  HOH HOH B . 
U 7 HOH 120 920  781  HOH HOH B . 
U 7 HOH 121 921  775  HOH HOH B . 
U 7 HOH 122 922  554  HOH HOH B . 
U 7 HOH 123 923  596  HOH HOH B . 
U 7 HOH 124 924  827  HOH HOH B . 
U 7 HOH 125 925  1328 HOH HOH B . 
U 7 HOH 126 926  1021 HOH HOH B . 
U 7 HOH 127 927  842  HOH HOH B . 
U 7 HOH 128 928  101  HOH HOH B . 
U 7 HOH 129 929  730  HOH HOH B . 
U 7 HOH 130 930  845  HOH HOH B . 
U 7 HOH 131 931  490  HOH HOH B . 
U 7 HOH 132 932  355  HOH HOH B . 
U 7 HOH 133 933  694  HOH HOH B . 
U 7 HOH 134 934  501  HOH HOH B . 
U 7 HOH 135 935  547  HOH HOH B . 
U 7 HOH 136 936  618  HOH HOH B . 
U 7 HOH 137 937  1048 HOH HOH B . 
U 7 HOH 138 938  743  HOH HOH B . 
U 7 HOH 139 939  736  HOH HOH B . 
U 7 HOH 140 940  1257 HOH HOH B . 
U 7 HOH 141 941  436  HOH HOH B . 
U 7 HOH 142 942  802  HOH HOH B . 
U 7 HOH 143 943  49   HOH HOH B . 
U 7 HOH 144 944  1013 HOH HOH B . 
U 7 HOH 145 945  1268 HOH HOH B . 
U 7 HOH 146 946  821  HOH HOH B . 
U 7 HOH 147 947  518  HOH HOH B . 
U 7 HOH 148 948  1064 HOH HOH B . 
U 7 HOH 149 949  548  HOH HOH B . 
U 7 HOH 150 950  321  HOH HOH B . 
U 7 HOH 151 951  717  HOH HOH B . 
U 7 HOH 152 952  69   HOH HOH B . 
U 7 HOH 153 953  745  HOH HOH B . 
U 7 HOH 154 954  369  HOH HOH B . 
U 7 HOH 155 955  557  HOH HOH B . 
U 7 HOH 156 956  425  HOH HOH B . 
U 7 HOH 157 957  556  HOH HOH B . 
U 7 HOH 158 958  654  HOH HOH B . 
U 7 HOH 159 959  363  HOH HOH B . 
U 7 HOH 160 960  690  HOH HOH B . 
U 7 HOH 161 961  1206 HOH HOH B . 
U 7 HOH 162 962  699  HOH HOH B . 
U 7 HOH 163 963  1054 HOH HOH B . 
U 7 HOH 164 964  679  HOH HOH B . 
U 7 HOH 165 965  473  HOH HOH B . 
U 7 HOH 166 966  254  HOH HOH B . 
U 7 HOH 167 967  277  HOH HOH B . 
U 7 HOH 168 968  589  HOH HOH B . 
U 7 HOH 169 969  310  HOH HOH B . 
U 7 HOH 170 970  457  HOH HOH B . 
U 7 HOH 171 971  713  HOH HOH B . 
U 7 HOH 172 972  844  HOH HOH B . 
U 7 HOH 173 973  374  HOH HOH B . 
U 7 HOH 174 974  1029 HOH HOH B . 
U 7 HOH 175 975  763  HOH HOH B . 
U 7 HOH 176 976  245  HOH HOH B . 
U 7 HOH 177 977  641  HOH HOH B . 
U 7 HOH 178 978  1097 HOH HOH B . 
U 7 HOH 179 979  443  HOH HOH B . 
U 7 HOH 180 980  403  HOH HOH B . 
U 7 HOH 181 981  141  HOH HOH B . 
U 7 HOH 182 982  691  HOH HOH B . 
U 7 HOH 183 983  119  HOH HOH B . 
U 7 HOH 184 984  287  HOH HOH B . 
U 7 HOH 185 985  1010 HOH HOH B . 
U 7 HOH 186 986  588  HOH HOH B . 
U 7 HOH 187 987  1014 HOH HOH B . 
U 7 HOH 188 988  592  HOH HOH B . 
U 7 HOH 189 989  241  HOH HOH B . 
U 7 HOH 190 990  767  HOH HOH B . 
U 7 HOH 191 991  704  HOH HOH B . 
U 7 HOH 192 992  305  HOH HOH B . 
U 7 HOH 193 993  779  HOH HOH B . 
U 7 HOH 194 994  649  HOH HOH B . 
U 7 HOH 195 995  760  HOH HOH B . 
U 7 HOH 196 996  1088 HOH HOH B . 
U 7 HOH 197 997  1281 HOH HOH B . 
U 7 HOH 198 998  1262 HOH HOH B . 
U 7 HOH 199 999  599  HOH HOH B . 
U 7 HOH 200 1000 658  HOH HOH B . 
U 7 HOH 201 1001 512  HOH HOH B . 
U 7 HOH 202 1002 164  HOH HOH B . 
U 7 HOH 203 1003 604  HOH HOH B . 
U 7 HOH 204 1004 672  HOH HOH B . 
U 7 HOH 205 1005 667  HOH HOH B . 
U 7 HOH 206 1006 1004 HOH HOH B . 
U 7 HOH 207 1007 1092 HOH HOH B . 
U 7 HOH 208 1008 715  HOH HOH B . 
U 7 HOH 209 1009 1125 HOH HOH B . 
U 7 HOH 210 1010 1018 HOH HOH B . 
U 7 HOH 211 1011 702  HOH HOH B . 
U 7 HOH 212 1012 837  HOH HOH B . 
U 7 HOH 213 1013 755  HOH HOH B . 
U 7 HOH 214 1014 558  HOH HOH B . 
U 7 HOH 215 1015 867  HOH HOH B . 
U 7 HOH 216 1016 200  HOH HOH B . 
U 7 HOH 217 1017 1015 HOH HOH B . 
U 7 HOH 218 1018 807  HOH HOH B . 
U 7 HOH 219 1019 1165 HOH HOH B . 
U 7 HOH 220 1020 566  HOH HOH B . 
U 7 HOH 221 1021 732  HOH HOH B . 
U 7 HOH 222 1022 693  HOH HOH B . 
U 7 HOH 223 1023 380  HOH HOH B . 
U 7 HOH 224 1024 687  HOH HOH B . 
U 7 HOH 225 1025 1009 HOH HOH B . 
U 7 HOH 226 1026 396  HOH HOH B . 
U 7 HOH 227 1027 68   HOH HOH B . 
U 7 HOH 228 1028 737  HOH HOH B . 
U 7 HOH 229 1029 361  HOH HOH B . 
U 7 HOH 230 1030 489  HOH HOH B . 
U 7 HOH 231 1031 191  HOH HOH B . 
U 7 HOH 232 1032 840  HOH HOH B . 
U 7 HOH 233 1033 804  HOH HOH B . 
U 7 HOH 234 1034 784  HOH HOH B . 
U 7 HOH 235 1035 711  HOH HOH B . 
U 7 HOH 236 1036 578  HOH HOH B . 
U 7 HOH 237 1037 1019 HOH HOH B . 
U 7 HOH 238 1038 738  HOH HOH B . 
U 7 HOH 239 1039 735  HOH HOH B . 
U 7 HOH 240 1040 749  HOH HOH B . 
U 7 HOH 241 1041 47   HOH HOH B . 
U 7 HOH 242 1042 994  HOH HOH B . 
U 7 HOH 243 1043 205  HOH HOH B . 
U 7 HOH 244 1044 1016 HOH HOH B . 
U 7 HOH 245 1045 1275 HOH HOH B . 
U 7 HOH 246 1046 987  HOH HOH B . 
U 7 HOH 247 1047 701  HOH HOH B . 
U 7 HOH 248 1048 637  HOH HOH B . 
U 7 HOH 249 1049 874  HOH HOH B . 
U 7 HOH 250 1050 616  HOH HOH B . 
U 7 HOH 251 1051 524  HOH HOH B . 
U 7 HOH 252 1052 347  HOH HOH B . 
U 7 HOH 253 1053 733  HOH HOH B . 
U 7 HOH 254 1054 73   HOH HOH B . 
U 7 HOH 255 1055 793  HOH HOH B . 
U 7 HOH 256 1056 814  HOH HOH B . 
U 7 HOH 257 1057 811  HOH HOH B . 
U 7 HOH 258 1058 1213 HOH HOH B . 
U 7 HOH 259 1059 496  HOH HOH B . 
U 7 HOH 260 1060 502  HOH HOH B . 
U 7 HOH 261 1061 718  HOH HOH B . 
U 7 HOH 262 1062 404  HOH HOH B . 
U 7 HOH 263 1063 338  HOH HOH B . 
U 7 HOH 264 1064 610  HOH HOH B . 
U 7 HOH 265 1065 635  HOH HOH B . 
U 7 HOH 266 1066 1121 HOH HOH B . 
U 7 HOH 267 1067 540  HOH HOH B . 
U 7 HOH 268 1068 795  HOH HOH B . 
U 7 HOH 269 1069 216  HOH HOH B . 
U 7 HOH 270 1070 824  HOH HOH B . 
U 7 HOH 271 1071 571  HOH HOH B . 
U 7 HOH 272 1072 1038 HOH HOH B . 
U 7 HOH 273 1073 302  HOH HOH B . 
U 7 HOH 274 1074 809  HOH HOH B . 
U 7 HOH 275 1075 559  HOH HOH B . 
U 7 HOH 276 1076 1008 HOH HOH B . 
U 7 HOH 277 1077 1000 HOH HOH B . 
U 7 HOH 278 1078 662  HOH HOH B . 
U 7 HOH 279 1079 309  HOH HOH B . 
U 7 HOH 280 1080 835  HOH HOH B . 
U 7 HOH 281 1081 806  HOH HOH B . 
U 7 HOH 282 1082 757  HOH HOH B . 
U 7 HOH 283 1083 1071 HOH HOH B . 
U 7 HOH 284 1084 488  HOH HOH B . 
U 7 HOH 285 1085 709  HOH HOH B . 
U 7 HOH 286 1086 1246 HOH HOH B . 
U 7 HOH 287 1087 462  HOH HOH B . 
U 7 HOH 288 1088 744  HOH HOH B . 
U 7 HOH 289 1089 1068 HOH HOH B . 
U 7 HOH 290 1090 620  HOH HOH B . 
U 7 HOH 291 1091 519  HOH HOH B . 
U 7 HOH 292 1092 1003 HOH HOH B . 
U 7 HOH 293 1093 594  HOH HOH B . 
U 7 HOH 294 1094 433  HOH HOH B . 
U 7 HOH 295 1095 818  HOH HOH B . 
U 7 HOH 296 1096 834  HOH HOH B . 
U 7 HOH 297 1097 1140 HOH HOH B . 
U 7 HOH 298 1098 503  HOH HOH B . 
U 7 HOH 299 1099 440  HOH HOH B . 
U 7 HOH 300 1100 815  HOH HOH B . 
U 7 HOH 301 1101 816  HOH HOH B . 
U 7 HOH 302 1102 1159 HOH HOH B . 
U 7 HOH 303 1103 724  HOH HOH B . 
U 7 HOH 304 1104 776  HOH HOH B . 
U 7 HOH 305 1105 1049 HOH HOH B . 
U 7 HOH 306 1106 991  HOH HOH B . 
U 7 HOH 307 1107 351  HOH HOH B . 
U 7 HOH 308 1108 122  HOH HOH B . 
U 7 HOH 309 1109 579  HOH HOH B . 
U 7 HOH 310 1110 598  HOH HOH B . 
U 7 HOH 311 1111 671  HOH HOH B . 
U 7 HOH 312 1112 379  HOH HOH B . 
U 7 HOH 313 1113 830  HOH HOH B . 
U 7 HOH 314 1114 1031 HOH HOH B . 
U 7 HOH 315 1115 608  HOH HOH B . 
U 7 HOH 316 1116 113  HOH HOH B . 
U 7 HOH 317 1117 689  HOH HOH B . 
U 7 HOH 318 1118 764  HOH HOH B . 
U 7 HOH 319 1119 700  HOH HOH B . 
U 7 HOH 320 1120 797  HOH HOH B . 
U 7 HOH 321 1121 838  HOH HOH B . 
U 7 HOH 322 1122 727  HOH HOH B . 
U 7 HOH 323 1123 958  HOH HOH B . 
U 7 HOH 324 1124 577  HOH HOH B . 
U 7 HOH 325 1125 240  HOH HOH B . 
U 7 HOH 326 1126 224  HOH HOH B . 
U 7 HOH 327 1127 127  HOH HOH B . 
U 7 HOH 328 1128 682  HOH HOH B . 
U 7 HOH 329 1129 390  HOH HOH B . 
U 7 HOH 330 1130 587  HOH HOH B . 
U 7 HOH 331 1131 997  HOH HOH B . 
U 7 HOH 332 1132 710  HOH HOH B . 
U 7 HOH 333 1133 1044 HOH HOH B . 
U 7 HOH 334 1134 345  HOH HOH B . 
U 7 HOH 335 1135 146  HOH HOH B . 
U 7 HOH 336 1136 586  HOH HOH B . 
U 7 HOH 337 1137 777  HOH HOH B . 
U 7 HOH 338 1138 1075 HOH HOH B . 
U 7 HOH 339 1139 298  HOH HOH B . 
U 7 HOH 340 1140 395  HOH HOH B . 
U 7 HOH 341 1141 434  HOH HOH B . 
U 7 HOH 342 1142 1017 HOH HOH B . 
U 7 HOH 343 1143 783  HOH HOH B . 
U 7 HOH 344 1144 752  HOH HOH B . 
U 7 HOH 345 1145 794  HOH HOH B . 
U 7 HOH 346 1146 438  HOH HOH B . 
U 7 HOH 347 1147 798  HOH HOH B . 
U 7 HOH 348 1148 444  HOH HOH B . 
U 7 HOH 349 1149 1322 HOH HOH B . 
U 7 HOH 350 1150 1099 HOH HOH B . 
U 7 HOH 351 1151 401  HOH HOH B . 
U 7 HOH 352 1152 972  HOH HOH B . 
U 7 HOH 353 1153 1032 HOH HOH B . 
U 7 HOH 354 1154 1037 HOH HOH B . 
U 7 HOH 355 1155 726  HOH HOH B . 
U 7 HOH 356 1156 768  HOH HOH B . 
U 7 HOH 357 1157 1062 HOH HOH B . 
U 7 HOH 358 1158 993  HOH HOH B . 
U 7 HOH 359 1159 92   HOH HOH B . 
U 7 HOH 360 1160 1260 HOH HOH B . 
U 7 HOH 361 1161 235  HOH HOH B . 
U 7 HOH 362 1162 660  HOH HOH B . 
U 7 HOH 363 1163 106  HOH HOH B . 
U 7 HOH 364 1164 955  HOH HOH B . 
U 7 HOH 365 1165 813  HOH HOH B . 
U 7 HOH 366 1166 1123 HOH HOH B . 
U 7 HOH 367 1167 470  HOH HOH B . 
U 7 HOH 368 1168 676  HOH HOH B . 
U 7 HOH 369 1169 1294 HOH HOH B . 
U 7 HOH 370 1170 803  HOH HOH B . 
U 7 HOH 371 1171 102  HOH HOH B . 
U 7 HOH 372 1172 631  HOH HOH B . 
U 7 HOH 373 1173 935  HOH HOH B . 
U 7 HOH 374 1174 668  HOH HOH B . 
U 7 HOH 375 1175 714  HOH HOH B . 
U 7 HOH 376 1176 453  HOH HOH B . 
U 7 HOH 377 1177 193  HOH HOH B . 
U 7 HOH 378 1178 1066 HOH HOH B . 
U 7 HOH 379 1179 770  HOH HOH B . 
U 7 HOH 380 1180 375  HOH HOH B . 
U 7 HOH 381 1181 789  HOH HOH B . 
U 7 HOH 382 1182 962  HOH HOH B . 
U 7 HOH 383 1183 978  HOH HOH B . 
U 7 HOH 384 1184 605  HOH HOH B . 
U 7 HOH 385 1185 728  HOH HOH B . 
U 7 HOH 386 1186 328  HOH HOH B . 
U 7 HOH 387 1187 162  HOH HOH B . 
U 7 HOH 388 1188 750  HOH HOH B . 
U 7 HOH 389 1189 1095 HOH HOH B . 
U 7 HOH 390 1190 873  HOH HOH B . 
U 7 HOH 391 1191 1174 HOH HOH B . 
U 7 HOH 392 1192 373  HOH HOH B . 
U 7 HOH 393 1193 82   HOH HOH B . 
U 7 HOH 394 1194 801  HOH HOH B . 
U 7 HOH 395 1195 499  HOH HOH B . 
U 7 HOH 396 1196 1309 HOH HOH B . 
U 7 HOH 397 1197 712  HOH HOH B . 
U 7 HOH 398 1198 248  HOH HOH B . 
U 7 HOH 399 1199 791  HOH HOH B . 
U 7 HOH 400 1200 734  HOH HOH B . 
U 7 HOH 401 1201 748  HOH HOH B . 
U 7 HOH 402 1202 939  HOH HOH B . 
U 7 HOH 403 1203 729  HOH HOH B . 
U 7 HOH 404 1204 708  HOH HOH B . 
U 7 HOH 405 1205 1278 HOH HOH B . 
U 7 HOH 406 1206 21   HOH HOH B . 
U 7 HOH 407 1207 688  HOH HOH B . 
U 7 HOH 408 1208 1327 HOH HOH B . 
U 7 HOH 409 1209 963  HOH HOH B . 
U 7 HOH 410 1210 766  HOH HOH B . 
U 7 HOH 411 1211 826  HOH HOH B . 
U 7 HOH 412 1212 1319 HOH HOH B . 
U 7 HOH 413 1213 680  HOH HOH B . 
U 7 HOH 414 1214 686  HOH HOH B . 
U 7 HOH 415 1215 609  HOH HOH B . 
U 7 HOH 416 1216 1128 HOH HOH B . 
U 7 HOH 417 1217 94   HOH HOH B . 
U 7 HOH 418 1218 945  HOH HOH B . 
U 7 HOH 419 1219 841  HOH HOH B . 
U 7 HOH 420 1220 754  HOH HOH B . 
U 7 HOH 421 1221 1118 HOH HOH B . 
U 7 HOH 422 1222 593  HOH HOH B . 
U 7 HOH 423 1223 411  HOH HOH B . 
U 7 HOH 424 1224 51   HOH HOH B . 
U 7 HOH 425 1225 651  HOH HOH B . 
U 7 HOH 426 1226 614  HOH HOH B . 
U 7 HOH 427 1227 670  HOH HOH B . 
U 7 HOH 428 1228 522  HOH HOH B . 
U 7 HOH 429 1229 199  HOH HOH B . 
U 7 HOH 430 1230 799  HOH HOH B . 
U 7 HOH 431 1231 619  HOH HOH B . 
U 7 HOH 432 1232 1318 HOH HOH B . 
U 7 HOH 433 1233 611  HOH HOH B . 
U 7 HOH 434 1234 640  HOH HOH B . 
U 7 HOH 435 1235 1288 HOH HOH B . 
U 7 HOH 436 1236 825  HOH HOH B . 
U 7 HOH 437 1237 606  HOH HOH B . 
U 7 HOH 438 1238 980  HOH HOH B . 
U 7 HOH 439 1239 100  HOH HOH B . 
U 7 HOH 440 1240 1002 HOH HOH B . 
U 7 HOH 441 1241 441  HOH HOH B . 
U 7 HOH 442 1242 1079 HOH HOH B . 
U 7 HOH 443 1243 1273 HOH HOH B . 
U 7 HOH 444 1244 1244 HOH HOH B . 
U 7 HOH 445 1245 762  HOH HOH B . 
U 7 HOH 446 1246 645  HOH HOH B . 
U 7 HOH 447 1247 531  HOH HOH B . 
U 7 HOH 448 1248 555  HOH HOH B . 
U 7 HOH 449 1249 828  HOH HOH B . 
U 7 HOH 450 1250 2    HOH HOH B . 
U 7 HOH 451 1251 377  HOH HOH B . 
U 7 HOH 452 1252 655  HOH HOH B . 
U 7 HOH 453 1253 1126 HOH HOH B . 
U 7 HOH 454 1254 319  HOH HOH B . 
U 7 HOH 455 1255 74   HOH HOH B . 
U 7 HOH 456 1256 788  HOH HOH B . 
U 7 HOH 457 1257 695  HOH HOH B . 
U 7 HOH 458 1258 661  HOH HOH B . 
U 7 HOH 459 1259 590  HOH HOH B . 
U 7 HOH 460 1260 643  HOH HOH B . 
U 7 HOH 461 1261 796  HOH HOH B . 
U 7 HOH 462 1262 934  HOH HOH B . 
U 7 HOH 463 1263 685  HOH HOH B . 
U 7 HOH 464 1264 1307 HOH HOH B . 
U 7 HOH 465 1265 1100 HOH HOH B . 
U 7 HOH 466 1266 1274 HOH HOH B . 
U 7 HOH 467 1267 399  HOH HOH B . 
U 7 HOH 468 1268 360  HOH HOH B . 
U 7 HOH 469 1269 464  HOH HOH B . 
U 7 HOH 470 1270 1249 HOH HOH B . 
U 7 HOH 471 1271 622  HOH HOH B . 
U 7 HOH 472 1272 1306 HOH HOH B . 
U 7 HOH 473 1273 756  HOH HOH B . 
U 7 HOH 474 1274 772  HOH HOH B . 
U 7 HOH 475 1275 185  HOH HOH B . 
U 7 HOH 476 1276 630  HOH HOH B . 
U 7 HOH 477 1277 989  HOH HOH B . 
U 7 HOH 478 1278 1272 HOH HOH B . 
U 7 HOH 479 1279 1187 HOH HOH B . 
U 7 HOH 480 1280 487  HOH HOH B . 
U 7 HOH 481 1281 759  HOH HOH B . 
U 7 HOH 482 1282 415  HOH HOH B . 
U 7 HOH 483 1283 327  HOH HOH B . 
U 7 HOH 484 1284 1255 HOH HOH B . 
U 7 HOH 485 1285 1276 HOH HOH B . 
U 7 HOH 486 1286 1252 HOH HOH B . 
U 7 HOH 487 1287 1241 HOH HOH B . 
U 7 HOH 488 1288 846  HOH HOH B . 
U 7 HOH 489 1289 805  HOH HOH B . 
U 7 HOH 490 1290 988  HOH HOH B . 
U 7 HOH 491 1291 1190 HOH HOH B . 
U 7 HOH 492 1292 1232 HOH HOH B . 
U 7 HOH 493 1293 1077 HOH HOH B . 
U 7 HOH 494 1294 1001 HOH HOH B . 
U 7 HOH 495 1295 765  HOH HOH B . 
U 7 HOH 496 1296 1266 HOH HOH B . 
U 7 HOH 497 1297 800  HOH HOH B . 
U 7 HOH 498 1298 769  HOH HOH B . 
U 7 HOH 499 1299 1235 HOH HOH B . 
U 7 HOH 500 1300 1    HOH HOH B . 
U 7 HOH 501 1301 719  HOH HOH B . 
U 7 HOH 502 1302 1270 HOH HOH B . 
U 7 HOH 503 1303 1248 HOH HOH B . 
U 7 HOH 504 1304 839  HOH HOH B . 
U 7 HOH 505 1305 954  HOH HOH B . 
U 7 HOH 506 1306 318  HOH HOH B . 
U 7 HOH 507 1307 72   HOH HOH B . 
U 7 HOH 508 1308 121  HOH HOH B . 
U 7 HOH 509 1309 943  HOH HOH B . 
U 7 HOH 510 1310 1006 HOH HOH B . 
U 7 HOH 511 1311 650  HOH HOH B . 
U 7 HOH 512 1312 1132 HOH HOH B . 
U 7 HOH 513 1313 774  HOH HOH B . 
U 7 HOH 514 1314 114  HOH HOH B . 
U 7 HOH 515 1315 202  HOH HOH B . 
U 7 HOH 516 1316 753  HOH HOH B . 
U 7 HOH 517 1317 155  HOH HOH B . 
U 7 HOH 518 1318 1271 HOH HOH B . 
U 7 HOH 519 1319 836  HOH HOH B . 
U 7 HOH 520 1320 90   HOH HOH B . 
U 7 HOH 521 1321 1289 HOH HOH B . 
U 7 HOH 522 1322 812  HOH HOH B . 
U 7 HOH 523 1323 175  HOH HOH B . 
U 7 HOH 524 1324 1119 HOH HOH B . 
U 7 HOH 525 1325 751  HOH HOH B . 
U 7 HOH 526 1326 455  HOH HOH B . 
U 7 HOH 527 1327 1074 HOH HOH B . 
U 7 HOH 528 1328 1163 HOH HOH B . 
U 7 HOH 529 1329 270  HOH HOH B . 
U 7 HOH 530 1330 638  HOH HOH B . 
U 7 HOH 531 1331 644  HOH HOH B . 
U 7 HOH 532 1332 992  HOH HOH B . 
U 7 HOH 533 1333 1051 HOH HOH B . 
U 7 HOH 534 1334 285  HOH HOH B . 
U 7 HOH 535 1335 1210 HOH HOH B . 
U 7 HOH 536 1336 1267 HOH HOH B . 
U 7 HOH 537 1337 460  HOH HOH B . 
U 7 HOH 538 1338 868  HOH HOH B . 
U 7 HOH 539 1339 722  HOH HOH B . 
U 7 HOH 540 1340 1250 HOH HOH B . 
U 7 HOH 541 1341 1325 HOH HOH B . 
U 7 HOH 542 1342 831  HOH HOH B . 
U 7 HOH 543 1343 1096 HOH HOH B . 
U 7 HOH 544 1344 947  HOH HOH B . 
U 7 HOH 545 1345 625  HOH HOH B . 
U 7 HOH 546 1346 1129 HOH HOH B . 
U 7 HOH 547 1347 95   HOH HOH B . 
U 7 HOH 548 1348 1298 HOH HOH B . 
U 7 HOH 549 1349 723  HOH HOH B . 
U 7 HOH 550 1350 785  HOH HOH B . 
U 7 HOH 551 1351 513  HOH HOH B . 
U 7 HOH 552 1352 1089 HOH HOH B . 
U 7 HOH 553 1353 747  HOH HOH B . 
U 7 HOH 554 1354 998  HOH HOH B . 
U 7 HOH 555 1355 339  HOH HOH B . 
U 7 HOH 556 1356 698  HOH HOH B . 
U 7 HOH 557 1357 1254 HOH HOH B . 
U 7 HOH 558 1358 999  HOH HOH B . 
U 7 HOH 559 1359 282  HOH HOH B . 
U 7 HOH 560 1360 746  HOH HOH B . 
U 7 HOH 561 1361 83   HOH HOH B . 
U 7 HOH 562 1362 847  HOH HOH B . 
U 7 HOH 563 1363 1261 HOH HOH B . 
U 7 HOH 564 1364 1112 HOH HOH B . 
U 7 HOH 565 1365 466  HOH HOH B . 
U 7 HOH 566 1366 507  HOH HOH B . 
U 7 HOH 567 1367 115  HOH HOH B . 
U 7 HOH 568 1368 1277 HOH HOH B . 
U 7 HOH 569 1369 469  HOH HOH B . 
U 7 HOH 570 1370 1167 HOH HOH B . 
U 7 HOH 571 1371 1205 HOH HOH B . 
U 7 HOH 572 1372 1223 HOH HOH B . 
U 7 HOH 573 1373 990  HOH HOH B . 
U 7 HOH 574 1374 389  HOH HOH B . 
U 7 HOH 575 1375 108  HOH HOH B . 
U 7 HOH 576 1376 1020 HOH HOH B . 
U 7 HOH 577 1377 378  HOH HOH B . 
U 7 HOH 578 1378 508  HOH HOH B . 
U 7 HOH 579 1379 1264 HOH HOH B . 
U 7 HOH 580 1380 1321 HOH HOH B . 
U 7 HOH 581 1381 986  HOH HOH B . 
U 7 HOH 582 1382 1055 HOH HOH B . 
U 7 HOH 583 1383 942  HOH HOH B . 
U 7 HOH 584 1384 657  HOH HOH B . 
U 7 HOH 585 1385 976  HOH HOH B . 
U 7 HOH 586 1386 569  HOH HOH B . 
U 7 HOH 587 1387 279  HOH HOH B . 
U 7 HOH 588 1388 1039 HOH HOH B . 
U 7 HOH 589 1389 585  HOH HOH B . 
U 7 HOH 590 1390 1052 HOH HOH B . 
U 7 HOH 591 1391 600  HOH HOH B . 
U 7 HOH 592 1392 570  HOH HOH B . 
U 7 HOH 593 1393 1007 HOH HOH B . 
U 7 HOH 594 1394 530  HOH HOH B . 
U 7 HOH 595 1395 165  HOH HOH B . 
U 7 HOH 596 1396 1200 HOH HOH B . 
U 7 HOH 597 1397 1251 HOH HOH B . 
U 7 HOH 598 1398 93   HOH HOH B . 
U 7 HOH 599 1399 985  HOH HOH B . 
U 7 HOH 600 1400 1135 HOH HOH B . 
U 7 HOH 601 1401 424  HOH HOH B . 
U 7 HOH 602 1402 706  HOH HOH B . 
U 7 HOH 603 1403 964  HOH HOH B . 
U 7 HOH 604 1404 1263 HOH HOH B . 
U 7 HOH 605 1405 322  HOH HOH B . 
U 7 HOH 606 1406 334  HOH HOH B . 
U 7 HOH 607 1407 928  HOH HOH B . 
U 7 HOH 608 1408 1154 HOH HOH B . 
U 7 HOH 609 1409 1207 HOH HOH B . 
U 7 HOH 610 1410 132  HOH HOH B . 
U 7 HOH 611 1411 703  HOH HOH B . 
U 7 HOH 612 1412 410  HOH HOH B . 
U 7 HOH 613 1413 1303 HOH HOH B . 
U 7 HOH 614 1414 1308 HOH HOH B . 
U 7 HOH 615 1415 1183 HOH HOH B . 
U 7 HOH 616 1416 1259 HOH HOH B . 
U 7 HOH 617 1417 576  HOH HOH B . 
U 7 HOH 618 1418 1256 HOH HOH B . 
U 7 HOH 619 1419 742  HOH HOH B . 
U 7 HOH 620 1420 916  HOH HOH B . 
U 7 HOH 621 1421 454  HOH HOH B . 
U 7 HOH 622 1422 969  HOH HOH B . 
U 7 HOH 623 1423 1060 HOH HOH B . 
U 7 HOH 624 1424 452  HOH HOH B . 
U 7 HOH 625 1425 1238 HOH HOH B . 
U 7 HOH 626 1426 1243 HOH HOH B . 
U 7 HOH 627 1427 539  HOH HOH B . 
U 7 HOH 628 1428 741  HOH HOH B . 
U 7 HOH 629 1429 675  HOH HOH B . 
U 7 HOH 630 1430 967  HOH HOH B . 
U 7 HOH 631 1431 632  HOH HOH B . 
U 7 HOH 632 1432 386  HOH HOH B . 
U 7 HOH 633 1433 1186 HOH HOH B . 
U 7 HOH 634 1434 348  HOH HOH B . 
U 7 HOH 635 1435 414  HOH HOH B . 
U 7 HOH 636 1436 479  HOH HOH B . 
U 7 HOH 637 1437 75   HOH HOH B . 
U 7 HOH 638 1438 1011 HOH HOH B . 
U 7 HOH 639 1439 974  HOH HOH B . 
U 7 HOH 640 1440 1258 HOH HOH B . 
U 7 HOH 641 1441 843  HOH HOH B . 
U 7 HOH 642 1442 780  HOH HOH B . 
U 7 HOH 643 1443 906  HOH HOH B . 
U 7 HOH 644 1444 819  HOH HOH B . 
U 7 HOH 645 1445 681  HOH HOH B . 
U 7 HOH 646 1446 924  HOH HOH B . 
U 7 HOH 647 1447 833  HOH HOH B . 
U 7 HOH 648 1448 1175 HOH HOH B . 
U 7 HOH 649 1449 1302 HOH HOH B . 
U 7 HOH 650 1450 1195 HOH HOH B . 
U 7 HOH 651 1451 435  HOH HOH B . 
U 7 HOH 652 1452 1050 HOH HOH B . 
U 7 HOH 653 1453 1053 HOH HOH B . 
U 7 HOH 654 1454 573  HOH HOH B . 
U 7 HOH 655 1455 607  HOH HOH B . 
U 7 HOH 656 1456 1269 HOH HOH B . 
U 7 HOH 657 1457 664  HOH HOH B . 
U 7 HOH 658 1458 1130 HOH HOH B . 
U 7 HOH 659 1459 1046 HOH HOH B . 
U 7 HOH 660 1460 1221 HOH HOH B . 
U 7 HOH 661 1461 1117 HOH HOH B . 
U 7 HOH 662 1462 1239 HOH HOH B . 
U 7 HOH 663 1463 1247 HOH HOH B . 
U 7 HOH 664 1464 1107 HOH HOH B . 
U 7 HOH 665 1465 603  HOH HOH B . 
U 7 HOH 666 1466 491  HOH HOH B . 
U 7 HOH 667 1467 1057 HOH HOH B . 
U 7 HOH 668 1468 541  HOH HOH B . 
U 7 HOH 669 1469 413  HOH HOH B . 
U 7 HOH 670 1470 1131 HOH HOH B . 
U 7 HOH 671 1471 848  HOH HOH B . 
U 7 HOH 672 1472 89   HOH HOH B . 
U 7 HOH 673 1473 792  HOH HOH B . 
U 7 HOH 674 1474 65   HOH HOH B . 
U 7 HOH 675 1475 1158 HOH HOH B . 
U 7 HOH 676 1476 639  HOH HOH B . 
U 7 HOH 677 1477 510  HOH HOH B . 
U 7 HOH 678 1478 1228 HOH HOH B . 
U 7 HOH 679 1479 656  HOH HOH B . 
U 7 HOH 680 1480 397  HOH HOH B . 
U 7 HOH 681 1481 1184 HOH HOH B . 
U 7 HOH 682 1482 1226 HOH HOH B . 
U 7 HOH 683 1483 394  HOH HOH B . 
U 7 HOH 684 1484 1240 HOH HOH B . 
U 7 HOH 685 1485 923  HOH HOH B . 
U 7 HOH 686 1486 697  HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 0 A LYS 34  ? NZ  ? A LYS 25  NZ  
2  1 Y 0 A LYS 36  ? CG  ? A LYS 27  CG  
3  1 Y 0 A LYS 36  ? CD  ? A LYS 27  CD  
4  1 Y 0 A LYS 36  ? CE  ? A LYS 27  CE  
5  1 Y 0 A LYS 36  ? NZ  ? A LYS 27  NZ  
6  1 Y 0 A ASP 123 ? CG  ? A ASP 114 CG  
7  1 Y 0 A ASP 123 ? OD1 ? A ASP 114 OD1 
8  1 Y 0 A ASP 123 ? OD2 ? A ASP 114 OD2 
9  1 Y 0 A TYR 133 ? CG  ? A TYR 124 CG  
10 1 Y 0 A TYR 133 ? CD1 ? A TYR 124 CD1 
11 1 Y 0 A TYR 133 ? CD2 ? A TYR 124 CD2 
12 1 Y 0 A TYR 133 ? CE1 ? A TYR 124 CE1 
13 1 Y 0 A TYR 133 ? CE2 ? A TYR 124 CE2 
14 1 Y 0 A TYR 133 ? CZ  ? A TYR 124 CZ  
15 1 Y 0 A TYR 133 ? OH  ? A TYR 124 OH  
16 1 Y 0 A MET 134 ? CG  ? A MET 125 CG  
17 1 Y 0 A MET 134 ? SD  ? A MET 125 SD  
18 1 Y 0 A MET 134 ? CE  ? A MET 125 CE  
19 1 Y 0 A ARG 135 ? CD  ? A ARG 126 CD  
20 1 Y 0 A ARG 135 ? NE  ? A ARG 126 NE  
21 1 Y 0 A ARG 135 ? CZ  ? A ARG 126 CZ  
22 1 Y 0 A ARG 135 ? NH1 ? A ARG 126 NH1 
23 1 Y 0 A ARG 135 ? NH2 ? A ARG 126 NH2 
24 1 Y 0 A LYS 136 ? CD  ? A LYS 127 CD  
25 1 Y 0 A LYS 136 ? CE  ? A LYS 127 CE  
26 1 Y 0 A LYS 136 ? NZ  ? A LYS 127 NZ  
27 1 Y 0 A LYS 162 ? NZ  ? A LYS 153 NZ  
28 1 Y 0 A LYS 342 ? NZ  ? A LYS 333 NZ  
29 1 Y 0 A LYS 370 ? CE  ? A LYS 361 CE  
30 1 Y 0 A LYS 370 ? NZ  ? A LYS 361 NZ  
31 1 Y 0 A LYS 445 ? CE  ? A LYS 436 CE  
32 1 Y 0 A LYS 445 ? NZ  ? A LYS 436 NZ  
33 1 Y 0 A GLU 451 ? CG  ? A GLU 442 CG  
34 1 Y 0 A GLU 451 ? CD  ? A GLU 442 CD  
35 1 Y 0 A GLU 451 ? OE1 ? A GLU 442 OE1 
36 1 Y 0 A GLU 451 ? OE2 ? A GLU 442 OE2 
37 1 Y 0 A PRO 452 ? CG  ? A PRO 443 CG  
38 1 Y 0 A PRO 452 ? CD  ? A PRO 443 CD  
39 1 Y 0 A ASP 453 ? CG  ? A ASP 444 CG  
40 1 Y 0 A ASP 453 ? OD1 ? A ASP 444 OD1 
41 1 Y 0 A ASP 453 ? OD2 ? A ASP 444 OD2 
42 1 Y 0 A ASN 454 ? CG  ? A ASN 445 CG  
43 1 Y 0 A ASN 454 ? OD1 ? A ASN 445 OD1 
44 1 Y 0 A ASN 454 ? ND2 ? A ASN 445 ND2 
45 1 Y 0 A SER 455 ? OG  ? A SER 446 OG  
46 1 Y 0 A SER 457 ? OG  ? A SER 448 OG  
47 1 Y 0 A LYS 531 ? CE  ? A LYS 522 CE  
48 1 Y 0 A LYS 531 ? NZ  ? A LYS 522 NZ  
49 1 Y 0 A LYS 559 ? CE  ? A LYS 550 CE  
50 1 Y 0 A LYS 559 ? NZ  ? A LYS 550 NZ  
51 1 Y 0 A ASN 580 ? OD1 ? A ASN 571 OD1 
52 1 Y 0 A ASN 580 ? ND2 ? A ASN 571 ND2 
53 1 Y 0 A LYS 647 ? NZ  ? A LYS 638 NZ  
54 1 Y 0 B ASP 123 ? CG  ? B ASP 114 CG  
55 1 Y 0 B ASP 123 ? OD1 ? B ASP 114 OD1 
56 1 Y 0 B ASP 123 ? OD2 ? B ASP 114 OD2 
57 1 Y 0 B ASN 125 ? CG  ? B ASN 116 CG  
58 1 Y 0 B ASN 125 ? OD1 ? B ASN 116 OD1 
59 1 Y 0 B ASN 125 ? ND2 ? B ASN 116 ND2 
60 1 Y 0 B ASN 131 ? CG  ? B ASN 122 CG  
61 1 Y 0 B ASN 131 ? OD1 ? B ASN 122 OD1 
62 1 Y 0 B ASN 131 ? ND2 ? B ASN 122 ND2 
63 1 Y 0 B GLU 132 ? CG  ? B GLU 123 CG  
64 1 Y 0 B GLU 132 ? CD  ? B GLU 123 CD  
65 1 Y 0 B GLU 132 ? OE1 ? B GLU 123 OE1 
66 1 Y 0 B GLU 132 ? OE2 ? B GLU 123 OE2 
67 1 Y 0 B TYR 133 ? CG  ? B TYR 124 CG  
68 1 Y 0 B TYR 133 ? CD1 ? B TYR 124 CD1 
69 1 Y 0 B TYR 133 ? CD2 ? B TYR 124 CD2 
70 1 Y 0 B TYR 133 ? CE1 ? B TYR 124 CE1 
71 1 Y 0 B TYR 133 ? CE2 ? B TYR 124 CE2 
72 1 Y 0 B TYR 133 ? CZ  ? B TYR 124 CZ  
73 1 Y 0 B TYR 133 ? OH  ? B TYR 124 OH  
74 1 Y 0 B MET 134 ? CG  ? B MET 125 CG  
75 1 Y 0 B MET 134 ? SD  ? B MET 125 SD  
76 1 Y 0 B MET 134 ? CE  ? B MET 125 CE  
77 1 Y 0 B LYS 136 ? NZ  ? B LYS 127 NZ  
78 1 Y 0 B LYS 162 ? NZ  ? B LYS 153 NZ  
79 1 Y 0 B LYS 342 ? NZ  ? B LYS 333 NZ  
80 1 Y 0 B LYS 347 ? CE  ? B LYS 338 CE  
81 1 Y 0 B LYS 347 ? NZ  ? B LYS 338 NZ  
82 1 Y 0 B LYS 445 ? CE  ? B LYS 436 CE  
83 1 Y 0 B LYS 445 ? NZ  ? B LYS 436 NZ  
84 1 Y 0 B GLU 451 ? CG  ? B GLU 442 CG  
85 1 Y 0 B GLU 451 ? CD  ? B GLU 442 CD  
86 1 Y 0 B GLU 451 ? OE1 ? B GLU 442 OE1 
87 1 Y 0 B GLU 451 ? OE2 ? B GLU 442 OE2 
88 1 Y 0 B ASN 454 ? CG  ? B ASN 445 CG  
89 1 Y 0 B ASN 454 ? OD1 ? B ASN 445 OD1 
90 1 Y 0 B ASN 454 ? ND2 ? B ASN 445 ND2 
91 1 Y 0 B SER 455 ? OG  ? B SER 446 OG  
92 1 Y 0 B SER 546 ? N   ? B SER 537 N   
93 1 Y 0 B SER 546 ? CB  ? B SER 537 CB  
94 1 Y 0 B SER 546 ? OG  ? B SER 537 OG  
95 1 Y 0 B ASP 617 ? CG  ? B ASP 608 CG  
96 1 Y 0 B ASP 617 ? OD1 ? B ASP 608 OD1 
97 1 Y 0 B ASP 617 ? OD2 ? B ASP 608 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       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5 1 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? . 2 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? SHELXDE ? ? ? . 3 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? ARP     ? ? ? . 4 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? . 5 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? . 6 
? refinement       ? ? ? ? ? ? ? ? ? ? ? MAIN    ? ? ? . 7 
# 
_cell.length_a           91.357 
_cell.length_b           212.916 
_cell.length_c           84.931 
_cell.angle_alpha        90.000 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.entry_id           5J72 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_symmetry.entry_id                         5J72 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
# 
_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                   5J72 
_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            2.98 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         58.72 
_exptl_crystal.description                 cubic 
_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_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            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '1.6 M trisodium citrate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
loop_
_diffrn.ambient_environment 
_diffrn.ambient_temp 
_diffrn.ambient_temp_details 
_diffrn.ambient_temp_esd 
_diffrn.crystal_id 
_diffrn.crystal_support 
_diffrn.crystal_treatment 
_diffrn.details 
_diffrn.id 
_diffrn.ambient_pressure 
_diffrn.ambient_pressure_esd 
_diffrn.ambient_pressure_gt 
_diffrn.ambient_pressure_lt 
_diffrn.ambient_temp_gt 
_diffrn.ambient_temp_lt 
? 100 ? ? 1 ? ? ? 1 ? ? ? ? ? ? 
? 100 ? ? 1 ? ? ? 2 ? ? ? ? ? ? 
# 
loop_
_diffrn_detector.details 
_diffrn_detector.detector 
_diffrn_detector.diffrn_id 
_diffrn_detector.type 
_diffrn_detector.area_resol_mean 
_diffrn_detector.dtime 
_diffrn_detector.pdbx_frames_total 
_diffrn_detector.pdbx_collection_time_total 
_diffrn_detector.pdbx_collection_date 
? PIXEL 1 'DECTRIS PILATUS 6M' ? ? ? ? 2013-07-02 
? PIXEL 2 'DECTRIS PILATUS 6M' ? ? ? ? 2015-05-26 
# 
loop_
_diffrn_radiation.collimation 
_diffrn_radiation.diffrn_id 
_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 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l 
_diffrn_radiation.pdbx_wavelength_list 
_diffrn_radiation.pdbx_wavelength 
_diffrn_radiation.pdbx_diffrn_protocol 
_diffrn_radiation.pdbx_analyzer 
_diffrn_radiation.pdbx_scattering_type 
? 1 ? ? ? ? ? ? ? ? 1 M ? ? 'SINGLE WAVELENGTH' ? x-ray 
? 2 ? ? ? ? ? ? ? ? 2 M ? ? 'SINGLE WAVELENGTH' ? x-ray 
# 
loop_
_diffrn_radiation_wavelength.id 
_diffrn_radiation_wavelength.wavelength 
_diffrn_radiation_wavelength.wt 
1 1.282 1.0 
2 0.918 1.0 
3 1.272 1.0 
4 1.283 1.0 
5 1.379 1.0 
6 1.485 1.0 
7 1.490 1.0 
# 
loop_
_diffrn_source.current 
_diffrn_source.details 
_diffrn_source.diffrn_id 
_diffrn_source.power 
_diffrn_source.size 
_diffrn_source.source 
_diffrn_source.target 
_diffrn_source.type 
_diffrn_source.voltage 
_diffrn_source.take-off_angle 
_diffrn_source.pdbx_wavelength_list 
_diffrn_source.pdbx_wavelength 
_diffrn_source.pdbx_synchrotron_beamline 
_diffrn_source.pdbx_synchrotron_site 
? ? 1 ? ? SYNCHROTRON ? 'BESSY BEAMLINE 14.1' ? ? 1.282                                      ? 14.1 BESSY 
? ? 2 ? ? SYNCHROTRON ? 'BESSY BEAMLINE 14.1' ? ? '0.918, 1.272, 1.283, 1.379, 1.485, 1.490' ? 14.1 BESSY 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         5J72 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.7 
_reflns.d_resolution_low                 30 
_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                       180746 
_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             99.5 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  11.3 
_reflns.pdbx_Rmerge_I_obs                0.049 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  ? 
_reflns.pdbx_netI_over_av_sigmaI         ? 
_reflns.pdbx_netI_over_sigmaI            22.9 
_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_R_split                     ? 
# 
_reflns_shell.d_res_high                  . 
_reflns_shell.d_res_low                   ? 
_reflns_shell.meanI_over_sigI_all         ? 
_reflns_shell.meanI_over_sigI_obs         2 
_reflns_shell.number_measured_all         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_possible             ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.number_unique_obs           ? 
_reflns_shell.percent_possible_all        87 
_reflns_shell.percent_possible_obs        ? 
_reflns_shell.Rmerge_F_all                ? 
_reflns_shell.Rmerge_F_obs                ? 
_reflns_shell.Rmerge_I_all                ? 
_reflns_shell.Rmerge_I_obs                0.71 
_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_Rsym_value             ? 
_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_R_split                ? 
# 
_refine.entry_id                                 5J72 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.aniso_B[1][1]                            -0.953 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][2]                            -1.483 
_refine.aniso_B[2][3]                            0.000 
_refine.aniso_B[3][3]                            2.436 
_refine.B_iso_max                                166.56 
_refine.B_iso_mean                               33.10 
_refine.B_iso_min                                12.76 
_refine.correlation_coeff_Fo_to_Fc               0.9677 
_refine.correlation_coeff_Fo_to_Fc_free          0.9611 
_refine.details                                  ? 
_refine.ls_d_res_high                            1.70 
_refine.ls_d_res_low                             29.85 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     180744 
_refine.ls_number_reflns_R_free                  180746 
_refine.ls_number_reflns_R_work                  180744 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    100.00 
_refine.ls_percent_reflns_R_free                 100.00 
_refine.ls_R_factor_all                          0.1785 
_refine.ls_R_factor_obs                          0.1785 
_refine.ls_R_factor_R_free                       0.2009 
_refine.ls_R_factor_R_work                       0.1785 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_ls_cross_valid_method               'FREE KICK' 
_refine.pdbx_method_to_determine_struct          SAD 
_refine.pdbx_starting_model                      'Cwp8 CWB2 trimer, 1JWQ' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            NONE 
_refine.solvent_model_details                    'MASK FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 -20.72 
_refine.solvent_model_param_ksol                 0.39 
_refine.pdbx_overall_phase_error                 21.8 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_number_parameters                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        9730 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         39 
_refine_hist.number_atoms_solvent             1329 
_refine_hist.number_atoms_total               11098 
_refine_hist.d_res_high                       1.70 
_refine_hist.d_res_low                        29.85 
# 
_refine_ls_shell.d_res_high                       1.70 
_refine_ls_shell.d_res_low                        1.73 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               1.00 
_refine_ls_shell.number_reflns_R_work             7890 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.3555 
_refine_ls_shell.R_factor_R_free                  0.3716 
_refine_ls_shell.percent_reflns_R_free            100.00 
_refine_ls_shell.number_reflns_R_free             7890 
_refine_ls_shell.number_reflns_all                7890 
_refine_ls_shell.number_reflns_obs                7890 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                     5J72 
_struct.title                        'Cwp6 from Clostridium difficile' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               ? 
# 
_struct_keywords.entry_id        5J72 
_struct_keywords.text            'amidase_3, CWB2 domain, cell wall protein, S-layer, hydrolase' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 4 ? 
H N N 4 ? 
I N N 5 ? 
J N N 2 ? 
K N N 2 ? 
L N N 2 ? 
M N N 3 ? 
N N N 3 ? 
O N N 4 ? 
P N N 4 ? 
Q N N 6 ? 
R N N 6 ? 
S N N 5 ? 
T N N 7 ? 
U N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q183L9_PEPD6 
_struct_ref.pdbx_db_accession          Q183L9 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SDININLQRKSVVLGSKSNASVKFKEKLNADSITLNFMCYDMPLEATLNYNEKTDSYEGVINYNKDPEYLNVWELQSIKI
NGKDEQKVLNKEDLESMGLNLKDYDVTQEFIISDANSTKAVNEYMRKTSAPVKKLAGATRFETAVEISKQGWKDGSSKVV
IVNGELAADGITATPLASTYDAPILLANKDDIPESTKAELKRLNPSDVIIIGDDGSVSQKAVSQIKSAVNVNVTRIGGVD
RHETSLLIAKEIDKYHDVNKIYIANGYAGEYDALNISSKAGEDQQPIILANKDSVPQGTYNWLSSQGLEEAYYIGGSQSL
SSKIIDQISKIAKNGTSKNRVSGADRHETNANVIKTFYPDKELSAMLVAKSDIIVDSITAGPLAAKLKAPILITPKTYVS
AYHSTNLSEKTAETVYQIGDGMKDSVINSIASSLSKHNAPTEPDNSGSAAGKTVVIDPGHGGSDSGATSGLNGGAQEKKY
TLNTALATTEYLRSKGINVVMTRDTDKTMALGERTALSNTIKPDLFTSIHYNASNGSGNGVEIYYKVKDKNGGTTKTAAS
NILKRILEKFNMKNRGIKTRTLDNGKDYLYVLRNNNYPAILVECAFIDNKSDMDKLNTAEKVKTMGTQIGIGIEDTVK
;
_struct_ref.pdbx_align_begin           38 
# 
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 5J72 A 1 ? 638 ? Q183L9 38 ? 675 ? 10 647 
2 1 5J72 B 1 ? 638 ? Q183L9 38 ? 675 ? 10 647 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,H,I,T       
2 1 B,J,K,L,M,N,O,P,Q,R,S,U 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASN A 90  ? MET A 97  ? ASN A 99  MET A 106 1 ? 8  
HELX_P HELX_P2  AA2 ASN A 100 ? ASP A 105 ? ASN A 109 ASP A 114 5 ? 6  
HELX_P HELX_P3  AA3 THR A 139 ? TRP A 152 ? THR A 148 TRP A 161 1 ? 14 
HELX_P HELX_P4  AA4 LEU A 166 ? ILE A 171 ? LEU A 175 ILE A 180 5 ? 6  
HELX_P HELX_P5  AA5 ALA A 173 ? ASP A 181 ? ALA A 182 ASP A 190 1 ? 9  
HELX_P HELX_P6  AA6 PRO A 193 ? ASN A 204 ? PRO A 202 ASN A 213 1 ? 12 
HELX_P HELX_P7  AA7 SER A 218 ? VAL A 229 ? SER A 227 VAL A 238 1 ? 12 
HELX_P HELX_P8  AA8 ASP A 240 ? LYS A 254 ? ASP A 249 LYS A 263 1 ? 15 
HELX_P HELX_P9  AA9 GLY A 269 ? GLN A 284 ? GLY A 278 GLN A 293 1 ? 16 
HELX_P HELX_P10 AB1 PRO A 296 ? GLN A 306 ? PRO A 305 GLN A 315 1 ? 11 
HELX_P HELX_P11 AB2 SER A 321 ? LYS A 330 ? SER A 330 LYS A 339 1 ? 10 
HELX_P HELX_P12 AB3 THR A 336 ? LYS A 338 ? THR A 345 LYS A 347 5 ? 3  
HELX_P HELX_P13 AB4 ASP A 345 ? TYR A 358 ? ASP A 354 TYR A 367 1 ? 14 
HELX_P HELX_P14 AB5 ILE A 374 ? LYS A 388 ? ILE A 383 LYS A 397 1 ? 15 
HELX_P HELX_P15 AB6 SER A 400 ? TYR A 402 ? SER A 409 TYR A 411 5 ? 3  
HELX_P HELX_P16 AB7 HIS A 403 ? LYS A 410 ? HIS A 412 LYS A 419 1 ? 8  
HELX_P HELX_P17 AB8 LYS A 423 ? LEU A 434 ? LYS A 432 LEU A 443 1 ? 12 
HELX_P HELX_P18 AB9 GLU A 442 ? GLY A 447 ? GLU A 451 GLY A 456 1 ? 6  
HELX_P HELX_P19 AC1 GLY A 470 ? GLY A 474 ? GLY A 479 GLY A 483 5 ? 5  
HELX_P HELX_P20 AC2 GLU A 477 ? LYS A 495 ? GLU A 486 LYS A 504 1 ? 19 
HELX_P HELX_P21 AC3 ALA A 510 ? LYS A 522 ? ALA A 519 LYS A 531 1 ? 13 
HELX_P HELX_P22 AC4 LYS A 546 ? LYS A 550 ? LYS A 555 LYS A 559 5 ? 5  
HELX_P HELX_P23 AC5 GLY A 553 ? PHE A 570 ? GLY A 562 PHE A 579 1 ? 18 
HELX_P HELX_P24 AC6 LEU A 589 ? ASN A 594 ? LEU A 598 ASN A 603 1 ? 6  
HELX_P HELX_P25 AC7 ASN A 609 ? LYS A 615 ? ASN A 618 LYS A 624 1 ? 7  
HELX_P HELX_P26 AC8 THR A 618 ? LYS A 638 ? THR A 627 LYS A 647 1 ? 21 
HELX_P HELX_P27 AC9 ASN B 90  ? MET B 97  ? ASN B 99  MET B 106 1 ? 8  
HELX_P HELX_P28 AD1 ASN B 100 ? ASP B 105 ? ASN B 109 ASP B 114 5 ? 6  
HELX_P HELX_P29 AD2 ALA B 115 ? SER B 117 ? ALA B 124 SER B 126 5 ? 3  
HELX_P HELX_P30 AD3 THR B 139 ? TRP B 152 ? THR B 148 TRP B 161 1 ? 14 
HELX_P HELX_P31 AD4 LEU B 166 ? ILE B 171 ? LEU B 175 ILE B 180 5 ? 6  
HELX_P HELX_P32 AD5 THR B 172 ? ASP B 181 ? THR B 181 ASP B 190 1 ? 10 
HELX_P HELX_P33 AD6 PRO B 193 ? ASN B 204 ? PRO B 202 ASN B 213 1 ? 12 
HELX_P HELX_P34 AD7 SER B 218 ? VAL B 229 ? SER B 227 VAL B 238 1 ? 12 
HELX_P HELX_P35 AD8 ASP B 240 ? HIS B 256 ? ASP B 249 HIS B 265 1 ? 17 
HELX_P HELX_P36 AD9 GLY B 269 ? GLN B 284 ? GLY B 278 GLN B 293 1 ? 16 
HELX_P HELX_P37 AE1 PRO B 296 ? SER B 305 ? PRO B 305 SER B 314 1 ? 10 
HELX_P HELX_P38 AE2 SER B 321 ? LYS B 330 ? SER B 330 LYS B 339 1 ? 10 
HELX_P HELX_P39 AE3 THR B 336 ? LYS B 338 ? THR B 345 LYS B 347 5 ? 3  
HELX_P HELX_P40 AE4 ASP B 345 ? TYR B 358 ? ASP B 354 TYR B 367 1 ? 14 
HELX_P HELX_P41 AE5 ILE B 374 ? LYS B 388 ? ILE B 383 LYS B 397 1 ? 15 
HELX_P HELX_P42 AE6 SER B 400 ? TYR B 402 ? SER B 409 TYR B 411 5 ? 3  
HELX_P HELX_P43 AE7 HIS B 403 ? LYS B 410 ? HIS B 412 LYS B 419 1 ? 8  
HELX_P HELX_P44 AE8 LYS B 423 ? LEU B 434 ? LYS B 432 LEU B 443 1 ? 12 
HELX_P HELX_P45 AE9 GLU B 442 ? SER B 446 ? GLU B 451 SER B 455 5 ? 5  
HELX_P HELX_P46 AF1 GLU B 477 ? LYS B 495 ? GLU B 486 LYS B 504 1 ? 19 
HELX_P HELX_P47 AF2 ALA B 510 ? LYS B 522 ? ALA B 519 LYS B 531 1 ? 13 
HELX_P HELX_P48 AF3 LYS B 546 ? LYS B 550 ? LYS B 555 LYS B 559 5 ? 5  
HELX_P HELX_P49 AF4 GLY B 553 ? PHE B 570 ? GLY B 562 PHE B 579 1 ? 18 
HELX_P HELX_P50 AF5 LEU B 589 ? ASN B 594 ? LEU B 598 ASN B 603 1 ? 6  
HELX_P HELX_P51 AF6 ASN B 609 ? LYS B 615 ? ASN B 618 LYS B 624 1 ? 7  
HELX_P HELX_P52 AF7 THR B 618 ? LYS B 638 ? THR B 627 LYS B 647 1 ? 21 
# 
_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 ? ? A ASN 6   OD1 ? ? ? 1_555 C CA  .  CA A ? A ASN 15  A CA  701  1_555 ? ? ? ? ? ? ? 2.646 ? ? 
metalc2  metalc ? ? A ASP 181 OD2 ? ? ? 1_555 C CA  .  CA B ? A ASP 190 A CA  701  1_555 ? ? ? ? ? ? ? 2.895 ? ? 
metalc3  metalc ? ? A SER 329 O   ? ? ? 1_555 D CA  .  CA ? ? A SER 338 A CA  702  1_555 ? ? ? ? ? ? ? 2.446 ? ? 
metalc4  metalc ? ? A ALA 332 O   ? ? ? 1_555 D CA  .  CA ? ? A ALA 341 A CA  702  1_555 ? ? ? ? ? ? ? 2.462 ? ? 
metalc5  metalc ? ? A LEU 407 O   ? ? ? 1_555 E NA  .  NA ? ? A LEU 416 A NA  703  1_555 ? ? ? ? ? ? ? 2.334 ? ? 
metalc6  metalc ? ? A SER 408 O   ? ? ? 1_555 E NA  .  NA ? ? A SER 417 A NA  703  1_555 ? ? ? ? ? ? ? 2.572 ? ? 
metalc7  metalc ? ? A LYS 410 O   ? ? ? 1_555 E NA  .  NA ? ? A LYS 419 A NA  703  1_555 ? ? ? ? ? ? ? 2.276 ? ? 
metalc8  metalc ? ? A SER 433 O   ? ? ? 1_555 E NA  .  NA ? ? A SER 442 A NA  703  1_555 ? ? ? ? ? ? ? 2.089 ? ? 
metalc9  metalc ? ? A LYS 436 O   ? ? ? 1_555 E NA  .  NA ? ? A LYS 445 A NA  703  1_555 ? ? ? ? ? ? ? 2.307 ? ? 
metalc10 metalc ? ? A HIS 460 NE2 ? ? ? 1_555 I ZN  .  ZN ? ? A HIS 469 A ZN  707  1_555 ? ? ? ? ? ? ? 2.247 ? ? 
metalc11 metalc ? ? A GLU 477 OE1 ? ? ? 1_555 I ZN  .  ZN ? ? A GLU 486 A ZN  707  1_555 ? ? ? ? ? ? ? 2.212 ? ? 
metalc12 metalc ? ? A HIS 530 ND1 ? ? ? 1_555 I ZN  .  ZN ? ? A HIS 539 A ZN  707  1_555 ? ? ? ? ? ? ? 2.198 ? ? 
metalc13 metalc ? ? C CA  .   CA  A ? ? 1_555 T HOH .  O  ? ? A CA  701 A HOH 979  1_555 ? ? ? ? ? ? ? 2.099 ? ? 
metalc14 metalc ? ? C CA  .   CA  B ? ? 1_555 T HOH .  O  ? ? A CA  701 A HOH 979  1_555 ? ? ? ? ? ? ? 2.469 ? ? 
metalc15 metalc ? ? C CA  .   CA  A ? ? 1_555 T HOH .  O  ? ? A CA  701 A HOH 1007 1_555 ? ? ? ? ? ? ? 2.401 ? ? 
metalc16 metalc ? ? C CA  .   CA  B ? ? 1_555 T HOH .  O  ? ? A CA  701 A HOH 1007 1_555 ? ? ? ? ? ? ? 3.047 ? ? 
metalc17 metalc ? ? C CA  .   CA  B ? ? 1_555 T HOH .  O  ? ? A CA  701 A HOH 1155 1_555 ? ? ? ? ? ? ? 2.307 ? ? 
metalc18 metalc ? ? C CA  .   CA  A ? ? 1_555 T HOH .  O  ? ? A CA  701 A HOH 1181 1_555 ? ? ? ? ? ? ? 2.301 ? ? 
metalc19 metalc ? ? C CA  .   CA  B ? ? 1_555 T HOH .  O  ? ? A CA  701 A HOH 1181 1_555 ? ? ? ? ? ? ? 2.810 ? ? 
metalc20 metalc ? ? C CA  .   CA  A ? ? 1_555 T HOH .  O  ? ? A CA  701 A HOH 1204 1_555 ? ? ? ? ? ? ? 2.326 ? ? 
metalc21 metalc ? ? C CA  .   CA  B ? ? 1_555 T HOH .  O  ? ? A CA  701 A HOH 1361 1_555 ? ? ? ? ? ? ? 2.844 ? ? 
metalc22 metalc ? ? D CA  .   CA  ? ? ? 1_555 T HOH .  O  ? ? A CA  702 A HOH 997  1_555 ? ? ? ? ? ? ? 2.182 ? ? 
metalc23 metalc ? ? D CA  .   CA  ? ? ? 4_456 B LYS 25 O  ? ? A CA  702 B LYS 34   1_555 ? ? ? ? ? ? ? 2.703 ? ? 
metalc24 metalc ? ? D CA  .   CA  ? ? ? 1_555 U HOH .  O  ? ? A CA  702 B HOH 830  4_556 ? ? ? ? ? ? ? 2.652 ? ? 
metalc25 metalc ? ? I ZN  .   ZN  ? ? ? 1_555 T HOH .  O  ? ? A ZN  707 A HOH 912  1_555 ? ? ? ? ? ? ? 2.347 ? ? 
metalc26 metalc ? ? I ZN  .   ZN  ? ? ? 1_555 T HOH .  O  ? ? A ZN  707 A HOH 1240 1_555 ? ? ? ? ? ? ? 2.159 ? ? 
metalc27 metalc ? ? I ZN  .   ZN  ? ? ? 1_555 T HOH .  O  ? ? A ZN  707 A HOH 1278 1_555 ? ? ? ? ? ? ? 2.156 ? ? 
metalc28 metalc ? ? B ASN 6   OD1 ? ? ? 1_555 J CA  .  CA ? ? B ASN 15  B CA  701  1_555 ? ? ? ? ? ? ? 2.485 ? ? 
metalc29 metalc ? ? B ASN 100 OD1 ? ? ? 1_555 K CA  .  CA ? ? B ASN 109 B CA  702  1_555 ? ? ? ? ? ? ? 2.149 ? ? 
metalc30 metalc ? ? B ASP 103 OD1 ? ? ? 1_555 K CA  .  CA ? ? B ASP 112 B CA  702  1_555 ? ? ? ? ? ? ? 2.363 ? ? 
metalc31 metalc ? ? B LEU 407 O   ? ? ? 1_555 M NA  .  NA ? ? B LEU 416 B NA  704  1_555 ? ? ? ? ? ? ? 2.356 ? ? 
metalc32 metalc ? ? B SER 408 O   ? ? ? 1_555 M NA  .  NA ? ? B SER 417 B NA  704  1_555 ? ? ? ? ? ? ? 2.489 ? ? 
metalc33 metalc ? ? B LYS 410 O   ? ? ? 1_555 M NA  .  NA ? ? B LYS 419 B NA  704  1_555 ? ? ? ? ? ? ? 2.220 ? ? 
metalc34 metalc ? ? B SER 433 O   ? ? ? 1_555 M NA  .  NA ? ? B SER 442 B NA  704  1_555 ? ? ? ? ? ? ? 2.223 ? ? 
metalc35 metalc ? ? B LYS 436 O   ? ? ? 1_555 M NA  .  NA ? ? B LYS 445 B NA  704  1_555 ? ? ? ? ? ? ? 2.398 ? ? 
metalc36 metalc ? ? B HIS 460 NE2 ? ? ? 1_555 S ZN  .  ZN ? ? B HIS 469 B ZN  710  1_555 ? ? ? ? ? ? ? 2.168 ? ? 
metalc37 metalc ? ? B GLU 477 OE1 ? ? ? 1_555 S ZN  .  ZN ? ? B GLU 486 B ZN  710  1_555 ? ? ? ? ? ? ? 2.242 ? ? 
metalc38 metalc ? ? B HIS 530 ND1 ? ? ? 1_555 S ZN  .  ZN ? ? B HIS 539 B ZN  710  1_555 ? ? ? ? ? ? ? 2.173 ? ? 
metalc39 metalc ? ? B THR 581 O   ? ? ? 1_555 L CA  .  CA ? ? B THR 590 B CA  703  1_555 ? ? ? ? ? ? ? 2.474 ? ? 
metalc40 metalc ? ? B THR 581 OG1 ? ? ? 1_555 L CA  .  CA ? ? B THR 590 B CA  703  1_555 ? ? ? ? ? ? ? 2.463 ? ? 
metalc41 metalc ? ? B THR 581 O   ? ? ? 1_555 L CA  .  CA ? ? B THR 590 B CA  703  2_565 ? ? ? ? ? ? ? 2.431 ? ? 
metalc42 metalc ? ? B THR 581 OG1 ? ? ? 1_555 L CA  .  CA ? ? B THR 590 B CA  703  2_565 ? ? ? ? ? ? ? 2.467 ? ? 
metalc43 metalc ? ? B LEU 582 O   ? ? ? 1_555 L CA  .  CA ? ? B LEU 591 B CA  703  1_555 ? ? ? ? ? ? ? 2.494 ? ? 
metalc44 metalc ? ? B LEU 582 O   ? ? ? 1_555 L CA  .  CA ? ? B LEU 591 B CA  703  2_565 ? ? ? ? ? ? ? 2.441 ? ? 
metalc45 metalc ? ? B ASP 583 O   ? ? ? 1_555 N NA  .  NA ? ? B ASP 592 B NA  705  1_555 ? ? ? ? ? ? ? 2.773 ? ? 
metalc46 metalc ? ? B ASP 583 O   ? ? ? 1_555 N NA  .  NA ? ? B ASP 592 B NA  705  2_565 ? ? ? ? ? ? ? 2.730 ? ? 
metalc47 metalc ? ? J CA  .   CA  ? ? ? 1_555 U HOH .  O  ? ? B CA  701 B HOH 886  1_555 ? ? ? ? ? ? ? 2.263 ? ? 
metalc48 metalc ? ? J CA  .   CA  ? ? ? 1_555 U HOH .  O  ? ? B CA  701 B HOH 909  1_555 ? ? ? ? ? ? ? 2.387 ? ? 
metalc49 metalc ? ? J CA  .   CA  ? ? ? 1_555 U HOH .  O  ? ? B CA  701 B HOH 997  1_555 ? ? ? ? ? ? ? 2.370 ? ? 
metalc50 metalc ? ? J CA  .   CA  ? ? ? 1_555 U HOH .  O  ? ? B CA  701 B HOH 1088 1_555 ? ? ? ? ? ? ? 2.332 ? ? 
metalc51 metalc ? ? J CA  .   CA  ? ? ? 1_555 U HOH .  O  ? ? B CA  701 B HOH 1273 1_555 ? ? ? ? ? ? ? 2.437 ? ? 
metalc52 metalc ? ? K CA  .   CA  ? ? ? 1_555 U HOH .  O  ? ? B CA  702 B HOH 891  1_555 ? ? ? ? ? ? ? 2.429 ? ? 
metalc53 metalc ? ? K CA  .   CA  ? ? ? 1_555 U HOH .  O  ? ? B CA  702 B HOH 1061 1_555 ? ? ? ? ? ? ? 2.787 ? ? 
metalc54 metalc ? ? K CA  .   CA  ? ? ? 1_555 U HOH .  O  ? ? B CA  702 B HOH 1201 1_555 ? ? ? ? ? ? ? 2.619 ? ? 
metalc55 metalc ? ? K CA  .   CA  ? ? ? 1_555 U HOH .  O  ? ? B CA  702 B HOH 1349 1_555 ? ? ? ? ? ? ? 2.525 ? ? 
metalc56 metalc ? ? N NA  .   NA  ? ? ? 1_555 U HOH .  O  ? ? B NA  705 B HOH 1208 1_555 ? ? ? ? ? ? ? 2.831 ? ? 
metalc57 metalc ? ? N NA  .   NA  ? ? ? 1_555 U HOH .  O  ? ? B NA  705 B HOH 1208 2_565 ? ? ? ? ? ? ? 2.844 ? ? 
metalc58 metalc ? ? S ZN  .   ZN  ? ? ? 1_555 U HOH .  O  ? ? B ZN  710 B HOH 1196 1_555 ? ? ? ? ? ? ? 2.635 ? ? 
metalc59 metalc ? ? S ZN  .   ZN  ? ? ? 1_555 U HOH .  O  ? ? B ZN  710 B HOH 1235 1_555 ? ? ? ? ? ? ? 2.195 ? ? 
metalc60 metalc ? ? S ZN  .   ZN  ? ? ? 1_555 U HOH .  O  ? ? B ZN  710 B HOH 1321 1_555 ? ? ? ? ? ? ? 2.255 ? ? 
# 
_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 ? A ASN 6   ? A ASN 15   ? 1_555 CA A C CA . ? A CA 701 ? 1_555 O   ? T HOH .   ? A HOH 979  ? 1_555 164.5 ? 
2   OD1 ? A ASN 6   ? A ASN 15   ? 1_555 CA A C CA . ? A CA 701 ? 1_555 O   ? T HOH .   ? A HOH 1007 ? 1_555 86.4  ? 
3   O   ? T HOH .   ? A HOH 979  ? 1_555 CA A C CA . ? A CA 701 ? 1_555 O   ? T HOH .   ? A HOH 1007 ? 1_555 78.2  ? 
4   OD1 ? A ASN 6   ? A ASN 15   ? 1_555 CA A C CA . ? A CA 701 ? 1_555 O   ? T HOH .   ? A HOH 1181 ? 1_555 90.4  ? 
5   O   ? T HOH .   ? A HOH 979  ? 1_555 CA A C CA . ? A CA 701 ? 1_555 O   ? T HOH .   ? A HOH 1181 ? 1_555 105.1 ? 
6   O   ? T HOH .   ? A HOH 1007 ? 1_555 CA A C CA . ? A CA 701 ? 1_555 O   ? T HOH .   ? A HOH 1181 ? 1_555 176.7 ? 
7   OD1 ? A ASN 6   ? A ASN 15   ? 1_555 CA A C CA . ? A CA 701 ? 1_555 O   ? T HOH .   ? A HOH 1204 ? 1_555 88.8  ? 
8   O   ? T HOH .   ? A HOH 979  ? 1_555 CA A C CA . ? A CA 701 ? 1_555 O   ? T HOH .   ? A HOH 1204 ? 1_555 92.0  ? 
9   O   ? T HOH .   ? A HOH 1007 ? 1_555 CA A C CA . ? A CA 701 ? 1_555 O   ? T HOH .   ? A HOH 1204 ? 1_555 97.3  ? 
10  O   ? T HOH .   ? A HOH 1181 ? 1_555 CA A C CA . ? A CA 701 ? 1_555 O   ? T HOH .   ? A HOH 1204 ? 1_555 81.9  ? 
11  OD2 ? A ASP 181 ? A ASP 190  ? 1_555 CA B C CA . ? A CA 701 ? 1_555 O   ? T HOH .   ? A HOH 979  ? 1_555 151.7 ? 
12  OD2 ? A ASP 181 ? A ASP 190  ? 1_555 CA B C CA . ? A CA 701 ? 1_555 O   ? T HOH .   ? A HOH 1007 ? 1_555 136.0 ? 
13  O   ? T HOH .   ? A HOH 979  ? 1_555 CA B C CA . ? A CA 701 ? 1_555 O   ? T HOH .   ? A HOH 1007 ? 1_555 61.1  ? 
14  OD2 ? A ASP 181 ? A ASP 190  ? 1_555 CA B C CA . ? A CA 701 ? 1_555 O   ? T HOH .   ? A HOH 1155 ? 1_555 95.2  ? 
15  O   ? T HOH .   ? A HOH 979  ? 1_555 CA B C CA . ? A CA 701 ? 1_555 O   ? T HOH .   ? A HOH 1155 ? 1_555 77.7  ? 
16  O   ? T HOH .   ? A HOH 1007 ? 1_555 CA B C CA . ? A CA 701 ? 1_555 O   ? T HOH .   ? A HOH 1155 ? 1_555 128.0 ? 
17  OD2 ? A ASP 181 ? A ASP 190  ? 1_555 CA B C CA . ? A CA 701 ? 1_555 O   ? T HOH .   ? A HOH 1181 ? 1_555 71.0  ? 
18  O   ? T HOH .   ? A HOH 979  ? 1_555 CA B C CA . ? A CA 701 ? 1_555 O   ? T HOH .   ? A HOH 1181 ? 1_555 82.6  ? 
19  O   ? T HOH .   ? A HOH 1007 ? 1_555 CA B C CA . ? A CA 701 ? 1_555 O   ? T HOH .   ? A HOH 1181 ? 1_555 106.6 ? 
20  O   ? T HOH .   ? A HOH 1155 ? 1_555 CA B C CA . ? A CA 701 ? 1_555 O   ? T HOH .   ? A HOH 1181 ? 1_555 97.3  ? 
21  OD2 ? A ASP 181 ? A ASP 190  ? 1_555 CA B C CA . ? A CA 701 ? 1_555 O   ? T HOH .   ? A HOH 1361 ? 1_555 94.5  ? 
22  O   ? T HOH .   ? A HOH 979  ? 1_555 CA B C CA . ? A CA 701 ? 1_555 O   ? T HOH .   ? A HOH 1361 ? 1_555 112.0 ? 
23  O   ? T HOH .   ? A HOH 1007 ? 1_555 CA B C CA . ? A CA 701 ? 1_555 O   ? T HOH .   ? A HOH 1361 ? 1_555 82.1  ? 
24  O   ? T HOH .   ? A HOH 1155 ? 1_555 CA B C CA . ? A CA 701 ? 1_555 O   ? T HOH .   ? A HOH 1361 ? 1_555 85.7  ? 
25  O   ? T HOH .   ? A HOH 1181 ? 1_555 CA B C CA . ? A CA 701 ? 1_555 O   ? T HOH .   ? A HOH 1361 ? 1_555 165.4 ? 
26  O   ? A SER 329 ? A SER 338  ? 1_555 CA ? D CA . ? A CA 702 ? 1_555 O   ? A ALA 332 ? A ALA 341  ? 1_555 79.4  ? 
27  O   ? A SER 329 ? A SER 338  ? 1_555 CA ? D CA . ? A CA 702 ? 1_555 O   ? T HOH .   ? A HOH 997  ? 1_555 109.3 ? 
28  O   ? A ALA 332 ? A ALA 341  ? 1_555 CA ? D CA . ? A CA 702 ? 1_555 O   ? T HOH .   ? A HOH 997  ? 1_555 87.5  ? 
29  O   ? A SER 329 ? A SER 338  ? 1_555 CA ? D CA . ? A CA 702 ? 1_555 O   ? B LYS 25  ? B LYS 34   ? 1_555 95.7  ? 
30  O   ? A ALA 332 ? A ALA 341  ? 1_555 CA ? D CA . ? A CA 702 ? 1_555 O   ? B LYS 25  ? B LYS 34   ? 1_555 99.8  ? 
31  O   ? T HOH .   ? A HOH 997  ? 1_555 CA ? D CA . ? A CA 702 ? 1_555 O   ? B LYS 25  ? B LYS 34   ? 1_555 20.3  ? 
32  O   ? A SER 329 ? A SER 338  ? 1_555 CA ? D CA . ? A CA 702 ? 1_555 O   ? U HOH .   ? B HOH 830  ? 4_556 106.5 ? 
33  O   ? A ALA 332 ? A ALA 341  ? 1_555 CA ? D CA . ? A CA 702 ? 1_555 O   ? U HOH .   ? B HOH 830  ? 4_556 162.9 ? 
34  O   ? T HOH .   ? A HOH 997  ? 1_555 CA ? D CA . ? A CA 702 ? 1_555 O   ? U HOH .   ? B HOH 830  ? 4_556 105.1 ? 
35  O   ? B LYS 25  ? B LYS 34   ? 1_555 CA ? D CA . ? A CA 702 ? 1_555 O   ? U HOH .   ? B HOH 830  ? 4_556 95.6  ? 
36  O   ? A LEU 407 ? A LEU 416  ? 1_555 NA ? E NA . ? A NA 703 ? 1_555 O   ? A SER 408 ? A SER 417  ? 1_555 82.6  ? 
37  O   ? A LEU 407 ? A LEU 416  ? 1_555 NA ? E NA . ? A NA 703 ? 1_555 O   ? A LYS 410 ? A LYS 419  ? 1_555 92.7  ? 
38  O   ? A SER 408 ? A SER 417  ? 1_555 NA ? E NA . ? A NA 703 ? 1_555 O   ? A LYS 410 ? A LYS 419  ? 1_555 108.1 ? 
39  O   ? A LEU 407 ? A LEU 416  ? 1_555 NA ? E NA . ? A NA 703 ? 1_555 O   ? A SER 433 ? A SER 442  ? 1_555 89.9  ? 
40  O   ? A SER 408 ? A SER 417  ? 1_555 NA ? E NA . ? A NA 703 ? 1_555 O   ? A SER 433 ? A SER 442  ? 1_555 141.7 ? 
41  O   ? A LYS 410 ? A LYS 419  ? 1_555 NA ? E NA . ? A NA 703 ? 1_555 O   ? A SER 433 ? A SER 442  ? 1_555 109.8 ? 
42  O   ? A LEU 407 ? A LEU 416  ? 1_555 NA ? E NA . ? A NA 703 ? 1_555 O   ? A LYS 436 ? A LYS 445  ? 1_555 164.5 ? 
43  O   ? A SER 408 ? A SER 417  ? 1_555 NA ? E NA . ? A NA 703 ? 1_555 O   ? A LYS 436 ? A LYS 445  ? 1_555 87.6  ? 
44  O   ? A LYS 410 ? A LYS 419  ? 1_555 NA ? E NA . ? A NA 703 ? 1_555 O   ? A LYS 436 ? A LYS 445  ? 1_555 101.9 ? 
45  O   ? A SER 433 ? A SER 442  ? 1_555 NA ? E NA . ? A NA 703 ? 1_555 O   ? A LYS 436 ? A LYS 445  ? 1_555 90.2  ? 
46  NE2 ? A HIS 460 ? A HIS 469  ? 1_555 ZN ? I ZN . ? A ZN 707 ? 1_555 OE1 ? A GLU 477 ? A GLU 486  ? 1_555 90.5  ? 
47  NE2 ? A HIS 460 ? A HIS 469  ? 1_555 ZN ? I ZN . ? A ZN 707 ? 1_555 ND1 ? A HIS 530 ? A HIS 539  ? 1_555 95.3  ? 
48  OE1 ? A GLU 477 ? A GLU 486  ? 1_555 ZN ? I ZN . ? A ZN 707 ? 1_555 ND1 ? A HIS 530 ? A HIS 539  ? 1_555 89.3  ? 
49  NE2 ? A HIS 460 ? A HIS 469  ? 1_555 ZN ? I ZN . ? A ZN 707 ? 1_555 O   ? T HOH .   ? A HOH 912  ? 1_555 81.0  ? 
50  OE1 ? A GLU 477 ? A GLU 486  ? 1_555 ZN ? I ZN . ? A ZN 707 ? 1_555 O   ? T HOH .   ? A HOH 912  ? 1_555 98.3  ? 
51  ND1 ? A HIS 530 ? A HIS 539  ? 1_555 ZN ? I ZN . ? A ZN 707 ? 1_555 O   ? T HOH .   ? A HOH 912  ? 1_555 171.5 ? 
52  NE2 ? A HIS 460 ? A HIS 469  ? 1_555 ZN ? I ZN . ? A ZN 707 ? 1_555 O   ? T HOH .   ? A HOH 1240 ? 1_555 156.6 ? 
53  OE1 ? A GLU 477 ? A GLU 486  ? 1_555 ZN ? I ZN . ? A ZN 707 ? 1_555 O   ? T HOH .   ? A HOH 1240 ? 1_555 88.9  ? 
54  ND1 ? A HIS 530 ? A HIS 539  ? 1_555 ZN ? I ZN . ? A ZN 707 ? 1_555 O   ? T HOH .   ? A HOH 1240 ? 1_555 108.0 ? 
55  O   ? T HOH .   ? A HOH 912  ? 1_555 ZN ? I ZN . ? A ZN 707 ? 1_555 O   ? T HOH .   ? A HOH 1240 ? 1_555 76.0  ? 
56  NE2 ? A HIS 460 ? A HIS 469  ? 1_555 ZN ? I ZN . ? A ZN 707 ? 1_555 O   ? T HOH .   ? A HOH 1278 ? 1_555 93.1  ? 
57  OE1 ? A GLU 477 ? A GLU 486  ? 1_555 ZN ? I ZN . ? A ZN 707 ? 1_555 O   ? T HOH .   ? A HOH 1278 ? 1_555 176.4 ? 
58  ND1 ? A HIS 530 ? A HIS 539  ? 1_555 ZN ? I ZN . ? A ZN 707 ? 1_555 O   ? T HOH .   ? A HOH 1278 ? 1_555 89.8  ? 
59  O   ? T HOH .   ? A HOH 912  ? 1_555 ZN ? I ZN . ? A ZN 707 ? 1_555 O   ? T HOH .   ? A HOH 1278 ? 1_555 82.8  ? 
60  O   ? T HOH .   ? A HOH 1240 ? 1_555 ZN ? I ZN . ? A ZN 707 ? 1_555 O   ? T HOH .   ? A HOH 1278 ? 1_555 88.0  ? 
61  OD1 ? B ASN 6   ? B ASN 15   ? 1_555 CA ? J CA . ? B CA 701 ? 1_555 O   ? U HOH .   ? B HOH 886  ? 1_555 88.2  ? 
62  OD1 ? B ASN 6   ? B ASN 15   ? 1_555 CA ? J CA . ? B CA 701 ? 1_555 O   ? U HOH .   ? B HOH 909  ? 1_555 172.4 ? 
63  O   ? U HOH .   ? B HOH 886  ? 1_555 CA ? J CA . ? B CA 701 ? 1_555 O   ? U HOH .   ? B HOH 909  ? 1_555 90.7  ? 
64  OD1 ? B ASN 6   ? B ASN 15   ? 1_555 CA ? J CA . ? B CA 701 ? 1_555 O   ? U HOH .   ? B HOH 997  ? 1_555 90.3  ? 
65  O   ? U HOH .   ? B HOH 886  ? 1_555 CA ? J CA . ? B CA 701 ? 1_555 O   ? U HOH .   ? B HOH 997  ? 1_555 92.1  ? 
66  O   ? U HOH .   ? B HOH 909  ? 1_555 CA ? J CA . ? B CA 701 ? 1_555 O   ? U HOH .   ? B HOH 997  ? 1_555 82.2  ? 
67  OD1 ? B ASN 6   ? B ASN 15   ? 1_555 CA ? J CA . ? B CA 701 ? 1_555 O   ? U HOH .   ? B HOH 1088 ? 1_555 93.6  ? 
68  O   ? U HOH .   ? B HOH 886  ? 1_555 CA ? J CA . ? B CA 701 ? 1_555 O   ? U HOH .   ? B HOH 1088 ? 1_555 169.6 ? 
69  O   ? U HOH .   ? B HOH 909  ? 1_555 CA ? J CA . ? B CA 701 ? 1_555 O   ? U HOH .   ? B HOH 1088 ? 1_555 88.9  ? 
70  O   ? U HOH .   ? B HOH 997  ? 1_555 CA ? J CA . ? B CA 701 ? 1_555 O   ? U HOH .   ? B HOH 1088 ? 1_555 98.1  ? 
71  OD1 ? B ASN 6   ? B ASN 15   ? 1_555 CA ? J CA . ? B CA 701 ? 1_555 O   ? U HOH .   ? B HOH 1273 ? 1_555 86.0  ? 
72  O   ? U HOH .   ? B HOH 886  ? 1_555 CA ? J CA . ? B CA 701 ? 1_555 O   ? U HOH .   ? B HOH 1273 ? 1_555 85.2  ? 
73  O   ? U HOH .   ? B HOH 909  ? 1_555 CA ? J CA . ? B CA 701 ? 1_555 O   ? U HOH .   ? B HOH 1273 ? 1_555 101.4 ? 
74  O   ? U HOH .   ? B HOH 997  ? 1_555 CA ? J CA . ? B CA 701 ? 1_555 O   ? U HOH .   ? B HOH 1273 ? 1_555 175.5 ? 
75  O   ? U HOH .   ? B HOH 1088 ? 1_555 CA ? J CA . ? B CA 701 ? 1_555 O   ? U HOH .   ? B HOH 1273 ? 1_555 84.7  ? 
76  OD1 ? B ASN 100 ? B ASN 109  ? 1_555 CA ? K CA . ? B CA 702 ? 1_555 OD1 ? B ASP 103 ? B ASP 112  ? 1_555 105.4 ? 
77  OD1 ? B ASN 100 ? B ASN 109  ? 1_555 CA ? K CA . ? B CA 702 ? 1_555 O   ? U HOH .   ? B HOH 891  ? 1_555 106.9 ? 
78  OD1 ? B ASP 103 ? B ASP 112  ? 1_555 CA ? K CA . ? B CA 702 ? 1_555 O   ? U HOH .   ? B HOH 891  ? 1_555 85.4  ? 
79  OD1 ? B ASN 100 ? B ASN 109  ? 1_555 CA ? K CA . ? B CA 702 ? 1_555 O   ? U HOH .   ? B HOH 1061 ? 1_555 165.1 ? 
80  OD1 ? B ASP 103 ? B ASP 112  ? 1_555 CA ? K CA . ? B CA 702 ? 1_555 O   ? U HOH .   ? B HOH 1061 ? 1_555 89.4  ? 
81  O   ? U HOH .   ? B HOH 891  ? 1_555 CA ? K CA . ? B CA 702 ? 1_555 O   ? U HOH .   ? B HOH 1061 ? 1_555 74.9  ? 
82  OD1 ? B ASN 100 ? B ASN 109  ? 1_555 CA ? K CA . ? B CA 702 ? 1_555 O   ? U HOH .   ? B HOH 1201 ? 1_555 99.7  ? 
83  OD1 ? B ASP 103 ? B ASP 112  ? 1_555 CA ? K CA . ? B CA 702 ? 1_555 O   ? U HOH .   ? B HOH 1201 ? 1_555 95.1  ? 
84  O   ? U HOH .   ? B HOH 891  ? 1_555 CA ? K CA . ? B CA 702 ? 1_555 O   ? U HOH .   ? B HOH 1201 ? 1_555 152.2 ? 
85  O   ? U HOH .   ? B HOH 1061 ? 1_555 CA ? K CA . ? B CA 702 ? 1_555 O   ? U HOH .   ? B HOH 1201 ? 1_555 77.3  ? 
86  OD1 ? B ASN 100 ? B ASN 109  ? 1_555 CA ? K CA . ? B CA 702 ? 1_555 O   ? U HOH .   ? B HOH 1349 ? 1_555 91.6  ? 
87  OD1 ? B ASP 103 ? B ASP 112  ? 1_555 CA ? K CA . ? B CA 702 ? 1_555 O   ? U HOH .   ? B HOH 1349 ? 1_555 162.0 ? 
88  O   ? U HOH .   ? B HOH 891  ? 1_555 CA ? K CA . ? B CA 702 ? 1_555 O   ? U HOH .   ? B HOH 1349 ? 1_555 83.9  ? 
89  O   ? U HOH .   ? B HOH 1061 ? 1_555 CA ? K CA . ? B CA 702 ? 1_555 O   ? U HOH .   ? B HOH 1349 ? 1_555 73.8  ? 
90  O   ? U HOH .   ? B HOH 1201 ? 1_555 CA ? K CA . ? B CA 702 ? 1_555 O   ? U HOH .   ? B HOH 1349 ? 1_555 87.7  ? 
91  O   ? B LEU 407 ? B LEU 416  ? 1_555 NA ? M NA . ? B NA 704 ? 1_555 O   ? B SER 408 ? B SER 417  ? 1_555 83.7  ? 
92  O   ? B LEU 407 ? B LEU 416  ? 1_555 NA ? M NA . ? B NA 704 ? 1_555 O   ? B LYS 410 ? B LYS 419  ? 1_555 95.1  ? 
93  O   ? B SER 408 ? B SER 417  ? 1_555 NA ? M NA . ? B NA 704 ? 1_555 O   ? B LYS 410 ? B LYS 419  ? 1_555 113.1 ? 
94  O   ? B LEU 407 ? B LEU 416  ? 1_555 NA ? M NA . ? B NA 704 ? 1_555 O   ? B SER 433 ? B SER 442  ? 1_555 88.3  ? 
95  O   ? B SER 408 ? B SER 417  ? 1_555 NA ? M NA . ? B NA 704 ? 1_555 O   ? B SER 433 ? B SER 442  ? 1_555 136.1 ? 
96  O   ? B LYS 410 ? B LYS 419  ? 1_555 NA ? M NA . ? B NA 704 ? 1_555 O   ? B SER 433 ? B SER 442  ? 1_555 110.6 ? 
97  O   ? B LEU 407 ? B LEU 416  ? 1_555 NA ? M NA . ? B NA 704 ? 1_555 O   ? B LYS 436 ? B LYS 445  ? 1_555 162.0 ? 
98  O   ? B SER 408 ? B SER 417  ? 1_555 NA ? M NA . ? B NA 704 ? 1_555 O   ? B LYS 436 ? B LYS 445  ? 1_555 90.7  ? 
99  O   ? B LYS 410 ? B LYS 419  ? 1_555 NA ? M NA . ? B NA 704 ? 1_555 O   ? B LYS 436 ? B LYS 445  ? 1_555 102.8 ? 
100 O   ? B SER 433 ? B SER 442  ? 1_555 NA ? M NA . ? B NA 704 ? 1_555 O   ? B LYS 436 ? B LYS 445  ? 1_555 84.0  ? 
101 NE2 ? B HIS 460 ? B HIS 469  ? 1_555 ZN ? S ZN . ? B ZN 710 ? 1_555 OE1 ? B GLU 477 ? B GLU 486  ? 1_555 88.5  ? 
102 NE2 ? B HIS 460 ? B HIS 469  ? 1_555 ZN ? S ZN . ? B ZN 710 ? 1_555 ND1 ? B HIS 530 ? B HIS 539  ? 1_555 99.6  ? 
103 OE1 ? B GLU 477 ? B GLU 486  ? 1_555 ZN ? S ZN . ? B ZN 710 ? 1_555 ND1 ? B HIS 530 ? B HIS 539  ? 1_555 93.3  ? 
104 NE2 ? B HIS 460 ? B HIS 469  ? 1_555 ZN ? S ZN . ? B ZN 710 ? 1_555 O   ? U HOH .   ? B HOH 1196 ? 1_555 78.8  ? 
105 OE1 ? B GLU 477 ? B GLU 486  ? 1_555 ZN ? S ZN . ? B ZN 710 ? 1_555 O   ? U HOH .   ? B HOH 1196 ? 1_555 98.6  ? 
106 ND1 ? B HIS 530 ? B HIS 539  ? 1_555 ZN ? S ZN . ? B ZN 710 ? 1_555 O   ? U HOH .   ? B HOH 1196 ? 1_555 167.9 ? 
107 NE2 ? B HIS 460 ? B HIS 469  ? 1_555 ZN ? S ZN . ? B ZN 710 ? 1_555 O   ? U HOH .   ? B HOH 1235 ? 1_555 158.4 ? 
108 OE1 ? B GLU 477 ? B GLU 486  ? 1_555 ZN ? S ZN . ? B ZN 710 ? 1_555 O   ? U HOH .   ? B HOH 1235 ? 1_555 93.3  ? 
109 ND1 ? B HIS 530 ? B HIS 539  ? 1_555 ZN ? S ZN . ? B ZN 710 ? 1_555 O   ? U HOH .   ? B HOH 1235 ? 1_555 101.8 ? 
110 O   ? U HOH .   ? B HOH 1196 ? 1_555 ZN ? S ZN . ? B ZN 710 ? 1_555 O   ? U HOH .   ? B HOH 1235 ? 1_555 79.6  ? 
111 NE2 ? B HIS 460 ? B HIS 469  ? 1_555 ZN ? S ZN . ? B ZN 710 ? 1_555 O   ? U HOH .   ? B HOH 1321 ? 1_555 89.5  ? 
112 OE1 ? B GLU 477 ? B GLU 486  ? 1_555 ZN ? S ZN . ? B ZN 710 ? 1_555 O   ? U HOH .   ? B HOH 1321 ? 1_555 175.1 ? 
113 ND1 ? B HIS 530 ? B HIS 539  ? 1_555 ZN ? S ZN . ? B ZN 710 ? 1_555 O   ? U HOH .   ? B HOH 1321 ? 1_555 91.4  ? 
114 O   ? U HOH .   ? B HOH 1196 ? 1_555 ZN ? S ZN . ? B ZN 710 ? 1_555 O   ? U HOH .   ? B HOH 1321 ? 1_555 76.6  ? 
115 O   ? U HOH .   ? B HOH 1235 ? 1_555 ZN ? S ZN . ? B ZN 710 ? 1_555 O   ? U HOH .   ? B HOH 1321 ? 1_555 87.0  ? 
116 O   ? B THR 581 ? B THR 590  ? 1_555 CA ? L CA . ? B CA 703 ? 1_555 OG1 ? B THR 581 ? B THR 590  ? 1_555 79.5  ? 
117 O   ? B THR 581 ? B THR 590  ? 1_555 CA ? L CA . ? B CA 703 ? 1_555 O   ? B THR 581 ? B THR 590  ? 1_555 0.0   ? 
118 OG1 ? B THR 581 ? B THR 590  ? 1_555 CA ? L CA . ? B CA 703 ? 1_555 O   ? B THR 581 ? B THR 590  ? 1_555 79.5  ? 
119 O   ? B THR 581 ? B THR 590  ? 1_555 CA ? L CA . ? B CA 703 ? 1_555 OG1 ? B THR 581 ? B THR 590  ? 1_555 79.5  ? 
120 OG1 ? B THR 581 ? B THR 590  ? 1_555 CA ? L CA . ? B CA 703 ? 1_555 OG1 ? B THR 581 ? B THR 590  ? 1_555 0.0   ? 
121 O   ? B THR 581 ? B THR 590  ? 1_555 CA ? L CA . ? B CA 703 ? 1_555 OG1 ? B THR 581 ? B THR 590  ? 1_555 79.5  ? 
122 O   ? B THR 581 ? B THR 590  ? 1_555 CA ? L CA . ? B CA 703 ? 1_555 O   ? B LEU 582 ? B LEU 591  ? 1_555 79.2  ? 
123 OG1 ? B THR 581 ? B THR 590  ? 1_555 CA ? L CA . ? B CA 703 ? 1_555 O   ? B LEU 582 ? B LEU 591  ? 1_555 90.3  ? 
124 O   ? B THR 581 ? B THR 590  ? 1_555 CA ? L CA . ? B CA 703 ? 1_555 O   ? B LEU 582 ? B LEU 591  ? 1_555 79.2  ? 
125 OG1 ? B THR 581 ? B THR 590  ? 1_555 CA ? L CA . ? B CA 703 ? 1_555 O   ? B LEU 582 ? B LEU 591  ? 1_555 90.3  ? 
126 O   ? B THR 581 ? B THR 590  ? 1_555 CA ? L CA . ? B CA 703 ? 1_555 O   ? B LEU 582 ? B LEU 591  ? 1_555 79.2  ? 
127 OG1 ? B THR 581 ? B THR 590  ? 1_555 CA ? L CA . ? B CA 703 ? 1_555 O   ? B LEU 582 ? B LEU 591  ? 1_555 90.3  ? 
128 O   ? B THR 581 ? B THR 590  ? 1_555 CA ? L CA . ? B CA 703 ? 1_555 O   ? B LEU 582 ? B LEU 591  ? 1_555 79.2  ? 
129 OG1 ? B THR 581 ? B THR 590  ? 1_555 CA ? L CA . ? B CA 703 ? 1_555 O   ? B LEU 582 ? B LEU 591  ? 1_555 90.3  ? 
130 O   ? B LEU 582 ? B LEU 591  ? 1_555 CA ? L CA . ? B CA 703 ? 1_555 O   ? B LEU 582 ? B LEU 591  ? 1_555 0.0   ? 
131 O   ? B ASP 583 ? B ASP 592  ? 1_555 NA ? N NA . ? B NA 705 ? 1_555 O   ? B ASP 583 ? B ASP 592  ? 1_555 0.0   ? 
132 O   ? B ASP 583 ? B ASP 592  ? 1_555 NA ? N NA . ? B NA 705 ? 1_555 O   ? U HOH .   ? B HOH 1208 ? 1_555 125.4 ? 
133 O   ? B ASP 583 ? B ASP 592  ? 1_555 NA ? N NA . ? B NA 705 ? 1_555 O   ? U HOH .   ? B HOH 1208 ? 1_555 125.4 ? 
134 O   ? B ASP 583 ? B ASP 592  ? 1_555 NA ? N NA . ? B NA 705 ? 1_555 O   ? U HOH .   ? B HOH 1208 ? 2_565 101.7 ? 
135 O   ? B ASP 583 ? B ASP 592  ? 1_555 NA ? N NA . ? B NA 705 ? 1_555 O   ? U HOH .   ? B HOH 1208 ? 2_565 101.7 ? 
136 O   ? U HOH .   ? B HOH 1208 ? 1_555 NA ? N NA . ? B NA 705 ? 1_555 O   ? U HOH .   ? B HOH 1208 ? 2_565 87.8  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 7 ? 
AA3 ? 2 ? 
AA4 ? 4 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 4 ? 
AA8 ? 6 ? 
AA9 ? 2 ? 
AB1 ? 8 ? 
AB2 ? 7 ? 
AB3 ? 2 ? 
AB4 ? 4 ? 
AB5 ? 4 ? 
AB6 ? 4 ? 
AB7 ? 4 ? 
AB8 ? 6 ? 
AB9 ? 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 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA7 1 2 ? parallel      
AA7 2 3 ? parallel      
AA7 3 4 ? parallel      
AA8 1 2 ? parallel      
AA8 2 3 ? parallel      
AA8 3 4 ? parallel      
AA8 4 5 ? anti-parallel 
AA8 5 6 ? parallel      
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB1 4 5 ? anti-parallel 
AB1 5 6 ? anti-parallel 
AB1 6 7 ? anti-parallel 
AB1 7 8 ? parallel      
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB2 4 5 ? anti-parallel 
AB2 5 6 ? anti-parallel 
AB2 6 7 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB4 1 2 ? parallel      
AB4 2 3 ? parallel      
AB4 3 4 ? parallel      
AB5 1 2 ? parallel      
AB5 2 3 ? parallel      
AB5 3 4 ? parallel      
AB6 1 2 ? parallel      
AB6 2 3 ? parallel      
AB6 3 4 ? parallel      
AB7 1 2 ? parallel      
AB7 2 3 ? parallel      
AB7 3 4 ? parallel      
AB8 1 2 ? parallel      
AB8 2 3 ? parallel      
AB8 3 4 ? parallel      
AB8 4 5 ? anti-parallel 
AB8 5 6 ? parallel      
AB9 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 ILE A 3   ? LEU A 7   ? ILE A 12  LEU A 16  
AA1 2 SER A 16  ? PHE A 24  ? SER A 25  PHE A 33  
AA1 3 SER A 56  ? TYR A 63  ? SER A 65  TYR A 72  
AA1 4 MET A 42  ? ASN A 51  ? MET A 51  ASN A 60  
AA1 5 SER A 32  ? CYS A 39  ? SER A 41  CYS A 48  
AA1 6 VAL A 72  ? ASN A 81  ? VAL A 81  ASN A 90  
AA1 7 VAL A 106 ? GLU A 109 ? VAL A 115 GLU A 118 
AA1 8 SER A 11  ? VAL A 13  ? SER A 20  VAL A 22  
AA2 1 ILE A 3   ? LEU A 7   ? ILE A 12  LEU A 16  
AA2 2 SER A 16  ? PHE A 24  ? SER A 25  PHE A 33  
AA2 3 SER A 56  ? TYR A 63  ? SER A 65  TYR A 72  
AA2 4 MET A 42  ? ASN A 51  ? MET A 51  ASN A 60  
AA2 5 SER A 32  ? CYS A 39  ? SER A 41  CYS A 48  
AA2 6 VAL A 72  ? ASN A 81  ? VAL A 81  ASN A 90  
AA2 7 GLN A 86  ? LEU A 89  ? GLN A 95  LEU A 98  
AA3 1 ILE A 112 ? SER A 113 ? ILE A 121 SER A 122 
AA3 2 THR A 128 ? SER A 129 ? THR A 137 SER A 138 
AA4 1 VAL A 132 ? LEU A 135 ? VAL A 141 LEU A 144 
AA4 2 THR A 411 ? ILE A 418 ? THR A 420 ILE A 427 
AA4 3 GLU A 362 ? LYS A 370 ? GLU A 371 LYS A 379 
AA4 4 ILE A 391 ? THR A 394 ? ILE A 400 THR A 403 
AA5 1 ILE A 184 ? ALA A 187 ? ILE A 193 ALA A 196 
AA5 2 LYS A 158 ? ASN A 163 ? LYS A 167 ASN A 172 
AA5 3 ASP A 207 ? ILE A 211 ? ASP A 216 ILE A 220 
AA5 4 ASN A 232 ? ILE A 236 ? ASN A 241 ILE A 245 
AA6 1 ILE A 287 ? ALA A 290 ? ILE A 296 ALA A 299 
AA6 2 LYS A 260 ? ASN A 265 ? LYS A 269 ASN A 274 
AA6 3 LEU A 308 ? ILE A 314 ? LEU A 317 ILE A 323 
AA6 4 ALA A 332 ? ASN A 334 ? ALA A 341 ASN A 343 
AA7 1 ILE A 287 ? ALA A 290 ? ILE A 296 ALA A 299 
AA7 2 LYS A 260 ? ASN A 265 ? LYS A 269 ASN A 274 
AA7 3 LEU A 308 ? ILE A 314 ? LEU A 317 ILE A 323 
AA7 4 ARG A 340 ? VAL A 341 ? ARG A 349 VAL A 350 
AA8 1 ASN A 498 ? MET A 501 ? ASN A 507 MET A 510 
AA8 2 THR A 453 ? PRO A 458 ? THR A 462 PRO A 467 
AA8 3 LEU A 525 ? ASN A 532 ? LEU A 534 ASN A 541 
AA8 4 ALA A 599 ? PHE A 606 ? ALA A 608 PHE A 615 
AA8 5 VAL A 541 ? TYR A 544 ? VAL A 550 TYR A 553 
AA8 6 ASN A 574 ? LYS A 578 ? ASN A 583 LYS A 587 
AA9 1 THR A 468 ? SER A 469 ? THR A 477 SER A 478 
AA9 2 ALA A 475 ? GLN A 476 ? ALA A 484 GLN A 485 
AB1 1 ILE B 3   ? LEU B 7   ? ILE B 12  LEU B 16  
AB1 2 LYS B 17  ? PHE B 24  ? LYS B 26  PHE B 33  
AB1 3 SER B 56  ? ASN B 62  ? SER B 65  ASN B 71  
AB1 4 MET B 42  ? ASN B 51  ? MET B 51  ASN B 60  
AB1 5 SER B 32  ? CYS B 39  ? SER B 41  CYS B 48  
AB1 6 VAL B 72  ? ASN B 81  ? VAL B 81  ASN B 90  
AB1 7 VAL B 106 ? GLN B 108 ? VAL B 115 GLN B 117 
AB1 8 SER B 11  ? VAL B 12  ? SER B 20  VAL B 21  
AB2 1 ILE B 3   ? LEU B 7   ? ILE B 12  LEU B 16  
AB2 2 LYS B 17  ? PHE B 24  ? LYS B 26  PHE B 33  
AB2 3 SER B 56  ? ASN B 62  ? SER B 65  ASN B 71  
AB2 4 MET B 42  ? ASN B 51  ? MET B 51  ASN B 60  
AB2 5 SER B 32  ? CYS B 39  ? SER B 41  CYS B 48  
AB2 6 VAL B 72  ? ASN B 81  ? VAL B 81  ASN B 90  
AB2 7 GLN B 86  ? LEU B 89  ? GLN B 95  LEU B 98  
AB3 1 ILE B 112 ? SER B 113 ? ILE B 121 SER B 122 
AB3 2 THR B 128 ? SER B 129 ? THR B 137 SER B 138 
AB4 1 VAL B 132 ? LEU B 135 ? VAL B 141 LEU B 144 
AB4 2 THR B 411 ? ILE B 418 ? THR B 420 ILE B 427 
AB4 3 GLU B 362 ? LYS B 370 ? GLU B 371 LYS B 379 
AB4 4 ILE B 391 ? THR B 394 ? ILE B 400 THR B 403 
AB5 1 ILE B 184 ? ALA B 187 ? ILE B 193 ALA B 196 
AB5 2 LYS B 158 ? ASN B 163 ? LYS B 167 ASN B 172 
AB5 3 ASP B 207 ? ILE B 211 ? ASP B 216 ILE B 220 
AB5 4 ASN B 232 ? ILE B 236 ? ASN B 241 ILE B 245 
AB6 1 ILE B 287 ? ALA B 290 ? ILE B 296 ALA B 299 
AB6 2 LYS B 260 ? ASN B 265 ? LYS B 269 ASN B 274 
AB6 3 LEU B 308 ? ILE B 314 ? LEU B 317 ILE B 323 
AB6 4 ALA B 332 ? ASN B 334 ? ALA B 341 ASN B 343 
AB7 1 ILE B 287 ? ALA B 290 ? ILE B 296 ALA B 299 
AB7 2 LYS B 260 ? ASN B 265 ? LYS B 269 ASN B 274 
AB7 3 LEU B 308 ? ILE B 314 ? LEU B 317 ILE B 323 
AB7 4 ARG B 340 ? VAL B 341 ? ARG B 349 VAL B 350 
AB8 1 ASN B 498 ? MET B 501 ? ASN B 507 MET B 510 
AB8 2 THR B 453 ? PRO B 458 ? THR B 462 PRO B 467 
AB8 3 LEU B 525 ? ASN B 532 ? LEU B 534 ASN B 541 
AB8 4 ALA B 599 ? PHE B 606 ? ALA B 608 PHE B 615 
AB8 5 VAL B 541 ? TYR B 544 ? VAL B 550 TYR B 553 
AB8 6 ASN B 574 ? LYS B 578 ? ASN B 583 LYS B 587 
AB9 1 THR B 468 ? SER B 469 ? THR B 477 SER B 478 
AB9 2 ALA B 475 ? GLN B 476 ? ALA B 484 GLN B 485 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ASN A 6   ? N ASN A 15  O SER A 21  ? O SER A 30  
AA1 2 3 N VAL A 22  ? N VAL A 31  O TYR A 57  ? O TYR A 66  
AA1 3 4 O SER A 56  ? O SER A 65  N ASN A 51  ? N ASN A 60  
AA1 4 5 O LEU A 48  ? O LEU A 57  N ILE A 33  ? N ILE A 42  
AA1 5 6 N ASN A 36  ? N ASN A 45  O GLN A 76  ? O GLN A 85  
AA1 6 7 N TRP A 73  ? N TRP A 82  O VAL A 106 ? O VAL A 115 
AA1 7 8 O THR A 107 ? O THR A 116 N VAL A 12  ? N VAL A 21  
AA2 1 2 N ASN A 6   ? N ASN A 15  O SER A 21  ? O SER A 30  
AA2 2 3 N VAL A 22  ? N VAL A 31  O TYR A 57  ? O TYR A 66  
AA2 3 4 O SER A 56  ? O SER A 65  N ASN A 51  ? N ASN A 60  
AA2 4 5 O LEU A 48  ? O LEU A 57  N ILE A 33  ? N ILE A 42  
AA2 5 6 N ASN A 36  ? N ASN A 45  O GLN A 76  ? O GLN A 85  
AA2 6 7 N ILE A 80  ? N ILE A 89  O LYS A 87  ? O LYS A 96  
AA3 1 2 N ILE A 112 ? N ILE A 121 O SER A 129 ? O SER A 138 
AA4 1 2 N LEU A 135 ? N LEU A 144 O GLN A 417 ? O GLN A 426 
AA4 2 3 O TYR A 416 ? O TYR A 425 N VAL A 368 ? N VAL A 377 
AA4 3 4 N LEU A 367 ? N LEU A 376 O LEU A 392 ? O LEU A 401 
AA5 1 2 O LEU A 185 ? O LEU A 194 N VAL A 160 ? N VAL A 169 
AA5 2 3 N ILE A 161 ? N ILE A 170 O ILE A 209 ? O ILE A 218 
AA5 3 4 N VAL A 208 ? N VAL A 217 O THR A 234 ? O THR A 243 
AA6 1 2 O ALA A 290 ? O ALA A 299 N ALA A 264 ? N ALA A 273 
AA6 2 3 N ILE A 263 ? N ILE A 272 O ILE A 314 ? O ILE A 323 
AA6 3 4 N LEU A 308 ? N LEU A 317 O LYS A 333 ? O LYS A 342 
AA7 1 2 O ALA A 290 ? O ALA A 299 N ALA A 264 ? N ALA A 273 
AA7 2 3 N ILE A 263 ? N ILE A 272 O ILE A 314 ? O ILE A 323 
AA7 3 4 N TYR A 313 ? N TYR A 322 O VAL A 341 ? O VAL A 350 
AA8 1 2 O ASN A 498 ? O ASN A 507 N VAL A 454 ? N VAL A 463 
AA8 2 3 N ASP A 457 ? N ASP A 466 O ILE A 529 ? O ILE A 538 
AA8 3 4 N HIS A 530 ? N HIS A 539 O VAL A 602 ? O VAL A 611 
AA8 4 5 O GLU A 603 ? O GLU A 612 N GLU A 542 ? N GLU A 551 
AA8 5 6 N ILE A 543 ? N ILE A 552 O LYS A 578 ? O LYS A 587 
AA9 1 2 N SER A 469 ? N SER A 478 O ALA A 475 ? O ALA A 484 
AB1 1 2 N ASN B 6   ? N ASN B 15  O SER B 21  ? O SER B 30  
AB1 2 3 N VAL B 22  ? N VAL B 31  O TYR B 57  ? O TYR B 66  
AB1 3 4 O SER B 56  ? O SER B 65  N ASN B 51  ? N ASN B 60  
AB1 4 5 O LEU B 44  ? O LEU B 53  N PHE B 37  ? N PHE B 46  
AB1 5 6 N ASN B 36  ? N ASN B 45  O GLN B 76  ? O GLN B 85  
AB1 6 7 N TRP B 73  ? N TRP B 82  O VAL B 106 ? O VAL B 115 
AB1 7 8 O THR B 107 ? O THR B 116 N VAL B 12  ? N VAL B 21  
AB2 1 2 N ASN B 6   ? N ASN B 15  O SER B 21  ? O SER B 30  
AB2 2 3 N VAL B 22  ? N VAL B 31  O TYR B 57  ? O TYR B 66  
AB2 3 4 O SER B 56  ? O SER B 65  N ASN B 51  ? N ASN B 60  
AB2 4 5 O LEU B 44  ? O LEU B 53  N PHE B 37  ? N PHE B 46  
AB2 5 6 N ASN B 36  ? N ASN B 45  O GLN B 76  ? O GLN B 85  
AB2 6 7 N ILE B 80  ? N ILE B 89  O LYS B 87  ? O LYS B 96  
AB3 1 2 N ILE B 112 ? N ILE B 121 O SER B 129 ? O SER B 138 
AB4 1 2 N LEU B 135 ? N LEU B 144 O GLN B 417 ? O GLN B 426 
AB4 2 3 O TYR B 416 ? O TYR B 425 N VAL B 368 ? N VAL B 377 
AB4 3 4 N LEU B 367 ? N LEU B 376 O LEU B 392 ? O LEU B 401 
AB5 1 2 O LEU B 185 ? O LEU B 194 N VAL B 160 ? N VAL B 169 
AB5 2 3 N ILE B 161 ? N ILE B 170 O ILE B 209 ? O ILE B 218 
AB5 3 4 N ILE B 210 ? N ILE B 219 O THR B 234 ? O THR B 243 
AB6 1 2 O ALA B 290 ? O ALA B 299 N ALA B 264 ? N ALA B 273 
AB6 2 3 N ILE B 263 ? N ILE B 272 O ILE B 314 ? O ILE B 323 
AB6 3 4 N LEU B 308 ? N LEU B 317 O LYS B 333 ? O LYS B 342 
AB7 1 2 O ALA B 290 ? O ALA B 299 N ALA B 264 ? N ALA B 273 
AB7 2 3 N ILE B 263 ? N ILE B 272 O ILE B 314 ? O ILE B 323 
AB7 3 4 N TYR B 313 ? N TYR B 322 O VAL B 341 ? O VAL B 350 
AB8 1 2 O ASN B 498 ? O ASN B 507 N VAL B 454 ? N VAL B 463 
AB8 2 3 N ASP B 457 ? N ASP B 466 O ILE B 529 ? O ILE B 538 
AB8 3 4 N ASN B 532 ? N ASN B 541 O ALA B 605 ? O ALA B 614 
AB8 4 5 O GLU B 603 ? O GLU B 612 N GLU B 542 ? N GLU B 551 
AB8 5 6 N ILE B 543 ? N ILE B 552 O LYS B 578 ? O LYS B 587 
AB9 1 2 N SER B 469 ? N SER B 478 O ALA B 475 ? O ALA B 484 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A CA  701 ? 8  'binding site for residue CA A 701'                   
AC2 Software A CA  702 ? 5  'binding site for residue CA A 702'                   
AC3 Software A NA  703 ? 6  'binding site for residue NA A 703'                   
AC4 Software A CL  704 ? 3  'binding site for residue CL A 704'                   
AC5 Software A CL  705 ? 5  'binding site for residue CL A 705'                   
AC6 Software A CL  706 ? 6  'binding site for residue CL A 706'                   
AC7 Software A ZN  707 ? 6  'binding site for residue ZN A 707'                   
AC8 Software B CA  701 ? 6  'binding site for residue CA B 701'                   
AC9 Software B CA  702 ? 6  'binding site for residue CA B 702'                   
AD1 Software B CA  703 ? 4  'binding site for residue CA B 703'                   
AD2 Software B NA  704 ? 5  'binding site for residue NA B 704'                   
AD3 Software B NA  705 ? 8  'binding site for residue NA B 705'                   
AD4 Software B CL  706 ? 3  'binding site for residue CL B 706'                   
AD5 Software B CL  707 ? 5  'binding site for residue CL B 707'                   
AD6 Software B CIT 708 ? 11 'binding site for residue CIT B 708'                  
AD7 Software B CIT 709 ? 9  'binding site for residue CIT B 709'                  
AD8 Software B ZN  710 ? 6  'binding site for residue ZN B 710'                   
AD9 Software B GLY 547 ? 6  'binding site for Di-peptide GLY B 545 and GLY B 547' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1   AC1 8  ASN A 6   ? ASN A 15   . ? 1_555 ? 
2   AC1 8  ASP A 181 ? ASP A 190  . ? 1_555 ? 
3   AC1 8  HOH T .   ? HOH A 979  . ? 1_555 ? 
4   AC1 8  HOH T .   ? HOH A 1007 . ? 1_555 ? 
5   AC1 8  HOH T .   ? HOH A 1155 . ? 1_555 ? 
6   AC1 8  HOH T .   ? HOH A 1181 . ? 1_555 ? 
7   AC1 8  HOH T .   ? HOH A 1204 . ? 1_555 ? 
8   AC1 8  HOH T .   ? HOH A 1361 . ? 1_555 ? 
9   AC2 5  SER A 329 ? SER A 338  . ? 1_555 ? 
10  AC2 5  ALA A 332 ? ALA A 341  . ? 1_555 ? 
11  AC2 5  HOH T .   ? HOH A 997  . ? 1_555 ? 
12  AC2 5  LYS B 25  ? LYS B 34   . ? 4_556 ? 
13  AC2 5  HOH U .   ? HOH B 830  . ? 4_556 ? 
14  AC3 6  LEU A 407 ? LEU A 416  . ? 1_555 ? 
15  AC3 6  SER A 408 ? SER A 417  . ? 1_555 ? 
16  AC3 6  LYS A 410 ? LYS A 419  . ? 1_555 ? 
17  AC3 6  SER A 433 ? SER A 442  . ? 1_555 ? 
18  AC3 6  LYS A 436 ? LYS A 445  . ? 1_555 ? 
19  AC3 6  ALA A 439 ? ALA A 448  . ? 1_555 ? 
20  AC4 3  LYS A 10  ? LYS A 19   . ? 1_555 ? 
21  AC4 3  GLN A 150 ? GLN A 159  . ? 1_555 ? 
22  AC4 3  TYR A 416 ? TYR A 425  . ? 1_555 ? 
23  AC5 5  ARG A 593 ? ARG A 602  . ? 1_555 ? 
24  AC5 5  ASN A 594 ? ASN A 603  . ? 1_555 ? 
25  AC5 5  HOH T .   ? HOH A 1060 . ? 1_555 ? 
26  AC5 5  HOH T .   ? HOH A 1442 . ? 1_555 ? 
27  AC5 5  HOH U .   ? HOH B 1139 . ? 1_555 ? 
28  AC6 6  GLN A 8   ? GLN A 17   . ? 1_555 ? 
29  AC6 6  ARG A 9   ? ARG A 18   . ? 1_555 ? 
30  AC6 6  LYS A 17  ? LYS A 26   . ? 1_555 ? 
31  AC6 6  HOH T .   ? HOH A 842  . ? 1_555 ? 
32  AC6 6  HOH T .   ? HOH A 844  . ? 1_555 ? 
33  AC6 6  HOH T .   ? HOH A 1203 . ? 1_555 ? 
34  AC7 6  HIS A 460 ? HIS A 469  . ? 1_555 ? 
35  AC7 6  GLU A 477 ? GLU A 486  . ? 1_555 ? 
36  AC7 6  HIS A 530 ? HIS A 539  . ? 1_555 ? 
37  AC7 6  HOH T .   ? HOH A 912  . ? 1_555 ? 
38  AC7 6  HOH T .   ? HOH A 1240 . ? 1_555 ? 
39  AC7 6  HOH T .   ? HOH A 1278 . ? 1_555 ? 
40  AC8 6  ASN B 6   ? ASN B 15   . ? 1_555 ? 
41  AC8 6  HOH U .   ? HOH B 886  . ? 1_555 ? 
42  AC8 6  HOH U .   ? HOH B 909  . ? 1_555 ? 
43  AC8 6  HOH U .   ? HOH B 997  . ? 1_555 ? 
44  AC8 6  HOH U .   ? HOH B 1088 . ? 1_555 ? 
45  AC8 6  HOH U .   ? HOH B 1273 . ? 1_555 ? 
46  AC9 6  ASN B 100 ? ASN B 109  . ? 1_555 ? 
47  AC9 6  ASP B 103 ? ASP B 112  . ? 1_555 ? 
48  AC9 6  HOH U .   ? HOH B 891  . ? 1_555 ? 
49  AC9 6  HOH U .   ? HOH B 1061 . ? 1_555 ? 
50  AC9 6  HOH U .   ? HOH B 1201 . ? 1_555 ? 
51  AC9 6  HOH U .   ? HOH B 1349 . ? 1_555 ? 
52  AD1 4  THR B 581 ? THR B 590  . ? 1_555 ? 
53  AD1 4  THR B 581 ? THR B 590  . ? 2_565 ? 
54  AD1 4  LEU B 582 ? LEU B 591  . ? 1_555 ? 
55  AD1 4  LEU B 582 ? LEU B 591  . ? 2_565 ? 
56  AD2 5  LEU B 407 ? LEU B 416  . ? 1_555 ? 
57  AD2 5  SER B 408 ? SER B 417  . ? 1_555 ? 
58  AD2 5  LYS B 410 ? LYS B 419  . ? 1_555 ? 
59  AD2 5  SER B 433 ? SER B 442  . ? 1_555 ? 
60  AD2 5  LYS B 436 ? LYS B 445  . ? 1_555 ? 
61  AD3 8  ASP B 583 ? ASP B 592  . ? 2_565 ? 
62  AD3 8  ASP B 583 ? ASP B 592  . ? 1_555 ? 
63  AD3 8  ASN B 584 ? ASN B 593  . ? 1_555 ? 
64  AD3 8  ASN B 584 ? ASN B 593  . ? 2_565 ? 
65  AD3 8  GLY B 585 ? GLY B 594  . ? 2_565 ? 
66  AD3 8  GLY B 585 ? GLY B 594  . ? 1_555 ? 
67  AD3 8  HOH U .   ? HOH B 1208 . ? 2_565 ? 
68  AD3 8  HOH U .   ? HOH B 1208 . ? 1_555 ? 
69  AD4 3  LYS B 10  ? LYS B 19   . ? 1_555 ? 
70  AD4 3  GLN B 150 ? GLN B 159  . ? 1_555 ? 
71  AD4 3  TYR B 416 ? TYR B 425  . ? 1_555 ? 
72  AD5 5  ARG B 140 ? ARG B 149  . ? 1_555 ? 
73  AD5 5  ILE B 374 ? ILE B 383  . ? 1_555 ? 
74  AD5 5  VAL B 375 ? VAL B 384  . ? 1_555 ? 
75  AD5 5  HOH U .   ? HOH B 1035 . ? 1_555 ? 
76  AD5 5  HOH U .   ? HOH B 1333 . ? 1_555 ? 
77  AD6 11 ASN B 584 ? ASN B 593  . ? 1_555 ? 
78  AD6 11 LYS B 586 ? LYS B 595  . ? 1_555 ? 
79  AD6 11 TYR B 590 ? TYR B 599  . ? 1_555 ? 
80  AD6 11 ARG B 593 ? ARG B 602  . ? 1_555 ? 
81  AD6 11 ASN B 594 ? ASN B 603  . ? 1_555 ? 
82  AD6 11 HOH U .   ? HOH B 824  . ? 1_555 ? 
83  AD6 11 HOH U .   ? HOH B 837  . ? 1_555 ? 
84  AD6 11 HOH U .   ? HOH B 847  . ? 1_555 ? 
85  AD6 11 HOH U .   ? HOH B 895  . ? 1_555 ? 
86  AD6 11 HOH U .   ? HOH B 1019 . ? 1_555 ? 
87  AD6 11 HOH U .   ? HOH B 1102 . ? 1_555 ? 
88  AD7 9  TYR B 271 ? TYR B 280  . ? 1_555 ? 
89  AD7 9  ASP B 345 ? ASP B 354  . ? 1_555 ? 
90  AD7 9  ARG B 346 ? ARG B 355  . ? 1_555 ? 
91  AD7 9  HOH U .   ? HOH B 814  . ? 1_555 ? 
92  AD7 9  HOH U .   ? HOH B 915  . ? 1_555 ? 
93  AD7 9  HOH U .   ? HOH B 1128 . ? 1_555 ? 
94  AD7 9  HOH U .   ? HOH B 1131 . ? 1_555 ? 
95  AD7 9  HOH U .   ? HOH B 1155 . ? 1_555 ? 
96  AD7 9  HOH U .   ? HOH B 1222 . ? 1_555 ? 
97  AD8 6  HIS B 460 ? HIS B 469  . ? 1_555 ? 
98  AD8 6  GLU B 477 ? GLU B 486  . ? 1_555 ? 
99  AD8 6  HIS B 530 ? HIS B 539  . ? 1_555 ? 
100 AD8 6  HOH U .   ? HOH B 1196 . ? 1_555 ? 
101 AD8 6  HOH U .   ? HOH B 1235 . ? 1_555 ? 
102 AD8 6  HOH U .   ? HOH B 1321 . ? 1_555 ? 
103 AD9 6  ALA B 533 ? ALA B 542  . ? 2_565 ? 
104 AD9 6  SER B 537 ? SER B 546  . ? 1_555 ? 
105 AD9 6  SER B 537 ? SER B 546  . ? 2_565 ? 
106 AD9 6  ASN B 539 ? ASN B 548  . ? 1_555 ? 
107 AD9 6  PHE B 606 ? PHE B 615  . ? 1_555 ? 
108 AD9 6  ASN B 609 ? ASN B 618  . ? 1_555 ? 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A HOH 1320 ? ? O A HOH 1422 ? ? 1.61 
2 1 O   B HOH 1124 ? ? O B HOH 1362 ? ? 1.82 
3 1 OD1 A ASP 11   ? ? O A HOH 801  ? ? 2.03 
4 1 OD2 A ASP 11   ? ? O A HOH 802  ? ? 2.03 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 CA B GLY 545 ? ? 1_555 CA B GLY 547 ? ? 2_565 1.58 
2 1 N  B SER 546 ? ? 1_555 C  B SER 546 ? ? 2_565 1.98 
3 1 O  A ASN 131 ? ? 1_555 CG A ASN 580 ? ? 4_455 2.15 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CB A SER 187 ? ? OG A SER 187 ? B 1.496 1.418 0.078 0.013 N 
2 1 CA B ARG 18  ? ? CB B ARG 18  ? B 1.686 1.535 0.151 0.022 N 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_1             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              18 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             B 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              18 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             C 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              18 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                97.17 
_pdbx_validate_rmsd_angle.angle_target_value         110.40 
_pdbx_validate_rmsd_angle.angle_deviation            -13.23 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.00 
_pdbx_validate_rmsd_angle.linker_flag                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 TYR A 49  ? ? 57.05   -117.84 
2  1 LEU A 79  ? ? 69.37   165.86  
3  1 ASN A 80  ? ? -149.48 31.53   
4  1 ASP A 123 ? ? -155.11 -38.46  
5  1 ALA A 124 ? ? 65.18   -161.79 
6  1 SER A 126 ? ? -164.43 90.17   
7  1 THR A 127 ? ? -91.23  49.30   
8  1 ALA A 129 ? ? 70.09   -165.84 
9  1 MET A 134 ? ? -160.63 99.62   
10 1 GLU A 451 ? ? -152.55 -42.57  
11 1 HIS A 469 ? ? 62.34   -162.69 
12 1 SER A 543 ? ? -162.26 -78.92  
13 1 ASN A 544 ? ? -154.67 -158.90 
14 1 SER A 546 ? ? -51.81  -74.93  
15 1 TYR B 49  ? ? 59.68   -110.10 
16 1 LEU B 79  ? ? 73.52   165.53  
17 1 ASN B 80  ? ? -148.22 26.72   
18 1 SER B 126 ? ? 177.25  122.96  
19 1 THR B 127 ? ? -151.05 -64.49  
20 1 LYS B 128 ? ? -179.05 127.50  
21 1 ASN B 131 ? ? -67.98  30.13   
22 1 MET B 134 ? ? -55.31  -75.03  
23 1 SER B 351 ? ? -133.05 -159.88 
24 1 GLU B 451 ? ? -136.48 -59.77  
25 1 PRO B 452 ? ? -29.37  -32.61  
26 1 ASP B 453 ? ? -68.69  8.94    
27 1 HIS B 469 ? ? 64.62   -163.16 
28 1 ALA B 542 ? ? 143.38  -64.43  
29 1 SER B 543 ? ? 78.77   37.38   
30 1 SER B 546 ? ? -162.03 64.98   
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 TYR A 113 ? ? 0.074 'SIDE CHAIN' 
2 1 TYR B 606 ? ? 0.074 'SIDE CHAIN' 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 B CA 703 ? L CA . 
2 1 B NA 705 ? N NA . 
# 
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 0 A ALA 124 ? A ALA 115 
2  1 Y 0 A ASN 125 ? A ASN 116 
3  1 Y 0 A SER 126 ? A SER 117 
4  1 Y 0 A THR 127 ? A THR 118 
5  1 Y 0 A LYS 128 ? A LYS 119 
6  1 Y 0 A ALA 129 ? A ALA 120 
7  1 Y 0 A VAL 130 ? A VAL 121 
8  1 Y 0 A ASN 131 ? A ASN 122 
9  1 Y 0 A GLU 132 ? A GLU 123 
10 1 Y 0 B SER 126 ? B SER 117 
11 1 Y 0 B THR 127 ? B THR 118 
12 1 Y 0 B LYS 128 ? B LYS 119 
13 1 Y 0 B ALA 129 ? B ALA 120 
14 1 Y 0 B VAL 130 ? B VAL 121 
15 1 Y 0 B PRO 452 ? B PRO 443 
16 1 Y 0 B ASP 453 ? B ASP 444 
17 1 Y 0 B SER 543 ? B SER 534 
18 1 Y 0 B ASN 544 ? B ASN 535 
19 1 Y 0 B GLY 545 ? B GLY 536 
# 
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  
CIT C1   C  N N 75  
CIT O1   O  N N 76  
CIT O2   O  N N 77  
CIT C2   C  N N 78  
CIT C3   C  N N 79  
CIT O7   O  N N 80  
CIT C4   C  N N 81  
CIT C5   C  N N 82  
CIT O3   O  N N 83  
CIT O4   O  N N 84  
CIT C6   C  N N 85  
CIT O5   O  N N 86  
CIT O6   O  N N 87  
CIT HO2  H  N N 88  
CIT H21  H  N N 89  
CIT H22  H  N N 90  
CIT HO7  H  N N 91  
CIT H41  H  N N 92  
CIT H42  H  N N 93  
CIT HO4  H  N N 94  
CIT HO6  H  N N 95  
CL  CL   CL N N 96  
CYS N    N  N N 97  
CYS CA   C  N R 98  
CYS C    C  N N 99  
CYS O    O  N N 100 
CYS CB   C  N N 101 
CYS SG   S  N N 102 
CYS OXT  O  N N 103 
CYS H    H  N N 104 
CYS H2   H  N N 105 
CYS HA   H  N N 106 
CYS HB2  H  N N 107 
CYS HB3  H  N N 108 
CYS HG   H  N N 109 
CYS HXT  H  N N 110 
GLN N    N  N N 111 
GLN CA   C  N S 112 
GLN C    C  N N 113 
GLN O    O  N N 114 
GLN CB   C  N N 115 
GLN CG   C  N N 116 
GLN CD   C  N N 117 
GLN OE1  O  N N 118 
GLN NE2  N  N N 119 
GLN OXT  O  N N 120 
GLN H    H  N N 121 
GLN H2   H  N N 122 
GLN HA   H  N N 123 
GLN HB2  H  N N 124 
GLN HB3  H  N N 125 
GLN HG2  H  N N 126 
GLN HG3  H  N N 127 
GLN HE21 H  N N 128 
GLN HE22 H  N N 129 
GLN HXT  H  N N 130 
GLU N    N  N N 131 
GLU CA   C  N S 132 
GLU C    C  N N 133 
GLU O    O  N N 134 
GLU CB   C  N N 135 
GLU CG   C  N N 136 
GLU CD   C  N N 137 
GLU OE1  O  N N 138 
GLU OE2  O  N N 139 
GLU OXT  O  N N 140 
GLU H    H  N N 141 
GLU H2   H  N N 142 
GLU HA   H  N N 143 
GLU HB2  H  N N 144 
GLU HB3  H  N N 145 
GLU HG2  H  N N 146 
GLU HG3  H  N N 147 
GLU HE2  H  N N 148 
GLU HXT  H  N N 149 
GLY N    N  N N 150 
GLY CA   C  N N 151 
GLY C    C  N N 152 
GLY O    O  N N 153 
GLY OXT  O  N N 154 
GLY H    H  N N 155 
GLY H2   H  N N 156 
GLY HA2  H  N N 157 
GLY HA3  H  N N 158 
GLY HXT  H  N N 159 
HIS N    N  N N 160 
HIS CA   C  N S 161 
HIS C    C  N N 162 
HIS O    O  N N 163 
HIS CB   C  N N 164 
HIS CG   C  Y N 165 
HIS ND1  N  Y N 166 
HIS CD2  C  Y N 167 
HIS CE1  C  Y N 168 
HIS NE2  N  Y N 169 
HIS OXT  O  N N 170 
HIS H    H  N N 171 
HIS H2   H  N N 172 
HIS HA   H  N N 173 
HIS HB2  H  N N 174 
HIS HB3  H  N N 175 
HIS HD1  H  N N 176 
HIS HD2  H  N N 177 
HIS HE1  H  N N 178 
HIS HE2  H  N N 179 
HIS HXT  H  N N 180 
HOH O    O  N N 181 
HOH H1   H  N N 182 
HOH H2   H  N N 183 
ILE N    N  N N 184 
ILE CA   C  N S 185 
ILE C    C  N N 186 
ILE O    O  N N 187 
ILE CB   C  N S 188 
ILE CG1  C  N N 189 
ILE CG2  C  N N 190 
ILE CD1  C  N N 191 
ILE OXT  O  N N 192 
ILE H    H  N N 193 
ILE H2   H  N N 194 
ILE HA   H  N N 195 
ILE HB   H  N N 196 
ILE HG12 H  N N 197 
ILE HG13 H  N N 198 
ILE HG21 H  N N 199 
ILE HG22 H  N N 200 
ILE HG23 H  N N 201 
ILE HD11 H  N N 202 
ILE HD12 H  N N 203 
ILE HD13 H  N N 204 
ILE HXT  H  N N 205 
LEU N    N  N N 206 
LEU CA   C  N S 207 
LEU C    C  N N 208 
LEU O    O  N N 209 
LEU CB   C  N N 210 
LEU CG   C  N N 211 
LEU CD1  C  N N 212 
LEU CD2  C  N N 213 
LEU OXT  O  N N 214 
LEU H    H  N N 215 
LEU H2   H  N N 216 
LEU HA   H  N N 217 
LEU HB2  H  N N 218 
LEU HB3  H  N N 219 
LEU HG   H  N N 220 
LEU HD11 H  N N 221 
LEU HD12 H  N N 222 
LEU HD13 H  N N 223 
LEU HD21 H  N N 224 
LEU HD22 H  N N 225 
LEU HD23 H  N N 226 
LEU HXT  H  N N 227 
LYS N    N  N N 228 
LYS CA   C  N S 229 
LYS C    C  N N 230 
LYS O    O  N N 231 
LYS CB   C  N N 232 
LYS CG   C  N N 233 
LYS CD   C  N N 234 
LYS CE   C  N N 235 
LYS NZ   N  N N 236 
LYS OXT  O  N N 237 
LYS H    H  N N 238 
LYS H2   H  N N 239 
LYS HA   H  N N 240 
LYS HB2  H  N N 241 
LYS HB3  H  N N 242 
LYS HG2  H  N N 243 
LYS HG3  H  N N 244 
LYS HD2  H  N N 245 
LYS HD3  H  N N 246 
LYS HE2  H  N N 247 
LYS HE3  H  N N 248 
LYS HZ1  H  N N 249 
LYS HZ2  H  N N 250 
LYS HZ3  H  N N 251 
LYS HXT  H  N N 252 
MET N    N  N N 253 
MET CA   C  N S 254 
MET C    C  N N 255 
MET O    O  N N 256 
MET CB   C  N N 257 
MET CG   C  N N 258 
MET SD   S  N N 259 
MET CE   C  N N 260 
MET OXT  O  N N 261 
MET H    H  N N 262 
MET H2   H  N N 263 
MET HA   H  N N 264 
MET HB2  H  N N 265 
MET HB3  H  N N 266 
MET HG2  H  N N 267 
MET HG3  H  N N 268 
MET HE1  H  N N 269 
MET HE2  H  N N 270 
MET HE3  H  N N 271 
MET HXT  H  N N 272 
NA  NA   NA N N 273 
PHE N    N  N N 274 
PHE CA   C  N S 275 
PHE C    C  N N 276 
PHE O    O  N N 277 
PHE CB   C  N N 278 
PHE CG   C  Y N 279 
PHE CD1  C  Y N 280 
PHE CD2  C  Y N 281 
PHE CE1  C  Y N 282 
PHE CE2  C  Y N 283 
PHE CZ   C  Y N 284 
PHE OXT  O  N N 285 
PHE H    H  N N 286 
PHE H2   H  N N 287 
PHE HA   H  N N 288 
PHE HB2  H  N N 289 
PHE HB3  H  N N 290 
PHE HD1  H  N N 291 
PHE HD2  H  N N 292 
PHE HE1  H  N N 293 
PHE HE2  H  N N 294 
PHE HZ   H  N N 295 
PHE HXT  H  N N 296 
PRO N    N  N N 297 
PRO CA   C  N S 298 
PRO C    C  N N 299 
PRO O    O  N N 300 
PRO CB   C  N N 301 
PRO CG   C  N N 302 
PRO CD   C  N N 303 
PRO OXT  O  N N 304 
PRO H    H  N N 305 
PRO HA   H  N N 306 
PRO HB2  H  N N 307 
PRO HB3  H  N N 308 
PRO HG2  H  N N 309 
PRO HG3  H  N N 310 
PRO HD2  H  N N 311 
PRO HD3  H  N N 312 
PRO HXT  H  N N 313 
SER N    N  N N 314 
SER CA   C  N S 315 
SER C    C  N N 316 
SER O    O  N N 317 
SER CB   C  N N 318 
SER OG   O  N N 319 
SER OXT  O  N N 320 
SER H    H  N N 321 
SER H2   H  N N 322 
SER HA   H  N N 323 
SER HB2  H  N N 324 
SER HB3  H  N N 325 
SER HG   H  N N 326 
SER HXT  H  N N 327 
THR N    N  N N 328 
THR CA   C  N S 329 
THR C    C  N N 330 
THR O    O  N N 331 
THR CB   C  N R 332 
THR OG1  O  N N 333 
THR CG2  C  N N 334 
THR OXT  O  N N 335 
THR H    H  N N 336 
THR H2   H  N N 337 
THR HA   H  N N 338 
THR HB   H  N N 339 
THR HG1  H  N N 340 
THR HG21 H  N N 341 
THR HG22 H  N N 342 
THR HG23 H  N N 343 
THR HXT  H  N N 344 
TRP N    N  N N 345 
TRP CA   C  N S 346 
TRP C    C  N N 347 
TRP O    O  N N 348 
TRP CB   C  N N 349 
TRP CG   C  Y N 350 
TRP CD1  C  Y N 351 
TRP CD2  C  Y N 352 
TRP NE1  N  Y N 353 
TRP CE2  C  Y N 354 
TRP CE3  C  Y N 355 
TRP CZ2  C  Y N 356 
TRP CZ3  C  Y N 357 
TRP CH2  C  Y N 358 
TRP OXT  O  N N 359 
TRP H    H  N N 360 
TRP H2   H  N N 361 
TRP HA   H  N N 362 
TRP HB2  H  N N 363 
TRP HB3  H  N N 364 
TRP HD1  H  N N 365 
TRP HE1  H  N N 366 
TRP HE3  H  N N 367 
TRP HZ2  H  N N 368 
TRP HZ3  H  N N 369 
TRP HH2  H  N N 370 
TRP HXT  H  N N 371 
TYR N    N  N N 372 
TYR CA   C  N S 373 
TYR C    C  N N 374 
TYR O    O  N N 375 
TYR CB   C  N N 376 
TYR CG   C  Y N 377 
TYR CD1  C  Y N 378 
TYR CD2  C  Y N 379 
TYR CE1  C  Y N 380 
TYR CE2  C  Y N 381 
TYR CZ   C  Y N 382 
TYR OH   O  N N 383 
TYR OXT  O  N N 384 
TYR H    H  N N 385 
TYR H2   H  N N 386 
TYR HA   H  N N 387 
TYR HB2  H  N N 388 
TYR HB3  H  N N 389 
TYR HD1  H  N N 390 
TYR HD2  H  N N 391 
TYR HE1  H  N N 392 
TYR HE2  H  N N 393 
TYR HH   H  N N 394 
TYR HXT  H  N N 395 
VAL N    N  N N 396 
VAL CA   C  N S 397 
VAL C    C  N N 398 
VAL O    O  N N 399 
VAL CB   C  N N 400 
VAL CG1  C  N N 401 
VAL CG2  C  N N 402 
VAL OXT  O  N N 403 
VAL H    H  N N 404 
VAL H2   H  N N 405 
VAL HA   H  N N 406 
VAL HB   H  N N 407 
VAL HG11 H  N N 408 
VAL HG12 H  N N 409 
VAL HG13 H  N N 410 
VAL HG21 H  N N 411 
VAL HG22 H  N N 412 
VAL HG23 H  N N 413 
VAL HXT  H  N N 414 
ZN  ZN   ZN N N 415 
# 
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  
CIT C1  O1   doub N N 70  
CIT C1  O2   sing N N 71  
CIT C1  C2   sing N N 72  
CIT O2  HO2  sing N N 73  
CIT C2  C3   sing N N 74  
CIT C2  H21  sing N N 75  
CIT C2  H22  sing N N 76  
CIT C3  O7   sing N N 77  
CIT C3  C4   sing N N 78  
CIT C3  C6   sing N N 79  
CIT O7  HO7  sing N N 80  
CIT C4  C5   sing N N 81  
CIT C4  H41  sing N N 82  
CIT C4  H42  sing N N 83  
CIT C5  O3   doub N N 84  
CIT C5  O4   sing N N 85  
CIT O4  HO4  sing N N 86  
CIT C6  O5   doub N N 87  
CIT C6  O6   sing N N 88  
CIT O6  HO6  sing N N 89  
CYS N   CA   sing N N 90  
CYS N   H    sing N N 91  
CYS N   H2   sing N N 92  
CYS CA  C    sing N N 93  
CYS CA  CB   sing N N 94  
CYS CA  HA   sing N N 95  
CYS C   O    doub N N 96  
CYS C   OXT  sing N N 97  
CYS CB  SG   sing N N 98  
CYS CB  HB2  sing N N 99  
CYS CB  HB3  sing N N 100 
CYS SG  HG   sing N N 101 
CYS OXT HXT  sing N N 102 
GLN N   CA   sing N N 103 
GLN N   H    sing N N 104 
GLN N   H2   sing N N 105 
GLN CA  C    sing N N 106 
GLN CA  CB   sing N N 107 
GLN CA  HA   sing N N 108 
GLN C   O    doub N N 109 
GLN C   OXT  sing N N 110 
GLN CB  CG   sing N N 111 
GLN CB  HB2  sing N N 112 
GLN CB  HB3  sing N N 113 
GLN CG  CD   sing N N 114 
GLN CG  HG2  sing N N 115 
GLN CG  HG3  sing N N 116 
GLN CD  OE1  doub N N 117 
GLN CD  NE2  sing N N 118 
GLN NE2 HE21 sing N N 119 
GLN NE2 HE22 sing N N 120 
GLN OXT HXT  sing N N 121 
GLU N   CA   sing N N 122 
GLU N   H    sing N N 123 
GLU N   H2   sing N N 124 
GLU CA  C    sing N N 125 
GLU CA  CB   sing N N 126 
GLU CA  HA   sing N N 127 
GLU C   O    doub N N 128 
GLU C   OXT  sing N N 129 
GLU CB  CG   sing N N 130 
GLU CB  HB2  sing N N 131 
GLU CB  HB3  sing N N 132 
GLU CG  CD   sing N N 133 
GLU CG  HG2  sing N N 134 
GLU CG  HG3  sing N N 135 
GLU CD  OE1  doub N N 136 
GLU CD  OE2  sing N N 137 
GLU OE2 HE2  sing N N 138 
GLU OXT HXT  sing N N 139 
GLY N   CA   sing N N 140 
GLY N   H    sing N N 141 
GLY N   H2   sing N N 142 
GLY CA  C    sing N N 143 
GLY CA  HA2  sing N N 144 
GLY CA  HA3  sing N N 145 
GLY C   O    doub N N 146 
GLY C   OXT  sing N N 147 
GLY OXT HXT  sing N N 148 
HIS N   CA   sing N N 149 
HIS N   H    sing N N 150 
HIS N   H2   sing N N 151 
HIS CA  C    sing N N 152 
HIS CA  CB   sing N N 153 
HIS CA  HA   sing N N 154 
HIS C   O    doub N N 155 
HIS C   OXT  sing N N 156 
HIS CB  CG   sing N N 157 
HIS CB  HB2  sing N N 158 
HIS CB  HB3  sing N N 159 
HIS CG  ND1  sing Y N 160 
HIS CG  CD2  doub Y N 161 
HIS ND1 CE1  doub Y N 162 
HIS ND1 HD1  sing N N 163 
HIS CD2 NE2  sing Y N 164 
HIS CD2 HD2  sing N N 165 
HIS CE1 NE2  sing Y N 166 
HIS CE1 HE1  sing N N 167 
HIS NE2 HE2  sing N N 168 
HIS OXT HXT  sing N N 169 
HOH O   H1   sing N N 170 
HOH O   H2   sing N N 171 
ILE N   CA   sing N N 172 
ILE N   H    sing N N 173 
ILE N   H2   sing N N 174 
ILE CA  C    sing N N 175 
ILE CA  CB   sing N N 176 
ILE CA  HA   sing N N 177 
ILE C   O    doub N N 178 
ILE C   OXT  sing N N 179 
ILE CB  CG1  sing N N 180 
ILE CB  CG2  sing N N 181 
ILE CB  HB   sing N N 182 
ILE CG1 CD1  sing N N 183 
ILE CG1 HG12 sing N N 184 
ILE CG1 HG13 sing N N 185 
ILE CG2 HG21 sing N N 186 
ILE CG2 HG22 sing N N 187 
ILE CG2 HG23 sing N N 188 
ILE CD1 HD11 sing N N 189 
ILE CD1 HD12 sing N N 190 
ILE CD1 HD13 sing N N 191 
ILE OXT HXT  sing N N 192 
LEU N   CA   sing N N 193 
LEU N   H    sing N N 194 
LEU N   H2   sing N N 195 
LEU CA  C    sing N N 196 
LEU CA  CB   sing N N 197 
LEU CA  HA   sing N N 198 
LEU C   O    doub N N 199 
LEU C   OXT  sing N N 200 
LEU CB  CG   sing N N 201 
LEU CB  HB2  sing N N 202 
LEU CB  HB3  sing N N 203 
LEU CG  CD1  sing N N 204 
LEU CG  CD2  sing N N 205 
LEU CG  HG   sing N N 206 
LEU CD1 HD11 sing N N 207 
LEU CD1 HD12 sing N N 208 
LEU CD1 HD13 sing N N 209 
LEU CD2 HD21 sing N N 210 
LEU CD2 HD22 sing N N 211 
LEU CD2 HD23 sing N N 212 
LEU OXT HXT  sing N N 213 
LYS N   CA   sing N N 214 
LYS N   H    sing N N 215 
LYS N   H2   sing N N 216 
LYS CA  C    sing N N 217 
LYS CA  CB   sing N N 218 
LYS CA  HA   sing N N 219 
LYS C   O    doub N N 220 
LYS C   OXT  sing N N 221 
LYS CB  CG   sing N N 222 
LYS CB  HB2  sing N N 223 
LYS CB  HB3  sing N N 224 
LYS CG  CD   sing N N 225 
LYS CG  HG2  sing N N 226 
LYS CG  HG3  sing N N 227 
LYS CD  CE   sing N N 228 
LYS CD  HD2  sing N N 229 
LYS CD  HD3  sing N N 230 
LYS CE  NZ   sing N N 231 
LYS CE  HE2  sing N N 232 
LYS CE  HE3  sing N N 233 
LYS NZ  HZ1  sing N N 234 
LYS NZ  HZ2  sing N N 235 
LYS NZ  HZ3  sing N N 236 
LYS OXT HXT  sing N N 237 
MET N   CA   sing N N 238 
MET N   H    sing N N 239 
MET N   H2   sing N N 240 
MET CA  C    sing N N 241 
MET CA  CB   sing N N 242 
MET CA  HA   sing N N 243 
MET C   O    doub N N 244 
MET C   OXT  sing N N 245 
MET CB  CG   sing N N 246 
MET CB  HB2  sing N N 247 
MET CB  HB3  sing N N 248 
MET CG  SD   sing N N 249 
MET CG  HG2  sing N N 250 
MET CG  HG3  sing N N 251 
MET SD  CE   sing N N 252 
MET CE  HE1  sing N N 253 
MET CE  HE2  sing N N 254 
MET CE  HE3  sing N N 255 
MET OXT HXT  sing N N 256 
PHE N   CA   sing N N 257 
PHE N   H    sing N N 258 
PHE N   H2   sing N N 259 
PHE CA  C    sing N N 260 
PHE CA  CB   sing N N 261 
PHE CA  HA   sing N N 262 
PHE C   O    doub N N 263 
PHE C   OXT  sing N N 264 
PHE CB  CG   sing N N 265 
PHE CB  HB2  sing N N 266 
PHE CB  HB3  sing N N 267 
PHE CG  CD1  doub Y N 268 
PHE CG  CD2  sing Y N 269 
PHE CD1 CE1  sing Y N 270 
PHE CD1 HD1  sing N N 271 
PHE CD2 CE2  doub Y N 272 
PHE CD2 HD2  sing N N 273 
PHE CE1 CZ   doub Y N 274 
PHE CE1 HE1  sing N N 275 
PHE CE2 CZ   sing Y N 276 
PHE CE2 HE2  sing N N 277 
PHE CZ  HZ   sing N N 278 
PHE OXT HXT  sing N N 279 
PRO N   CA   sing N N 280 
PRO N   CD   sing N N 281 
PRO N   H    sing N N 282 
PRO CA  C    sing N N 283 
PRO CA  CB   sing N N 284 
PRO CA  HA   sing N N 285 
PRO C   O    doub N N 286 
PRO C   OXT  sing N N 287 
PRO CB  CG   sing N N 288 
PRO CB  HB2  sing N N 289 
PRO CB  HB3  sing N N 290 
PRO CG  CD   sing N N 291 
PRO CG  HG2  sing N N 292 
PRO CG  HG3  sing N N 293 
PRO CD  HD2  sing N N 294 
PRO CD  HD3  sing N N 295 
PRO OXT HXT  sing N N 296 
SER N   CA   sing N N 297 
SER N   H    sing N N 298 
SER N   H2   sing N N 299 
SER CA  C    sing N N 300 
SER CA  CB   sing N N 301 
SER CA  HA   sing N N 302 
SER C   O    doub N N 303 
SER C   OXT  sing N N 304 
SER CB  OG   sing N N 305 
SER CB  HB2  sing N N 306 
SER CB  HB3  sing N N 307 
SER OG  HG   sing N N 308 
SER OXT HXT  sing N N 309 
THR N   CA   sing N N 310 
THR N   H    sing N N 311 
THR N   H2   sing N N 312 
THR CA  C    sing N N 313 
THR CA  CB   sing N N 314 
THR CA  HA   sing N N 315 
THR C   O    doub N N 316 
THR C   OXT  sing N N 317 
THR CB  OG1  sing N N 318 
THR CB  CG2  sing N N 319 
THR CB  HB   sing N N 320 
THR OG1 HG1  sing N N 321 
THR CG2 HG21 sing N N 322 
THR CG2 HG22 sing N N 323 
THR CG2 HG23 sing N N 324 
THR OXT HXT  sing N N 325 
TRP N   CA   sing N N 326 
TRP N   H    sing N N 327 
TRP N   H2   sing N N 328 
TRP CA  C    sing N N 329 
TRP CA  CB   sing N N 330 
TRP CA  HA   sing N N 331 
TRP C   O    doub N N 332 
TRP C   OXT  sing N N 333 
TRP CB  CG   sing N N 334 
TRP CB  HB2  sing N N 335 
TRP CB  HB3  sing N N 336 
TRP CG  CD1  doub Y N 337 
TRP CG  CD2  sing Y N 338 
TRP CD1 NE1  sing Y N 339 
TRP CD1 HD1  sing N N 340 
TRP CD2 CE2  doub Y N 341 
TRP CD2 CE3  sing Y N 342 
TRP NE1 CE2  sing Y N 343 
TRP NE1 HE1  sing N N 344 
TRP CE2 CZ2  sing Y N 345 
TRP CE3 CZ3  doub Y N 346 
TRP CE3 HE3  sing N N 347 
TRP CZ2 CH2  doub Y N 348 
TRP CZ2 HZ2  sing N N 349 
TRP CZ3 CH2  sing Y N 350 
TRP CZ3 HZ3  sing N N 351 
TRP CH2 HH2  sing N N 352 
TRP OXT HXT  sing N N 353 
TYR N   CA   sing N N 354 
TYR N   H    sing N N 355 
TYR N   H2   sing N N 356 
TYR CA  C    sing N N 357 
TYR CA  CB   sing N N 358 
TYR CA  HA   sing N N 359 
TYR C   O    doub N N 360 
TYR C   OXT  sing N N 361 
TYR CB  CG   sing N N 362 
TYR CB  HB2  sing N N 363 
TYR CB  HB3  sing N N 364 
TYR CG  CD1  doub Y N 365 
TYR CG  CD2  sing Y N 366 
TYR CD1 CE1  sing Y N 367 
TYR CD1 HD1  sing N N 368 
TYR CD2 CE2  doub Y N 369 
TYR CD2 HD2  sing N N 370 
TYR CE1 CZ   doub Y N 371 
TYR CE1 HE1  sing N N 372 
TYR CE2 CZ   sing Y N 373 
TYR CE2 HE2  sing N N 374 
TYR CZ  OH   sing N N 375 
TYR OH  HH   sing N N 376 
TYR OXT HXT  sing N N 377 
VAL N   CA   sing N N 378 
VAL N   H    sing N N 379 
VAL N   H2   sing N N 380 
VAL CA  C    sing N N 381 
VAL CA  CB   sing N N 382 
VAL CA  HA   sing N N 383 
VAL C   O    doub N N 384 
VAL C   OXT  sing N N 385 
VAL CB  CG1  sing N N 386 
VAL CB  CG2  sing N N 387 
VAL CB  HB   sing N N 388 
VAL CG1 HG11 sing N N 389 
VAL CG1 HG12 sing N N 390 
VAL CG1 HG13 sing N N 391 
VAL CG2 HG21 sing N N 392 
VAL CG2 HG22 sing N N 393 
VAL CG2 HG23 sing N N 394 
VAL OXT HXT  sing N N 395 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Slovenian Research Agency'     Slovenia P1-0048            1 
'Centre of Excellence CIPKeBiP' Slovenia OP13.1.1.2.02.0005 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1JWQ 
_pdbx_initial_refinement_model.details          'Cwp8 CWB2 trimer, 1JWQ' 
# 
_atom_sites.entry_id                    5J72 
_atom_sites.fract_transf_matrix[1][1]   0.010946 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.004697 
_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]   0.011774 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CA 
CL 
H  
N  
NA 
O  
S  
ZN 
# 
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   . SER A 1 1   ? 41.064  109.221 12.538  1.00 53.97  ? 10   SER A N   1 
ATOM   2     C  CA  . SER A 1 1   ? 40.019  110.161 12.151  1.00 48.38  ? 10   SER A CA  1 
ATOM   3     C  C   . SER A 1 1   ? 39.270  110.747 13.347  1.00 41.27  ? 10   SER A C   1 
ATOM   4     O  O   . SER A 1 1   ? 39.435  110.298 14.463  1.00 40.18  ? 10   SER A O   1 
ATOM   5     C  CB  . SER A 1 1   ? 39.061  109.479 11.199  1.00 46.79  ? 10   SER A CB  1 
ATOM   6     O  OG  . SER A 1 1   ? 39.800  109.175 10.028  1.00 50.36  ? 10   SER A OG  1 
ATOM   7     N  N   . ASP A 1 2   ? 38.500  111.756 13.125  1.00 36.20  ? 11   ASP A N   1 
ATOM   8     C  CA  . ASP A 1 2   ? 37.763  112.400 14.201  1.00 40.07  ? 11   ASP A CA  1 
ATOM   9     C  C   . ASP A 1 2   ? 36.739  111.476 14.820  1.00 33.87  ? 11   ASP A C   1 
ATOM   10    O  O   . ASP A 1 2   ? 36.501  111.558 16.028  1.00 31.33  ? 11   ASP A O   1 
ATOM   11    C  CB  . ASP A 1 2   ? 37.046  113.635 13.651  1.00 44.77  ? 11   ASP A CB  1 
ATOM   12    C  CG  . ASP A 1 2   ? 38.084  114.675 13.216  1.00 57.79  ? 11   ASP A CG  1 
ATOM   13    O  OD1 . ASP A 1 2   ? 39.046  114.920 13.996  1.00 63.34  ? 11   ASP A OD1 1 
ATOM   14    O  OD2 . ASP A 1 2   ? 37.944  115.225 12.098  1.00 58.09  ? 11   ASP A OD2 1 
ATOM   15    N  N   . ILE A 1 3   ? 36.146  110.591 13.989  1.00 29.92  ? 12   ILE A N   1 
ATOM   16    C  CA  . ILE A 1 3   ? 35.147  109.651 14.467  1.00 25.85  ? 12   ILE A CA  1 
ATOM   17    C  C   . ILE A 1 3   ? 35.268  108.370 13.698  1.00 27.86  ? 12   ILE A C   1 
ATOM   18    O  O   . ILE A 1 3   ? 35.417  108.416 12.465  1.00 28.99  ? 12   ILE A O   1 
ATOM   19    C  CB  . ILE A 1 3   ? 33.723  110.260 14.350  1.00 26.98  ? 12   ILE A CB  1 
ATOM   20    C  CG1 . ILE A 1 3   ? 32.690  109.255 14.841  1.00 28.23  ? 12   ILE A CG1 1 
ATOM   21    C  CG2 . ILE A 1 3   ? 33.463  110.684 12.889  1.00 31.58  ? 12   ILE A CG2 1 
ATOM   22    C  CD1 . ILE A 1 3   ? 31.337  109.922 15.144  1.00 38.97  ? 12   ILE A CD1 1 
ATOM   23    N  N   . ASN A 1 4   ? 35.235  107.241 14.377  1.00 22.93  ? 13   ASN A N   1 
ATOM   24    C  CA  . ASN A 1 4   ? 35.316  105.978 13.654  1.00 19.99  ? 13   ASN A CA  1 
ATOM   25    C  C   . ASN A 1 4   ? 34.155  105.130 14.186  1.00 21.59  ? 13   ASN A C   1 
ATOM   26    O  O   . ASN A 1 4   ? 34.002  105.038 15.410  1.00 22.60  ? 13   ASN A O   1 
ATOM   27    C  CB  . ASN A 1 4   ? 36.650  105.234 13.941  1.00 23.50  ? 13   ASN A CB  1 
ATOM   28    C  CG  . ASN A 1 4   ? 36.650  103.894 13.144  1.00 29.83  ? 13   ASN A CG  1 
ATOM   29    O  OD1 . ASN A 1 4   ? 36.225  102.822 13.669  1.00 31.31  ? 13   ASN A OD1 1 
ATOM   30    N  ND2 . ASN A 1 4   ? 37.018  103.875 11.861  1.00 31.36  ? 13   ASN A ND2 1 
ATOM   31    N  N   . ILE A 1 5   ? 33.350  104.543 13.325  1.00 19.86  ? 14   ILE A N   1 
ATOM   32    C  CA  . ILE A 1 5   ? 32.246  103.708 13.825  1.00 21.33  ? 14   ILE A CA  1 
ATOM   33    C  C   . ILE A 1 5   ? 32.516  102.246 13.353  1.00 23.52  ? 14   ILE A C   1 
ATOM   34    O  O   . ILE A 1 5   ? 32.532  101.996 12.147  1.00 24.23  ? 14   ILE A O   1 
ATOM   35    C  CB  . ILE A 1 5   ? 30.931  104.227 13.202  1.00 19.75  ? 14   ILE A CB  1 
ATOM   36    C  CG1 . ILE A 1 5   ? 30.620  105.647 13.707  1.00 19.75  ? 14   ILE A CG1 1 
ATOM   37    C  CG2 . ILE A 1 5   ? 29.780  103.307 13.563  1.00 19.83  ? 14   ILE A CG2 1 
ATOM   38    C  CD1 . ILE A 1 5   ? 29.376  106.271 12.927  1.00 21.93  ? 14   ILE A CD1 1 
ATOM   39    N  N   . ASN A 1 6   ? 32.619  101.332 14.255  1.00 17.72  ? 15   ASN A N   1 
ATOM   40    C  CA  . ASN A 1 6   ? 32.915  99.939  13.870  1.00 17.09  ? 15   ASN A CA  1 
ATOM   41    C  C   . ASN A 1 6   ? 31.732  99.038  14.215  1.00 18.79  ? 15   ASN A C   1 
ATOM   42    O  O   . ASN A 1 6   ? 31.502  98.785  15.410  1.00 21.75  ? 15   ASN A O   1 
ATOM   43    C  CB  . ASN A 1 6   ? 34.130  99.469  14.652  1.00 21.42  ? 15   ASN A CB  1 
ATOM   44    C  CG  . ASN A 1 6   ? 34.534  98.039  14.213  1.00 33.82  ? 15   ASN A CG  1 
ATOM   45    O  OD1 . ASN A 1 6   ? 34.325  97.621  13.049  1.00 32.57  ? 15   ASN A OD1 1 
ATOM   46    N  ND2 . ASN A 1 6   ? 35.172  97.257  15.044  1.00 38.09  ? 15   ASN A ND2 1 
ATOM   47    N  N   . LEU A 1 7   ? 30.996  98.583  13.189  1.00 17.84  ? 16   LEU A N   1 
ATOM   48    C  CA  . LEU A 1 7   ? 29.827  97.720  13.402  1.00 15.79  ? 16   LEU A CA  1 
ATOM   49    C  C   . LEU A 1 7   ? 30.251  96.275  13.104  1.00 17.49  ? 16   LEU A C   1 
ATOM   50    O  O   . LEU A 1 7   ? 30.941  96.020  12.111  1.00 20.02  ? 16   LEU A O   1 
ATOM   51    C  CB  . LEU A 1 7   ? 28.677  98.100  12.438  1.00 18.28  ? 16   LEU A CB  1 
ATOM   52    C  CG  . LEU A 1 7   ? 28.178  99.561  12.646  1.00 20.02  ? 16   LEU A CG  1 
ATOM   53    C  CD1 . LEU A 1 7   ? 26.934  99.775  11.682  1.00 19.49  ? 16   LEU A CD1 1 
ATOM   54    C  CD2 . LEU A 1 7   ? 27.831  99.823  14.135  1.00 20.48  ? 16   LEU A CD2 1 
ATOM   55    N  N   . GLN A 1 8   ? 29.845  95.359  13.952  1.00 17.83  ? 17   GLN A N   1 
ATOM   56    C  CA  . GLN A 1 8   ? 30.277  93.943  13.713  1.00 19.34  ? 17   GLN A CA  1 
ATOM   57    C  C   . GLN A 1 8   ? 29.627  93.277  12.478  1.00 21.89  ? 17   GLN A C   1 
ATOM   58    O  O   . GLN A 1 8   ? 30.320  92.607  11.676  1.00 20.45  ? 17   GLN A O   1 
ATOM   59    C  CB  . GLN A 1 8   ? 29.979  93.141  14.958  1.00 18.20  ? 17   GLN A CB  1 
ATOM   60    C  CG  . GLN A 1 8   ? 30.304  91.609  14.783  1.00 18.83  ? 17   GLN A CG  1 
ATOM   61    C  CD  . GLN A 1 8   ? 29.907  90.858  16.035  1.00 22.94  ? 17   GLN A CD  1 
ATOM   62    O  OE1 . GLN A 1 8   ? 28.971  91.244  16.729  1.00 18.52  ? 17   GLN A OE1 1 
ATOM   63    N  NE2 . GLN A 1 8   ? 30.605  89.711  16.328  1.00 17.63  ? 17   GLN A NE2 1 
ATOM   64    N  N   . ARG A 1 9   ? 28.300  93.491  12.282  1.00 20.84  ? 18   ARG A N   1 
ATOM   65    C  CA  . ARG A 1 9   ? 27.516  92.800  11.217  1.00 21.67  ? 18   ARG A CA  1 
ATOM   66    C  C   . ARG A 1 9   ? 26.825  93.766  10.332  1.00 20.23  ? 18   ARG A C   1 
ATOM   67    O  O   . ARG A 1 9   ? 26.290  94.742  10.829  1.00 20.08  ? 18   ARG A O   1 
ATOM   68    C  CB  . ARG A 1 9   ? 26.359  91.972  11.841  1.00 19.67  ? 18   ARG A CB  1 
ATOM   69    C  CG  . ARG A 1 9   ? 26.729  91.159  13.072  1.00 29.93  ? 18   ARG A CG  1 
ATOM   70    C  CD  . ARG A 1 9   ? 25.822  89.915  13.284  1.00 30.30  ? 18   ARG A CD  1 
ATOM   71    N  NE  . ARG A 1 9   ? 26.259  89.304  14.562  1.00 39.45  ? 18   ARG A NE  1 
ATOM   72    C  CZ  . ARG A 1 9   ? 27.245  88.406  14.697  1.00 35.11  ? 18   ARG A CZ  1 
ATOM   73    N  NH1 . ARG A 1 9   ? 27.598  87.975  15.896  1.00 33.95  ? 18   ARG A NH1 1 
ATOM   74    N  NH2 . ARG A 1 9   ? 27.855  87.922  13.638  1.00 22.61  ? 18   ARG A NH2 1 
ATOM   75    N  N   . LYS A 1 10  ? 26.814  93.515  8.999   1.00 19.22  ? 19   LYS A N   1 
ATOM   76    C  CA  . LYS A 1 10  ? 26.122  94.391  8.071   1.00 20.31  ? 19   LYS A CA  1 
ATOM   77    C  C   . LYS A 1 10  ? 24.894  93.658  7.484   1.00 17.35  ? 19   LYS A C   1 
ATOM   78    O  O   . LYS A 1 10  ? 24.088  94.245  6.757   1.00 18.92  ? 19   LYS A O   1 
ATOM   79    C  CB  . LYS A 1 10  ? 27.051  94.756  6.935   1.00 20.54  ? 19   LYS A CB  1 
ATOM   80    C  CG  . LYS A 1 10  ? 28.309  95.533  7.438   1.00 27.94  ? 19   LYS A CG  1 
ATOM   81    C  CD  . LYS A 1 10  ? 27.867  96.766  8.259   1.00 28.66  ? 19   LYS A CD  1 
ATOM   82    C  CE  . LYS A 1 10  ? 27.809  98.030  7.462   1.00 39.39  ? 19   LYS A CE  1 
ATOM   83    N  NZ  . LYS A 1 10  ? 28.866  98.121  6.364   1.00 32.52  ? 19   LYS A NZ  1 
ATOM   84    N  N   . SER A 1 11  ? 24.768  92.367  7.790   1.00 17.43  ? 20   SER A N   1 
ATOM   85    C  CA  . SER A 1 11  ? 23.596  91.564  7.374   1.00 18.65  ? 20   SER A CA  1 
ATOM   86    C  C   . SER A 1 11  ? 23.075  90.895  8.652   1.00 20.64  ? 20   SER A C   1 
ATOM   87    O  O   . SER A 1 11  ? 23.858  90.212  9.351   1.00 19.73  ? 20   SER A O   1 
ATOM   88    C  CB  . SER A 1 11  ? 24.018  90.529  6.332   1.00 20.88  ? 20   SER A CB  1 
ATOM   89    O  OG  . SER A 1 11  ? 22.894  89.798  5.883   1.00 25.86  ? 20   SER A OG  1 
ATOM   90    N  N   . VAL A 1 12  ? 21.801  91.103  9.014   1.00 17.57  ? 21   VAL A N   1 
ATOM   91    C  CA  . VAL A 1 12  ? 21.261  90.557  10.259  1.00 17.32  ? 21   VAL A CA  1 
ATOM   92    C  C   . VAL A 1 12  ? 19.854  89.950  9.996   1.00 15.00  ? 21   VAL A C   1 
ATOM   93    O  O   . VAL A 1 12  ? 19.418  89.956  8.847   1.00 15.71  ? 21   VAL A O   1 
ATOM   94    C  CB  . VAL A 1 12  ? 21.162  91.687  11.349  1.00 15.73  ? 21   VAL A CB  1 
ATOM   95    C  CG1 . VAL A 1 12  ? 22.570  92.251  11.650  1.00 17.94  ? 21   VAL A CG1 1 
ATOM   96    C  CG2 . VAL A 1 12  ? 20.230  92.813  10.889  1.00 16.90  ? 21   VAL A CG2 1 
ATOM   97    N  N   . VAL A 1 13  ? 19.217  89.460  11.037  1.00 15.75  ? 22   VAL A N   1 
ATOM   98    C  CA  . VAL A 1 13  ? 17.819  88.990  10.942  1.00 15.14  ? 22   VAL A CA  1 
ATOM   99    C  C   . VAL A 1 13  ? 17.189  89.505  12.236  1.00 16.76  ? 22   VAL A C   1 
ATOM   100   O  O   . VAL A 1 13  ? 17.859  89.991  13.118  1.00 16.76  ? 22   VAL A O   1 
ATOM   101   C  CB  . VAL A 1 13  ? 17.667  87.429  10.852  1.00 17.87  ? 22   VAL A CB  1 
ATOM   102   C  CG1 . VAL A 1 13  ? 18.401  86.865  9.615   1.00 17.17  ? 22   VAL A CG1 1 
ATOM   103   C  CG2 . VAL A 1 13  ? 18.266  86.791  12.090  1.00 16.08  ? 22   VAL A CG2 1 
ATOM   104   N  N   . LEU A 1 14  ? 15.874  89.381  12.368  1.00 17.83  ? 23   LEU A N   1 
ATOM   105   C  CA  . LEU A 1 14  ? 15.203  89.785  13.617  1.00 17.65  ? 23   LEU A CA  1 
ATOM   106   C  C   . LEU A 1 14  ? 15.787  89.007  14.775  1.00 17.08  ? 23   LEU A C   1 
ATOM   107   O  O   . LEU A 1 14  ? 15.876  87.743  14.694  1.00 17.66  ? 23   LEU A O   1 
ATOM   108   C  CB  . LEU A 1 14  ? 13.671  89.493  13.414  1.00 15.82  ? 23   LEU A CB  1 
ATOM   109   C  CG  . LEU A 1 14  ? 12.809  89.945  14.610  1.00 17.84  ? 23   LEU A CG  1 
ATOM   110   C  CD1 . LEU A 1 14  ? 12.763  91.509  14.734  1.00 16.47  ? 23   LEU A CD1 1 
ATOM   111   C  CD2 . LEU A 1 14  ? 11.352  89.435  14.361  1.00 20.00  ? 23   LEU A CD2 1 
ATOM   112   N  N   . GLY A 1 15  ? 16.218  89.707  15.828  1.00 18.41  ? 24   GLY A N   1 
ATOM   113   C  CA  . GLY A 1 15  ? 16.806  89.072  16.991  1.00 22.16  ? 24   GLY A CA  1 
ATOM   114   C  C   . GLY A 1 15  ? 18.339  89.061  16.955  1.00 22.36  ? 24   GLY A C   1 
ATOM   115   O  O   . GLY A 1 15  ? 18.960  88.664  17.933  1.00 20.57  ? 24   GLY A O   1 
ATOM   116   N  N   . SER A 1 16  ? 18.973  89.461  15.845  1.00 19.45  ? 25   SER A N   1 
ATOM   117   C  CA  . SER A 1 16  ? 20.472  89.453  15.858  1.00 18.87  ? 25   SER A CA  1 
ATOM   118   C  C   . SER A 1 16  ? 21.025  90.440  16.846  1.00 19.91  ? 25   SER A C   1 
ATOM   119   O  O   . SER A 1 16  ? 20.387  91.439  17.224  1.00 18.41  ? 25   SER A O   1 
ATOM   120   C  CB  . SER A 1 16  ? 21.052  89.864  14.499  1.00 16.72  ? 25   SER A CB  1 
ATOM   121   O  OG  . SER A 1 16  ? 20.739  88.936  13.477  1.00 18.21  ? 25   SER A OG  1 
ATOM   122   N  N   . LYS A 1 17  ? 22.292  90.203  17.234  1.00 16.97  ? 26   LYS A N   1 
ATOM   123   C  CA  . LYS A 1 17  ? 23.028  91.128  18.108  1.00 18.69  ? 26   LYS A CA  1 
ATOM   124   C  C   . LYS A 1 17  ? 24.282  91.510  17.333  1.00 18.67  ? 26   LYS A C   1 
ATOM   125   O  O   . LYS A 1 17  ? 24.819  90.665  16.624  1.00 20.18  ? 26   LYS A O   1 
ATOM   126   C  CB  . LYS A 1 17  ? 23.416  90.483  19.444  1.00 24.61  ? 26   LYS A CB  1 
ATOM   127   C  CG  . LYS A 1 17  ? 22.166  90.219  20.278  1.00 29.04  ? 26   LYS A CG  1 
ATOM   128   C  CD  . LYS A 1 17  ? 22.501  89.310  21.412  1.00 40.85  ? 26   LYS A CD  1 
ATOM   129   C  CE  . LYS A 1 17  ? 21.275  88.947  22.236  1.00 53.01  ? 26   LYS A CE  1 
ATOM   130   N  NZ  . LYS A 1 17  ? 20.427  90.138  22.571  1.00 60.54  ? 26   LYS A NZ  1 
ATOM   131   N  N   . SER A 1 18  ? 24.694  92.750  17.409  1.00 16.83  ? 27   SER A N   1 
ATOM   132   C  CA  . SER A 1 18  ? 25.891  93.162  16.697  1.00 19.33  ? 27   SER A CA  1 
ATOM   133   C  C   . SER A 1 18  ? 26.721  94.073  17.611  1.00 21.53  ? 27   SER A C   1 
ATOM   134   O  O   . SER A 1 18  ? 26.214  95.091  18.114  1.00 20.66  ? 27   SER A O   1 
ATOM   135   C  CB  . SER A 1 18  ? 25.513  93.906  15.406  1.00 18.25  ? 27   SER A CB  1 
ATOM   136   O  OG  . SER A 1 18  ? 26.677  94.418  14.760  1.00 18.72  ? 27   SER A OG  1 
ATOM   137   N  N   . ASN A 1 19  ? 28.009  93.738  17.831  1.00 18.48  ? 28   ASN A N   1 
ATOM   138   C  CA  . ASN A 1 19  ? 28.787  94.629  18.665  1.00 19.72  ? 28   ASN A CA  1 
ATOM   139   C  C   . ASN A 1 19  ? 29.102  95.927  17.921  1.00 21.40  ? 28   ASN A C   1 
ATOM   140   O  O   . ASN A 1 19  ? 29.442  95.895  16.733  1.00 21.82  ? 28   ASN A O   1 
ATOM   141   C  CB  . ASN A 1 19  ? 30.146  93.969  19.085  1.00 20.42  ? 28   ASN A CB  1 
ATOM   142   C  CG  . ASN A 1 19  ? 29.944  92.732  19.896  1.00 22.73  ? 28   ASN A CG  1 
ATOM   143   O  OD1 . ASN A 1 19  ? 28.980  92.667  20.667  1.00 25.05  ? 28   ASN A OD1 1 
ATOM   144   N  ND2 . ASN A 1 19  ? 30.810  91.730  19.794  1.00 23.32  ? 28   ASN A ND2 1 
ATOM   145   N  N   . ALA A 1 20  ? 29.049  97.055  18.623  1.00 20.80  ? 29   ALA A N   1 
ATOM   146   C  CA  . ALA A 1 20  ? 29.374  98.349  18.000  1.00 20.40  ? 29   ALA A CA  1 
ATOM   147   C  C   . ALA A 1 20  ? 30.385  99.079  18.855  1.00 22.19  ? 29   ALA A C   1 
ATOM   148   O  O   . ALA A 1 20  ? 30.303  99.071  20.094  1.00 22.17  ? 29   ALA A O   1 
ATOM   149   C  CB  . ALA A 1 20  ? 28.129  99.231  17.891  1.00 18.65  ? 29   ALA A CB  1 
ATOM   150   N  N   . SER A 1 21  ? 31.306  99.726  18.201  1.00 22.52  ? 30   SER A N   1 
ATOM   151   C  CA  . SER A 1 21  ? 32.324  100.486 18.882  1.00 26.08  ? 30   SER A CA  1 
ATOM   152   C  C   . SER A 1 21  ? 32.490  101.829 18.141  1.00 25.60  ? 30   SER A C   1 
ATOM   153   O  O   . SER A 1 21  ? 32.709  101.823 16.914  1.00 27.82  ? 30   SER A O   1 
ATOM   154   C  CB  . SER A 1 21  ? 33.621  99.664  18.855  1.00 29.49  ? 30   SER A CB  1 
ATOM   155   O  OG  . SER A 1 21  ? 34.732  100.445 19.249  1.00 37.93  ? 30   SER A OG  1 
ATOM   156   N  N   . VAL A 1 22  ? 32.360  102.954 18.855  1.00 21.91  ? 31   VAL A N   1 
ATOM   157   C  CA  . VAL A 1 22  ? 32.570  104.277 18.307  1.00 21.90  ? 31   VAL A CA  1 
ATOM   158   C  C   . VAL A 1 22  ? 33.737  104.982 19.045  1.00 23.33  ? 31   VAL A C   1 
ATOM   159   O  O   . VAL A 1 22  ? 33.745  105.056 20.278  1.00 21.15  ? 31   VAL A O   1 
ATOM   160   C  CB  . VAL A 1 22  ? 31.301  105.123 18.400  1.00 21.46  ? 31   VAL A CB  1 
ATOM   161   C  CG1 . VAL A 1 22  ? 31.564  106.517 17.859  1.00 22.05  ? 31   VAL A CG1 1 
ATOM   162   C  CG2 . VAL A 1 22  ? 30.188  104.455 17.578  1.00 22.30  ? 31   VAL A CG2 1 
ATOM   163   N  N   . LYS A 1 23  ? 34.697  105.506 18.285  1.00 22.34  ? 32   LYS A N   1 
ATOM   164   C  CA  . LYS A 1 23  ? 35.849  106.161 18.896  1.00 21.55  ? 32   LYS A CA  1 
ATOM   165   C  C   . LYS A 1 23  ? 35.900  107.581 18.425  1.00 23.38  ? 32   LYS A C   1 
ATOM   166   O  O   . LYS A 1 23  ? 35.805  107.795 17.201  1.00 24.53  ? 32   LYS A O   1 
ATOM   167   C  CB  . LYS A 1 23  ? 37.129  105.408 18.451  1.00 25.34  ? 32   LYS A CB  1 
ATOM   168   C  CG  . LYS A 1 23  ? 38.390  105.883 19.219  1.00 39.38  ? 32   LYS A CG  1 
ATOM   169   C  CD  . LYS A 1 23  ? 39.540  104.848 19.023  1.00 46.29  ? 32   LYS A CD  1 
ATOM   170   C  CE  . LYS A 1 23  ? 40.109  104.368 20.333  1.00 53.42  ? 32   LYS A CE  1 
ATOM   171   N  NZ  . LYS A 1 23  ? 40.567  105.509 21.164  1.00 57.92  ? 32   LYS A NZ  1 
ATOM   172   N  N   . PHE A 1 24  ? 36.004  108.549 19.331  1.00 22.59  ? 33   PHE A N   1 
ATOM   173   C  CA  . PHE A 1 24  ? 36.099  109.962 18.946  1.00 23.51  ? 33   PHE A CA  1 
ATOM   174   C  C   . PHE A 1 24  ? 37.520  110.475 19.245  1.00 26.10  ? 33   PHE A C   1 
ATOM   175   O  O   . PHE A 1 24  ? 38.053  110.118 20.293  1.00 26.63  ? 33   PHE A O   1 
ATOM   176   C  CB  . PHE A 1 24  ? 35.184  110.896 19.782  1.00 23.65  ? 33   PHE A CB  1 
ATOM   177   C  CG  . PHE A 1 24  ? 33.731  110.799 19.397  1.00 26.87  ? 33   PHE A CG  1 
ATOM   178   C  CD1 . PHE A 1 24  ? 32.961  109.718 19.806  1.00 29.35  ? 33   PHE A CD1 1 
ATOM   179   C  CD2 . PHE A 1 24  ? 33.125  111.803 18.658  1.00 28.99  ? 33   PHE A CD2 1 
ATOM   180   C  CE1 . PHE A 1 24  ? 31.605  109.654 19.486  1.00 29.85  ? 33   PHE A CE1 1 
ATOM   181   C  CE2 . PHE A 1 24  ? 31.742  111.741 18.333  1.00 30.42  ? 33   PHE A CE2 1 
ATOM   182   C  CZ  . PHE A 1 24  ? 31.003  110.665 18.756  1.00 26.78  ? 33   PHE A CZ  1 
ATOM   183   N  N   . LYS A 1 25  ? 38.072  111.297 18.380  1.00 28.96  ? 34   LYS A N   1 
ATOM   184   C  CA  . LYS A 1 25  ? 39.384  111.894 18.651  1.00 37.19  ? 34   LYS A CA  1 
ATOM   185   C  C   . LYS A 1 25  ? 39.212  112.822 19.887  1.00 35.17  ? 34   LYS A C   1 
ATOM   186   O  O   . LYS A 1 25  ? 40.036  112.841 20.802  1.00 34.82  ? 34   LYS A O   1 
ATOM   187   C  CB  . LYS A 1 25  ? 39.843  112.724 17.442  1.00 38.52  ? 34   LYS A CB  1 
ATOM   188   C  CG  . LYS A 1 25  ? 41.123  113.533 17.803  1.00 47.45  ? 34   LYS A CG  1 
ATOM   189   C  CD  . LYS A 1 25  ? 42.352  112.873 17.255  1.00 53.76  ? 34   LYS A CD  1 
ATOM   190   C  CE  . LYS A 1 25  ? 43.567  113.696 17.613  1.00 60.43  ? 34   LYS A CE  1 
ATOM   191   N  NZ  . LYS A 1 25  ? 44.322  114.137 16.413  0.00 0.00   ? 34   LYS A NZ  1 
ATOM   192   N  N   . GLU A 1 26  ? 38.119  113.565 19.908  1.00 28.38  ? 35   GLU A N   1 
ATOM   193   C  CA  . GLU A 1 26  ? 37.825  114.481 20.984  1.00 28.83  ? 35   GLU A CA  1 
ATOM   194   C  C   . GLU A 1 26  ? 37.411  113.776 22.304  1.00 33.54  ? 35   GLU A C   1 
ATOM   195   O  O   . GLU A 1 26  ? 36.722  112.747 22.269  1.00 31.69  ? 35   GLU A O   1 
ATOM   196   C  CB  . GLU A 1 26  ? 36.698  115.401 20.534  1.00 28.14  ? 35   GLU A CB  1 
ATOM   197   C  CG  . GLU A 1 26  ? 36.416  116.517 21.538  1.00 33.05  ? 35   GLU A CG  1 
ATOM   198   C  CD  . GLU A 1 26  ? 35.211  117.394 21.142  1.00 38.25  ? 35   GLU A CD  1 
ATOM   199   O  OE1 . GLU A 1 26  ? 34.924  118.332 21.877  1.00 45.76  ? 35   GLU A OE1 1 
ATOM   200   O  OE2 . GLU A 1 26  ? 34.557  117.148 20.127  1.00 33.97  ? 35   GLU A OE2 1 
ATOM   201   N  N   . LYS A 1 27  ? 37.840  114.307 23.465  1.00 31.10  ? 36   LYS A N   1 
ATOM   202   C  CA  . LYS A 1 27  ? 37.411  113.768 24.774  1.00 34.21  ? 36   LYS A CA  1 
ATOM   203   C  C   . LYS A 1 27  ? 36.047  114.456 25.011  1.00 35.63  ? 36   LYS A C   1 
ATOM   204   O  O   . LYS A 1 27  ? 35.948  115.682 25.035  1.00 34.15  ? 36   LYS A O   1 
ATOM   205   C  CB  . LYS A 1 27  ? 38.449  114.088 25.898  1.00 37.52  ? 36   LYS A CB  1 
ATOM   206   C  CG  . LYS A 1 27  ? 38.150  113.377 27.210  0.00 0.00   ? 36   LYS A CG  1 
ATOM   207   C  CD  . LYS A 1 27  ? 39.102  113.829 28.306  0.00 0.00   ? 36   LYS A CD  1 
ATOM   208   C  CE  . LYS A 1 27  ? 38.867  113.061 29.583  0.00 0.00   ? 36   LYS A CE  1 
ATOM   209   N  NZ  . LYS A 1 27  ? 39.875  113.408 30.619  0.00 0.00   ? 36   LYS A NZ  1 
ATOM   210   N  N   . LEU A 1 28  ? 34.974  113.661 25.143  1.00 33.98  ? 37   LEU A N   1 
ATOM   211   C  CA  . LEU A 1 28  ? 33.629  114.252 25.223  1.00 32.55  ? 37   LEU A CA  1 
ATOM   212   C  C   . LEU A 1 28  ? 33.101  114.510 26.602  1.00 32.83  ? 37   LEU A C   1 
ATOM   213   O  O   . LEU A 1 28  ? 32.079  115.205 26.713  1.00 35.34  ? 37   LEU A O   1 
ATOM   214   C  CB  . LEU A 1 28  ? 32.637  113.310 24.499  1.00 29.65  ? 37   LEU A CB  1 
ATOM   215   C  CG  . LEU A 1 28  ? 33.022  112.970 23.031  1.00 26.19  ? 37   LEU A CG  1 
ATOM   216   C  CD1 . LEU A 1 28  ? 31.941  112.034 22.406  1.00 26.65  ? 37   LEU A CD1 1 
ATOM   217   C  CD2 . LEU A 1 28  ? 33.150  114.247 22.165  1.00 27.09  ? 37   LEU A CD2 1 
ATOM   218   N  N   . ASN A 1 29  ? 33.714  113.973 27.628  1.00 30.95  ? 38   ASN A N   1 
ATOM   219   C  CA  . ASN A 1 29  ? 33.176  114.175 28.976  1.00 35.68  ? 38   ASN A CA  1 
ATOM   220   C  C   . ASN A 1 29  ? 31.758  113.586 29.051  1.00 33.83  ? 38   ASN A C   1 
ATOM   221   O  O   . ASN A 1 29  ? 30.815  114.230 29.491  1.00 33.33  ? 38   ASN A O   1 
ATOM   222   C  CB  . ASN A 1 29  ? 33.159  115.669 29.349  1.00 38.76  ? 38   ASN A CB  1 
ATOM   223   C  CG  . ASN A 1 29  ? 32.808  115.882 30.820  1.00 50.41  ? 38   ASN A CG  1 
ATOM   224   O  OD1 . ASN A 1 29  ? 33.064  115.016 31.670  1.00 50.08  ? 38   ASN A OD1 1 
ATOM   225   N  ND2 . ASN A 1 29  ? 32.199  117.012 31.198  1.00 53.83  ? 38   ASN A ND2 1 
ATOM   226   N  N   . ALA A 1 30  ? 31.613  112.348 28.629  1.00 31.24  ? 39   ALA A N   1 
ATOM   227   C  CA  . ALA A 1 30  ? 30.287  111.724 28.639  1.00 28.45  ? 39   ALA A CA  1 
ATOM   228   C  C   . ALA A 1 30  ? 30.471  110.242 28.805  1.00 26.50  ? 39   ALA A C   1 
ATOM   229   O  O   . ALA A 1 30  ? 31.304  109.635 28.126  1.00 26.59  ? 39   ALA A O   1 
ATOM   230   C  CB  . ALA A 1 30  ? 29.575  112.031 27.315  1.00 24.50  ? 39   ALA A CB  1 
ATOM   231   N  N   . ASP A 1 31  ? 29.682  109.644 29.688  1.00 24.70  ? 40   ASP A N   1 
ATOM   232   C  CA  . ASP A 1 31  ? 29.776  108.229 29.939  1.00 26.52  ? 40   ASP A CA  1 
ATOM   233   C  C   . ASP A 1 31  ? 29.165  107.336 28.850  1.00 25.82  ? 40   ASP A C   1 
ATOM   234   O  O   . ASP A 1 31  ? 29.438  106.140 28.824  1.00 23.50  ? 40   ASP A O   1 
ATOM   235   C  CB  . ASP A 1 31  ? 29.054  107.879 31.237  1.00 31.31  ? 40   ASP A CB  1 
ATOM   236   C  CG  . ASP A 1 31  ? 29.731  108.462 32.463  1.00 44.88  ? 40   ASP A CG  1 
ATOM   237   O  OD1 . ASP A 1 31  ? 30.963  108.713 32.403  1.00 48.84  ? 40   ASP A OD1 1 
ATOM   238   O  OD2 . ASP A 1 31  ? 29.033  108.667 33.468  1.00 49.61  ? 40   ASP A OD2 1 
ATOM   239   N  N   . SER A 1 32  ? 28.328  107.899 27.958  1.00 23.87  ? 41   SER A N   1 
ATOM   240   C  CA  . SER A 1 32  ? 27.719  107.056 26.919  1.00 21.11  ? 41   SER A CA  1 
ATOM   241   C  C   . SER A 1 32  ? 27.263  107.913 25.774  1.00 20.58  ? 41   SER A C   1 
ATOM   242   O  O   . SER A 1 32  ? 27.187  109.147 25.922  1.00 19.11  ? 41   SER A O   1 
ATOM   243   C  CB  . SER A 1 32  ? 26.498  106.310 27.467  1.00 21.59  ? 41   SER A CB  1 
ATOM   244   O  OG  . SER A 1 32  ? 25.442  107.231 27.720  1.00 21.18  ? 41   SER A OG  1 
ATOM   245   N  N   . ILE A 1 33  ? 26.982  107.275 24.640  1.00 20.04  ? 42   ILE A N   1 
ATOM   246   C  CA  . ILE A 1 33  ? 26.394  107.924 23.451  1.00 18.77  ? 42   ILE A CA  1 
ATOM   247   C  C   . ILE A 1 33  ? 25.276  107.017 22.982  1.00 17.80  ? 42   ILE A C   1 
ATOM   248   O  O   . ILE A 1 33  ? 25.272  105.831 23.295  1.00 19.93  ? 42   ILE A O   1 
ATOM   249   C  CB  . ILE A 1 33  ? 27.372  108.131 22.294  1.00 18.19  ? 42   ILE A CB  1 
ATOM   250   C  CG1 . ILE A 1 33  ? 27.891  106.747 21.801  1.00 19.13  ? 42   ILE A CG1 1 
ATOM   251   C  CG2 . ILE A 1 33  ? 28.557  109.054 22.782  1.00 21.76  ? 42   ILE A CG2 1 
ATOM   252   C  CD1 . ILE A 1 33  ? 28.871  106.963 20.624  1.00 19.00  ? 42   ILE A CD1 1 
ATOM   253   N  N   . THR A 1 34  ? 24.327  107.565 22.218  1.00 20.08  ? 43   THR A N   1 
ATOM   254   C  CA  . THR A 1 34  ? 23.219  106.807 21.695  1.00 18.39  ? 43   THR A CA  1 
ATOM   255   C  C   . THR A 1 34  ? 23.187  106.965 20.191  1.00 17.89  ? 43   THR A C   1 
ATOM   256   O  O   . THR A 1 34  ? 23.179  108.076 19.686  1.00 19.61  ? 43   THR A O   1 
ATOM   257   C  CB  . THR A 1 34  ? 21.911  107.299 22.287  1.00 19.97  ? 43   THR A CB  1 
ATOM   258   O  OG1 . THR A 1 34  ? 21.991  107.122 23.686  1.00 21.25  ? 43   THR A OG1 1 
ATOM   259   C  CG2 . THR A 1 34  ? 20.698  106.469 21.794  1.00 19.59  ? 43   THR A CG2 1 
ATOM   260   N  N   . LEU A 1 35  ? 23.181  105.841 19.483  1.00 13.07  ? 44   LEU A N   1 
ATOM   261   C  CA  . LEU A 1 35  ? 23.125  105.859 18.010  1.00 15.02  ? 44   LEU A CA  1 
ATOM   262   C  C   . LEU A 1 35  ? 21.662  105.686 17.671  1.00 18.43  ? 44   LEU A C   1 
ATOM   263   O  O   . LEU A 1 35  ? 21.000  104.798 18.287  1.00 19.48  ? 44   LEU A O   1 
ATOM   264   C  CB  . LEU A 1 35  ? 23.902  104.670 17.489  1.00 17.50  ? 44   LEU A CB  1 
ATOM   265   C  CG  . LEU A 1 35  ? 25.424  104.992 17.246  1.00 25.57  ? 44   LEU A CG  1 
ATOM   266   C  CD1 . LEU A 1 35  ? 26.118  105.425 18.563  1.00 27.63  ? 44   LEU A CD1 1 
ATOM   267   C  CD2 . LEU A 1 35  ? 26.054  103.708 16.629  1.00 24.97  ? 44   LEU A CD2 1 
ATOM   268   N  N   . ASN A 1 36  ? 21.150  106.491 16.728  1.00 16.97  ? 45   ASN A N   1 
ATOM   269   C  CA  . ASN A 1 36  ? 19.758  106.332 16.314  1.00 15.73  ? 45   ASN A CA  1 
ATOM   270   C  C   . ASN A 1 36  ? 19.785  105.929 14.855  1.00 15.16  ? 45   ASN A C   1 
ATOM   271   O  O   . ASN A 1 36  ? 20.470  106.536 14.044  1.00 17.30  ? 45   ASN A O   1 
ATOM   272   C  CB  . ASN A 1 36  ? 18.978  107.650 16.515  1.00 19.04  ? 45   ASN A CB  1 
ATOM   273   C  CG  . ASN A 1 36  ? 17.571  107.507 16.028  1.00 30.91  ? 45   ASN A CG  1 
ATOM   274   O  OD1 . ASN A 1 36  ? 17.330  107.696 14.803  1.00 29.84  ? 45   ASN A OD1 1 
ATOM   275   N  ND2 . ASN A 1 36  ? 16.593  107.057 16.874  1.00 29.30  ? 45   ASN A ND2 1 
ATOM   276   N  N   . PHE A 1 37  ? 19.036  104.853 14.523  1.00 14.61  ? 46   PHE A N   1 
ATOM   277   C  CA  . PHE A 1 37  ? 18.920  104.414 13.120  1.00 14.72  ? 46   PHE A CA  1 
ATOM   278   C  C   . PHE A 1 37  ? 17.450  104.450 12.744  1.00 16.86  ? 46   PHE A C   1 
ATOM   279   O  O   . PHE A 1 37  ? 16.598  104.412 13.641  1.00 17.18  ? 46   PHE A O   1 
ATOM   280   C  CB  . PHE A 1 37  ? 19.324  102.913 13.014  1.00 15.77  ? 46   PHE A CB  1 
ATOM   281   C  CG  . PHE A 1 37  ? 20.719  102.614 13.546  1.00 17.74  ? 46   PHE A CG  1 
ATOM   282   C  CD1 . PHE A 1 37  ? 20.914  102.268 14.872  1.00 21.94  ? 46   PHE A CD1 1 
ATOM   283   C  CD2 . PHE A 1 37  ? 21.811  102.673 12.726  1.00 18.63  ? 46   PHE A CD2 1 
ATOM   284   C  CE1 . PHE A 1 37  ? 22.195  101.971 15.360  1.00 21.28  ? 46   PHE A CE1 1 
ATOM   285   C  CE2 . PHE A 1 37  ? 23.109  102.378 13.214  1.00 16.66  ? 46   PHE A CE2 1 
ATOM   286   C  CZ  . PHE A 1 37  ? 23.269  102.032 14.522  1.00 16.56  ? 46   PHE A CZ  1 
ATOM   287   N  N   . MET A 1 38  ? 17.138  104.447 11.427  1.00 16.65  ? 47   MET A N   1 
ATOM   288   C  CA  . MET A 1 38  ? 15.736  104.338 11.031  1.00 17.50  ? 47   MET A CA  1 
ATOM   289   C  C   . MET A 1 38  ? 15.656  103.422 9.857   1.00 17.38  ? 47   MET A C   1 
ATOM   290   O  O   . MET A 1 38  ? 16.573  103.400 9.019   1.00 17.81  ? 47   MET A O   1 
ATOM   291   C  CB  . MET A 1 38  ? 15.128  105.685 10.504  1.00 17.71  ? 47   MET A CB  1 
ATOM   292   C  CG  A MET A 1 38  ? 15.025  106.762 11.591  0.68 24.17  ? 47   MET A CG  1 
ATOM   293   C  CG  B MET A 1 38  ? 15.128  106.662 11.804  0.32 27.13  ? 47   MET A CG  1 
ATOM   294   S  SD  A MET A 1 38  ? 13.614  106.535 12.745  0.68 22.27  ? 47   MET A SD  1 
ATOM   295   S  SD  B MET A 1 38  ? 14.063  108.046 11.329  0.32 25.16  ? 47   MET A SD  1 
ATOM   296   C  CE  A MET A 1 38  ? 12.192  106.989 11.659  0.68 21.13  ? 47   MET A CE  1 
ATOM   297   C  CE  B MET A 1 38  ? 12.509  107.270 11.237  0.32 22.88  ? 47   MET A CE  1 
ATOM   298   N  N   . CYS A 1 39  ? 14.569  102.654 9.788   1.00 17.01  ? 48   CYS A N   1 
ATOM   299   C  CA  . CYS A 1 39  ? 14.309  101.878 8.588   1.00 17.72  ? 48   CYS A CA  1 
ATOM   300   C  C   . CYS A 1 39  ? 12.849  102.382 8.198   1.00 19.39  ? 48   CYS A C   1 
ATOM   301   O  O   . CYS A 1 39  ? 11.899  102.046 8.902   1.00 17.32  ? 48   CYS A O   1 
ATOM   302   C  CB  . CYS A 1 39  ? 14.336  100.376 8.874   1.00 18.61  ? 48   CYS A CB  1 
ATOM   303   S  SG  . CYS A 1 39  ? 13.871  99.394  7.397   1.00 20.06  ? 48   CYS A SG  1 
ATOM   304   N  N   . TYR A 1 40  ? 12.737  103.184 7.114   1.00 19.06  ? 49   TYR A N   1 
ATOM   305   C  CA  . TYR A 1 40  ? 11.470  103.849 6.699   1.00 19.67  ? 49   TYR A CA  1 
ATOM   306   C  C   . TYR A 1 40  ? 11.032  104.680 7.906   1.00 21.82  ? 49   TYR A C   1 
ATOM   307   O  O   . TYR A 1 40  ? 11.817  105.545 8.311   1.00 21.98  ? 49   TYR A O   1 
ATOM   308   C  CB  . TYR A 1 40  ? 10.437  102.777 6.281   1.00 18.60  ? 49   TYR A CB  1 
ATOM   309   C  CG  . TYR A 1 40  ? 9.270   103.406 5.577   1.00 22.01  ? 49   TYR A CG  1 
ATOM   310   C  CD1 . TYR A 1 40  ? 9.462   104.257 4.495   1.00 27.40  ? 49   TYR A CD1 1 
ATOM   311   C  CD2 . TYR A 1 40  ? 7.963   103.171 6.005   1.00 27.35  ? 49   TYR A CD2 1 
ATOM   312   C  CE1 . TYR A 1 40  ? 8.379   104.860 3.851   1.00 28.50  ? 49   TYR A CE1 1 
ATOM   313   C  CE2 . TYR A 1 40  ? 6.880   103.772 5.371   1.00 26.21  ? 49   TYR A CE2 1 
ATOM   314   C  CZ  . TYR A 1 40  ? 7.094   104.607 4.290   1.00 32.73  ? 49   TYR A CZ  1 
ATOM   315   O  OH  . TYR A 1 40  ? 6.000   105.145 3.621   1.00 37.21  ? 49   TYR A OH  1 
ATOM   316   N  N   . ASP A 1 41  ? 9.881   104.429 8.522   1.00 19.23  ? 50   ASP A N   1 
ATOM   317   C  CA  . ASP A 1 41  ? 9.489   105.255 9.670   1.00 20.97  ? 50   ASP A CA  1 
ATOM   318   C  C   . ASP A 1 41  ? 9.705   104.599 11.017  1.00 23.82  ? 50   ASP A C   1 
ATOM   319   O  O   . ASP A 1 41  ? 9.196   105.068 12.034  1.00 23.07  ? 50   ASP A O   1 
ATOM   320   C  CB  . ASP A 1 41  ? 8.009   105.649 9.505   1.00 23.67  ? 50   ASP A CB  1 
ATOM   321   C  CG  . ASP A 1 41  ? 7.063   104.491 9.534   1.00 31.26  ? 50   ASP A CG  1 
ATOM   322   O  OD1 . ASP A 1 41  ? 7.528   103.325 9.427   1.00 28.92  ? 50   ASP A OD1 1 
ATOM   323   O  OD2 . ASP A 1 41  ? 5.826   104.737 9.679   1.00 36.63  ? 50   ASP A OD2 1 
ATOM   324   N  N   . MET A 1 42  ? 10.497  103.494 11.083  1.00 21.34  ? 51   MET A N   1 
ATOM   325   C  CA  . MET A 1 42  ? 10.666  102.820 12.374  1.00 15.93  ? 51   MET A CA  1 
ATOM   326   C  C   . MET A 1 42  ? 12.083  103.079 12.951  1.00 19.15  ? 51   MET A C   1 
ATOM   327   O  O   . MET A 1 42  ? 13.060  102.894 12.265  1.00 17.86  ? 51   MET A O   1 
ATOM   328   C  CB  . MET A 1 42  ? 10.496  101.282 12.170  1.00 19.01  ? 51   MET A CB  1 
ATOM   329   C  CG  . MET A 1 42  ? 10.728  100.496 13.454  1.00 23.05  ? 51   MET A CG  1 
ATOM   330   S  SD  . MET A 1 42  ? 10.335  98.754  13.114  1.00 26.62  ? 51   MET A SD  1 
ATOM   331   C  CE  . MET A 1 42  ? 8.508   98.761  13.243  1.00 30.67  ? 51   MET A CE  1 
ATOM   332   N  N   . PRO A 1 43  ? 12.175  103.495 14.200  1.00 20.52  ? 52   PRO A N   1 
ATOM   333   C  CA  . PRO A 1 43  ? 13.476  103.776 14.846  1.00 20.85  ? 52   PRO A CA  1 
ATOM   334   C  C   . PRO A 1 43  ? 14.049  102.571 15.559  1.00 21.91  ? 52   PRO A C   1 
ATOM   335   O  O   . PRO A 1 43  ? 13.325  101.667 16.001  1.00 19.64  ? 52   PRO A O   1 
ATOM   336   C  CB  . PRO A 1 43  ? 13.123  104.885 15.848  1.00 21.53  ? 52   PRO A CB  1 
ATOM   337   C  CG  . PRO A 1 43  ? 11.674  104.497 16.303  1.00 23.88  ? 52   PRO A CG  1 
ATOM   338   C  CD  . PRO A 1 43  ? 11.009  103.908 15.046  1.00 21.39  ? 52   PRO A CD  1 
ATOM   339   N  N   . LEU A 1 44  ? 15.363  102.562 15.687  1.00 17.24  ? 53   LEU A N   1 
ATOM   340   C  CA  . LEU A 1 44  ? 16.094  101.504 16.407  1.00 18.19  ? 53   LEU A CA  1 
ATOM   341   C  C   . LEU A 1 44  ? 17.240  102.257 17.100  1.00 18.70  ? 53   LEU A C   1 
ATOM   342   O  O   . LEU A 1 44  ? 17.889  103.077 16.446  1.00 17.85  ? 53   LEU A O   1 
ATOM   343   C  CB  . LEU A 1 44  ? 16.722  100.534 15.419  1.00 18.25  ? 53   LEU A CB  1 
ATOM   344   C  CG  . LEU A 1 44  ? 17.580  99.403  16.120  1.00 21.35  ? 53   LEU A CG  1 
ATOM   345   C  CD1 . LEU A 1 44  ? 16.670  98.444  16.783  1.00 25.57  ? 53   LEU A CD1 1 
ATOM   346   C  CD2 . LEU A 1 44  ? 18.306  98.615  15.058  1.00 23.34  ? 53   LEU A CD2 1 
ATOM   347   N  N   . GLU A 1 45  ? 17.483  102.051 18.357  1.00 16.95  ? 54   GLU A N   1 
ATOM   348   C  CA  . GLU A 1 45  ? 18.595  102.772 18.966  1.00 19.75  ? 54   GLU A CA  1 
ATOM   349   C  C   . GLU A 1 45  ? 19.476  101.819 19.776  1.00 20.92  ? 54   GLU A C   1 
ATOM   350   O  O   . GLU A 1 45  ? 19.081  100.692 20.088  1.00 17.90  ? 54   GLU A O   1 
ATOM   351   C  CB  A GLU A 1 45  ? 18.109  103.930 19.837  0.53 22.83  ? 54   GLU A CB  1 
ATOM   352   C  CB  B GLU A 1 45  ? 17.962  103.758 20.004  0.47 25.49  ? 54   GLU A CB  1 
ATOM   353   C  CG  A GLU A 1 45  ? 17.410  103.536 21.118  0.53 24.64  ? 54   GLU A CG  1 
ATOM   354   C  CG  B GLU A 1 45  ? 17.360  104.904 19.225  0.47 25.52  ? 54   GLU A CG  1 
ATOM   355   C  CD  A GLU A 1 45  ? 17.192  104.748 22.004  0.53 26.51  ? 54   GLU A CD  1 
ATOM   356   C  CD  B GLU A 1 45  ? 17.261  106.189 20.025  0.47 21.42  ? 54   GLU A CD  1 
ATOM   357   O  OE1 A GLU A 1 45  ? 17.569  104.713 23.198  0.53 18.62  ? 54   GLU A OE1 1 
ATOM   358   O  OE1 B GLU A 1 45  ? 17.522  107.238 19.447  0.47 17.07  ? 54   GLU A OE1 1 
ATOM   359   O  OE2 A GLU A 1 45  ? 16.640  105.741 21.490  0.53 26.19  ? 54   GLU A OE2 1 
ATOM   360   O  OE2 B GLU A 1 45  ? 16.919  106.129 21.227  0.47 26.88  ? 54   GLU A OE2 1 
ATOM   361   N  N   . ALA A 1 46  ? 20.715  102.270 20.047  1.00 18.45  ? 55   ALA A N   1 
ATOM   362   C  CA  . ALA A 1 46  ? 21.651  101.475 20.855  1.00 20.20  ? 55   ALA A CA  1 
ATOM   363   C  C   . ALA A 1 46  ? 22.463  102.440 21.687  1.00 19.86  ? 55   ALA A C   1 
ATOM   364   O  O   . ALA A 1 46  ? 22.912  103.489 21.169  1.00 19.50  ? 55   ALA A O   1 
ATOM   365   C  CB  . ALA A 1 46  ? 22.580  100.675 19.969  1.00 18.45  ? 55   ALA A CB  1 
ATOM   366   N  N   . THR A 1 47  ? 22.661  102.124 22.974  1.00 20.70  ? 56   THR A N   1 
ATOM   367   C  CA  . THR A 1 47  ? 23.465  103.009 23.826  1.00 22.30  ? 56   THR A CA  1 
ATOM   368   C  C   . THR A 1 47  ? 24.822  102.354 24.026  1.00 22.49  ? 56   THR A C   1 
ATOM   369   O  O   . THR A 1 47  ? 24.883  101.179 24.358  1.00 23.75  ? 56   THR A O   1 
ATOM   370   C  CB  . THR A 1 47  ? 22.713  103.281 25.136  1.00 27.96  ? 56   THR A CB  1 
ATOM   371   O  OG1 . THR A 1 47  ? 21.647  104.148 24.753  1.00 30.01  ? 56   THR A OG1 1 
ATOM   372   C  CG2 . THR A 1 47  ? 23.572  104.032 26.184  1.00 29.83  ? 56   THR A CG2 1 
ATOM   373   N  N   . LEU A 1 48  ? 25.912  103.110 23.780  1.00 19.37  ? 57   LEU A N   1 
ATOM   374   C  CA  . LEU A 1 48  ? 27.277  102.571 23.890  1.00 18.24  ? 57   LEU A CA  1 
ATOM   375   C  C   . LEU A 1 48  ? 27.945  103.269 25.056  1.00 20.69  ? 57   LEU A C   1 
ATOM   376   O  O   . LEU A 1 48  ? 27.915  104.504 25.128  1.00 21.39  ? 57   LEU A O   1 
ATOM   377   C  CB  . LEU A 1 48  ? 28.022  102.859 22.548  1.00 19.69  ? 57   LEU A CB  1 
ATOM   378   C  CG  . LEU A 1 48  ? 27.233  102.458 21.279  1.00 21.80  ? 57   LEU A CG  1 
ATOM   379   C  CD1 . LEU A 1 48  ? 28.163  102.661 20.133  1.00 18.10  ? 57   LEU A CD1 1 
ATOM   380   C  CD2 . LEU A 1 48  ? 26.743  100.962 21.346  1.00 24.14  ? 57   LEU A CD2 1 
ATOM   381   N  N   . ASN A 1 49  ? 28.540  102.502 25.972  1.00 21.35  ? 58   ASN A N   1 
ATOM   382   C  CA  . ASN A 1 49  ? 29.176  103.064 27.172  1.00 21.90  ? 58   ASN A CA  1 
ATOM   383   C  C   . ASN A 1 49  ? 30.668  103.214 27.030  1.00 22.22  ? 58   ASN A C   1 
ATOM   384   O  O   . ASN A 1 49  ? 31.316  102.342 26.482  1.00 23.10  ? 58   ASN A O   1 
ATOM   385   C  CB  . ASN A 1 49  ? 28.904  102.123 28.305  1.00 21.50  ? 58   ASN A CB  1 
ATOM   386   C  CG  . ASN A 1 49  ? 27.421  102.121 28.594  1.00 29.20  ? 58   ASN A CG  1 
ATOM   387   O  OD1 . ASN A 1 49  ? 26.768  101.107 28.383  1.00 35.69  ? 58   ASN A OD1 1 
ATOM   388   N  ND2 . ASN A 1 49  ? 26.833  103.214 29.050  1.00 27.83  ? 58   ASN A ND2 1 
ATOM   389   N  N   . TYR A 1 50  ? 31.204  104.310 27.564  1.00 24.40  ? 59   TYR A N   1 
ATOM   390   C  CA  . TYR A 1 50  ? 32.616  104.597 27.482  1.00 23.34  ? 59   TYR A CA  1 
ATOM   391   C  C   . TYR A 1 50  ? 33.473  103.543 28.203  1.00 24.93  ? 59   TYR A C   1 
ATOM   392   O  O   . TYR A 1 50  ? 33.202  103.199 29.358  1.00 27.23  ? 59   TYR A O   1 
ATOM   393   C  CB  . TYR A 1 50  ? 32.865  105.973 28.073  1.00 25.26  ? 59   TYR A CB  1 
ATOM   394   C  CG  . TYR A 1 50  ? 34.274  106.447 27.788  1.00 28.89  ? 59   TYR A CG  1 
ATOM   395   C  CD1 . TYR A 1 50  ? 34.679  106.756 26.495  1.00 29.04  ? 59   TYR A CD1 1 
ATOM   396   C  CD2 . TYR A 1 50  ? 35.203  106.588 28.820  1.00 34.77  ? 59   TYR A CD2 1 
ATOM   397   C  CE1 . TYR A 1 50  ? 35.978  107.201 26.232  1.00 36.24  ? 59   TYR A CE1 1 
ATOM   398   C  CE2 . TYR A 1 50  ? 36.496  107.044 28.571  1.00 37.07  ? 59   TYR A CE2 1 
ATOM   399   C  CZ  . TYR A 1 50  ? 36.880  107.347 27.286  1.00 42.22  ? 59   TYR A CZ  1 
ATOM   400   O  OH  . TYR A 1 50  ? 38.164  107.770 27.088  1.00 44.33  ? 59   TYR A OH  1 
ATOM   401   N  N   . ASN A 1 51  ? 34.500  103.072 27.532  1.00 26.72  ? 60   ASN A N   1 
ATOM   402   C  CA  . ASN A 1 51  ? 35.398  102.073 28.112  1.00 28.94  ? 60   ASN A CA  1 
ATOM   403   C  C   . ASN A 1 51  ? 36.773  102.761 28.156  1.00 32.31  ? 60   ASN A C   1 
ATOM   404   O  O   . ASN A 1 51  ? 37.375  102.977 27.114  1.00 34.32  ? 60   ASN A O   1 
ATOM   405   C  CB  . ASN A 1 51  ? 35.382  100.799 27.281  1.00 29.27  ? 60   ASN A CB  1 
ATOM   406   C  CG  . ASN A 1 51  ? 36.423  99.752  27.746  1.00 41.03  ? 60   ASN A CG  1 
ATOM   407   O  OD1 . ASN A 1 51  ? 37.251  100.030 28.617  1.00 41.80  ? 60   ASN A OD1 1 
ATOM   408   N  ND2 . ASN A 1 51  ? 36.497  98.576  27.155  1.00 40.62  ? 60   ASN A ND2 1 
ATOM   409   N  N   . GLU A 1 52  ? 37.244  103.134 29.369  1.00 38.74  ? 61   GLU A N   1 
ATOM   410   C  CA  . GLU A 1 52  ? 38.551  103.805 29.507  1.00 47.27  ? 61   GLU A CA  1 
ATOM   411   C  C   . GLU A 1 52  ? 39.674  102.922 29.069  1.00 49.05  ? 61   GLU A C   1 
ATOM   412   O  O   . GLU A 1 52  ? 40.652  103.439 28.550  1.00 52.51  ? 61   GLU A O   1 
ATOM   413   C  CB  . GLU A 1 52  ? 38.769  104.302 30.934  1.00 54.10  ? 61   GLU A CB  1 
ATOM   414   C  CG  . GLU A 1 52  ? 37.892  105.522 31.127  1.00 67.10  ? 61   GLU A CG  1 
ATOM   415   C  CD  . GLU A 1 52  ? 38.531  106.614 31.939  1.00 73.44  ? 61   GLU A CD  1 
ATOM   416   O  OE1 . GLU A 1 52  ? 38.708  106.407 33.168  1.00 79.36  ? 61   GLU A OE1 1 
ATOM   417   O  OE2 . GLU A 1 52  ? 38.840  107.684 31.358  1.00 78.16  ? 61   GLU A OE2 1 
ATOM   418   N  N   . LYS A 1 53  ? 39.560  101.625 29.203  1.00 49.54  ? 62   LYS A N   1 
ATOM   419   C  CA  . LYS A 1 53  ? 40.659  100.796 28.724  1.00 54.54  ? 62   LYS A CA  1 
ATOM   420   C  C   . LYS A 1 53  ? 40.918  101.108 27.255  1.00 55.23  ? 62   LYS A C   1 
ATOM   421   O  O   . LYS A 1 53  ? 42.054  101.306 26.861  1.00 53.46  ? 62   LYS A O   1 
ATOM   422   C  CB  . LYS A 1 53  ? 40.296  99.302  28.864  1.00 58.92  ? 62   LYS A CB  1 
ATOM   423   C  CG  . LYS A 1 53  ? 41.370  98.341  28.357  1.00 66.55  ? 62   LYS A CG  1 
ATOM   424   C  CD  . LYS A 1 53  ? 40.970  96.846  28.597  1.00 73.94  ? 62   LYS A CD  1 
ATOM   425   C  CE  . LYS A 1 53  ? 42.048  96.074  29.369  1.00 77.94  ? 62   LYS A CE  1 
ATOM   426   N  NZ  . LYS A 1 53  ? 42.042  94.611  29.040  1.00 79.69  ? 62   LYS A NZ  1 
ATOM   427   N  N   . THR A 1 54  ? 39.854  101.174 26.430  1.00 49.71  ? 63   THR A N   1 
ATOM   428   C  CA  . THR A 1 54  ? 40.048  101.388 25.008  1.00 41.13  ? 63   THR A CA  1 
ATOM   429   C  C   . THR A 1 54  ? 39.781  102.824 24.547  1.00 37.16  ? 63   THR A C   1 
ATOM   430   O  O   . THR A 1 54  ? 39.955  103.079 23.362  1.00 36.64  ? 63   THR A O   1 
ATOM   431   C  CB  . THR A 1 54  ? 39.120  100.426 24.225  1.00 40.93  ? 63   THR A CB  1 
ATOM   432   O  OG1 . THR A 1 54  ? 37.758  100.765 24.580  1.00 38.48  ? 63   THR A OG1 1 
ATOM   433   C  CG2 . THR A 1 54  ? 39.356  98.944  24.576  1.00 38.87  ? 63   THR A CG2 1 
ATOM   434   N  N   . ASP A 1 55  ? 39.353  103.743 25.433  1.00 34.09  ? 64   ASP A N   1 
ATOM   435   C  CA  . ASP A 1 55  ? 39.043  105.116 24.999  1.00 34.87  ? 64   ASP A CA  1 
ATOM   436   C  C   . ASP A 1 55  ? 37.962  105.070 23.831  1.00 32.62  ? 64   ASP A C   1 
ATOM   437   O  O   . ASP A 1 55  ? 38.054  105.795 22.846  1.00 29.43  ? 64   ASP A O   1 
ATOM   438   C  CB  . ASP A 1 55  ? 40.337  105.800 24.484  1.00 38.46  ? 64   ASP A CB  1 
ATOM   439   C  CG  . ASP A 1 55  ? 40.079  107.221 24.037  1.00 46.87  ? 64   ASP A CG  1 
ATOM   440   O  OD1 . ASP A 1 55  ? 40.627  107.617 22.986  1.00 52.58  ? 64   ASP A OD1 1 
ATOM   441   O  OD2 . ASP A 1 55  ? 39.303  107.930 24.715  1.00 51.19  ? 64   ASP A OD2 1 
ATOM   442   N  N   . SER A 1 56  ? 36.985  104.199 23.969  1.00 28.83  ? 65   SER A N   1 
ATOM   443   C  CA  . SER A 1 56  ? 35.942  103.971 22.923  1.00 29.82  ? 65   SER A CA  1 
ATOM   444   C  C   . SER A 1 56  ? 34.561  103.801 23.584  1.00 29.15  ? 65   SER A C   1 
ATOM   445   O  O   . SER A 1 56  ? 34.500  103.440 24.742  1.00 25.06  ? 65   SER A O   1 
ATOM   446   C  CB  . SER A 1 56  ? 36.222  102.648 22.217  1.00 32.50  ? 65   SER A CB  1 
ATOM   447   O  OG  . SER A 1 56  ? 36.894  102.929 21.010  1.00 46.28  ? 65   SER A OG  1 
ATOM   448   N  N   . TYR A 1 57  ? 33.485  104.046 22.838  1.00 24.53  ? 66   TYR A N   1 
ATOM   449   C  CA  . TYR A 1 57  ? 32.139  103.820 23.372  1.00 21.25  ? 66   TYR A CA  1 
ATOM   450   C  C   . TYR A 1 57  ? 31.771  102.422 22.794  1.00 20.97  ? 66   TYR A C   1 
ATOM   451   O  O   . TYR A 1 57  ? 31.825  102.227 21.562  1.00 22.29  ? 66   TYR A O   1 
ATOM   452   C  CB  . TYR A 1 57  ? 31.219  104.953 22.887  1.00 18.63  ? 66   TYR A CB  1 
ATOM   453   C  CG  . TYR A 1 57  ? 31.547  106.252 23.609  1.00 20.22  ? 66   TYR A CG  1 
ATOM   454   C  CD1 . TYR A 1 57  ? 32.529  107.120 23.122  1.00 24.44  ? 66   TYR A CD1 1 
ATOM   455   C  CD2 . TYR A 1 57  ? 30.894  106.597 24.780  1.00 18.97  ? 66   TYR A CD2 1 
ATOM   456   C  CE1 . TYR A 1 57  ? 32.843  108.298 23.795  1.00 20.35  ? 66   TYR A CE1 1 
ATOM   457   C  CE2 . TYR A 1 57  ? 31.200  107.765 25.459  1.00 20.09  ? 66   TYR A CE2 1 
ATOM   458   C  CZ  . TYR A 1 57  ? 32.175  108.606 24.968  1.00 25.75  ? 66   TYR A CZ  1 
ATOM   459   O  OH  . TYR A 1 57  ? 32.494  109.729 25.697  1.00 25.77  ? 66   TYR A OH  1 
ATOM   460   N  N   . GLU A 1 58  ? 31.403  101.479 23.655  1.00 20.76  ? 67   GLU A N   1 
ATOM   461   C  CA  . GLU A 1 58  ? 31.161  100.116 23.210  1.00 21.01  ? 67   GLU A CA  1 
ATOM   462   C  C   . GLU A 1 58  ? 29.816  99.615  23.679  1.00 21.80  ? 67   GLU A C   1 
ATOM   463   O  O   . GLU A 1 58  ? 29.381  99.951  24.792  1.00 21.52  ? 67   GLU A O   1 
ATOM   464   C  CB  . GLU A 1 58  ? 32.233  99.166  23.848  1.00 23.92  ? 67   GLU A CB  1 
ATOM   465   C  CG  . GLU A 1 58  ? 33.672  99.506  23.408  1.00 30.42  ? 67   GLU A CG  1 
ATOM   466   C  CD  . GLU A 1 58  ? 34.723  98.688  24.187  1.00 45.29  ? 67   GLU A CD  1 
ATOM   467   O  OE1 . GLU A 1 58  ? 35.925  98.829  23.886  1.00 53.03  ? 67   GLU A OE1 1 
ATOM   468   O  OE2 . GLU A 1 58  ? 34.347  97.928  25.105  1.00 51.10  ? 67   GLU A OE2 1 
ATOM   469   N  N   . GLY A 1 59  ? 29.159  98.807  22.871  1.00 20.33  ? 68   GLY A N   1 
ATOM   470   C  CA  . GLY A 1 59  ? 27.888  98.258  23.308  1.00 18.71  ? 68   GLY A CA  1 
ATOM   471   C  C   . GLY A 1 59  ? 27.419  97.323  22.234  1.00 23.64  ? 68   GLY A C   1 
ATOM   472   O  O   . GLY A 1 59  ? 28.163  96.939  21.302  1.00 21.96  ? 68   GLY A O   1 
ATOM   473   N  N   . VAL A 1 60  ? 26.124  96.961  22.334  1.00 19.97  ? 69   VAL A N   1 
ATOM   474   C  CA  . VAL A 1 60  ? 25.569  96.003  21.402  1.00 19.43  ? 69   VAL A CA  1 
ATOM   475   C  C   . VAL A 1 60  ? 24.300  96.530  20.724  1.00 20.92  ? 69   VAL A C   1 
ATOM   476   O  O   . VAL A 1 60  ? 23.482  97.093  21.436  1.00 21.90  ? 69   VAL A O   1 
ATOM   477   C  CB  . VAL A 1 60  ? 25.215  94.751  22.250  1.00 21.72  ? 69   VAL A CB  1 
ATOM   478   C  CG1 . VAL A 1 60  ? 24.471  93.711  21.359  1.00 21.84  ? 69   VAL A CG1 1 
ATOM   479   C  CG2 . VAL A 1 60  ? 26.520  94.129  22.885  1.00 23.08  ? 69   VAL A CG2 1 
ATOM   480   N  N   . ILE A 1 61  ? 24.140  96.408  19.408  1.00 17.57  ? 70   ILE A N   1 
ATOM   481   C  CA  . ILE A 1 61  ? 22.880  96.809  18.784  1.00 16.54  ? 70   ILE A CA  1 
ATOM   482   C  C   . ILE A 1 61  ? 22.019  95.514  18.799  1.00 20.13  ? 70   ILE A C   1 
ATOM   483   O  O   . ILE A 1 61  ? 22.498  94.456  18.393  1.00 20.63  ? 70   ILE A O   1 
ATOM   484   C  CB  . ILE A 1 61  ? 23.104  97.298  17.311  1.00 16.99  ? 70   ILE A CB  1 
ATOM   485   C  CG1 . ILE A 1 61  ? 24.043  98.560  17.314  1.00 17.35  ? 70   ILE A CG1 1 
ATOM   486   C  CG2 . ILE A 1 61  ? 21.715  97.616  16.655  1.00 16.51  ? 70   ILE A CG2 1 
ATOM   487   C  CD1 . ILE A 1 61  ? 24.678  98.772  15.890  1.00 17.82  ? 70   ILE A CD1 1 
ATOM   488   N  N   . ASN A 1 62  ? 20.764  95.594  19.289  1.00 17.38  ? 71   ASN A N   1 
ATOM   489   C  CA  . ASN A 1 62  ? 19.872  94.426  19.320  1.00 18.33  ? 71   ASN A CA  1 
ATOM   490   C  C   . ASN A 1 62  ? 18.814  94.664  18.229  1.00 17.60  ? 71   ASN A C   1 
ATOM   491   O  O   . ASN A 1 62  ? 18.009  95.572  18.401  1.00 18.65  ? 71   ASN A O   1 
ATOM   492   C  CB  . ASN A 1 62  ? 19.177  94.373  20.710  1.00 21.82  ? 71   ASN A CB  1 
ATOM   493   C  CG  . ASN A 1 62  ? 20.223  93.965  21.753  1.00 33.03  ? 71   ASN A CG  1 
ATOM   494   O  OD1 . ASN A 1 62  ? 20.570  92.772  21.818  1.00 37.26  ? 71   ASN A OD1 1 
ATOM   495   N  ND2 . ASN A 1 62  ? 20.779  94.857  22.565  1.00 35.37  ? 71   ASN A ND2 1 
ATOM   496   N  N   . TYR A 1 63  ? 18.833  93.909  17.159  1.00 16.81  ? 72   TYR A N   1 
ATOM   497   C  CA  . TYR A 1 63  ? 17.923  94.103  16.052  1.00 14.95  ? 72   TYR A CA  1 
ATOM   498   C  C   . TYR A 1 63  ? 16.572  93.399  16.395  1.00 18.07  ? 72   TYR A C   1 
ATOM   499   O  O   . TYR A 1 63  ? 16.195  92.425  15.749  1.00 19.78  ? 72   TYR A O   1 
ATOM   500   C  CB  . TYR A 1 63  ? 18.564  93.499  14.776  1.00 15.14  ? 72   TYR A CB  1 
ATOM   501   C  CG  . TYR A 1 63  ? 19.712  94.386  14.328  1.00 18.27  ? 72   TYR A CG  1 
ATOM   502   C  CD1 . TYR A 1 63  ? 21.028  94.099  14.691  1.00 19.03  ? 72   TYR A CD1 1 
ATOM   503   C  CD2 . TYR A 1 63  ? 19.478  95.541  13.576  1.00 18.73  ? 72   TYR A CD2 1 
ATOM   504   C  CE1 . TYR A 1 63  ? 22.080  94.931  14.301  1.00 16.87  ? 72   TYR A CE1 1 
ATOM   505   C  CE2 . TYR A 1 63  ? 20.516  96.392  13.211  1.00 16.39  ? 72   TYR A CE2 1 
ATOM   506   C  CZ  . TYR A 1 63  ? 21.815  96.078  13.571  1.00 16.24  ? 72   TYR A CZ  1 
ATOM   507   O  OH  . TYR A 1 63  ? 22.819  96.942  13.279  1.00 15.11  ? 72   TYR A OH  1 
ATOM   508   N  N   A ASN A 1 64  ? 15.873  93.904  17.381  0.48 18.01  ? 73   ASN A N   1 
ATOM   509   N  N   B ASN A 1 64  ? 15.957  94.107  17.347  0.52 14.43  ? 73   ASN A N   1 
ATOM   510   C  CA  A ASN A 1 64  ? 14.640  93.244  17.758  0.48 17.64  ? 73   ASN A CA  1 
ATOM   511   C  CA  B ASN A 1 64  ? 14.719  93.518  17.825  0.52 18.50  ? 73   ASN A CA  1 
ATOM   512   C  C   A ASN A 1 64  ? 13.398  93.980  17.230  0.48 19.06  ? 73   ASN A C   1 
ATOM   513   C  C   B ASN A 1 64  ? 13.489  94.268  17.326  0.52 19.41  ? 73   ASN A C   1 
ATOM   514   O  O   A ASN A 1 64  ? 12.309  93.726  17.758  0.48 18.84  ? 73   ASN A O   1 
ATOM   515   O  O   B ASN A 1 64  ? 12.465  94.220  18.001  0.52 20.34  ? 73   ASN A O   1 
ATOM   516   C  CB  A ASN A 1 64  ? 14.579  93.134  19.304  0.48 18.55  ? 73   ASN A CB  1 
ATOM   517   C  CB  B ASN A 1 64  ? 14.702  93.541  19.362  0.52 19.59  ? 73   ASN A CB  1 
ATOM   518   C  CG  A ASN A 1 64  ? 14.801  94.462  20.015  0.48 22.80  ? 73   ASN A CG  1 
ATOM   519   C  CG  B ASN A 1 64  ? 15.657  92.607  20.047  0.52 24.10  ? 73   ASN A CG  1 
ATOM   520   O  OD1 A ASN A 1 64  ? 14.891  94.503  21.268  0.48 27.27  ? 73   ASN A OD1 1 
ATOM   521   O  OD1 B ASN A 1 64  ? 15.916  92.794  21.255  0.52 27.04  ? 73   ASN A OD1 1 
ATOM   522   N  ND2 A ASN A 1 64  ? 14.873  95.598  19.327  0.48 19.78  ? 73   ASN A ND2 1 
ATOM   523   N  ND2 B ASN A 1 64  ? 16.229  91.587  19.376  0.52 22.46  ? 73   ASN A ND2 1 
ATOM   524   N  N   . LYS A 1 65  ? 13.549  94.889  16.221  1.00 18.59  ? 74   LYS A N   1 
ATOM   525   C  CA  . LYS A 1 65  ? 12.383  95.581  15.638  1.00 19.21  ? 74   LYS A CA  1 
ATOM   526   C  C   . LYS A 1 65  ? 12.137  95.015  14.246  1.00 21.52  ? 74   LYS A C   1 
ATOM   527   O  O   . LYS A 1 65  ? 13.082  94.785  13.495  1.00 19.58  ? 74   LYS A O   1 
ATOM   528   C  CB  . LYS A 1 65  ? 12.645  97.110  15.527  1.00 22.98  ? 74   LYS A CB  1 
ATOM   529   C  CG  . LYS A 1 65  ? 12.912  97.837  16.873  1.00 33.33  ? 74   LYS A CG  1 
ATOM   530   C  CD  . LYS A 1 65  ? 11.714  97.919  17.771  1.00 43.15  ? 74   LYS A CD  1 
ATOM   531   C  CE  . LYS A 1 65  ? 10.647  98.872  17.255  1.00 54.35  ? 74   LYS A CE  1 
ATOM   532   N  NZ  . LYS A 1 65  ? 11.100  100.305 17.265  1.00 60.66  ? 74   LYS A NZ  1 
ATOM   533   N  N   . ASP A 1 66  ? 10.862  94.783  13.881  1.00 17.93  ? 75   ASP A N   1 
ATOM   534   C  CA  . ASP A 1 66  ? 10.517  94.220  12.584  1.00 16.50  ? 75   ASP A CA  1 
ATOM   535   C  C   . ASP A 1 66  ? 9.881   95.314  11.733  1.00 20.38  ? 75   ASP A C   1 
ATOM   536   O  O   . ASP A 1 66  ? 8.744   95.700  11.960  1.00 19.49  ? 75   ASP A O   1 
ATOM   537   C  CB  . ASP A 1 66  ? 9.585   93.023  12.792  1.00 17.97  ? 75   ASP A CB  1 
ATOM   538   C  CG  . ASP A 1 66  ? 9.843   91.910  11.800  1.00 24.12  ? 75   ASP A CG  1 
ATOM   539   O  OD1 . ASP A 1 66  ? 10.691  92.083  10.907  1.00 22.46  ? 75   ASP A OD1 1 
ATOM   540   O  OD2 . ASP A 1 66  ? 9.167   90.895  11.879  1.00 26.09  ? 75   ASP A OD2 1 
ATOM   541   N  N   . PRO A 1 67  ? 10.571  95.828  10.713  1.00 20.07  ? 76   PRO A N   1 
ATOM   542   C  CA  . PRO A 1 67  ? 10.023  96.909  9.893   1.00 21.24  ? 76   PRO A CA  1 
ATOM   543   C  C   . PRO A 1 67  ? 8.870   96.526  8.972   1.00 18.31  ? 76   PRO A C   1 
ATOM   544   O  O   . PRO A 1 67  ? 8.890   95.481  8.347   1.00 20.16  ? 76   PRO A O   1 
ATOM   545   C  CB  . PRO A 1 67  ? 11.279  97.427  9.161   1.00 22.82  ? 76   PRO A CB  1 
ATOM   546   C  CG  . PRO A 1 67  ? 12.073  96.129  8.940   1.00 26.61  ? 76   PRO A CG  1 
ATOM   547   C  CD  . PRO A 1 67  ? 11.941  95.437  10.270  1.00 25.29  ? 76   PRO A CD  1 
ATOM   548   N  N   . GLU A 1 68  ? 7.863   97.414  8.913   1.00 18.63  ? 77   GLU A N   1 
ATOM   549   C  CA  . GLU A 1 68  ? 6.679   97.172  8.063   1.00 16.02  ? 77   GLU A CA  1 
ATOM   550   C  C   . GLU A 1 68  ? 7.022   97.310  6.586   1.00 15.30  ? 77   GLU A C   1 
ATOM   551   O  O   . GLU A 1 68  ? 6.376   96.689  5.724   1.00 18.15  ? 77   GLU A O   1 
ATOM   552   C  CB  . GLU A 1 68  ? 5.562   98.194  8.384   1.00 19.27  ? 77   GLU A CB  1 
ATOM   553   C  CG  . GLU A 1 68  ? 5.071   98.034  9.832   1.00 20.68  ? 77   GLU A CG  1 
ATOM   554   C  CD  . GLU A 1 68  ? 4.320   96.724  10.080  1.00 24.12  ? 77   GLU A CD  1 
ATOM   555   O  OE1 . GLU A 1 68  ? 3.968   95.985  9.139   1.00 20.62  ? 77   GLU A OE1 1 
ATOM   556   O  OE2 . GLU A 1 68  ? 4.057   96.423  11.261  1.00 21.55  ? 77   GLU A OE2 1 
ATOM   557   N  N   . TYR A 1 69  ? 8.057   98.126  6.297   1.00 17.18  ? 78   TYR A N   1 
ATOM   558   C  CA  . TYR A 1 69  ? 8.410   98.346  4.890   1.00 15.36  ? 78   TYR A CA  1 
ATOM   559   C  C   . TYR A 1 69  ? 9.885   98.720  4.871   1.00 14.44  ? 78   TYR A C   1 
ATOM   560   O  O   . TYR A 1 69  ? 10.337  99.435  5.794   1.00 16.03  ? 78   TYR A O   1 
ATOM   561   C  CB  . TYR A 1 69  ? 7.553   99.536  4.322   1.00 18.37  ? 78   TYR A CB  1 
ATOM   562   C  CG  . TYR A 1 69  ? 7.882   99.958  2.901   1.00 19.35  ? 78   TYR A CG  1 
ATOM   563   C  CD1 . TYR A 1 69  ? 7.854   99.048  1.857   1.00 22.41  ? 78   TYR A CD1 1 
ATOM   564   C  CD2 . TYR A 1 69  ? 8.212   101.295 2.604   1.00 17.92  ? 78   TYR A CD2 1 
ATOM   565   C  CE1 . TYR A 1 69  ? 8.155   99.435  0.557   1.00 24.97  ? 78   TYR A CE1 1 
ATOM   566   C  CE2 . TYR A 1 69  ? 8.495   101.686 1.305   1.00 24.65  ? 78   TYR A CE2 1 
ATOM   567   C  CZ  . TYR A 1 69  ? 8.472   100.754 0.295   1.00 25.15  ? 78   TYR A CZ  1 
ATOM   568   O  OH  . TYR A 1 69  ? 8.782   101.142 -0.980  1.00 29.38  ? 78   TYR A OH  1 
ATOM   569   N  N   . LEU A 1 70  ? 10.587  98.245  3.806   1.00 15.36  ? 79   LEU A N   1 
ATOM   570   C  CA  . LEU A 1 70  ? 12.058  98.390  3.644   1.00 14.39  ? 79   LEU A CA  1 
ATOM   571   C  C   . LEU A 1 70  ? 12.756  97.506  4.689   1.00 17.53  ? 79   LEU A C   1 
ATOM   572   O  O   . LEU A 1 70  ? 12.147  96.976  5.632   1.00 15.84  ? 79   LEU A O   1 
ATOM   573   C  CB  . LEU A 1 70  ? 12.599  99.851  3.766   1.00 13.60  ? 79   LEU A CB  1 
ATOM   574   C  CG  . LEU A 1 70  ? 11.864  100.850 2.879   1.00 20.90  ? 79   LEU A CG  1 
ATOM   575   C  CD1 . LEU A 1 70  ? 12.475  102.279 2.901   1.00 20.57  ? 79   LEU A CD1 1 
ATOM   576   C  CD2 . LEU A 1 70  ? 11.959  100.288 1.491   1.00 20.40  ? 79   LEU A CD2 1 
ATOM   577   N  N   . ASN A 1 71  ? 14.055  97.291  4.499   1.00 15.51  ? 80   ASN A N   1 
ATOM   578   C  CA  . ASN A 1 71  ? 14.759  96.425  5.437   1.00 16.00  ? 80   ASN A CA  1 
ATOM   579   C  C   . ASN A 1 71  ? 16.214  96.828  5.585   1.00 18.94  ? 80   ASN A C   1 
ATOM   580   O  O   . ASN A 1 71  ? 17.094  95.968  5.852   1.00 18.65  ? 80   ASN A O   1 
ATOM   581   C  CB  . ASN A 1 71  ? 14.656  94.923  4.974   1.00 17.35  ? 80   ASN A CB  1 
ATOM   582   C  CG  . ASN A 1 71  ? 15.458  94.619  3.710   1.00 20.53  ? 80   ASN A CG  1 
ATOM   583   O  OD1 . ASN A 1 71  ? 15.775  95.506  2.908   1.00 22.92  ? 80   ASN A OD1 1 
ATOM   584   N  ND2 . ASN A 1 71  ? 15.881  93.355  3.488   1.00 19.85  ? 80   ASN A ND2 1 
ATOM   585   N  N   . VAL A 1 72  ? 16.486  98.129  5.446   1.00 16.32  ? 81   VAL A N   1 
ATOM   586   C  CA  . VAL A 1 72  ? 17.878  98.584  5.653   1.00 15.66  ? 81   VAL A CA  1 
ATOM   587   C  C   . VAL A 1 72  ? 17.855  99.644  6.757   1.00 17.92  ? 81   VAL A C   1 
ATOM   588   O  O   . VAL A 1 72  ? 17.140  100.660 6.617   1.00 17.57  ? 81   VAL A O   1 
ATOM   589   C  CB  . VAL A 1 72  ? 18.475  99.180  4.365   1.00 18.10  ? 81   VAL A CB  1 
ATOM   590   C  CG1 . VAL A 1 72  ? 19.897  99.719  4.680   1.00 15.93  ? 81   VAL A CG1 1 
ATOM   591   C  CG2 . VAL A 1 72  ? 18.527  98.095  3.256   1.00 17.05  ? 81   VAL A CG2 1 
ATOM   592   N  N   . TRP A 1 73  ? 18.591  99.417  7.832   1.00 16.77  ? 82   TRP A N   1 
ATOM   593   C  CA  . TRP A 1 73  ? 18.699  100.345 8.929   1.00 17.20  ? 82   TRP A CA  1 
ATOM   594   C  C   . TRP A 1 73  ? 19.740  101.388 8.561   1.00 17.37  ? 82   TRP A C   1 
ATOM   595   O  O   . TRP A 1 73  ? 20.875  101.015 8.256   1.00 17.03  ? 82   TRP A O   1 
ATOM   596   C  CB  . TRP A 1 73  ? 19.164  99.595  10.192  1.00 16.56  ? 82   TRP A CB  1 
ATOM   597   C  CG  . TRP A 1 73  ? 18.161  98.660  10.686  1.00 17.32  ? 82   TRP A CG  1 
ATOM   598   C  CD1 . TRP A 1 73  ? 18.177  97.291  10.587  1.00 16.35  ? 82   TRP A CD1 1 
ATOM   599   C  CD2 . TRP A 1 73  ? 16.905  99.006  11.312  1.00 15.32  ? 82   TRP A CD2 1 
ATOM   600   N  NE1 . TRP A 1 73  ? 16.983  96.775  11.080  1.00 16.32  ? 82   TRP A NE1 1 
ATOM   601   C  CE2 . TRP A 1 73  ? 16.194  97.809  11.540  1.00 19.49  ? 82   TRP A CE2 1 
ATOM   602   C  CE3 . TRP A 1 73  ? 16.324  100.230 11.718  1.00 19.67  ? 82   TRP A CE3 1 
ATOM   603   C  CZ2 . TRP A 1 73  ? 14.926  97.795  12.149  1.00 16.78  ? 82   TRP A CZ2 1 
ATOM   604   C  CZ3 . TRP A 1 73  ? 15.063  100.217 12.331  1.00 19.14  ? 82   TRP A CZ3 1 
ATOM   605   C  CH2 . TRP A 1 73  ? 14.380  99.015  12.535  1.00 17.32  ? 82   TRP A CH2 1 
ATOM   606   N  N   . GLU A 1 74  ? 19.377  102.673 8.604   1.00 17.27  ? 83   GLU A N   1 
ATOM   607   C  CA  . GLU A 1 74  ? 20.291  103.767 8.201   1.00 18.70  ? 83   GLU A CA  1 
ATOM   608   C  C   . GLU A 1 74  ? 20.581  104.624 9.393   1.00 19.11  ? 83   GLU A C   1 
ATOM   609   O  O   . GLU A 1 74  ? 19.665  105.024 10.119  1.00 19.12  ? 83   GLU A O   1 
ATOM   610   C  CB  . GLU A 1 74  ? 19.604  104.630 7.118   1.00 21.50  ? 83   GLU A CB  1 
ATOM   611   C  CG  . GLU A 1 74  ? 19.376  103.758 5.875   1.00 18.66  ? 83   GLU A CG  1 
ATOM   612   C  CD  . GLU A 1 74  ? 18.811  104.530 4.657   1.00 29.05  ? 83   GLU A CD  1 
ATOM   613   O  OE1 . GLU A 1 74  ? 18.925  105.724 4.605   1.00 35.41  ? 83   GLU A OE1 1 
ATOM   614   O  OE2 . GLU A 1 74  ? 18.251  103.892 3.770   1.00 32.01  ? 83   GLU A OE2 1 
ATOM   615   N  N   . LEU A 1 75  ? 21.849  104.908 9.627   1.00 16.00  ? 84   LEU A N   1 
ATOM   616   C  CA  . LEU A 1 75  ? 22.227  105.705 10.804  1.00 16.46  ? 84   LEU A CA  1 
ATOM   617   C  C   . LEU A 1 75  ? 21.768  107.164 10.637  1.00 16.53  ? 84   LEU A C   1 
ATOM   618   O  O   . LEU A 1 75  ? 22.043  107.774 9.603   1.00 17.58  ? 84   LEU A O   1 
ATOM   619   C  CB  . LEU A 1 75  ? 23.801  105.701 10.913  1.00 19.77  ? 84   LEU A CB  1 
ATOM   620   C  CG  . LEU A 1 75  ? 24.327  106.542 12.105  1.00 19.78  ? 84   LEU A CG  1 
ATOM   621   C  CD1 . LEU A 1 75  ? 23.892  106.062 13.475  1.00 18.25  ? 84   LEU A CD1 1 
ATOM   622   C  CD2 . LEU A 1 75  ? 25.896  106.542 11.982  1.00 20.82  ? 84   LEU A CD2 1 
ATOM   623   N  N   . GLN A 1 76  ? 21.056  107.723 11.634  1.00 15.97  ? 85   GLN A N   1 
ATOM   624   C  CA  . GLN A 1 76  ? 20.565  109.129 11.567  1.00 15.25  ? 85   GLN A CA  1 
ATOM   625   C  C   . GLN A 1 76  ? 21.353  110.095 12.427  1.00 16.88  ? 85   GLN A C   1 
ATOM   626   O  O   . GLN A 1 76  ? 21.531  111.243 12.026  1.00 18.88  ? 85   GLN A O   1 
ATOM   627   C  CB  . GLN A 1 76  ? 19.147  109.188 12.086  1.00 17.62  ? 85   GLN A CB  1 
ATOM   628   C  CG  . GLN A 1 76  ? 18.257  108.111 11.409  1.00 20.30  ? 85   GLN A CG  1 
ATOM   629   C  CD  . GLN A 1 76  ? 18.061  108.433 9.986   1.00 25.44  ? 85   GLN A CD  1 
ATOM   630   O  OE1 . GLN A 1 76  ? 17.529  109.486 9.652   1.00 31.05  ? 85   GLN A OE1 1 
ATOM   631   N  NE2 . GLN A 1 76  ? 18.429  107.550 9.080   1.00 20.36  ? 85   GLN A NE2 1 
ATOM   632   N  N   . SER A 1 77  ? 21.816  109.665 13.565  1.00 17.43  ? 86   SER A N   1 
ATOM   633   C  CA  . SER A 1 77  ? 22.434  110.606 14.464  1.00 18.94  ? 86   SER A CA  1 
ATOM   634   C  C   . SER A 1 77  ? 23.100  109.939 15.626  1.00 20.29  ? 86   SER A C   1 
ATOM   635   O  O   . SER A 1 77  ? 22.887  108.758 15.913  1.00 18.54  ? 86   SER A O   1 
ATOM   636   C  CB  . SER A 1 77  ? 21.345  111.557 15.027  1.00 20.47  ? 86   SER A CB  1 
ATOM   637   O  OG  . SER A 1 77  ? 20.401  110.827 15.810  1.00 20.64  ? 86   SER A OG  1 
ATOM   638   N  N   . ILE A 1 78  ? 23.937  110.718 16.326  1.00 18.34  ? 87   ILE A N   1 
ATOM   639   C  CA  . ILE A 1 78  ? 24.553  110.245 17.559  1.00 17.69  ? 87   ILE A CA  1 
ATOM   640   C  C   . ILE A 1 78  ? 24.293  111.280 18.611  1.00 18.53  ? 87   ILE A C   1 
ATOM   641   O  O   . ILE A 1 78  ? 24.569  112.468 18.374  1.00 19.62  ? 87   ILE A O   1 
ATOM   642   C  CB  . ILE A 1 78  ? 26.099  110.084 17.371  1.00 19.72  ? 87   ILE A CB  1 
ATOM   643   C  CG1 . ILE A 1 78  ? 26.377  108.974 16.370  1.00 18.26  ? 87   ILE A CG1 1 
ATOM   644   C  CG2 . ILE A 1 78  ? 26.725  109.770 18.749  1.00 18.95  ? 87   ILE A CG2 1 
ATOM   645   C  CD1 . ILE A 1 78  ? 27.912  108.796 16.028  1.00 22.25  ? 87   ILE A CD1 1 
ATOM   646   N  N   . LYS A 1 79  ? 23.771  110.864 19.768  1.00 18.75  ? 88   LYS A N   1 
ATOM   647   C  CA  . LYS A 1 79  ? 23.539  111.813 20.823  1.00 19.42  ? 88   LYS A CA  1 
ATOM   648   C  C   . LYS A 1 79  ? 24.607  111.555 21.902  1.00 19.79  ? 88   LYS A C   1 
ATOM   649   O  O   . LYS A 1 79  ? 24.765  110.400 22.311  1.00 20.86  ? 88   LYS A O   1 
ATOM   650   C  CB  . LYS A 1 79  ? 22.133  111.599 21.479  1.00 17.55  ? 88   LYS A CB  1 
ATOM   651   C  CG  . LYS A 1 79  ? 21.909  112.580 22.664  1.00 18.12  ? 88   LYS A CG  1 
ATOM   652   C  CD  . LYS A 1 79  ? 20.415  112.603 23.134  1.00 21.02  ? 88   LYS A CD  1 
ATOM   653   C  CE  . LYS A 1 79  ? 20.262  113.268 24.469  1.00 23.01  ? 88   LYS A CE  1 
ATOM   654   N  NZ  . LYS A 1 79  ? 18.815  113.485 24.785  1.00 21.16  ? 88   LYS A NZ  1 
ATOM   655   N  N   . ILE A 1 80  ? 25.306  112.595 22.328  1.00 20.05  ? 89   ILE A N   1 
ATOM   656   C  CA  . ILE A 1 80  ? 26.328  112.460 23.372  1.00 20.03  ? 89   ILE A CA  1 
ATOM   657   C  C   . ILE A 1 80  ? 25.687  112.740 24.708  1.00 23.45  ? 89   ILE A C   1 
ATOM   658   O  O   . ILE A 1 80  ? 25.209  113.852 24.940  1.00 24.74  ? 89   ILE A O   1 
ATOM   659   C  CB  . ILE A 1 80  ? 27.451  113.434 23.027  1.00 23.56  ? 89   ILE A CB  1 
ATOM   660   C  CG1 . ILE A 1 80  ? 28.007  113.067 21.614  1.00 23.74  ? 89   ILE A CG1 1 
ATOM   661   C  CG2 . ILE A 1 80  ? 28.543  113.394 24.122  1.00 23.75  ? 89   ILE A CG2 1 
ATOM   662   C  CD1 . ILE A 1 80  ? 28.887  114.187 20.980  1.00 26.12  ? 89   ILE A CD1 1 
ATOM   663   N  N   . ASN A 1 81  ? 25.654  111.741 25.564  1.00 21.23  ? 90   ASN A N   1 
ATOM   664   C  CA  . ASN A 1 81  ? 24.940  111.893 26.836  1.00 24.14  ? 90   ASN A CA  1 
ATOM   665   C  C   . ASN A 1 81  ? 25.832  112.514 27.971  1.00 26.71  ? 90   ASN A C   1 
ATOM   666   O  O   . ASN A 1 81  ? 26.066  111.818 28.959  1.00 30.68  ? 90   ASN A O   1 
ATOM   667   C  CB  . ASN A 1 81  ? 24.402  110.514 27.256  1.00 25.58  ? 90   ASN A CB  1 
ATOM   668   C  CG  . ASN A 1 81  ? 23.479  109.896 26.199  1.00 27.06  ? 90   ASN A CG  1 
ATOM   669   O  OD1 . ASN A 1 81  ? 22.593  110.612 25.663  1.00 26.83  ? 90   ASN A OD1 1 
ATOM   670   N  ND2 . ASN A 1 81  ? 23.627  108.605 25.823  1.00 24.34  ? 90   ASN A ND2 1 
ATOM   671   N  N   . GLY A 1 82  ? 26.316  113.745 27.850  1.00 29.07  ? 91   GLY A N   1 
ATOM   672   C  CA  . GLY A 1 82  ? 27.073  114.345 28.958  1.00 33.22  ? 91   GLY A CA  1 
ATOM   673   C  C   . GLY A 1 82  ? 26.190  114.578 30.178  1.00 37.74  ? 91   GLY A C   1 
ATOM   674   O  O   . GLY A 1 82  ? 24.966  114.640 30.065  1.00 41.10  ? 91   GLY A O   1 
ATOM   675   N  N   . LYS A 1 83  ? 26.794  114.718 31.356  1.00 44.19  ? 92   LYS A N   1 
ATOM   676   C  CA  . LYS A 1 83  ? 26.045  114.961 32.606  1.00 52.80  ? 92   LYS A CA  1 
ATOM   677   C  C   . LYS A 1 83  ? 25.342  116.320 32.570  1.00 55.60  ? 92   LYS A C   1 
ATOM   678   O  O   . LYS A 1 83  ? 24.145  116.409 32.870  1.00 54.42  ? 92   LYS A O   1 
ATOM   679   C  CB  . LYS A 1 83  ? 26.990  114.940 33.823  1.00 58.88  ? 92   LYS A CB  1 
ATOM   680   C  CG  . LYS A 1 83  ? 26.237  114.998 35.154  1.00 66.58  ? 92   LYS A CG  1 
ATOM   681   C  CD  . LYS A 1 83  ? 27.205  114.942 36.356  1.00 71.44  ? 92   LYS A CD  1 
ATOM   682   C  CE  . LYS A 1 83  ? 27.532  116.343 36.849  1.00 73.13  ? 92   LYS A CE  1 
ATOM   683   N  NZ  . LYS A 1 83  ? 28.401  116.317 38.054  1.00 76.35  ? 92   LYS A NZ  1 
ATOM   684   N  N   . ASP A 1 84  ? 26.089  117.374 32.183  1.00 53.56  ? 93   ASP A N   1 
ATOM   685   C  CA  . ASP A 1 84  ? 25.519  118.713 32.140  1.00 54.24  ? 93   ASP A CA  1 
ATOM   686   C  C   . ASP A 1 84  ? 25.121  119.161 30.758  1.00 54.95  ? 93   ASP A C   1 
ATOM   687   O  O   . ASP A 1 84  ? 24.219  119.983 30.629  1.00 55.81  ? 93   ASP A O   1 
ATOM   688   C  CB  . ASP A 1 84  ? 26.516  119.722 32.731  1.00 56.97  ? 93   ASP A CB  1 
ATOM   689   C  CG  . ASP A 1 84  ? 26.816  119.428 34.193  1.00 61.17  ? 93   ASP A CG  1 
ATOM   690   O  OD1 . ASP A 1 84  ? 25.875  119.046 34.928  1.00 63.43  ? 93   ASP A OD1 1 
ATOM   691   O  OD2 . ASP A 1 84  ? 27.985  119.566 34.595  1.00 64.26  ? 93   ASP A OD2 1 
ATOM   692   N  N   . GLU A 1 85  ? 25.785  118.657 29.728  1.00 51.64  ? 94   GLU A N   1 
ATOM   693   C  CA  . GLU A 1 85  ? 25.438  119.056 28.380  1.00 47.01  ? 94   GLU A CA  1 
ATOM   694   C  C   . GLU A 1 85  ? 25.259  117.838 27.478  1.00 42.40  ? 94   GLU A C   1 
ATOM   695   O  O   . GLU A 1 85  ? 25.985  116.847 27.623  1.00 36.49  ? 94   GLU A O   1 
ATOM   696   C  CB  . GLU A 1 85  ? 26.530  119.937 27.803  1.00 50.57  ? 94   GLU A CB  1 
ATOM   697   C  CG  . GLU A 1 85  ? 26.168  120.514 26.461  1.00 63.71  ? 94   GLU A CG  1 
ATOM   698   C  CD  . GLU A 1 85  ? 27.301  121.371 25.910  1.00 76.94  ? 94   GLU A CD  1 
ATOM   699   O  OE1 . GLU A 1 85  ? 28.333  120.781 25.496  1.00 79.93  ? 94   GLU A OE1 1 
ATOM   700   O  OE2 . GLU A 1 85  ? 27.153  122.627 25.904  1.00 74.96  ? 94   GLU A OE2 1 
ATOM   701   N  N   . GLN A 1 86  ? 24.279  117.896 26.565  1.00 32.26  ? 95   GLN A N   1 
ATOM   702   C  CA  . GLN A 1 86  ? 24.080  116.803 25.636  1.00 27.39  ? 95   GLN A CA  1 
ATOM   703   C  C   . GLN A 1 86  ? 24.247  117.425 24.274  1.00 32.19  ? 95   GLN A C   1 
ATOM   704   O  O   . GLN A 1 86  ? 23.806  118.567 24.073  1.00 39.00  ? 95   GLN A O   1 
ATOM   705   C  CB  . GLN A 1 86  ? 22.696  116.172 25.813  1.00 26.86  ? 95   GLN A CB  1 
ATOM   706   C  CG  . GLN A 1 86  ? 22.561  115.524 27.200  1.00 30.62  ? 95   GLN A CG  1 
ATOM   707   C  CD  . GLN A 1 86  ? 22.237  116.554 28.299  1.00 38.89  ? 95   GLN A CD  1 
ATOM   708   O  OE1 . GLN A 1 86  ? 22.895  116.590 29.355  1.00 41.52  ? 95   GLN A OE1 1 
ATOM   709   N  NE2 . GLN A 1 86  ? 21.245  117.401 28.098  1.00 31.75  ? 95   GLN A NE2 1 
ATOM   710   N  N   . LYS A 1 87  ? 24.882  116.787 23.386  1.00 28.02  ? 96   LYS A N   1 
ATOM   711   C  CA  . LYS A 1 87  ? 25.065  117.354 22.071  1.00 25.45  ? 96   LYS A CA  1 
ATOM   712   C  C   . LYS A 1 87  ? 24.563  116.308 21.100  1.00 23.40  ? 96   LYS A C   1 
ATOM   713   O  O   . LYS A 1 87  ? 24.782  115.128 21.362  1.00 23.03  ? 96   LYS A O   1 
ATOM   714   C  CB  . LYS A 1 87  ? 26.568  117.650 21.874  1.00 28.42  ? 96   LYS A CB  1 
ATOM   715   C  CG  . LYS A 1 87  ? 26.937  118.029 20.452  1.00 32.89  ? 96   LYS A CG  1 
ATOM   716   C  CD  . LYS A 1 87  ? 28.456  118.449 20.389  1.00 40.25  ? 96   LYS A CD  1 
ATOM   717   C  CE  . LYS A 1 87  ? 28.816  118.933 19.047  1.00 47.10  ? 96   LYS A CE  1 
ATOM   718   N  NZ  . LYS A 1 87  ? 28.061  120.176 18.701  1.00 62.78  ? 96   LYS A NZ  1 
ATOM   719   N  N   . VAL A 1 88  ? 23.907  116.701 20.017  1.00 21.04  ? 97   VAL A N   1 
ATOM   720   C  CA  . VAL A 1 88  ? 23.435  115.719 19.052  1.00 19.49  ? 97   VAL A CA  1 
ATOM   721   C  C   . VAL A 1 88  ? 24.064  116.009 17.739  1.00 18.73  ? 97   VAL A C   1 
ATOM   722   O  O   . VAL A 1 88  ? 24.042  117.165 17.269  1.00 20.76  ? 97   VAL A O   1 
ATOM   723   C  CB  . VAL A 1 88  ? 21.889  115.801 18.908  1.00 20.01  ? 97   VAL A CB  1 
ATOM   724   C  CG1 . VAL A 1 88  ? 21.392  114.934 17.752  1.00 23.47  ? 97   VAL A CG1 1 
ATOM   725   C  CG2 . VAL A 1 88  ? 21.231  115.373 20.233  1.00 18.24  ? 97   VAL A CG2 1 
ATOM   726   N  N   . LEU A 1 89  ? 24.674  114.983 17.147  1.00 16.39  ? 98   LEU A N   1 
ATOM   727   C  CA  . LEU A 1 89  ? 25.224  115.111 15.816  1.00 16.30  ? 98   LEU A CA  1 
ATOM   728   C  C   . LEU A 1 89  ? 24.181  114.515 14.858  1.00 19.18  ? 98   LEU A C   1 
ATOM   729   O  O   . LEU A 1 89  ? 23.939  113.281 14.910  1.00 18.93  ? 98   LEU A O   1 
ATOM   730   C  CB  . LEU A 1 89  ? 26.547  114.305 15.658  1.00 19.13  ? 98   LEU A CB  1 
ATOM   731   C  CG  . LEU A 1 89  ? 27.610  114.677 16.765  1.00 25.70  ? 98   LEU A CG  1 
ATOM   732   C  CD1 . LEU A 1 89  ? 28.813  113.730 16.690  1.00 24.19  ? 98   LEU A CD1 1 
ATOM   733   C  CD2 . LEU A 1 89  ? 28.080  116.098 16.554  1.00 25.88  ? 98   LEU A CD2 1 
ATOM   734   N  N   . ASN A 1 90  ? 23.564  115.332 13.998  1.00 19.65  ? 99   ASN A N   1 
ATOM   735   C  CA  . ASN A 1 90  ? 22.601  114.744 13.068  1.00 20.07  ? 99   ASN A CA  1 
ATOM   736   C  C   . ASN A 1 90  ? 23.303  114.358 11.753  1.00 19.53  ? 99   ASN A C   1 
ATOM   737   O  O   . ASN A 1 90  ? 24.550  114.428 11.683  1.00 18.28  ? 99   ASN A O   1 
ATOM   738   C  CB  . ASN A 1 90  ? 21.373  115.740 12.858  1.00 17.46  ? 99   ASN A CB  1 
ATOM   739   C  CG  . ASN A 1 90  ? 21.747  117.045 12.211  1.00 21.37  ? 99   ASN A CG  1 
ATOM   740   O  OD1 . ASN A 1 90  ? 22.881  117.270 11.729  1.00 23.02  ? 99   ASN A OD1 1 
ATOM   741   N  ND2 . ASN A 1 90  ? 20.792  117.975 12.103  1.00 21.66  ? 99   ASN A ND2 1 
ATOM   742   N  N   . LYS A 1 91  ? 22.549  113.930 10.740  1.00 18.55  ? 100  LYS A N   1 
ATOM   743   C  CA  . LYS A 1 91  ? 23.203  113.466 9.470   1.00 20.20  ? 100  LYS A CA  1 
ATOM   744   C  C   . LYS A 1 91  ? 24.119  114.443 8.894   1.00 22.40  ? 100  LYS A C   1 
ATOM   745   O  O   . LYS A 1 91  ? 25.240  114.099 8.505   1.00 21.49  ? 100  LYS A O   1 
ATOM   746   C  CB  . LYS A 1 91  ? 22.182  113.190 8.385   1.00 25.22  ? 100  LYS A CB  1 
ATOM   747   C  CG  . LYS A 1 91  ? 21.254  112.079 8.750   1.00 36.59  ? 100  LYS A CG  1 
ATOM   748   C  CD  . LYS A 1 91  ? 21.117  111.127 7.545   1.00 46.03  ? 100  LYS A CD  1 
ATOM   749   C  CE  . LYS A 1 91  ? 20.609  111.813 6.340   1.00 53.44  ? 100  LYS A CE  1 
ATOM   750   N  NZ  . LYS A 1 91  ? 19.560  110.953 5.679   1.00 64.75  ? 100  LYS A NZ  1 
ATOM   751   N  N   . GLU A 1 92  ? 23.663  115.708 8.797   1.00 22.53  ? 101  GLU A N   1 
ATOM   752   C  CA  . GLU A 1 92  ? 24.548  116.729 8.218   1.00 22.52  ? 101  GLU A CA  1 
ATOM   753   C  C   . GLU A 1 92  ? 25.793  116.927 9.043   1.00 21.13  ? 101  GLU A C   1 
ATOM   754   O  O   . GLU A 1 92  ? 26.875  117.103 8.475   1.00 23.68  ? 101  GLU A O   1 
ATOM   755   C  CB  . GLU A 1 92  ? 23.744  118.058 8.071   1.00 22.17  ? 101  GLU A CB  1 
ATOM   756   C  CG  . GLU A 1 92  ? 24.596  119.192 7.554   1.00 29.32  ? 101  GLU A CG  1 
ATOM   757   C  CD  . GLU A 1 92  ? 23.737  120.462 7.224   1.00 38.03  ? 101  GLU A CD  1 
ATOM   758   O  OE1 . GLU A 1 92  ? 24.324  121.443 6.768   1.00 42.09  ? 101  GLU A OE1 1 
ATOM   759   O  OE2 . GLU A 1 92  ? 22.492  120.460 7.427   1.00 39.78  ? 101  GLU A OE2 1 
ATOM   760   N  N   . ASP A 1 93  ? 25.702  116.907 10.365  1.00 20.19  ? 102  ASP A N   1 
ATOM   761   C  CA  . ASP A 1 93  ? 26.921  117.095 11.184  1.00 18.80  ? 102  ASP A CA  1 
ATOM   762   C  C   . ASP A 1 93  ? 27.843  115.916 10.955  1.00 22.13  ? 102  ASP A C   1 
ATOM   763   O  O   . ASP A 1 93  ? 29.060  116.086 10.834  1.00 23.10  ? 102  ASP A O   1 
ATOM   764   C  CB  . ASP A 1 93  ? 26.576  117.101 12.701  1.00 19.76  ? 102  ASP A CB  1 
ATOM   765   C  CG  . ASP A 1 93  ? 25.649  118.259 13.073  1.00 24.87  ? 102  ASP A CG  1 
ATOM   766   O  OD1 . ASP A 1 93  ? 24.881  118.126 14.080  1.00 23.17  ? 102  ASP A OD1 1 
ATOM   767   O  OD2 . ASP A 1 93  ? 25.680  119.278 12.368  1.00 27.35  ? 102  ASP A OD2 1 
ATOM   768   N  N   . LEU A 1 94  ? 27.284  114.694 10.943  1.00 18.13  ? 103  LEU A N   1 
ATOM   769   C  CA  . LEU A 1 94  ? 28.147  113.524 10.776  1.00 19.79  ? 103  LEU A CA  1 
ATOM   770   C  C   . LEU A 1 94  ? 28.856  113.555 9.392   1.00 20.86  ? 103  LEU A C   1 
ATOM   771   O  O   . LEU A 1 94  ? 30.044  113.192 9.316   1.00 22.79  ? 103  LEU A O   1 
ATOM   772   C  CB  . LEU A 1 94  ? 27.354  112.247 10.941  1.00 17.69  ? 103  LEU A CB  1 
ATOM   773   C  CG  . LEU A 1 94  ? 26.815  112.029 12.335  1.00 19.22  ? 103  LEU A CG  1 
ATOM   774   C  CD1 . LEU A 1 94  ? 25.832  110.883 12.316  1.00 20.60  ? 103  LEU A CD1 1 
ATOM   775   C  CD2 . LEU A 1 94  ? 27.942  111.702 13.229  1.00 19.57  ? 103  LEU A CD2 1 
ATOM   776   N  N   . GLU A 1 95  ? 28.156  113.973 8.348   1.00 21.11  ? 104  GLU A N   1 
ATOM   777   C  CA  . GLU A 1 95  ? 28.743  114.081 7.016   1.00 23.14  ? 104  GLU A CA  1 
ATOM   778   C  C   . GLU A 1 95  ? 29.793  115.195 7.003   1.00 28.00  ? 104  GLU A C   1 
ATOM   779   O  O   . GLU A 1 95  ? 30.791  115.065 6.299   1.00 28.20  ? 104  GLU A O   1 
ATOM   780   C  CB  . GLU A 1 95  ? 27.672  114.374 5.981   1.00 25.88  ? 104  GLU A CB  1 
ATOM   781   C  CG  . GLU A 1 95  ? 26.829  113.138 5.734   1.00 34.60  ? 104  GLU A CG  1 
ATOM   782   C  CD  . GLU A 1 95  ? 25.600  113.424 4.875   1.00 43.30  ? 104  GLU A CD  1 
ATOM   783   O  OE1 . GLU A 1 95  ? 25.074  112.479 4.284   1.00 44.29  ? 104  GLU A OE1 1 
ATOM   784   O  OE2 . GLU A 1 95  ? 25.150  114.599 4.810   1.00 43.26  ? 104  GLU A OE2 1 
ATOM   785   N  N   . SER A 1 96  ? 29.582  116.273 7.813   1.00 24.63  ? 105  SER A N   1 
ATOM   786   C  CA  . SER A 1 96  ? 30.547  117.375 7.896   1.00 26.02  ? 105  SER A CA  1 
ATOM   787   C  C   . SER A 1 96  ? 31.825  116.872 8.570   1.00 26.24  ? 105  SER A C   1 
ATOM   788   O  O   . SER A 1 96  ? 32.885  117.465 8.387   1.00 25.28  ? 105  SER A O   1 
ATOM   789   C  CB  . SER A 1 96  ? 29.981  118.516 8.770   1.00 27.39  ? 105  SER A CB  1 
ATOM   790   O  OG  . SER A 1 96  ? 28.988  119.107 7.958   1.00 35.16  ? 105  SER A OG  1 
ATOM   791   N  N   . MET A 1 97  ? 31.722  115.800 9.356   1.00 27.38  ? 106  MET A N   1 
ATOM   792   C  CA  . MET A 1 97  ? 32.906  115.248 10.041  1.00 29.03  ? 106  MET A CA  1 
ATOM   793   C  C   . MET A 1 97  ? 33.548  114.135 9.253   1.00 30.33  ? 106  MET A C   1 
ATOM   794   O  O   . MET A 1 97  ? 34.356  113.394 9.815   1.00 31.02  ? 106  MET A O   1 
ATOM   795   C  CB  . MET A 1 97  ? 32.546  114.719 11.390  1.00 33.94  ? 106  MET A CB  1 
ATOM   796   C  CG  . MET A 1 97  ? 32.099  115.761 12.265  1.00 46.43  ? 106  MET A CG  1 
ATOM   797   S  SD  . MET A 1 97  ? 31.500  114.987 13.782  1.00 53.09  ? 106  MET A SD  1 
ATOM   798   C  CE  . MET A 1 97  ? 33.034  114.406 14.435  1.00 49.73  ? 106  MET A CE  1 
ATOM   799   N  N   . GLY A 1 98  ? 33.227  114.014 8.001   1.00 27.41  ? 107  GLY A N   1 
ATOM   800   C  CA  . GLY A 1 98  ? 33.902  113.023 7.185   1.00 34.64  ? 107  GLY A CA  1 
ATOM   801   C  C   . GLY A 1 98  ? 33.230  111.660 6.989   1.00 32.73  ? 107  GLY A C   1 
ATOM   802   O  O   . GLY A 1 98  ? 33.779  110.820 6.281   1.00 32.73  ? 107  GLY A O   1 
ATOM   803   N  N   . LEU A 1 99  ? 32.079  111.423 7.571   1.00 24.57  ? 108  LEU A N   1 
ATOM   804   C  CA  . LEU A 1 99  ? 31.486  110.092 7.411   1.00 22.48  ? 108  LEU A CA  1 
ATOM   805   C  C   . LEU A 1 99  ? 30.661  109.992 6.219   1.00 24.61  ? 108  LEU A C   1 
ATOM   806   O  O   . LEU A 1 99  ? 30.036  110.970 5.803   1.00 23.73  ? 108  LEU A O   1 
ATOM   807   C  CB  . LEU A 1 99  ? 30.621  109.810 8.646   1.00 25.41  ? 108  LEU A CB  1 
ATOM   808   C  CG  . LEU A 1 99  ? 31.431  109.702 9.928   1.00 26.93  ? 108  LEU A CG  1 
ATOM   809   C  CD1 . LEU A 1 99  ? 30.513  109.423 11.095  1.00 30.57  ? 108  LEU A CD1 1 
ATOM   810   C  CD2 . LEU A 1 99  ? 32.451  108.552 9.855   1.00 30.17  ? 108  LEU A CD2 1 
ATOM   811   N  N   . ASN A 1 100 ? 30.634  108.795 5.600   1.00 22.19  ? 109  ASN A N   1 
ATOM   812   C  CA  . ASN A 1 100 ? 29.726  108.560 4.505   1.00 24.05  ? 109  ASN A CA  1 
ATOM   813   C  C   . ASN A 1 100 ? 28.687  107.604 5.131   1.00 24.64  ? 109  ASN A C   1 
ATOM   814   O  O   . ASN A 1 100 ? 28.982  106.419 5.310   1.00 22.26  ? 109  ASN A O   1 
ATOM   815   C  CB  . ASN A 1 100 ? 30.384  107.886 3.341   1.00 31.30  ? 109  ASN A CB  1 
ATOM   816   C  CG  . ASN A 1 100 ? 29.408  107.763 2.214   1.00 46.05  ? 109  ASN A CG  1 
ATOM   817   O  OD1 . ASN A 1 100 ? 29.064  106.654 1.806   1.00 56.19  ? 109  ASN A OD1 1 
ATOM   818   N  ND2 . ASN A 1 100 ? 28.861  108.840 1.674   1.00 54.14  ? 109  ASN A ND2 1 
ATOM   819   N  N   . LEU A 1 101 ? 27.499  108.104 5.474   1.00 23.85  ? 110  LEU A N   1 
ATOM   820   C  CA  . LEU A 1 101 ? 26.560  107.280 6.253   1.00 22.68  ? 110  LEU A CA  1 
ATOM   821   C  C   . LEU A 1 101 ? 26.109  105.987 5.624   1.00 17.37  ? 110  LEU A C   1 
ATOM   822   O  O   . LEU A 1 101 ? 25.808  105.043 6.362   1.00 18.86  ? 110  LEU A O   1 
ATOM   823   C  CB  . LEU A 1 101 ? 25.350  108.154 6.637   1.00 23.63  ? 110  LEU A CB  1 
ATOM   824   C  CG  . LEU A 1 101 ? 25.814  109.369 7.471   1.00 26.05  ? 110  LEU A CG  1 
ATOM   825   C  CD1 . LEU A 1 101 ? 24.620  110.202 7.775   1.00 30.39  ? 110  LEU A CD1 1 
ATOM   826   C  CD2 . LEU A 1 101 ? 26.491  108.891 8.736   1.00 32.15  ? 110  LEU A CD2 1 
ATOM   827   N  N   . LYS A 1 102 ? 26.078  105.881 4.294   1.00 19.52  ? 111  LYS A N   1 
ATOM   828   C  CA  . LYS A 1 102 ? 25.692  104.638 3.724   1.00 21.61  ? 111  LYS A CA  1 
ATOM   829   C  C   . LYS A 1 102 ? 26.689  103.521 4.059   1.00 20.96  ? 111  LYS A C   1 
ATOM   830   O  O   . LYS A 1 102 ? 26.326  102.333 3.963   1.00 18.54  ? 111  LYS A O   1 
ATOM   831   C  CB  . LYS A 1 102 ? 25.574  104.726 2.196   1.00 24.95  ? 111  LYS A CB  1 
ATOM   832   C  CG  . LYS A 1 102 ? 24.224  105.378 1.750   1.00 40.13  ? 111  LYS A CG  1 
ATOM   833   C  CD  . LYS A 1 102 ? 23.113  104.327 1.334   1.00 53.42  ? 111  LYS A CD  1 
ATOM   834   C  CE  . LYS A 1 102 ? 21.729  104.657 1.931   1.00 55.67  ? 111  LYS A CE  1 
ATOM   835   N  NZ  . LYS A 1 102 ? 20.779  103.457 2.046   1.00 50.11  ? 111  LYS A NZ  1 
ATOM   836   N  N   . ASP A 1 103 ? 27.916  103.879 4.422   1.00 17.24  ? 112  ASP A N   1 
ATOM   837   C  CA  . ASP A 1 103 ? 28.858  102.810 4.780   1.00 19.31  ? 112  ASP A CA  1 
ATOM   838   C  C   . ASP A 1 103 ? 28.375  102.025 6.025   1.00 20.33  ? 112  ASP A C   1 
ATOM   839   O  O   . ASP A 1 103 ? 28.909  100.923 6.293   1.00 20.41  ? 112  ASP A O   1 
ATOM   840   C  CB  . ASP A 1 103 ? 30.203  103.411 5.211   1.00 19.67  ? 112  ASP A CB  1 
ATOM   841   C  CG  . ASP A 1 103 ? 30.947  104.101 4.100   1.00 24.60  ? 112  ASP A CG  1 
ATOM   842   O  OD1 . ASP A 1 103 ? 31.910  104.803 4.401   1.00 27.21  ? 112  ASP A OD1 1 
ATOM   843   O  OD2 . ASP A 1 103 ? 30.555  103.941 2.922   1.00 22.30  ? 112  ASP A OD2 1 
ATOM   844   N  N   . TYR A 1 104 ? 27.430  102.571 6.802   1.00 18.04  ? 113  TYR A N   1 
ATOM   845   C  CA  . TYR A 1 104 ? 26.974  101.866 8.009   1.00 18.03  ? 113  TYR A CA  1 
ATOM   846   C  C   . TYR A 1 104 ? 25.592  101.195 7.831   1.00 18.40  ? 113  TYR A C   1 
ATOM   847   O  O   . TYR A 1 104 ? 25.064  100.678 8.799   1.00 18.22  ? 113  TYR A O   1 
ATOM   848   C  CB  . TYR A 1 104 ? 26.912  102.835 9.220   1.00 19.96  ? 113  TYR A CB  1 
ATOM   849   C  CG  . TYR A 1 104 ? 28.232  103.544 9.327   1.00 21.16  ? 113  TYR A CG  1 
ATOM   850   C  CD1 . TYR A 1 104 ? 28.371  104.863 8.889   1.00 22.06  ? 113  TYR A CD1 1 
ATOM   851   C  CD2 . TYR A 1 104 ? 29.390  102.857 9.729   1.00 16.78  ? 113  TYR A CD2 1 
ATOM   852   C  CE1 . TYR A 1 104 ? 29.616  105.477 8.824   1.00 24.87  ? 113  TYR A CE1 1 
ATOM   853   C  CE2 . TYR A 1 104 ? 30.656  103.470 9.655   1.00 16.02  ? 113  TYR A CE2 1 
ATOM   854   C  CZ  . TYR A 1 104 ? 30.750  104.777 9.190   1.00 24.52  ? 113  TYR A CZ  1 
ATOM   855   O  OH  . TYR A 1 104 ? 31.960  105.388 8.978   1.00 26.52  ? 113  TYR A OH  1 
ATOM   856   N  N   . ASP A 1 105 ? 25.033  101.189 6.629   1.00 17.38  ? 114  ASP A N   1 
ATOM   857   C  CA  . ASP A 1 105 ? 23.686  100.571 6.449   1.00 16.38  ? 114  ASP A CA  1 
ATOM   858   C  C   . ASP A 1 105 ? 23.710  99.094  6.797   1.00 19.86  ? 114  ASP A C   1 
ATOM   859   O  O   . ASP A 1 105 ? 24.651  98.390  6.392   1.00 18.20  ? 114  ASP A O   1 
ATOM   860   C  CB  . ASP A 1 105 ? 23.328  100.651 4.972   1.00 16.49  ? 114  ASP A CB  1 
ATOM   861   C  CG  . ASP A 1 105 ? 22.881  102.026 4.524   1.00 24.65  ? 114  ASP A CG  1 
ATOM   862   O  OD1 . ASP A 1 105 ? 22.814  102.941 5.360   1.00 21.31  ? 114  ASP A OD1 1 
ATOM   863   O  OD2 . ASP A 1 105 ? 22.612  102.180 3.350   1.00 22.47  ? 114  ASP A OD2 1 
ATOM   864   N  N   . VAL A 1 106 ? 22.708  98.606  7.499   1.00 17.32  ? 115  VAL A N   1 
ATOM   865   C  CA  . VAL A 1 106 ? 22.665  97.196  7.897   1.00 15.67  ? 115  VAL A CA  1 
ATOM   866   C  C   . VAL A 1 106 ? 21.406  96.600  7.349   1.00 18.47  ? 115  VAL A C   1 
ATOM   867   O  O   . VAL A 1 106 ? 20.332  97.199  7.571   1.00 18.25  ? 115  VAL A O   1 
ATOM   868   C  CB  . VAL A 1 106 ? 22.723  97.116  9.451   1.00 17.57  ? 115  VAL A CB  1 
ATOM   869   C  CG1 . VAL A 1 106 ? 22.410  95.692  9.911   1.00 17.24  ? 115  VAL A CG1 1 
ATOM   870   C  CG2 . VAL A 1 106 ? 24.120  97.565  9.929   1.00 16.17  ? 115  VAL A CG2 1 
ATOM   871   N  N   . THR A 1 107 ? 21.513  95.487  6.586   1.00 16.33  ? 116  THR A N   1 
ATOM   872   C  CA  . THR A 1 107 ? 20.338  94.878  5.982   1.00 16.12  ? 116  THR A CA  1 
ATOM   873   C  C   . THR A 1 107 ? 19.781  93.785  6.886   1.00 20.31  ? 116  THR A C   1 
ATOM   874   O  O   . THR A 1 107 ? 20.517  92.870  7.323   1.00 17.18  ? 116  THR A O   1 
ATOM   875   C  CB  . THR A 1 107 ? 20.727  94.309  4.599   1.00 20.15  ? 116  THR A CB  1 
ATOM   876   O  OG1 . THR A 1 107 ? 21.255  95.373  3.826   1.00 19.86  ? 116  THR A OG1 1 
ATOM   877   C  CG2 . THR A 1 107 ? 19.527  93.717  3.880   1.00 18.70  ? 116  THR A CG2 1 
ATOM   878   N  N   . GLN A 1 108 ? 18.480  93.863  7.170   1.00 16.37  ? 117  GLN A N   1 
ATOM   879   C  CA  . GLN A 1 108 ? 17.807  92.854  8.002   1.00 17.39  ? 117  GLN A CA  1 
ATOM   880   C  C   . GLN A 1 108 ? 17.029  91.946  7.083   1.00 17.74  ? 117  GLN A C   1 
ATOM   881   O  O   . GLN A 1 108 ? 15.983  92.311  6.521   1.00 18.26  ? 117  GLN A O   1 
ATOM   882   C  CB  . GLN A 1 108 ? 16.872  93.536  9.023   1.00 17.18  ? 117  GLN A CB  1 
ATOM   883   C  CG  . GLN A 1 108 ? 16.185  92.532  9.956   1.00 17.08  ? 117  GLN A CG  1 
ATOM   884   C  CD  . GLN A 1 108 ? 15.582  93.289  11.125  1.00 18.32  ? 117  GLN A CD  1 
ATOM   885   O  OE1 . GLN A 1 108 ? 16.202  94.177  11.697  1.00 18.56  ? 117  GLN A OE1 1 
ATOM   886   N  NE2 . GLN A 1 108 ? 14.364  92.888  11.561  1.00 17.48  ? 117  GLN A NE2 1 
ATOM   887   N  N   . GLU A 1 109 ? 17.516  90.717  6.909   1.00 19.78  ? 118  GLU A N   1 
ATOM   888   C  CA  . GLU A 1 109 ? 16.851  89.756  6.022   1.00 17.87  ? 118  GLU A CA  1 
ATOM   889   C  C   . GLU A 1 109 ? 15.957  88.855  6.867   1.00 18.43  ? 118  GLU A C   1 
ATOM   890   O  O   . GLU A 1 109 ? 15.930  88.962  8.091   1.00 18.67  ? 118  GLU A O   1 
ATOM   891   C  CB  . GLU A 1 109 ? 17.906  88.853  5.377   1.00 19.32  ? 118  GLU A CB  1 
ATOM   892   C  CG  . GLU A 1 109 ? 19.027  89.629  4.748   1.00 25.72  ? 118  GLU A CG  1 
ATOM   893   C  CD  . GLU A 1 109 ? 18.683  90.044  3.306   1.00 37.46  ? 118  GLU A CD  1 
ATOM   894   O  OE1 . GLU A 1 109 ? 19.598  90.479  2.590   1.00 40.51  ? 118  GLU A OE1 1 
ATOM   895   O  OE2 . GLU A 1 109 ? 17.522  89.941  2.906   1.00 38.58  ? 118  GLU A OE2 1 
ATOM   896   N  N   . PHE A 1 110 ? 15.228  87.953  6.217   1.00 19.19  ? 119  PHE A N   1 
ATOM   897   C  CA  . PHE A 1 110 ? 14.382  87.024  6.956   1.00 19.70  ? 119  PHE A CA  1 
ATOM   898   C  C   . PHE A 1 110 ? 14.389  85.639  6.325   1.00 18.20  ? 119  PHE A C   1 
ATOM   899   O  O   . PHE A 1 110 ? 14.757  85.508  5.162   1.00 19.95  ? 119  PHE A O   1 
ATOM   900   C  CB  . PHE A 1 110 ? 12.930  87.563  7.096   1.00 20.47  ? 119  PHE A CB  1 
ATOM   901   C  CG  . PHE A 1 110 ? 12.207  87.714  5.783   1.00 21.08  ? 119  PHE A CG  1 
ATOM   902   C  CD1 . PHE A 1 110 ? 12.224  88.916  5.103   1.00 24.69  ? 119  PHE A CD1 1 
ATOM   903   C  CD2 . PHE A 1 110 ? 11.490  86.653  5.241   1.00 21.82  ? 119  PHE A CD2 1 
ATOM   904   C  CE1 . PHE A 1 110 ? 11.562  89.060  3.896   1.00 30.12  ? 119  PHE A CE1 1 
ATOM   905   C  CE2 . PHE A 1 110 ? 10.827  86.789  4.029   1.00 22.74  ? 119  PHE A CE2 1 
ATOM   906   C  CZ  . PHE A 1 110 ? 10.870  87.993  3.359   1.00 29.99  ? 119  PHE A CZ  1 
ATOM   907   N  N   . ILE A 1 111 ? 14.027  84.628  7.091   1.00 19.23  ? 120  ILE A N   1 
ATOM   908   C  CA  . ILE A 1 111 ? 13.987  83.216  6.605   1.00 20.96  ? 120  ILE A CA  1 
ATOM   909   C  C   . ILE A 1 111 ? 13.016  83.119  5.461   1.00 24.20  ? 120  ILE A C   1 
ATOM   910   O  O   . ILE A 1 111 ? 11.863  83.562  5.621   1.00 22.90  ? 120  ILE A O   1 
ATOM   911   C  CB  . ILE A 1 111 ? 13.536  82.351  7.797   1.00 23.74  ? 120  ILE A CB  1 
ATOM   912   C  CG1 . ILE A 1 111 ? 14.742  82.167  8.743   1.00 23.71  ? 120  ILE A CG1 1 
ATOM   913   C  CG2 . ILE A 1 111 ? 13.012  80.978  7.282   1.00 25.39  ? 120  ILE A CG2 1 
ATOM   914   C  CD1 . ILE A 1 111 ? 14.253  81.751  10.187  1.00 26.20  ? 120  ILE A CD1 1 
ATOM   915   N  N   . ILE A 1 112 ? 13.421  82.559  4.359   1.00 26.81  ? 121  ILE A N   1 
ATOM   916   C  CA  . ILE A 1 112 ? 12.523  82.486  3.234   1.00 34.62  ? 121  ILE A CA  1 
ATOM   917   C  C   . ILE A 1 112 ? 11.906  81.085  3.110   1.00 41.30  ? 121  ILE A C   1 
ATOM   918   O  O   . ILE A 1 112 ? 12.400  80.120  3.699   1.00 35.82  ? 121  ILE A O   1 
ATOM   919   C  CB  . ILE A 1 112 ? 13.199  82.884  1.910   1.00 43.31  ? 121  ILE A CB  1 
ATOM   920   C  CG1 . ILE A 1 112 ? 14.351  81.976  1.584   1.00 47.35  ? 121  ILE A CG1 1 
ATOM   921   C  CG2 . ILE A 1 112 ? 13.664  84.363  1.990   1.00 48.59  ? 121  ILE A CG2 1 
ATOM   922   C  CD1 . ILE A 1 112 ? 15.170  82.550  0.416   1.00 51.51  ? 121  ILE A CD1 1 
ATOM   923   N  N   . SER A 1 113 ? 10.814  81.005  2.349   1.00 40.87  ? 122  SER A N   1 
ATOM   924   C  CA  . SER A 1 113 ? 10.096  79.759  2.138   1.00 49.61  ? 122  SER A CA  1 
ATOM   925   C  C   . SER A 1 113 ? 10.133  79.459  0.654   1.00 53.70  ? 122  SER A C   1 
ATOM   926   O  O   . SER A 1 113 ? 9.804   80.336  -0.123  1.00 54.72  ? 122  SER A O   1 
ATOM   927   C  CB  . SER A 1 113 ? 8.659   79.908  2.636   1.00 53.65  ? 122  SER A CB  1 
ATOM   928   O  OG  . SER A 1 113 ? 8.622   80.199  4.026   1.00 53.68  ? 122  SER A OG  1 
ATOM   929   N  N   . ASP A 1 114 ? 10.531  78.264  0.233   1.00 59.52  ? 123  ASP A N   1 
ATOM   930   C  CA  . ASP A 1 114 ? 10.582  78.050  -1.227  1.00 68.65  ? 123  ASP A CA  1 
ATOM   931   C  C   . ASP A 1 114 ? 10.453  76.610  -1.644  1.00 71.54  ? 123  ASP A C   1 
ATOM   932   O  O   . ASP A 1 114 ? 9.808   76.320  -2.660  1.00 71.92  ? 123  ASP A O   1 
ATOM   933   C  CB  . ASP A 1 114 ? 11.931  78.551  -1.847  1.00 70.33  ? 123  ASP A CB  1 
ATOM   934   C  CG  . ASP A 1 114 ? 12.382  79.929  -1.419  0.00 0.00   ? 123  ASP A CG  1 
ATOM   935   O  OD1 . ASP A 1 114 ? 11.942  80.918  -2.041  0.00 0.00   ? 123  ASP A OD1 1 
ATOM   936   O  OD2 . ASP A 1 114 ? 13.181  80.019  -0.472  0.00 0.00   ? 123  ASP A OD2 1 
ATOM   937   N  N   . ALA A 1 115 ? 11.073  75.708  -0.868  0.00 0.00   ? 124  ALA A N   1 
ATOM   938   C  CA  . ALA A 1 115 ? 11.123  74.288  -1.192  0.00 0.00   ? 124  ALA A CA  1 
ATOM   939   C  C   . ALA A 1 115 ? 11.945  74.188  -2.477  0.00 0.00   ? 124  ALA A C   1 
ATOM   940   O  O   . ALA A 1 115 ? 12.672  75.130  -2.794  0.00 0.00   ? 124  ALA A O   1 
ATOM   941   C  CB  . ALA A 1 115 ? 9.720   73.727  -1.397  0.00 0.00   ? 124  ALA A CB  1 
ATOM   942   N  N   . ASN A 1 116 ? 11.864  73.088  -3.211  0.00 0.00   ? 125  ASN A N   1 
ATOM   943   C  CA  . ASN A 1 116 ? 12.630  73.024  -4.452  0.00 0.00   ? 125  ASN A CA  1 
ATOM   944   C  C   . ASN A 1 116 ? 11.705  73.183  -5.651  0.00 0.00   ? 125  ASN A C   1 
ATOM   945   O  O   . ASN A 1 116 ? 12.180  73.365  -6.770  0.00 0.00   ? 125  ASN A O   1 
ATOM   946   C  CB  . ASN A 1 116 ? 13.399  71.708  -4.552  0.00 0.00   ? 125  ASN A CB  1 
ATOM   947   C  CG  . ASN A 1 116 ? 12.536  70.497  -4.322  0.00 0.00   ? 125  ASN A CG  1 
ATOM   948   O  OD1 . ASN A 1 116 ? 12.293  70.124  -3.169  0.00 0.00   ? 125  ASN A OD1 1 
ATOM   949   N  ND2 . ASN A 1 116 ? 12.026  69.834  -5.360  0.00 0.00   ? 125  ASN A ND2 1 
ATOM   950   N  N   . SER A 1 117 ? 10.386  73.125  -5.426  0.00 0.00   ? 126  SER A N   1 
ATOM   951   C  CA  . SER A 1 117 ? 9.434   73.259  -6.520  0.00 0.00   ? 126  SER A CA  1 
ATOM   952   C  C   . SER A 1 117 ? 8.018   73.544  -6.031  0.00 0.00   ? 126  SER A C   1 
ATOM   953   O  O   . SER A 1 117 ? 7.254   72.612  -5.787  0.00 0.00   ? 126  SER A O   1 
ATOM   954   C  CB  . SER A 1 117 ? 9.420   71.983  -7.356  0.00 0.00   ? 126  SER A CB  1 
ATOM   955   O  OG  . SER A 1 117 ? 9.624   72.276  -8.728  0.00 0.00   ? 126  SER A OG  1 
ATOM   956   N  N   . THR A 1 118 ? 7.660   74.824  -5.883  0.00 0.00   ? 127  THR A N   1 
ATOM   957   C  CA  . THR A 1 118 ? 6.306   75.170  -5.463  0.00 0.00   ? 127  THR A CA  1 
ATOM   958   C  C   . THR A 1 118 ? 5.449   75.357  -6.722  0.00 0.00   ? 127  THR A C   1 
ATOM   959   O  O   . THR A 1 118 ? 4.759   76.364  -6.873  0.00 0.00   ? 127  THR A O   1 
ATOM   960   C  CB  . THR A 1 118 ? 6.325   76.425  -4.569  0.00 0.00   ? 127  THR A CB  1 
ATOM   961   O  OG1 . THR A 1 118 ? 7.216   76.189  -3.476  0.00 0.00   ? 127  THR A OG1 1 
ATOM   962   C  CG2 . THR A 1 118 ? 4.944   76.756  -4.005  0.00 0.00   ? 127  THR A CG2 1 
ATOM   963   N  N   . LYS A 1 119 ? 5.516   74.382  -7.643  0.00 0.00   ? 128  LYS A N   1 
ATOM   964   C  CA  . LYS A 1 119 ? 4.722   74.422  -8.866  0.00 0.00   ? 128  LYS A CA  1 
ATOM   965   C  C   . LYS A 1 119 ? 3.285   74.183  -8.439  0.00 0.00   ? 128  LYS A C   1 
ATOM   966   O  O   . LYS A 1 119 ? 2.866   73.034  -8.301  0.00 0.00   ? 128  LYS A O   1 
ATOM   967   C  CB  . LYS A 1 119 ? 5.192   73.341  -9.849  0.00 0.00   ? 128  LYS A CB  1 
ATOM   968   C  CG  . LYS A 1 119 ? 6.586   73.613  -10.394 0.00 0.00   ? 128  LYS A CG  1 
ATOM   969   C  CD  . LYS A 1 119 ? 6.703   73.172  -11.841 0.00 0.00   ? 128  LYS A CD  1 
ATOM   970   C  CE  . LYS A 1 119 ? 8.043   72.531  -12.105 0.00 0.00   ? 128  LYS A CE  1 
ATOM   971   N  NZ  . LYS A 1 119 ? 8.021   71.724  -13.353 0.00 0.00   ? 128  LYS A NZ  1 
ATOM   972   N  N   . ALA A 1 120 ? 2.538   75.275  -8.218  0.00 0.00   ? 129  ALA A N   1 
ATOM   973   C  CA  . ALA A 1 120 ? 1.165   75.223  -7.725  0.00 0.00   ? 129  ALA A CA  1 
ATOM   974   C  C   . ALA A 1 120 ? 1.241   74.763  -6.266  0.00 0.00   ? 129  ALA A C   1 
ATOM   975   O  O   . ALA A 1 120 ? 2.330   74.782  -5.691  0.00 0.00   ? 129  ALA A O   1 
ATOM   976   C  CB  . ALA A 1 120 ? 0.325   74.258  -8.554  0.00 0.00   ? 129  ALA A CB  1 
ATOM   977   N  N   . VAL A 1 121 ? 0.130   74.356  -5.654  0.00 0.00   ? 130  VAL A N   1 
ATOM   978   C  CA  . VAL A 1 121 ? 0.209   73.920  -4.261  0.00 0.00   ? 130  VAL A CA  1 
ATOM   979   C  C   . VAL A 1 121 ? -0.588  72.635  -4.068  0.00 0.00   ? 130  VAL A C   1 
ATOM   980   O  O   . VAL A 1 121 ? -1.750  72.562  -4.460  0.00 0.00   ? 130  VAL A O   1 
ATOM   981   C  CB  . VAL A 1 121 ? -0.288  75.045  -3.318  0.00 0.00   ? 130  VAL A CB  1 
ATOM   982   C  CG1 . VAL A 1 121 ? -0.163  74.610  -1.863  0.00 0.00   ? 130  VAL A CG1 1 
ATOM   983   C  CG2 . VAL A 1 121 ? 0.517   76.322  -3.547  0.00 0.00   ? 130  VAL A CG2 1 
ATOM   984   N  N   . ASN A 1 122 ? 0.045   71.618  -3.467  0.00 0.00   ? 131  ASN A N   1 
ATOM   985   C  CA  . ASN A 1 122 ? -0.595  70.322  -3.233  0.00 0.00   ? 131  ASN A CA  1 
ATOM   986   C  C   . ASN A 1 122 ? -0.826  70.046  -1.746  0.00 0.00   ? 131  ASN A C   1 
ATOM   987   O  O   . ASN A 1 122 ? -1.756  69.327  -1.391  0.00 0.00   ? 131  ASN A O   1 
ATOM   988   C  CB  . ASN A 1 122 ? 0.265   69.194  -3.825  0.00 0.00   ? 131  ASN A CB  1 
ATOM   989   C  CG  . ASN A 1 122 ? 1.754   69.456  -3.772  0.00 0.00   ? 131  ASN A CG  1 
ATOM   990   O  OD1 . ASN A 1 122 ? 2.464   69.163  -4.742  0.00 0.00   ? 131  ASN A OD1 1 
ATOM   991   N  ND2 . ASN A 1 122 ? 2.322   69.962  -2.679  0.00 0.00   ? 131  ASN A ND2 1 
ATOM   992   N  N   . GLU A 1 123 ? 0.016   70.616  -0.882  0.00 0.00   ? 132  GLU A N   1 
ATOM   993   C  CA  . GLU A 1 123 ? -0.081  70.432  0.565   0.00 0.00   ? 132  GLU A CA  1 
ATOM   994   C  C   . GLU A 1 123 ? 0.384   71.712  1.238   0.00 0.00   ? 132  GLU A C   1 
ATOM   995   O  O   . GLU A 1 123 ? 0.847   72.613  0.540   0.00 0.00   ? 132  GLU A O   1 
ATOM   996   C  CB  . GLU A 1 123 ? 0.796   69.253  1.011   0.00 0.00   ? 132  GLU A CB  1 
ATOM   997   C  CG  . GLU A 1 123 ? 0.129   68.376  2.053   0.00 0.00   ? 132  GLU A CG  1 
ATOM   998   C  CD  . GLU A 1 123 ? 1.105   67.407  2.688   0.00 0.00   ? 132  GLU A CD  1 
ATOM   999   O  OE1 . GLU A 1 123 ? 0.986   66.187  2.436   0.00 0.00   ? 132  GLU A OE1 1 
ATOM   1000  O  OE2 . GLU A 1 123 ? 1.992   67.873  3.434   0.00 0.00   ? 132  GLU A OE2 1 
ATOM   1001  N  N   . TYR A 1 124 ? 0.285   71.822  2.566   1.00 114.24 ? 133  TYR A N   1 
ATOM   1002  C  CA  . TYR A 1 124 ? 0.740   73.073  3.155   1.00 113.48 ? 133  TYR A CA  1 
ATOM   1003  C  C   . TYR A 1 124 ? 1.829   72.926  4.203   1.00 113.51 ? 133  TYR A C   1 
ATOM   1004  O  O   . TYR A 1 124 ? 1.536   72.856  5.386   1.00 114.51 ? 133  TYR A O   1 
ATOM   1005  C  CB  . TYR A 1 124 ? -0.419  73.884  3.763   1.00 112.35 ? 133  TYR A CB  1 
ATOM   1006  C  CG  . TYR A 1 124 ? -1.703  73.143  4.058   0.00 0.00   ? 133  TYR A CG  1 
ATOM   1007  C  CD1 . TYR A 1 124 ? -2.788  73.220  3.195   0.00 0.00   ? 133  TYR A CD1 1 
ATOM   1008  C  CD2 . TYR A 1 124 ? -1.858  72.424  5.234   0.00 0.00   ? 133  TYR A CD2 1 
ATOM   1009  C  CE1 . TYR A 1 124 ? -3.996  72.606  3.500   0.00 0.00   ? 133  TYR A CE1 1 
ATOM   1010  C  CE2 . TYR A 1 124 ? -3.061  71.808  5.549   0.00 0.00   ? 133  TYR A CE2 1 
ATOM   1011  C  CZ  . TYR A 1 124 ? -4.130  71.904  4.682   0.00 0.00   ? 133  TYR A CZ  1 
ATOM   1012  O  OH  . TYR A 1 124 ? -5.330  71.331  5.025   0.00 0.00   ? 133  TYR A OH  1 
ATOM   1013  N  N   . MET A 1 125 ? 3.085   72.883  3.763   1.00 112.50 ? 134  MET A N   1 
ATOM   1014  C  CA  . MET A 1 125 ? 4.266   72.818  4.627   1.00 109.33 ? 134  MET A CA  1 
ATOM   1015  C  C   . MET A 1 125 ? 5.434   73.277  3.751   1.00 107.29 ? 134  MET A C   1 
ATOM   1016  O  O   . MET A 1 125 ? 5.939   72.497  2.946   1.00 107.03 ? 134  MET A O   1 
ATOM   1017  C  CB  . MET A 1 125 ? 4.486   71.393  5.186   1.00 107.70 ? 134  MET A CB  1 
ATOM   1018  C  CG  . MET A 1 125 ? 5.355   71.384  6.426   0.00 0.00   ? 134  MET A CG  1 
ATOM   1019  S  SD  . MET A 1 125 ? 5.270   69.832  7.355   0.00 0.00   ? 134  MET A SD  1 
ATOM   1020  C  CE  . MET A 1 125 ? 6.721   70.039  8.394   0.00 0.00   ? 134  MET A CE  1 
ATOM   1021  N  N   . ARG A 1 126 ? 5.849   74.544  3.882   1.00 103.72 ? 135  ARG A N   1 
ATOM   1022  C  CA  . ARG A 1 126 ? 6.936   75.040  3.040   1.00 96.81  ? 135  ARG A CA  1 
ATOM   1023  C  C   . ARG A 1 126 ? 8.314   74.822  3.686   1.00 89.91  ? 135  ARG A C   1 
ATOM   1024  O  O   . ARG A 1 126 ? 8.442   74.940  4.907   1.00 86.98  ? 135  ARG A O   1 
ATOM   1025  C  CB  . ARG A 1 126 ? 6.720   76.534  2.737   1.00 92.71  ? 135  ARG A CB  1 
ATOM   1026  C  CG  . ARG A 1 126 ? 6.094   76.754  1.364   1.00 92.25  ? 135  ARG A CG  1 
ATOM   1027  C  CD  . ARG A 1 126 ? 6.490   78.093  0.747   0.00 0.00   ? 135  ARG A CD  1 
ATOM   1028  N  NE  . ARG A 1 126 ? 5.364   79.022  0.765   0.00 0.00   ? 135  ARG A NE  1 
ATOM   1029  C  CZ  . ARG A 1 126 ? 5.468   80.339  0.638   0.00 0.00   ? 135  ARG A CZ  1 
ATOM   1030  N  NH1 . ARG A 1 126 ? 4.384   81.103  0.683   0.00 0.00   ? 135  ARG A NH1 1 
ATOM   1031  N  NH2 . ARG A 1 126 ? 6.656   80.904  0.464   0.00 0.00   ? 135  ARG A NH2 1 
ATOM   1032  N  N   . LYS A 1 127 ? 9.332   74.473  2.872   1.00 81.02  ? 136  LYS A N   1 
ATOM   1033  C  CA  . LYS A 1 127 ? 10.683  74.298  3.384   1.00 69.03  ? 136  LYS A CA  1 
ATOM   1034  C  C   . LYS A 1 127 ? 11.265  75.715  3.589   1.00 58.60  ? 136  LYS A C   1 
ATOM   1035  O  O   . LYS A 1 127 ? 11.190  76.541  2.693   1.00 55.13  ? 136  LYS A O   1 
ATOM   1036  C  CB  . LYS A 1 127 ? 11.539  73.505  2.385   1.00 66.50  ? 136  LYS A CB  1 
ATOM   1037  C  CG  . LYS A 1 127 ? 11.206  72.026  2.363   1.00 69.60  ? 136  LYS A CG  1 
ATOM   1038  C  CD  . LYS A 1 127 ? 11.848  71.340  1.170   0.00 0.00   ? 136  LYS A CD  1 
ATOM   1039  C  CE  . LYS A 1 127 ? 10.973  70.225  0.657   0.00 0.00   ? 136  LYS A CE  1 
ATOM   1040  N  NZ  . LYS A 1 127 ? 11.728  69.295  -0.217  0.00 0.00   ? 136  LYS A NZ  1 
ATOM   1041  N  N   . THR A 1 128 ? 11.810  75.990  4.745   1.00 50.66  ? 137  THR A N   1 
ATOM   1042  C  CA  . THR A 1 128 ? 12.351  77.317  5.003   1.00 41.47  ? 137  THR A CA  1 
ATOM   1043  C  C   . THR A 1 128 ? 13.859  77.329  4.934   1.00 38.77  ? 137  THR A C   1 
ATOM   1044  O  O   . THR A 1 128 ? 14.470  76.271  5.158   1.00 32.78  ? 137  THR A O   1 
ATOM   1045  C  CB  . THR A 1 128 ? 11.959  77.723  6.379   1.00 39.70  ? 137  THR A CB  1 
ATOM   1046  O  OG1 . THR A 1 128 ? 12.468  76.757  7.291   1.00 41.19  ? 137  THR A OG1 1 
ATOM   1047  C  CG2 . THR A 1 128 ? 10.443  77.882  6.516   1.00 41.12  ? 137  THR A CG2 1 
ATOM   1048  N  N   . SER A 1 129 ? 14.472  78.491  4.655   1.00 29.74  ? 138  SER A N   1 
ATOM   1049  C  CA  . SER A 1 129 ? 15.931  78.514  4.678   1.00 29.11  ? 138  SER A CA  1 
ATOM   1050  C  C   . SER A 1 129 ? 16.456  79.832  5.236   1.00 27.97  ? 138  SER A C   1 
ATOM   1051  O  O   . SER A 1 129 ? 15.823  80.883  5.060   1.00 24.70  ? 138  SER A O   1 
ATOM   1052  C  CB  . SER A 1 129 ? 16.491  78.286  3.289   1.00 29.80  ? 138  SER A CB  1 
ATOM   1053  O  OG  . SER A 1 129 ? 15.989  79.171  2.306   1.00 32.72  ? 138  SER A OG  1 
ATOM   1054  N  N   . ALA A 1 130 ? 17.605  79.756  5.957   1.00 26.66  ? 139  ALA A N   1 
ATOM   1055  C  CA  . ALA A 1 130 ? 18.265  80.958  6.491   1.00 23.72  ? 139  ALA A CA  1 
ATOM   1056  C  C   . ALA A 1 130 ? 18.652  81.804  5.334   1.00 22.95  ? 139  ALA A C   1 
ATOM   1057  O  O   . ALA A 1 130 ? 18.995  81.288  4.266   1.00 23.93  ? 139  ALA A O   1 
ATOM   1058  C  CB  . ALA A 1 130 ? 19.505  80.540  7.295   1.00 23.38  ? 139  ALA A CB  1 
ATOM   1059  N  N   . PRO A 1 131 ? 18.594  83.150  5.438   1.00 21.59  ? 140  PRO A N   1 
ATOM   1060  C  CA  . PRO A 1 131 ? 18.984  83.958  4.273   1.00 20.51  ? 140  PRO A CA  1 
ATOM   1061  C  C   . PRO A 1 131 ? 20.482  83.755  3.883   1.00 23.04  ? 140  PRO A C   1 
ATOM   1062  O  O   . PRO A 1 131 ? 21.329  83.600  4.770   1.00 24.67  ? 140  PRO A O   1 
ATOM   1063  C  CB  . PRO A 1 131 ? 18.716  85.415  4.753   1.00 21.79  ? 140  PRO A CB  1 
ATOM   1064  C  CG  . PRO A 1 131 ? 18.804  85.319  6.305   1.00 23.22  ? 140  PRO A CG  1 
ATOM   1065  C  CD  . PRO A 1 131 ? 18.130  83.975  6.565   1.00 22.68  ? 140  PRO A CD  1 
ATOM   1066  N  N   . VAL A 1 132 ? 20.779  83.783  2.593   1.00 22.93  ? 141  VAL A N   1 
ATOM   1067  C  CA  . VAL A 1 132 ? 22.137  83.576  2.113   1.00 26.14  ? 141  VAL A CA  1 
ATOM   1068  C  C   . VAL A 1 132 ? 22.688  84.865  1.570   1.00 27.41  ? 141  VAL A C   1 
ATOM   1069  O  O   . VAL A 1 132 ? 22.045  85.523  0.732   1.00 24.32  ? 141  VAL A O   1 
ATOM   1070  C  CB  . VAL A 1 132 ? 22.058  82.493  1.008   1.00 22.21  ? 141  VAL A CB  1 
ATOM   1071  C  CG1 . VAL A 1 132 ? 23.363  82.337  0.235   1.00 21.56  ? 141  VAL A CG1 1 
ATOM   1072  C  CG2 . VAL A 1 132 ? 21.653  81.155  1.626   1.00 19.77  ? 141  VAL A CG2 1 
ATOM   1073  N  N   . LYS A 1 133 ? 23.896  85.241  2.022   1.00 23.36  ? 142  LYS A N   1 
ATOM   1074  C  CA  . LYS A 1 133 ? 24.561  86.425  1.462   1.00 24.83  ? 142  LYS A CA  1 
ATOM   1075  C  C   . LYS A 1 133 ? 25.734  85.890  0.634   1.00 24.58  ? 142  LYS A C   1 
ATOM   1076  O  O   . LYS A 1 133 ? 26.631  85.262  1.191   1.00 23.50  ? 142  LYS A O   1 
ATOM   1077  C  CB  . LYS A 1 133 ? 25.011  87.331  2.626   1.00 27.82  ? 142  LYS A CB  1 
ATOM   1078  C  CG  . LYS A 1 133 ? 25.922  88.461  2.112   1.00 29.04  ? 142  LYS A CG  1 
ATOM   1079  C  CD  . LYS A 1 133 ? 25.091  89.594  1.543   1.00 31.02  ? 142  LYS A CD  1 
ATOM   1080  C  CE  . LYS A 1 133 ? 25.992  90.707  0.999   1.00 34.94  ? 142  LYS A CE  1 
ATOM   1081  N  NZ  . LYS A 1 133 ? 25.190  91.669  0.218   1.00 40.51  ? 142  LYS A NZ  1 
ATOM   1082  N  N   . LYS A 1 134 ? 25.762  86.101  -0.665  1.00 22.81  ? 143  LYS A N   1 
ATOM   1083  C  CA  . LYS A 1 134 ? 26.849  85.564  -1.473  1.00 23.20  ? 143  LYS A CA  1 
ATOM   1084  C  C   . LYS A 1 134 ? 27.993  86.600  -1.647  1.00 25.92  ? 143  LYS A C   1 
ATOM   1085  O  O   . LYS A 1 134 ? 27.731  87.727  -2.030  1.00 24.06  ? 143  LYS A O   1 
ATOM   1086  C  CB  . LYS A 1 134 ? 26.310  85.154  -2.847  1.00 26.45  ? 143  LYS A CB  1 
ATOM   1087  C  CG  . LYS A 1 134 ? 27.376  84.502  -3.691  1.00 28.26  ? 143  LYS A CG  1 
ATOM   1088  C  CD  . LYS A 1 134 ? 26.794  83.897  -4.935  1.00 32.74  ? 143  LYS A CD  1 
ATOM   1089  C  CE  . LYS A 1 134 ? 27.868  83.115  -5.646  1.00 32.46  ? 143  LYS A CE  1 
ATOM   1090  N  NZ  . LYS A 1 134 ? 27.499  82.893  -7.059  1.00 42.34  ? 143  LYS A NZ  1 
ATOM   1091  N  N   . LEU A 1 135 ? 29.232  86.216  -1.343  1.00 24.83  ? 144  LEU A N   1 
ATOM   1092  C  CA  . LEU A 1 135 ? 30.414  87.112  -1.444  1.00 21.17  ? 144  LEU A CA  1 
ATOM   1093  C  C   . LEU A 1 135 ? 31.315  86.455  -2.427  1.00 21.72  ? 144  LEU A C   1 
ATOM   1094  O  O   . LEU A 1 135 ? 32.070  85.530  -2.081  1.00 21.92  ? 144  LEU A O   1 
ATOM   1095  C  CB  . LEU A 1 135 ? 31.116  87.240  -0.037  1.00 19.91  ? 144  LEU A CB  1 
ATOM   1096  C  CG  . LEU A 1 135 ? 30.169  87.760  1.048   1.00 18.99  ? 144  LEU A CG  1 
ATOM   1097  C  CD1 . LEU A 1 135 ? 30.917  87.797  2.490   1.00 16.94  ? 144  LEU A CD1 1 
ATOM   1098  C  CD2 . LEU A 1 135 ? 29.647  89.234  0.671   1.00 19.07  ? 144  LEU A CD2 1 
ATOM   1099  N  N   . ALA A 1 136 ? 31.269  86.900  -3.676  1.00 21.48  ? 145  ALA A N   1 
ATOM   1100  C  CA  . ALA A 1 136 ? 32.061  86.198  -4.663  1.00 23.35  ? 145  ALA A CA  1 
ATOM   1101  C  C   . ALA A 1 136 ? 32.262  86.996  -5.911  1.00 22.94  ? 145  ALA A C   1 
ATOM   1102  O  O   . ALA A 1 136 ? 31.406  87.829  -6.224  1.00 25.38  ? 145  ALA A O   1 
ATOM   1103  C  CB  . ALA A 1 136 ? 31.294  84.931  -5.064  1.00 26.74  ? 145  ALA A CB  1 
ATOM   1104  N  N   . GLY A 1 137 ? 33.351  86.724  -6.631  1.00 23.15  ? 146  GLY A N   1 
ATOM   1105  C  CA  . GLY A 1 137 ? 33.595  87.338  -7.934  1.00 26.90  ? 146  GLY A CA  1 
ATOM   1106  C  C   . GLY A 1 137 ? 34.095  86.265  -8.911  1.00 31.69  ? 146  GLY A C   1 
ATOM   1107  O  O   . GLY A 1 137 ? 34.040  85.070  -8.589  1.00 32.10  ? 146  GLY A O   1 
ATOM   1108  N  N   . ALA A 1 138 ? 34.601  86.667  -10.085 1.00 34.40  ? 147  ALA A N   1 
ATOM   1109  C  CA  . ALA A 1 138 ? 35.085  85.759  -11.137 1.00 38.02  ? 147  ALA A CA  1 
ATOM   1110  C  C   . ALA A 1 138 ? 36.236  84.893  -10.696 1.00 39.63  ? 147  ALA A C   1 
ATOM   1111  O  O   . ALA A 1 138 ? 36.282  83.727  -11.054 1.00 39.79  ? 147  ALA A O   1 
ATOM   1112  C  CB  . ALA A 1 138 ? 35.511  86.572  -12.352 1.00 36.90  ? 147  ALA A CB  1 
ATOM   1113  N  N   . THR A 1 139 ? 37.187  85.444  -9.933  1.00 38.03  ? 148  THR A N   1 
ATOM   1114  C  CA  . THR A 1 139 ? 38.307  84.668  -9.433  1.00 38.03  ? 148  THR A CA  1 
ATOM   1115  C  C   . THR A 1 139 ? 38.479  84.920  -7.935  1.00 35.76  ? 148  THR A C   1 
ATOM   1116  O  O   . THR A 1 139 ? 37.765  85.749  -7.343  1.00 33.04  ? 148  THR A O   1 
ATOM   1117  C  CB  . THR A 1 139 ? 39.609  85.041  -10.166 1.00 40.35  ? 148  THR A CB  1 
ATOM   1118  O  OG1 . THR A 1 139 ? 40.119  86.259  -9.623  1.00 41.78  ? 148  THR A OG1 1 
ATOM   1119  C  CG2 . THR A 1 139 ? 39.387  85.276  -11.688 1.00 43.55  ? 148  THR A CG2 1 
ATOM   1120  N  N   . ARG A 1 140 ? 39.427  84.216  -7.355  1.00 32.40  ? 149  ARG A N   1 
ATOM   1121  C  CA  . ARG A 1 140 ? 39.741  84.343  -5.964  1.00 28.94  ? 149  ARG A CA  1 
ATOM   1122  C  C   . ARG A 1 140 ? 40.055  85.845  -5.619  1.00 27.37  ? 149  ARG A C   1 
ATOM   1123  O  O   . ARG A 1 140 ? 39.734  86.277  -4.509  1.00 24.36  ? 149  ARG A O   1 
ATOM   1124  C  CB  . ARG A 1 140 ? 40.955  83.476  -5.643  1.00 25.40  ? 149  ARG A CB  1 
ATOM   1125  C  CG  . ARG A 1 140 ? 42.194  83.822  -6.477  1.00 27.91  ? 149  ARG A CG  1 
ATOM   1126  C  CD  . ARG A 1 140 ? 43.314  82.707  -6.341  1.00 32.26  ? 149  ARG A CD  1 
ATOM   1127  N  NE  . ARG A 1 140 ? 42.750  81.423  -6.788  1.00 31.78  ? 149  ARG A NE  1 
ATOM   1128  C  CZ  . ARG A 1 140 ? 43.222  80.219  -6.484  1.00 38.05  ? 149  ARG A CZ  1 
ATOM   1129  N  NH1 . ARG A 1 140 ? 44.330  80.090  -5.765  1.00 33.60  ? 149  ARG A NH1 1 
ATOM   1130  N  NH2 . ARG A 1 140 ? 42.564  79.135  -6.861  1.00 33.60  ? 149  ARG A NH2 1 
ATOM   1131  N  N   . PHE A 1 141 ? 40.688  86.587  -6.532  1.00 25.52  ? 150  PHE A N   1 
ATOM   1132  C  CA  . PHE A 1 141 ? 41.025  88.008  -6.273  1.00 25.10  ? 150  PHE A CA  1 
ATOM   1133  C  C   . PHE A 1 141 ? 39.744  88.821  -6.092  1.00 25.30  ? 150  PHE A C   1 
ATOM   1134  O  O   . PHE A 1 141 ? 39.685  89.601  -5.160  1.00 24.06  ? 150  PHE A O   1 
ATOM   1135  C  CB  . PHE A 1 141 ? 41.835  88.615  -7.448  1.00 24.70  ? 150  PHE A CB  1 
ATOM   1136  C  CG  . PHE A 1 141 ? 43.153  87.937  -7.583  1.00 26.72  ? 150  PHE A CG  1 
ATOM   1137  C  CD1 . PHE A 1 141 ? 44.248  88.362  -6.847  1.00 29.35  ? 150  PHE A CD1 1 
ATOM   1138  C  CD2 . PHE A 1 141 ? 43.299  86.817  -8.410  1.00 32.64  ? 150  PHE A CD2 1 
ATOM   1139  C  CE1 . PHE A 1 141 ? 45.474  87.686  -6.919  1.00 31.94  ? 150  PHE A CE1 1 
ATOM   1140  C  CE2 . PHE A 1 141 ? 44.525  86.144  -8.482  1.00 26.76  ? 150  PHE A CE2 1 
ATOM   1141  C  CZ  . PHE A 1 141 ? 45.603  86.580  -7.735  1.00 33.74  ? 150  PHE A CZ  1 
ATOM   1142  N  N   . GLU A 1 142 ? 38.724  88.648  -7.002  1.00 22.12  ? 151  GLU A N   1 
ATOM   1143  C  CA  . GLU A 1 142 ? 37.498  89.415  -6.855  1.00 25.29  ? 151  GLU A CA  1 
ATOM   1144  C  C   . GLU A 1 142 ? 36.704  88.927  -5.687  1.00 23.01  ? 151  GLU A C   1 
ATOM   1145  O  O   . GLU A 1 142 ? 35.981  89.728  -5.086  1.00 23.68  ? 151  GLU A O   1 
ATOM   1146  C  CB  . GLU A 1 142 ? 36.592  89.362  -8.105  1.00 27.19  ? 151  GLU A CB  1 
ATOM   1147  C  CG  . GLU A 1 142 ? 37.196  90.037  -9.325  1.00 35.33  ? 151  GLU A CG  1 
ATOM   1148  C  CD  . GLU A 1 142 ? 38.195  89.150  -10.048 1.00 49.13  ? 151  GLU A CD  1 
ATOM   1149  O  OE1 . GLU A 1 142 ? 38.199  87.918  -9.846  1.00 49.96  ? 151  GLU A OE1 1 
ATOM   1150  O  OE2 . GLU A 1 142 ? 38.998  89.695  -10.814 1.00 52.02  ? 151  GLU A OE2 1 
ATOM   1151  N  N   . THR A 1 143 ? 36.787  87.623  -5.358  1.00 19.90  ? 152  THR A N   1 
ATOM   1152  C  CA  . THR A 1 143 ? 36.048  87.149  -4.194  1.00 17.79  ? 152  THR A CA  1 
ATOM   1153  C  C   . THR A 1 143 ? 36.643  87.821  -2.912  1.00 20.25  ? 152  THR A C   1 
ATOM   1154  O  O   . THR A 1 143 ? 35.850  88.222  -2.052  1.00 19.17  ? 152  THR A O   1 
ATOM   1155  C  CB  . THR A 1 143 ? 36.116  85.608  -4.096  1.00 23.29  ? 152  THR A CB  1 
ATOM   1156  O  OG1 . THR A 1 143 ? 35.224  85.120  -5.068  1.00 23.66  ? 152  THR A OG1 1 
ATOM   1157  C  CG2 . THR A 1 143 ? 35.639  85.058  -2.717  1.00 19.29  ? 152  THR A CG2 1 
ATOM   1158  N  N   . ALA A 1 144 ? 37.985  87.938  -2.811  1.00 19.72  ? 153  ALA A N   1 
ATOM   1159  C  CA  . ALA A 1 144 ? 38.578  88.582  -1.628  1.00 19.89  ? 153  ALA A CA  1 
ATOM   1160  C  C   . ALA A 1 144 ? 38.068  90.064  -1.543  1.00 21.28  ? 153  ALA A C   1 
ATOM   1161  O  O   . ALA A 1 144 ? 37.810  90.582  -0.451  1.00 18.00  ? 153  ALA A O   1 
ATOM   1162  C  CB  . ALA A 1 144 ? 40.089  88.553  -1.704  1.00 18.37  ? 153  ALA A CB  1 
ATOM   1163  N  N   . VAL A 1 145 ? 37.884  90.704  -2.680  1.00 19.79  ? 154  VAL A N   1 
ATOM   1164  C  CA  . VAL A 1 145 ? 37.373  92.088  -2.660  1.00 18.89  ? 154  VAL A CA  1 
ATOM   1165  C  C   . VAL A 1 145 ? 35.946  92.122  -2.148  1.00 20.13  ? 154  VAL A C   1 
ATOM   1166  O  O   . VAL A 1 145 ? 35.580  93.037  -1.386  1.00 18.47  ? 154  VAL A O   1 
ATOM   1167  C  CB  . VAL A 1 145 ? 37.488  92.696  -4.089  1.00 19.93  ? 154  VAL A CB  1 
ATOM   1168  C  CG1 . VAL A 1 145 ? 36.727  94.061  -4.171  1.00 21.59  ? 154  VAL A CG1 1 
ATOM   1169  C  CG2 . VAL A 1 145 ? 38.990  92.928  -4.424  1.00 19.27  ? 154  VAL A CG2 1 
ATOM   1170  N  N   . GLU A 1 146 ? 35.078  91.141  -2.538  1.00 19.50  ? 155  GLU A N   1 
ATOM   1171  C  CA  . GLU A 1 146 ? 33.714  91.229  -2.036  1.00 18.17  ? 155  GLU A CA  1 
ATOM   1172  C  C   . GLU A 1 146 ? 33.672  91.010  -0.535  1.00 16.75  ? 155  GLU A C   1 
ATOM   1173  O  O   . GLU A 1 146 ? 32.799  91.546  0.131   1.00 17.29  ? 155  GLU A O   1 
ATOM   1174  C  CB  . GLU A 1 146 ? 32.796  90.218  -2.727  1.00 21.38  ? 155  GLU A CB  1 
ATOM   1175  C  CG  . GLU A 1 146 ? 32.657  90.529  -4.227  1.00 24.94  ? 155  GLU A CG  1 
ATOM   1176  C  CD  . GLU A 1 146 ? 32.077  91.963  -4.442  1.00 33.21  ? 155  GLU A CD  1 
ATOM   1177  O  OE1 . GLU A 1 146 ? 32.714  92.781  -5.141  1.00 39.20  ? 155  GLU A OE1 1 
ATOM   1178  O  OE2 . GLU A 1 146 ? 31.021  92.259  -3.877  1.00 35.07  ? 155  GLU A OE2 1 
ATOM   1179  N  N   . ILE A 1 147 ? 34.611  90.208  -0.004  1.00 15.82  ? 156  ILE A N   1 
ATOM   1180  C  CA  . ILE A 1 147 ? 34.660  89.953  1.441   1.00 15.54  ? 156  ILE A CA  1 
ATOM   1181  C  C   . ILE A 1 147 ? 35.081  91.258  2.170   1.00 15.61  ? 156  ILE A C   1 
ATOM   1182  O  O   . ILE A 1 147 ? 34.539  91.617  3.214   1.00 17.34  ? 156  ILE A O   1 
ATOM   1183  C  CB  . ILE A 1 147 ? 35.652  88.798  1.687   1.00 16.54  ? 156  ILE A CB  1 
ATOM   1184  C  CG1 . ILE A 1 147 ? 35.017  87.430  1.233   1.00 17.50  ? 156  ILE A CG1 1 
ATOM   1185  C  CG2 . ILE A 1 147 ? 35.951  88.697  3.218   1.00 16.81  ? 156  ILE A CG2 1 
ATOM   1186  C  CD1 . ILE A 1 147 ? 36.108  86.298  1.150   1.00 16.68  ? 156  ILE A CD1 1 
ATOM   1187  N  N   . SER A 1 148 ? 36.070  91.900  1.621   1.00 17.41  ? 157  SER A N   1 
ATOM   1188  C  CA  . SER A 1 148 ? 36.613  93.167  2.125   1.00 12.76  ? 157  SER A CA  1 
ATOM   1189  C  C   . SER A 1 148 ? 35.478  94.244  2.190   1.00 15.26  ? 157  SER A C   1 
ATOM   1190  O  O   . SER A 1 148 ? 35.283  94.916  3.208   1.00 16.57  ? 157  SER A O   1 
ATOM   1191  C  CB  . SER A 1 148 ? 37.756  93.603  1.160   1.00 15.85  ? 157  SER A CB  1 
ATOM   1192  O  OG  . SER A 1 148 ? 38.223  94.865  1.628   1.00 18.72  ? 157  SER A OG  1 
ATOM   1193  N  N   . LYS A 1 149 ? 34.683  94.355  1.125   1.00 15.87  ? 158  LYS A N   1 
ATOM   1194  C  CA  . LYS A 1 149 ? 33.553  95.334  1.095   1.00 19.30  ? 158  LYS A CA  1 
ATOM   1195  C  C   . LYS A 1 149 ? 32.522  95.001  2.079   1.00 20.16  ? 158  LYS A C   1 
ATOM   1196  O  O   . LYS A 1 149 ? 31.857  95.883  2.616   1.00 20.10  ? 158  LYS A O   1 
ATOM   1197  C  CB  . LYS A 1 149 ? 32.926  95.345  -0.296  1.00 19.89  ? 158  LYS A CB  1 
ATOM   1198  C  CG  . LYS A 1 149 ? 33.825  96.069  -1.249  1.00 21.81  ? 158  LYS A CG  1 
ATOM   1199  C  CD  . LYS A 1 149 ? 33.288  95.986  -2.693  1.00 35.64  ? 158  LYS A CD  1 
ATOM   1200  C  CE  . LYS A 1 149 ? 34.239  96.800  -3.558  1.00 50.67  ? 158  LYS A CE  1 
ATOM   1201  N  NZ  . LYS A 1 149 ? 33.897  96.776  -5.027  1.00 60.63  ? 158  LYS A NZ  1 
ATOM   1202  N  N   . GLN A 1 150 ? 32.337  93.714  2.360   1.00 18.05  ? 159  GLN A N   1 
ATOM   1203  C  CA  . GLN A 1 150 ? 31.346  93.341  3.366   1.00 17.22  ? 159  GLN A CA  1 
ATOM   1204  C  C   . GLN A 1 150 ? 31.739  93.699  4.764   1.00 20.87  ? 159  GLN A C   1 
ATOM   1205  O  O   . GLN A 1 150 ? 30.910  94.248  5.512   1.00 19.58  ? 159  GLN A O   1 
ATOM   1206  C  CB  . GLN A 1 150 ? 31.098  91.795  3.308   1.00 18.77  ? 159  GLN A CB  1 
ATOM   1207  C  CG  . GLN A 1 150 ? 29.957  91.325  4.216   1.00 19.38  ? 159  GLN A CG  1 
ATOM   1208  C  CD  . GLN A 1 150 ? 28.605  91.888  3.760   1.00 20.74  ? 159  GLN A CD  1 
ATOM   1209  O  OE1 . GLN A 1 150 ? 28.420  92.247  2.579   1.00 21.23  ? 159  GLN A OE1 1 
ATOM   1210  N  NE2 . GLN A 1 150 ? 27.633  91.903  4.693   1.00 19.63  ? 159  GLN A NE2 1 
ATOM   1211  N  N   . GLY A 1 151 ? 32.985  93.411  5.201   1.00 18.53  ? 160  GLY A N   1 
ATOM   1212  C  CA  . GLY A 1 151 ? 33.263  93.692  6.610   1.00 16.71  ? 160  GLY A CA  1 
ATOM   1213  C  C   . GLY A 1 151 ? 33.988  95.023  6.847   1.00 17.57  ? 160  GLY A C   1 
ATOM   1214  O  O   . GLY A 1 151 ? 34.150  95.472  7.996   1.00 18.36  ? 160  GLY A O   1 
ATOM   1215  N  N   . TRP A 1 152 ? 34.433  95.662  5.739   1.00 16.53  ? 161  TRP A N   1 
ATOM   1216  C  CA  . TRP A 1 152 ? 35.247  96.926  5.850   1.00 17.64  ? 161  TRP A CA  1 
ATOM   1217  C  C   . TRP A 1 152 ? 34.717  97.922  4.835   1.00 17.53  ? 161  TRP A C   1 
ATOM   1218  O  O   . TRP A 1 152 ? 35.465  98.556  4.069   1.00 16.79  ? 161  TRP A O   1 
ATOM   1219  C  CB  . TRP A 1 152 ? 36.764  96.567  5.560   1.00 14.17  ? 161  TRP A CB  1 
ATOM   1220  C  CG  . TRP A 1 152 ? 37.296  95.689  6.633   1.00 17.11  ? 161  TRP A CG  1 
ATOM   1221  C  CD1 . TRP A 1 152 ? 37.967  96.082  7.768   1.00 17.44  ? 161  TRP A CD1 1 
ATOM   1222  C  CD2 . TRP A 1 152 ? 37.177  94.240  6.716   1.00 17.69  ? 161  TRP A CD2 1 
ATOM   1223  N  NE1 . TRP A 1 152 ? 38.290  94.968  8.537   1.00 18.77  ? 161  TRP A NE1 1 
ATOM   1224  C  CE2 . TRP A 1 152 ? 37.814  93.831  7.909   1.00 21.27  ? 161  TRP A CE2 1 
ATOM   1225  C  CE3 . TRP A 1 152 ? 36.587  93.265  5.903   1.00 17.04  ? 161  TRP A CE3 1 
ATOM   1226  C  CZ2 . TRP A 1 152 ? 37.895  92.472  8.296   1.00 19.27  ? 161  TRP A CZ2 1 
ATOM   1227  C  CZ3 . TRP A 1 152 ? 36.647  91.919  6.290   1.00 17.06  ? 161  TRP A CZ3 1 
ATOM   1228  C  CH2 . TRP A 1 152 ? 37.304  91.537  7.468   1.00 15.60  ? 161  TRP A CH2 1 
ATOM   1229  N  N   . LYS A 1 153 ? 33.392  98.120  4.840   1.00 16.29  ? 162  LYS A N   1 
ATOM   1230  C  CA  . LYS A 1 153 ? 32.802  99.041  3.856   1.00 16.94  ? 162  LYS A CA  1 
ATOM   1231  C  C   . LYS A 1 153 ? 33.318  100.467 4.113   1.00 18.97  ? 162  LYS A C   1 
ATOM   1232  O  O   . LYS A 1 153 ? 33.545  101.250 3.177   1.00 17.10  ? 162  LYS A O   1 
ATOM   1233  C  CB  . LYS A 1 153 ? 31.264  99.009  3.990   1.00 15.48  ? 162  LYS A CB  1 
ATOM   1234  C  CG  . LYS A 1 153 ? 30.607  99.939  2.964   1.00 21.89  ? 162  LYS A CG  1 
ATOM   1235  C  CD  . LYS A 1 153 ? 30.869  99.405  1.584   1.00 34.74  ? 162  LYS A CD  1 
ATOM   1236  C  CE  . LYS A 1 153 ? 30.288  100.307 0.524   1.00 50.11  ? 162  LYS A CE  1 
ATOM   1237  N  NZ  . LYS A 1 153 ? 28.815  100.178 0.440   0.00 0.00   ? 162  LYS A NZ  1 
ATOM   1238  N  N   . ASP A 1 154 ? 33.550  100.773 5.371   1.00 14.48  ? 163  ASP A N   1 
ATOM   1239  C  CA  . ASP A 1 154 ? 34.014  102.114 5.709   1.00 20.21  ? 163  ASP A CA  1 
ATOM   1240  C  C   . ASP A 1 154 ? 35.535  102.224 5.650   1.00 23.17  ? 163  ASP A C   1 
ATOM   1241  O  O   . ASP A 1 154 ? 36.092  103.244 6.099   1.00 20.13  ? 163  ASP A O   1 
ATOM   1242  C  CB  . ASP A 1 154 ? 33.547  102.486 7.145   1.00 23.28  ? 163  ASP A CB  1 
ATOM   1243  C  CG  . ASP A 1 154 ? 33.981  101.477 8.197   1.00 27.99  ? 163  ASP A CG  1 
ATOM   1244  O  OD1 . ASP A 1 154 ? 34.192  101.875 9.334   1.00 31.79  ? 163  ASP A OD1 1 
ATOM   1245  O  OD2 . ASP A 1 154 ? 34.122  100.294 7.864   1.00 29.21  ? 163  ASP A OD2 1 
ATOM   1246  N  N   . GLY A 1 155 ? 36.206  101.199 5.171   1.00 17.41  ? 164  GLY A N   1 
ATOM   1247  C  CA  . GLY A 1 155 ? 37.661  101.299 4.999   1.00 16.70  ? 164  GLY A CA  1 
ATOM   1248  C  C   . GLY A 1 155 ? 38.442  100.501 6.026   1.00 20.47  ? 164  GLY A C   1 
ATOM   1249  O  O   . GLY A 1 155 ? 37.872  99.898  6.933   1.00 18.41  ? 164  GLY A O   1 
ATOM   1250  N  N   . SER A 1 156 ? 39.779  100.507 5.905   1.00 17.66  ? 165  SER A N   1 
ATOM   1251  C  CA  . SER A 1 156 ? 40.601  99.771  6.879   1.00 17.09  ? 165  SER A CA  1 
ATOM   1252  C  C   . SER A 1 156 ? 41.979  100.421 6.931   1.00 19.51  ? 165  SER A C   1 
ATOM   1253  O  O   . SER A 1 156 ? 42.545  100.651 5.845   1.00 20.61  ? 165  SER A O   1 
ATOM   1254  C  CB  . SER A 1 156 ? 40.778  98.316  6.429   1.00 21.20  ? 165  SER A CB  1 
ATOM   1255  O  OG  . SER A 1 156 ? 41.387  97.625  7.521   1.00 20.51  ? 165  SER A OG  1 
ATOM   1256  N  N   . SER A 1 157 ? 42.548  100.669 8.130   1.00 18.30  ? 166  SER A N   1 
ATOM   1257  C  CA  . SER A 1 157 ? 43.878  101.319 8.091   1.00 18.44  ? 166  SER A CA  1 
ATOM   1258  C  C   . SER A 1 157 ? 44.968  100.317 7.722   1.00 19.40  ? 166  SER A C   1 
ATOM   1259  O  O   . SER A 1 157 ? 46.028  100.717 7.267   1.00 18.38  ? 166  SER A O   1 
ATOM   1260  C  CB  . SER A 1 157 ? 44.176  102.010 9.423   1.00 23.91  ? 166  SER A CB  1 
ATOM   1261  O  OG  . SER A 1 157 ? 44.232  101.004 10.411  1.00 33.43  ? 166  SER A OG  1 
ATOM   1262  N  N   . LYS A 1 158 ? 44.716  99.025  7.903   1.00 18.73  ? 167  LYS A N   1 
ATOM   1263  C  CA  . LYS A 1 158 ? 45.680  97.987  7.521   1.00 16.27  ? 167  LYS A CA  1 
ATOM   1264  C  C   . LYS A 1 158 ? 45.030  96.992  6.557   1.00 20.09  ? 167  LYS A C   1 
ATOM   1265  O  O   . LYS A 1 158 ? 43.801  96.770  6.619   1.00 18.67  ? 167  LYS A O   1 
ATOM   1266  C  CB  . LYS A 1 158 ? 46.145  97.170  8.727   1.00 17.34  ? 167  LYS A CB  1 
ATOM   1267  C  CG  . LYS A 1 158 ? 46.982  97.991  9.728   1.00 23.26  ? 167  LYS A CG  1 
ATOM   1268  C  CD  . LYS A 1 158 ? 47.334  97.107  10.987  1.00 26.03  ? 167  LYS A CD  1 
ATOM   1269  C  CE  . LYS A 1 158 ? 48.618  97.533  11.663  1.00 31.75  ? 167  LYS A CE  1 
ATOM   1270  N  NZ  . LYS A 1 158 ? 48.432  98.806  12.318  1.00 42.51  ? 167  LYS A NZ  1 
ATOM   1271  N  N   . VAL A 1 159 ? 45.818  96.428  5.669   1.00 17.78  ? 168  VAL A N   1 
ATOM   1272  C  CA  . VAL A 1 159 ? 45.395  95.375  4.757   1.00 16.28  ? 168  VAL A CA  1 
ATOM   1273  C  C   . VAL A 1 159 ? 46.498  94.334  4.782   1.00 20.65  ? 168  VAL A C   1 
ATOM   1274  O  O   . VAL A 1 159 ? 47.679  94.700  4.669   1.00 18.88  ? 168  VAL A O   1 
ATOM   1275  C  CB  . VAL A 1 159 ? 45.173  95.836  3.278   1.00 16.94  ? 168  VAL A CB  1 
ATOM   1276  C  CG1 . VAL A 1 159 ? 44.770  94.636  2.385   1.00 15.87  ? 168  VAL A CG1 1 
ATOM   1277  C  CG2 . VAL A 1 159 ? 44.073  96.930  3.215   1.00 18.43  ? 168  VAL A CG2 1 
ATOM   1278  N  N   . VAL A 1 160 ? 46.122  93.046  4.902   1.00 18.68  ? 169  VAL A N   1 
ATOM   1279  C  CA  . VAL A 1 160 ? 47.094  91.966  4.845   1.00 17.50  ? 169  VAL A CA  1 
ATOM   1280  C  C   . VAL A 1 160 ? 47.100  91.458  3.429   1.00 19.58  ? 169  VAL A C   1 
ATOM   1281  O  O   . VAL A 1 160 ? 46.052  91.292  2.799   1.00 21.05  ? 169  VAL A O   1 
ATOM   1282  C  CB  . VAL A 1 160 ? 46.734  90.863  5.848   1.00 18.19  ? 169  VAL A CB  1 
ATOM   1283  C  CG1 . VAL A 1 160 ? 47.668  89.600  5.661   1.00 18.27  ? 169  VAL A CG1 1 
ATOM   1284  C  CG2 . VAL A 1 160 ? 46.859  91.439  7.248   1.00 17.13  ? 169  VAL A CG2 1 
ATOM   1285  N  N   . ILE A 1 161 ? 48.288  91.170  2.904   1.00 18.78  ? 170  ILE A N   1 
ATOM   1286  C  CA  . ILE A 1 161 ? 48.333  90.666  1.532   1.00 17.12  ? 170  ILE A CA  1 
ATOM   1287  C  C   . ILE A 1 161 ? 49.071  89.309  1.536   1.00 22.41  ? 170  ILE A C   1 
ATOM   1288  O  O   . ILE A 1 161 ? 50.079  89.178  2.215   1.00 22.98  ? 170  ILE A O   1 
ATOM   1289  C  CB  . ILE A 1 161 ? 49.190  91.687  0.718   1.00 22.22  ? 170  ILE A CB  1 
ATOM   1290  C  CG1 . ILE A 1 161 ? 48.362  92.988  0.415   1.00 24.98  ? 170  ILE A CG1 1 
ATOM   1291  C  CG2 . ILE A 1 161 ? 49.615  90.991  -0.585  1.00 25.02  ? 170  ILE A CG2 1 
ATOM   1292  C  CD1 . ILE A 1 161 ? 47.434  92.810  -0.776  1.00 24.30  ? 170  ILE A CD1 1 
ATOM   1293  N  N   . VAL A 1 162 ? 48.562  88.376  0.805   1.00 21.33  ? 171  VAL A N   1 
ATOM   1294  C  CA  . VAL A 1 162 ? 49.131  87.015  0.685   1.00 23.02  ? 171  VAL A CA  1 
ATOM   1295  C  C   . VAL A 1 162 ? 49.149  86.770  -0.804  1.00 22.36  ? 171  VAL A C   1 
ATOM   1296  O  O   . VAL A 1 162 ? 48.334  87.314  -1.518  1.00 23.37  ? 171  VAL A O   1 
ATOM   1297  C  CB  . VAL A 1 162 ? 48.151  86.046  1.395   1.00 25.44  ? 171  VAL A CB  1 
ATOM   1298  C  CG1 . VAL A 1 162 ? 48.356  84.631  0.917   1.00 33.41  ? 171  VAL A CG1 1 
ATOM   1299  C  CG2 . VAL A 1 162 ? 48.336  86.185  2.935   1.00 28.44  ? 171  VAL A CG2 1 
ATOM   1300  N  N   . ASN A 1 163 ? 50.090  85.965  -1.268  1.00 24.31  ? 172  ASN A N   1 
ATOM   1301  C  CA  . ASN A 1 163 ? 50.123  85.574  -2.667  1.00 24.49  ? 172  ASN A CA  1 
ATOM   1302  C  C   . ASN A 1 163 ? 48.946  84.691  -2.931  1.00 28.66  ? 172  ASN A C   1 
ATOM   1303  O  O   . ASN A 1 163 ? 48.834  83.651  -2.255  1.00 32.63  ? 172  ASN A O   1 
ATOM   1304  C  CB  . ASN A 1 163 ? 51.416  84.788  -2.923  1.00 30.91  ? 172  ASN A CB  1 
ATOM   1305  C  CG  . ASN A 1 163 ? 51.536  84.302  -4.360  1.00 33.10  ? 172  ASN A CG  1 
ATOM   1306  O  OD1 . ASN A 1 163 ? 50.560  83.856  -4.973  1.00 31.48  ? 172  ASN A OD1 1 
ATOM   1307  N  ND2 . ASN A 1 163 ? 52.737  84.415  -4.985  1.00 32.73  ? 172  ASN A ND2 1 
ATOM   1308  N  N   . GLY A 1 164 ? 48.090  85.032  -3.908  1.00 28.60  ? 173  GLY A N   1 
ATOM   1309  C  CA  . GLY A 1 164 ? 46.859  84.288  -4.137  1.00 32.28  ? 173  GLY A CA  1 
ATOM   1310  C  C   . GLY A 1 164 ? 46.985  82.891  -4.712  1.00 38.51  ? 173  GLY A C   1 
ATOM   1311  O  O   . GLY A 1 164 ? 46.048  82.116  -4.581  1.00 37.68  ? 173  GLY A O   1 
ATOM   1312  N  N   . GLU A 1 165 ? 48.112  82.562  -5.369  1.00 43.64  ? 174  GLU A N   1 
ATOM   1313  C  CA  . GLU A 1 165 ? 48.274  81.206  -5.936  1.00 48.79  ? 174  GLU A CA  1 
ATOM   1314  C  C   . GLU A 1 165 ? 49.162  80.397  -5.006  1.00 48.26  ? 174  GLU A C   1 
ATOM   1315  O  O   . GLU A 1 165 ? 49.341  79.225  -5.244  1.00 50.43  ? 174  GLU A O   1 
ATOM   1316  C  CB  . GLU A 1 165 ? 48.846  81.264  -7.386  1.00 55.62  ? 174  GLU A CB  1 
ATOM   1317  C  CG  . GLU A 1 165 ? 48.150  82.293  -8.289  1.00 64.03  ? 174  GLU A CG  1 
ATOM   1318  C  CD  . GLU A 1 165 ? 46.707  81.929  -8.680  1.00 72.32  ? 174  GLU A CD  1 
ATOM   1319  O  OE1 . GLU A 1 165 ? 46.252  80.823  -8.314  1.00 76.35  ? 174  GLU A OE1 1 
ATOM   1320  O  OE2 . GLU A 1 165 ? 46.028  82.754  -9.358  1.00 69.33  ? 174  GLU A OE2 1 
ATOM   1321  N  N   . LEU A 1 166 ? 49.738  80.997  -3.960  1.00 44.73  ? 175  LEU A N   1 
ATOM   1322  C  CA  . LEU A 1 166 ? 50.494  80.258  -2.962  1.00 47.38  ? 175  LEU A CA  1 
ATOM   1323  C  C   . LEU A 1 166 ? 49.723  80.457  -1.675  1.00 50.98  ? 175  LEU A C   1 
ATOM   1324  O  O   . LEU A 1 166 ? 50.329  80.692  -0.610  1.00 52.05  ? 175  LEU A O   1 
ATOM   1325  C  CB  . LEU A 1 166 ? 51.919  80.723  -2.612  1.00 52.91  ? 175  LEU A CB  1 
ATOM   1326  C  CG  . LEU A 1 166 ? 52.965  80.743  -3.689  1.00 56.43  ? 175  LEU A CG  1 
ATOM   1327  C  CD1 . LEU A 1 166 ? 54.043  81.674  -3.118  1.00 56.21  ? 175  LEU A CD1 1 
ATOM   1328  C  CD2 . LEU A 1 166 ? 53.538  79.336  -3.981  1.00 56.86  ? 175  LEU A CD2 1 
ATOM   1329  N  N   . ALA A 1 167 ? 48.415  80.378  -1.736  1.00 50.05  ? 176  ALA A N   1 
ATOM   1330  C  CA  . ALA A 1 167 ? 47.633  80.659  -0.548  1.00 53.02  ? 176  ALA A CA  1 
ATOM   1331  C  C   . ALA A 1 167 ? 48.008  79.803  0.678   1.00 56.67  ? 176  ALA A C   1 
ATOM   1332  O  O   . ALA A 1 167 ? 47.853  80.285  1.798   1.00 57.67  ? 176  ALA A O   1 
ATOM   1333  C  CB  . ALA A 1 167 ? 46.159  80.494  -0.884  1.00 53.97  ? 176  ALA A CB  1 
ATOM   1334  N  N   . ALA A 1 168 ? 48.522  78.557  0.493   1.00 58.72  ? 177  ALA A N   1 
ATOM   1335  C  CA  . ALA A 1 168 ? 48.861  77.697  1.642   1.00 59.64  ? 177  ALA A CA  1 
ATOM   1336  C  C   . ALA A 1 168 ? 49.809  78.403  2.555   1.00 62.72  ? 177  ALA A C   1 
ATOM   1337  O  O   . ALA A 1 168 ? 49.903  78.057  3.733   1.00 64.88  ? 177  ALA A O   1 
ATOM   1338  C  CB  . ALA A 1 168 ? 49.482  76.388  1.178   1.00 61.75  ? 177  ALA A CB  1 
ATOM   1339  N  N   . ASP A 1 169 ? 50.500  79.408  2.035   1.00 62.73  ? 178  ASP A N   1 
ATOM   1340  C  CA  . ASP A 1 169 ? 51.428  80.169  2.843   1.00 61.99  ? 178  ASP A CA  1 
ATOM   1341  C  C   . ASP A 1 169 ? 50.738  81.141  3.779   1.00 60.45  ? 178  ASP A C   1 
ATOM   1342  O  O   . ASP A 1 169 ? 51.274  81.434  4.836   1.00 60.85  ? 178  ASP A O   1 
ATOM   1343  C  CB  . ASP A 1 169 ? 52.377  80.925  1.931   1.00 68.14  ? 178  ASP A CB  1 
ATOM   1344  C  CG  . ASP A 1 169 ? 53.655  80.148  1.691   1.00 77.70  ? 178  ASP A CG  1 
ATOM   1345  O  OD1 . ASP A 1 169 ? 54.303  80.378  0.636   1.00 80.23  ? 178  ASP A OD1 1 
ATOM   1346  O  OD2 . ASP A 1 169 ? 54.014  79.307  2.559   1.00 79.42  ? 178  ASP A OD2 1 
ATOM   1347  N  N   . GLY A 1 170 ? 49.565  81.650  3.418   1.00 55.37  ? 179  GLY A N   1 
ATOM   1348  C  CA  . GLY A 1 170 ? 48.878  82.577  4.302   1.00 50.35  ? 179  GLY A CA  1 
ATOM   1349  C  C   . GLY A 1 170 ? 47.904  81.887  5.232   1.00 42.80  ? 179  GLY A C   1 
ATOM   1350  O  O   . GLY A 1 170 ? 47.044  82.520  5.810   1.00 40.77  ? 179  GLY A O   1 
ATOM   1351  N  N   . ILE A 1 171 ? 48.039  80.547  5.404   1.00 32.33  ? 180  ILE A N   1 
ATOM   1352  C  CA  . ILE A 1 171 ? 47.109  79.837  6.228   1.00 28.38  ? 180  ILE A CA  1 
ATOM   1353  C  C   . ILE A 1 171 ? 47.218  80.208  7.710   1.00 31.69  ? 180  ILE A C   1 
ATOM   1354  O  O   . ILE A 1 171 ? 46.342  79.801  8.462   1.00 39.32  ? 180  ILE A O   1 
ATOM   1355  C  CB  A ILE A 1 171 ? 47.366  78.344  5.973   0.43 33.93  ? 180  ILE A CB  1 
ATOM   1356  C  CB  B ILE A 1 171 ? 47.338  78.192  6.288   0.57 35.63  ? 180  ILE A CB  1 
ATOM   1357  C  CG1 A ILE A 1 171 ? 46.146  77.703  5.342   0.43 32.66  ? 180  ILE A CG1 1 
ATOM   1358  C  CG1 B ILE A 1 171 ? 48.808  77.938  6.809   0.57 33.50  ? 180  ILE A CG1 1 
ATOM   1359  C  CG2 A ILE A 1 171 ? 47.781  77.643  7.247   0.43 35.82  ? 180  ILE A CG2 1 
ATOM   1360  C  CG2 B ILE A 1 171 ? 47.064  77.595  4.886   0.57 36.42  ? 180  ILE A CG2 1 
ATOM   1361  C  CD1 A ILE A 1 171 ? 46.415  76.280  4.984   0.43 28.44  ? 180  ILE A CD1 1 
ATOM   1362  C  CD1 B ILE A 1 171 ? 49.472  76.596  6.394   0.57 32.93  ? 180  ILE A CD1 1 
ATOM   1363  N  N   . THR A 1 172 ? 48.260  80.885  8.174   1.00 22.43  ? 181  THR A N   1 
ATOM   1364  C  CA  . THR A 1 172 ? 48.266  81.251  9.606   1.00 18.40  ? 181  THR A CA  1 
ATOM   1365  C  C   . THR A 1 172 ? 48.049  82.800  9.711   1.00 20.01  ? 181  THR A C   1 
ATOM   1366  O  O   . THR A 1 172 ? 48.139  83.362  10.814  1.00 23.42  ? 181  THR A O   1 
ATOM   1367  C  CB  . THR A 1 172 ? 49.617  80.881  10.264  1.00 23.71  ? 181  THR A CB  1 
ATOM   1368  O  OG1 . THR A 1 172 ? 50.646  81.466  9.484   1.00 30.66  ? 181  THR A OG1 1 
ATOM   1369  C  CG2 . THR A 1 172 ? 49.783  79.319  10.327  1.00 25.61  ? 181  THR A CG2 1 
ATOM   1370  N  N   . ALA A 1 173 ? 47.743  83.448  8.592   1.00 22.79  ? 182  ALA A N   1 
ATOM   1371  C  CA  . ALA A 1 173 ? 47.513  84.915  8.540   1.00 21.80  ? 182  ALA A CA  1 
ATOM   1372  C  C   . ALA A 1 173 ? 46.200  85.327  9.161   1.00 20.25  ? 182  ALA A C   1 
ATOM   1373  O  O   . ALA A 1 173 ? 46.139  86.446  9.625   1.00 19.97  ? 182  ALA A O   1 
ATOM   1374  C  CB  . ALA A 1 173 ? 47.510  85.383  7.101   1.00 21.08  ? 182  ALA A CB  1 
ATOM   1375  N  N   . THR A 1 174 ? 45.137  84.444  9.238   1.00 21.12  ? 183  THR A N   1 
ATOM   1376  C  CA  . THR A 1 174 ? 43.856  84.932  9.779   1.00 18.93  ? 183  THR A CA  1 
ATOM   1377  C  C   . THR A 1 174 ? 43.912  85.455  11.159  1.00 18.66  ? 183  THR A C   1 
ATOM   1378  O  O   . THR A 1 174 ? 43.327  86.501  11.403  1.00 17.55  ? 183  THR A O   1 
ATOM   1379  C  CB  . THR A 1 174 ? 42.711  83.844  9.614   1.00 20.47  ? 183  THR A CB  1 
ATOM   1380  O  OG1 . THR A 1 174 ? 42.454  83.774  8.216   1.00 23.11  ? 183  THR A OG1 1 
ATOM   1381  C  CG2 . THR A 1 174 ? 41.465  84.209  10.341  1.00 20.68  ? 183  THR A CG2 1 
ATOM   1382  N  N   . PRO A 1 175 ? 44.587  84.803  12.141  1.00 20.17  ? 184  PRO A N   1 
ATOM   1383  C  CA  . PRO A 1 175 ? 44.609  85.366  13.498  1.00 18.14  ? 184  PRO A CA  1 
ATOM   1384  C  C   . PRO A 1 175 ? 45.289  86.760  13.583  1.00 16.72  ? 184  PRO A C   1 
ATOM   1385  O  O   . PRO A 1 175 ? 44.957  87.574  14.434  1.00 20.45  ? 184  PRO A O   1 
ATOM   1386  C  CB  . PRO A 1 175 ? 45.353  84.279  14.318  1.00 19.55  ? 184  PRO A CB  1 
ATOM   1387  C  CG  . PRO A 1 175 ? 45.066  83.025  13.565  1.00 20.82  ? 184  PRO A CG  1 
ATOM   1388  C  CD  . PRO A 1 175 ? 45.156  83.439  12.108  1.00 22.67  ? 184  PRO A CD  1 
ATOM   1389  N  N   . LEU A 1 176 ? 46.268  86.988  12.699  1.00 18.49  ? 185  LEU A N   1 
ATOM   1390  C  CA  . LEU A 1 176 ? 46.922  88.314  12.699  1.00 18.37  ? 185  LEU A CA  1 
ATOM   1391  C  C   . LEU A 1 176 ? 45.995  89.339  12.026  1.00 16.93  ? 185  LEU A C   1 
ATOM   1392  O  O   . LEU A 1 176 ? 45.853  90.448  12.524  1.00 19.42  ? 185  LEU A O   1 
ATOM   1393  C  CB  . LEU A 1 176 ? 48.211  88.216  11.905  1.00 16.39  ? 185  LEU A CB  1 
ATOM   1394  C  CG  . LEU A 1 176 ? 48.993  89.591  11.842  1.00 17.67  ? 185  LEU A CG  1 
ATOM   1395  C  CD1 . LEU A 1 176 ? 49.291  90.087  13.286  1.00 23.12  ? 185  LEU A CD1 1 
ATOM   1396  C  CD2 . LEU A 1 176 ? 50.338  89.347  11.131  1.00 25.42  ? 185  LEU A CD2 1 
ATOM   1397  N  N   . ALA A 1 177 ? 45.407  88.992  10.844  1.00 17.42  ? 186  ALA A N   1 
ATOM   1398  C  CA  . ALA A 1 177 ? 44.447  89.914  10.238  1.00 16.86  ? 186  ALA A CA  1 
ATOM   1399  C  C   . ALA A 1 177 ? 43.336  90.243  11.225  1.00 17.33  ? 186  ALA A C   1 
ATOM   1400  O  O   . ALA A 1 177 ? 42.901  91.401  11.271  1.00 17.69  ? 186  ALA A O   1 
ATOM   1401  C  CB  . ALA A 1 177 ? 43.833  89.298  8.967   1.00 16.59  ? 186  ALA A CB  1 
ATOM   1402  N  N   . SER A 1 178 ? 42.904  89.265  12.033  1.00 19.70  ? 187  SER A N   1 
ATOM   1403  C  CA  . SER A 1 178 ? 41.848  89.508  13.009  1.00 18.38  ? 187  SER A CA  1 
ATOM   1404  C  C   . SER A 1 178 ? 42.347  90.403  14.129  1.00 22.50  ? 187  SER A C   1 
ATOM   1405  O  O   . SER A 1 178 ? 41.590  91.246  14.637  1.00 22.43  ? 187  SER A O   1 
ATOM   1406  C  CB  . SER A 1 178 ? 41.345  88.198  13.626  1.00 23.19  ? 187  SER A CB  1 
ATOM   1407  O  OG  A SER A 1 178 ? 41.083  87.250  12.587  0.79 27.28  ? 187  SER A OG  1 
ATOM   1408  O  OG  B SER A 1 178 ? 40.862  88.493  15.011  0.21 29.58  ? 187  SER A OG  1 
ATOM   1409  N  N   . THR A 1 179 ? 43.621  90.239  14.534  1.00 18.99  ? 188  THR A N   1 
ATOM   1410  C  CA  . THR A 1 179 ? 44.156  91.106  15.571  1.00 17.95  ? 188  THR A CA  1 
ATOM   1411  C  C   . THR A 1 179 ? 44.208  92.567  15.062  1.00 20.32  ? 188  THR A C   1 
ATOM   1412  O  O   . THR A 1 179 ? 43.950  93.495  15.840  1.00 23.90  ? 188  THR A O   1 
ATOM   1413  C  CB  . THR A 1 179 ? 45.600  90.634  15.924  1.00 21.53  ? 188  THR A CB  1 
ATOM   1414  O  OG1 . THR A 1 179 ? 45.462  89.326  16.536  1.00 21.58  ? 188  THR A OG1 1 
ATOM   1415  C  CG2 . THR A 1 179 ? 46.281  91.578  16.903  1.00 23.76  ? 188  THR A CG2 1 
ATOM   1416  N  N   . TYR A 1 180 ? 44.540  92.752  13.772  1.00 19.52  ? 189  TYR A N   1 
ATOM   1417  C  CA  . TYR A 1 180 ? 44.528  94.095  13.180  1.00 23.21  ? 189  TYR A CA  1 
ATOM   1418  C  C   . TYR A 1 180 ? 43.092  94.559  12.812  1.00 27.09  ? 189  TYR A C   1 
ATOM   1419  O  O   . TYR A 1 180 ? 42.892  95.745  12.528  1.00 29.89  ? 189  TYR A O   1 
ATOM   1420  C  CB  . TYR A 1 180 ? 45.234  94.083  11.828  1.00 22.10  ? 189  TYR A CB  1 
ATOM   1421  C  CG  . TYR A 1 180 ? 46.716  93.771  11.805  1.00 22.87  ? 189  TYR A CG  1 
ATOM   1422  C  CD1 . TYR A 1 180 ? 47.545  94.140  12.858  1.00 22.10  ? 189  TYR A CD1 1 
ATOM   1423  C  CD2 . TYR A 1 180 ? 47.289  93.153  10.711  1.00 20.57  ? 189  TYR A CD2 1 
ATOM   1424  C  CE1 . TYR A 1 180 ? 48.920  93.896  12.812  1.00 22.50  ? 189  TYR A CE1 1 
ATOM   1425  C  CE2 . TYR A 1 180 ? 48.663  92.913  10.647  1.00 23.01  ? 189  TYR A CE2 1 
ATOM   1426  C  CZ  . TYR A 1 180 ? 49.462  93.291  11.698  1.00 23.16  ? 189  TYR A CZ  1 
ATOM   1427  O  OH  . TYR A 1 180 ? 50.796  93.056  11.555  1.00 24.78  ? 189  TYR A OH  1 
ATOM   1428  N  N   . ASP A 1 181 ? 42.150  93.628  12.751  1.00 26.12  ? 190  ASP A N   1 
ATOM   1429  C  CA  . ASP A 1 181 ? 40.763  93.875  12.269  1.00 27.89  ? 190  ASP A CA  1 
ATOM   1430  C  C   . ASP A 1 181 ? 40.928  94.390  10.823  1.00 27.39  ? 190  ASP A C   1 
ATOM   1431  O  O   . ASP A 1 181 ? 40.529  95.486  10.458  1.00 24.06  ? 190  ASP A O   1 
ATOM   1432  C  CB  . ASP A 1 181 ? 40.000  94.868  13.185  1.00 34.47  ? 190  ASP A CB  1 
ATOM   1433  C  CG  . ASP A 1 181 ? 38.516  95.017  12.799  1.00 43.53  ? 190  ASP A CG  1 
ATOM   1434  O  OD1 . ASP A 1 181 ? 37.993  94.144  12.021  1.00 39.84  ? 190  ASP A OD1 1 
ATOM   1435  O  OD2 . ASP A 1 181 ? 37.887  95.994  13.259  1.00 47.97  ? 190  ASP A OD2 1 
ATOM   1436  N  N   . ALA A 1 182 ? 41.557  93.552  9.999   1.00 19.80  ? 191  ALA A N   1 
ATOM   1437  C  CA  . ALA A 1 182 ? 41.871  93.880  8.621   1.00 17.89  ? 191  ALA A CA  1 
ATOM   1438  C  C   . ALA A 1 182 ? 41.494  92.761  7.669   1.00 18.39  ? 191  ALA A C   1 
ATOM   1439  O  O   . ALA A 1 182 ? 41.491  91.607  8.064   1.00 19.61  ? 191  ALA A O   1 
ATOM   1440  C  CB  . ALA A 1 182 ? 43.387  94.050  8.506   1.00 17.77  ? 191  ALA A CB  1 
ATOM   1441  N  N   . PRO A 1 183 ? 41.176  93.098  6.431   1.00 15.19  ? 192  PRO A N   1 
ATOM   1442  C  CA  . PRO A 1 183 ? 40.873  92.062  5.474   1.00 15.59  ? 192  PRO A CA  1 
ATOM   1443  C  C   . PRO A 1 183 ? 42.203  91.530  4.844   1.00 18.34  ? 192  PRO A C   1 
ATOM   1444  O  O   . PRO A 1 183 ? 43.264  92.199  4.931   1.00 17.62  ? 192  PRO A O   1 
ATOM   1445  C  CB  . PRO A 1 183 ? 40.076  92.793  4.388   1.00 15.37  ? 192  PRO A CB  1 
ATOM   1446  C  CG  . PRO A 1 183 ? 40.705  94.195  4.378   1.00 13.95  ? 192  PRO A CG  1 
ATOM   1447  C  CD  . PRO A 1 183 ? 40.981  94.469  5.888   1.00 15.27  ? 192  PRO A CD  1 
ATOM   1448  N  N   . ILE A 1 184 ? 42.119  90.379  4.206   1.00 16.85  ? 193  ILE A N   1 
ATOM   1449  C  CA  . ILE A 1 184 ? 43.250  89.841  3.493   1.00 18.25  ? 193  ILE A CA  1 
ATOM   1450  C  C   . ILE A 1 184 ? 42.889  90.012  1.995   1.00 16.18  ? 193  ILE A C   1 
ATOM   1451  O  O   . ILE A 1 184 ? 41.818  89.570  1.541   1.00 18.25  ? 193  ILE A O   1 
ATOM   1452  C  CB  . ILE A 1 184 ? 43.430  88.353  3.806   1.00 16.51  ? 193  ILE A CB  1 
ATOM   1453  C  CG1 . ILE A 1 184 ? 43.970  88.198  5.243   1.00 18.51  ? 193  ILE A CG1 1 
ATOM   1454  C  CG2 . ILE A 1 184 ? 44.318  87.716  2.677   1.00 18.01  ? 193  ILE A CG2 1 
ATOM   1455  C  CD1 . ILE A 1 184 ? 43.967  86.729  5.821   1.00 18.03  ? 193  ILE A CD1 1 
ATOM   1456  N  N   . LEU A 1 185 ? 43.753  90.683  1.240   1.00 17.03  ? 194  LEU A N   1 
ATOM   1457  C  CA  . LEU A 1 185 ? 43.533  90.770  -0.207  1.00 16.75  ? 194  LEU A CA  1 
ATOM   1458  C  C   . LEU A 1 185 ? 44.697  89.962  -0.873  1.00 20.15  ? 194  LEU A C   1 
ATOM   1459  O  O   . LEU A 1 185 ? 45.683  89.655  -0.216  1.00 20.32  ? 194  LEU A O   1 
ATOM   1460  C  CB  . LEU A 1 185 ? 43.588  92.232  -0.776  1.00 17.47  ? 194  LEU A CB  1 
ATOM   1461  C  CG  . LEU A 1 185 ? 42.431  93.100  -0.256  1.00 20.41  ? 194  LEU A CG  1 
ATOM   1462  C  CD1 . LEU A 1 185 ? 42.593  94.553  -0.794  1.00 20.38  ? 194  LEU A CD1 1 
ATOM   1463  C  CD2 . LEU A 1 185 ? 41.030  92.496  -0.615  1.00 18.44  ? 194  LEU A CD2 1 
ATOM   1464  N  N   . LEU A 1 186 ? 44.579  89.708  -2.155  1.00 20.01  ? 195  LEU A N   1 
ATOM   1465  C  CA  . LEU A 1 186 ? 45.562  88.839  -2.795  1.00 21.94  ? 195  LEU A CA  1 
ATOM   1466  C  C   . LEU A 1 186 ? 46.422  89.486  -3.873  1.00 23.59  ? 195  LEU A C   1 
ATOM   1467  O  O   . LEU A 1 186 ? 45.944  90.315  -4.652  1.00 23.76  ? 195  LEU A O   1 
ATOM   1468  C  CB  . LEU A 1 186 ? 44.764  87.676  -3.462  1.00 22.10  ? 195  LEU A CB  1 
ATOM   1469  C  CG  . LEU A 1 186 ? 43.854  86.916  -2.487  1.00 21.68  ? 195  LEU A CG  1 
ATOM   1470  C  CD1 . LEU A 1 186 ? 43.046  85.884  -3.235  1.00 23.83  ? 195  LEU A CD1 1 
ATOM   1471  C  CD2 . LEU A 1 186 ? 44.672  86.299  -1.367  1.00 18.15  ? 195  LEU A CD2 1 
ATOM   1472  N  N   . ALA A 1 187 ? 47.688  89.045  -3.918  1.00 24.79  ? 196  ALA A N   1 
ATOM   1473  C  CA  . ALA A 1 187 ? 48.674  89.520  -4.884  1.00 26.03  ? 196  ALA A CA  1 
ATOM   1474  C  C   . ALA A 1 187 ? 49.239  88.318  -5.695  1.00 31.60  ? 196  ALA A C   1 
ATOM   1475  O  O   . ALA A 1 187 ? 48.991  87.157  -5.349  1.00 29.81  ? 196  ALA A O   1 
ATOM   1476  C  CB  . ALA A 1 187 ? 49.835  90.119  -4.134  1.00 26.90  ? 196  ALA A CB  1 
ATOM   1477  N  N   . ASN A 1 188 ? 49.971  88.647  -6.772  1.00 32.58  ? 197  ASN A N   1 
ATOM   1478  C  CA  . ASN A 1 188 ? 50.733  87.684  -7.545  1.00 35.37  ? 197  ASN A CA  1 
ATOM   1479  C  C   . ASN A 1 188 ? 52.146  87.930  -7.066  1.00 36.49  ? 197  ASN A C   1 
ATOM   1480  O  O   . ASN A 1 188 ? 52.391  88.896  -6.325  1.00 33.18  ? 197  ASN A O   1 
ATOM   1481  C  CB  . ASN A 1 188 ? 50.584  87.934  -9.024  1.00 35.47  ? 197  ASN A CB  1 
ATOM   1482  C  CG  . ASN A 1 188 ? 49.233  87.467  -9.482  1.00 34.50  ? 197  ASN A CG  1 
ATOM   1483  O  OD1 . ASN A 1 188 ? 48.839  86.338  -9.158  1.00 38.27  ? 197  ASN A OD1 1 
ATOM   1484  N  ND2 . ASN A 1 188 ? 48.461  88.222  -10.228 1.00 34.31  ? 197  ASN A ND2 1 
ATOM   1485  N  N   . LYS A 1 189 ? 53.107  87.100  -7.457  1.00 33.83  ? 198  LYS A N   1 
ATOM   1486  C  CA  . LYS A 1 189 ? 54.451  87.321  -6.936  1.00 32.99  ? 198  LYS A CA  1 
ATOM   1487  C  C   . LYS A 1 189 ? 55.046  88.654  -7.338  1.00 31.20  ? 198  LYS A C   1 
ATOM   1488  O  O   . LYS A 1 189 ? 55.762  89.276  -6.529  1.00 32.39  ? 198  LYS A O   1 
ATOM   1489  C  CB  . LYS A 1 189 ? 55.417  86.205  -7.453  1.00 38.45  ? 198  LYS A CB  1 
ATOM   1490  C  CG  . LYS A 1 189 ? 56.810  86.360  -6.882  1.00 45.36  ? 198  LYS A CG  1 
ATOM   1491  C  CD  . LYS A 1 189 ? 57.809  85.425  -7.562  1.00 54.55  ? 198  LYS A CD  1 
ATOM   1492  C  CE  . LYS A 1 189 ? 59.147  85.624  -6.905  1.00 64.99  ? 198  LYS A CE  1 
ATOM   1493  N  NZ  . LYS A 1 189 ? 60.213  84.856  -7.607  1.00 76.18  ? 198  LYS A NZ  1 
ATOM   1494  N  N   . ASP A 1 190 ? 54.775  89.102  -8.570  1.00 32.22  ? 199  ASP A N   1 
ATOM   1495  C  CA  . ASP A 1 190 ? 55.404  90.348  -9.021  1.00 40.77  ? 199  ASP A CA  1 
ATOM   1496  C  C   . ASP A 1 190 ? 54.423  91.460  -9.417  1.00 44.38  ? 199  ASP A C   1 
ATOM   1497  O  O   . ASP A 1 190 ? 54.852  92.481  -9.941  1.00 43.17  ? 199  ASP A O   1 
ATOM   1498  C  CB  . ASP A 1 190 ? 56.338  90.019  -10.235 1.00 44.40  ? 199  ASP A CB  1 
ATOM   1499  C  CG  . ASP A 1 190 ? 57.453  89.066  -9.850  1.00 48.12  ? 199  ASP A CG  1 
ATOM   1500  O  OD1 . ASP A 1 190 ? 58.163  89.352  -8.866  1.00 48.37  ? 199  ASP A OD1 1 
ATOM   1501  O  OD2 . ASP A 1 190 ? 57.600  88.024  -10.521 1.00 52.53  ? 199  ASP A OD2 1 
ATOM   1502  N  N   . ASP A 1 191 ? 53.123  91.283  -9.185  1.00 43.92  ? 200  ASP A N   1 
ATOM   1503  C  CA  . ASP A 1 191 ? 52.131  92.317  -9.539  1.00 43.97  ? 200  ASP A CA  1 
ATOM   1504  C  C   . ASP A 1 191 ? 50.864  92.168  -8.697  1.00 41.25  ? 200  ASP A C   1 
ATOM   1505  O  O   . ASP A 1 191 ? 50.711  91.155  -8.003  1.00 37.52  ? 200  ASP A O   1 
ATOM   1506  C  CB  . ASP A 1 191 ? 51.704  92.170  -11.008 1.00 44.13  ? 200  ASP A CB  1 
ATOM   1507  C  CG  . ASP A 1 191 ? 50.904  90.876  -11.292 1.00 55.41  ? 200  ASP A CG  1 
ATOM   1508  O  OD1 . ASP A 1 191 ? 51.530  89.860  -11.665 1.00 56.27  ? 200  ASP A OD1 1 
ATOM   1509  O  OD2 . ASP A 1 191 ? 49.652  90.884  -11.125 1.00 56.55  ? 200  ASP A OD2 1 
ATOM   1510  N  N   . ILE A 1 192 ? 49.966  93.152  -8.759  1.00 36.53  ? 201  ILE A N   1 
ATOM   1511  C  CA  . ILE A 1 192 ? 48.675  92.974  -8.136  1.00 33.87  ? 201  ILE A CA  1 
ATOM   1512  C  C   . ILE A 1 192 ? 47.705  93.208  -9.233  1.00 32.31  ? 201  ILE A C   1 
ATOM   1513  O  O   . ILE A 1 192 ? 47.932  94.094  -10.058 1.00 31.35  ? 201  ILE A O   1 
ATOM   1514  C  CB  . ILE A 1 192 ? 48.379  93.900  -6.926  1.00 31.30  ? 201  ILE A CB  1 
ATOM   1515  C  CG1 . ILE A 1 192 ? 48.783  95.397  -7.245  1.00 32.43  ? 201  ILE A CG1 1 
ATOM   1516  C  CG2 . ILE A 1 192 ? 49.123  93.375  -5.720  1.00 30.02  ? 201  ILE A CG2 1 
ATOM   1517  C  CD1 . ILE A 1 192 ? 48.187  96.409  -6.207  1.00 29.48  ? 201  ILE A CD1 1 
ATOM   1518  N  N   . PRO A 1 193 ? 46.619  92.422  -9.331  1.00 33.22  ? 202  PRO A N   1 
ATOM   1519  C  CA  . PRO A 1 193 ? 45.654  92.674  -10.404 1.00 31.91  ? 202  PRO A CA  1 
ATOM   1520  C  C   . PRO A 1 193 ? 44.824  93.932  -10.104 1.00 33.04  ? 202  PRO A C   1 
ATOM   1521  O  O   . PRO A 1 193 ? 44.828  94.456  -8.993  1.00 28.36  ? 202  PRO A O   1 
ATOM   1522  C  CB  . PRO A 1 193 ? 44.792  91.423  -10.416 1.00 31.91  ? 202  PRO A CB  1 
ATOM   1523  C  CG  . PRO A 1 193 ? 44.933  90.841  -9.094  1.00 34.45  ? 202  PRO A CG  1 
ATOM   1524  C  CD  . PRO A 1 193 ? 46.368  91.126  -8.691  1.00 34.90  ? 202  PRO A CD  1 
ATOM   1525  N  N   . GLU A 1 194 ? 44.082  94.385  -11.097 1.00 29.78  ? 203  GLU A N   1 
ATOM   1526  C  CA  . GLU A 1 194 ? 43.289  95.573  -10.983 1.00 26.92  ? 203  GLU A CA  1 
ATOM   1527  C  C   . GLU A 1 194 ? 42.259  95.486  -9.847  1.00 30.96  ? 203  GLU A C   1 
ATOM   1528  O  O   . GLU A 1 194 ? 42.008  96.483  -9.182  1.00 27.61  ? 203  GLU A O   1 
ATOM   1529  C  CB  . GLU A 1 194 ? 42.573  95.773  -12.331 1.00 33.42  ? 203  GLU A CB  1 
ATOM   1530  C  CG  . GLU A 1 194 ? 41.556  96.905  -12.336 1.00 45.37  ? 203  GLU A CG  1 
ATOM   1531  C  CD  . GLU A 1 194 ? 42.149  98.305  -11.989 1.00 56.02  ? 203  GLU A CD  1 
ATOM   1532  O  OE1 . GLU A 1 194 ? 43.332  98.568  -12.311 1.00 57.25  ? 203  GLU A OE1 1 
ATOM   1533  O  OE2 . GLU A 1 194 ? 41.402  99.130  -11.407 1.00 54.55  ? 203  GLU A OE2 1 
ATOM   1534  N  N   . SER A 1 195 ? 41.639  94.306  -9.659  1.00 27.65  ? 204  SER A N   1 
ATOM   1535  C  CA  . SER A 1 195 ? 40.662  94.099  -8.607  1.00 27.17  ? 204  SER A CA  1 
ATOM   1536  C  C   . SER A 1 195 ? 41.351  94.461  -7.245  1.00 23.74  ? 204  SER A C   1 
ATOM   1537  O  O   . SER A 1 195 ? 40.793  95.288  -6.515  1.00 24.64  ? 204  SER A O   1 
ATOM   1538  C  CB  . SER A 1 195 ? 40.162  92.642  -8.667  1.00 27.50  ? 204  SER A CB  1 
ATOM   1539  O  OG  . SER A 1 195 ? 41.236  91.735  -8.464  1.00 31.87  ? 204  SER A OG  1 
ATOM   1540  N  N   . THR A 1 196 ? 42.526  93.935  -6.937  1.00 20.32  ? 205  THR A N   1 
ATOM   1541  C  CA  . THR A 1 196 ? 43.201  94.255  -5.658  1.00 20.76  ? 205  THR A CA  1 
ATOM   1542  C  C   . THR A 1 196 ? 43.625  95.767  -5.605  1.00 21.97  ? 205  THR A C   1 
ATOM   1543  O  O   . THR A 1 196 ? 43.462  96.424  -4.589  1.00 20.96  ? 205  THR A O   1 
ATOM   1544  C  CB  . THR A 1 196 ? 44.476  93.372  -5.497  1.00 20.16  ? 205  THR A CB  1 
ATOM   1545  O  OG1 . THR A 1 196 ? 44.032  92.015  -5.458  1.00 22.60  ? 205  THR A OG1 1 
ATOM   1546  C  CG2 . THR A 1 196 ? 45.271  93.708  -4.209  1.00 20.62  ? 205  THR A CG2 1 
ATOM   1547  N  N   . LYS A 1 197 ? 44.170  96.293  -6.733  1.00 21.12  ? 206  LYS A N   1 
ATOM   1548  C  CA  . LYS A 1 197 ? 44.584  97.700  -6.772  1.00 24.44  ? 206  LYS A CA  1 
ATOM   1549  C  C   . LYS A 1 197 ? 43.381  98.607  -6.436  1.00 23.67  ? 206  LYS A C   1 
ATOM   1550  O  O   . LYS A 1 197 ? 43.530  99.518  -5.647  1.00 23.14  ? 206  LYS A O   1 
ATOM   1551  C  CB  . LYS A 1 197 ? 45.121  97.976  -8.200  1.00 31.53  ? 206  LYS A CB  1 
ATOM   1552  C  CG  . LYS A 1 197 ? 45.141  99.455  -8.583  1.00 44.20  ? 206  LYS A CG  1 
ATOM   1553  C  CD  . LYS A 1 197 ? 45.730  99.630  -10.037 1.00 54.70  ? 206  LYS A CD  1 
ATOM   1554  C  CE  . LYS A 1 197 ? 45.723  101.098 -10.458 1.00 58.55  ? 206  LYS A CE  1 
ATOM   1555  N  NZ  . LYS A 1 197 ? 46.957  101.768 -9.962  1.00 59.82  ? 206  LYS A NZ  1 
ATOM   1556  N  N   . ALA A 1 198 ? 42.198  98.356  -7.014  1.00 21.24  ? 207  ALA A N   1 
ATOM   1557  C  CA  . ALA A 1 198 ? 41.060  99.237  -6.781  1.00 22.43  ? 207  ALA A CA  1 
ATOM   1558  C  C   . ALA A 1 198 ? 40.543  99.098  -5.363  1.00 20.99  ? 207  ALA A C   1 
ATOM   1559  O  O   . ALA A 1 198 ? 40.077  100.096 -4.790  1.00 20.68  ? 207  ALA A O   1 
ATOM   1560  C  CB  . ALA A 1 198 ? 39.920  98.918  -7.786  1.00 21.12  ? 207  ALA A CB  1 
ATOM   1561  N  N   . GLU A 1 199 ? 40.587  97.873  -4.778  1.00 18.74  ? 208  GLU A N   1 
ATOM   1562  C  CA  . GLU A 1 199 ? 40.065  97.764  -3.421  1.00 19.85  ? 208  GLU A CA  1 
ATOM   1563  C  C   . GLU A 1 199 ? 41.063  98.381  -2.423  1.00 19.73  ? 208  GLU A C   1 
ATOM   1564  O  O   . GLU A 1 199 ? 40.635  98.945  -1.423  1.00 18.73  ? 208  GLU A O   1 
ATOM   1565  C  CB  . GLU A 1 199 ? 39.775  96.250  -3.097  1.00 19.57  ? 208  GLU A CB  1 
ATOM   1566  C  CG  . GLU A 1 199 ? 39.245  96.009  -1.661  1.00 17.15  ? 208  GLU A CG  1 
ATOM   1567  C  CD  . GLU A 1 199 ? 37.886  96.690  -1.389  1.00 19.70  ? 208  GLU A CD  1 
ATOM   1568  O  OE1 . GLU A 1 199 ? 37.267  97.263  -2.346  1.00 21.42  ? 208  GLU A OE1 1 
ATOM   1569  O  OE2 . GLU A 1 199 ? 37.428  96.645  -0.214  1.00 20.43  ? 208  GLU A OE2 1 
ATOM   1570  N  N   . LEU A 1 200 ? 42.398  98.241  -2.648  1.00 18.84  ? 209  LEU A N   1 
ATOM   1571  C  CA  . LEU A 1 200 ? 43.364  98.904  -1.794  1.00 19.85  ? 209  LEU A CA  1 
ATOM   1572  C  C   . LEU A 1 200 ? 43.050  100.436 -1.851  1.00 19.85  ? 209  LEU A C   1 
ATOM   1573  O  O   . LEU A 1 200 ? 43.024  101.107 -0.827  1.00 18.91  ? 209  LEU A O   1 
ATOM   1574  C  CB  . LEU A 1 200 ? 44.826  98.734  -2.304  1.00 21.33  ? 209  LEU A CB  1 
ATOM   1575  C  CG  . LEU A 1 200 ? 45.442  97.358  -2.032  1.00 22.90  ? 209  LEU A CG  1 
ATOM   1576  C  CD1 . LEU A 1 200 ? 46.744  97.257  -2.738  1.00 24.30  ? 209  LEU A CD1 1 
ATOM   1577  C  CD2 . LEU A 1 200 ? 45.642  97.210  -0.517  1.00 21.28  ? 209  LEU A CD2 1 
ATOM   1578  N  N   . LYS A 1 201 ? 42.797  100.982 -3.037  1.00 16.68  ? 210  LYS A N   1 
ATOM   1579  C  CA  . LYS A 1 201 ? 42.481  102.425 -3.079  1.00 19.01  ? 210  LYS A CA  1 
ATOM   1580  C  C   . LYS A 1 201 ? 41.191  102.769 -2.308  1.00 21.23  ? 210  LYS A C   1 
ATOM   1581  O  O   . LYS A 1 201 ? 41.126  103.771 -1.560  1.00 20.15  ? 210  LYS A O   1 
ATOM   1582  C  CB  . LYS A 1 201 ? 42.259  102.877 -4.558  1.00 22.06  ? 210  LYS A CB  1 
ATOM   1583  C  CG  . LYS A 1 201 ? 43.603  102.929 -5.311  1.00 27.52  ? 210  LYS A CG  1 
ATOM   1584  C  CD  . LYS A 1 201 ? 43.340  103.421 -6.813  1.00 39.43  ? 210  LYS A CD  1 
ATOM   1585  C  CE  . LYS A 1 201 ? 44.632  103.673 -7.598  1.00 52.36  ? 210  LYS A CE  1 
ATOM   1586  N  NZ  . LYS A 1 201 ? 45.404  104.902 -7.132  1.00 51.23  ? 210  LYS A NZ  1 
ATOM   1587  N  N   . ARG A 1 202 ? 40.182  101.944 -2.479  1.00 18.13  ? 211  ARG A N   1 
ATOM   1588  C  CA  . ARG A 1 202 ? 38.895  102.196 -1.802  1.00 14.48  ? 211  ARG A CA  1 
ATOM   1589  C  C   . ARG A 1 202 ? 39.042  102.129 -0.273  1.00 14.73  ? 211  ARG A C   1 
ATOM   1590  O  O   . ARG A 1 202 ? 38.453  102.960 0.415   1.00 16.88  ? 211  ARG A O   1 
ATOM   1591  C  CB  . ARG A 1 202 ? 37.852  101.113 -2.241  1.00 16.81  ? 211  ARG A CB  1 
ATOM   1592  C  CG  . ARG A 1 202 ? 36.404  101.554 -1.926  1.00 17.78  ? 211  ARG A CG  1 
ATOM   1593  C  CD  . ARG A 1 202 ? 35.415  100.355 -2.055  1.00 21.60  ? 211  ARG A CD  1 
ATOM   1594  N  NE  . ARG A 1 202 ? 35.708  99.296  -1.087  1.00 20.04  ? 211  ARG A NE  1 
ATOM   1595  C  CZ  . ARG A 1 202 ? 35.375  99.378  0.198   1.00 19.85  ? 211  ARG A CZ  1 
ATOM   1596  N  NH1 . ARG A 1 202 ? 35.720  98.410  1.036   1.00 19.01  ? 211  ARG A NH1 1 
ATOM   1597  N  NH2 . ARG A 1 202 ? 34.694  100.440 0.656   1.00 18.84  ? 211  ARG A NH2 1 
ATOM   1598  N  N   . LEU A 1 203 ? 39.806  101.152 0.237   1.00 15.57  ? 212  LEU A N   1 
ATOM   1599  C  CA  . LEU A 1 203 ? 39.975  100.995 1.719   1.00 14.14  ? 212  LEU A CA  1 
ATOM   1600  C  C   . LEU A 1 203 ? 40.798  102.127 2.318   1.00 17.18  ? 212  LEU A C   1 
ATOM   1601  O  O   . LEU A 1 203 ? 40.726  102.310 3.536   1.00 15.66  ? 212  LEU A O   1 
ATOM   1602  C  CB  . LEU A 1 203 ? 40.739  99.671  2.060   1.00 15.31  ? 212  LEU A CB  1 
ATOM   1603  C  CG  . LEU A 1 203 ? 39.896  98.421  1.708   1.00 16.25  ? 212  LEU A CG  1 
ATOM   1604  C  CD1 . LEU A 1 203 ? 40.757  97.167  1.701   1.00 13.14  ? 212  LEU A CD1 1 
ATOM   1605  C  CD2 . LEU A 1 203 ? 38.810  98.235  2.755   1.00 15.88  ? 212  LEU A CD2 1 
ATOM   1606  N  N   . ASN A 1 204 ? 41.610  102.802 1.496   1.00 18.18  ? 213  ASN A N   1 
ATOM   1607  C  CA  . ASN A 1 204 ? 42.513  103.910 1.906   1.00 17.88  ? 213  ASN A CA  1 
ATOM   1608  C  C   . ASN A 1 204 ? 43.362  103.528 3.163   1.00 19.76  ? 213  ASN A C   1 
ATOM   1609  O  O   . ASN A 1 204 ? 43.325  104.197 4.195   1.00 20.76  ? 213  ASN A O   1 
ATOM   1610  C  CB  . ASN A 1 204 ? 41.729  105.147 2.220   1.00 20.58  ? 213  ASN A CB  1 
ATOM   1611  C  CG  . ASN A 1 204 ? 42.745  106.364 2.235   1.00 25.76  ? 213  ASN A CG  1 
ATOM   1612  O  OD1 . ASN A 1 204 ? 43.654  106.409 1.371   1.00 31.73  ? 213  ASN A OD1 1 
ATOM   1613  N  ND2 . ASN A 1 204 ? 42.674  107.216 3.146   1.00 25.12  ? 213  ASN A ND2 1 
ATOM   1614  N  N   . PRO A 1 205 ? 44.074  102.420 3.104   1.00 17.65  ? 214  PRO A N   1 
ATOM   1615  C  CA  . PRO A 1 205 ? 44.870  102.040 4.286   1.00 15.20  ? 214  PRO A CA  1 
ATOM   1616  C  C   . PRO A 1 205 ? 46.104  102.914 4.433   1.00 19.18  ? 214  PRO A C   1 
ATOM   1617  O  O   . PRO A 1 205 ? 46.531  103.567 3.471   1.00 19.80  ? 214  PRO A O   1 
ATOM   1618  C  CB  . PRO A 1 205 ? 45.295  100.595 3.952   1.00 17.40  ? 214  PRO A CB  1 
ATOM   1619  C  CG  . PRO A 1 205 ? 45.410  100.619 2.436   1.00 18.19  ? 214  PRO A CG  1 
ATOM   1620  C  CD  . PRO A 1 205 ? 44.242  101.491 1.986   1.00 17.75  ? 214  PRO A CD  1 
ATOM   1621  N  N   . SER A 1 206 ? 46.688  102.873 5.598   1.00 18.78  ? 215  SER A N   1 
ATOM   1622  C  CA  . SER A 1 206 ? 47.979  103.537 5.920   1.00 22.19  ? 215  SER A CA  1 
ATOM   1623  C  C   . SER A 1 206 ? 49.081  102.474 5.842   1.00 23.73  ? 215  SER A C   1 
ATOM   1624  O  O   . SER A 1 206 ? 50.250  102.804 5.645   1.00 21.69  ? 215  SER A O   1 
ATOM   1625  C  CB  . SER A 1 206 ? 47.981  103.978 7.393   1.00 25.80  ? 215  SER A CB  1 
ATOM   1626  O  OG  . SER A 1 206 ? 47.150  105.099 7.541   1.00 36.32  ? 215  SER A OG  1 
ATOM   1627  N  N   . ASP A 1 207 ? 48.723  101.181 6.021   1.00 19.87  ? 216  ASP A N   1 
ATOM   1628  C  CA  . ASP A 1 207 ? 49.767  100.137 6.093   1.00 21.64  ? 216  ASP A CA  1 
ATOM   1629  C  C   . ASP A 1 207 ? 49.339  98.860  5.424   1.00 21.66  ? 216  ASP A C   1 
ATOM   1630  O  O   . ASP A 1 207 ? 48.175  98.444  5.579   1.00 21.08  ? 216  ASP A O   1 
ATOM   1631  C  CB  . ASP A 1 207 ? 50.021  99.810  7.603   1.00 23.25  ? 216  ASP A CB  1 
ATOM   1632  C  CG  . ASP A 1 207 ? 50.675  100.921 8.398   1.00 33.55  ? 216  ASP A CG  1 
ATOM   1633  O  OD1 . ASP A 1 207 ? 49.949  101.773 8.932   1.00 37.00  ? 216  ASP A OD1 1 
ATOM   1634  O  OD2 . ASP A 1 207 ? 51.928  100.942 8.473   1.00 37.18  ? 216  ASP A OD2 1 
ATOM   1635  N  N   . VAL A 1 208 ? 50.217  98.230  4.671   1.00 19.19  ? 217  VAL A N   1 
ATOM   1636  C  CA  . VAL A 1 208 ? 49.965  96.912  4.091   1.00 17.92  ? 217  VAL A CA  1 
ATOM   1637  C  C   . VAL A 1 208 ? 50.988  95.946  4.757   1.00 23.33  ? 217  VAL A C   1 
ATOM   1638  O  O   . VAL A 1 208 ? 52.194  96.277  4.903   1.00 23.15  ? 217  VAL A O   1 
ATOM   1639  C  CB  . VAL A 1 208 ? 50.084  96.916  2.535   1.00 18.89  ? 217  VAL A CB  1 
ATOM   1640  C  CG1 . VAL A 1 208 ? 50.236  95.517  1.993   1.00 21.36  ? 217  VAL A CG1 1 
ATOM   1641  C  CG2 . VAL A 1 208 ? 48.851  97.565  1.916   1.00 20.70  ? 217  VAL A CG2 1 
ATOM   1642  N  N   . ILE A 1 209 ? 50.508  94.759  5.177   1.00 18.73  ? 218  ILE A N   1 
ATOM   1643  C  CA  . ILE A 1 209 ? 51.364  93.786  5.852   1.00 19.35  ? 218  ILE A CA  1 
ATOM   1644  C  C   . ILE A 1 209 ? 51.372  92.596  4.903   1.00 22.60  ? 218  ILE A C   1 
ATOM   1645  O  O   . ILE A 1 209 ? 50.353  91.939  4.592   1.00 20.88  ? 218  ILE A O   1 
ATOM   1646  C  CB  . ILE A 1 209 ? 50.857  93.422  7.284   1.00 18.56  ? 218  ILE A CB  1 
ATOM   1647  C  CG1 . ILE A 1 209 ? 50.834  94.637  8.182   1.00 23.46  ? 218  ILE A CG1 1 
ATOM   1648  C  CG2 . ILE A 1 209 ? 51.737  92.302  7.915   1.00 22.85  ? 218  ILE A CG2 1 
ATOM   1649  C  CD1 . ILE A 1 209 ? 49.450  95.428  8.132   1.00 24.14  ? 218  ILE A CD1 1 
ATOM   1650  N  N   . ILE A 1 210 ? 52.560  92.324  4.363   1.00 20.26  ? 219  ILE A N   1 
ATOM   1651  C  CA  . ILE A 1 210 ? 52.732  91.209  3.464   1.00 23.19  ? 219  ILE A CA  1 
ATOM   1652  C  C   . ILE A 1 210 ? 53.175  89.967  4.270   1.00 24.30  ? 219  ILE A C   1 
ATOM   1653  O  O   . ILE A 1 210 ? 54.048  90.069  5.128   1.00 25.22  ? 219  ILE A O   1 
ATOM   1654  C  CB  . ILE A 1 210 ? 53.813  91.508  2.406   1.00 29.80  ? 219  ILE A CB  1 
ATOM   1655  C  CG1 . ILE A 1 210 ? 53.291  92.589  1.420   1.00 34.38  ? 219  ILE A CG1 1 
ATOM   1656  C  CG2 . ILE A 1 210 ? 54.141  90.218  1.701   1.00 28.90  ? 219  ILE A CG2 1 
ATOM   1657  C  CD1 . ILE A 1 210 ? 54.417  93.204  0.638   1.00 43.05  ? 219  ILE A CD1 1 
ATOM   1658  N  N   . ILE A 1 211 ? 52.537  88.838  4.009   1.00 26.10  ? 220  ILE A N   1 
ATOM   1659  C  CA  . ILE A 1 211 ? 52.886  87.578  4.683   1.00 29.81  ? 220  ILE A CA  1 
ATOM   1660  C  C   . ILE A 1 211 ? 53.641  86.777  3.632   1.00 32.01  ? 220  ILE A C   1 
ATOM   1661  O  O   . ILE A 1 211 ? 53.092  86.504  2.565   1.00 32.92  ? 220  ILE A O   1 
ATOM   1662  C  CB  . ILE A 1 211 ? 51.633  86.829  5.163   1.00 28.26  ? 220  ILE A CB  1 
ATOM   1663  C  CG1 . ILE A 1 211 ? 50.850  87.692  6.178   1.00 24.82  ? 220  ILE A CG1 1 
ATOM   1664  C  CG2 . ILE A 1 211 ? 52.047  85.409  5.784   1.00 23.52  ? 220  ILE A CG2 1 
ATOM   1665  C  CD1 . ILE A 1 211 ? 51.677  88.191  7.337   1.00 20.93  ? 220  ILE A CD1 1 
ATOM   1666  N  N   . GLY A 1 212 ? 54.875  86.400  3.930   1.00 32.23  ? 221  GLY A N   1 
ATOM   1667  C  CA  . GLY A 1 212 ? 55.663  85.663  2.945   1.00 36.71  ? 221  GLY A CA  1 
ATOM   1668  C  C   . GLY A 1 212 ? 56.964  86.421  2.678   1.00 42.34  ? 221  GLY A C   1 
ATOM   1669  O  O   . GLY A 1 212 ? 57.037  87.659  2.798   1.00 39.17  ? 221  GLY A O   1 
ATOM   1670  N  N   . ASP A 1 213 ? 58.033  85.697  2.330   1.00 43.88  ? 222  ASP A N   1 
ATOM   1671  C  CA  . ASP A 1 213 ? 59.302  86.410  2.056   1.00 45.46  ? 222  ASP A CA  1 
ATOM   1672  C  C   . ASP A 1 213 ? 59.282  86.906  0.579   1.00 42.42  ? 222  ASP A C   1 
ATOM   1673  O  O   . ASP A 1 213 ? 58.291  86.647  -0.118  1.00 38.65  ? 222  ASP A O   1 
ATOM   1674  C  CB  . ASP A 1 213 ? 60.533  85.515  2.383   1.00 47.58  ? 222  ASP A CB  1 
ATOM   1675  C  CG  . ASP A 1 213 ? 60.687  84.241  1.566   1.00 51.42  ? 222  ASP A CG  1 
ATOM   1676  O  OD1 . ASP A 1 213 ? 59.931  84.060  0.567   1.00 49.58  ? 222  ASP A OD1 1 
ATOM   1677  O  OD2 . ASP A 1 213 ? 61.577  83.421  1.914   1.00 53.80  ? 222  ASP A OD2 1 
ATOM   1678  N  N   . ASP A 1 214 ? 60.352  87.583  0.084   1.00 41.28  ? 223  ASP A N   1 
ATOM   1679  C  CA  . ASP A 1 214 ? 60.277  88.143  -1.279  1.00 46.36  ? 223  ASP A CA  1 
ATOM   1680  C  C   . ASP A 1 214 ? 60.133  87.113  -2.344  1.00 48.28  ? 223  ASP A C   1 
ATOM   1681  O  O   . ASP A 1 214 ? 59.785  87.442  -3.484  1.00 45.51  ? 223  ASP A O   1 
ATOM   1682  C  CB  . ASP A 1 214 ? 61.452  89.080  -1.588  1.00 51.50  ? 223  ASP A CB  1 
ATOM   1683  C  CG  . ASP A 1 214 ? 62.810  88.434  -1.468  1.00 63.69  ? 223  ASP A CG  1 
ATOM   1684  O  OD1 . ASP A 1 214 ? 63.809  89.180  -1.374  1.00 64.06  ? 223  ASP A OD1 1 
ATOM   1685  O  OD2 . ASP A 1 214 ? 62.878  87.173  -1.459  1.00 66.83  ? 223  ASP A OD2 1 
ATOM   1686  N  N   . GLY A 1 215 ? 60.365  85.840  -1.991  1.00 46.89  ? 224  GLY A N   1 
ATOM   1687  C  CA  . GLY A 1 215 ? 60.163  84.780  -2.962  1.00 44.64  ? 224  GLY A CA  1 
ATOM   1688  C  C   . GLY A 1 215 ? 58.678  84.583  -3.210  1.00 45.38  ? 224  GLY A C   1 
ATOM   1689  O  O   . GLY A 1 215 ? 58.285  84.169  -4.291  1.00 44.84  ? 224  GLY A O   1 
ATOM   1690  N  N   . SER A 1 216 ? 57.829  84.900  -2.188  1.00 42.93  ? 225  SER A N   1 
ATOM   1691  C  CA  . SER A 1 216 ? 56.360  84.754  -2.303  1.00 41.12  ? 225  SER A CA  1 
ATOM   1692  C  C   . SER A 1 216 ? 55.716  86.014  -2.914  1.00 37.27  ? 225  SER A C   1 
ATOM   1693  O  O   . SER A 1 216 ? 54.945  85.947  -3.881  1.00 37.94  ? 225  SER A O   1 
ATOM   1694  C  CB  . SER A 1 216 ? 55.774  84.490  -0.924  1.00 41.47  ? 225  SER A CB  1 
ATOM   1695  O  OG  . SER A 1 216 ? 54.418  84.123  -1.110  1.00 50.42  ? 225  SER A OG  1 
ATOM   1696  N  N   . VAL A 1 217 ? 56.073  87.154  -2.341  1.00 36.41  ? 226  VAL A N   1 
ATOM   1697  C  CA  . VAL A 1 217 ? 55.601  88.454  -2.826  1.00 36.11  ? 226  VAL A CA  1 
ATOM   1698  C  C   . VAL A 1 217 ? 56.849  89.339  -2.914  1.00 29.46  ? 226  VAL A C   1 
ATOM   1699  O  O   . VAL A 1 217 ? 57.406  89.739  -1.889  1.00 32.31  ? 226  VAL A O   1 
ATOM   1700  C  CB  . VAL A 1 217 ? 54.522  89.046  -1.876  1.00 31.71  ? 226  VAL A CB  1 
ATOM   1701  C  CG1 . VAL A 1 217 ? 54.001  90.368  -2.484  1.00 31.47  ? 226  VAL A CG1 1 
ATOM   1702  C  CG2 . VAL A 1 217 ? 53.372  88.029  -1.702  1.00 28.31  ? 226  VAL A CG2 1 
ATOM   1703  N  N   . SER A 1 218 ? 57.256  89.636  -4.124  1.00 33.95  ? 227  SER A N   1 
ATOM   1704  C  CA  . SER A 1 218 ? 58.525  90.363  -4.390  1.00 37.85  ? 227  SER A CA  1 
ATOM   1705  C  C   . SER A 1 218 ? 58.427  91.877  -4.296  1.00 39.80  ? 227  SER A C   1 
ATOM   1706  O  O   . SER A 1 218 ? 57.340  92.436  -4.123  1.00 38.92  ? 227  SER A O   1 
ATOM   1707  C  CB  . SER A 1 218 ? 58.998  90.023  -5.805  1.00 35.69  ? 227  SER A CB  1 
ATOM   1708  O  OG  . SER A 1 218 ? 58.289  90.781  -6.761  1.00 33.90  ? 227  SER A OG  1 
ATOM   1709  N  N   . GLN A 1 219 ? 59.575  92.542  -4.428  1.00 39.35  ? 228  GLN A N   1 
ATOM   1710  C  CA  . GLN A 1 219 ? 59.637  93.994  -4.434  1.00 40.43  ? 228  GLN A CA  1 
ATOM   1711  C  C   . GLN A 1 219 ? 58.851  94.523  -5.627  1.00 39.04  ? 228  GLN A C   1 
ATOM   1712  O  O   . GLN A 1 219 ? 58.401  95.666  -5.612  1.00 39.13  ? 228  GLN A O   1 
ATOM   1713  C  CB  . GLN A 1 219 ? 61.107  94.445  -4.571  1.00 46.06  ? 228  GLN A CB  1 
ATOM   1714  C  CG  . GLN A 1 219 ? 61.220  95.976  -4.699  1.00 59.28  ? 228  GLN A CG  1 
ATOM   1715  C  CD  . GLN A 1 219 ? 60.475  96.759  -3.606  1.00 65.42  ? 228  GLN A CD  1 
ATOM   1716  O  OE1 . GLN A 1 219 ? 60.465  96.392  -2.410  1.00 68.37  ? 228  GLN A OE1 1 
ATOM   1717  N  NE2 . GLN A 1 219 ? 59.801  97.837  -4.010  1.00 62.71  ? 228  GLN A NE2 1 
ATOM   1718  N  N   . LYS A 1 220 ? 58.710  93.724  -6.690  1.00 35.33  ? 229  LYS A N   1 
ATOM   1719  C  CA  . LYS A 1 220 ? 57.969  94.228  -7.841  1.00 35.86  ? 229  LYS A CA  1 
ATOM   1720  C  C   . LYS A 1 220 ? 56.502  94.358  -7.444  1.00 36.77  ? 229  LYS A C   1 
ATOM   1721  O  O   . LYS A 1 220 ? 55.838  95.297  -7.875  1.00 35.05  ? 229  LYS A O   1 
ATOM   1722  C  CB  . LYS A 1 220 ? 58.052  93.285  -9.042  1.00 39.25  ? 229  LYS A CB  1 
ATOM   1723  C  CG  . LYS A 1 220 ? 59.491  92.974  -9.460  1.00 46.43  ? 229  LYS A CG  1 
ATOM   1724  C  CD  . LYS A 1 220 ? 59.566  92.745  -10.966 1.00 51.84  ? 229  LYS A CD  1 
ATOM   1725  C  CE  . LYS A 1 220 ? 61.025  92.510  -11.392 1.00 56.68  ? 229  LYS A CE  1 
ATOM   1726  N  NZ  . LYS A 1 220 ? 61.119  92.236  -12.846 1.00 59.53  ? 229  LYS A NZ  1 
ATOM   1727  N  N   . ALA A 1 221 ? 55.996  93.390  -6.652  1.00 33.67  ? 230  ALA A N   1 
ATOM   1728  C  CA  . ALA A 1 221 ? 54.614  93.538  -6.200  1.00 31.01  ? 230  ALA A CA  1 
ATOM   1729  C  C   . ALA A 1 221 ? 54.593  94.689  -5.193  1.00 27.30  ? 230  ALA A C   1 
ATOM   1730  O  O   . ALA A 1 221 ? 53.624  95.446  -5.184  1.00 30.42  ? 230  ALA A O   1 
ATOM   1731  C  CB  . ALA A 1 221 ? 54.107  92.236  -5.545  1.00 29.36  ? 230  ALA A CB  1 
ATOM   1732  N  N   . VAL A 1 222 ? 55.606  94.841  -4.353  1.00 26.59  ? 231  VAL A N   1 
ATOM   1733  C  CA  . VAL A 1 222 ? 55.577  95.926  -3.397  1.00 29.83  ? 231  VAL A CA  1 
ATOM   1734  C  C   . VAL A 1 222 ? 55.435  97.250  -4.164  1.00 33.98  ? 231  VAL A C   1 
ATOM   1735  O  O   . VAL A 1 222 ? 54.641  98.087  -3.742  1.00 30.44  ? 231  VAL A O   1 
ATOM   1736  C  CB  . VAL A 1 222 ? 56.817  95.914  -2.501  1.00 32.36  ? 231  VAL A CB  1 
ATOM   1737  C  CG1 . VAL A 1 222 ? 56.887  97.176  -1.661  1.00 32.10  ? 231  VAL A CG1 1 
ATOM   1738  C  CG2 . VAL A 1 222 ? 56.798  94.667  -1.597  1.00 36.53  ? 231  VAL A CG2 1 
ATOM   1739  N  N   . SER A 1 223 ? 56.158  97.441  -5.298  1.00 32.42  ? 232  SER A N   1 
ATOM   1740  C  CA  . SER A 1 223 ? 56.021  98.721  -5.998  1.00 32.89  ? 232  SER A CA  1 
ATOM   1741  C  C   . SER A 1 223 ? 54.690  98.883  -6.561  1.00 30.68  ? 232  SER A C   1 
ATOM   1742  O  O   . SER A 1 223 ? 54.192  100.011 -6.539  1.00 31.62  ? 232  SER A O   1 
ATOM   1743  C  CB  . SER A 1 223 ? 57.050  98.867  -7.128  1.00 39.32  ? 232  SER A CB  1 
ATOM   1744  O  OG  . SER A 1 223 ? 58.324  98.595  -6.569  1.00 46.69  ? 232  SER A OG  1 
ATOM   1745  N  N   . GLN A 1 224 ? 54.057  97.838  -7.074  1.00 28.62  ? 233  GLN A N   1 
ATOM   1746  C  CA  . GLN A 1 224 ? 52.713  98.082  -7.623  1.00 29.09  ? 233  GLN A CA  1 
ATOM   1747  C  C   . GLN A 1 224 ? 51.690  98.408  -6.487  1.00 25.50  ? 233  GLN A C   1 
ATOM   1748  O  O   . GLN A 1 224 ? 50.746  99.153  -6.706  1.00 26.11  ? 233  GLN A O   1 
ATOM   1749  C  CB  . GLN A 1 224 ? 52.187  96.896  -8.417  1.00 32.00  ? 233  GLN A CB  1 
ATOM   1750  C  CG  . GLN A 1 224 ? 52.959  96.682  -9.699  1.00 38.50  ? 233  GLN A CG  1 
ATOM   1751  C  CD  . GLN A 1 224 ? 52.205  95.745  -10.628 1.00 45.83  ? 233  GLN A CD  1 
ATOM   1752  O  OE1 . GLN A 1 224 ? 51.044  95.419  -10.436 1.00 42.75  ? 233  GLN A OE1 1 
ATOM   1753  N  NE2 . GLN A 1 224 ? 52.878  95.269  -11.670 1.00 52.34  ? 233  GLN A NE2 1 
ATOM   1754  N  N   . ILE A 1 225 ? 51.912  97.859  -5.292  1.00 25.60  ? 234  ILE A N   1 
ATOM   1755  C  CA  . ILE A 1 225 ? 51.002  98.171  -4.186  1.00 23.51  ? 234  ILE A CA  1 
ATOM   1756  C  C   . ILE A 1 225 ? 51.192  99.656  -3.853  1.00 25.43  ? 234  ILE A C   1 
ATOM   1757  O  O   . ILE A 1 225 ? 50.204  100.372 -3.729  1.00 26.60  ? 234  ILE A O   1 
ATOM   1758  C  CB  . ILE A 1 225 ? 51.402  97.292  -2.987  1.00 24.17  ? 234  ILE A CB  1 
ATOM   1759  C  CG1 . ILE A 1 225 ? 50.938  95.800  -3.282  1.00 25.09  ? 234  ILE A CG1 1 
ATOM   1760  C  CG2 . ILE A 1 225 ? 50.759  97.834  -1.668  1.00 21.01  ? 234  ILE A CG2 1 
ATOM   1761  C  CD1 . ILE A 1 225 ? 51.518  94.849  -2.237  1.00 24.72  ? 234  ILE A CD1 1 
ATOM   1762  N  N   . LYS A 1 226 ? 52.448  100.117 -3.719  1.00 23.07  ? 235  LYS A N   1 
ATOM   1763  C  CA  . LYS A 1 226 ? 52.636  101.552 -3.355  1.00 28.24  ? 235  LYS A CA  1 
ATOM   1764  C  C   . LYS A 1 226 ? 52.164  102.482 -4.473  1.00 29.03  ? 235  LYS A C   1 
ATOM   1765  O  O   . LYS A 1 226 ? 51.834  103.646 -4.209  1.00 28.48  ? 235  LYS A O   1 
ATOM   1766  C  CB  . LYS A 1 226 ? 54.098  101.827 -3.015  1.00 25.60  ? 235  LYS A CB  1 
ATOM   1767  C  CG  . LYS A 1 226 ? 54.482  101.123 -1.736  1.00 26.62  ? 235  LYS A CG  1 
ATOM   1768  C  CD  . LYS A 1 226 ? 55.979  101.280 -1.508  1.00 35.69  ? 235  LYS A CD  1 
ATOM   1769  C  CE  . LYS A 1 226 ? 56.247  101.233 -0.041  1.00 45.93  ? 235  LYS A CE  1 
ATOM   1770  N  NZ  . LYS A 1 226 ? 57.641  100.835 0.260   1.00 56.63  ? 235  LYS A NZ  1 
ATOM   1771  N  N   . SER A 1 227 ? 52.117  102.005 -5.721  1.00 27.49  ? 236  SER A N   1 
ATOM   1772  C  CA  . SER A 1 227 ? 51.607  102.872 -6.782  1.00 28.76  ? 236  SER A CA  1 
ATOM   1773  C  C   . SER A 1 227 ? 50.163  102.997 -6.625  1.00 28.70  ? 236  SER A C   1 
ATOM   1774  O  O   . SER A 1 227 ? 49.594  104.018 -7.010  1.00 29.85  ? 236  SER A O   1 
ATOM   1775  C  CB  . SER A 1 227 ? 51.865  102.285 -8.164  1.00 30.80  ? 236  SER A CB  1 
ATOM   1776  O  OG  . SER A 1 227 ? 53.228  102.530 -8.436  1.00 42.86  ? 236  SER A OG  1 
ATOM   1777  N  N   . ALA A 1 228 ? 49.524  101.985 -6.079  1.00 26.76  ? 237  ALA A N   1 
ATOM   1778  C  CA  . ALA A 1 228 ? 48.090  102.098 -5.880  1.00 26.30  ? 237  ALA A CA  1 
ATOM   1779  C  C   . ALA A 1 228 ? 47.804  103.027 -4.725  1.00 26.71  ? 237  ALA A C   1 
ATOM   1780  O  O   . ALA A 1 228 ? 46.983  103.935 -4.877  1.00 26.32  ? 237  ALA A O   1 
ATOM   1781  C  CB  . ALA A 1 228 ? 47.467  100.712 -5.600  1.00 28.35  ? 237  ALA A CB  1 
ATOM   1782  N  N   . VAL A 1 229 ? 48.448  102.809 -3.565  1.00 23.91  ? 238  VAL A N   1 
ATOM   1783  C  CA  . VAL A 1 229 ? 48.244  103.621 -2.363  1.00 23.53  ? 238  VAL A CA  1 
ATOM   1784  C  C   . VAL A 1 229 ? 49.608  103.668 -1.726  1.00 24.22  ? 238  VAL A C   1 
ATOM   1785  O  O   . VAL A 1 229 ? 50.206  102.601 -1.519  1.00 21.51  ? 238  VAL A O   1 
ATOM   1786  C  CB  A VAL A 1 229 ? 47.192  103.008 -1.401  0.59 26.65  ? 238  VAL A CB  1 
ATOM   1787  C  CB  B VAL A 1 229 ? 47.235  102.914 -1.356  0.41 26.82  ? 238  VAL A CB  1 
ATOM   1788  C  CG1 A VAL A 1 229 ? 46.949  103.937 -0.198  0.59 23.95  ? 238  VAL A CG1 1 
ATOM   1789  C  CG1 B VAL A 1 229 ? 45.813  103.114 -1.884  0.41 25.36  ? 238  VAL A CG1 1 
ATOM   1790  C  CG2 A VAL A 1 229 ? 45.877  102.766 -2.160  0.59 25.30  ? 238  VAL A CG2 1 
ATOM   1791  C  CG2 B VAL A 1 229 ? 47.503  101.422 -1.170  0.41 22.49  ? 238  VAL A CG2 1 
ATOM   1792  N  N   . ASN A 1 230 ? 50.132  104.895 -1.424  1.00 18.87  ? 239  ASN A N   1 
ATOM   1793  C  CA  . ASN A 1 230 ? 51.492  105.009 -0.909  1.00 18.42  ? 239  ASN A CA  1 
ATOM   1794  C  C   . ASN A 1 230 ? 51.588  104.666 0.553   1.00 19.02  ? 239  ASN A C   1 
ATOM   1795  O  O   . ASN A 1 230 ? 51.937  105.502 1.393   1.00 20.77  ? 239  ASN A O   1 
ATOM   1796  C  CB  . ASN A 1 230 ? 52.025  106.422 -1.136  1.00 18.54  ? 239  ASN A CB  1 
ATOM   1797  C  CG  . ASN A 1 230 ? 53.516  106.468 -0.940  1.00 23.18  ? 239  ASN A CG  1 
ATOM   1798  O  OD1 . ASN A 1 230 ? 54.200  105.451 -1.226  1.00 23.90  ? 239  ASN A OD1 1 
ATOM   1799  N  ND2 . ASN A 1 230 ? 54.122  107.558 -0.504  1.00 21.22  ? 239  ASN A ND2 1 
ATOM   1800  N  N   . VAL A 1 231 ? 51.309  103.380 0.862   1.00 21.67  ? 240  VAL A N   1 
ATOM   1801  C  CA  . VAL A 1 231 ? 51.347  102.925 2.246   1.00 19.34  ? 240  VAL A CA  1 
ATOM   1802  C  C   . VAL A 1 231 ? 52.749  102.525 2.744   1.00 20.16  ? 240  VAL A C   1 
ATOM   1803  O  O   . VAL A 1 231 ? 53.656  102.334 1.956   1.00 22.42  ? 240  VAL A O   1 
ATOM   1804  C  CB  . VAL A 1 231 ? 50.513  101.609 2.319   1.00 18.10  ? 240  VAL A CB  1 
ATOM   1805  C  CG1 . VAL A 1 231 ? 49.017  101.887 2.051   1.00 20.27  ? 240  VAL A CG1 1 
ATOM   1806  C  CG2 . VAL A 1 231 ? 51.079  100.570 1.304   1.00 21.13  ? 240  VAL A CG2 1 
ATOM   1807  N  N   . ASN A 1 232 ? 52.873  102.372 4.064   1.00 20.63  ? 241  ASN A N   1 
ATOM   1808  C  CA  . ASN A 1 232 ? 54.039  101.766 4.671   1.00 23.77  ? 241  ASN A CA  1 
ATOM   1809  C  C   . ASN A 1 232 ? 53.868  100.285 4.472   1.00 26.32  ? 241  ASN A C   1 
ATOM   1810  O  O   . ASN A 1 232 ? 52.771  99.755  4.779   1.00 24.64  ? 241  ASN A O   1 
ATOM   1811  C  CB  . ASN A 1 232 ? 54.043  102.011 6.127   1.00 25.44  ? 241  ASN A CB  1 
ATOM   1812  C  CG  . ASN A 1 232 ? 54.256  103.463 6.410   1.00 39.56  ? 241  ASN A CG  1 
ATOM   1813  O  OD1 . ASN A 1 232 ? 53.648  103.965 7.360   1.00 47.38  ? 241  ASN A OD1 1 
ATOM   1814  N  ND2 . ASN A 1 232 ? 55.018  104.193 5.596   1.00 38.68  ? 241  ASN A ND2 1 
ATOM   1815  N  N   . VAL A 1 233 ? 54.892  99.586  3.967   1.00 24.52  ? 242  VAL A N   1 
ATOM   1816  C  CA  . VAL A 1 233 ? 54.742  98.161  3.783   1.00 25.87  ? 242  VAL A CA  1 
ATOM   1817  C  C   . VAL A 1 233 ? 55.544  97.360  4.829   1.00 30.19  ? 242  VAL A C   1 
ATOM   1818  O  O   . VAL A 1 233 ? 56.783  97.482  4.883   1.00 27.61  ? 242  VAL A O   1 
ATOM   1819  C  CB  . VAL A 1 233 ? 55.163  97.746  2.379   1.00 26.01  ? 242  VAL A CB  1 
ATOM   1820  C  CG1 . VAL A 1 233 ? 55.148  96.230  2.282   1.00 26.36  ? 242  VAL A CG1 1 
ATOM   1821  C  CG2 . VAL A 1 233 ? 54.227  98.343  1.330   1.00 25.80  ? 242  VAL A CG2 1 
ATOM   1822  N  N   . THR A 1 234 ? 54.870  96.560  5.673   1.00 26.86  ? 243  THR A N   1 
ATOM   1823  C  CA  . THR A 1 234 ? 55.548  95.721  6.665   1.00 23.31  ? 243  THR A CA  1 
ATOM   1824  C  C   . THR A 1 234 ? 55.646  94.362  6.076   1.00 25.14  ? 243  THR A C   1 
ATOM   1825  O  O   . THR A 1 234 ? 54.785  93.947  5.267   1.00 26.51  ? 243  THR A O   1 
ATOM   1826  C  CB  . THR A 1 234 ? 54.723  95.677  7.963   1.00 26.65  ? 243  THR A CB  1 
ATOM   1827  O  OG1 . THR A 1 234 ? 54.894  96.934  8.634   1.00 28.17  ? 243  THR A OG1 1 
ATOM   1828  C  CG2 . THR A 1 234 ? 55.152  94.545  8.925   1.00 30.95  ? 243  THR A CG2 1 
ATOM   1829  N  N   . ARG A 1 235 ? 56.674  93.579  6.438   1.00 25.50  ? 244  ARG A N   1 
ATOM   1830  C  CA  . ARG A 1 235 ? 56.746  92.230  5.865   1.00 28.20  ? 244  ARG A CA  1 
ATOM   1831  C  C   . ARG A 1 235 ? 57.053  91.271  7.003   1.00 27.65  ? 244  ARG A C   1 
ATOM   1832  O  O   . ARG A 1 235 ? 57.907  91.564  7.853   1.00 25.64  ? 244  ARG A O   1 
ATOM   1833  C  CB  . ARG A 1 235 ? 57.869  92.076  4.810   1.00 33.99  ? 244  ARG A CB  1 
ATOM   1834  C  CG  . ARG A 1 235 ? 57.778  90.692  4.106   1.00 35.56  ? 244  ARG A CG  1 
ATOM   1835  C  CD  . ARG A 1 235 ? 58.956  90.434  3.156   1.00 41.73  ? 244  ARG A CD  1 
ATOM   1836  N  NE  . ARG A 1 235 ? 58.889  91.283  1.969   1.00 37.23  ? 244  ARG A NE  1 
ATOM   1837  C  CZ  . ARG A 1 235 ? 58.370  90.884  0.819   1.00 33.18  ? 244  ARG A CZ  1 
ATOM   1838  N  NH1 . ARG A 1 235 ? 57.873  89.659  0.698   1.00 31.87  ? 244  ARG A NH1 1 
ATOM   1839  N  NH2 . ARG A 1 235 ? 58.338  91.705  -0.222  1.00 33.50  ? 244  ARG A NH2 1 
ATOM   1840  N  N   . ILE A 1 236 ? 56.337  90.165  7.035   1.00 27.47  ? 245  ILE A N   1 
ATOM   1841  C  CA  . ILE A 1 236 ? 56.492  89.130  8.068   1.00 29.99  ? 245  ILE A CA  1 
ATOM   1842  C  C   . ILE A 1 236 ? 56.642  87.878  7.249   1.00 30.10  ? 245  ILE A C   1 
ATOM   1843  O  O   . ILE A 1 236 ? 55.710  87.455  6.583   1.00 29.71  ? 245  ILE A O   1 
ATOM   1844  C  CB  . ILE A 1 236 ? 55.297  89.006  8.998   1.00 33.86  ? 245  ILE A CB  1 
ATOM   1845  C  CG1 . ILE A 1 236 ? 55.070  90.325  9.786   1.00 32.93  ? 245  ILE A CG1 1 
ATOM   1846  C  CG2 . ILE A 1 236 ? 55.569  87.833  9.974   1.00 37.03  ? 245  ILE A CG2 1 
ATOM   1847  C  CD1 . ILE A 1 236 ? 53.686  90.409  10.360  1.00 34.16  ? 245  ILE A CD1 1 
ATOM   1848  N  N   . GLY A 1 237 ? 57.829  87.267  7.271   1.00 32.30  ? 246  GLY A N   1 
ATOM   1849  C  CA  . GLY A 1 237 ? 58.046  86.069  6.457   1.00 38.11  ? 246  GLY A CA  1 
ATOM   1850  C  C   . GLY A 1 237 ? 59.360  85.442  6.888   1.00 43.22  ? 246  GLY A C   1 
ATOM   1851  O  O   . GLY A 1 237 ? 60.366  86.141  6.979   1.00 43.23  ? 246  GLY A O   1 
ATOM   1852  N  N   . GLY A 1 238 ? 59.343  84.140  7.191   1.00 42.56  ? 247  GLY A N   1 
ATOM   1853  C  CA  . GLY A 1 238 ? 60.553  83.462  7.620   1.00 41.80  ? 247  GLY A CA  1 
ATOM   1854  C  C   . GLY A 1 238 ? 61.044  82.547  6.521   1.00 41.51  ? 247  GLY A C   1 
ATOM   1855  O  O   . GLY A 1 238 ? 60.541  82.607  5.402   1.00 40.44  ? 247  GLY A O   1 
ATOM   1856  N  N   . VAL A 1 239 ? 62.025  81.649  6.868   1.00 45.47  ? 248  VAL A N   1 
ATOM   1857  C  CA  . VAL A 1 239 ? 62.630  80.704  5.907   1.00 48.50  ? 248  VAL A CA  1 
ATOM   1858  C  C   . VAL A 1 239 ? 61.641  79.656  5.414   1.00 44.98  ? 248  VAL A C   1 
ATOM   1859  O  O   . VAL A 1 239 ? 61.775  79.155  4.311   1.00 43.06  ? 248  VAL A O   1 
ATOM   1860  C  CB  . VAL A 1 239 ? 63.874  80.028  6.568   1.00 52.10  ? 248  VAL A CB  1 
ATOM   1861  C  CG1 . VAL A 1 239 ? 63.469  79.167  7.771   1.00 54.95  ? 248  VAL A CG1 1 
ATOM   1862  C  CG2 . VAL A 1 239 ? 64.613  79.166  5.547   1.00 55.78  ? 248  VAL A CG2 1 
ATOM   1863  N  N   . ASP A 1 240 ? 60.637  79.318  6.231   1.00 38.72  ? 249  ASP A N   1 
ATOM   1864  C  CA  . ASP A 1 240 ? 59.663  78.312  5.851   1.00 32.03  ? 249  ASP A CA  1 
ATOM   1865  C  C   . ASP A 1 240 ? 58.348  78.625  6.592   1.00 28.12  ? 249  ASP A C   1 
ATOM   1866  O  O   . ASP A 1 240 ? 58.331  79.563  7.377   1.00 30.43  ? 249  ASP A O   1 
ATOM   1867  C  CB  . ASP A 1 240 ? 60.170  76.889  6.237   1.00 31.31  ? 249  ASP A CB  1 
ATOM   1868  C  CG  . ASP A 1 240 ? 60.322  76.559  7.726   1.00 39.97  ? 249  ASP A CG  1 
ATOM   1869  O  OD1 . ASP A 1 240 ? 59.909  77.362  8.568   1.00 37.67  ? 249  ASP A OD1 1 
ATOM   1870  O  OD2 . ASP A 1 240 ? 60.860  75.486  8.040   1.00 46.40  ? 249  ASP A OD2 1 
ATOM   1871  N  N   . ARG A 1 241 ? 57.311  77.867  6.362   1.00 31.22  ? 250  ARG A N   1 
ATOM   1872  C  CA  . ARG A 1 241 ? 55.994  78.065  7.030   1.00 30.96  ? 250  ARG A CA  1 
ATOM   1873  C  C   . ARG A 1 241 ? 56.110  78.028  8.515   1.00 28.62  ? 250  ARG A C   1 
ATOM   1874  O  O   . ARG A 1 241 ? 55.411  78.769  9.173   1.00 27.85  ? 250  ARG A O   1 
ATOM   1875  C  CB  . ARG A 1 241 ? 55.053  76.907  6.707   1.00 31.84  ? 250  ARG A CB  1 
ATOM   1876  C  CG  . ARG A 1 241 ? 54.979  76.653  5.246   1.00 36.15  ? 250  ARG A CG  1 
ATOM   1877  C  CD  . ARG A 1 241 ? 54.168  75.444  4.937   1.00 31.05  ? 250  ARG A CD  1 
ATOM   1878  N  NE  . ARG A 1 241 ? 53.850  75.476  3.527   1.00 33.59  ? 250  ARG A NE  1 
ATOM   1879  C  CZ  . ARG A 1 241 ? 52.912  74.736  2.983   1.00 37.02  ? 250  ARG A CZ  1 
ATOM   1880  N  NH1 . ARG A 1 241 ? 52.211  73.902  3.728   1.00 32.45  ? 250  ARG A NH1 1 
ATOM   1881  N  NH2 . ARG A 1 241 ? 52.652  74.824  1.685   1.00 42.04  ? 250  ARG A NH2 1 
ATOM   1882  N  N   . HIS A 1 242 ? 56.975  77.165  9.096   1.00 27.92  ? 251  HIS A N   1 
ATOM   1883  C  CA  . HIS A 1 242 ? 57.014  77.094  10.569  1.00 25.41  ? 251  HIS A CA  1 
ATOM   1884  C  C   . HIS A 1 242 ? 57.514  78.345  11.143  1.00 28.51  ? 251  HIS A C   1 
ATOM   1885  O  O   . HIS A 1 242 ? 56.937  78.827  12.124  1.00 26.84  ? 251  HIS A O   1 
ATOM   1886  C  CB  . HIS A 1 242 ? 57.908  75.933  11.116  1.00 30.13  ? 251  HIS A CB  1 
ATOM   1887  C  CG  . HIS A 1 242 ? 57.705  74.649  10.392  1.00 38.95  ? 251  HIS A CG  1 
ATOM   1888  N  ND1 . HIS A 1 242 ? 56.663  73.794  10.692  1.00 44.06  ? 251  HIS A ND1 1 
ATOM   1889  C  CD2 . HIS A 1 242 ? 58.395  74.076  9.379   1.00 44.28  ? 251  HIS A CD2 1 
ATOM   1890  C  CE1 . HIS A 1 242 ? 56.737  72.754  9.876   1.00 42.54  ? 251  HIS A CE1 1 
ATOM   1891  N  NE2 . HIS A 1 242 ? 57.771  72.894  9.075   1.00 48.15  ? 251  HIS A NE2 1 
ATOM   1892  N  N   . GLU A 1 243 ? 58.604  78.927  10.563  1.00 29.09  ? 252  GLU A N   1 
ATOM   1893  C  CA  . GLU A 1 243 ? 59.131  80.157  11.122  1.00 31.28  ? 252  GLU A CA  1 
ATOM   1894  C  C   . GLU A 1 243 ? 58.137  81.336  10.874  1.00 23.68  ? 252  GLU A C   1 
ATOM   1895  O  O   . GLU A 1 243 ? 57.991  82.163  11.731  1.00 27.51  ? 252  GLU A O   1 
ATOM   1896  C  CB  . GLU A 1 243 ? 60.492  80.549  10.460  1.00 30.26  ? 252  GLU A CB  1 
ATOM   1897  C  CG  . GLU A 1 243 ? 61.158  81.607  11.358  1.00 36.40  ? 252  GLU A CG  1 
ATOM   1898  C  CD  . GLU A 1 243 ? 62.464  82.190  10.744  1.00 41.08  ? 252  GLU A CD  1 
ATOM   1899  O  OE1 . GLU A 1 243 ? 62.746  82.017  9.535   1.00 46.33  ? 252  GLU A OE1 1 
ATOM   1900  O  OE2 . GLU A 1 243 ? 63.167  82.835  11.509  1.00 50.38  ? 252  GLU A OE2 1 
ATOM   1901  N  N   . THR A 1 244 ? 57.541  81.400  9.712   1.00 27.02  ? 253  THR A N   1 
ATOM   1902  C  CA  . THR A 1 244 ? 56.550  82.460  9.469   1.00 25.06  ? 253  THR A CA  1 
ATOM   1903  C  C   . THR A 1 244 ? 55.414  82.393  10.506  1.00 21.79  ? 253  THR A C   1 
ATOM   1904  O  O   . THR A 1 244 ? 55.021  83.437  10.999  1.00 23.70  ? 253  THR A O   1 
ATOM   1905  C  CB  . THR A 1 244 ? 55.989  82.318  8.074   1.00 29.14  ? 253  THR A CB  1 
ATOM   1906  O  OG1 . THR A 1 244 ? 57.083  82.525  7.178   1.00 27.64  ? 253  THR A OG1 1 
ATOM   1907  C  CG2 . THR A 1 244 ? 54.878  83.405  7.790   1.00 29.52  ? 253  THR A CG2 1 
ATOM   1908  N  N   . SER A 1 245 ? 54.919  81.161  10.876  1.00 21.09  ? 254  SER A N   1 
ATOM   1909  C  CA  . SER A 1 245 ? 53.855  81.077  11.876  1.00 22.96  ? 254  SER A CA  1 
ATOM   1910  C  C   . SER A 1 245 ? 54.393  81.577  13.187  1.00 23.24  ? 254  SER A C   1 
ATOM   1911  O  O   . SER A 1 245 ? 53.693  82.224  13.968  1.00 21.68  ? 254  SER A O   1 
ATOM   1912  C  CB  . SER A 1 245 ? 53.294  79.643  11.963  1.00 24.79  ? 254  SER A CB  1 
ATOM   1913  O  OG  . SER A 1 245 ? 54.078  78.711  12.701  1.00 30.78  ? 254  SER A OG  1 
ATOM   1914  N  N   . LEU A 1 246 ? 55.708  81.317  13.464  1.00 23.71  ? 255  LEU A N   1 
ATOM   1915  C  CA  . LEU A 1 246 ? 56.293  81.852  14.707  1.00 20.92  ? 255  LEU A CA  1 
ATOM   1916  C  C   . LEU A 1 246 ? 56.353  83.372  14.630  1.00 17.64  ? 255  LEU A C   1 
ATOM   1917  O  O   . LEU A 1 246 ? 56.019  84.067  15.599  1.00 21.32  ? 255  LEU A O   1 
ATOM   1918  C  CB  . LEU A 1 246 ? 57.823  81.346  14.963  1.00 20.88  ? 255  LEU A CB  1 
ATOM   1919  C  CG  . LEU A 1 246 ? 58.466  82.011  16.231  1.00 27.70  ? 255  LEU A CG  1 
ATOM   1920  C  CD1 . LEU A 1 246 ? 57.651  81.735  17.455  1.00 28.43  ? 255  LEU A CD1 1 
ATOM   1921  C  CD2 . LEU A 1 246 ? 59.967  81.482  16.421  1.00 29.23  ? 255  LEU A CD2 1 
ATOM   1922  N  N   . LEU A 1 247 ? 56.786  83.906  13.497  1.00 20.19  ? 256  LEU A N   1 
ATOM   1923  C  CA  . LEU A 1 247 ? 56.912  85.389  13.395  1.00 22.00  ? 256  LEU A CA  1 
ATOM   1924  C  C   . LEU A 1 247 ? 55.524  86.063  13.499  1.00 20.52  ? 256  LEU A C   1 
ATOM   1925  O  O   . LEU A 1 247 ? 55.393  87.139  14.078  1.00 18.34  ? 256  LEU A O   1 
ATOM   1926  C  CB  . LEU A 1 247 ? 57.574  85.710  12.054  1.00 25.18  ? 256  LEU A CB  1 
ATOM   1927  C  CG  . LEU A 1 247 ? 59.096  85.268  12.038  1.00 28.09  ? 256  LEU A CG  1 
ATOM   1928  C  CD1 . LEU A 1 247 ? 59.613  85.326  10.571  1.00 30.45  ? 256  LEU A CD1 1 
ATOM   1929  C  CD2 . LEU A 1 247 ? 59.869  86.186  13.026  1.00 29.87  ? 256  LEU A CD2 1 
ATOM   1930  N  N   . ILE A 1 248 ? 54.484  85.391  12.978  1.00 20.62  ? 257  ILE A N   1 
ATOM   1931  C  CA  . ILE A 1 248 ? 53.118  85.945  13.108  1.00 18.04  ? 257  ILE A CA  1 
ATOM   1932  C  C   . ILE A 1 248 ? 52.710  85.918  14.569  1.00 20.74  ? 257  ILE A C   1 
ATOM   1933  O  O   . ILE A 1 248 ? 52.140  86.869  15.100  1.00 20.69  ? 257  ILE A O   1 
ATOM   1934  C  CB  . ILE A 1 248 ? 52.200  85.083  12.254  1.00 20.73  ? 257  ILE A CB  1 
ATOM   1935  C  CG1 . ILE A 1 248 ? 52.466  85.408  10.749  1.00 23.45  ? 257  ILE A CG1 1 
ATOM   1936  C  CG2 . ILE A 1 248 ? 50.728  85.335  12.664  1.00 20.00  ? 257  ILE A CG2 1 
ATOM   1937  C  CD1 . ILE A 1 248 ? 51.719  84.472  9.778   1.00 23.46  ? 257  ILE A CD1 1 
ATOM   1938  N  N   . ALA A 1 249 ? 53.039  84.810  15.250  1.00 21.01  ? 258  ALA A N   1 
ATOM   1939  C  CA  . ALA A 1 249 ? 52.696  84.734  16.668  1.00 19.91  ? 258  ALA A CA  1 
ATOM   1940  C  C   . ALA A 1 249 ? 53.409  85.861  17.462  1.00 21.14  ? 258  ALA A C   1 
ATOM   1941  O  O   . ALA A 1 249 ? 52.817  86.431  18.391  1.00 20.77  ? 258  ALA A O   1 
ATOM   1942  C  CB  . ALA A 1 249 ? 53.071  83.334  17.231  1.00 20.33  ? 258  ALA A CB  1 
ATOM   1943  N  N   . LYS A 1 250 ? 54.689  86.147  17.143  1.00 22.26  ? 259  LYS A N   1 
ATOM   1944  C  CA  . LYS A 1 250 ? 55.371  87.235  17.875  1.00 21.11  ? 259  LYS A CA  1 
ATOM   1945  C  C   . LYS A 1 250 ? 54.732  88.590  17.556  1.00 20.89  ? 259  LYS A C   1 
ATOM   1946  O  O   . LYS A 1 250 ? 54.689  89.493  18.410  1.00 24.04  ? 259  LYS A O   1 
ATOM   1947  C  CB  . LYS A 1 250 ? 56.868  87.286  17.449  1.00 23.78  ? 259  LYS A CB  1 
ATOM   1948  C  CG  . LYS A 1 250 ? 57.630  86.043  17.970  1.00 26.31  ? 259  LYS A CG  1 
ATOM   1949  C  CD  . LYS A 1 250 ? 59.101  86.066  17.385  1.00 28.80  ? 259  LYS A CD  1 
ATOM   1950  C  CE  . LYS A 1 250 ? 59.907  84.883  17.868  1.00 37.19  ? 259  LYS A CE  1 
ATOM   1951  N  NZ  . LYS A 1 250 ? 61.357  85.062  17.573  1.00 46.88  ? 259  LYS A NZ  1 
ATOM   1952  N  N   . GLU A 1 251 ? 54.233  88.730  16.315  1.00 21.60  ? 260  GLU A N   1 
ATOM   1953  C  CA  . GLU A 1 251 ? 53.575  89.995  15.964  1.00 22.45  ? 260  GLU A CA  1 
ATOM   1954  C  C   . GLU A 1 251 ? 52.268  90.137  16.776  1.00 22.55  ? 260  GLU A C   1 
ATOM   1955  O  O   . GLU A 1 251 ? 51.983  91.194  17.331  1.00 21.71  ? 260  GLU A O   1 
ATOM   1956  C  CB  . GLU A 1 251 ? 53.326  90.044  14.457  1.00 23.55  ? 260  GLU A CB  1 
ATOM   1957  C  CG  . GLU A 1 251 ? 52.495  91.284  14.080  1.00 32.47  ? 260  GLU A CG  1 
ATOM   1958  C  CD  . GLU A 1 251 ? 53.310  92.612  13.947  1.00 44.39  ? 260  GLU A CD  1 
ATOM   1959  O  OE1 . GLU A 1 251 ? 54.548  92.592  14.138  1.00 35.24  ? 260  GLU A OE1 1 
ATOM   1960  O  OE2 . GLU A 1 251 ? 52.674  93.670  13.627  1.00 45.65  ? 260  GLU A OE2 1 
ATOM   1961  N  N   . ILE A 1 252 ? 51.473  89.030  16.888  1.00 21.19  ? 261  ILE A N   1 
ATOM   1962  C  CA  . ILE A 1 252 ? 50.257  89.137  17.681  1.00 18.91  ? 261  ILE A CA  1 
ATOM   1963  C  C   . ILE A 1 252 ? 50.611  89.516  19.143  1.00 19.45  ? 261  ILE A C   1 
ATOM   1964  O  O   . ILE A 1 252 ? 49.919  90.320  19.773  1.00 20.71  ? 261  ILE A O   1 
ATOM   1965  C  CB  . ILE A 1 252 ? 49.484  87.760  17.623  1.00 17.66  ? 261  ILE A CB  1 
ATOM   1966  C  CG1 . ILE A 1 252 ? 48.946  87.521  16.178  1.00 20.02  ? 261  ILE A CG1 1 
ATOM   1967  C  CG2 . ILE A 1 252 ? 48.318  87.769  18.646  1.00 19.86  ? 261  ILE A CG2 1 
ATOM   1968  C  CD1 . ILE A 1 252 ? 48.471  86.030  15.899  1.00 21.03  ? 261  ILE A CD1 1 
ATOM   1969  N  N   . ASP A 1 253 ? 51.693  88.934  19.661  1.00 20.71  ? 262  ASP A N   1 
ATOM   1970  C  CA  . ASP A 1 253 ? 52.105  89.194  21.047  1.00 24.40  ? 262  ASP A CA  1 
ATOM   1971  C  C   . ASP A 1 253 ? 52.455  90.703  21.308  1.00 26.51  ? 262  ASP A C   1 
ATOM   1972  O  O   . ASP A 1 253 ? 52.479  91.128  22.466  1.00 28.46  ? 262  ASP A O   1 
ATOM   1973  C  CB  . ASP A 1 253 ? 53.318  88.310  21.370  1.00 24.05  ? 262  ASP A CB  1 
ATOM   1974  C  CG  . ASP A 1 253 ? 53.670  88.338  22.808  1.00 33.29  ? 262  ASP A CG  1 
ATOM   1975  O  OD1 . ASP A 1 253 ? 52.827  87.938  23.629  1.00 32.66  ? 262  ASP A OD1 1 
ATOM   1976  O  OD2 . ASP A 1 253 ? 54.760  88.782  23.120  1.00 36.36  ? 262  ASP A OD2 1 
ATOM   1977  N  N   . LYS A 1 254 ? 52.694  91.483  20.253  1.00 26.00  ? 263  LYS A N   1 
ATOM   1978  C  CA  . LYS A 1 254 ? 52.936  92.932  20.431  1.00 22.57  ? 263  LYS A CA  1 
ATOM   1979  C  C   . LYS A 1 254 ? 51.633  93.629  20.718  1.00 27.83  ? 263  LYS A C   1 
ATOM   1980  O  O   . LYS A 1 254 ? 51.643  94.756  21.239  1.00 30.31  ? 263  LYS A O   1 
ATOM   1981  C  CB  . LYS A 1 254 ? 53.495  93.535  19.150  1.00 24.86  ? 263  LYS A CB  1 
ATOM   1982  C  CG  . LYS A 1 254 ? 54.938  93.161  18.827  1.00 25.33  ? 263  LYS A CG  1 
ATOM   1983  C  CD  . LYS A 1 254 ? 55.171  93.673  17.416  1.00 32.62  ? 263  LYS A CD  1 
ATOM   1984  C  CE  . LYS A 1 254 ? 56.632  93.890  17.030  1.00 50.47  ? 263  LYS A CE  1 
ATOM   1985  N  NZ  . LYS A 1 254 ? 56.755  95.003  15.970  1.00 53.33  ? 263  LYS A NZ  1 
ATOM   1986  N  N   . TYR A 1 255 ? 50.476  92.994  20.377  1.00 23.53  ? 264  TYR A N   1 
ATOM   1987  C  CA  . TYR A 1 255 ? 49.150  93.606  20.633  1.00 23.82  ? 264  TYR A CA  1 
ATOM   1988  C  C   . TYR A 1 255 ? 48.520  93.139  21.920  1.00 25.85  ? 264  TYR A C   1 
ATOM   1989  O  O   . TYR A 1 255 ? 47.921  93.938  22.638  1.00 25.79  ? 264  TYR A O   1 
ATOM   1990  C  CB  . TYR A 1 255 ? 48.189  93.235  19.488  1.00 27.68  ? 264  TYR A CB  1 
ATOM   1991  C  CG  . TYR A 1 255 ? 48.503  94.030  18.248  1.00 34.75  ? 264  TYR A CG  1 
ATOM   1992  C  CD1 . TYR A 1 255 ? 49.641  93.756  17.483  1.00 31.30  ? 264  TYR A CD1 1 
ATOM   1993  C  CD2 . TYR A 1 255 ? 47.707  95.111  17.877  1.00 39.97  ? 264  TYR A CD2 1 
ATOM   1994  C  CE1 . TYR A 1 255 ? 49.993  94.570  16.392  1.00 31.94  ? 264  TYR A CE1 1 
ATOM   1995  C  CE2 . TYR A 1 255 ? 48.043  95.914  16.789  1.00 42.25  ? 264  TYR A CE2 1 
ATOM   1996  C  CZ  . TYR A 1 255 ? 49.187  95.652  16.060  1.00 37.89  ? 264  TYR A CZ  1 
ATOM   1997  O  OH  . TYR A 1 255 ? 49.451  96.507  15.016  1.00 47.69  ? 264  TYR A OH  1 
ATOM   1998  N  N   . HIS A 1 256 ? 48.604  91.819  22.210  1.00 26.58  ? 265  HIS A N   1 
ATOM   1999  C  CA  . HIS A 1 256 ? 48.046  91.301  23.464  1.00 26.58  ? 265  HIS A CA  1 
ATOM   2000  C  C   . HIS A 1 256 ? 48.769  89.989  23.729  1.00 26.84  ? 265  HIS A C   1 
ATOM   2001  O  O   . HIS A 1 256 ? 49.389  89.431  22.824  1.00 27.21  ? 265  HIS A O   1 
ATOM   2002  C  CB  . HIS A 1 256 ? 46.522  91.094  23.398  1.00 24.53  ? 265  HIS A CB  1 
ATOM   2003  C  CG  . HIS A 1 256 ? 46.101  90.285  22.217  1.00 28.55  ? 265  HIS A CG  1 
ATOM   2004  N  ND1 . HIS A 1 256 ? 45.588  90.870  21.076  1.00 29.17  ? 265  HIS A ND1 1 
ATOM   2005  C  CD2 . HIS A 1 256 ? 46.127  88.948  21.990  1.00 27.36  ? 265  HIS A CD2 1 
ATOM   2006  C  CE1 . HIS A 1 256 ? 45.340  89.912  20.197  1.00 30.53  ? 265  HIS A CE1 1 
ATOM   2007  N  NE2 . HIS A 1 256 ? 45.654  88.741  20.717  1.00 25.83  ? 265  HIS A NE2 1 
ATOM   2008  N  N   . ASP A 1 257 ? 48.682  89.487  24.954  1.00 26.11  ? 266  ASP A N   1 
ATOM   2009  C  CA  . ASP A 1 257 ? 49.450  88.288  25.239  1.00 27.89  ? 266  ASP A CA  1 
ATOM   2010  C  C   . ASP A 1 257 ? 49.046  87.049  24.479  1.00 25.83  ? 266  ASP A C   1 
ATOM   2011  O  O   . ASP A 1 257 ? 47.856  86.740  24.376  1.00 27.95  ? 266  ASP A O   1 
ATOM   2012  C  CB  . ASP A 1 257 ? 49.324  87.943  26.755  1.00 33.40  ? 266  ASP A CB  1 
ATOM   2013  C  CG  . ASP A 1 257 ? 50.027  88.941  27.690  1.00 43.94  ? 266  ASP A CG  1 
ATOM   2014  O  OD1 . ASP A 1 257 ? 49.725  88.932  28.887  1.00 48.38  ? 266  ASP A OD1 1 
ATOM   2015  O  OD2 . ASP A 1 257 ? 50.866  89.735  27.202  1.00 44.60  ? 266  ASP A OD2 1 
ATOM   2016  N  N   . VAL A 1 258 ? 50.025  86.344  23.985  1.00 26.50  ? 267  VAL A N   1 
ATOM   2017  C  CA  . VAL A 1 258 ? 49.748  85.061  23.390  1.00 27.08  ? 267  VAL A CA  1 
ATOM   2018  C  C   . VAL A 1 258 ? 49.756  84.027  24.542  1.00 31.15  ? 267  VAL A C   1 
ATOM   2019  O  O   . VAL A 1 258 ? 50.792  83.836  25.173  1.00 32.37  ? 267  VAL A O   1 
ATOM   2020  C  CB  . VAL A 1 258 ? 50.775  84.719  22.316  1.00 27.66  ? 267  VAL A CB  1 
ATOM   2021  C  CG1 . VAL A 1 258 ? 50.713  83.222  21.966  1.00 29.99  ? 267  VAL A CG1 1 
ATOM   2022  C  CG2 . VAL A 1 258 ? 50.491  85.564  21.066  1.00 27.87  ? 267  VAL A CG2 1 
ATOM   2023  N  N   . ASN A 1 259 ? 48.615  83.389  24.828  1.00 29.06  ? 268  ASN A N   1 
ATOM   2024  C  CA  . ASN A 1 259 ? 48.606  82.379  25.888  1.00 30.85  ? 268  ASN A CA  1 
ATOM   2025  C  C   . ASN A 1 259 ? 47.895  81.093  25.476  1.00 28.43  ? 268  ASN A C   1 
ATOM   2026  O  O   . ASN A 1 259 ? 47.693  80.216  26.291  1.00 27.38  ? 268  ASN A O   1 
ATOM   2027  C  CB  . ASN A 1 259 ? 47.985  82.941  27.138  1.00 33.41  ? 268  ASN A CB  1 
ATOM   2028  C  CG  . ASN A 1 259 ? 46.614  83.448  26.930  1.00 44.54  ? 268  ASN A CG  1 
ATOM   2029  O  OD1 . ASN A 1 259 ? 45.940  83.129  25.931  1.00 47.61  ? 268  ASN A OD1 1 
ATOM   2030  N  ND2 . ASN A 1 259 ? 46.154  84.328  27.800  1.00 54.09  ? 268  ASN A ND2 1 
ATOM   2031  N  N   . LYS A 1 260 ? 47.531  80.980  24.208  1.00 24.36  ? 269  LYS A N   1 
ATOM   2032  C  CA  . LYS A 1 260 ? 46.874  79.786  23.700  1.00 24.08  ? 269  LYS A CA  1 
ATOM   2033  C  C   . LYS A 1 260 ? 47.394  79.540  22.280  1.00 23.34  ? 269  LYS A C   1 
ATOM   2034  O  O   . LYS A 1 260 ? 47.616  80.515  21.541  1.00 24.17  ? 269  LYS A O   1 
ATOM   2035  C  CB  . LYS A 1 260 ? 45.342  80.014  23.675  1.00 24.80  ? 269  LYS A CB  1 
ATOM   2036  C  CG  . LYS A 1 260 ? 44.631  79.121  22.664  1.00 32.86  ? 269  LYS A CG  1 
ATOM   2037  C  CD  . LYS A 1 260 ? 43.098  78.935  23.036  1.00 39.18  ? 269  LYS A CD  1 
ATOM   2038  C  CE  . LYS A 1 260 ? 42.434  80.143  23.604  1.00 40.98  ? 269  LYS A CE  1 
ATOM   2039  N  NZ  . LYS A 1 260 ? 40.916  79.978  23.630  1.00 38.35  ? 269  LYS A NZ  1 
ATOM   2040  N  N   . ILE A 1 261 ? 47.624  78.283  21.891  1.00 19.96  ? 270  ILE A N   1 
ATOM   2041  C  CA  . ILE A 1 261 ? 48.040  78.028  20.526  1.00 17.89  ? 270  ILE A CA  1 
ATOM   2042  C  C   . ILE A 1 261 ? 47.223  76.872  19.948  1.00 23.06  ? 270  ILE A C   1 
ATOM   2043  O  O   . ILE A 1 261 ? 46.747  75.997  20.661  1.00 21.66  ? 270  ILE A O   1 
ATOM   2044  C  CB  . ILE A 1 261 ? 49.555  77.707  20.389  1.00 22.59  ? 270  ILE A CB  1 
ATOM   2045  C  CG1 . ILE A 1 261 ? 49.938  76.465  21.229  1.00 22.45  ? 270  ILE A CG1 1 
ATOM   2046  C  CG2 . ILE A 1 261 ? 50.375  78.953  20.806  1.00 21.52  ? 270  ILE A CG2 1 
ATOM   2047  C  CD1 . ILE A 1 261 ? 51.415  76.070  20.974  1.00 21.60  ? 270  ILE A CD1 1 
ATOM   2048  N  N   . TYR A 1 262 ? 47.027  76.919  18.636  1.00 18.91  ? 271  TYR A N   1 
ATOM   2049  C  CA  . TYR A 1 262 ? 46.353  75.884  17.905  1.00 19.01  ? 271  TYR A CA  1 
ATOM   2050  C  C   . TYR A 1 262 ? 47.436  75.359  17.009  1.00 18.84  ? 271  TYR A C   1 
ATOM   2051  O  O   . TYR A 1 262 ? 47.906  76.071  16.146  1.00 20.60  ? 271  TYR A O   1 
ATOM   2052  C  CB  . TYR A 1 262 ? 45.197  76.473  17.050  1.00 17.33  ? 271  TYR A CB  1 
ATOM   2053  C  CG  . TYR A 1 262 ? 44.068  76.992  17.930  1.00 18.09  ? 271  TYR A CG  1 
ATOM   2054  C  CD1 . TYR A 1 262 ? 43.083  76.136  18.410  1.00 17.28  ? 271  TYR A CD1 1 
ATOM   2055  C  CD2 . TYR A 1 262 ? 43.991  78.329  18.280  1.00 17.99  ? 271  TYR A CD2 1 
ATOM   2056  C  CE1 . TYR A 1 262 ? 42.040  76.596  19.193  1.00 18.13  ? 271  TYR A CE1 1 
ATOM   2057  C  CE2 . TYR A 1 262 ? 42.957  78.807  19.099  1.00 18.20  ? 271  TYR A CE2 1 
ATOM   2058  C  CZ  . TYR A 1 262 ? 41.982  77.927  19.546  1.00 18.38  ? 271  TYR A CZ  1 
ATOM   2059  O  OH  . TYR A 1 262 ? 40.971  78.330  20.368  1.00 22.88  ? 271  TYR A OH  1 
ATOM   2060  N  N   . ILE A 1 263 ? 47.832  74.069  17.184  1.00 19.18  ? 272  ILE A N   1 
ATOM   2061  C  CA  . ILE A 1 263 ? 48.931  73.514  16.383  1.00 20.02  ? 272  ILE A CA  1 
ATOM   2062  C  C   . ILE A 1 263 ? 48.426  72.693  15.205  1.00 21.24  ? 272  ILE A C   1 
ATOM   2063  O  O   . ILE A 1 263 ? 47.449  71.912  15.339  1.00 20.52  ? 272  ILE A O   1 
ATOM   2064  C  CB  . ILE A 1 263 ? 49.759  72.606  17.333  1.00 24.40  ? 272  ILE A CB  1 
ATOM   2065  C  CG1 . ILE A 1 263 ? 50.412  73.469  18.425  1.00 26.46  ? 272  ILE A CG1 1 
ATOM   2066  C  CG2 . ILE A 1 263 ? 50.811  71.863  16.533  1.00 22.79  ? 272  ILE A CG2 1 
ATOM   2067  C  CD1 . ILE A 1 263 ? 50.961  72.610  19.605  1.00 25.77  ? 272  ILE A CD1 1 
ATOM   2068  N  N   . ALA A 1 264 ? 49.057  72.836  14.068  1.00 17.07  ? 273  ALA A N   1 
ATOM   2069  C  CA  . ALA A 1 264 ? 48.748  71.995  12.900  1.00 20.46  ? 273  ALA A CA  1 
ATOM   2070  C  C   . ALA A 1 264 ? 50.105  71.607  12.270  1.00 22.98  ? 273  ALA A C   1 
ATOM   2071  O  O   . ALA A 1 264 ? 51.124  72.301  12.492  1.00 21.11  ? 273  ALA A O   1 
ATOM   2072  C  CB  . ALA A 1 264 ? 47.910  72.751  11.846  1.00 22.26  ? 273  ALA A CB  1 
ATOM   2073  N  N   . ASN A 1 265 ? 50.111  70.506  11.490  1.00 24.83  ? 274  ASN A N   1 
ATOM   2074  C  CA  . ASN A 1 265 ? 51.341  70.076  10.808  1.00 25.69  ? 274  ASN A CA  1 
ATOM   2075  C  C   . ASN A 1 265 ? 51.537  71.037  9.619   1.00 24.39  ? 274  ASN A C   1 
ATOM   2076  O  O   . ASN A 1 265 ? 50.663  71.145  8.804   1.00 24.72  ? 274  ASN A O   1 
ATOM   2077  C  CB  . ASN A 1 265 ? 51.199  68.614  10.374  1.00 26.30  ? 274  ASN A CB  1 
ATOM   2078  C  CG  . ASN A 1 265 ? 52.493  68.100  9.803   1.00 32.17  ? 274  ASN A CG  1 
ATOM   2079  O  OD1 . ASN A 1 265 ? 53.011  68.698  8.848   1.00 29.24  ? 274  ASN A OD1 1 
ATOM   2080  N  ND2 . ASN A 1 265 ? 53.066  67.014  10.341  1.00 29.48  ? 274  ASN A ND2 1 
ATOM   2081  N  N   . GLY A 1 266 ? 52.678  71.757  9.577   1.00 23.34  ? 275  GLY A N   1 
ATOM   2082  C  CA  . GLY A 1 266 ? 52.924  72.766  8.550   1.00 23.87  ? 275  GLY A CA  1 
ATOM   2083  C  C   . GLY A 1 266 ? 52.753  72.293  7.138   1.00 26.66  ? 275  GLY A C   1 
ATOM   2084  O  O   . GLY A 1 266 ? 52.080  72.937  6.338   1.00 23.83  ? 275  GLY A O   1 
ATOM   2085  N  N   . TYR A 1 267 ? 53.391  71.142  6.788   1.00 27.21  ? 276  TYR A N   1 
ATOM   2086  C  CA  . TYR A 1 267 ? 53.325  70.683  5.412   1.00 29.23  ? 276  TYR A CA  1 
ATOM   2087  C  C   . TYR A 1 267 ? 52.301  69.565  5.209   1.00 31.46  ? 276  TYR A C   1 
ATOM   2088  O  O   . TYR A 1 267 ? 51.804  69.381  4.094   1.00 32.83  ? 276  TYR A O   1 
ATOM   2089  C  CB  . TYR A 1 267 ? 54.742  70.222  4.929   1.00 27.44  ? 276  TYR A CB  1 
ATOM   2090  C  CG  . TYR A 1 267 ? 55.627  71.422  4.681   1.00 29.51  ? 276  TYR A CG  1 
ATOM   2091  C  CD1 . TYR A 1 267 ? 55.671  72.033  3.436   1.00 32.74  ? 276  TYR A CD1 1 
ATOM   2092  C  CD2 . TYR A 1 267 ? 56.395  71.971  5.705   1.00 34.76  ? 276  TYR A CD2 1 
ATOM   2093  C  CE1 . TYR A 1 267 ? 56.454  73.160  3.216   1.00 33.27  ? 276  TYR A CE1 1 
ATOM   2094  C  CE2 . TYR A 1 267 ? 57.178  73.098  5.493   1.00 34.09  ? 276  TYR A CE2 1 
ATOM   2095  C  CZ  . TYR A 1 267 ? 57.202  73.686  4.248   1.00 40.00  ? 276  TYR A CZ  1 
ATOM   2096  O  OH  . TYR A 1 267 ? 57.973  74.801  4.035   1.00 55.38  ? 276  TYR A OH  1 
ATOM   2097  N  N   . ALA A 1 268 ? 51.958  68.830  6.255   1.00 30.83  ? 277  ALA A N   1 
ATOM   2098  C  CA  . ALA A 1 268 ? 50.987  67.777  6.003   1.00 31.91  ? 277  ALA A CA  1 
ATOM   2099  C  C   . ALA A 1 268 ? 49.604  68.150  6.561   1.00 37.36  ? 277  ALA A C   1 
ATOM   2100  O  O   . ALA A 1 268 ? 48.676  67.363  6.399   1.00 38.59  ? 277  ALA A O   1 
ATOM   2101  C  CB  . ALA A 1 268 ? 51.453  66.475  6.665   1.00 34.75  ? 277  ALA A CB  1 
ATOM   2102  N  N   . GLY A 1 269 ? 49.439  69.342  7.213   1.00 34.55  ? 278  GLY A N   1 
ATOM   2103  C  CA  . GLY A 1 269 ? 48.129  69.661  7.765   1.00 30.31  ? 278  GLY A CA  1 
ATOM   2104  C  C   . GLY A 1 269 ? 47.617  71.010  7.339   1.00 28.20  ? 278  GLY A C   1 
ATOM   2105  O  O   . GLY A 1 269 ? 47.148  71.805  8.159   1.00 26.77  ? 278  GLY A O   1 
ATOM   2106  N  N   . GLU A 1 270 ? 47.723  71.280  6.043   1.00 28.21  ? 279  GLU A N   1 
ATOM   2107  C  CA  . GLU A 1 270 ? 47.250  72.550  5.511   1.00 30.62  ? 279  GLU A CA  1 
ATOM   2108  C  C   . GLU A 1 270 ? 45.745  72.708  5.794   1.00 28.97  ? 279  GLU A C   1 
ATOM   2109  O  O   . GLU A 1 270 ? 45.310  73.792  6.193   1.00 26.04  ? 279  GLU A O   1 
ATOM   2110  C  CB  . GLU A 1 270 ? 47.509  72.610  3.998   1.00 32.68  ? 279  GLU A CB  1 
ATOM   2111  C  CG  . GLU A 1 270 ? 48.994  72.793  3.688   1.00 36.92  ? 279  GLU A CG  1 
ATOM   2112  C  CD  . GLU A 1 270 ? 49.297  72.834  2.159   1.00 47.17  ? 279  GLU A CD  1 
ATOM   2113  O  OE1 . GLU A 1 270 ? 50.493  72.975  1.803   1.00 47.40  ? 279  GLU A OE1 1 
ATOM   2114  O  OE2 . GLU A 1 270 ? 48.350  72.755  1.337   1.00 48.16  ? 279  GLU A OE2 1 
ATOM   2115  N  N   . TYR A 1 271 ? 44.939  71.624  5.554   1.00 27.81  ? 280  TYR A N   1 
ATOM   2116  C  CA  . TYR A 1 271 ? 43.503  71.725  5.817   1.00 25.45  ? 280  TYR A CA  1 
ATOM   2117  C  C   . TYR A 1 271 ? 43.243  71.699  7.308   1.00 23.25  ? 280  TYR A C   1 
ATOM   2118  O  O   . TYR A 1 271 ? 42.223  72.207  7.735   1.00 22.53  ? 280  TYR A O   1 
ATOM   2119  C  CB  . TYR A 1 271 ? 42.720  70.612  5.115   1.00 26.81  ? 280  TYR A CB  1 
ATOM   2120  C  CG  . TYR A 1 271 ? 42.412  71.048  3.704   1.00 27.20  ? 280  TYR A CG  1 
ATOM   2121  C  CD1 . TYR A 1 271 ? 43.275  70.739  2.653   1.00 32.74  ? 280  TYR A CD1 1 
ATOM   2122  C  CD2 . TYR A 1 271 ? 41.272  71.785  3.418   1.00 27.30  ? 280  TYR A CD2 1 
ATOM   2123  C  CE1 . TYR A 1 271 ? 43.001  71.141  1.358   1.00 38.40  ? 280  TYR A CE1 1 
ATOM   2124  C  CE2 . TYR A 1 271 ? 40.997  72.209  2.115   1.00 33.13  ? 280  TYR A CE2 1 
ATOM   2125  C  CZ  . TYR A 1 271 ? 41.861  71.877  1.091   1.00 37.46  ? 280  TYR A CZ  1 
ATOM   2126  O  OH  . TYR A 1 271 ? 41.608  72.268  -0.203  1.00 34.28  ? 280  TYR A OH  1 
ATOM   2127  N  N   . ASP A 1 272 ? 44.133  71.150  8.119   1.00 21.79  ? 281  ASP A N   1 
ATOM   2128  C  CA  . ASP A 1 272 ? 43.937  71.235  9.571   1.00 20.99  ? 281  ASP A CA  1 
ATOM   2129  C  C   . ASP A 1 272 ? 44.059  72.727  9.979   1.00 23.54  ? 281  ASP A C   1 
ATOM   2130  O  O   . ASP A 1 272 ? 43.258  73.262  10.772  1.00 19.65  ? 281  ASP A O   1 
ATOM   2131  C  CB  . ASP A 1 272 ? 45.038  70.413  10.275  1.00 21.97  ? 281  ASP A CB  1 
ATOM   2132  C  CG  . ASP A 1 272 ? 44.832  68.932  10.046  1.00 29.55  ? 281  ASP A CG  1 
ATOM   2133  O  OD1 . ASP A 1 272 ? 43.657  68.471  10.105  1.00 27.93  ? 281  ASP A OD1 1 
ATOM   2134  O  OD2 . ASP A 1 272 ? 45.831  68.219  9.777   1.00 27.13  ? 281  ASP A OD2 1 
ATOM   2135  N  N   . ALA A 1 273 ? 45.108  73.406  9.443   1.00 20.92  ? 282  ALA A N   1 
ATOM   2136  C  CA  . ALA A 1 273 ? 45.339  74.830  9.754   1.00 22.34  ? 282  ALA A CA  1 
ATOM   2137  C  C   . ALA A 1 273 ? 44.089  75.654  9.246   1.00 21.70  ? 282  ALA A C   1 
ATOM   2138  O  O   . ALA A 1 273 ? 43.530  76.488  9.962   1.00 20.42  ? 282  ALA A O   1 
ATOM   2139  C  CB  . ALA A 1 273 ? 46.630  75.302  9.072   1.00 23.14  ? 282  ALA A CB  1 
ATOM   2140  N  N   . LEU A 1 274 ? 43.674  75.411  8.034   1.00 20.29  ? 283  LEU A N   1 
ATOM   2141  C  CA  . LEU A 1 274 ? 42.514  76.110  7.487   1.00 21.41  ? 283  LEU A CA  1 
ATOM   2142  C  C   . LEU A 1 274 ? 41.274  75.862  8.323   1.00 22.08  ? 283  LEU A C   1 
ATOM   2143  O  O   . LEU A 1 274 ? 40.543  76.803  8.648   1.00 19.52  ? 283  LEU A O   1 
ATOM   2144  C  CB  A LEU A 1 274 ? 42.293  75.588  6.073   0.38 22.56  ? 283  LEU A CB  1 
ATOM   2145  C  CB  B LEU A 1 274 ? 42.245  75.469  6.052   0.62 20.39  ? 283  LEU A CB  1 
ATOM   2146  C  CG  A LEU A 1 274 ? 41.561  76.533  5.175   0.38 27.05  ? 283  LEU A CG  1 
ATOM   2147  C  CG  B LEU A 1 274 ? 41.114  76.094  5.215   0.62 24.93  ? 283  LEU A CG  1 
ATOM   2148  C  CD1 A LEU A 1 274 ? 42.507  77.646  4.779   0.38 27.57  ? 283  LEU A CD1 1 
ATOM   2149  C  CD1 B LEU A 1 274 ? 41.261  75.669  3.760   0.62 26.45  ? 283  LEU A CD1 1 
ATOM   2150  C  CD2 A LEU A 1 274 ? 41.038  75.770  3.956   0.38 28.25  ? 283  LEU A CD2 1 
ATOM   2151  C  CD2 B LEU A 1 274 ? 39.754  75.667  5.647   0.62 27.26  ? 283  LEU A CD2 1 
ATOM   2152  N  N   . ASN A 1 275 ? 41.032  74.588  8.706   1.00 18.18  ? 284  ASN A N   1 
ATOM   2153  C  CA  . ASN A 1 275 ? 39.836  74.294  9.499   1.00 20.88  ? 284  ASN A CA  1 
ATOM   2154  C  C   . ASN A 1 275 ? 39.791  75.013  10.865  1.00 18.94  ? 284  ASN A C   1 
ATOM   2155  O  O   . ASN A 1 275 ? 38.709  75.272  11.321  1.00 19.68  ? 284  ASN A O   1 
ATOM   2156  C  CB  . ASN A 1 275 ? 39.746  72.728  9.762   1.00 21.44  ? 284  ASN A CB  1 
ATOM   2157  C  CG  . ASN A 1 275 ? 39.068  72.057  8.554   1.00 22.77  ? 284  ASN A CG  1 
ATOM   2158  O  OD1 . ASN A 1 275 ? 38.172  72.675  7.951   1.00 20.54  ? 284  ASN A OD1 1 
ATOM   2159  N  ND2 . ASN A 1 275 ? 39.481  70.847  8.100   1.00 19.34  ? 284  ASN A ND2 1 
ATOM   2160  N  N   . ILE A 1 276 ? 40.967  75.311  11.533  1.00 18.35  ? 285  ILE A N   1 
ATOM   2161  C  CA  . ILE A 1 276 ? 40.900  75.971  12.847  1.00 17.94  ? 285  ILE A CA  1 
ATOM   2162  C  C   . ILE A 1 276 ? 41.071  77.526  12.723  1.00 19.07  ? 285  ILE A C   1 
ATOM   2163  O  O   . ILE A 1 276 ? 41.016  78.242  13.714  1.00 18.08  ? 285  ILE A O   1 
ATOM   2164  C  CB  . ILE A 1 276 ? 42.013  75.346  13.742  1.00 16.64  ? 285  ILE A CB  1 
ATOM   2165  C  CG1 . ILE A 1 276 ? 41.766  75.707  15.219  1.00 18.83  ? 285  ILE A CG1 1 
ATOM   2166  C  CG2 . ILE A 1 276 ? 43.424  75.856  13.270  1.00 15.57  ? 285  ILE A CG2 1 
ATOM   2167  C  CD1 . ILE A 1 276 ? 40.372  75.195  15.793  1.00 15.38  ? 285  ILE A CD1 1 
ATOM   2168  N  N   . SER A 1 277 ? 41.247  78.010  11.493  1.00 18.03  ? 286  SER A N   1 
ATOM   2169  C  CA  . SER A 1 277 ? 41.512  79.435  11.209  1.00 20.14  ? 286  SER A CA  1 
ATOM   2170  C  C   . SER A 1 277 ? 40.442  80.385  11.756  1.00 21.81  ? 286  SER A C   1 
ATOM   2171  O  O   . SER A 1 277 ? 40.763  81.425  12.367  1.00 18.91  ? 286  SER A O   1 
ATOM   2172  C  CB  . SER A 1 277 ? 41.553  79.634  9.669   1.00 21.00  ? 286  SER A CB  1 
ATOM   2173  O  OG  . SER A 1 277 ? 42.900  79.498  9.308   1.00 36.11  ? 286  SER A OG  1 
ATOM   2174  N  N   . SER A 1 278 ? 39.159  80.052  11.562  1.00 20.26  ? 287  SER A N   1 
ATOM   2175  C  CA  . SER A 1 278 ? 38.159  81.007  12.023  1.00 19.08  ? 287  SER A CA  1 
ATOM   2176  C  C   . SER A 1 278 ? 38.158  81.054  13.522  1.00 19.04  ? 287  SER A C   1 
ATOM   2177  O  O   . SER A 1 278 ? 37.891  82.120  14.084  1.00 19.59  ? 287  SER A O   1 
ATOM   2178  C  CB  . SER A 1 278 ? 36.743  80.685  11.480  1.00 19.36  ? 287  SER A CB  1 
ATOM   2179  O  OG  . SER A 1 278 ? 36.262  79.438  11.985  1.00 19.05  ? 287  SER A OG  1 
ATOM   2180  N  N   . LYS A 1 279 ? 38.481  79.958  14.164  1.00 16.80  ? 288  LYS A N   1 
ATOM   2181  C  CA  . LYS A 1 279 ? 38.400  79.955  15.614  1.00 15.06  ? 288  LYS A CA  1 
ATOM   2182  C  C   . LYS A 1 279 ? 39.660  80.670  16.207  1.00 18.01  ? 288  LYS A C   1 
ATOM   2183  O  O   . LYS A 1 279 ? 39.548  81.503  17.128  1.00 17.84  ? 288  LYS A O   1 
ATOM   2184  C  CB  . LYS A 1 279 ? 38.323  78.486  16.069  1.00 17.79  ? 288  LYS A CB  1 
ATOM   2185  C  CG  . LYS A 1 279 ? 38.481  78.353  17.596  1.00 16.15  ? 288  LYS A CG  1 
ATOM   2186  C  CD  . LYS A 1 279 ? 37.352  79.122  18.350  1.00 21.37  ? 288  LYS A CD  1 
ATOM   2187  C  CE  . LYS A 1 279 ? 37.421  78.802  19.847  1.00 28.12  ? 288  LYS A CE  1 
ATOM   2188  N  NZ  . LYS A 1 279 ? 36.812  79.865  20.684  1.00 33.14  ? 288  LYS A NZ  1 
ATOM   2189  N  N   . ALA A 1 280 ? 40.825  80.324  15.681  1.00 16.39  ? 289  ALA A N   1 
ATOM   2190  C  CA  . ALA A 1 280 ? 42.070  80.994  16.091  1.00 14.67  ? 289  ALA A CA  1 
ATOM   2191  C  C   . ALA A 1 280 ? 41.878  82.543  15.834  1.00 18.53  ? 289  ALA A C   1 
ATOM   2192  O  O   . ALA A 1 280 ? 42.353  83.381  16.590  1.00 18.11  ? 289  ALA A O   1 
ATOM   2193  C  CB  . ALA A 1 280 ? 43.237  80.474  15.207  1.00 14.81  ? 289  ALA A CB  1 
ATOM   2194  N  N   . GLY A 1 281 ? 41.175  82.893  14.700  1.00 16.70  ? 290  GLY A N   1 
ATOM   2195  C  CA  . GLY A 1 281 ? 40.950  84.314  14.392  1.00 18.87  ? 290  GLY A CA  1 
ATOM   2196  C  C   . GLY A 1 281 ? 40.034  84.969  15.401  1.00 18.99  ? 290  GLY A C   1 
ATOM   2197  O  O   . GLY A 1 281 ? 40.294  86.096  15.836  1.00 17.95  ? 290  GLY A O   1 
ATOM   2198  N  N   . GLU A 1 282 ? 38.959  84.313  15.765  1.00 16.24  ? 291  GLU A N   1 
ATOM   2199  C  CA  . GLU A 1 282 ? 38.025  84.894  16.756  1.00 18.61  ? 291  GLU A CA  1 
ATOM   2200  C  C   . GLU A 1 282 ? 38.738  85.082  18.112  1.00 20.74  ? 291  GLU A C   1 
ATOM   2201  O  O   . GLU A 1 282 ? 38.534  86.091  18.766  1.00 19.34  ? 291  GLU A O   1 
ATOM   2202  C  CB  . GLU A 1 282 ? 36.818  83.911  16.975  1.00 19.85  ? 291  GLU A CB  1 
ATOM   2203  C  CG  . GLU A 1 282 ? 35.903  84.385  18.063  1.00 29.08  ? 291  GLU A CG  1 
ATOM   2204  C  CD  . GLU A 1 282 ? 34.753  83.386  18.337  1.00 37.67  ? 291  GLU A CD  1 
ATOM   2205  O  OE1 . GLU A 1 282 ? 34.302  82.724  17.392  1.00 35.32  ? 291  GLU A OE1 1 
ATOM   2206  O  OE2 . GLU A 1 282 ? 34.298  83.315  19.506  1.00 44.15  ? 291  GLU A OE2 1 
ATOM   2207  N  N   . ASP A 1 283 ? 39.588  84.122  18.494  1.00 20.74  ? 292  ASP A N   1 
ATOM   2208  C  CA  . ASP A 1 283 ? 40.330  84.219  19.759  1.00 21.26  ? 292  ASP A CA  1 
ATOM   2209  C  C   . ASP A 1 283 ? 41.533  85.155  19.633  1.00 19.98  ? 292  ASP A C   1 
ATOM   2210  O  O   . ASP A 1 283 ? 42.068  85.557  20.638  1.00 19.10  ? 292  ASP A O   1 
ATOM   2211  C  CB  . ASP A 1 283 ? 40.916  82.856  20.123  1.00 20.95  ? 292  ASP A CB  1 
ATOM   2212  C  CG  . ASP A 1 283 ? 39.875  81.819  20.573  1.00 31.29  ? 292  ASP A CG  1 
ATOM   2213  O  OD1 . ASP A 1 283 ? 38.660  82.157  20.609  1.00 26.59  ? 292  ASP A OD1 1 
ATOM   2214  O  OD2 . ASP A 1 283 ? 40.284  80.677  20.900  1.00 30.72  ? 292  ASP A OD2 1 
ATOM   2215  N  N   . GLN A 1 284 ? 41.956  85.481  18.376  1.00 17.24  ? 293  GLN A N   1 
ATOM   2216  C  CA  . GLN A 1 284 ? 43.184  86.282  18.134  1.00 21.56  ? 293  GLN A CA  1 
ATOM   2217  C  C   . GLN A 1 284 ? 44.349  85.609  18.811  1.00 22.21  ? 293  GLN A C   1 
ATOM   2218  O  O   . GLN A 1 284 ? 45.163  86.274  19.491  1.00 20.74  ? 293  GLN A O   1 
ATOM   2219  C  CB  . GLN A 1 284 ? 43.029  87.749  18.646  1.00 18.41  ? 293  GLN A CB  1 
ATOM   2220  C  CG  . GLN A 1 284 ? 41.836  88.376  17.938  1.00 20.01  ? 293  GLN A CG  1 
ATOM   2221  C  CD  . GLN A 1 284 ? 41.637  89.848  18.307  1.00 26.83  ? 293  GLN A CD  1 
ATOM   2222  O  OE1 . GLN A 1 284 ? 42.547  90.520  18.759  1.00 27.56  ? 293  GLN A OE1 1 
ATOM   2223  N  NE2 . GLN A 1 284 ? 40.432  90.361  18.080  1.00 27.58  ? 293  GLN A NE2 1 
ATOM   2224  N  N   . GLN A 1 285 ? 44.436  84.288  18.654  1.00 18.46  ? 294  GLN A N   1 
ATOM   2225  C  CA  . GLN A 1 285 ? 45.575  83.538  19.241  1.00 19.24  ? 294  GLN A CA  1 
ATOM   2226  C  C   . GLN A 1 285 ? 46.139  82.803  18.051  1.00 19.75  ? 294  GLN A C   1 
ATOM   2227  O  O   . GLN A 1 285 ? 45.435  82.382  17.106  1.00 20.77  ? 294  GLN A O   1 
ATOM   2228  C  CB  . GLN A 1 285 ? 45.142  82.657  20.425  1.00 18.83  ? 294  GLN A CB  1 
ATOM   2229  C  CG  . GLN A 1 285 ? 44.660  83.519  21.591  1.00 24.54  ? 294  GLN A CG  1 
ATOM   2230  C  CD  . GLN A 1 285 ? 45.812  84.163  22.360  1.00 23.87  ? 294  GLN A CD  1 
ATOM   2231  O  OE1 . GLN A 1 285 ? 46.875  83.571  22.580  1.00 24.28  ? 294  GLN A OE1 1 
ATOM   2232  N  NE2 . GLN A 1 285 ? 45.627  85.412  22.742  1.00 24.71  ? 294  GLN A NE2 1 
ATOM   2233  N  N   . PRO A 1 286 ? 47.460  82.617  18.022  1.00 19.73  ? 295  PRO A N   1 
ATOM   2234  C  CA  . PRO A 1 286 ? 48.040  81.974  16.844  1.00 17.79  ? 295  PRO A CA  1 
ATOM   2235  C  C   . PRO A 1 286 ? 47.895  80.496  16.526  1.00 20.73  ? 295  PRO A C   1 
ATOM   2236  O  O   . PRO A 1 286 ? 47.703  79.649  17.385  1.00 18.72  ? 295  PRO A O   1 
ATOM   2237  C  CB  . PRO A 1 286 ? 49.530  82.296  16.985  1.00 22.25  ? 295  PRO A CB  1 
ATOM   2238  C  CG  . PRO A 1 286 ? 49.755  82.445  18.472  1.00 22.62  ? 295  PRO A CG  1 
ATOM   2239  C  CD  . PRO A 1 286 ? 48.424  82.762  19.134  1.00 20.41  ? 295  PRO A CD  1 
ATOM   2240  N  N   . ILE A 1 287 ? 48.033  80.245  15.232  1.00 16.86  ? 296  ILE A N   1 
ATOM   2241  C  CA  . ILE A 1 287 ? 48.139  78.879  14.705  1.00 19.16  ? 296  ILE A CA  1 
ATOM   2242  C  C   . ILE A 1 287 ? 49.664  78.657  14.590  1.00 22.23  ? 296  ILE A C   1 
ATOM   2243  O  O   . ILE A 1 287 ? 50.375  79.443  13.943  1.00 20.38  ? 296  ILE A O   1 
ATOM   2244  C  CB  . ILE A 1 287 ? 47.498  78.734  13.308  1.00 19.01  ? 296  ILE A CB  1 
ATOM   2245  C  CG1 . ILE A 1 287 ? 45.947  78.932  13.401  1.00 18.17  ? 296  ILE A CG1 1 
ATOM   2246  C  CG2 . ILE A 1 287 ? 47.845  77.324  12.735  1.00 20.39  ? 296  ILE A CG2 1 
ATOM   2247  C  CD1 . ILE A 1 287 ? 45.358  79.126  11.938  1.00 19.56  ? 296  ILE A CD1 1 
ATOM   2248  N  N   . ILE A 1 288 ? 50.160  77.619  15.272  1.00 20.82  ? 297  ILE A N   1 
ATOM   2249  C  CA  . ILE A 1 288 ? 51.590  77.342  15.282  1.00 22.20  ? 297  ILE A CA  1 
ATOM   2250  C  C   . ILE A 1 288 ? 51.771  76.142  14.413  1.00 23.74  ? 297  ILE A C   1 
ATOM   2251  O  O   . ILE A 1 288 ? 51.136  75.101  14.630  1.00 22.89  ? 297  ILE A O   1 
ATOM   2252  C  CB  . ILE A 1 288 ? 52.031  77.070  16.731  1.00 22.02  ? 297  ILE A CB  1 
ATOM   2253  C  CG1 . ILE A 1 288 ? 51.976  78.375  17.594  1.00 23.48  ? 297  ILE A CG1 1 
ATOM   2254  C  CG2 . ILE A 1 288 ? 53.471  76.459  16.714  1.00 23.29  ? 297  ILE A CG2 1 
ATOM   2255  C  CD1 . ILE A 1 288 ? 53.032  79.463  17.191  1.00 20.87  ? 297  ILE A CD1 1 
ATOM   2256  N  N   . LEU A 1 289 ? 52.602  76.262  13.394  1.00 24.98  ? 298  LEU A N   1 
ATOM   2257  C  CA  . LEU A 1 289 ? 52.824  75.133  12.526  1.00 22.05  ? 298  LEU A CA  1 
ATOM   2258  C  C   . LEU A 1 289 ? 54.024  74.261  13.022  1.00 24.71  ? 298  LEU A C   1 
ATOM   2259  O  O   . LEU A 1 289 ? 55.077  74.779  13.385  1.00 27.60  ? 298  LEU A O   1 
ATOM   2260  C  CB  . LEU A 1 289 ? 53.053  75.613  11.090  1.00 22.02  ? 298  LEU A CB  1 
ATOM   2261  C  CG  . LEU A 1 289 ? 51.843  76.368  10.527  1.00 24.10  ? 298  LEU A CG  1 
ATOM   2262  C  CD1 . LEU A 1 289 ? 52.147  76.766  9.030   1.00 26.68  ? 298  LEU A CD1 1 
ATOM   2263  C  CD2 . LEU A 1 289 ? 50.572  75.436  10.571  1.00 24.52  ? 298  LEU A CD2 1 
ATOM   2264  N  N   . ALA A 1 290 ? 53.850  72.965  12.985  1.00 27.35  ? 299  ALA A N   1 
ATOM   2265  C  CA  . ALA A 1 290 ? 54.850  72.042  13.530  1.00 29.56  ? 299  ALA A CA  1 
ATOM   2266  C  C   . ALA A 1 290 ? 55.176  70.893  12.591  1.00 27.59  ? 299  ALA A C   1 
ATOM   2267  O  O   . ALA A 1 290 ? 54.613  70.727  11.500  1.00 26.55  ? 299  ALA A O   1 
ATOM   2268  C  CB  . ALA A 1 290 ? 54.289  71.452  14.820  1.00 27.47  ? 299  ALA A CB  1 
ATOM   2269  N  N   . ASN A 1 291 ? 56.183  70.082  13.047  1.00 28.78  ? 300  ASN A N   1 
ATOM   2270  C  CA  . ASN A 1 291 ? 56.536  68.841  12.382  1.00 30.49  ? 300  ASN A CA  1 
ATOM   2271  C  C   . ASN A 1 291 ? 55.711  67.759  13.089  1.00 31.80  ? 300  ASN A C   1 
ATOM   2272  O  O   . ASN A 1 291 ? 55.095  68.026  14.121  1.00 30.43  ? 300  ASN A O   1 
ATOM   2273  C  CB  . ASN A 1 291 ? 58.073  68.549  12.551  1.00 33.09  ? 300  ASN A CB  1 
ATOM   2274  C  CG  . ASN A 1 291 ? 58.868  69.566  11.788  1.00 37.75  ? 300  ASN A CG  1 
ATOM   2275  O  OD1 . ASN A 1 291 ? 58.779  69.583  10.580  1.00 43.15  ? 300  ASN A OD1 1 
ATOM   2276  N  ND2 . ASN A 1 291 ? 59.555  70.509  12.407  1.00 40.95  ? 300  ASN A ND2 1 
ATOM   2277  N  N   . LYS A 1 292 ? 55.720  66.543  12.589  1.00 31.99  ? 301  LYS A N   1 
ATOM   2278  C  CA  . LYS A 1 292 ? 54.954  65.480  13.215  1.00 31.38  ? 301  LYS A CA  1 
ATOM   2279  C  C   . LYS A 1 292 ? 55.292  65.244  14.680  1.00 31.98  ? 301  LYS A C   1 
ATOM   2280  O  O   . LYS A 1 292 ? 54.375  65.065  15.483  1.00 30.47  ? 301  LYS A O   1 
ATOM   2281  C  CB  . LYS A 1 292 ? 55.169  64.192  12.445  1.00 33.68  ? 301  LYS A CB  1 
ATOM   2282  C  CG  . LYS A 1 292 ? 54.399  63.038  13.059  1.00 38.66  ? 301  LYS A CG  1 
ATOM   2283  C  CD  . LYS A 1 292 ? 54.270  61.904  12.051  1.00 45.48  ? 301  LYS A CD  1 
ATOM   2284  C  CE  . LYS A 1 292 ? 54.126  60.581  12.722  1.00 52.34  ? 301  LYS A CE  1 
ATOM   2285  N  NZ  . LYS A 1 292 ? 54.560  59.479  11.819  1.00 56.01  ? 301  LYS A NZ  1 
ATOM   2286  N  N   . ASP A 1 293 ? 56.585  65.244  15.070  1.00 33.14  ? 302  ASP A N   1 
ATOM   2287  C  CA  . ASP A 1 293 ? 56.905  64.970  16.484  1.00 35.01  ? 302  ASP A CA  1 
ATOM   2288  C  C   . ASP A 1 293 ? 57.342  66.139  17.293  1.00 33.43  ? 302  ASP A C   1 
ATOM   2289  O  O   . ASP A 1 293 ? 57.618  65.955  18.489  1.00 34.26  ? 302  ASP A O   1 
ATOM   2290  C  CB  . ASP A 1 293 ? 58.016  63.905  16.603  1.00 41.07  ? 302  ASP A CB  1 
ATOM   2291  C  CG  . ASP A 1 293 ? 57.695  62.652  15.825  1.00 47.07  ? 302  ASP A CG  1 
ATOM   2292  O  OD1 . ASP A 1 293 ? 56.593  62.114  15.999  1.00 42.73  ? 302  ASP A OD1 1 
ATOM   2293  O  OD2 . ASP A 1 293 ? 58.551  62.216  15.036  1.00 52.22  ? 302  ASP A OD2 1 
ATOM   2294  N  N   . SER A 1 294 ? 57.426  67.336  16.743  1.00 30.55  ? 303  SER A N   1 
ATOM   2295  C  CA  . SER A 1 294 ? 57.850  68.431  17.615  1.00 30.38  ? 303  SER A CA  1 
ATOM   2296  C  C   . SER A 1 294 ? 57.646  69.782  16.877  1.00 29.24  ? 303  SER A C   1 
ATOM   2297  O  O   . SER A 1 294 ? 57.529  69.800  15.636  1.00 27.73  ? 303  SER A O   1 
ATOM   2298  C  CB  . SER A 1 294 ? 59.348  68.304  17.929  1.00 31.14  ? 303  SER A CB  1 
ATOM   2299  O  OG  . SER A 1 294 ? 60.055  68.451  16.694  1.00 29.50  ? 303  SER A OG  1 
ATOM   2300  N  N   . VAL A 1 295 ? 57.612  70.863  17.625  1.00 28.48  ? 304  VAL A N   1 
ATOM   2301  C  CA  . VAL A 1 295 ? 57.661  72.157  16.929  1.00 34.69  ? 304  VAL A CA  1 
ATOM   2302  C  C   . VAL A 1 295 ? 59.200  72.428  16.783  1.00 37.97  ? 304  VAL A C   1 
ATOM   2303  O  O   . VAL A 1 295 ? 59.970  71.879  17.584  1.00 35.02  ? 304  VAL A O   1 
ATOM   2304  C  CB  . VAL A 1 295 ? 56.994  73.277  17.755  1.00 34.68  ? 304  VAL A CB  1 
ATOM   2305  C  CG1 . VAL A 1 295 ? 55.518  72.902  18.033  1.00 32.40  ? 304  VAL A CG1 1 
ATOM   2306  C  CG2 . VAL A 1 295 ? 57.743  73.513  19.087  1.00 33.40  ? 304  VAL A CG2 1 
ATOM   2307  N  N   . PRO A 1 296 ? 59.679  73.235  15.823  1.00 37.30  ? 305  PRO A N   1 
ATOM   2308  C  CA  . PRO A 1 296 ? 61.131  73.521  15.678  1.00 37.98  ? 305  PRO A CA  1 
ATOM   2309  C  C   . PRO A 1 296 ? 61.650  74.172  16.939  1.00 37.20  ? 305  PRO A C   1 
ATOM   2310  O  O   . PRO A 1 296 ? 60.887  74.768  17.714  1.00 33.91  ? 305  PRO A O   1 
ATOM   2311  C  CB  . PRO A 1 296 ? 61.174  74.468  14.461  1.00 41.21  ? 305  PRO A CB  1 
ATOM   2312  C  CG  . PRO A 1 296 ? 59.897  74.094  13.677  1.00 42.60  ? 305  PRO A CG  1 
ATOM   2313  C  CD  . PRO A 1 296 ? 58.891  73.894  14.771  1.00 40.69  ? 305  PRO A CD  1 
ATOM   2314  N  N   . GLN A 1 297 ? 62.980  74.123  17.151  1.00 36.12  ? 306  GLN A N   1 
ATOM   2315  C  CA  . GLN A 1 297 ? 63.548  74.652  18.380  1.00 36.27  ? 306  GLN A CA  1 
ATOM   2316  C  C   . GLN A 1 297 ? 63.258  76.109  18.625  1.00 32.89  ? 306  GLN A C   1 
ATOM   2317  O  O   . GLN A 1 297 ? 63.016  76.506  19.763  1.00 29.96  ? 306  GLN A O   1 
ATOM   2318  C  CB  . GLN A 1 297 ? 65.110  74.446  18.359  1.00 41.09  ? 306  GLN A CB  1 
ATOM   2319  C  CG  . GLN A 1 297 ? 65.818  74.776  19.711  1.00 52.29  ? 306  GLN A CG  1 
ATOM   2320  C  CD  . GLN A 1 297 ? 65.349  73.898  20.880  1.00 59.68  ? 306  GLN A CD  1 
ATOM   2321  O  OE1 . GLN A 1 297 ? 65.193  72.676  20.761  1.00 59.45  ? 306  GLN A OE1 1 
ATOM   2322  N  NE2 . GLN A 1 297 ? 65.087  74.513  22.042  1.00 63.05  ? 306  GLN A NE2 1 
ATOM   2323  N  N   . GLY A 1 298 ? 63.335  76.943  17.565  1.00 31.73  ? 307  GLY A N   1 
ATOM   2324  C  CA  . GLY A 1 298 ? 63.084  78.363  17.757  1.00 32.45  ? 307  GLY A CA  1 
ATOM   2325  C  C   . GLY A 1 298 ? 61.677  78.586  18.292  1.00 28.78  ? 307  GLY A C   1 
ATOM   2326  O  O   . GLY A 1 298 ? 61.475  79.386  19.212  1.00 29.91  ? 307  GLY A O   1 
ATOM   2327  N  N   . THR A 1 299 ? 60.709  77.886  17.718  1.00 29.46  ? 308  THR A N   1 
ATOM   2328  C  CA  . THR A 1 299 ? 59.304  78.000  18.202  1.00 29.74  ? 308  THR A CA  1 
ATOM   2329  C  C   . THR A 1 299 ? 59.214  77.542  19.638  1.00 27.84  ? 308  THR A C   1 
ATOM   2330  O  O   . THR A 1 299 ? 58.667  78.237  20.513  1.00 28.15  ? 308  THR A O   1 
ATOM   2331  C  CB  . THR A 1 299 ? 58.448  77.161  17.299  1.00 29.75  ? 308  THR A CB  1 
ATOM   2332  O  OG1 . THR A 1 299 ? 58.647  77.665  15.970  1.00 29.68  ? 308  THR A OG1 1 
ATOM   2333  C  CG2 . THR A 1 299 ? 56.961  77.239  17.650  1.00 26.98  ? 308  THR A CG2 1 
ATOM   2334  N  N   . TYR A 1 300 ? 59.801  76.356  19.906  1.00 30.34  ? 309  TYR A N   1 
ATOM   2335  C  CA  . TYR A 1 300 ? 59.791  75.822  21.273  1.00 27.63  ? 309  TYR A CA  1 
ATOM   2336  C  C   . TYR A 1 300 ? 60.382  76.809  22.261  1.00 28.70  ? 309  TYR A C   1 
ATOM   2337  O  O   . TYR A 1 300 ? 59.813  77.033  23.334  1.00 30.15  ? 309  TYR A O   1 
ATOM   2338  C  CB  . TYR A 1 300 ? 60.542  74.454  21.298  1.00 29.97  ? 309  TYR A CB  1 
ATOM   2339  C  CG  . TYR A 1 300 ? 60.542  73.852  22.690  1.00 33.72  ? 309  TYR A CG  1 
ATOM   2340  C  CD1 . TYR A 1 300 ? 59.437  73.157  23.166  1.00 34.78  ? 309  TYR A CD1 1 
ATOM   2341  C  CD2 . TYR A 1 300 ? 61.638  74.006  23.539  1.00 37.73  ? 309  TYR A CD2 1 
ATOM   2342  C  CE1 . TYR A 1 300 ? 59.419  72.618  24.462  1.00 31.57  ? 309  TYR A CE1 1 
ATOM   2343  C  CE2 . TYR A 1 300 ? 61.633  73.482  24.836  1.00 34.31  ? 309  TYR A CE2 1 
ATOM   2344  C  CZ  . TYR A 1 300 ? 60.526  72.783  25.291  1.00 35.77  ? 309  TYR A CZ  1 
ATOM   2345  O  OH  . TYR A 1 300 ? 60.546  72.241  26.565  1.00 33.05  ? 309  TYR A OH  1 
ATOM   2346  N  N   . ASN A 1 301 ? 61.535  77.464  21.930  1.00 30.48  ? 310  ASN A N   1 
ATOM   2347  C  CA  . ASN A 1 301 ? 62.123  78.384  22.923  1.00 30.55  ? 310  ASN A CA  1 
ATOM   2348  C  C   . ASN A 1 301 ? 61.236  79.564  23.196  1.00 30.57  ? 310  ASN A C   1 
ATOM   2349  O  O   . ASN A 1 301 ? 61.120  79.995  24.338  1.00 29.89  ? 310  ASN A O   1 
ATOM   2350  C  CB  . ASN A 1 301 ? 63.560  78.889  22.460  1.00 33.18  ? 310  ASN A CB  1 
ATOM   2351  C  CG  . ASN A 1 301 ? 64.567  77.740  22.384  1.00 39.49  ? 310  ASN A CG  1 
ATOM   2352  O  OD1 . ASN A 1 301 ? 64.468  76.808  23.192  1.00 46.04  ? 310  ASN A OD1 1 
ATOM   2353  N  ND2 . ASN A 1 301 ? 65.487  77.661  21.408  1.00 42.23  ? 310  ASN A ND2 1 
ATOM   2354  N  N   . TRP A 1 302 ? 60.590  80.104  22.172  1.00 29.91  ? 311  TRP A N   1 
ATOM   2355  C  CA  . TRP A 1 302 ? 59.701  81.268  22.405  1.00 27.34  ? 311  TRP A CA  1 
ATOM   2356  C  C   . TRP A 1 302 ? 58.443  80.808  23.166  1.00 25.71  ? 311  TRP A C   1 
ATOM   2357  O  O   . TRP A 1 302 ? 58.065  81.450  24.147  1.00 26.75  ? 311  TRP A O   1 
ATOM   2358  C  CB  . TRP A 1 302 ? 59.363  81.870  21.016  1.00 26.62  ? 311  TRP A CB  1 
ATOM   2359  C  CG  . TRP A 1 302 ? 58.545  83.127  21.107  1.00 25.69  ? 311  TRP A CG  1 
ATOM   2360  C  CD1 . TRP A 1 302 ? 58.984  84.378  21.401  1.00 29.98  ? 311  TRP A CD1 1 
ATOM   2361  C  CD2 . TRP A 1 302 ? 57.120  83.233  20.963  1.00 29.04  ? 311  TRP A CD2 1 
ATOM   2362  N  NE1 . TRP A 1 302 ? 57.944  85.246  21.472  1.00 32.50  ? 311  TRP A NE1 1 
ATOM   2363  C  CE2 . TRP A 1 302 ? 56.779  84.577  21.193  1.00 32.56  ? 311  TRP A CE2 1 
ATOM   2364  C  CE3 . TRP A 1 302 ? 56.095  82.312  20.638  1.00 30.38  ? 311  TRP A CE3 1 
ATOM   2365  C  CZ2 . TRP A 1 302 ? 55.457  85.039  21.118  1.00 30.19  ? 311  TRP A CZ2 1 
ATOM   2366  C  CZ3 . TRP A 1 302 ? 54.790  82.770  20.564  1.00 26.06  ? 311  TRP A CZ3 1 
ATOM   2367  C  CH2 . TRP A 1 302 ? 54.482  84.126  20.807  1.00 26.80  ? 311  TRP A CH2 1 
ATOM   2368  N  N   . LEU A 1 303 ? 57.805  79.706  22.743  1.00 26.60  ? 312  LEU A N   1 
ATOM   2369  C  CA  . LEU A 1 303 ? 56.595  79.226  23.438  1.00 23.58  ? 312  LEU A CA  1 
ATOM   2370  C  C   . LEU A 1 303 ? 56.907  78.922  24.905  1.00 25.23  ? 312  LEU A C   1 
ATOM   2371  O  O   . LEU A 1 303 ? 56.083  79.184  25.776  1.00 26.36  ? 312  LEU A O   1 
ATOM   2372  C  CB  . LEU A 1 303 ? 56.110  77.932  22.782  1.00 25.04  ? 312  LEU A CB  1 
ATOM   2373  C  CG  . LEU A 1 303 ? 55.537  78.077  21.353  1.00 28.05  ? 312  LEU A CG  1 
ATOM   2374  C  CD1 . LEU A 1 303 ? 55.216  76.663  20.883  1.00 24.56  ? 312  LEU A CD1 1 
ATOM   2375  C  CD2 . LEU A 1 303 ? 54.268  79.027  21.329  1.00 25.48  ? 312  LEU A CD2 1 
ATOM   2376  N  N   . SER A 1 304 ? 58.126  78.366  25.180  1.00 26.63  ? 313  SER A N   1 
ATOM   2377  C  CA  . SER A 1 304 ? 58.467  78.044  26.572  1.00 28.75  ? 313  SER A CA  1 
ATOM   2378  C  C   . SER A 1 304 ? 58.441  79.277  27.410  1.00 31.49  ? 313  SER A C   1 
ATOM   2379  O  O   . SER A 1 304 ? 58.055  79.202  28.568  1.00 32.51  ? 313  SER A O   1 
ATOM   2380  C  CB  . SER A 1 304 ? 59.853  77.396  26.673  1.00 29.97  ? 313  SER A CB  1 
ATOM   2381  O  OG  . SER A 1 304 ? 59.885  76.214  25.902  1.00 32.82  ? 313  SER A OG  1 
ATOM   2382  N  N   . SER A 1 305 ? 58.823  80.442  26.848  1.00 30.28  ? 314  SER A N   1 
ATOM   2383  C  CA  . SER A 1 305 ? 58.807  81.652  27.657  1.00 36.59  ? 314  SER A CA  1 
ATOM   2384  C  C   . SER A 1 305 ? 57.462  82.414  27.633  1.00 36.18  ? 314  SER A C   1 
ATOM   2385  O  O   . SER A 1 305 ? 57.352  83.460  28.287  1.00 33.67  ? 314  SER A O   1 
ATOM   2386  C  CB  . SER A 1 305 ? 59.928  82.587  27.195  1.00 41.15  ? 314  SER A CB  1 
ATOM   2387  O  OG  . SER A 1 305 ? 61.076  81.818  26.887  1.00 49.67  ? 314  SER A OG  1 
ATOM   2388  N  N   . GLN A 1 306 ? 56.460  81.914  26.916  1.00 33.68  ? 315  GLN A N   1 
ATOM   2389  C  CA  . GLN A 1 306 ? 55.164  82.602  26.885  1.00 36.15  ? 315  GLN A CA  1 
ATOM   2390  C  C   . GLN A 1 306 ? 54.247  82.257  28.024  1.00 37.26  ? 315  GLN A C   1 
ATOM   2391  O  O   . GLN A 1 306 ? 53.272  82.971  28.225  1.00 40.13  ? 315  GLN A O   1 
ATOM   2392  C  CB  . GLN A 1 306 ? 54.415  82.272  25.586  1.00 35.95  ? 315  GLN A CB  1 
ATOM   2393  C  CG  . GLN A 1 306 ? 54.969  83.024  24.424  1.00 36.66  ? 315  GLN A CG  1 
ATOM   2394  C  CD  . GLN A 1 306 ? 54.819  84.510  24.699  1.00 39.06  ? 315  GLN A CD  1 
ATOM   2395  O  OE1 . GLN A 1 306 ? 55.799  85.222  24.744  1.00 35.88  ? 315  GLN A OE1 1 
ATOM   2396  N  NE2 . GLN A 1 306 ? 53.576  85.019  24.935  1.00 42.07  ? 315  GLN A NE2 1 
ATOM   2397  N  N   . GLY A 1 307 ? 54.521  81.185  28.783  1.00 36.99  ? 316  GLY A N   1 
ATOM   2398  C  CA  . GLY A 1 307 ? 53.589  80.799  29.836  1.00 37.62  ? 316  GLY A CA  1 
ATOM   2399  C  C   . GLY A 1 307 ? 52.218  80.444  29.253  1.00 36.06  ? 316  GLY A C   1 
ATOM   2400  O  O   . GLY A 1 307 ? 51.191  80.971  29.682  1.00 35.47  ? 316  GLY A O   1 
ATOM   2401  N  N   . LEU A 1 308 ? 52.201  79.563  28.262  1.00 32.42  ? 317  LEU A N   1 
ATOM   2402  C  CA  . LEU A 1 308 ? 50.936  79.157  27.629  1.00 31.75  ? 317  LEU A CA  1 
ATOM   2403  C  C   . LEU A 1 308 ? 49.923  78.571  28.602  1.00 32.64  ? 317  LEU A C   1 
ATOM   2404  O  O   . LEU A 1 308 ? 50.276  77.753  29.489  1.00 29.07  ? 317  LEU A O   1 
ATOM   2405  C  CB  . LEU A 1 308 ? 51.210  78.089  26.608  1.00 30.20  ? 317  LEU A CB  1 
ATOM   2406  C  CG  . LEU A 1 308 ? 52.086  78.524  25.485  1.00 36.02  ? 317  LEU A CG  1 
ATOM   2407  C  CD1 . LEU A 1 308 ? 52.425  77.312  24.621  1.00 33.07  ? 317  LEU A CD1 1 
ATOM   2408  C  CD2 . LEU A 1 308 ? 51.327  79.619  24.681  1.00 34.09  ? 317  LEU A CD2 1 
ATOM   2409  N  N   . GLU A 1 309 ? 48.679  78.972  28.446  1.00 25.53  ? 318  GLU A N   1 
ATOM   2410  C  CA  . GLU A 1 309 ? 47.624  78.418  29.246  1.00 25.83  ? 318  GLU A CA  1 
ATOM   2411  C  C   . GLU A 1 309 ? 47.042  77.197  28.558  1.00 29.69  ? 318  GLU A C   1 
ATOM   2412  O  O   . GLU A 1 309 ? 46.682  76.246  29.247  1.00 31.00  ? 318  GLU A O   1 
ATOM   2413  C  CB  . GLU A 1 309 ? 46.566  79.477  29.437  1.00 31.84  ? 318  GLU A CB  1 
ATOM   2414  C  CG  . GLU A 1 309 ? 47.180  80.610  30.257  1.00 45.66  ? 318  GLU A CG  1 
ATOM   2415  C  CD  . GLU A 1 309 ? 46.205  81.712  30.618  1.00 62.47  ? 318  GLU A CD  1 
ATOM   2416  O  OE1 . GLU A 1 309 ? 45.012  81.633  30.220  1.00 69.63  ? 318  GLU A OE1 1 
ATOM   2417  O  OE2 . GLU A 1 309 ? 46.647  82.680  31.306  1.00 67.22  ? 318  GLU A OE2 1 
ATOM   2418  N  N   . GLU A 1 310 ? 46.976  77.186  27.211  1.00 23.62  ? 319  GLU A N   1 
ATOM   2419  C  CA  . GLU A 1 310 ? 46.302  76.092  26.508  1.00 24.16  ? 319  GLU A CA  1 
ATOM   2420  C  C   . GLU A 1 310 ? 46.926  75.827  25.180  1.00 22.23  ? 319  GLU A C   1 
ATOM   2421  O  O   . GLU A 1 310 ? 47.381  76.767  24.559  1.00 23.46  ? 319  GLU A O   1 
ATOM   2422  C  CB  . GLU A 1 310 ? 44.801  76.452  26.201  1.00 26.70  ? 319  GLU A CB  1 
ATOM   2423  C  CG  . GLU A 1 310 ? 43.909  76.637  27.415  1.00 34.26  ? 319  GLU A CG  1 
ATOM   2424  C  CD  . GLU A 1 310 ? 42.606  77.347  27.055  1.00 47.15  ? 319  GLU A CD  1 
ATOM   2425  O  OE1 . GLU A 1 310 ? 42.211  78.252  27.807  1.00 52.15  ? 319  GLU A OE1 1 
ATOM   2426  O  OE2 . GLU A 1 310 ? 41.986  77.000  26.030  1.00 51.61  ? 319  GLU A OE2 1 
ATOM   2427  N  N   . ALA A 1 311 ? 47.000  74.537  24.766  1.00 19.86  ? 320  ALA A N   1 
ATOM   2428  C  CA  . ALA A 1 311 ? 47.494  74.148  23.443  1.00 19.40  ? 320  ALA A CA  1 
ATOM   2429  C  C   . ALA A 1 311 ? 46.491  73.138  22.882  1.00 22.24  ? 320  ALA A C   1 
ATOM   2430  O  O   . ALA A 1 311 ? 46.057  72.216  23.593  1.00 23.80  ? 320  ALA A O   1 
ATOM   2431  C  CB  . ALA A 1 311 ? 48.867  73.517  23.522  1.00 21.78  ? 320  ALA A CB  1 
ATOM   2432  N  N   . TYR A 1 312 ? 46.126  73.290  21.628  1.00 22.03  ? 321  TYR A N   1 
ATOM   2433  C  CA  . TYR A 1 312 ? 45.210  72.374  20.959  1.00 21.76  ? 321  TYR A CA  1 
ATOM   2434  C  C   . TYR A 1 312 ? 45.933  71.800  19.799  1.00 22.43  ? 321  TYR A C   1 
ATOM   2435  O  O   . TYR A 1 312 ? 46.803  72.454  19.259  1.00 21.03  ? 321  TYR A O   1 
ATOM   2436  C  CB  . TYR A 1 312 ? 43.945  73.091  20.462  1.00 20.09  ? 321  TYR A CB  1 
ATOM   2437  C  CG  . TYR A 1 312 ? 43.094  73.563  21.604  1.00 21.42  ? 321  TYR A CG  1 
ATOM   2438  C  CD1 . TYR A 1 312 ? 43.283  74.824  22.159  1.00 20.50  ? 321  TYR A CD1 1 
ATOM   2439  C  CD2 . TYR A 1 312 ? 42.126  72.730  22.172  1.00 23.10  ? 321  TYR A CD2 1 
ATOM   2440  C  CE1 . TYR A 1 312 ? 42.541  75.254  23.248  1.00 27.81  ? 321  TYR A CE1 1 
ATOM   2441  C  CE2 . TYR A 1 312 ? 41.374  73.154  23.274  1.00 26.92  ? 321  TYR A CE2 1 
ATOM   2442  C  CZ  . TYR A 1 312 ? 41.591  74.410  23.802  1.00 31.70  ? 321  TYR A CZ  1 
ATOM   2443  O  OH  . TYR A 1 312 ? 40.894  74.844  24.900  1.00 33.66  ? 321  TYR A OH  1 
ATOM   2444  N  N   . TYR A 1 313 ? 45.627  70.552  19.435  1.00 19.40  ? 322  TYR A N   1 
ATOM   2445  C  CA  . TYR A 1 313 ? 46.284  69.868  18.315  1.00 19.53  ? 322  TYR A CA  1 
ATOM   2446  C  C   . TYR A 1 313 ? 45.252  69.532  17.264  1.00 22.07  ? 322  TYR A C   1 
ATOM   2447  O  O   . TYR A 1 313 ? 44.354  68.715  17.532  1.00 23.27  ? 322  TYR A O   1 
ATOM   2448  C  CB  . TYR A 1 313 ? 46.944  68.556  18.836  1.00 20.87  ? 322  TYR A CB  1 
ATOM   2449  C  CG  . TYR A 1 313 ? 47.784  68.815  20.062  1.00 21.36  ? 322  TYR A CG  1 
ATOM   2450  C  CD1 . TYR A 1 313 ? 49.112  69.243  19.948  1.00 24.70  ? 322  TYR A CD1 1 
ATOM   2451  C  CD2 . TYR A 1 313 ? 47.254  68.668  21.340  1.00 24.75  ? 322  TYR A CD2 1 
ATOM   2452  C  CE1 . TYR A 1 313 ? 49.872  69.517  21.079  1.00 24.54  ? 322  TYR A CE1 1 
ATOM   2453  C  CE2 . TYR A 1 313 ? 48.007  68.948  22.467  1.00 21.10  ? 322  TYR A CE2 1 
ATOM   2454  C  CZ  . TYR A 1 313 ? 49.312  69.377  22.333  1.00 25.32  ? 322  TYR A CZ  1 
ATOM   2455  O  OH  . TYR A 1 313 ? 50.052  69.709  23.452  1.00 25.30  ? 322  TYR A OH  1 
ATOM   2456  N  N   . ILE A 1 314 ? 45.371  70.089  16.067  1.00 20.02  ? 323  ILE A N   1 
ATOM   2457  C  CA  . ILE A 1 314 ? 44.392  69.839  15.029  1.00 22.16  ? 323  ILE A CA  1 
ATOM   2458  C  C   . ILE A 1 314 ? 45.024  68.881  14.051  1.00 24.07  ? 323  ILE A C   1 
ATOM   2459  O  O   . ILE A 1 314 ? 45.953  69.268  13.362  1.00 24.28  ? 323  ILE A O   1 
ATOM   2460  C  CB  . ILE A 1 314 ? 43.987  71.177  14.269  1.00 22.33  ? 323  ILE A CB  1 
ATOM   2461  C  CG1 . ILE A 1 314 ? 43.665  72.301  15.294  1.00 20.90  ? 323  ILE A CG1 1 
ATOM   2462  C  CG2 . ILE A 1 314 ? 42.773  70.936  13.315  1.00 19.71  ? 323  ILE A CG2 1 
ATOM   2463  C  CD1 . ILE A 1 314 ? 42.562  71.963  16.354  1.00 21.68  ? 323  ILE A CD1 1 
ATOM   2464  N  N   . GLY A 1 315 ? 44.555  67.650  13.980  1.00 21.06  ? 324  GLY A N   1 
ATOM   2465  C  CA  . GLY A 1 315 ? 45.195  66.683  13.090  1.00 25.18  ? 324  GLY A CA  1 
ATOM   2466  C  C   . GLY A 1 315 ? 45.265  65.324  13.792  1.00 28.05  ? 324  GLY A C   1 
ATOM   2467  O  O   . GLY A 1 315 ? 45.294  65.280  15.020  1.00 26.53  ? 324  GLY A O   1 
ATOM   2468  N  N   . GLY A 1 316 ? 45.294  64.226  13.026  1.00 28.18  ? 325  GLY A N   1 
ATOM   2469  C  CA  . GLY A 1 316 ? 45.377  62.891  13.627  1.00 29.60  ? 325  GLY A CA  1 
ATOM   2470  C  C   . GLY A 1 316 ? 46.813  62.544  14.003  1.00 31.86  ? 325  GLY A C   1 
ATOM   2471  O  O   . GLY A 1 316 ? 47.737  63.350  13.851  1.00 28.22  ? 325  GLY A O   1 
ATOM   2472  N  N   . SER A 1 317 ? 46.993  61.307  14.507  1.00 29.13  ? 326  SER A N   1 
ATOM   2473  C  CA  . SER A 1 317 ? 48.265  60.729  14.972  1.00 34.71  ? 326  SER A CA  1 
ATOM   2474  C  C   . SER A 1 317 ? 49.357  60.742  13.928  1.00 32.62  ? 326  SER A C   1 
ATOM   2475  O  O   . SER A 1 317 ? 50.533  60.883  14.263  1.00 35.14  ? 326  SER A O   1 
ATOM   2476  C  CB  . SER A 1 317 ? 48.033  59.265  15.379  1.00 35.55  ? 326  SER A CB  1 
ATOM   2477  O  OG  . SER A 1 317 ? 47.362  59.377  16.615  1.00 46.08  ? 326  SER A OG  1 
ATOM   2478  N  N   . GLN A 1 318 ? 48.984  60.585  12.687  1.00 31.87  ? 327  GLN A N   1 
ATOM   2479  C  CA  . GLN A 1 318 ? 49.943  60.595  11.617  1.00 35.86  ? 327  GLN A CA  1 
ATOM   2480  C  C   . GLN A 1 318 ? 50.436  61.986  11.306  1.00 37.95  ? 327  GLN A C   1 
ATOM   2481  O  O   . GLN A 1 318 ? 51.463  62.112  10.628  1.00 36.18  ? 327  GLN A O   1 
ATOM   2482  C  CB  . GLN A 1 318 ? 49.338  60.029  10.325  1.00 43.43  ? 327  GLN A CB  1 
ATOM   2483  C  CG  . GLN A 1 318 ? 47.939  59.432  10.468  1.00 56.50  ? 327  GLN A CG  1 
ATOM   2484  C  CD  . GLN A 1 318 ? 46.859  60.463  10.798  1.00 57.40  ? 327  GLN A CD  1 
ATOM   2485  O  OE1 . GLN A 1 318 ? 46.358  60.481  11.899  1.00 54.86  ? 327  GLN A OE1 1 
ATOM   2486  N  NE2 . GLN A 1 318 ? 46.487  61.342  9.858   1.00 56.60  ? 327  GLN A NE2 1 
ATOM   2487  N  N   . SER A 1 319 ? 49.708  63.049  11.742  1.00 32.51  ? 328  SER A N   1 
ATOM   2488  C  CA  . SER A 1 319 ? 50.165  64.421  11.466  1.00 30.59  ? 328  SER A CA  1 
ATOM   2489  C  C   . SER A 1 319 ? 50.829  65.025  12.649  1.00 26.99  ? 328  SER A C   1 
ATOM   2490  O  O   . SER A 1 319 ? 51.759  65.790  12.479  1.00 27.27  ? 328  SER A O   1 
ATOM   2491  C  CB  . SER A 1 319 ? 48.982  65.306  11.075  1.00 31.54  ? 328  SER A CB  1 
ATOM   2492  O  OG  . SER A 1 319 ? 48.470  64.848  9.841   1.00 34.95  ? 328  SER A OG  1 
ATOM   2493  N  N   . LEU A 1 320 ? 50.305  64.723  13.874  1.00 26.65  ? 329  LEU A N   1 
ATOM   2494  C  CA  . LEU A 1 320 ? 50.834  65.238  15.146  1.00 25.61  ? 329  LEU A CA  1 
ATOM   2495  C  C   . LEU A 1 320 ? 50.865  64.039  16.041  1.00 26.92  ? 329  LEU A C   1 
ATOM   2496  O  O   . LEU A 1 320 ? 49.809  63.560  16.455  1.00 26.83  ? 329  LEU A O   1 
ATOM   2497  C  CB  . LEU A 1 320 ? 49.879  66.325  15.715  1.00 24.57  ? 329  LEU A CB  1 
ATOM   2498  C  CG  . LEU A 1 320 ? 49.814  67.564  14.779  1.00 25.91  ? 329  LEU A CG  1 
ATOM   2499  C  CD1 . LEU A 1 320 ? 48.722  68.514  15.323  1.00 27.15  ? 329  LEU A CD1 1 
ATOM   2500  C  CD2 . LEU A 1 320 ? 51.227  68.279  14.741  1.00 22.68  ? 329  LEU A CD2 1 
ATOM   2501  N  N   . SER A 1 321 ? 52.075  63.528  16.365  1.00 26.16  ? 330  SER A N   1 
ATOM   2502  C  CA  . SER A 1 321 ? 52.118  62.279  17.146  1.00 29.23  ? 330  SER A CA  1 
ATOM   2503  C  C   . SER A 1 321 ? 52.074  62.576  18.644  1.00 32.54  ? 330  SER A C   1 
ATOM   2504  O  O   . SER A 1 321 ? 52.086  63.738  19.056  1.00 29.48  ? 330  SER A O   1 
ATOM   2505  C  CB  . SER A 1 321 ? 53.437  61.567  16.824  1.00 32.18  ? 330  SER A CB  1 
ATOM   2506  O  OG  . SER A 1 321 ? 54.484  62.274  17.478  1.00 31.17  ? 330  SER A OG  1 
ATOM   2507  N  N   . SER A 1 322 ? 52.082  61.508  19.482  1.00 29.24  ? 331  SER A N   1 
ATOM   2508  C  CA  . SER A 1 322 ? 52.084  61.692  20.926  1.00 31.83  ? 331  SER A CA  1 
ATOM   2509  C  C   . SER A 1 322 ? 53.362  62.400  21.371  1.00 31.02  ? 331  SER A C   1 
ATOM   2510  O  O   . SER A 1 322 ? 53.402  62.950  22.468  1.00 30.26  ? 331  SER A O   1 
ATOM   2511  C  CB  . SER A 1 322 ? 51.976  60.331  21.628  1.00 39.50  ? 331  SER A CB  1 
ATOM   2512  O  OG  . SER A 1 322 ? 53.036  59.516  21.159  1.00 47.00  ? 331  SER A OG  1 
ATOM   2513  N  N   . LYS A 1 323 ? 54.404  62.399  20.529  1.00 29.58  ? 332  LYS A N   1 
ATOM   2514  C  CA  . LYS A 1 323 ? 55.652  63.051  20.919  1.00 32.87  ? 332  LYS A CA  1 
ATOM   2515  C  C   . LYS A 1 323 ? 55.472  64.584  20.950  1.00 32.05  ? 332  LYS A C   1 
ATOM   2516  O  O   . LYS A 1 323 ? 55.971  65.245  21.873  1.00 28.67  ? 332  LYS A O   1 
ATOM   2517  C  CB  . LYS A 1 323 ? 56.763  62.666  19.926  1.00 36.12  ? 332  LYS A CB  1 
ATOM   2518  C  CG  . LYS A 1 323 ? 57.413  61.296  20.265  1.00 43.22  ? 332  LYS A CG  1 
ATOM   2519  C  CD  . LYS A 1 323 ? 58.068  60.711  19.036  1.00 54.06  ? 332  LYS A CD  1 
ATOM   2520  C  CE  . LYS A 1 323 ? 58.553  59.291  19.261  1.00 67.34  ? 332  LYS A CE  1 
ATOM   2521  N  NZ  . LYS A 1 323 ? 58.400  58.462  18.031  1.00 73.28  ? 332  LYS A NZ  1 
ATOM   2522  N  N   . ILE A 1 324 ? 54.727  65.162  19.973  1.00 28.12  ? 333  ILE A N   1 
ATOM   2523  C  CA  . ILE A 1 324 ? 54.575  66.641  20.068  1.00 24.44  ? 333  ILE A CA  1 
ATOM   2524  C  C   . ILE A 1 324 ? 53.622  66.962  21.204  1.00 27.31  ? 333  ILE A C   1 
ATOM   2525  O  O   . ILE A 1 324 ? 53.796  67.978  21.867  1.00 28.52  ? 333  ILE A O   1 
ATOM   2526  C  CB  . ILE A 1 324 ? 54.152  67.203  18.692  1.00 31.36  ? 333  ILE A CB  1 
ATOM   2527  C  CG1 . ILE A 1 324 ? 54.365  68.775  18.692  1.00 32.41  ? 333  ILE A CG1 1 
ATOM   2528  C  CG2 . ILE A 1 324 ? 52.715  66.763  18.359  1.00 29.30  ? 333  ILE A CG2 1 
ATOM   2529  C  CD1 . ILE A 1 324 ? 53.989  69.398  17.390  1.00 31.48  ? 333  ILE A CD1 1 
ATOM   2530  N  N   . ILE A 1 325 ? 52.607  66.110  21.475  1.00 26.07  ? 334  ILE A N   1 
ATOM   2531  C  CA  . ILE A 1 325 ? 51.740  66.416  22.620  1.00 28.13  ? 334  ILE A CA  1 
ATOM   2532  C  C   . ILE A 1 325 ? 52.563  66.390  23.934  1.00 29.41  ? 334  ILE A C   1 
ATOM   2533  O  O   . ILE A 1 325 ? 52.387  67.220  24.813  1.00 29.23  ? 334  ILE A O   1 
ATOM   2534  C  CB  . ILE A 1 325 ? 50.549  65.427  22.648  1.00 28.55  ? 334  ILE A CB  1 
ATOM   2535  C  CG1 . ILE A 1 325 ? 49.672  65.673  21.396  1.00 28.89  ? 334  ILE A CG1 1 
ATOM   2536  C  CG2 . ILE A 1 325 ? 49.744  65.569  23.936  1.00 27.01  ? 334  ILE A CG2 1 
ATOM   2537  C  CD1 . ILE A 1 325 ? 48.338  64.927  21.415  1.00 34.87  ? 334  ILE A CD1 1 
ATOM   2538  N  N   . ASP A 1 326 ? 53.456  65.431  24.055  1.00 31.71  ? 335  ASP A N   1 
ATOM   2539  C  CA  . ASP A 1 326 ? 54.308  65.349  25.223  1.00 35.32  ? 335  ASP A CA  1 
ATOM   2540  C  C   . ASP A 1 326 ? 55.161  66.600  25.347  1.00 34.18  ? 335  ASP A C   1 
ATOM   2541  O  O   . ASP A 1 326 ? 55.286  67.138  26.447  1.00 34.33  ? 335  ASP A O   1 
ATOM   2542  C  CB  . ASP A 1 326 ? 55.277  64.174  25.077  1.00 42.06  ? 335  ASP A CB  1 
ATOM   2543  C  CG  . ASP A 1 326 ? 56.224  64.173  26.265  1.00 57.80  ? 335  ASP A CG  1 
ATOM   2544  O  OD1 . ASP A 1 326 ? 57.422  64.540  26.086  1.00 61.61  ? 335  ASP A OD1 1 
ATOM   2545  O  OD2 . ASP A 1 326 ? 55.772  63.829  27.374  1.00 63.60  ? 335  ASP A OD2 1 
ATOM   2546  N  N   . GLN A 1 327 ? 55.777  67.039  24.239  1.00 30.01  ? 336  GLN A N   1 
ATOM   2547  C  CA  . GLN A 1 327 ? 56.634  68.244  24.225  1.00 28.07  ? 336  GLN A CA  1 
ATOM   2548  C  C   . GLN A 1 327 ? 55.864  69.474  24.680  1.00 29.63  ? 336  GLN A C   1 
ATOM   2549  O  O   . GLN A 1 327 ? 56.303  70.184  25.590  1.00 27.89  ? 336  GLN A O   1 
ATOM   2550  C  CB  . GLN A 1 327 ? 57.124  68.496  22.818  1.00 25.98  ? 336  GLN A CB  1 
ATOM   2551  C  CG  . GLN A 1 327 ? 58.049  69.710  22.740  1.00 30.28  ? 336  GLN A CG  1 
ATOM   2552  C  CD  . GLN A 1 327 ? 58.426  70.029  21.294  1.00 36.43  ? 336  GLN A CD  1 
ATOM   2553  O  OE1 . GLN A 1 327 ? 57.577  70.082  20.408  1.00 36.90  ? 336  GLN A OE1 1 
ATOM   2554  N  NE2 . GLN A 1 327 ? 59.702  70.324  21.018  1.00 35.49  ? 336  GLN A NE2 1 
ATOM   2555  N  N   . ILE A 1 328 ? 54.681  69.696  24.067  1.00 26.56  ? 337  ILE A N   1 
ATOM   2556  C  CA  . ILE A 1 328 ? 53.907  70.898  24.364  1.00 25.16  ? 337  ILE A CA  1 
ATOM   2557  C  C   . ILE A 1 328 ? 53.159  70.806  25.667  1.00 26.61  ? 337  ILE A C   1 
ATOM   2558  O  O   . ILE A 1 328 ? 53.030  71.803  26.401  1.00 27.95  ? 337  ILE A O   1 
ATOM   2559  C  CB  . ILE A 1 328 ? 52.964  71.180  23.163  1.00 25.96  ? 337  ILE A CB  1 
ATOM   2560  C  CG1 . ILE A 1 328 ? 53.811  71.399  21.893  1.00 24.21  ? 337  ILE A CG1 1 
ATOM   2561  C  CG2 . ILE A 1 328 ? 52.059  72.410  23.517  1.00 24.78  ? 337  ILE A CG2 1 
ATOM   2562  C  CD1 . ILE A 1 328 ? 54.854  72.558  22.067  1.00 27.29  ? 337  ILE A CD1 1 
ATOM   2563  N  N   . SER A 1 329 ? 52.642  69.615  25.993  1.00 28.20  ? 338  SER A N   1 
ATOM   2564  C  CA  . SER A 1 329 ? 51.981  69.453  27.268  1.00 27.62  ? 338  SER A CA  1 
ATOM   2565  C  C   . SER A 1 329 ? 52.898  69.886  28.409  1.00 26.31  ? 338  SER A C   1 
ATOM   2566  O  O   . SER A 1 329 ? 52.412  70.367  29.430  1.00 27.39  ? 338  SER A O   1 
ATOM   2567  C  CB  . SER A 1 329 ? 51.629  67.973  27.495  1.00 30.24  ? 338  SER A CB  1 
ATOM   2568  O  OG  . SER A 1 329 ? 50.833  67.858  28.666  1.00 35.27  ? 338  SER A OG  1 
ATOM   2569  N  N   . LYS A 1 330 ? 54.210  69.671  28.272  1.00 25.78  ? 339  LYS A N   1 
ATOM   2570  C  CA  . LYS A 1 330 ? 55.179  70.033  29.342  1.00 27.32  ? 339  LYS A CA  1 
ATOM   2571  C  C   . LYS A 1 330 ? 55.348  71.547  29.498  1.00 31.48  ? 339  LYS A C   1 
ATOM   2572  O  O   . LYS A 1 330 ? 55.766  72.011  30.576  1.00 30.99  ? 339  LYS A O   1 
ATOM   2573  C  CB  . LYS A 1 330 ? 56.522  69.392  29.018  1.00 28.35  ? 339  LYS A CB  1 
ATOM   2574  C  CG  . LYS A 1 330 ? 56.474  67.911  29.321  1.00 28.77  ? 339  LYS A CG  1 
ATOM   2575  C  CD  . LYS A 1 330 ? 57.768  67.205  29.028  1.00 31.94  ? 339  LYS A CD  1 
ATOM   2576  C  CE  . LYS A 1 330 ? 57.595  65.786  29.513  1.00 40.15  ? 339  LYS A CE  1 
ATOM   2577  N  NZ  . LYS A 1 330 ? 58.419  64.855  28.728  1.00 44.44  ? 339  LYS A NZ  1 
ATOM   2578  N  N   . ILE A 1 331 ? 55.017  72.329  28.453  1.00 29.54  ? 340  ILE A N   1 
ATOM   2579  C  CA  . ILE A 1 331 ? 55.185  73.792  28.583  1.00 31.69  ? 340  ILE A CA  1 
ATOM   2580  C  C   . ILE A 1 331 ? 53.839  74.556  28.539  1.00 33.83  ? 340  ILE A C   1 
ATOM   2581  O  O   . ILE A 1 331 ? 53.862  75.770  28.612  1.00 35.79  ? 340  ILE A O   1 
ATOM   2582  C  CB  . ILE A 1 331 ? 56.188  74.379  27.537  1.00 30.74  ? 340  ILE A CB  1 
ATOM   2583  C  CG1 . ILE A 1 331 ? 55.723  74.068  26.075  1.00 29.33  ? 340  ILE A CG1 1 
ATOM   2584  C  CG2 . ILE A 1 331 ? 57.570  73.814  27.813  1.00 28.05  ? 340  ILE A CG2 1 
ATOM   2585  C  CD1 . ILE A 1 331 ? 56.290  75.076  25.018  1.00 27.90  ? 340  ILE A CD1 1 
ATOM   2586  N  N   . ALA A 1 332 ? 52.684  73.874  28.441  1.00 30.08  ? 341  ALA A N   1 
ATOM   2587  C  CA  . ALA A 1 332 ? 51.387  74.558  28.471  1.00 27.65  ? 341  ALA A CA  1 
ATOM   2588  C  C   . ALA A 1 332 ? 50.615  74.102  29.740  1.00 28.19  ? 341  ALA A C   1 
ATOM   2589  O  O   . ALA A 1 332 ? 50.779  72.952  30.121  1.00 26.30  ? 341  ALA A O   1 
ATOM   2590  C  CB  . ALA A 1 332 ? 50.583  74.179  27.232  1.00 27.01  ? 341  ALA A CB  1 
ATOM   2591  N  N   . LYS A 1 333 ? 49.803  74.933  30.384  1.00 25.99  ? 342  LYS A N   1 
ATOM   2592  C  CA  . LYS A 1 333 ? 49.100  74.468  31.559  1.00 26.65  ? 342  LYS A CA  1 
ATOM   2593  C  C   . LYS A 1 333 ? 48.114  73.382  31.179  1.00 31.02  ? 342  LYS A C   1 
ATOM   2594  O  O   . LYS A 1 333 ? 47.971  72.401  31.929  1.00 27.93  ? 342  LYS A O   1 
ATOM   2595  C  CB  . LYS A 1 333 ? 48.379  75.606  32.267  1.00 26.59  ? 342  LYS A CB  1 
ATOM   2596  C  CG  . LYS A 1 333 ? 49.352  76.590  32.901  1.00 29.58  ? 342  LYS A CG  1 
ATOM   2597  C  CD  . LYS A 1 333 ? 48.597  77.613  33.761  1.00 40.24  ? 342  LYS A CD  1 
ATOM   2598  C  CE  . LYS A 1 333 ? 49.539  78.497  34.562  1.00 51.19  ? 342  LYS A CE  1 
ATOM   2599  N  NZ  . LYS A 1 333 ? 50.674  79.003  33.740  0.00 0.00   ? 342  LYS A NZ  1 
ATOM   2600  N  N   A ASN A 1 334 ? 47.459  73.515  30.006  0.77 27.62  ? 343  ASN A N   1 
ATOM   2601  N  N   B ASN A 1 334 ? 47.471  73.527  30.027  0.23 32.48  ? 343  ASN A N   1 
ATOM   2602  C  CA  A ASN A 1 334 ? 46.445  72.545  29.562  0.77 28.53  ? 343  ASN A CA  1 
ATOM   2603  C  CA  B ASN A 1 334 ? 46.502  72.540  29.569  0.23 34.08  ? 343  ASN A CA  1 
ATOM   2604  C  C   A ASN A 1 334 ? 46.731  72.203  28.094  0.77 28.83  ? 343  ASN A C   1 
ATOM   2605  C  C   B ASN A 1 334 ? 46.780  72.184  28.111  0.23 34.26  ? 343  ASN A C   1 
ATOM   2606  O  O   A ASN A 1 334 ? 46.233  72.856  27.187  0.77 26.76  ? 343  ASN A O   1 
ATOM   2607  O  O   B ASN A 1 334 ? 46.288  72.847  27.201  0.23 32.79  ? 343  ASN A O   1 
ATOM   2608  C  CB  A ASN A 1 334 ? 45.052  73.194  29.820  0.77 32.63  ? 343  ASN A CB  1 
ATOM   2609  C  CB  B ASN A 1 334 ? 45.085  73.093  29.736  0.23 37.03  ? 343  ASN A CB  1 
ATOM   2610  C  CG  A ASN A 1 334 ? 43.849  72.616  29.088  0.77 42.83  ? 343  ASN A CG  1 
ATOM   2611  C  CG  B ASN A 1 334 ? 44.431  72.634  31.011  0.23 43.74  ? 343  ASN A CG  1 
ATOM   2612  O  OD1 A ASN A 1 334 ? 43.902  71.519  28.523  0.77 44.63  ? 343  ASN A OD1 1 
ATOM   2613  O  OD1 B ASN A 1 334 ? 45.115  72.281  31.975  0.23 47.09  ? 343  ASN A OD1 1 
ATOM   2614  N  ND2 A ASN A 1 334 ? 42.679  73.298  29.090  0.77 46.61  ? 343  ASN A ND2 1 
ATOM   2615  N  ND2 B ASN A 1 334 ? 43.104  72.581  31.100  0.23 48.95  ? 343  ASN A ND2 1 
ATOM   2616  N  N   . GLY A 1 335 ? 47.550  71.171  27.874  1.00 27.12  ? 344  GLY A N   1 
ATOM   2617  C  CA  . GLY A 1 335 ? 47.955  70.777  26.523  1.00 26.21  ? 344  GLY A CA  1 
ATOM   2618  C  C   . GLY A 1 335 ? 48.023  69.274  26.359  1.00 25.91  ? 344  GLY A C   1 
ATOM   2619  O  O   . GLY A 1 335 ? 48.894  68.781  25.668  1.00 26.32  ? 344  GLY A O   1 
ATOM   2620  N  N   . THR A 1 336 ? 47.111  68.519  27.025  1.00 27.80  ? 345  THR A N   1 
ATOM   2621  C  CA  . THR A 1 336 ? 47.133  67.057  26.892  1.00 27.76  ? 345  THR A CA  1 
ATOM   2622  C  C   . THR A 1 336 ? 46.410  66.626  25.637  1.00 30.59  ? 345  THR A C   1 
ATOM   2623  O  O   . THR A 1 336 ? 45.816  67.462  24.936  1.00 27.61  ? 345  THR A O   1 
ATOM   2624  C  CB  . THR A 1 336 ? 46.456  66.381  28.101  1.00 30.07  ? 345  THR A CB  1 
ATOM   2625  O  OG1 . THR A 1 336 ? 45.049  66.571  28.017  1.00 28.76  ? 345  THR A OG1 1 
ATOM   2626  C  CG2 . THR A 1 336 ? 46.977  66.958  29.451  1.00 30.40  ? 345  THR A CG2 1 
ATOM   2627  N  N   . SER A 1 337 ? 46.421  65.313  25.376  1.00 28.61  ? 346  SER A N   1 
ATOM   2628  C  CA  . SER A 1 337 ? 45.798  64.725  24.192  1.00 27.94  ? 346  SER A CA  1 
ATOM   2629  C  C   . SER A 1 337 ? 44.343  64.933  24.175  1.00 26.78  ? 346  SER A C   1 
ATOM   2630  O  O   . SER A 1 337 ? 43.707  64.747  23.128  1.00 29.35  ? 346  SER A O   1 
ATOM   2631  C  CB  . SER A 1 337 ? 46.137  63.227  24.112  1.00 33.41  ? 346  SER A CB  1 
ATOM   2632  O  OG  . SER A 1 337 ? 45.596  62.573  25.254  1.00 34.56  ? 346  SER A OG  1 
ATOM   2633  N  N   . LYS A 1 338 ? 43.754  65.302  25.300  1.00 25.05  ? 347  LYS A N   1 
ATOM   2634  C  CA  . LYS A 1 338 ? 42.325  65.599  25.336  1.00 29.24  ? 347  LYS A CA  1 
ATOM   2635  C  C   . LYS A 1 338 ? 42.007  66.796  24.363  1.00 30.40  ? 347  LYS A C   1 
ATOM   2636  O  O   . LYS A 1 338 ? 40.871  66.995  23.935  1.00 26.07  ? 347  LYS A O   1 
ATOM   2637  C  CB  . LYS A 1 338 ? 41.957  66.023  26.751  1.00 37.55  ? 347  LYS A CB  1 
ATOM   2638  C  CG  . LYS A 1 338 ? 40.464  65.963  27.011  1.00 56.11  ? 347  LYS A CG  1 
ATOM   2639  C  CD  . LYS A 1 338 ? 39.864  67.362  27.235  1.00 64.24  ? 347  LYS A CD  1 
ATOM   2640  C  CE  . LYS A 1 338 ? 38.363  67.364  26.981  1.00 71.85  ? 347  LYS A CE  1 
ATOM   2641  N  NZ  . LYS A 1 338 ? 37.911  68.573  26.230  1.00 74.31  ? 347  LYS A NZ  1 
ATOM   2642  N  N   . ASN A 1 339 ? 43.042  67.600  24.062  1.00 27.58  ? 348  ASN A N   1 
ATOM   2643  C  CA  . ASN A 1 339 ? 42.866  68.796  23.228  1.00 25.87  ? 348  ASN A CA  1 
ATOM   2644  C  C   . ASN A 1 339 ? 43.127  68.497  21.773  1.00 25.56  ? 348  ASN A C   1 
ATOM   2645  O  O   . ASN A 1 339 ? 43.271  69.430  20.969  1.00 24.96  ? 348  ASN A O   1 
ATOM   2646  C  CB  . ASN A 1 339 ? 43.816  69.896  23.722  1.00 25.01  ? 348  ASN A CB  1 
ATOM   2647  C  CG  . ASN A 1 339 ? 43.379  70.422  25.063  1.00 31.81  ? 348  ASN A CG  1 
ATOM   2648  O  OD1 . ASN A 1 339 ? 42.310  70.033  25.560  1.00 32.72  ? 348  ASN A OD1 1 
ATOM   2649  N  ND2 . ASN A 1 339 ? 44.080  71.358  25.696  1.00 27.99  ? 348  ASN A ND2 1 
ATOM   2650  N  N   . ARG A 1 340 ? 43.202  67.209  21.398  1.00 20.78  ? 349  ARG A N   1 
ATOM   2651  C  CA  . ARG A 1 340 ? 43.353  66.885  19.986  1.00 23.10  ? 349  ARG A CA  1 
ATOM   2652  C  C   . ARG A 1 340 ? 42.000  66.866  19.274  1.00 23.66  ? 349  ARG A C   1 
ATOM   2653  O  O   . ARG A 1 340 ? 41.026  66.336  19.794  1.00 24.00  ? 349  ARG A O   1 
ATOM   2654  C  CB  . ARG A 1 340 ? 43.982  65.476  19.765  1.00 23.15  ? 349  ARG A CB  1 
ATOM   2655  C  CG  . ARG A 1 340 ? 44.125  65.143  18.280  1.00 26.48  ? 349  ARG A CG  1 
ATOM   2656  C  CD  . ARG A 1 340 ? 44.388  63.624  18.042  1.00 27.22  ? 349  ARG A CD  1 
ATOM   2657  N  NE  . ARG A 1 340 ? 45.674  63.185  18.631  1.00 25.83  ? 349  ARG A NE  1 
ATOM   2658  C  CZ  . ARG A 1 340 ? 46.867  63.310  18.057  1.00 25.89  ? 349  ARG A CZ  1 
ATOM   2659  N  NH1 . ARG A 1 340 ? 46.987  63.904  16.879  1.00 23.60  ? 349  ARG A NH1 1 
ATOM   2660  N  NH2 . ARG A 1 340 ? 47.957  62.808  18.647  1.00 25.69  ? 349  ARG A NH2 1 
ATOM   2661  N  N   . VAL A 1 341 ? 41.920  67.434  18.077  1.00 21.28  ? 350  VAL A N   1 
ATOM   2662  C  CA  . VAL A 1 341 ? 40.680  67.378  17.329  1.00 19.96  ? 350  VAL A CA  1 
ATOM   2663  C  C   . VAL A 1 341 ? 41.078  66.862  15.963  1.00 20.94  ? 350  VAL A C   1 
ATOM   2664  O  O   . VAL A 1 341 ? 42.000  67.414  15.341  1.00 23.52  ? 350  VAL A O   1 
ATOM   2665  C  CB  . VAL A 1 341 ? 39.992  68.780  17.172  1.00 22.82  ? 350  VAL A CB  1 
ATOM   2666  C  CG1 . VAL A 1 341 ? 38.779  68.664  16.227  1.00 20.37  ? 350  VAL A CG1 1 
ATOM   2667  C  CG2 . VAL A 1 341 ? 39.543  69.299  18.553  1.00 23.80  ? 350  VAL A CG2 1 
ATOM   2668  N  N   . SER A 1 342 ? 40.446  65.817  15.468  1.00 23.77  ? 351  SER A N   1 
ATOM   2669  C  CA  . SER A 1 342 ? 40.910  65.327  14.153  1.00 28.94  ? 351  SER A CA  1 
ATOM   2670  C  C   . SER A 1 342 ? 39.774  64.826  13.317  1.00 27.80  ? 351  SER A C   1 
ATOM   2671  O  O   . SER A 1 342 ? 38.643  65.186  13.579  1.00 28.41  ? 351  SER A O   1 
ATOM   2672  C  CB  . SER A 1 342 ? 41.946  64.208  14.340  1.00 33.29  ? 351  SER A CB  1 
ATOM   2673  O  OG  . SER A 1 342 ? 41.324  63.138  15.036  1.00 35.06  ? 351  SER A OG  1 
ATOM   2674  N  N   . GLY A 1 343 ? 40.058  64.068  12.268  1.00 27.08  ? 352  GLY A N   1 
ATOM   2675  C  CA  . GLY A 1 343 ? 38.997  63.581  11.397  1.00 24.60  ? 352  GLY A CA  1 
ATOM   2676  C  C   . GLY A 1 343 ? 39.622  62.721  10.320  1.00 27.29  ? 352  GLY A C   1 
ATOM   2677  O  O   . GLY A 1 343 ? 40.784  62.840  10.036  1.00 25.46  ? 352  GLY A O   1 
ATOM   2678  N  N   . ALA A 1 344 ? 38.810  61.839  9.703   1.00 28.86  ? 353  ALA A N   1 
ATOM   2679  C  CA  . ALA A 1 344 ? 39.274  60.946  8.634   1.00 30.80  ? 353  ALA A CA  1 
ATOM   2680  C  C   . ALA A 1 344 ? 39.728  61.747  7.428   1.00 30.78  ? 353  ALA A C   1 
ATOM   2681  O  O   . ALA A 1 344 ? 40.581  61.311  6.672   1.00 27.68  ? 353  ALA A O   1 
ATOM   2682  C  CB  . ALA A 1 344 ? 38.117  60.028  8.228   1.00 30.85  ? 353  ALA A CB  1 
ATOM   2683  N  N   . ASP A 1 345 ? 39.127  62.942  7.222   1.00 25.35  ? 354  ASP A N   1 
ATOM   2684  C  CA  . ASP A 1 345 ? 39.526  63.764  6.125   1.00 23.45  ? 354  ASP A CA  1 
ATOM   2685  C  C   . ASP A 1 345 ? 39.196  65.280  6.407   1.00 23.62  ? 354  ASP A C   1 
ATOM   2686  O  O   . ASP A 1 345 ? 38.773  65.578  7.522   1.00 24.76  ? 354  ASP A O   1 
ATOM   2687  C  CB  . ASP A 1 345 ? 38.828  63.351  4.832   1.00 24.93  ? 354  ASP A CB  1 
ATOM   2688  C  CG  . ASP A 1 345 ? 37.292  63.409  4.833   1.00 30.80  ? 354  ASP A CG  1 
ATOM   2689  O  OD1 . ASP A 1 345 ? 36.718  64.245  5.552   1.00 29.64  ? 354  ASP A OD1 1 
ATOM   2690  O  OD2 . ASP A 1 345 ? 36.669  62.611  4.108   1.00 32.12  ? 354  ASP A OD2 1 
ATOM   2691  N  N   . ARG A 1 346 ? 39.404  66.167  5.427   1.00 23.11  ? 355  ARG A N   1 
ATOM   2692  C  CA  . ARG A 1 346 ? 39.217  67.626  5.655   1.00 21.83  ? 355  ARG A CA  1 
ATOM   2693  C  C   . ARG A 1 346 ? 37.765  67.945  6.072   1.00 22.47  ? 355  ARG A C   1 
ATOM   2694  O  O   . ARG A 1 346 ? 37.566  68.894  6.839   1.00 19.89  ? 355  ARG A O   1 
ATOM   2695  C  CB  . ARG A 1 346 ? 39.638  68.424  4.377   1.00 20.15  ? 355  ARG A CB  1 
ATOM   2696  C  CG  . ARG A 1 346 ? 38.668  68.197  3.218   1.00 22.92  ? 355  ARG A CG  1 
ATOM   2697  C  CD  . ARG A 1 346 ? 39.167  68.866  1.939   1.00 30.40  ? 355  ARG A CD  1 
ATOM   2698  N  NE  . ARG A 1 346 ? 40.367  68.208  1.468   1.00 36.31  ? 355  ARG A NE  1 
ATOM   2699  C  CZ  . ARG A 1 346 ? 40.947  68.456  0.302   1.00 44.57  ? 355  ARG A CZ  1 
ATOM   2700  N  NH1 . ARG A 1 346 ? 40.428  69.351  -0.528  1.00 41.08  ? 355  ARG A NH1 1 
ATOM   2701  N  NH2 . ARG A 1 346 ? 42.056  67.820  -0.039  1.00 41.03  ? 355  ARG A NH2 1 
ATOM   2702  N  N   . HIS A 1 347 ? 36.747  67.140  5.611   1.00 20.07  ? 356  HIS A N   1 
ATOM   2703  C  CA  . HIS A 1 347 ? 35.365  67.447  5.944   1.00 20.91  ? 356  HIS A CA  1 
ATOM   2704  C  C   . HIS A 1 347 ? 35.028  66.987  7.295   1.00 21.25  ? 356  HIS A C   1 
ATOM   2705  O  O   . HIS A 1 347 ? 34.375  67.723  8.032   1.00 20.77  ? 356  HIS A O   1 
ATOM   2706  C  CB  . HIS A 1 347 ? 34.410  66.855  4.903   1.00 21.29  ? 356  HIS A CB  1 
ATOM   2707  C  CG  . HIS A 1 347 ? 34.758  67.287  3.519   1.00 24.06  ? 356  HIS A CG  1 
ATOM   2708  N  ND1 . HIS A 1 347 ? 35.169  66.390  2.556   1.00 23.20  ? 356  HIS A ND1 1 
ATOM   2709  C  CD2 . HIS A 1 347 ? 34.745  68.510  2.930   1.00 25.13  ? 356  HIS A CD2 1 
ATOM   2710  C  CE1 . HIS A 1 347 ? 35.402  67.059  1.435   1.00 25.21  ? 356  HIS A CE1 1 
ATOM   2711  N  NE2 . HIS A 1 347 ? 35.157  68.342  1.631   1.00 27.03  ? 356  HIS A NE2 1 
ATOM   2712  N  N   . GLU A 1 348 ? 35.472  65.742  7.683   1.00 19.82  ? 357  GLU A N   1 
ATOM   2713  C  CA  . GLU A 1 348 ? 35.223  65.321  9.065   1.00 18.72  ? 357  GLU A CA  1 
ATOM   2714  C  C   . GLU A 1 348 ? 35.976  66.200  10.001  1.00 18.26  ? 357  GLU A C   1 
ATOM   2715  O  O   . GLU A 1 348 ? 35.457  66.518  11.082  1.00 18.62  ? 357  GLU A O   1 
ATOM   2716  C  CB  . GLU A 1 348 ? 35.618  63.812  9.346   1.00 17.60  ? 357  GLU A CB  1 
ATOM   2717  C  CG  . GLU A 1 348 ? 34.965  63.415  10.694  1.00 21.80  ? 357  GLU A CG  1 
ATOM   2718  C  CD  . GLU A 1 348 ? 35.157  61.927  11.002  1.00 29.08  ? 357  GLU A CD  1 
ATOM   2719  O  OE1 . GLU A 1 348 ? 36.088  61.351  10.459  1.00 27.42  ? 357  GLU A OE1 1 
ATOM   2720  O  OE2 . GLU A 1 348 ? 34.370  61.386  11.789  1.00 32.44  ? 357  GLU A OE2 1 
ATOM   2721  N  N   . THR A 1 349 ? 37.186  66.629  9.637   1.00 18.58  ? 358  THR A N   1 
ATOM   2722  C  CA  . THR A 1 349 ? 37.900  67.494  10.610  1.00 18.78  ? 358  THR A CA  1 
ATOM   2723  C  C   . THR A 1 349 ? 37.151  68.898  10.736  1.00 16.68  ? 358  THR A C   1 
ATOM   2724  O  O   . THR A 1 349 ? 37.020  69.432  11.809  1.00 17.40  ? 358  THR A O   1 
ATOM   2725  C  CB  . THR A 1 349 ? 39.310  67.743  10.094  1.00 22.27  ? 358  THR A CB  1 
ATOM   2726  O  OG1 . THR A 1 349 ? 39.977  66.451  9.948   1.00 21.47  ? 358  THR A OG1 1 
ATOM   2727  C  CG2 . THR A 1 349 ? 40.086  68.620  11.059  1.00 22.47  ? 358  THR A CG2 1 
ATOM   2728  N  N   . ASN A 1 350 ? 36.674  69.399  9.604   1.00 16.84  ? 359  ASN A N   1 
ATOM   2729  C  CA  . ASN A 1 350 ? 35.892  70.662  9.636   1.00 18.02  ? 359  ASN A CA  1 
ATOM   2730  C  C   . ASN A 1 350 ? 34.684  70.492  10.564  1.00 18.52  ? 359  ASN A C   1 
ATOM   2731  O  O   . ASN A 1 350 ? 34.416  71.333  11.445  1.00 16.75  ? 359  ASN A O   1 
ATOM   2732  C  CB  . ASN A 1 350 ? 35.471  70.989  8.226   1.00 14.89  ? 359  ASN A CB  1 
ATOM   2733  C  CG  . ASN A 1 350 ? 34.739  72.332  8.154   1.00 19.76  ? 359  ASN A CG  1 
ATOM   2734  O  OD1 . ASN A 1 350 ? 33.526  72.346  7.894   1.00 17.36  ? 359  ASN A OD1 1 
ATOM   2735  N  ND2 . ASN A 1 350 ? 35.426  73.496  8.399   1.00 15.87  ? 359  ASN A ND2 1 
ATOM   2736  N  N   . ALA A 1 351 ? 33.944  69.333  10.431  1.00 18.41  ? 360  ALA A N   1 
ATOM   2737  C  CA  . ALA A 1 351 ? 32.755  69.127  11.292  1.00 19.47  ? 360  ALA A CA  1 
ATOM   2738  C  C   . ALA A 1 351 ? 33.164  68.968  12.736  1.00 18.77  ? 360  ALA A C   1 
ATOM   2739  O  O   . ALA A 1 351 ? 32.448  69.478  13.627  1.00 20.72  ? 360  ALA A O   1 
ATOM   2740  C  CB  . ALA A 1 351 ? 31.956  67.867  10.835  1.00 17.93  ? 360  ALA A CB  1 
ATOM   2741  N  N   . ASN A 1 352 ? 34.314  68.302  13.031  1.00 18.07  ? 361  ASN A N   1 
ATOM   2742  C  CA  . ASN A 1 352 ? 34.670  68.139  14.455  1.00 17.75  ? 361  ASN A CA  1 
ATOM   2743  C  C   . ASN A 1 352 ? 35.137  69.469  15.061  1.00 18.33  ? 361  ASN A C   1 
ATOM   2744  O  O   . ASN A 1 352 ? 34.945  69.705  16.281  1.00 19.44  ? 361  ASN A O   1 
ATOM   2745  C  CB  . ASN A 1 352 ? 35.810  67.063  14.640  1.00 21.80  ? 361  ASN A CB  1 
ATOM   2746  C  CG  . ASN A 1 352 ? 35.206  65.652  14.535  1.00 32.89  ? 361  ASN A CG  1 
ATOM   2747  O  OD1 . ASN A 1 352 ? 34.007  65.450  14.868  1.00 28.23  ? 361  ASN A OD1 1 
ATOM   2748  N  ND2 . ASN A 1 352 ? 35.942  64.658  14.082  1.00 28.43  ? 361  ASN A ND2 1 
ATOM   2749  N  N   . VAL A 1 353 ? 35.792  70.309  14.251  1.00 19.59  ? 362  VAL A N   1 
ATOM   2750  C  CA  . VAL A 1 353 ? 36.185  71.639  14.803  1.00 17.54  ? 362  VAL A CA  1 
ATOM   2751  C  C   . VAL A 1 353 ? 34.908  72.440  15.113  1.00 16.85  ? 362  VAL A C   1 
ATOM   2752  O  O   . VAL A 1 353 ? 34.825  73.105  16.133  1.00 20.23  ? 362  VAL A O   1 
ATOM   2753  C  CB  . VAL A 1 353 ? 37.034  72.404  13.756  1.00 18.92  ? 362  VAL A CB  1 
ATOM   2754  C  CG1 . VAL A 1 353 ? 37.035  73.924  14.050  1.00 17.75  ? 362  VAL A CG1 1 
ATOM   2755  C  CG2 . VAL A 1 353 ? 38.464  71.829  13.742  1.00 17.56  ? 362  VAL A CG2 1 
ATOM   2756  N  N   . ILE A 1 354 ? 33.945  72.437  14.162  1.00 18.40  ? 363  ILE A N   1 
ATOM   2757  C  CA  . ILE A 1 354 ? 32.699  73.173  14.428  1.00 19.86  ? 363  ILE A CA  1 
ATOM   2758  C  C   . ILE A 1 354 ? 32.044  72.585  15.670  1.00 20.46  ? 363  ILE A C   1 
ATOM   2759  O  O   . ILE A 1 354 ? 31.639  73.322  16.565  1.00 19.86  ? 363  ILE A O   1 
ATOM   2760  C  CB  . ILE A 1 354 ? 31.809  73.099  13.159  1.00 20.90  ? 363  ILE A CB  1 
ATOM   2761  C  CG1 . ILE A 1 354 ? 32.401  74.055  12.143  1.00 19.31  ? 363  ILE A CG1 1 
ATOM   2762  C  CG2 . ILE A 1 354 ? 30.330  73.568  13.398  1.00 22.23  ? 363  ILE A CG2 1 
ATOM   2763  C  CD1 . ILE A 1 354 ? 31.890  73.869  10.674  1.00 18.49  ? 363  ILE A CD1 1 
ATOM   2764  N  N   . LYS A 1 355 ? 31.964  71.244  15.768  1.00 17.87  ? 364  LYS A N   1 
ATOM   2765  C  CA  . LYS A 1 355 ? 31.328  70.684  16.959  1.00 22.10  ? 364  LYS A CA  1 
ATOM   2766  C  C   . LYS A 1 355 ? 32.049  71.037  18.239  1.00 24.55  ? 364  LYS A C   1 
ATOM   2767  O  O   . LYS A 1 355 ? 31.406  71.349  19.251  1.00 23.22  ? 364  LYS A O   1 
ATOM   2768  C  CB  . LYS A 1 355 ? 31.247  69.128  16.762  1.00 25.50  ? 364  LYS A CB  1 
ATOM   2769  C  CG  . LYS A 1 355 ? 30.876  68.368  18.021  1.00 30.25  ? 364  LYS A CG  1 
ATOM   2770  C  CD  . LYS A 1 355 ? 31.288  66.847  17.836  1.00 42.66  ? 364  LYS A CD  1 
ATOM   2771  C  CE  . LYS A 1 355 ? 32.796  66.706  17.932  1.00 60.88  ? 364  LYS A CE  1 
ATOM   2772  N  NZ  . LYS A 1 355 ? 33.257  65.298  17.738  1.00 70.34  ? 364  LYS A NZ  1 
ATOM   2773  N  N   . THR A 1 356 ? 33.372  71.032  18.222  1.00 20.06  ? 365  THR A N   1 
ATOM   2774  C  CA  . THR A 1 356 ? 34.118  71.291  19.446  1.00 18.42  ? 365  THR A CA  1 
ATOM   2775  C  C   . THR A 1 356 ? 34.271  72.746  19.823  1.00 22.33  ? 365  THR A C   1 
ATOM   2776  O  O   . THR A 1 356 ? 34.113  73.093  21.004  1.00 21.74  ? 365  THR A O   1 
ATOM   2777  C  CB  . THR A 1 356 ? 35.530  70.748  19.208  1.00 21.78  ? 365  THR A CB  1 
ATOM   2778  O  OG1 . THR A 1 356 ? 35.419  69.338  18.953  1.00 23.30  ? 365  THR A OG1 1 
ATOM   2779  C  CG2 . THR A 1 356 ? 36.502  70.995  20.399  1.00 22.57  ? 365  THR A CG2 1 
ATOM   2780  N  N   . PHE A 1 357 ? 34.585  73.588  18.855  1.00 19.88  ? 366  PHE A N   1 
ATOM   2781  C  CA  . PHE A 1 357 ? 34.883  75.024  19.134  1.00 21.20  ? 366  PHE A CA  1 
ATOM   2782  C  C   . PHE A 1 357 ? 33.733  75.963  18.932  1.00 19.13  ? 366  PHE A C   1 
ATOM   2783  O  O   . PHE A 1 357 ? 33.872  77.144  19.298  1.00 19.08  ? 366  PHE A O   1 
ATOM   2784  C  CB  . PHE A 1 357 ? 36.095  75.457  18.242  1.00 18.16  ? 366  PHE A CB  1 
ATOM   2785  C  CG  . PHE A 1 357 ? 37.350  74.692  18.657  1.00 18.51  ? 366  PHE A CG  1 
ATOM   2786  C  CD1 . PHE A 1 357 ? 37.894  73.737  17.843  1.00 19.86  ? 366  PHE A CD1 1 
ATOM   2787  C  CD2 . PHE A 1 357 ? 37.965  74.932  19.881  1.00 21.91  ? 366  PHE A CD2 1 
ATOM   2788  C  CE1 . PHE A 1 357 ? 39.033  73.027  18.215  1.00 23.23  ? 366  PHE A CE1 1 
ATOM   2789  C  CE2 . PHE A 1 357 ? 39.110  74.216  20.262  1.00 20.73  ? 366  PHE A CE2 1 
ATOM   2790  C  CZ  . PHE A 1 357 ? 39.630  73.279  19.425  1.00 19.45  ? 366  PHE A CZ  1 
ATOM   2791  N  N   . TYR A 1 358 ? 32.597  75.513  18.362  1.00 18.59  ? 367  TYR A N   1 
ATOM   2792  C  CA  . TYR A 1 358 ? 31.404  76.348  18.193  1.00 19.12  ? 367  TYR A CA  1 
ATOM   2793  C  C   . TYR A 1 358 ? 30.216  75.465  18.782  1.00 21.25  ? 367  TYR A C   1 
ATOM   2794  O  O   . TYR A 1 358 ? 29.308  75.072  18.046  1.00 20.46  ? 367  TYR A O   1 
ATOM   2795  C  CB  . TYR A 1 358 ? 31.122  76.645  16.687  1.00 20.58  ? 367  TYR A CB  1 
ATOM   2796  C  CG  . TYR A 1 358 ? 32.212  77.527  16.111  1.00 22.26  ? 367  TYR A CG  1 
ATOM   2797  C  CD1 . TYR A 1 358 ? 32.086  78.918  16.116  1.00 21.53  ? 367  TYR A CD1 1 
ATOM   2798  C  CD2 . TYR A 1 358 ? 33.406  76.976  15.631  1.00 16.76  ? 367  TYR A CD2 1 
ATOM   2799  C  CE1 . TYR A 1 358 ? 33.119  79.734  15.651  1.00 18.01  ? 367  TYR A CE1 1 
ATOM   2800  C  CE2 . TYR A 1 358 ? 34.443  77.787  15.166  1.00 16.01  ? 367  TYR A CE2 1 
ATOM   2801  C  CZ  . TYR A 1 358 ? 34.287  79.161  15.168  1.00 18.02  ? 367  TYR A CZ  1 
ATOM   2802  O  OH  . TYR A 1 358 ? 35.280  79.934  14.619  1.00 20.23  ? 367  TYR A OH  1 
ATOM   2803  N  N   . PRO A 1 359 ? 30.247  75.184  20.073  1.00 23.17  ? 368  PRO A N   1 
ATOM   2804  C  CA  . PRO A 1 359 ? 29.255  74.375  20.772  1.00 26.58  ? 368  PRO A CA  1 
ATOM   2805  C  C   . PRO A 1 359 ? 27.849  74.949  20.809  1.00 29.73  ? 368  PRO A C   1 
ATOM   2806  O  O   . PRO A 1 359 ? 26.907  74.187  20.965  1.00 30.23  ? 368  PRO A O   1 
ATOM   2807  C  CB  . PRO A 1 359 ? 29.858  74.236  22.171  1.00 27.05  ? 368  PRO A CB  1 
ATOM   2808  C  CG  . PRO A 1 359 ? 30.585  75.471  22.364  1.00 28.01  ? 368  PRO A CG  1 
ATOM   2809  C  CD  . PRO A 1 359 ? 31.240  75.709  21.027  1.00 25.58  ? 368  PRO A CD  1 
ATOM   2810  N  N   . ASP A 1 360 ? 27.686  76.262  20.700  1.00 27.66  ? 369  ASP A N   1 
ATOM   2811  C  CA  . ASP A 1 360 ? 26.346  76.811  20.761  1.00 27.13  ? 369  ASP A CA  1 
ATOM   2812  C  C   . ASP A 1 360 ? 25.423  76.205  19.715  1.00 29.17  ? 369  ASP A C   1 
ATOM   2813  O  O   . ASP A 1 360 ? 25.829  75.961  18.579  1.00 29.24  ? 369  ASP A O   1 
ATOM   2814  C  CB  . ASP A 1 360 ? 26.391  78.326  20.539  1.00 32.36  ? 369  ASP A CB  1 
ATOM   2815  C  CG  . ASP A 1 360 ? 27.044  79.142  21.653  1.00 39.32  ? 369  ASP A CG  1 
ATOM   2816  O  OD1 . ASP A 1 360 ? 27.385  78.565  22.687  1.00 40.58  ? 369  ASP A OD1 1 
ATOM   2817  O  OD2 . ASP A 1 360 ? 27.217  80.361  21.469  1.00 42.19  ? 369  ASP A OD2 1 
ATOM   2818  N  N   . LYS A 1 361 ? 24.137  75.955  20.091  1.00 27.18  ? 370  LYS A N   1 
ATOM   2819  C  CA  . LYS A 1 361 ? 23.199  75.443  19.106  1.00 29.70  ? 370  LYS A CA  1 
ATOM   2820  C  C   . LYS A 1 361 ? 22.705  76.541  18.186  1.00 27.16  ? 370  LYS A C   1 
ATOM   2821  O  O   . LYS A 1 361 ? 22.192  76.233  17.114  1.00 27.58  ? 370  LYS A O   1 
ATOM   2822  C  CB  . LYS A 1 361 ? 21.979  74.768  19.795  1.00 34.98  ? 370  LYS A CB  1 
ATOM   2823  C  CG  . LYS A 1 361 ? 22.341  73.425  20.431  1.00 39.45  ? 370  LYS A CG  1 
ATOM   2824  C  CD  . LYS A 1 361 ? 21.632  73.334  21.806  1.00 49.66  ? 370  LYS A CD  1 
ATOM   2825  C  CE  . LYS A 1 361 ? 22.554  72.861  22.898  0.00 0.00   ? 370  LYS A CE  1 
ATOM   2826  N  NZ  . LYS A 1 361 ? 22.756  73.925  23.911  0.00 0.00   ? 370  LYS A NZ  1 
ATOM   2827  N  N   . GLU A 1 362 ? 22.844  77.810  18.562  1.00 27.66  ? 371  GLU A N   1 
ATOM   2828  C  CA  . GLU A 1 362 ? 22.398  78.912  17.671  1.00 28.17  ? 371  GLU A CA  1 
ATOM   2829  C  C   . GLU A 1 362 ? 23.606  79.751  17.271  1.00 26.54  ? 371  GLU A C   1 
ATOM   2830  O  O   . GLU A 1 362 ? 24.169  80.457  18.104  1.00 30.22  ? 371  GLU A O   1 
ATOM   2831  C  CB  . GLU A 1 362 ? 21.338  79.796  18.388  1.00 29.88  ? 371  GLU A CB  1 
ATOM   2832  C  CG  . GLU A 1 362 ? 20.176  78.909  18.842  1.00 39.73  ? 371  GLU A CG  1 
ATOM   2833  C  CD  . GLU A 1 362 ? 18.911  79.683  19.199  1.00 51.31  ? 371  GLU A CD  1 
ATOM   2834  O  OE1 . GLU A 1 362 ? 19.022  80.829  19.712  1.00 51.40  ? 371  GLU A OE1 1 
ATOM   2835  O  OE2 . GLU A 1 362 ? 17.809  79.127  18.942  1.00 51.92  ? 371  GLU A OE2 1 
ATOM   2836  N  N   . LEU A 1 363 ? 24.029  79.648  16.035  1.00 25.12  ? 372  LEU A N   1 
ATOM   2837  C  CA  . LEU A 1 363 ? 25.203  80.415  15.619  1.00 24.44  ? 372  LEU A CA  1 
ATOM   2838  C  C   . LEU A 1 363 ? 24.739  81.779  15.077  1.00 24.69  ? 372  LEU A C   1 
ATOM   2839  O  O   . LEU A 1 363 ? 23.598  81.899  14.634  1.00 24.06  ? 372  LEU A O   1 
ATOM   2840  C  CB  . LEU A 1 363 ? 25.906  79.653  14.498  1.00 22.63  ? 372  LEU A CB  1 
ATOM   2841  C  CG  . LEU A 1 363 ? 26.352  78.223  14.897  1.00 22.86  ? 372  LEU A CG  1 
ATOM   2842  C  CD1 . LEU A 1 363 ? 26.836  77.544  13.599  1.00 22.26  ? 372  LEU A CD1 1 
ATOM   2843  C  CD2 . LEU A 1 363 ? 27.407  78.260  16.011  1.00 23.91  ? 372  LEU A CD2 1 
ATOM   2844  N  N   . SER A 1 364 ? 25.603  82.775  15.095  1.00 24.59  ? 373  SER A N   1 
ATOM   2845  C  CA  . SER A 1 364 ? 25.211  84.064  14.516  1.00 26.28  ? 373  SER A CA  1 
ATOM   2846  C  C   . SER A 1 364 ? 25.315  83.940  12.994  1.00 26.79  ? 373  SER A C   1 
ATOM   2847  O  O   . SER A 1 364 ? 24.655  84.670  12.268  1.00 24.82  ? 373  SER A O   1 
ATOM   2848  C  CB  . SER A 1 364 ? 26.169  85.148  14.992  1.00 27.18  ? 373  SER A CB  1 
ATOM   2849  O  OG  . SER A 1 364 ? 27.477  84.775  14.570  1.00 29.72  ? 373  SER A OG  1 
ATOM   2850  N  N   . ALA A 1 365 ? 26.168  83.030  12.495  1.00 21.06  ? 374  ALA A N   1 
ATOM   2851  C  CA  . ALA A 1 365 ? 26.310  82.894  11.046  1.00 17.23  ? 374  ALA A CA  1 
ATOM   2852  C  C   . ALA A 1 365 ? 27.066  81.641  10.689  1.00 18.70  ? 374  ALA A C   1 
ATOM   2853  O  O   . ALA A 1 365 ? 27.609  81.001  11.582  1.00 19.26  ? 374  ALA A O   1 
ATOM   2854  C  CB  . ALA A 1 365 ? 27.085  84.062  10.485  1.00 18.08  ? 374  ALA A CB  1 
ATOM   2855  N  N   . MET A 1 366 ? 27.109  81.307  9.396   1.00 18.69  ? 375  MET A N   1 
ATOM   2856  C  CA  . MET A 1 366 ? 27.929  80.180  8.944   1.00 18.59  ? 375  MET A CA  1 
ATOM   2857  C  C   . MET A 1 366 ? 28.459  80.604  7.680   1.00 20.73  ? 375  MET A C   1 
ATOM   2858  O  O   . MET A 1 366 ? 27.695  81.018  6.829   1.00 20.48  ? 375  MET A O   1 
ATOM   2859  C  CB  A MET A 1 366 ? 27.111  78.864  8.752   0.71 19.55  ? 375  MET A CB  1 
ATOM   2860  C  CB  B MET A 1 366 ? 27.234  78.817  8.898   0.29 23.93  ? 375  MET A CB  1 
ATOM   2861  C  CG  A MET A 1 366 ? 27.974  77.698  8.206   0.71 23.66  ? 375  MET A CG  1 
ATOM   2862  C  CG  B MET A 1 366 ? 28.138  77.697  8.357   0.29 25.72  ? 375  MET A CG  1 
ATOM   2863  S  SD  A MET A 1 366 ? 28.862  76.946  9.566   0.71 24.18  ? 375  MET A SD  1 
ATOM   2864  S  SD  B MET A 1 366 ? 27.561  76.017  8.708   0.29 25.68  ? 375  MET A SD  1 
ATOM   2865  C  CE  A MET A 1 366 ? 27.574  75.851  10.226  0.71 19.22  ? 375  MET A CE  1 
ATOM   2866  C  CE  B MET A 1 366 ? 27.545  76.029  10.488  0.29 23.06  ? 375  MET A CE  1 
ATOM   2867  N  N   . LEU A 1 367 ? 29.790  80.569  7.506   1.00 16.45  ? 376  LEU A N   1 
ATOM   2868  C  CA  . LEU A 1 367 ? 30.359  80.965  6.219   1.00 16.69  ? 376  LEU A CA  1 
ATOM   2869  C  C   . LEU A 1 367 ? 30.683  79.693  5.465   1.00 19.26  ? 376  LEU A C   1 
ATOM   2870  O  O   . LEU A 1 367 ? 31.408  78.854  5.999   1.00 21.89  ? 376  LEU A O   1 
ATOM   2871  C  CB  . LEU A 1 367 ? 31.670  81.826  6.413   1.00 16.83  ? 376  LEU A CB  1 
ATOM   2872  C  CG  . LEU A 1 367 ? 31.428  83.311  6.889   1.00 18.30  ? 376  LEU A CG  1 
ATOM   2873  C  CD1 . LEU A 1 367 ? 31.177  83.282  8.424   1.00 15.45  ? 376  LEU A CD1 1 
ATOM   2874  C  CD2 . LEU A 1 367 ? 32.633  84.223  6.589   1.00 21.08  ? 376  LEU A CD2 1 
ATOM   2875  N  N   . VAL A 1 368 ? 30.252  79.579  4.193   1.00 17.80  ? 377  VAL A N   1 
ATOM   2876  C  CA  . VAL A 1 368 ? 30.438  78.301  3.485   1.00 19.70  ? 377  VAL A CA  1 
ATOM   2877  C  C   . VAL A 1 368 ? 31.347  78.445  2.303   1.00 21.40  ? 377  VAL A C   1 
ATOM   2878  O  O   . VAL A 1 368 ? 31.040  79.198  1.393   1.00 21.47  ? 377  VAL A O   1 
ATOM   2879  C  CB  . VAL A 1 368 ? 29.042  77.794  2.988   1.00 20.20  ? 377  VAL A CB  1 
ATOM   2880  C  CG1 . VAL A 1 368 ? 29.231  76.466  2.190   1.00 21.51  ? 377  VAL A CG1 1 
ATOM   2881  C  CG2 . VAL A 1 368 ? 28.126  77.580  4.184   1.00 18.81  ? 377  VAL A CG2 1 
ATOM   2882  N  N   . ALA A 1 369 ? 32.496  77.726  2.316   1.00 19.02  ? 378  ALA A N   1 
ATOM   2883  C  CA  . ALA A 1 369 ? 33.464  77.789  1.255   1.00 19.30  ? 378  ALA A CA  1 
ATOM   2884  C  C   . ALA A 1 369 ? 33.653  76.382  0.621   1.00 22.35  ? 378  ALA A C   1 
ATOM   2885  O  O   . ALA A 1 369 ? 33.387  75.354  1.249   1.00 20.59  ? 378  ALA A O   1 
ATOM   2886  C  CB  . ALA A 1 369 ? 34.830  78.222  1.827   1.00 19.72  ? 378  ALA A CB  1 
ATOM   2887  N  N   . LYS A 1 370 ? 34.099  76.376  -0.627  1.00 22.86  ? 379  LYS A N   1 
ATOM   2888  C  CA  . LYS A 1 370 ? 34.382  75.151  -1.345  1.00 25.17  ? 379  LYS A CA  1 
ATOM   2889  C  C   . LYS A 1 370 ? 35.562  74.492  -0.704  1.00 22.59  ? 379  LYS A C   1 
ATOM   2890  O  O   . LYS A 1 370 ? 36.528  75.188  -0.408  1.00 23.54  ? 379  LYS A O   1 
ATOM   2891  C  CB  . LYS A 1 370 ? 34.721  75.515  -2.793  1.00 27.25  ? 379  LYS A CB  1 
ATOM   2892  C  CG  . LYS A 1 370 ? 33.490  76.020  -3.561  1.00 29.63  ? 379  LYS A CG  1 
ATOM   2893  C  CD  . LYS A 1 370 ? 33.842  76.465  -5.028  1.00 32.48  ? 379  LYS A CD  1 
ATOM   2894  C  CE  . LYS A 1 370 ? 34.706  77.704  -5.058  1.00 30.45  ? 379  LYS A CE  1 
ATOM   2895  N  NZ  . LYS A 1 370 ? 35.303  77.950  -6.402  1.00 38.97  ? 379  LYS A NZ  1 
ATOM   2896  N  N   . SER A 1 371 ? 35.589  73.161  -0.544  1.00 20.60  ? 380  SER A N   1 
ATOM   2897  C  CA  . SER A 1 371 ? 36.741  72.543  0.128   1.00 23.20  ? 380  SER A CA  1 
ATOM   2898  C  C   . SER A 1 371 ? 37.839  72.160  -0.830  1.00 28.70  ? 380  SER A C   1 
ATOM   2899  O  O   . SER A 1 371 ? 38.849  71.622  -0.375  1.00 29.66  ? 380  SER A O   1 
ATOM   2900  C  CB  . SER A 1 371 ? 36.301  71.278  0.851   1.00 25.62  ? 380  SER A CB  1 
ATOM   2901  O  OG  . SER A 1 371 ? 35.636  70.438  -0.081  1.00 24.13  ? 380  SER A OG  1 
ATOM   2902  N  N   . ASP A 1 372 ? 37.674  72.396  -2.135  1.00 27.95  ? 381  ASP A N   1 
ATOM   2903  C  CA  . ASP A 1 372 ? 38.750  72.018  -3.068  1.00 32.38  ? 381  ASP A CA  1 
ATOM   2904  C  C   . ASP A 1 372 ? 39.846  73.045  -3.188  1.00 35.55  ? 381  ASP A C   1 
ATOM   2905  O  O   . ASP A 1 372 ? 40.866  72.749  -3.790  1.00 37.24  ? 381  ASP A O   1 
ATOM   2906  C  CB  . ASP A 1 372 ? 38.221  71.729  -4.494  1.00 33.76  ? 381  ASP A CB  1 
ATOM   2907  C  CG  . ASP A 1 372 ? 37.365  72.824  -5.095  1.00 44.64  ? 381  ASP A CG  1 
ATOM   2908  O  OD1 . ASP A 1 372 ? 37.541  73.130  -6.290  1.00 52.97  ? 381  ASP A OD1 1 
ATOM   2909  O  OD2 . ASP A 1 372 ? 36.507  73.353  -4.396  1.00 45.77  ? 381  ASP A OD2 1 
ATOM   2910  N  N   . ILE A 1 373 ? 39.682  74.215  -2.641  1.00 35.61  ? 382  ILE A N   1 
ATOM   2911  C  CA  . ILE A 1 373 ? 40.756  75.193  -2.743  1.00 39.04  ? 382  ILE A CA  1 
ATOM   2912  C  C   . ILE A 1 373 ? 41.065  75.671  -1.344  1.00 37.90  ? 382  ILE A C   1 
ATOM   2913  O  O   . ILE A 1 373 ? 40.261  75.428  -0.430  1.00 39.34  ? 382  ILE A O   1 
ATOM   2914  C  CB  . ILE A 1 373 ? 40.314  76.338  -3.648  1.00 41.74  ? 382  ILE A CB  1 
ATOM   2915  C  CG1 . ILE A 1 373 ? 38.940  76.849  -3.200  1.00 44.86  ? 382  ILE A CG1 1 
ATOM   2916  C  CG2 . ILE A 1 373 ? 40.249  75.843  -5.118  1.00 44.09  ? 382  ILE A CG2 1 
ATOM   2917  C  CD1 . ILE A 1 373 ? 38.481  77.964  -4.094  1.00 52.73  ? 382  ILE A CD1 1 
ATOM   2918  N  N   . ILE A 1 374 ? 42.176  76.279  -1.141  1.00 28.97  ? 383  ILE A N   1 
ATOM   2919  C  CA  . ILE A 1 374 ? 42.476  76.756  0.202   1.00 31.52  ? 383  ILE A CA  1 
ATOM   2920  C  C   . ILE A 1 374 ? 42.182  78.289  0.324   1.00 29.08  ? 383  ILE A C   1 
ATOM   2921  O  O   . ILE A 1 374 ? 41.760  78.745  1.367   1.00 24.68  ? 383  ILE A O   1 
ATOM   2922  C  CB  . ILE A 1 374 ? 44.006  76.562  0.453   1.00 32.86  ? 383  ILE A CB  1 
ATOM   2923  C  CG1 . ILE A 1 374 ? 44.358  75.035  0.485   1.00 41.08  ? 383  ILE A CG1 1 
ATOM   2924  C  CG2 . ILE A 1 374 ? 44.418  77.250  1.749   1.00 33.25  ? 383  ILE A CG2 1 
ATOM   2925  C  CD1 . ILE A 1 374 ? 43.706  74.344  1.643   1.00 48.60  ? 383  ILE A CD1 1 
ATOM   2926  N  N   . VAL A 1 375 ? 42.425  79.037  -0.772  1.00 27.53  ? 384  VAL A N   1 
ATOM   2927  C  CA  . VAL A 1 375 ? 42.425  80.502  -0.670  1.00 24.43  ? 384  VAL A CA  1 
ATOM   2928  C  C   . VAL A 1 375 ? 41.088  81.114  -0.257  1.00 24.91  ? 384  VAL A C   1 
ATOM   2929  O  O   . VAL A 1 375 ? 41.137  82.093  0.467   1.00 24.68  ? 384  VAL A O   1 
ATOM   2930  C  CB  . VAL A 1 375 ? 42.899  81.082  -2.018  1.00 29.04  ? 384  VAL A CB  1 
ATOM   2931  C  CG1 . VAL A 1 375 ? 41.870  80.761  -3.125  1.00 28.96  ? 384  VAL A CG1 1 
ATOM   2932  C  CG2 . VAL A 1 375 ? 43.118  82.602  -1.896  1.00 29.61  ? 384  VAL A CG2 1 
ATOM   2933  N  N   . ASP A 1 376 ? 39.933  80.559  -0.669  1.00 23.38  ? 385  ASP A N   1 
ATOM   2934  C  CA  . ASP A 1 376 ? 38.672  81.226  -0.307  1.00 23.71  ? 385  ASP A CA  1 
ATOM   2935  C  C   . ASP A 1 376 ? 38.472  81.163  1.200   1.00 22.13  ? 385  ASP A C   1 
ATOM   2936  O  O   . ASP A 1 376 ? 37.862  82.073  1.764   1.00 21.13  ? 385  ASP A O   1 
ATOM   2937  C  CB  . ASP A 1 376 ? 37.484  80.578  -1.029  1.00 26.60  ? 385  ASP A CB  1 
ATOM   2938  C  CG  . ASP A 1 376 ? 37.331  81.061  -2.486  1.00 33.80  ? 385  ASP A CG  1 
ATOM   2939  O  OD1 . ASP A 1 376 ? 38.091  81.990  -2.906  1.00 29.41  ? 385  ASP A OD1 1 
ATOM   2940  O  OD2 . ASP A 1 376 ? 36.477  80.511  -3.209  1.00 32.79  ? 385  ASP A OD2 1 
ATOM   2941  N  N   . SER A 1 377 ? 38.927  80.065  1.857   1.00 21.20  ? 386  SER A N   1 
ATOM   2942  C  CA  . SER A 1 377 ? 38.738  79.984  3.322   1.00 19.27  ? 386  SER A CA  1 
ATOM   2943  C  C   . SER A 1 377 ? 39.719  80.947  3.990   1.00 21.21  ? 386  SER A C   1 
ATOM   2944  O  O   . SER A 1 377 ? 39.443  81.476  5.058   1.00 22.51  ? 386  SER A O   1 
ATOM   2945  C  CB  . SER A 1 377 ? 38.993  78.565  3.822   1.00 23.57  ? 386  SER A CB  1 
ATOM   2946  O  OG  . SER A 1 377 ? 37.917  77.754  3.371   1.00 25.28  ? 386  SER A OG  1 
ATOM   2947  N  N   . ILE A 1 378 ? 40.894  81.151  3.372   1.00 21.46  ? 387  ILE A N   1 
ATOM   2948  C  CA  . ILE A 1 378 ? 41.858  82.104  3.961   1.00 22.24  ? 387  ILE A CA  1 
ATOM   2949  C  C   . ILE A 1 378 ? 41.278  83.536  3.890   1.00 19.19  ? 387  ILE A C   1 
ATOM   2950  O  O   . ILE A 1 378 ? 41.281  84.233  4.884   1.00 21.63  ? 387  ILE A O   1 
ATOM   2951  C  CB  . ILE A 1 378 ? 43.193  82.082  3.143   1.00 24.63  ? 387  ILE A CB  1 
ATOM   2952  C  CG1 . ILE A 1 378 ? 43.955  80.794  3.430   1.00 31.20  ? 387  ILE A CG1 1 
ATOM   2953  C  CG2 . ILE A 1 378 ? 44.098  83.233  3.588   1.00 27.35  ? 387  ILE A CG2 1 
ATOM   2954  C  CD1 . ILE A 1 378 ? 45.137  80.673  2.483   1.00 34.64  ? 387  ILE A CD1 1 
ATOM   2955  N  N   . THR A 1 379 ? 40.747  83.935  2.719   1.00 18.80  ? 388  THR A N   1 
ATOM   2956  C  CA  . THR A 1 379 ? 40.241  85.320  2.665   1.00 20.38  ? 388  THR A CA  1 
ATOM   2957  C  C   . THR A 1 379 ? 38.942  85.463  3.475   1.00 20.19  ? 388  THR A C   1 
ATOM   2958  O  O   . THR A 1 379 ? 38.653  86.537  3.964   1.00 19.71  ? 388  THR A O   1 
ATOM   2959  C  CB  . THR A 1 379 ? 40.065  85.771  1.227   1.00 21.31  ? 388  THR A CB  1 
ATOM   2960  O  OG1 . THR A 1 379 ? 39.173  84.831  0.570   1.00 20.72  ? 388  THR A OG1 1 
ATOM   2961  C  CG2 . THR A 1 379 ? 41.418  85.838  0.511   1.00 19.05  ? 388  THR A CG2 1 
ATOM   2962  N  N   . ALA A 1 380 ? 38.157  84.386  3.640   1.00 19.92  ? 389  ALA A N   1 
ATOM   2963  C  CA  . ALA A 1 380 ? 36.940  84.504  4.455   1.00 16.28  ? 389  ALA A CA  1 
ATOM   2964  C  C   . ALA A 1 380 ? 37.291  84.549  5.919   1.00 17.94  ? 389  ALA A C   1 
ATOM   2965  O  O   . ALA A 1 380 ? 36.508  85.017  6.731   1.00 17.44  ? 389  ALA A O   1 
ATOM   2966  C  CB  . ALA A 1 380 ? 36.034  83.280  4.172   1.00 17.69  ? 389  ALA A CB  1 
ATOM   2967  N  N   . GLY A 1 381 ? 38.485  84.050  6.276   1.00 15.54  ? 390  GLY A N   1 
ATOM   2968  C  CA  . GLY A 1 381 ? 38.832  83.947  7.700   1.00 15.72  ? 390  GLY A CA  1 
ATOM   2969  C  C   . GLY A 1 381 ? 38.678  85.201  8.527   1.00 16.40  ? 390  GLY A C   1 
ATOM   2970  O  O   . GLY A 1 381 ? 38.087  85.153  9.623   1.00 15.03  ? 390  GLY A O   1 
ATOM   2971  N  N   . PRO A 1 382 ? 39.224  86.358  8.082   1.00 17.70  ? 391  PRO A N   1 
ATOM   2972  C  CA  . PRO A 1 382 ? 39.110  87.625  8.873   1.00 19.83  ? 391  PRO A CA  1 
ATOM   2973  C  C   . PRO A 1 382 ? 37.632  88.031  9.129   1.00 14.77  ? 391  PRO A C   1 
ATOM   2974  O  O   . PRO A 1 382 ? 37.282  88.589  10.139  1.00 16.15  ? 391  PRO A O   1 
ATOM   2975  C  CB  . PRO A 1 382 ? 39.919  88.635  7.999   1.00 17.06  ? 391  PRO A CB  1 
ATOM   2976  C  CG  . PRO A 1 382 ? 40.923  87.771  7.343   1.00 18.30  ? 391  PRO A CG  1 
ATOM   2977  C  CD  . PRO A 1 382 ? 40.114  86.542  6.918   1.00 17.45  ? 391  PRO A CD  1 
ATOM   2978  N  N   . LEU A 1 383 ? 36.807  87.750  8.126   1.00 13.26  ? 392  LEU A N   1 
ATOM   2979  C  CA  . LEU A 1 383 ? 35.367  88.089  8.257   1.00 14.34  ? 392  LEU A CA  1 
ATOM   2980  C  C   . LEU A 1 383 ? 34.677  87.133  9.171   1.00 13.54  ? 392  LEU A C   1 
ATOM   2981  O  O   . LEU A 1 383 ? 33.901  87.544  10.052  1.00 15.51  ? 392  LEU A O   1 
ATOM   2982  C  CB  . LEU A 1 383 ? 34.703  88.070  6.836   1.00 15.95  ? 392  LEU A CB  1 
ATOM   2983  C  CG  . LEU A 1 383 ? 33.149  88.375  6.924   1.00 14.60  ? 392  LEU A CG  1 
ATOM   2984  C  CD1 . LEU A 1 383 ? 32.907  89.820  7.403   1.00 16.54  ? 392  LEU A CD1 1 
ATOM   2985  C  CD2 . LEU A 1 383 ? 32.545  88.194  5.489   1.00 16.00  ? 392  LEU A CD2 1 
ATOM   2986  N  N   . ALA A 1 384 ? 34.988  85.815  9.040   1.00 14.90  ? 393  ALA A N   1 
ATOM   2987  C  CA  . ALA A 1 384 ? 34.410  84.827  9.966   1.00 15.19  ? 393  ALA A CA  1 
ATOM   2988  C  C   . ALA A 1 384 ? 34.836  85.203  11.422  1.00 16.06  ? 393  ALA A C   1 
ATOM   2989  O  O   . ALA A 1 384 ? 34.073  85.166  12.386  1.00 16.06  ? 393  ALA A O   1 
ATOM   2990  C  CB  . ALA A 1 384 ? 34.976  83.424  9.592   1.00 13.11  ? 393  ALA A CB  1 
ATOM   2991  N  N   . ALA A 1 385 ? 36.115  85.603  11.577  1.00 15.34  ? 394  ALA A N   1 
ATOM   2992  C  CA  . ALA A 1 385 ? 36.573  85.961  12.935  1.00 16.03  ? 394  ALA A CA  1 
ATOM   2993  C  C   . ALA A 1 385 ? 35.801  87.229  13.472  1.00 17.03  ? 394  ALA A C   1 
ATOM   2994  O  O   . ALA A 1 385 ? 35.410  87.260  14.619  1.00 18.82  ? 394  ALA A O   1 
ATOM   2995  C  CB  . ALA A 1 385 ? 38.044  86.319  12.870  1.00 14.61  ? 394  ALA A CB  1 
ATOM   2996  N  N   . LYS A 1 386 ? 35.634  88.233  12.635  1.00 16.33  ? 395  LYS A N   1 
ATOM   2997  C  CA  . LYS A 1 386 ? 34.896  89.485  13.005  1.00 15.70  ? 395  LYS A CA  1 
ATOM   2998  C  C   . LYS A 1 386 ? 33.423  89.111  13.428  1.00 16.84  ? 395  LYS A C   1 
ATOM   2999  O  O   . LYS A 1 386 ? 32.901  89.582  14.429  1.00 18.91  ? 395  LYS A O   1 
ATOM   3000  C  CB  . LYS A 1 386 ? 34.849  90.397  11.748  1.00 14.88  ? 395  LYS A CB  1 
ATOM   3001  C  CG  . LYS A 1 386 ? 34.107  91.751  12.031  1.00 18.15  ? 395  LYS A CG  1 
ATOM   3002  C  CD  . LYS A 1 386 ? 34.173  92.628  10.748  1.00 25.50  ? 395  LYS A CD  1 
ATOM   3003  C  CE  . LYS A 1 386 ? 33.294  93.883  10.924  1.00 35.45  ? 395  LYS A CE  1 
ATOM   3004  N  NZ  . LYS A 1 386 ? 33.864  94.862  11.911  1.00 36.71  ? 395  LYS A NZ  1 
ATOM   3005  N  N   . LEU A 1 387 ? 32.799  88.255  12.656  1.00 16.06  ? 396  LEU A N   1 
ATOM   3006  C  CA  . LEU A 1 387 ? 31.412  87.806  12.931  1.00 17.17  ? 396  LEU A CA  1 
ATOM   3007  C  C   . LEU A 1 387 ? 31.323  86.767  14.056  1.00 19.07  ? 396  LEU A C   1 
ATOM   3008  O  O   . LEU A 1 387 ? 30.205  86.431  14.494  1.00 19.67  ? 396  LEU A O   1 
ATOM   3009  C  CB  . LEU A 1 387 ? 30.831  87.163  11.644  1.00 16.58  ? 396  LEU A CB  1 
ATOM   3010  C  CG  . LEU A 1 387 ? 30.778  88.101  10.440  1.00 16.04  ? 396  LEU A CG  1 
ATOM   3011  C  CD1 . LEU A 1 387 ? 30.274  87.318  9.185   1.00 18.24  ? 396  LEU A CD1 1 
ATOM   3012  C  CD2 . LEU A 1 387 ? 29.820  89.336  10.825  1.00 18.06  ? 396  LEU A CD2 1 
ATOM   3013  N  N   . LYS A 1 388 ? 32.484  86.243  14.530  1.00 17.05  ? 397  LYS A N   1 
ATOM   3014  C  CA  . LYS A 1 388 ? 32.592  85.212  15.564  1.00 18.25  ? 397  LYS A CA  1 
ATOM   3015  C  C   . LYS A 1 388 ? 31.735  83.993  15.119  1.00 20.31  ? 397  LYS A C   1 
ATOM   3016  O  O   . LYS A 1 388 ? 30.891  83.492  15.896  1.00 19.78  ? 397  LYS A O   1 
ATOM   3017  C  CB  . LYS A 1 388 ? 32.206  85.752  16.936  1.00 21.08  ? 397  LYS A CB  1 
ATOM   3018  C  CG  . LYS A 1 388 ? 33.112  86.967  17.339  1.00 23.51  ? 397  LYS A CG  1 
ATOM   3019  C  CD  . LYS A 1 388 ? 32.724  87.377  18.776  1.00 29.81  ? 397  LYS A CD  1 
ATOM   3020  C  CE  . LYS A 1 388 ? 33.498  88.554  19.381  1.00 38.06  ? 397  LYS A CE  1 
ATOM   3021  N  NZ  . LYS A 1 388 ? 34.942  88.410  19.164  1.00 47.13  ? 397  LYS A NZ  1 
ATOM   3022  N  N   . ALA A 1 389 ? 31.961  83.566  13.900  1.00 19.85  ? 398  ALA A N   1 
ATOM   3023  C  CA  . ALA A 1 389 ? 31.221  82.497  13.216  1.00 21.19  ? 398  ALA A CA  1 
ATOM   3024  C  C   . ALA A 1 389 ? 32.191  81.514  12.542  1.00 19.93  ? 398  ALA A C   1 
ATOM   3025  O  O   . ALA A 1 389 ? 33.310  81.865  12.196  1.00 18.03  ? 398  ALA A O   1 
ATOM   3026  C  CB  . ALA A 1 389 ? 30.300  83.093  12.140  1.00 18.39  ? 398  ALA A CB  1 
ATOM   3027  N  N   . PRO A 1 390 ? 31.785  80.262  12.370  1.00 18.51  ? 399  PRO A N   1 
ATOM   3028  C  CA  . PRO A 1 390 ? 32.649  79.257  11.737  1.00 15.39  ? 399  PRO A CA  1 
ATOM   3029  C  C   . PRO A 1 390 ? 32.625  79.263  10.241  1.00 17.83  ? 399  PRO A C   1 
ATOM   3030  O  O   . PRO A 1 390 ? 31.684  79.744  9.596   1.00 17.64  ? 399  PRO A O   1 
ATOM   3031  C  CB  . PRO A 1 390 ? 32.067  77.914  12.244  1.00 15.66  ? 399  PRO A CB  1 
ATOM   3032  C  CG  . PRO A 1 390 ? 30.520  78.272  12.497  1.00 16.84  ? 399  PRO A CG  1 
ATOM   3033  C  CD  . PRO A 1 390 ? 30.495  79.732  12.901  1.00 16.67  ? 399  PRO A CD  1 
ATOM   3034  N  N   . ILE A 1 391 ? 33.693  78.690  9.664   1.00 16.60  ? 400  ILE A N   1 
ATOM   3035  C  CA  . ILE A 1 391 ? 33.695  78.447  8.231   1.00 15.21  ? 400  ILE A CA  1 
ATOM   3036  C  C   . ILE A 1 391 ? 33.420  76.926  8.051   1.00 19.11  ? 400  ILE A C   1 
ATOM   3037  O  O   . ILE A 1 391 ? 34.086  76.092  8.675   1.00 19.71  ? 400  ILE A O   1 
ATOM   3038  C  CB  . ILE A 1 391 ? 35.078  78.785  7.635   1.00 18.67  ? 400  ILE A CB  1 
ATOM   3039  C  CG1 . ILE A 1 391 ? 35.273  80.338  7.686   1.00 19.55  ? 400  ILE A CG1 1 
ATOM   3040  C  CG2 . ILE A 1 391 ? 35.185  78.282  6.158   1.00 19.81  ? 400  ILE A CG2 1 
ATOM   3041  C  CD1 . ILE A 1 391 ? 36.736  80.735  7.258   1.00 19.98  ? 400  ILE A CD1 1 
ATOM   3042  N  N   . LEU A 1 392 ? 32.447  76.603  7.218   1.00 19.84  ? 401  LEU A N   1 
ATOM   3043  C  CA  . LEU A 1 392 ? 32.137  75.221  6.850   1.00 18.63  ? 401  LEU A CA  1 
ATOM   3044  C  C   . LEU A 1 392 ? 32.686  75.001  5.479   1.00 19.01  ? 401  LEU A C   1 
ATOM   3045  O  O   . LEU A 1 392 ? 32.485  75.857  4.615   1.00 20.50  ? 401  LEU A O   1 
ATOM   3046  C  CB  . LEU A 1 392 ? 30.615  75.070  6.820   1.00 18.70  ? 401  LEU A CB  1 
ATOM   3047  C  CG  . LEU A 1 392 ? 30.184  73.603  6.573   1.00 22.99  ? 401  LEU A CG  1 
ATOM   3048  C  CD1 . LEU A 1 392 ? 28.963  73.332  7.393   1.00 29.59  ? 401  LEU A CD1 1 
ATOM   3049  C  CD2 . LEU A 1 392 ? 29.932  73.448  5.052   1.00 24.59  ? 401  LEU A CD2 1 
ATOM   3050  N  N   . ILE A 1 393 ? 33.410  73.870  5.234   1.00 17.38  ? 402  ILE A N   1 
ATOM   3051  C  CA  . ILE A 1 393 ? 33.874  73.634  3.884   1.00 16.98  ? 402  ILE A CA  1 
ATOM   3052  C  C   . ILE A 1 393 ? 33.183  72.354  3.338   1.00 20.00  ? 402  ILE A C   1 
ATOM   3053  O  O   . ILE A 1 393 ? 32.954  71.427  4.102   1.00 20.26  ? 402  ILE A O   1 
ATOM   3054  C  CB  . ILE A 1 393 ? 35.417  73.459  3.779   1.00 19.53  ? 402  ILE A CB  1 
ATOM   3055  C  CG1 . ILE A 1 393 ? 35.935  72.348  4.723   1.00 16.86  ? 402  ILE A CG1 1 
ATOM   3056  C  CG2 . ILE A 1 393 ? 36.089  74.845  4.160   1.00 20.95  ? 402  ILE A CG2 1 
ATOM   3057  C  CD1 . ILE A 1 393 ? 37.476  72.034  4.488   1.00 19.27  ? 402  ILE A CD1 1 
ATOM   3058  N  N   . THR A 1 394 ? 32.894  72.331  2.048   1.00 21.03  ? 403  THR A N   1 
ATOM   3059  C  CA  . THR A 1 394 ? 32.227  71.159  1.484   1.00 21.15  ? 403  THR A CA  1 
ATOM   3060  C  C   . THR A 1 394 ? 32.482  71.242  0.020   1.00 24.03  ? 403  THR A C   1 
ATOM   3061  O  O   . THR A 1 394 ? 32.783  72.305  -0.525  1.00 22.77  ? 403  THR A O   1 
ATOM   3062  C  CB  . THR A 1 394 ? 30.731  71.176  1.845   1.00 22.93  ? 403  THR A CB  1 
ATOM   3063  O  OG1 . THR A 1 394 ? 30.179  69.868  1.608   1.00 22.52  ? 403  THR A OG1 1 
ATOM   3064  C  CG2 . THR A 1 394 ? 29.936  72.241  1.043   1.00 21.24  ? 403  THR A CG2 1 
ATOM   3065  N  N   . PRO A 1 395 ? 32.415  70.093  -0.684  1.00 25.08  ? 404  PRO A N   1 
ATOM   3066  C  CA  . PRO A 1 395 ? 32.668  70.198  -2.122  1.00 24.70  ? 404  PRO A CA  1 
ATOM   3067  C  C   . PRO A 1 395 ? 31.580  70.992  -2.856  1.00 23.01  ? 404  PRO A C   1 
ATOM   3068  O  O   . PRO A 1 395 ? 30.486  71.171  -2.352  1.00 23.20  ? 404  PRO A O   1 
ATOM   3069  C  CB  . PRO A 1 395 ? 32.715  68.694  -2.575  1.00 25.16  ? 404  PRO A CB  1 
ATOM   3070  C  CG  . PRO A 1 395 ? 33.121  67.964  -1.337  1.00 24.30  ? 404  PRO A CG  1 
ATOM   3071  C  CD  . PRO A 1 395 ? 32.320  68.686  -0.250  1.00 23.45  ? 404  PRO A CD  1 
ATOM   3072  N  N   . LYS A 1 396 ? 31.874  71.385  -4.081  1.00 24.86  ? 405  LYS A N   1 
ATOM   3073  C  CA  . LYS A 1 396 ? 30.920  72.196  -4.860  1.00 29.20  ? 405  LYS A CA  1 
ATOM   3074  C  C   . LYS A 1 396 ? 29.613  71.474  -5.153  1.00 31.47  ? 405  LYS A C   1 
ATOM   3075  O  O   . LYS A 1 396 ? 28.580  72.114  -5.228  1.00 30.92  ? 405  LYS A O   1 
ATOM   3076  C  CB  . LYS A 1 396 ? 31.536  72.554  -6.224  1.00 29.76  ? 405  LYS A CB  1 
ATOM   3077  C  CG  . LYS A 1 396 ? 32.804  73.340  -6.165  1.00 36.85  ? 405  LYS A CG  1 
ATOM   3078  C  CD  . LYS A 1 396 ? 33.185  73.690  -7.598  1.00 43.51  ? 405  LYS A CD  1 
ATOM   3079  C  CE  . LYS A 1 396 ? 34.317  72.839  -8.069  1.00 55.25  ? 405  LYS A CE  1 
ATOM   3080  N  NZ  . LYS A 1 396 ? 35.467  73.682  -8.473  1.00 61.56  ? 405  LYS A NZ  1 
ATOM   3081  N  N   . THR A 1 397 ? 29.651  70.124  -5.303  1.00 31.60  ? 406  THR A N   1 
ATOM   3082  C  CA  . THR A 1 397 ? 28.434  69.419  -5.718  1.00 30.78  ? 406  THR A CA  1 
ATOM   3083  C  C   . THR A 1 397 ? 27.699  68.651  -4.651  1.00 31.10  ? 406  THR A C   1 
ATOM   3084  O  O   . THR A 1 397 ? 26.657  68.102  -4.973  1.00 33.03  ? 406  THR A O   1 
ATOM   3085  C  CB  . THR A 1 397 ? 28.782  68.475  -6.909  1.00 35.33  ? 406  THR A CB  1 
ATOM   3086  O  OG1 . THR A 1 397 ? 29.635  67.449  -6.386  1.00 37.28  ? 406  THR A OG1 1 
ATOM   3087  C  CG2 . THR A 1 397 ? 29.530  69.197  -8.062  1.00 35.32  ? 406  THR A CG2 1 
ATOM   3088  N  N   . TYR A 1 398 ? 28.162  68.572  -3.391  1.00 25.94  ? 407  TYR A N   1 
ATOM   3089  C  CA  . TYR A 1 398 ? 27.343  67.909  -2.389  1.00 24.57  ? 407  TYR A CA  1 
ATOM   3090  C  C   . TYR A 1 398 ? 27.657  68.356  -0.982  1.00 26.73  ? 407  TYR A C   1 
ATOM   3091  O  O   . TYR A 1 398 ? 28.751  68.875  -0.738  1.00 28.92  ? 407  TYR A O   1 
ATOM   3092  C  CB  . TYR A 1 398 ? 27.514  66.339  -2.447  1.00 26.82  ? 407  TYR A CB  1 
ATOM   3093  C  CG  . TYR A 1 398 ? 28.921  65.845  -2.149  1.00 25.81  ? 407  TYR A CG  1 
ATOM   3094  C  CD1 . TYR A 1 398 ? 29.902  65.846  -3.133  1.00 27.05  ? 407  TYR A CD1 1 
ATOM   3095  C  CD2 . TYR A 1 398 ? 29.254  65.338  -0.894  1.00 26.21  ? 407  TYR A CD2 1 
ATOM   3096  C  CE1 . TYR A 1 398 ? 31.182  65.357  -2.885  1.00 26.85  ? 407  TYR A CE1 1 
ATOM   3097  C  CE2 . TYR A 1 398 ? 30.534  64.839  -0.637  1.00 24.82  ? 407  TYR A CE2 1 
ATOM   3098  C  CZ  . TYR A 1 398 ? 31.489  64.856  -1.639  1.00 22.21  ? 407  TYR A CZ  1 
ATOM   3099  O  OH  . TYR A 1 398 ? 32.756  64.399  -1.409  1.00 29.26  ? 407  TYR A OH  1 
ATOM   3100  N  N   . VAL A 1 399 ? 26.734  68.193  -0.079  1.00 22.71  ? 408  VAL A N   1 
ATOM   3101  C  CA  . VAL A 1 399 ? 26.986  68.502  1.306   1.00 20.05  ? 408  VAL A CA  1 
ATOM   3102  C  C   . VAL A 1 399 ? 27.676  67.268  1.878   1.00 25.12  ? 408  VAL A C   1 
ATOM   3103  O  O   . VAL A 1 399 ? 27.113  66.160  1.828   1.00 25.66  ? 408  VAL A O   1 
ATOM   3104  C  CB  . VAL A 1 399 ? 25.701  68.786  2.079   1.00 22.99  ? 408  VAL A CB  1 
ATOM   3105  C  CG1 . VAL A 1 399 ? 26.011  69.009  3.586   1.00 23.12  ? 408  VAL A CG1 1 
ATOM   3106  C  CG2 . VAL A 1 399 ? 24.990  70.004  1.482   1.00 25.99  ? 408  VAL A CG2 1 
ATOM   3107  N  N   . SER A 1 400 ? 28.871  67.412  2.392   1.00 23.67  ? 409  SER A N   1 
ATOM   3108  C  CA  . SER A 1 400 ? 29.503  66.270  3.009   1.00 26.20  ? 409  SER A CA  1 
ATOM   3109  C  C   . SER A 1 400 ? 28.659  65.627  4.123   1.00 24.92  ? 409  SER A C   1 
ATOM   3110  O  O   . SER A 1 400 ? 28.024  66.267  4.969   1.00 22.49  ? 409  SER A O   1 
ATOM   3111  C  CB  . SER A 1 400 ? 30.870  66.679  3.583   1.00 26.18  ? 409  SER A CB  1 
ATOM   3112  O  OG  . SER A 1 400 ? 31.380  65.640  4.404   1.00 26.52  ? 409  SER A OG  1 
ATOM   3113  N  N   . ALA A 1 401 ? 28.651  64.264  4.148   1.00 24.80  ? 410  ALA A N   1 
ATOM   3114  C  CA  . ALA A 1 401 ? 27.894  63.541  5.178   1.00 24.40  ? 410  ALA A CA  1 
ATOM   3115  C  C   . ALA A 1 401 ? 28.371  63.820  6.574   1.00 21.51  ? 410  ALA A C   1 
ATOM   3116  O  O   . ALA A 1 401 ? 27.621  63.728  7.540   1.00 23.78  ? 410  ALA A O   1 
ATOM   3117  C  CB  . ALA A 1 401 ? 28.016  62.002  4.904   1.00 28.16  ? 410  ALA A CB  1 
ATOM   3118  N  N   . TYR A 1 402 ? 29.643  64.208  6.720   1.00 20.93  ? 411  TYR A N   1 
ATOM   3119  C  CA  . TYR A 1 402 ? 30.157  64.465  8.088   1.00 18.90  ? 411  TYR A CA  1 
ATOM   3120  C  C   . TYR A 1 402 ? 29.497  65.732  8.709   1.00 21.11  ? 411  TYR A C   1 
ATOM   3121  O  O   . TYR A 1 402 ? 29.539  65.887  9.930   1.00 21.87  ? 411  TYR A O   1 
ATOM   3122  C  CB  . TYR A 1 402 ? 31.677  64.676  8.015   1.00 21.96  ? 411  TYR A CB  1 
ATOM   3123  C  CG  . TYR A 1 402 ? 32.394  63.399  7.623   1.00 16.94  ? 411  TYR A CG  1 
ATOM   3124  C  CD1 . TYR A 1 402 ? 32.447  62.311  8.488   1.00 22.76  ? 411  TYR A CD1 1 
ATOM   3125  C  CD2 . TYR A 1 402 ? 32.999  63.277  6.392   1.00 20.76  ? 411  TYR A CD2 1 
ATOM   3126  C  CE1 . TYR A 1 402 ? 33.095  61.124  8.127   1.00 19.68  ? 411  TYR A CE1 1 
ATOM   3127  C  CE2 . TYR A 1 402 ? 33.633  62.094  6.006   1.00 23.34  ? 411  TYR A CE2 1 
ATOM   3128  C  CZ  . TYR A 1 402 ? 33.672  61.024  6.877   1.00 24.41  ? 411  TYR A CZ  1 
ATOM   3129  O  OH  . TYR A 1 402 ? 34.287  59.848  6.454   1.00 27.38  ? 411  TYR A OH  1 
ATOM   3130  N  N   . HIS A 1 403 ? 28.902  66.590  7.874   1.00 23.39  ? 412  HIS A N   1 
ATOM   3131  C  CA  . HIS A 1 403 ? 28.211  67.807  8.381   1.00 24.59  ? 412  HIS A CA  1 
ATOM   3132  C  C   . HIS A 1 403 ? 26.790  67.532  8.815   1.00 26.51  ? 412  HIS A C   1 
ATOM   3133  O  O   . HIS A 1 403 ? 26.168  68.387  9.432   1.00 22.92  ? 412  HIS A O   1 
ATOM   3134  C  CB  . HIS A 1 403 ? 28.147  68.900  7.269   1.00 21.23  ? 412  HIS A CB  1 
ATOM   3135  C  CG  . HIS A 1 403 ? 29.498  69.408  6.894   1.00 16.92  ? 412  HIS A CG  1 
ATOM   3136  N  ND1 . HIS A 1 403 ? 30.469  69.679  7.855   1.00 20.20  ? 412  HIS A ND1 1 
ATOM   3137  C  CD2 . HIS A 1 403 ? 30.068  69.630  5.691   1.00 17.98  ? 412  HIS A CD2 1 
ATOM   3138  C  CE1 . HIS A 1 403 ? 31.579  70.050  7.219   1.00 19.66  ? 412  HIS A CE1 1 
ATOM   3139  N  NE2 . HIS A 1 403 ? 31.363  70.037  5.915   1.00 19.01  ? 412  HIS A NE2 1 
ATOM   3140  N  N   . SER A 1 404 ? 26.267  66.301  8.560   1.00 27.62  ? 413  SER A N   1 
ATOM   3141  C  CA  . SER A 1 404 ? 24.843  66.089  8.832   1.00 31.63  ? 413  SER A CA  1 
ATOM   3142  C  C   . SER A 1 404 ? 24.390  66.412  10.186  1.00 27.52  ? 413  SER A C   1 
ATOM   3143  O  O   . SER A 1 404 ? 23.362  67.073  10.340  1.00 28.88  ? 413  SER A O   1 
ATOM   3144  C  CB  . SER A 1 404 ? 24.456  64.626  8.561   1.00 34.35  ? 413  SER A CB  1 
ATOM   3145  O  OG  . SER A 1 404 ? 24.757  64.334  7.221   1.00 41.05  ? 413  SER A OG  1 
ATOM   3146  N  N   . THR A 1 405 ? 25.077  65.940  11.193  1.00 27.08  ? 414  THR A N   1 
ATOM   3147  C  CA  . THR A 1 405 ? 24.635  66.199  12.562  1.00 29.68  ? 414  THR A CA  1 
ATOM   3148  C  C   . THR A 1 405 ? 24.669  67.683  12.985  1.00 31.55  ? 414  THR A C   1 
ATOM   3149  O  O   . THR A 1 405 ? 23.720  68.195  13.581  1.00 29.18  ? 414  THR A O   1 
ATOM   3150  C  CB  . THR A 1 405 ? 25.509  65.397  13.528  1.00 35.04  ? 414  THR A CB  1 
ATOM   3151  O  OG1 . THR A 1 405 ? 25.606  64.054  13.023  1.00 41.05  ? 414  THR A OG1 1 
ATOM   3152  C  CG2 . THR A 1 405 ? 24.957  65.355  14.913  1.00 36.70  ? 414  THR A CG2 1 
ATOM   3153  N  N   . ASN A 1 406 ? 25.808  68.358  12.738  1.00 26.64  ? 415  ASN A N   1 
ATOM   3154  C  CA  . ASN A 1 406 ? 25.914  69.774  13.076  1.00 22.67  ? 415  ASN A CA  1 
ATOM   3155  C  C   . ASN A 1 406 ? 24.815  70.560  12.305  1.00 22.68  ? 415  ASN A C   1 
ATOM   3156  O  O   . ASN A 1 406 ? 24.178  71.403  12.898  1.00 23.96  ? 415  ASN A O   1 
ATOM   3157  C  CB  . ASN A 1 406 ? 27.286  70.310  12.578  1.00 22.72  ? 415  ASN A CB  1 
ATOM   3158  C  CG  . ASN A 1 406 ? 28.459  69.849  13.459  1.00 29.23  ? 415  ASN A CG  1 
ATOM   3159  O  OD1 . ASN A 1 406 ? 28.255  69.413  14.606  1.00 27.81  ? 415  ASN A OD1 1 
ATOM   3160  N  ND2 . ASN A 1 406 ? 29.702  69.900  13.000  1.00 21.90  ? 415  ASN A ND2 1 
ATOM   3161  N  N   . LEU A 1 407 ? 24.637  70.301  10.983  1.00 22.99  ? 416  LEU A N   1 
ATOM   3162  C  CA  . LEU A 1 407 ? 23.646  71.087  10.215  1.00 23.21  ? 416  LEU A CA  1 
ATOM   3163  C  C   . LEU A 1 407 ? 22.211  70.829  10.768  1.00 27.90  ? 416  LEU A C   1 
ATOM   3164  O  O   . LEU A 1 407 ? 21.432  71.770  10.940  1.00 27.07  ? 416  LEU A O   1 
ATOM   3165  C  CB  . LEU A 1 407 ? 23.736  70.786  8.732   1.00 21.58  ? 416  LEU A CB  1 
ATOM   3166  C  CG  . LEU A 1 407 ? 25.071  71.226  8.123   1.00 24.44  ? 416  LEU A CG  1 
ATOM   3167  C  CD1 . LEU A 1 407 ? 25.099  70.866  6.696   1.00 25.03  ? 416  LEU A CD1 1 
ATOM   3168  C  CD2 . LEU A 1 407 ? 25.205  72.787  8.239   1.00 25.84  ? 416  LEU A CD2 1 
ATOM   3169  N  N   . SER A 1 408 ? 21.897  69.568  11.104  1.00 27.97  ? 417  SER A N   1 
ATOM   3170  C  CA  . SER A 1 408 ? 20.612  69.265  11.717  1.00 27.36  ? 417  SER A CA  1 
ATOM   3171  C  C   . SER A 1 408 ? 20.446  69.928  13.063  1.00 26.93  ? 417  SER A C   1 
ATOM   3172  O  O   . SER A 1 408 ? 19.466  70.659  13.269  1.00 29.62  ? 417  SER A O   1 
ATOM   3173  C  CB  . SER A 1 408 ? 20.427  67.744  11.893  1.00 30.39  ? 417  SER A CB  1 
ATOM   3174  O  OG  . SER A 1 408 ? 19.174  67.540  12.524  1.00 33.45  ? 417  SER A OG  1 
ATOM   3175  N  N   . GLU A 1 409 ? 21.355  69.758  13.975  1.00 27.02  ? 418  GLU A N   1 
ATOM   3176  C  CA  . GLU A 1 409 ? 21.108  70.304  15.306  1.00 25.69  ? 418  GLU A CA  1 
ATOM   3177  C  C   . GLU A 1 409 ? 21.151  71.812  15.430  1.00 28.14  ? 418  GLU A C   1 
ATOM   3178  O  O   . GLU A 1 409 ? 20.387  72.377  16.196  1.00 27.15  ? 418  GLU A O   1 
ATOM   3179  C  CB  . GLU A 1 409 ? 22.116  69.765  16.294  1.00 30.87  ? 418  GLU A CB  1 
ATOM   3180  C  CG  . GLU A 1 409 ? 22.041  68.237  16.371  1.00 46.18  ? 418  GLU A CG  1 
ATOM   3181  C  CD  . GLU A 1 409 ? 22.836  67.633  17.529  1.00 61.60  ? 418  GLU A CD  1 
ATOM   3182  O  OE1 . GLU A 1 409 ? 23.902  68.185  17.920  1.00 62.80  ? 418  GLU A OE1 1 
ATOM   3183  O  OE2 . GLU A 1 409 ? 22.380  66.579  18.044  1.00 66.42  ? 418  GLU A OE2 1 
ATOM   3184  N  N   . LYS A 1 410 ? 22.047  72.475  14.689  1.00 23.75  ? 419  LYS A N   1 
ATOM   3185  C  CA  . LYS A 1 410 ? 22.195  73.938  14.905  1.00 22.47  ? 419  LYS A CA  1 
ATOM   3186  C  C   . LYS A 1 410 ? 21.379  74.798  13.976  1.00 24.52  ? 419  LYS A C   1 
ATOM   3187  O  O   . LYS A 1 410 ? 20.821  74.335  12.984  1.00 24.29  ? 419  LYS A O   1 
ATOM   3188  C  CB  . LYS A 1 410 ? 23.684  74.333  14.671  1.00 22.89  ? 419  LYS A CB  1 
ATOM   3189  C  CG  . LYS A 1 410 ? 24.651  73.618  15.612  1.00 23.13  ? 419  LYS A CG  1 
ATOM   3190  C  CD  . LYS A 1 410 ? 26.149  74.180  15.484  1.00 24.25  ? 419  LYS A CD  1 
ATOM   3191  C  CE  . LYS A 1 410 ? 27.138  73.377  16.322  1.00 20.37  ? 419  LYS A CE  1 
ATOM   3192  N  NZ  . LYS A 1 410 ? 26.952  73.580  17.761  1.00 21.45  ? 419  LYS A NZ  1 
ATOM   3193  N  N   . THR A 1 411 ? 21.323  76.097  14.312  1.00 26.52  ? 420  THR A N   1 
ATOM   3194  C  CA  . THR A 1 411 ? 20.744  77.049  13.363  1.00 26.02  ? 420  THR A CA  1 
ATOM   3195  C  C   . THR A 1 411 ? 21.816  78.149  13.223  1.00 22.74  ? 420  THR A C   1 
ATOM   3196  O  O   . THR A 1 411 ? 22.686  78.245  14.090  1.00 21.26  ? 420  THR A O   1 
ATOM   3197  C  CB  . THR A 1 411 ? 19.420  77.696  13.904  1.00 28.68  ? 420  THR A CB  1 
ATOM   3198  O  OG1 . THR A 1 411 ? 19.694  78.365  15.152  1.00 23.71  ? 420  THR A OG1 1 
ATOM   3199  C  CG2 . THR A 1 411 ? 18.339  76.660  14.128  1.00 26.46  ? 420  THR A CG2 1 
ATOM   3200  N  N   . ALA A 1 412 ? 21.782  78.896  12.153  1.00 21.57  ? 421  ALA A N   1 
ATOM   3201  C  CA  . ALA A 1 412 ? 22.687  80.037  11.945  1.00 19.94  ? 421  ALA A CA  1 
ATOM   3202  C  C   . ALA A 1 412 ? 21.745  81.152  11.453  1.00 21.99  ? 421  ALA A C   1 
ATOM   3203  O  O   . ALA A 1 412 ? 20.893  80.890  10.592  1.00 24.03  ? 421  ALA A O   1 
ATOM   3204  C  CB  . ALA A 1 412 ? 23.700  79.740  10.857  1.00 20.67  ? 421  ALA A CB  1 
ATOM   3205  N  N   . GLU A 1 413 ? 21.929  82.402  11.941  1.00 22.61  ? 422  GLU A N   1 
ATOM   3206  C  CA  . GLU A 1 413 ? 21.045  83.503  11.463  1.00 20.79  ? 422  GLU A CA  1 
ATOM   3207  C  C   . GLU A 1 413 ? 21.264  83.827  10.031  1.00 21.95  ? 422  GLU A C   1 
ATOM   3208  O  O   . GLU A 1 413 ? 20.304  84.022  9.301   1.00 22.47  ? 422  GLU A O   1 
ATOM   3209  C  CB  . GLU A 1 413 ? 21.303  84.748  12.310  1.00 21.28  ? 422  GLU A CB  1 
ATOM   3210  C  CG  . GLU A 1 413 ? 20.960  84.449  13.744  1.00 27.41  ? 422  GLU A CG  1 
ATOM   3211  C  CD  . GLU A 1 413 ? 21.389  85.562  14.705  1.00 38.95  ? 422  GLU A CD  1 
ATOM   3212  O  OE1 . GLU A 1 413 ? 22.075  86.496  14.285  1.00 42.84  ? 422  GLU A OE1 1 
ATOM   3213  O  OE2 . GLU A 1 413 ? 21.023  85.484  15.886  1.00 49.05  ? 422  GLU A OE2 1 
ATOM   3214  N  N   . THR A 1 414 ? 22.526  83.865  9.580   1.00 20.84  ? 423  THR A N   1 
ATOM   3215  C  CA  . THR A 1 414 ? 22.859  84.197  8.213   1.00 21.42  ? 423  THR A CA  1 
ATOM   3216  C  C   . THR A 1 414 ? 23.880  83.208  7.645   1.00 22.00  ? 423  THR A C   1 
ATOM   3217  O  O   . THR A 1 414 ? 24.827  82.842  8.369   1.00 25.38  ? 423  THR A O   1 
ATOM   3218  C  CB  . THR A 1 414 ? 23.521  85.608  8.165   1.00 23.94  ? 423  THR A CB  1 
ATOM   3219  O  OG1 . THR A 1 414 ? 22.628  86.539  8.812   1.00 25.08  ? 423  THR A OG1 1 
ATOM   3220  C  CG2 . THR A 1 414 ? 23.825  86.075  6.748   1.00 22.40  ? 423  THR A CG2 1 
ATOM   3221  N  N   . VAL A 1 415 ? 23.733  82.856  6.389   1.00 21.89  ? 424  VAL A N   1 
ATOM   3222  C  CA  . VAL A 1 415 ? 24.666  81.951  5.771   1.00 21.56  ? 424  VAL A CA  1 
ATOM   3223  C  C   . VAL A 1 415 ? 25.372  82.756  4.731   1.00 22.70  ? 424  VAL A C   1 
ATOM   3224  O  O   . VAL A 1 415 ? 24.736  83.399  3.884   1.00 22.82  ? 424  VAL A O   1 
ATOM   3225  C  CB  . VAL A 1 415 ? 23.929  80.744  5.116   1.00 22.73  ? 424  VAL A CB  1 
ATOM   3226  C  CG1 . VAL A 1 415 ? 24.915  79.911  4.274   1.00 22.71  ? 424  VAL A CG1 1 
ATOM   3227  C  CG2 . VAL A 1 415 ? 23.260  79.896  6.169   1.00 26.01  ? 424  VAL A CG2 1 
ATOM   3228  N  N   . TYR A 1 416 ? 26.714  82.786  4.770   1.00 19.51  ? 425  TYR A N   1 
ATOM   3229  C  CA  . TYR A 1 416 ? 27.423  83.489  3.749   1.00 17.41  ? 425  TYR A CA  1 
ATOM   3230  C  C   . TYR A 1 416 ? 28.000  82.520  2.781   1.00 21.73  ? 425  TYR A C   1 
ATOM   3231  O  O   . TYR A 1 416 ? 28.705  81.600  3.214   1.00 23.88  ? 425  TYR A O   1 
ATOM   3232  C  CB  . TYR A 1 416 ? 28.609  84.282  4.330   1.00 17.35  ? 425  TYR A CB  1 
ATOM   3233  C  CG  . TYR A 1 416 ? 28.170  85.426  5.213   1.00 18.22  ? 425  TYR A CG  1 
ATOM   3234  C  CD1 . TYR A 1 416 ? 28.197  86.727  4.755   1.00 22.16  ? 425  TYR A CD1 1 
ATOM   3235  C  CD2 . TYR A 1 416 ? 27.766  85.202  6.523   1.00 17.85  ? 425  TYR A CD2 1 
ATOM   3236  C  CE1 . TYR A 1 416 ? 27.827  87.806  5.600   1.00 22.72  ? 425  TYR A CE1 1 
ATOM   3237  C  CE2 . TYR A 1 416 ? 27.403  86.259  7.360   1.00 20.38  ? 425  TYR A CE2 1 
ATOM   3238  C  CZ  . TYR A 1 416 ? 27.439  87.551  6.888   1.00 22.77  ? 425  TYR A CZ  1 
ATOM   3239  O  OH  . TYR A 1 416 ? 27.069  88.554  7.784   1.00 22.81  ? 425  TYR A OH  1 
ATOM   3240  N  N   . GLN A 1 417 ? 27.752  82.687  1.515   1.00 19.85  ? 426  GLN A N   1 
ATOM   3241  C  CA  . GLN A 1 417 ? 28.328  81.795  0.510   1.00 21.41  ? 426  GLN A CA  1 
ATOM   3242  C  C   . GLN A 1 417 ? 29.575  82.458  -0.055  1.00 22.25  ? 426  GLN A C   1 
ATOM   3243  O  O   . GLN A 1 417 ? 29.532  83.516  -0.687  1.00 24.50  ? 426  GLN A O   1 
ATOM   3244  C  CB  . GLN A 1 417 ? 27.309  81.552  -0.617  1.00 19.99  ? 426  GLN A CB  1 
ATOM   3245  C  CG  . GLN A 1 417 ? 27.899  80.846  -1.810  1.00 23.25  ? 426  GLN A CG  1 
ATOM   3246  C  CD  . GLN A 1 417 ? 26.768  80.590  -2.841  1.00 28.36  ? 426  GLN A CD  1 
ATOM   3247  O  OE1 . GLN A 1 417 ? 25.624  80.960  -2.607  1.00 26.58  ? 426  GLN A OE1 1 
ATOM   3248  N  NE2 . GLN A 1 417 ? 27.085  79.931  -3.971  1.00 26.83  ? 426  GLN A NE2 1 
ATOM   3249  N  N   . ILE A 1 418 ? 30.719  81.834  0.171   1.00 21.07  ? 427  ILE A N   1 
ATOM   3250  C  CA  . ILE A 1 418 ? 31.998  82.374  -0.284  1.00 18.43  ? 427  ILE A CA  1 
ATOM   3251  C  C   . ILE A 1 418 ? 32.415  81.846  -1.625  1.00 24.98  ? 427  ILE A C   1 
ATOM   3252  O  O   . ILE A 1 418 ? 32.510  80.632  -1.817  1.00 23.93  ? 427  ILE A O   1 
ATOM   3253  C  CB  . ILE A 1 418 ? 33.104  81.995  0.753   1.00 19.63  ? 427  ILE A CB  1 
ATOM   3254  C  CG1 . ILE A 1 418 ? 32.664  82.375  2.190   1.00 18.44  ? 427  ILE A CG1 1 
ATOM   3255  C  CG2 . ILE A 1 418 ? 34.435  82.673  0.359   1.00 18.83  ? 427  ILE A CG2 1 
ATOM   3256  C  CD1 . ILE A 1 418 ? 32.365  83.904  2.356   1.00 21.58  ? 427  ILE A CD1 1 
ATOM   3257  N  N   . GLY A 1 419 ? 32.678  82.723  -2.559  1.00 21.76  ? 428  GLY A N   1 
ATOM   3258  C  CA  . GLY A 1 419 ? 33.134  82.261  -3.838  1.00 20.47  ? 428  GLY A CA  1 
ATOM   3259  C  C   . GLY A 1 419 ? 31.987  81.774  -4.705  1.00 23.66  ? 428  GLY A C   1 
ATOM   3260  O  O   . GLY A 1 419 ? 30.864  81.579  -4.298  1.00 24.84  ? 428  GLY A O   1 
ATOM   3261  N  N   . ASP A 1 420 ? 32.334  81.605  -5.965  1.00 28.66  ? 429  ASP A N   1 
ATOM   3262  C  CA  . ASP A 1 420 ? 31.417  81.139  -6.983  1.00 33.74  ? 429  ASP A CA  1 
ATOM   3263  C  C   . ASP A 1 420 ? 31.752  79.665  -7.370  1.00 35.49  ? 429  ASP A C   1 
ATOM   3264  O  O   . ASP A 1 420 ? 32.925  79.289  -7.397  1.00 35.13  ? 429  ASP A O   1 
ATOM   3265  C  CB  . ASP A 1 420 ? 31.602  82.011  -8.227  1.00 40.88  ? 429  ASP A CB  1 
ATOM   3266  C  CG  . ASP A 1 420 ? 30.538  81.686  -9.241  1.00 50.23  ? 429  ASP A CG  1 
ATOM   3267  O  OD1 . ASP A 1 420 ? 30.896  81.257  -10.346 1.00 53.46  ? 429  ASP A OD1 1 
ATOM   3268  O  OD2 . ASP A 1 420 ? 29.334  81.849  -8.911  1.00 53.51  ? 429  ASP A OD2 1 
ATOM   3269  N  N   . GLY A 1 421 ? 30.746  78.854  -7.659  1.00 36.33  ? 430  GLY A N   1 
ATOM   3270  C  CA  . GLY A 1 421 ? 31.020  77.484  -8.088  1.00 37.58  ? 430  GLY A CA  1 
ATOM   3271  C  C   . GLY A 1 421 ? 30.259  76.439  -7.310  1.00 37.10  ? 430  GLY A C   1 
ATOM   3272  O  O   . GLY A 1 421 ? 30.049  75.349  -7.831  1.00 34.50  ? 430  GLY A O   1 
ATOM   3273  N  N   . MET A 1 422 ? 29.873  76.737  -6.062  1.00 31.16  ? 431  MET A N   1 
ATOM   3274  C  CA  . MET A 1 422 ? 29.120  75.786  -5.293  1.00 30.69  ? 431  MET A CA  1 
ATOM   3275  C  C   . MET A 1 422 ? 27.701  75.707  -5.885  1.00 34.20  ? 431  MET A C   1 
ATOM   3276  O  O   . MET A 1 422 ? 27.122  76.748  -6.199  1.00 33.26  ? 431  MET A O   1 
ATOM   3277  C  CB  . MET A 1 422 ? 29.054  76.201  -3.810  1.00 29.36  ? 431  MET A CB  1 
ATOM   3278  C  CG  . MET A 1 422 ? 28.338  75.146  -2.950  1.00 24.95  ? 431  MET A CG  1 
ATOM   3279  S  SD  . MET A 1 422 ? 28.696  75.361  -1.191  1.00 27.26  ? 431  MET A SD  1 
ATOM   3280  C  CE  . MET A 1 422 ? 30.401  75.061  -1.186  1.00 28.53  ? 431  MET A CE  1 
ATOM   3281  N  N   . LYS A 1 423 ? 27.135  74.499  -6.043  1.00 31.58  ? 432  LYS A N   1 
ATOM   3282  C  CA  . LYS A 1 423 ? 25.795  74.385  -6.639  1.00 32.61  ? 432  LYS A CA  1 
ATOM   3283  C  C   . LYS A 1 423 ? 24.729  74.989  -5.778  1.00 33.81  ? 432  LYS A C   1 
ATOM   3284  O  O   . LYS A 1 423 ? 24.817  74.931  -4.559  1.00 29.87  ? 432  LYS A O   1 
ATOM   3285  C  CB  . LYS A 1 423 ? 25.412  72.900  -6.855  1.00 35.05  ? 432  LYS A CB  1 
ATOM   3286  C  CG  . LYS A 1 423 ? 26.421  72.136  -7.685  1.00 44.74  ? 432  LYS A CG  1 
ATOM   3287  C  CD  . LYS A 1 423 ? 26.803  72.880  -8.927  1.00 54.78  ? 432  LYS A CD  1 
ATOM   3288  C  CE  . LYS A 1 423 ? 26.258  72.191  -10.144 1.00 61.40  ? 432  LYS A CE  1 
ATOM   3289  N  NZ  . LYS A 1 423 ? 27.366  71.772  -11.038 1.00 66.58  ? 432  LYS A NZ  1 
ATOM   3290  N  N   . ASP A 1 424 ? 23.676  75.549  -6.408  1.00 32.62  ? 433  ASP A N   1 
ATOM   3291  C  CA  . ASP A 1 424 ? 22.576  76.160  -5.665  1.00 35.27  ? 433  ASP A CA  1 
ATOM   3292  C  C   . ASP A 1 424 ? 22.002  75.196  -4.746  1.00 34.01  ? 433  ASP A C   1 
ATOM   3293  O  O   . ASP A 1 424 ? 21.574  75.483  -3.636  1.00 34.93  ? 433  ASP A O   1 
ATOM   3294  C  CB  . ASP A 1 424 ? 21.446  76.611  -6.646  1.00 41.84  ? 433  ASP A CB  1 
ATOM   3295  C  CG  . ASP A 1 424 ? 21.792  77.825  -7.498  1.00 51.66  ? 433  ASP A CG  1 
ATOM   3296  O  OD1 . ASP A 1 424 ? 22.804  78.489  -7.204  1.00 52.31  ? 433  ASP A OD1 1 
ATOM   3297  O  OD2 . ASP A 1 424 ? 21.053  78.103  -8.461  1.00 56.00  ? 433  ASP A OD2 1 
ATOM   3298  N  N   . SER A 1 425 ? 21.945  73.978  -5.252  1.00 36.17  ? 434  SER A N   1 
ATOM   3299  C  CA  . SER A 1 425 ? 21.420  72.818  -4.567  1.00 35.43  ? 434  SER A CA  1 
ATOM   3300  C  C   . SER A 1 425 ? 22.105  72.615  -3.169  1.00 32.46  ? 434  SER A C   1 
ATOM   3301  O  O   . SER A 1 425 ? 21.460  72.385  -2.148  1.00 32.39  ? 434  SER A O   1 
ATOM   3302  C  CB  . SER A 1 425 ? 21.709  71.613  -5.473  1.00 39.86  ? 434  SER A CB  1 
ATOM   3303  O  OG  . SER A 1 425 ? 21.395  70.408  -4.827  1.00 50.65  ? 434  SER A OG  1 
ATOM   3304  N  N   . VAL A 1 426 ? 23.418  72.689  -3.169  1.00 29.85  ? 435  VAL A N   1 
ATOM   3305  C  CA  . VAL A 1 426 ? 24.238  72.494  -1.962  1.00 29.53  ? 435  VAL A CA  1 
ATOM   3306  C  C   . VAL A 1 426 ? 24.099  73.636  -0.941  1.00 24.65  ? 435  VAL A C   1 
ATOM   3307  O  O   . VAL A 1 426 ? 23.825  73.373  0.230   1.00 23.86  ? 435  VAL A O   1 
ATOM   3308  C  CB  . VAL A 1 426 ? 25.685  72.373  -2.503  1.00 29.00  ? 435  VAL A CB  1 
ATOM   3309  C  CG1 . VAL A 1 426 ? 26.682  72.221  -1.341  1.00 27.49  ? 435  VAL A CG1 1 
ATOM   3310  C  CG2 . VAL A 1 426 ? 25.761  71.173  -3.477  1.00 31.40  ? 435  VAL A CG2 1 
ATOM   3311  N  N   . ILE A 1 427 ? 24.271  74.886  -1.406  1.00 27.31  ? 436  ILE A N   1 
ATOM   3312  C  CA  . ILE A 1 427 ? 24.165  76.011  -0.456  1.00 28.82  ? 436  ILE A CA  1 
ATOM   3313  C  C   . ILE A 1 427 ? 22.703  76.078  0.108   1.00 25.41  ? 436  ILE A C   1 
ATOM   3314  O  O   . ILE A 1 427 ? 22.490  76.291  1.318   1.00 24.10  ? 436  ILE A O   1 
ATOM   3315  C  CB  . ILE A 1 427 ? 24.645  77.332  -1.164  1.00 28.53  ? 436  ILE A CB  1 
ATOM   3316  C  CG1 . ILE A 1 427 ? 24.730  78.481  -0.104  1.00 28.89  ? 436  ILE A CG1 1 
ATOM   3317  C  CG2 . ILE A 1 427 ? 23.719  77.725  -2.323  1.00 27.79  ? 436  ILE A CG2 1 
ATOM   3318  C  CD1 . ILE A 1 427 ? 25.938  78.205  0.905   1.00 31.42  ? 436  ILE A CD1 1 
ATOM   3319  N  N   . ASN A 1 428 ? 21.701  75.818  -0.745  1.00 27.21  ? 437  ASN A N   1 
ATOM   3320  C  CA  . ASN A 1 428 ? 20.320  75.868  -0.258  1.00 31.75  ? 437  ASN A CA  1 
ATOM   3321  C  C   . ASN A 1 428 ? 20.037  74.780  0.719   1.00 28.50  ? 437  ASN A C   1 
ATOM   3322  O  O   . ASN A 1 428 ? 19.277  74.975  1.656   1.00 28.12  ? 437  ASN A O   1 
ATOM   3323  C  CB  . ASN A 1 428 ? 19.296  75.779  -1.439  1.00 36.06  ? 437  ASN A CB  1 
ATOM   3324  C  CG  . ASN A 1 428 ? 17.890  75.664  -0.862  1.00 52.55  ? 437  ASN A CG  1 
ATOM   3325  O  OD1 . ASN A 1 428 ? 17.319  74.557  -0.815  1.00 56.09  ? 437  ASN A OD1 1 
ATOM   3326  N  ND2 . ASN A 1 428 ? 17.308  76.733  -0.289  1.00 54.34  ? 437  ASN A ND2 1 
ATOM   3327  N  N   . SER A 1 429 ? 20.680  73.586  0.542   1.00 27.01  ? 438  SER A N   1 
ATOM   3328  C  CA  . SER A 1 429 ? 20.486  72.497  1.505   1.00 22.66  ? 438  SER A CA  1 
ATOM   3329  C  C   . SER A 1 429 ? 21.020  72.923  2.854   1.00 22.19  ? 438  SER A C   1 
ATOM   3330  O  O   . SER A 1 429 ? 20.411  72.711  3.900   1.00 23.34  ? 438  SER A O   1 
ATOM   3331  C  CB  . SER A 1 429 ? 21.251  71.233  1.051   1.00 25.38  ? 438  SER A CB  1 
ATOM   3332  O  OG  . SER A 1 429 ? 21.208  70.259  2.068   1.00 28.95  ? 438  SER A OG  1 
ATOM   3333  N  N   . ILE A 1 430 ? 22.240  73.516  2.838   1.00 24.37  ? 439  ILE A N   1 
ATOM   3334  C  CA  . ILE A 1 430 ? 22.828  73.957  4.102   1.00 21.38  ? 439  ILE A CA  1 
ATOM   3335  C  C   . ILE A 1 430 ? 21.976  75.074  4.777   1.00 20.03  ? 439  ILE A C   1 
ATOM   3336  O  O   . ILE A 1 430 ? 21.749  75.049  5.995   1.00 19.38  ? 439  ILE A O   1 
ATOM   3337  C  CB  . ILE A 1 430 ? 24.257  74.479  3.798   1.00 19.65  ? 439  ILE A CB  1 
ATOM   3338  C  CG1 . ILE A 1 430 ? 25.176  73.243  3.524   1.00 21.28  ? 439  ILE A CG1 1 
ATOM   3339  C  CG2 . ILE A 1 430 ? 24.802  75.245  5.060   1.00 22.14  ? 439  ILE A CG2 1 
ATOM   3340  C  CD1 . ILE A 1 430 ? 26.482  73.646  2.800   1.00 20.55  ? 439  ILE A CD1 1 
ATOM   3341  N  N   . ALA A 1 431 ? 21.562  76.046  3.970   1.00 22.12  ? 440  ALA A N   1 
ATOM   3342  C  CA  . ALA A 1 431 ? 20.734  77.178  4.471   1.00 25.12  ? 440  ALA A CA  1 
ATOM   3343  C  C   . ALA A 1 431 ? 19.383  76.631  5.028   1.00 25.33  ? 440  ALA A C   1 
ATOM   3344  O  O   . ALA A 1 431 ? 18.912  77.124  6.059   1.00 27.09  ? 440  ALA A O   1 
ATOM   3345  C  CB  . ALA A 1 431 ? 20.541  78.171  3.339   1.00 23.89  ? 440  ALA A CB  1 
ATOM   3346  N  N   . SER A 1 432 ? 18.795  75.546  4.396   1.00 27.46  ? 441  SER A N   1 
ATOM   3347  C  CA  . SER A 1 432 ? 17.527  74.965  4.974   1.00 26.09  ? 441  SER A CA  1 
ATOM   3348  C  C   . SER A 1 432 ? 17.789  74.299  6.291   1.00 27.01  ? 441  SER A C   1 
ATOM   3349  O  O   . SER A 1 432 ? 17.083  74.542  7.266   1.00 26.35  ? 441  SER A O   1 
ATOM   3350  C  CB  . SER A 1 432 ? 16.912  73.956  3.994   1.00 30.63  ? 441  SER A CB  1 
ATOM   3351  O  OG  . SER A 1 432 ? 16.787  74.558  2.720   1.00 34.16  ? 441  SER A OG  1 
ATOM   3352  N  N   . SER A 1 433 ? 18.881  73.436  6.386   1.00 23.52  ? 442  SER A N   1 
ATOM   3353  C  CA  . SER A 1 433 ? 19.131  72.835  7.710   1.00 23.59  ? 442  SER A CA  1 
ATOM   3354  C  C   . SER A 1 433 ? 19.358  73.809  8.778   1.00 22.98  ? 442  SER A C   1 
ATOM   3355  O  O   . SER A 1 433 ? 19.050  73.559  9.979   1.00 22.35  ? 442  SER A O   1 
ATOM   3356  C  CB  . SER A 1 433 ? 20.385  71.926  7.677   1.00 26.94  ? 442  SER A CB  1 
ATOM   3357  O  OG  . SER A 1 433 ? 20.339  71.033  6.565   1.00 31.15  ? 442  SER A OG  1 
ATOM   3358  N  N   . LEU A 1 434 ? 19.990  74.952  8.410   1.00 23.70  ? 443  LEU A N   1 
ATOM   3359  C  CA  . LEU A 1 434 ? 20.353  75.891  9.479   1.00 25.07  ? 443  LEU A CA  1 
ATOM   3360  C  C   . LEU A 1 434 ? 19.201  76.857  9.867   1.00 24.76  ? 443  LEU A C   1 
ATOM   3361  O  O   . LEU A 1 434 ? 19.414  77.777  10.670  1.00 25.83  ? 443  LEU A O   1 
ATOM   3362  C  CB  . LEU A 1 434 ? 21.641  76.713  9.029   1.00 20.70  ? 443  LEU A CB  1 
ATOM   3363  C  CG  . LEU A 1 434 ? 22.935  75.838  9.141   1.00 21.96  ? 443  LEU A CG  1 
ATOM   3364  C  CD1 . LEU A 1 434 ? 24.106  76.603  8.415   1.00 22.05  ? 443  LEU A CD1 1 
ATOM   3365  C  CD2 . LEU A 1 434 ? 23.209  75.601  10.663  1.00 21.54  ? 443  LEU A CD2 1 
ATOM   3366  N  N   . SER A 1 435 ? 17.981  76.647  9.280   1.00 27.17  ? 444  SER A N   1 
ATOM   3367  C  CA  . SER A 1 435 ? 16.818  77.493  9.661   1.00 28.34  ? 444  SER A CA  1 
ATOM   3368  C  C   . SER A 1 435 ? 16.098  76.857  10.824  1.00 32.45  ? 444  SER A C   1 
ATOM   3369  O  O   . SER A 1 435 ? 15.254  77.499  11.429  1.00 30.18  ? 444  SER A O   1 
ATOM   3370  C  CB  . SER A 1 435 ? 15.879  77.687  8.472   1.00 30.99  ? 444  SER A CB  1 
ATOM   3371  O  OG  . SER A 1 435 ? 15.240  76.475  8.096   1.00 31.16  ? 444  SER A OG  1 
ATOM   3372  N  N   . LYS A 1 436 ? 16.417  75.587  11.207  1.00 30.11  ? 445  LYS A N   1 
ATOM   3373  C  CA  . LYS A 1 436 ? 15.738  75.000  12.402  1.00 32.63  ? 445  LYS A CA  1 
ATOM   3374  C  C   . LYS A 1 436 ? 16.567  73.959  13.194  1.00 35.26  ? 445  LYS A C   1 
ATOM   3375  O  O   . LYS A 1 436 ? 17.437  73.291  12.635  1.00 35.62  ? 445  LYS A O   1 
ATOM   3376  C  CB  . LYS A 1 436 ? 14.419  74.304  11.987  1.00 37.87  ? 445  LYS A CB  1 
ATOM   3377  C  CG  . LYS A 1 436 ? 14.578  73.490  10.750  1.00 43.07  ? 445  LYS A CG  1 
ATOM   3378  C  CD  . LYS A 1 436 ? 13.575  73.927  9.661   1.00 54.26  ? 445  LYS A CD  1 
ATOM   3379  C  CE  . LYS A 1 436 ? 13.586  72.934  8.516   0.00 0.00   ? 445  LYS A CE  1 
ATOM   3380  N  NZ  . LYS A 1 436 ? 12.235  72.739  7.910   0.00 0.00   ? 445  LYS A NZ  1 
ATOM   3381  N  N   . HIS A 1 437 ? 16.292  73.857  14.481  1.00 35.52  ? 446  HIS A N   1 
ATOM   3382  C  CA  . HIS A 1 437 ? 16.910  72.873  15.345  1.00 39.55  ? 446  HIS A CA  1 
ATOM   3383  C  C   . HIS A 1 437 ? 16.338  71.492  15.020  1.00 41.63  ? 446  HIS A C   1 
ATOM   3384  O  O   . HIS A 1 437 ? 15.165  71.392  14.672  1.00 38.44  ? 446  HIS A O   1 
ATOM   3385  C  CB  . HIS A 1 437 ? 16.612  73.218  16.788  1.00 40.45  ? 446  HIS A CB  1 
ATOM   3386  C  CG  . HIS A 1 437 ? 17.361  74.429  17.220  1.00 48.94  ? 446  HIS A CG  1 
ATOM   3387  N  ND1 . HIS A 1 437 ? 18.737  74.527  17.084  1.00 49.35  ? 446  HIS A ND1 1 
ATOM   3388  C  CD2 . HIS A 1 437 ? 16.939  75.603  17.748  1.00 49.10  ? 446  HIS A CD2 1 
ATOM   3389  C  CE1 . HIS A 1 437 ? 19.109  75.721  17.522  1.00 48.35  ? 446  HIS A CE1 1 
ATOM   3390  N  NE2 . HIS A 1 437 ? 18.048  76.392  17.929  1.00 51.64  ? 446  HIS A NE2 1 
ATOM   3391  N  N   . ASN A 1 438 ? 17.161  70.430  15.103  1.00 42.00  ? 447  ASN A N   1 
ATOM   3392  C  CA  . ASN A 1 438 ? 16.688  69.076  14.817  1.00 44.35  ? 447  ASN A CA  1 
ATOM   3393  C  C   . ASN A 1 438 ? 16.091  69.047  13.458  1.00 45.71  ? 447  ASN A C   1 
ATOM   3394  O  O   . ASN A 1 438 ? 15.079  68.374  13.227  1.00 44.26  ? 447  ASN A O   1 
ATOM   3395  C  CB  . ASN A 1 438 ? 15.645  68.640  15.850  1.00 48.20  ? 447  ASN A CB  1 
ATOM   3396  C  CG  . ASN A 1 438 ? 16.228  68.645  17.220  1.00 59.25  ? 447  ASN A CG  1 
ATOM   3397  O  OD1 . ASN A 1 438 ? 17.356  68.151  17.409  1.00 65.62  ? 447  ASN A OD1 1 
ATOM   3398  N  ND2 . ASN A 1 438 ? 15.596  69.247  18.216  1.00 59.82  ? 447  ASN A ND2 1 
ATOM   3399  N  N   . ALA A 1 439 ? 16.679  69.805  12.546  1.00 44.74  ? 448  ALA A N   1 
ATOM   3400  C  CA  . ALA A 1 439 ? 16.199  69.831  11.180  1.00 47.97  ? 448  ALA A CA  1 
ATOM   3401  C  C   . ALA A 1 439 ? 16.267  68.428  10.544  1.00 56.79  ? 448  ALA A C   1 
ATOM   3402  O  O   . ALA A 1 439 ? 17.185  67.659  10.827  1.00 58.71  ? 448  ALA A O   1 
ATOM   3403  C  CB  . ALA A 1 439 ? 17.043  70.783  10.361  1.00 47.94  ? 448  ALA A CB  1 
ATOM   3404  N  N   . PRO A 1 440 ? 15.301  68.071  9.682   1.00 68.67  ? 449  PRO A N   1 
ATOM   3405  C  CA  . PRO A 1 440 ? 15.386  66.741  9.074   1.00 78.15  ? 449  PRO A CA  1 
ATOM   3406  C  C   . PRO A 1 440 ? 16.588  66.689  8.136   1.00 87.29  ? 449  PRO A C   1 
ATOM   3407  O  O   . PRO A 1 440 ? 17.038  67.725  7.648   1.00 90.27  ? 449  PRO A O   1 
ATOM   3408  C  CB  . PRO A 1 440 ? 14.044  66.595  8.348   1.00 81.08  ? 449  PRO A CB  1 
ATOM   3409  C  CG  . PRO A 1 440 ? 13.539  68.004  8.187   1.00 78.00  ? 449  PRO A CG  1 
ATOM   3410  C  CD  . PRO A 1 440 ? 14.011  68.718  9.396   1.00 74.05  ? 449  PRO A CD  1 
ATOM   3411  N  N   . THR A 1 441 ? 17.092  65.492  7.882   1.00 96.94  ? 450  THR A N   1 
ATOM   3412  C  CA  . THR A 1 441 ? 18.227  65.279  6.995   1.00 110.83 ? 450  THR A CA  1 
ATOM   3413  C  C   . THR A 1 441 ? 17.660  64.884  5.625   1.00 119.31 ? 450  THR A C   1 
ATOM   3414  O  O   . THR A 1 441 ? 17.322  63.706  5.443   1.00 123.08 ? 450  THR A O   1 
ATOM   3415  C  CB  . THR A 1 441 ? 19.124  64.174  7.605   1.00 116.19 ? 450  THR A CB  1 
ATOM   3416  O  OG1 . THR A 1 441 ? 18.290  63.049  7.917   1.00 117.69 ? 450  THR A OG1 1 
ATOM   3417  C  CG2 . THR A 1 441 ? 19.829  64.632  8.896   1.00 117.07 ? 450  THR A CG2 1 
ATOM   3418  N  N   . GLU A 1 442 ? 17.545  65.827  4.662   1.00 125.63 ? 451  GLU A N   1 
ATOM   3419  C  CA  . GLU A 1 442 ? 16.958  65.446  3.374   1.00 133.93 ? 451  GLU A CA  1 
ATOM   3420  C  C   . GLU A 1 442 ? 17.416  66.272  2.130   1.00 138.75 ? 451  GLU A C   1 
ATOM   3421  O  O   . GLU A 1 442 ? 17.656  65.668  1.079   1.00 140.59 ? 451  GLU A O   1 
ATOM   3422  C  CB  . GLU A 1 442 ? 15.418  65.463  3.513   1.00 136.58 ? 451  GLU A CB  1 
ATOM   3423  C  CG  . GLU A 1 442 ? 14.851  64.058  3.671   0.00 0.00   ? 451  GLU A CG  1 
ATOM   3424  C  CD  . GLU A 1 442 ? 13.857  63.919  4.825   0.00 0.00   ? 451  GLU A CD  1 
ATOM   3425  O  OE1 . GLU A 1 442 ? 14.202  64.290  5.975   0.00 0.00   ? 451  GLU A OE1 1 
ATOM   3426  O  OE2 . GLU A 1 442 ? 12.736  63.408  4.576   0.00 0.00   ? 451  GLU A OE2 1 
ATOM   3427  N  N   . PRO A 1 443 ? 17.549  67.610  2.155   1.00 144.07 ? 452  PRO A N   1 
ATOM   3428  C  CA  . PRO A 1 443 ? 17.996  68.295  0.920   1.00 150.29 ? 452  PRO A CA  1 
ATOM   3429  C  C   . PRO A 1 443 ? 19.371  67.784  0.408   1.00 154.54 ? 452  PRO A C   1 
ATOM   3430  O  O   . PRO A 1 443 ? 19.651  67.816  -0.801  1.00 156.32 ? 452  PRO A O   1 
ATOM   3431  C  CB  . PRO A 1 443 ? 17.958  69.775  1.315   1.00 151.19 ? 452  PRO A CB  1 
ATOM   3432  C  CG  . PRO A 1 443 ? 16.880  69.815  2.360   0.00 0.00   ? 452  PRO A CG  1 
ATOM   3433  C  CD  . PRO A 1 443 ? 17.177  68.595  3.184   0.00 0.00   ? 452  PRO A CD  1 
ATOM   3434  N  N   . ASP A 1 444 ? 20.219  67.322  1.354   1.00 158.41 ? 453  ASP A N   1 
ATOM   3435  C  CA  . ASP A 1 444 ? 21.546  66.750  1.090   1.00 162.11 ? 453  ASP A CA  1 
ATOM   3436  C  C   . ASP A 1 444 ? 21.482  65.677  -0.021  1.00 164.28 ? 453  ASP A C   1 
ATOM   3437  O  O   . ASP A 1 444 ? 22.505  65.359  -0.623  1.00 164.03 ? 453  ASP A O   1 
ATOM   3438  C  CB  . ASP A 1 444 ? 22.106  66.121  2.377   1.00 162.94 ? 453  ASP A CB  1 
ATOM   3439  C  CG  . ASP A 1 444 ? 21.162  65.131  3.040   0.00 0.00   ? 453  ASP A CG  1 
ATOM   3440  O  OD1 . ASP A 1 444 ? 20.061  64.914  2.510   0.00 0.00   ? 453  ASP A OD1 1 
ATOM   3441  O  OD2 . ASP A 1 444 ? 21.525  64.577  4.089   0.00 0.00   ? 453  ASP A OD2 1 
ATOM   3442  N  N   . ASN A 1 445 ? 20.288  65.097  -0.262  1.00 164.91 ? 454  ASN A N   1 
ATOM   3443  C  CA  . ASN A 1 445 ? 20.099  64.137  -1.347  1.00 165.14 ? 454  ASN A CA  1 
ATOM   3444  C  C   . ASN A 1 445 ? 19.270  64.808  -2.425  1.00 165.46 ? 454  ASN A C   1 
ATOM   3445  O  O   . ASN A 1 445 ? 19.533  64.600  -3.608  1.00 165.50 ? 454  ASN A O   1 
ATOM   3446  C  CB  . ASN A 1 445 ? 19.414  62.835  -0.875  1.00 164.97 ? 454  ASN A CB  1 
ATOM   3447  C  CG  . ASN A 1 445 ? 18.035  63.027  -0.297  0.00 0.00   ? 454  ASN A CG  1 
ATOM   3448  O  OD1 . ASN A 1 445 ? 17.034  62.989  -1.023  0.00 0.00   ? 454  ASN A OD1 1 
ATOM   3449  N  ND2 . ASN A 1 445 ? 17.895  63.222  1.005   0.00 0.00   ? 454  ASN A ND2 1 
ATOM   3450  N  N   . SER A 1 446 ? 18.275  65.631  -2.021  1.00 166.17 ? 455  SER A N   1 
ATOM   3451  C  CA  . SER A 1 446 ? 17.418  66.351  -2.979  1.00 166.56 ? 455  SER A CA  1 
ATOM   3452  C  C   . SER A 1 446 ? 18.234  66.969  -4.112  1.00 166.21 ? 455  SER A C   1 
ATOM   3453  O  O   . SER A 1 446 ? 17.711  67.183  -5.204  1.00 166.10 ? 455  SER A O   1 
ATOM   3454  C  CB  . SER A 1 446 ? 16.659  67.471  -2.277  1.00 166.29 ? 455  SER A CB  1 
ATOM   3455  O  OG  . SER A 1 446 ? 16.033  67.011  -1.092  0.00 0.00   ? 455  SER A OG  1 
ATOM   3456  N  N   . GLY A 1 447 ? 19.517  67.262  -3.825  1.00 164.53 ? 456  GLY A N   1 
ATOM   3457  C  CA  . GLY A 1 447 ? 20.429  67.846  -4.801  1.00 160.95 ? 456  GLY A CA  1 
ATOM   3458  C  C   . GLY A 1 447 ? 20.241  67.439  -6.245  1.00 157.32 ? 456  GLY A C   1 
ATOM   3459  O  O   . GLY A 1 447 ? 20.257  68.289  -7.135  1.00 156.32 ? 456  GLY A O   1 
ATOM   3460  N  N   . SER A 1 448 ? 20.079  66.136  -6.492  1.00 154.81 ? 457  SER A N   1 
ATOM   3461  C  CA  . SER A 1 448 ? 19.863  65.671  -7.859  1.00 150.91 ? 457  SER A CA  1 
ATOM   3462  C  C   . SER A 1 448 ? 18.380  65.781  -8.211  1.00 148.08 ? 457  SER A C   1 
ATOM   3463  O  O   . SER A 1 448 ? 17.544  65.235  -7.491  1.00 147.14 ? 457  SER A O   1 
ATOM   3464  C  CB  . SER A 1 448 ? 20.304  64.217  -8.022  1.00 149.11 ? 457  SER A CB  1 
ATOM   3465  O  OG  . SER A 1 448 ? 21.619  63.993  -7.543  0.00 0.00   ? 457  SER A OG  1 
ATOM   3466  N  N   . ALA A 1 449 ? 18.049  66.488  -9.303  1.00 144.57 ? 458  ALA A N   1 
ATOM   3467  C  CA  . ALA A 1 449 ? 16.656  66.610  -9.736  1.00 139.13 ? 458  ALA A CA  1 
ATOM   3468  C  C   . ALA A 1 449 ? 16.131  65.212  -10.068 1.00 134.06 ? 458  ALA A C   1 
ATOM   3469  O  O   . ALA A 1 449 ? 14.941  64.928  -9.941  1.00 131.70 ? 458  ALA A O   1 
ATOM   3470  C  CB  . ALA A 1 449 ? 16.568  67.511  -10.962 1.00 137.05 ? 458  ALA A CB  1 
ATOM   3471  N  N   . ALA A 1 450 ? 17.058  64.342  -10.486 1.00 127.66 ? 459  ALA A N   1 
ATOM   3472  C  CA  . ALA A 1 450 ? 16.823  62.946  -10.838 1.00 117.54 ? 459  ALA A CA  1 
ATOM   3473  C  C   . ALA A 1 450 ? 18.136  62.192  -10.582 1.00 110.07 ? 459  ALA A C   1 
ATOM   3474  O  O   . ALA A 1 450 ? 19.143  62.837  -10.282 1.00 107.25 ? 459  ALA A O   1 
ATOM   3475  C  CB  . ALA A 1 450 ? 16.426  62.835  -12.302 1.00 113.66 ? 459  ALA A CB  1 
ATOM   3476  N  N   . GLY A 1 451 ? 18.152  60.863  -10.688 1.00 100.70 ? 460  GLY A N   1 
ATOM   3477  C  CA  . GLY A 1 451 ? 19.389  60.128  -10.456 1.00 86.12  ? 460  GLY A CA  1 
ATOM   3478  C  C   . GLY A 1 451 ? 19.127  58.913  -9.596  1.00 70.18  ? 460  GLY A C   1 
ATOM   3479  O  O   . GLY A 1 451 ? 17.991  58.616  -9.273  1.00 66.69  ? 460  GLY A O   1 
ATOM   3480  N  N   . LYS A 1 452 ? 20.164  58.206  -9.231  1.00 59.65  ? 461  LYS A N   1 
ATOM   3481  C  CA  . LYS A 1 452 ? 20.000  57.017  -8.406  1.00 47.69  ? 461  LYS A CA  1 
ATOM   3482  C  C   . LYS A 1 452 ? 19.923  57.397  -6.908  1.00 41.90  ? 461  LYS A C   1 
ATOM   3483  O  O   . LYS A 1 452 ? 20.548  58.390  -6.495  1.00 39.37  ? 461  LYS A O   1 
ATOM   3484  C  CB  . LYS A 1 452 ? 21.183  56.078  -8.676  1.00 42.40  ? 461  LYS A CB  1 
ATOM   3485  C  CG  . LYS A 1 452 ? 21.285  55.687  -10.164 1.00 48.42  ? 461  LYS A CG  1 
ATOM   3486  C  CD  . LYS A 1 452 ? 19.990  55.000  -10.675 1.00 50.65  ? 461  LYS A CD  1 
ATOM   3487  C  CE  . LYS A 1 452 ? 20.016  54.807  -12.194 1.00 54.41  ? 461  LYS A CE  1 
ATOM   3488  N  NZ  . LYS A 1 452 ? 19.130  53.676  -12.589 1.00 60.69  ? 461  LYS A NZ  1 
ATOM   3489  N  N   . THR A 1 453 ? 19.142  56.633  -6.115  1.00 35.90  ? 462  THR A N   1 
ATOM   3490  C  CA  . THR A 1 453 ? 18.996  56.847  -4.682  1.00 34.91  ? 462  THR A CA  1 
ATOM   3491  C  C   . THR A 1 453 ? 19.357  55.583  -3.901  1.00 33.94  ? 462  THR A C   1 
ATOM   3492  O  O   . THR A 1 453 ? 18.903  54.498  -4.243  1.00 31.28  ? 462  THR A O   1 
ATOM   3493  C  CB  . THR A 1 453 ? 17.584  57.226  -4.355  1.00 38.40  ? 462  THR A CB  1 
ATOM   3494  O  OG1 . THR A 1 453 ? 17.322  58.470  -5.015  1.00 40.78  ? 462  THR A OG1 1 
ATOM   3495  C  CG2 . THR A 1 453 ? 17.351  57.383  -2.837  1.00 37.73  ? 462  THR A CG2 1 
ATOM   3496  N  N   . VAL A 1 454 ? 20.174  55.720  -2.860  1.00 28.66  ? 463  VAL A N   1 
ATOM   3497  C  CA  . VAL A 1 454 ? 20.586  54.565  -2.049  1.00 25.07  ? 463  VAL A CA  1 
ATOM   3498  C  C   . VAL A 1 454 ? 20.271  54.921  -0.592  1.00 26.35  ? 463  VAL A C   1 
ATOM   3499  O  O   . VAL A 1 454 ? 20.409  56.076  -0.198  1.00 25.32  ? 463  VAL A O   1 
ATOM   3500  C  CB  . VAL A 1 454 ? 22.106  54.333  -2.208  1.00 25.89  ? 463  VAL A CB  1 
ATOM   3501  C  CG1 . VAL A 1 454 ? 22.603  53.292  -1.231  1.00 26.07  ? 463  VAL A CG1 1 
ATOM   3502  C  CG2 . VAL A 1 454 ? 22.428  53.871  -3.632  1.00 26.02  ? 463  VAL A CG2 1 
ATOM   3503  N  N   . VAL A 1 455 ? 19.855  53.941  0.185   1.00 22.70  ? 464  VAL A N   1 
ATOM   3504  C  CA  . VAL A 1 455 ? 19.657  54.153  1.607   1.00 19.77  ? 464  VAL A CA  1 
ATOM   3505  C  C   . VAL A 1 455 ? 20.804  53.403  2.238   1.00 21.52  ? 464  VAL A C   1 
ATOM   3506  O  O   . VAL A 1 455 ? 21.064  52.237  1.922   1.00 21.37  ? 464  VAL A O   1 
ATOM   3507  C  CB  . VAL A 1 455 ? 18.309  53.666  2.100   1.00 21.10  ? 464  VAL A CB  1 
ATOM   3508  C  CG1 . VAL A 1 455 ? 18.269  53.632  3.652   1.00 21.47  ? 464  VAL A CG1 1 
ATOM   3509  C  CG2 . VAL A 1 455 ? 17.181  54.568  1.577   1.00 17.89  ? 464  VAL A CG2 1 
ATOM   3510  N  N   . ILE A 1 456 ? 21.565  54.098  3.141   1.00 21.39  ? 465  ILE A N   1 
ATOM   3511  C  CA  . ILE A 1 456 ? 22.679  53.487  3.853   1.00 18.44  ? 465  ILE A CA  1 
ATOM   3512  C  C   . ILE A 1 456 ? 22.224  53.351  5.332   1.00 19.45  ? 465  ILE A C   1 
ATOM   3513  O  O   . ILE A 1 456 ? 21.760  54.323  5.912   1.00 19.44  ? 465  ILE A O   1 
ATOM   3514  C  CB  . ILE A 1 456 ? 23.925  54.412  3.766   1.00 19.84  ? 465  ILE A CB  1 
ATOM   3515  C  CG1 . ILE A 1 456 ? 24.432  54.519  2.272   1.00 17.93  ? 465  ILE A CG1 1 
ATOM   3516  C  CG2 . ILE A 1 456 ? 25.028  53.877  4.646   1.00 21.03  ? 465  ILE A CG2 1 
ATOM   3517  C  CD1 . ILE A 1 456 ? 24.886  53.093  1.745   1.00 20.19  ? 465  ILE A CD1 1 
ATOM   3518  N  N   . ASP A 1 457 ? 22.384  52.152  5.907   1.00 18.79  ? 466  ASP A N   1 
ATOM   3519  C  CA  . ASP A 1 457 ? 21.936  51.920  7.286   1.00 17.90  ? 466  ASP A CA  1 
ATOM   3520  C  C   . ASP A 1 457 ? 23.057  51.401  8.187   1.00 19.88  ? 466  ASP A C   1 
ATOM   3521  O  O   . ASP A 1 457 ? 23.424  50.222  8.148   1.00 19.69  ? 466  ASP A O   1 
ATOM   3522  C  CB  . ASP A 1 457 ? 20.762  50.880  7.211   1.00 19.11  ? 466  ASP A CB  1 
ATOM   3523  C  CG  . ASP A 1 457 ? 20.302  50.395  8.582   1.00 23.59  ? 466  ASP A CG  1 
ATOM   3524  O  OD1 . ASP A 1 457 ? 20.086  51.246  9.461   1.00 23.58  ? 466  ASP A OD1 1 
ATOM   3525  O  OD2 . ASP A 1 457 ? 20.172  49.136  8.765   1.00 22.97  ? 466  ASP A OD2 1 
ATOM   3526  N  N   . PRO A 1 458 ? 23.657  52.254  9.005   1.00 19.41  ? 467  PRO A N   1 
ATOM   3527  C  CA  . PRO A 1 458 ? 24.734  51.866  9.960   1.00 20.10  ? 467  PRO A CA  1 
ATOM   3528  C  C   . PRO A 1 458 ? 24.036  51.041  11.084  1.00 19.06  ? 467  PRO A C   1 
ATOM   3529  O  O   . PRO A 1 458 ? 23.195  51.616  11.779  1.00 20.83  ? 467  PRO A O   1 
ATOM   3530  C  CB  . PRO A 1 458 ? 25.288  53.207  10.450  1.00 19.89  ? 467  PRO A CB  1 
ATOM   3531  C  CG  . PRO A 1 458 ? 24.553  54.290  9.684   1.00 22.49  ? 467  PRO A CG  1 
ATOM   3532  C  CD  . PRO A 1 458 ? 23.324  53.690  9.091   1.00 21.26  ? 467  PRO A CD  1 
ATOM   3533  N  N   . GLY A 1 459 ? 24.371  49.767  11.267  1.00 19.28  ? 468  GLY A N   1 
ATOM   3534  C  CA  . GLY A 1 459 ? 23.627  48.936  12.214  1.00 19.62  ? 468  GLY A CA  1 
ATOM   3535  C  C   . GLY A 1 459 ? 23.771  49.402  13.649  1.00 20.81  ? 468  GLY A C   1 
ATOM   3536  O  O   . GLY A 1 459 ? 24.781  50.017  14.001  1.00 19.57  ? 468  GLY A O   1 
ATOM   3537  N  N   . HIS A 1 460 ? 22.730  49.096  14.446  1.00 20.27  ? 469  HIS A N   1 
ATOM   3538  C  CA  . HIS A 1 460 ? 22.704  49.375  15.889  1.00 23.70  ? 469  HIS A CA  1 
ATOM   3539  C  C   . HIS A 1 460 ? 22.791  50.853  16.147  1.00 27.11  ? 469  HIS A C   1 
ATOM   3540  O  O   . HIS A 1 460 ? 22.498  51.640  15.245  1.00 23.40  ? 469  HIS A O   1 
ATOM   3541  C  CB  . HIS A 1 460 ? 23.885  48.627  16.526  1.00 28.41  ? 469  HIS A CB  1 
ATOM   3542  C  CG  . HIS A 1 460 ? 23.868  47.167  16.189  1.00 31.96  ? 469  HIS A CG  1 
ATOM   3543  N  ND1 . HIS A 1 460 ? 22.919  46.294  16.665  1.00 26.54  ? 469  HIS A ND1 1 
ATOM   3544  C  CD2 . HIS A 1 460 ? 24.672  46.446  15.337  1.00 31.36  ? 469  HIS A CD2 1 
ATOM   3545  C  CE1 . HIS A 1 460 ? 23.160  45.099  16.102  1.00 30.30  ? 469  HIS A CE1 1 
ATOM   3546  N  NE2 . HIS A 1 460 ? 24.210  45.102  15.276  1.00 34.86  ? 469  HIS A NE2 1 
ATOM   3547  N  N   . GLY A 1 461 ? 23.135  51.242  17.388  1.00 21.64  ? 470  GLY A N   1 
ATOM   3548  C  CA  . GLY A 1 461 ? 23.212  52.661  17.752  1.00 23.17  ? 470  GLY A CA  1 
ATOM   3549  C  C   . GLY A 1 461 ? 22.477  52.927  19.078  1.00 25.24  ? 470  GLY A C   1 
ATOM   3550  O  O   . GLY A 1 461 ? 21.531  52.209  19.426  1.00 25.06  ? 470  GLY A O   1 
ATOM   3551  N  N   . GLY A 1 462 ? 22.900  53.955  19.779  1.00 24.61  ? 471  GLY A N   1 
ATOM   3552  C  CA  . GLY A 1 462 ? 22.235  54.367  21.031  1.00 29.94  ? 471  GLY A CA  1 
ATOM   3553  C  C   . GLY A 1 462 ? 22.249  53.273  22.090  1.00 25.94  ? 471  GLY A C   1 
ATOM   3554  O  O   . GLY A 1 462 ? 23.318  52.764  22.451  1.00 29.91  ? 471  GLY A O   1 
ATOM   3555  N  N   . SER A 1 463 ? 21.070  52.881  22.561  1.00 30.23  ? 472  SER A N   1 
ATOM   3556  C  CA  . SER A 1 463 ? 20.940  51.824  23.587  1.00 33.74  ? 472  SER A CA  1 
ATOM   3557  C  C   . SER A 1 463 ? 21.503  50.460  23.130  1.00 36.61  ? 472  SER A C   1 
ATOM   3558  O  O   . SER A 1 463 ? 21.815  49.601  23.983  1.00 36.75  ? 472  SER A O   1 
ATOM   3559  C  CB  . SER A 1 463 ? 19.469  51.610  23.929  1.00 35.88  ? 472  SER A CB  1 
ATOM   3560  O  OG  . SER A 1 463 ? 18.850  52.837  24.275  1.00 43.65  ? 472  SER A OG  1 
ATOM   3561  N  N   . ASP A 1 464 ? 21.603  50.226  21.779  1.00 35.13  ? 473  ASP A N   1 
ATOM   3562  C  CA  . ASP A 1 464 ? 22.134  48.945  21.284  1.00 33.25  ? 473  ASP A CA  1 
ATOM   3563  C  C   . ASP A 1 464 ? 23.540  49.125  20.748  1.00 32.11  ? 473  ASP A C   1 
ATOM   3564  O  O   . ASP A 1 464 ? 23.719  49.710  19.671  1.00 31.55  ? 473  ASP A O   1 
ATOM   3565  C  CB  . ASP A 1 464 ? 21.188  48.394  20.162  1.00 32.83  ? 473  ASP A CB  1 
ATOM   3566  C  CG  . ASP A 1 464 ? 21.605  47.001  19.658  1.00 32.05  ? 473  ASP A CG  1 
ATOM   3567  O  OD1 . ASP A 1 464 ? 22.564  46.410  20.221  1.00 33.03  ? 473  ASP A OD1 1 
ATOM   3568  O  OD2 . ASP A 1 464 ? 20.990  46.510  18.714  1.00 33.45  ? 473  ASP A OD2 1 
ATOM   3569  N  N   . SER A 1 465 ? 24.558  48.641  21.440  1.00 32.42  ? 474  SER A N   1 
ATOM   3570  C  CA  . SER A 1 465 ? 25.931  48.859  20.946  1.00 35.06  ? 474  SER A CA  1 
ATOM   3571  C  C   . SER A 1 465 ? 26.343  47.830  19.870  1.00 33.44  ? 474  SER A C   1 
ATOM   3572  O  O   . SER A 1 465 ? 27.363  48.024  19.232  1.00 31.27  ? 474  SER A O   1 
ATOM   3573  C  CB  . SER A 1 465 ? 26.918  48.762  22.104  1.00 40.71  ? 474  SER A CB  1 
ATOM   3574  O  OG  . SER A 1 465 ? 26.903  47.411  22.557  1.00 43.24  ? 474  SER A OG  1 
ATOM   3575  N  N   . GLY A 1 466 ? 25.543  46.739  19.700  1.00 32.06  ? 475  GLY A N   1 
ATOM   3576  C  CA  . GLY A 1 466 ? 25.887  45.677  18.761  1.00 32.26  ? 475  GLY A CA  1 
ATOM   3577  C  C   . GLY A 1 466 ? 27.072  44.906  19.322  1.00 35.83  ? 475  GLY A C   1 
ATOM   3578  O  O   . GLY A 1 466 ? 27.359  45.042  20.515  1.00 33.81  ? 475  GLY A O   1 
ATOM   3579  N  N   . ALA A 1 467 ? 27.786  44.112  18.503  1.00 33.30  ? 476  ALA A N   1 
ATOM   3580  C  CA  . ALA A 1 467 ? 28.942  43.370  19.031  1.00 33.77  ? 476  ALA A CA  1 
ATOM   3581  C  C   . ALA A 1 467 ? 30.030  44.316  19.548  1.00 35.59  ? 476  ALA A C   1 
ATOM   3582  O  O   . ALA A 1 467 ? 30.157  45.444  19.071  1.00 34.36  ? 476  ALA A O   1 
ATOM   3583  C  CB  . ALA A 1 467 ? 29.539  42.497  17.934  1.00 36.88  ? 476  ALA A CB  1 
ATOM   3584  N  N   . THR A 1 468 ? 30.811  43.864  20.550  1.00 37.81  ? 477  THR A N   1 
ATOM   3585  C  CA  . THR A 1 468 ? 31.922  44.669  21.077  1.00 36.45  ? 477  THR A CA  1 
ATOM   3586  C  C   . THR A 1 468 ? 33.161  43.783  21.207  1.00 36.89  ? 477  THR A C   1 
ATOM   3587  O  O   . THR A 1 468 ? 33.060  42.556  21.107  1.00 36.51  ? 477  THR A O   1 
ATOM   3588  C  CB  . THR A 1 468 ? 31.554  45.294  22.434  1.00 40.91  ? 477  THR A CB  1 
ATOM   3589  O  OG1 . THR A 1 468 ? 31.398  44.219  23.372  1.00 39.25  ? 477  THR A OG1 1 
ATOM   3590  C  CG2 . THR A 1 468 ? 30.258  46.132  22.366  1.00 38.73  ? 477  THR A CG2 1 
ATOM   3591  N  N   . SER A 1 469 ? 34.331  44.386  21.411  1.00 34.75  ? 478  SER A N   1 
ATOM   3592  C  CA  . SER A 1 469 ? 35.552  43.610  21.531  1.00 34.88  ? 478  SER A CA  1 
ATOM   3593  C  C   . SER A 1 469 ? 36.603  44.511  22.180  1.00 35.92  ? 478  SER A C   1 
ATOM   3594  O  O   . SER A 1 469 ? 36.412  45.726  22.276  1.00 34.34  ? 478  SER A O   1 
ATOM   3595  C  CB  . SER A 1 469 ? 36.041  43.175  20.149  1.00 36.92  ? 478  SER A CB  1 
ATOM   3596  O  OG  . SER A 1 469 ? 36.971  44.128  19.643  1.00 36.79  ? 478  SER A OG  1 
ATOM   3597  N  N   . GLY A 1 470 ? 37.709  43.902  22.621  1.00 40.32  ? 479  GLY A N   1 
ATOM   3598  C  CA  . GLY A 1 470 ? 38.772  44.668  23.241  1.00 40.78  ? 479  GLY A CA  1 
ATOM   3599  C  C   . GLY A 1 470 ? 39.840  45.059  22.240  1.00 46.67  ? 479  GLY A C   1 
ATOM   3600  O  O   . GLY A 1 470 ? 40.825  45.680  22.635  1.00 48.92  ? 479  GLY A O   1 
ATOM   3601  N  N   . LEU A 1 471 ? 39.675  44.704  20.930  1.00 48.21  ? 480  LEU A N   1 
ATOM   3602  C  CA  . LEU A 1 471 ? 40.696  45.092  19.922  1.00 45.99  ? 480  LEU A CA  1 
ATOM   3603  C  C   . LEU A 1 471 ? 40.657  46.625  19.576  1.00 42.40  ? 480  LEU A C   1 
ATOM   3604  O  O   . LEU A 1 471 ? 39.625  47.313  19.776  1.00 38.84  ? 480  LEU A O   1 
ATOM   3605  C  CB  . LEU A 1 471 ? 40.516  44.270  18.635  1.00 44.03  ? 480  LEU A CB  1 
ATOM   3606  C  CG  . LEU A 1 471 ? 40.317  42.765  18.844  1.00 47.84  ? 480  LEU A CG  1 
ATOM   3607  C  CD1 . LEU A 1 471 ? 39.963  42.080  17.508  1.00 50.60  ? 480  LEU A CD1 1 
ATOM   3608  C  CD2 . LEU A 1 471 ? 41.608  42.135  19.409  1.00 47.65  ? 480  LEU A CD2 1 
ATOM   3609  N  N   . ASN A 1 472 ? 41.779  47.150  19.053  1.00 39.37  ? 481  ASN A N   1 
ATOM   3610  C  CA  . ASN A 1 472 ? 41.880  48.559  18.640  1.00 41.03  ? 481  ASN A CA  1 
ATOM   3611  C  C   . ASN A 1 472 ? 41.491  49.501  19.748  1.00 43.45  ? 481  ASN A C   1 
ATOM   3612  O  O   . ASN A 1 472 ? 40.836  50.516  19.507  1.00 44.03  ? 481  ASN A O   1 
ATOM   3613  C  CB  . ASN A 1 472 ? 40.995  48.851  17.372  1.00 42.63  ? 481  ASN A CB  1 
ATOM   3614  C  CG  . ASN A 1 472 ? 41.430  48.060  16.135  1.00 44.59  ? 481  ASN A CG  1 
ATOM   3615  O  OD1 . ASN A 1 472 ? 40.801  48.206  15.047  1.00 42.82  ? 481  ASN A OD1 1 
ATOM   3616  N  ND2 . ASN A 1 472 ? 42.452  47.148  16.211  1.00 37.84  ? 481  ASN A ND2 1 
ATOM   3617  N  N   . GLY A 1 473 ? 41.924  49.180  21.005  1.00 44.27  ? 482  GLY A N   1 
ATOM   3618  C  CA  . GLY A 1 473 ? 41.623  50.041  22.144  1.00 43.97  ? 482  GLY A CA  1 
ATOM   3619  C  C   . GLY A 1 473 ? 40.172  49.990  22.588  1.00 48.65  ? 482  GLY A C   1 
ATOM   3620  O  O   . GLY A 1 473 ? 39.704  50.896  23.268  1.00 49.38  ? 482  GLY A O   1 
ATOM   3621  N  N   . GLY A 1 474 ? 39.445  48.907  22.240  1.00 48.37  ? 483  GLY A N   1 
ATOM   3622  C  CA  . GLY A 1 474 ? 38.031  48.827  22.599  1.00 46.62  ? 483  GLY A CA  1 
ATOM   3623  C  C   . GLY A 1 474 ? 37.248  49.179  21.345  1.00 45.97  ? 483  GLY A C   1 
ATOM   3624  O  O   . GLY A 1 474 ? 37.475  50.218  20.702  1.00 41.43  ? 483  GLY A O   1 
ATOM   3625  N  N   . ALA A 1 475 ? 36.333  48.320  20.989  1.00 40.49  ? 484  ALA A N   1 
ATOM   3626  C  CA  . ALA A 1 475 ? 35.582  48.532  19.783  1.00 35.93  ? 484  ALA A CA  1 
ATOM   3627  C  C   . ALA A 1 475 ? 34.150  48.179  20.001  1.00 37.36  ? 484  ALA A C   1 
ATOM   3628  O  O   . ALA A 1 475 ? 33.814  47.166  20.666  1.00 34.04  ? 484  ALA A O   1 
ATOM   3629  C  CB  . ALA A 1 475 ? 36.172  47.638  18.657  1.00 35.83  ? 484  ALA A CB  1 
ATOM   3630  N  N   . GLN A 1 476 ? 33.277  49.028  19.435  1.00 33.90  ? 485  GLN A N   1 
ATOM   3631  C  CA  . GLN A 1 476 ? 31.845  48.821  19.493  1.00 32.05  ? 485  GLN A CA  1 
ATOM   3632  C  C   . GLN A 1 476 ? 31.335  48.828  18.079  1.00 30.50  ? 485  GLN A C   1 
ATOM   3633  O  O   . GLN A 1 476 ? 31.607  49.788  17.344  1.00 31.82  ? 485  GLN A O   1 
ATOM   3634  C  CB  . GLN A 1 476 ? 31.174  49.957  20.266  1.00 34.51  ? 485  GLN A CB  1 
ATOM   3635  C  CG  . GLN A 1 476 ? 31.387  49.828  21.786  1.00 42.41  ? 485  GLN A CG  1 
ATOM   3636  C  CD  . GLN A 1 476 ? 30.635  50.928  22.474  1.00 53.95  ? 485  GLN A CD  1 
ATOM   3637  O  OE1 . GLN A 1 476 ? 31.060  52.090  22.462  1.00 56.60  ? 485  GLN A OE1 1 
ATOM   3638  N  NE2 . GLN A 1 476 ? 29.486  50.618  23.059  1.00 59.11  ? 485  GLN A NE2 1 
ATOM   3639  N  N   . GLU A 1 477 ? 30.574  47.800  17.687  1.00 30.61  ? 486  GLU A N   1 
ATOM   3640  C  CA  . GLU A 1 477 ? 30.026  47.738  16.333  1.00 26.29  ? 486  GLU A CA  1 
ATOM   3641  C  C   . GLU A 1 477 ? 29.271  49.056  15.939  1.00 29.39  ? 486  GLU A C   1 
ATOM   3642  O  O   . GLU A 1 477 ? 29.433  49.539  14.798  1.00 28.80  ? 486  GLU A O   1 
ATOM   3643  C  CB  . GLU A 1 477 ? 29.071  46.540  16.236  1.00 26.15  ? 486  GLU A CB  1 
ATOM   3644  C  CG  . GLU A 1 477 ? 28.443  46.371  14.841  1.00 28.42  ? 486  GLU A CG  1 
ATOM   3645  C  CD  . GLU A 1 477 ? 27.505  45.161  14.765  1.00 34.88  ? 486  GLU A CD  1 
ATOM   3646  O  OE1 . GLU A 1 477 ? 26.945  44.919  13.690  1.00 29.71  ? 486  GLU A OE1 1 
ATOM   3647  O  OE2 . GLU A 1 477 ? 27.311  44.466  15.784  1.00 31.20  ? 486  GLU A OE2 1 
ATOM   3648  N  N   . LYS A 1 478 ? 28.435  49.615  16.840  1.00 25.66  ? 487  LYS A N   1 
ATOM   3649  C  CA  . LYS A 1 478 ? 27.650  50.818  16.500  1.00 24.75  ? 487  LYS A CA  1 
ATOM   3650  C  C   . LYS A 1 478 ? 28.528  52.015  16.093  1.00 25.88  ? 487  LYS A C   1 
ATOM   3651  O  O   . LYS A 1 478 ? 28.093  52.869  15.299  1.00 24.54  ? 487  LYS A O   1 
ATOM   3652  C  CB  . LYS A 1 478 ? 26.707  51.214  17.667  1.00 29.36  ? 487  LYS A CB  1 
ATOM   3653  C  CG  . LYS A 1 478 ? 27.427  51.864  18.877  1.00 30.16  ? 487  LYS A CG  1 
ATOM   3654  C  CD  . LYS A 1 478 ? 26.358  52.567  19.789  1.00 28.83  ? 487  LYS A CD  1 
ATOM   3655  C  CE  . LYS A 1 478 ? 26.871  52.895  21.179  1.00 28.63  ? 487  LYS A CE  1 
ATOM   3656  N  NZ  . LYS A 1 478 ? 25.917  53.862  21.848  1.00 29.82  ? 487  LYS A NZ  1 
ATOM   3657  N  N   . LYS A 1 479 ? 29.747  52.096  16.582  1.00 25.34  ? 488  LYS A N   1 
ATOM   3658  C  CA  . LYS A 1 479 ? 30.542  53.247  16.151  1.00 23.68  ? 488  LYS A CA  1 
ATOM   3659  C  C   . LYS A 1 479 ? 31.322  52.932  14.837  1.00 25.38  ? 488  LYS A C   1 
ATOM   3660  O  O   . LYS A 1 479 ? 31.564  53.826  14.023  1.00 26.57  ? 488  LYS A O   1 
ATOM   3661  C  CB  . LYS A 1 479 ? 31.583  53.577  17.178  1.00 31.96  ? 488  LYS A CB  1 
ATOM   3662  C  CG  . LYS A 1 479 ? 30.946  53.896  18.523  1.00 42.20  ? 488  LYS A CG  1 
ATOM   3663  C  CD  . LYS A 1 479 ? 31.996  54.023  19.567  1.00 49.34  ? 488  LYS A CD  1 
ATOM   3664  C  CE  . LYS A 1 479 ? 31.377  54.537  20.847  1.00 57.84  ? 488  LYS A CE  1 
ATOM   3665  N  NZ  . LYS A 1 479 ? 32.402  54.622  21.906  1.00 60.40  ? 488  LYS A NZ  1 
ATOM   3666  N  N   . TYR A 1 480 ? 31.732  51.668  14.671  1.00 25.00  ? 489  TYR A N   1 
ATOM   3667  C  CA  . TYR A 1 480 ? 32.465  51.344  13.461  1.00 26.69  ? 489  TYR A CA  1 
ATOM   3668  C  C   . TYR A 1 480 ? 31.463  51.349  12.329  1.00 26.03  ? 489  TYR A C   1 
ATOM   3669  O  O   . TYR A 1 480 ? 31.845  51.714  11.199  1.00 23.00  ? 489  TYR A O   1 
ATOM   3670  C  CB  . TYR A 1 480 ? 33.078  49.944  13.584  1.00 27.76  ? 489  TYR A CB  1 
ATOM   3671  C  CG  . TYR A 1 480 ? 34.480  50.007  14.116  1.00 32.55  ? 489  TYR A CG  1 
ATOM   3672  C  CD1 . TYR A 1 480 ? 35.573  49.839  13.268  1.00 33.44  ? 489  TYR A CD1 1 
ATOM   3673  C  CD2 . TYR A 1 480 ? 34.723  50.210  15.472  1.00 38.79  ? 489  TYR A CD2 1 
ATOM   3674  C  CE1 . TYR A 1 480 ? 36.867  49.868  13.751  1.00 34.01  ? 489  TYR A CE1 1 
ATOM   3675  C  CE2 . TYR A 1 480 ? 36.025  50.240  15.969  1.00 43.35  ? 489  TYR A CE2 1 
ATOM   3676  C  CZ  . TYR A 1 480 ? 37.094  50.065  15.104  1.00 42.54  ? 489  TYR A CZ  1 
ATOM   3677  O  OH  . TYR A 1 480 ? 38.393  50.065  15.562  1.00 33.79  ? 489  TYR A OH  1 
ATOM   3678  N  N   . THR A 1 481 ? 30.186  50.959  12.605  1.00 20.55  ? 490  THR A N   1 
ATOM   3679  C  CA  . THR A 1 481 ? 29.278  50.971  11.443  1.00 23.76  ? 490  THR A CA  1 
ATOM   3680  C  C   . THR A 1 481 ? 29.008  52.404  11.085  1.00 22.85  ? 490  THR A C   1 
ATOM   3681  O  O   . THR A 1 481 ? 28.891  52.715  9.883   1.00 20.59  ? 490  THR A O   1 
ATOM   3682  C  CB  . THR A 1 481 ? 27.921  50.244  11.711  1.00 25.32  ? 490  THR A CB  1 
ATOM   3683  O  OG1 . THR A 1 481 ? 27.233  50.896  12.776  1.00 23.71  ? 490  THR A OG1 1 
ATOM   3684  C  CG2 . THR A 1 481 ? 28.113  48.791  12.087  1.00 22.10  ? 490  THR A CG2 1 
ATOM   3685  N  N   . LEU A 1 482 ? 28.843  53.290  12.088  1.00 19.43  ? 491  LEU A N   1 
ATOM   3686  C  CA  . LEU A 1 482 ? 28.590  54.696  11.719  1.00 21.37  ? 491  LEU A CA  1 
ATOM   3687  C  C   . LEU A 1 482 ? 29.788  55.334  10.923  1.00 20.79  ? 491  LEU A C   1 
ATOM   3688  O  O   . LEU A 1 482 ? 29.573  56.002  9.915   1.00 20.78  ? 491  LEU A O   1 
ATOM   3689  C  CB  . LEU A 1 482 ? 28.290  55.577  12.974  1.00 20.47  ? 491  LEU A CB  1 
ATOM   3690  C  CG  . LEU A 1 482 ? 28.071  57.053  12.604  1.00 20.49  ? 491  LEU A CG  1 
ATOM   3691  C  CD1 . LEU A 1 482 ? 26.869  57.203  11.696  1.00 21.47  ? 491  LEU A CD1 1 
ATOM   3692  C  CD2 . LEU A 1 482 ? 27.895  57.832  13.909  1.00 25.97  ? 491  LEU A CD2 1 
ATOM   3693  N  N   . ASN A 1 483 ? 31.028  55.140  11.395  1.00 21.19  ? 492  ASN A N   1 
ATOM   3694  C  CA  . ASN A 1 483 ? 32.196  55.719  10.681  1.00 23.36  ? 492  ASN A CA  1 
ATOM   3695  C  C   . ASN A 1 483 ? 32.323  55.087  9.254   1.00 24.40  ? 492  ASN A C   1 
ATOM   3696  O  O   . ASN A 1 483 ? 32.638  55.794  8.322   1.00 20.87  ? 492  ASN A O   1 
ATOM   3697  C  CB  . ASN A 1 483 ? 33.445  55.462  11.462  1.00 25.63  ? 492  ASN A CB  1 
ATOM   3698  C  CG  . ASN A 1 483 ? 33.412  56.254  12.755  1.00 31.46  ? 492  ASN A CG  1 
ATOM   3699  O  OD1 . ASN A 1 483 ? 32.834  57.362  12.761  1.00 30.11  ? 492  ASN A OD1 1 
ATOM   3700  N  ND2 . ASN A 1 483 ? 33.886  55.697  13.892  1.00 33.69  ? 492  ASN A ND2 1 
ATOM   3701  N  N   . THR A 1 484 ? 32.045  53.775  9.128   1.00 22.65  ? 493  THR A N   1 
ATOM   3702  C  CA  . THR A 1 484 ? 32.123  53.142  7.808   1.00 22.10  ? 493  THR A CA  1 
ATOM   3703  C  C   . THR A 1 484 ? 31.037  53.744  6.896   1.00 19.72  ? 493  THR A C   1 
ATOM   3704  O  O   . THR A 1 484 ? 31.309  54.142  5.758   1.00 19.91  ? 493  THR A O   1 
ATOM   3705  C  CB  . THR A 1 484 ? 31.864  51.620  7.957   1.00 22.31  ? 493  THR A CB  1 
ATOM   3706  O  OG1 . THR A 1 484 ? 32.860  51.086  8.792   1.00 21.12  ? 493  THR A OG1 1 
ATOM   3707  C  CG2 . THR A 1 484 ? 31.909  50.899  6.547   1.00 21.67  ? 493  THR A CG2 1 
ATOM   3708  N  N   . ALA A 1 485 ? 29.793  53.854  7.429   1.00 18.82  ? 494  ALA A N   1 
ATOM   3709  C  CA  . ALA A 1 485 ? 28.666  54.328  6.658   1.00 16.89  ? 494  ALA A CA  1 
ATOM   3710  C  C   . ALA A 1 485 ? 28.822  55.765  6.232   1.00 17.08  ? 494  ALA A C   1 
ATOM   3711  O  O   . ALA A 1 485 ? 28.364  56.125  5.118   1.00 18.42  ? 494  ALA A O   1 
ATOM   3712  C  CB  . ALA A 1 485 ? 27.320  54.147  7.439   1.00 16.60  ? 494  ALA A CB  1 
ATOM   3713  N  N   . LEU A 1 486 ? 29.420  56.591  7.036   1.00 17.75  ? 495  LEU A N   1 
ATOM   3714  C  CA  . LEU A 1 486 ? 29.596  58.015  6.638   1.00 17.55  ? 495  LEU A CA  1 
ATOM   3715  C  C   . LEU A 1 486 ? 30.531  58.027  5.397   1.00 16.48  ? 495  LEU A C   1 
ATOM   3716  O  O   . LEU A 1 486 ? 30.308  58.810  4.474   1.00 19.61  ? 495  LEU A O   1 
ATOM   3717  C  CB  . LEU A 1 486 ? 30.269  58.825  7.819   1.00 16.96  ? 495  LEU A CB  1 
ATOM   3718  C  CG  . LEU A 1 486 ? 29.164  59.098  8.938   1.00 18.93  ? 495  LEU A CG  1 
ATOM   3719  C  CD1 . LEU A 1 486 ? 29.875  59.476  10.302  1.00 22.07  ? 495  LEU A CD1 1 
ATOM   3720  C  CD2 . LEU A 1 486 ? 28.182  60.240  8.498   1.00 20.06  ? 495  LEU A CD2 1 
ATOM   3721  N  N   . ALA A 1 487 ? 31.553  57.190  5.430   1.00 17.90  ? 496  ALA A N   1 
ATOM   3722  C  CA  . ALA A 1 487 ? 32.518  57.172  4.294   1.00 21.35  ? 496  ALA A CA  1 
ATOM   3723  C  C   . ALA A 1 487 ? 31.843  56.628  3.025   1.00 22.55  ? 496  ALA A C   1 
ATOM   3724  O  O   . ALA A 1 487 ? 32.115  57.109  1.925   1.00 21.53  ? 496  ALA A O   1 
ATOM   3725  C  CB  . ALA A 1 487 ? 33.718  56.340  4.686   1.00 19.84  ? 496  ALA A CB  1 
ATOM   3726  N  N   . THR A 1 488 ? 30.971  55.601  3.157   1.00 21.81  ? 497  THR A N   1 
ATOM   3727  C  CA  . THR A 1 488 ? 30.234  55.115  1.999   1.00 17.88  ? 497  THR A CA  1 
ATOM   3728  C  C   . THR A 1 488 ? 29.345  56.206  1.435   1.00 22.13  ? 497  THR A C   1 
ATOM   3729  O  O   . THR A 1 488 ? 29.219  56.394  0.213   1.00 20.14  ? 497  THR A O   1 
ATOM   3730  C  CB  . THR A 1 488 ? 29.301  53.930  2.440   1.00 19.92  ? 497  THR A CB  1 
ATOM   3731  O  OG1 . THR A 1 488 ? 30.131  52.917  2.983   1.00 18.38  ? 497  THR A OG1 1 
ATOM   3732  C  CG2 . THR A 1 488 ? 28.432  53.392  1.234   1.00 20.02  ? 497  THR A CG2 1 
ATOM   3733  N  N   . THR A 1 489 ? 28.644  56.930  2.345   1.00 19.21  ? 498  THR A N   1 
ATOM   3734  C  CA  . THR A 1 489 ? 27.761  57.992  1.881   1.00 20.57  ? 498  THR A CA  1 
ATOM   3735  C  C   . THR A 1 489 ? 28.571  59.068  1.133   1.00 19.16  ? 498  THR A C   1 
ATOM   3736  O  O   . THR A 1 489 ? 28.156  59.563  0.071   1.00 20.17  ? 498  THR A O   1 
ATOM   3737  C  CB  . THR A 1 489 ? 27.029  58.627  3.142   1.00 19.19  ? 498  THR A CB  1 
ATOM   3738  O  OG1 . THR A 1 489 ? 26.213  57.587  3.690   1.00 17.29  ? 498  THR A OG1 1 
ATOM   3739  C  CG2 . THR A 1 489 ? 26.104  59.768  2.764   1.00 18.38  ? 498  THR A CG2 1 
ATOM   3740  N  N   . GLU A 1 490 ? 29.692  59.416  1.704   1.00 19.39  ? 499  GLU A N   1 
ATOM   3741  C  CA  . GLU A 1 490 ? 30.536  60.477  1.130   1.00 19.55  ? 499  GLU A CA  1 
ATOM   3742  C  C   . GLU A 1 490 ? 30.973  60.050  -0.331  1.00 24.87  ? 499  GLU A C   1 
ATOM   3743  O  O   . GLU A 1 490 ? 30.918  60.848  -1.248  1.00 22.88  ? 499  GLU A O   1 
ATOM   3744  C  CB  . GLU A 1 490 ? 31.798  60.612  1.974   1.00 25.69  ? 499  GLU A CB  1 
ATOM   3745  C  CG  . GLU A 1 490 ? 32.505  61.892  1.589   1.00 37.20  ? 499  GLU A CG  1 
ATOM   3746  C  CD  . GLU A 1 490 ? 31.828  63.110  2.291   1.00 50.10  ? 499  GLU A CD  1 
ATOM   3747  O  OE1 . GLU A 1 490 ? 30.630  63.047  2.633   1.00 52.60  ? 499  GLU A OE1 1 
ATOM   3748  O  OE2 . GLU A 1 490 ? 32.514  64.103  2.501   1.00 56.32  ? 499  GLU A OE2 1 
ATOM   3749  N  N   . TYR A 1 491 ? 31.371  58.774  -0.496  1.00 23.30  ? 500  TYR A N   1 
ATOM   3750  C  CA  . TYR A 1 491 ? 31.777  58.325  -1.846  1.00 23.95  ? 500  TYR A CA  1 
ATOM   3751  C  C   . TYR A 1 491 ? 30.615  58.389  -2.775  1.00 26.17  ? 500  TYR A C   1 
ATOM   3752  O  O   . TYR A 1 491 ? 30.730  58.947  -3.880  1.00 23.53  ? 500  TYR A O   1 
ATOM   3753  C  CB  . TYR A 1 491 ? 32.334  56.910  -1.794  1.00 22.87  ? 500  TYR A CB  1 
ATOM   3754  C  CG  . TYR A 1 491 ? 32.663  56.451  -3.209  1.00 27.37  ? 500  TYR A CG  1 
ATOM   3755  C  CD1 . TYR A 1 491 ? 33.859  56.815  -3.814  1.00 27.09  ? 500  TYR A CD1 1 
ATOM   3756  C  CD2 . TYR A 1 491 ? 31.733  55.742  -3.963  1.00 27.14  ? 500  TYR A CD2 1 
ATOM   3757  C  CE1 . TYR A 1 491 ? 34.116  56.499  -5.145  1.00 30.45  ? 500  TYR A CE1 1 
ATOM   3758  C  CE2 . TYR A 1 491 ? 31.984  55.401  -5.297  1.00 26.24  ? 500  TYR A CE2 1 
ATOM   3759  C  CZ  . TYR A 1 491 ? 33.175  55.788  -5.881  1.00 33.15  ? 500  TYR A CZ  1 
ATOM   3760  O  OH  . TYR A 1 491 ? 33.412  55.462  -7.200  1.00 31.61  ? 500  TYR A OH  1 
ATOM   3761  N  N   . LEU A 1 492 ? 29.447  57.866  -2.371  1.00 22.61  ? 501  LEU A N   1 
ATOM   3762  C  CA  . LEU A 1 492 ? 28.302  57.892  -3.288  1.00 23.77  ? 501  LEU A CA  1 
ATOM   3763  C  C   . LEU A 1 492 ? 27.899  59.305  -3.687  1.00 26.08  ? 501  LEU A C   1 
ATOM   3764  O  O   . LEU A 1 492 ? 27.564  59.567  -4.858  1.00 23.75  ? 501  LEU A O   1 
ATOM   3765  C  CB  . LEU A 1 492 ? 27.094  57.184  -2.623  1.00 20.89  ? 501  LEU A CB  1 
ATOM   3766  C  CG  . LEU A 1 492 ? 27.344  55.654  -2.485  1.00 24.93  ? 501  LEU A CG  1 
ATOM   3767  C  CD1 . LEU A 1 492 ? 26.255  54.990  -1.623  1.00 20.06  ? 501  LEU A CD1 1 
ATOM   3768  C  CD2 . LEU A 1 492 ? 27.289  55.025  -3.926  1.00 23.97  ? 501  LEU A CD2 1 
ATOM   3769  N  N   . ARG A 1 493 ? 27.896  60.229  -2.712  1.00 22.17  ? 502  ARG A N   1 
ATOM   3770  C  CA  . ARG A 1 493 ? 27.495  61.592  -3.049  1.00 24.67  ? 502  ARG A CA  1 
ATOM   3771  C  C   . ARG A 1 493 ? 28.489  62.234  -3.995  1.00 22.63  ? 502  ARG A C   1 
ATOM   3772  O  O   . ARG A 1 493 ? 28.064  63.027  -4.836  1.00 24.62  ? 502  ARG A O   1 
ATOM   3773  C  CB  . ARG A 1 493 ? 27.399  62.470  -1.780  1.00 24.34  ? 502  ARG A CB  1 
ATOM   3774  C  CG  . ARG A 1 493 ? 26.271  62.017  -0.910  1.00 24.83  ? 502  ARG A CG  1 
ATOM   3775  C  CD  . ARG A 1 493 ? 25.967  63.048  0.193   1.00 24.94  ? 502  ARG A CD  1 
ATOM   3776  N  NE  . ARG A 1 493 ? 24.734  62.629  0.865   1.00 28.02  ? 502  ARG A NE  1 
ATOM   3777  C  CZ  . ARG A 1 493 ? 24.390  63.021  2.086   1.00 33.44  ? 502  ARG A CZ  1 
ATOM   3778  N  NH1 . ARG A 1 493 ? 25.175  63.852  2.776   1.00 27.29  ? 502  ARG A NH1 1 
ATOM   3779  N  NH2 . ARG A 1 493 ? 23.259  62.596  2.626   1.00 30.21  ? 502  ARG A NH2 1 
ATOM   3780  N  N   . SER A 1 494 ? 29.761  61.954  -3.835  1.00 24.01  ? 503  SER A N   1 
ATOM   3781  C  CA  . SER A 1 494 ? 30.772  62.544  -4.706  1.00 28.37  ? 503  SER A CA  1 
ATOM   3782  C  C   . SER A 1 494 ? 30.606  62.030  -6.171  1.00 34.00  ? 503  SER A C   1 
ATOM   3783  O  O   . SER A 1 494 ? 31.165  62.642  -7.088  1.00 30.61  ? 503  SER A O   1 
ATOM   3784  C  CB  . SER A 1 494 ? 32.156  62.204  -4.198  1.00 27.70  ? 503  SER A CB  1 
ATOM   3785  O  OG  . SER A 1 494 ? 32.506  60.887  -4.587  1.00 25.90  ? 503  SER A OG  1 
ATOM   3786  N  N   . LYS A 1 495 ? 29.863  60.921  -6.383  1.00 31.19  ? 504  LYS A N   1 
ATOM   3787  C  CA  . LYS A 1 495 ? 29.614  60.399  -7.750  1.00 27.38  ? 504  LYS A CA  1 
ATOM   3788  C  C   . LYS A 1 495 ? 28.213  60.751  -8.199  1.00 29.18  ? 504  LYS A C   1 
ATOM   3789  O  O   . LYS A 1 495 ? 27.744  60.192  -9.184  1.00 31.22  ? 504  LYS A O   1 
ATOM   3790  C  CB  . LYS A 1 495 ? 29.822  58.878  -7.774  1.00 25.14  ? 504  LYS A CB  1 
ATOM   3791  C  CG  . LYS A 1 495 ? 31.232  58.504  -7.356  1.00 23.11  ? 504  LYS A CG  1 
ATOM   3792  C  CD  . LYS A 1 495 ? 32.216  59.311  -8.182  1.00 31.76  ? 504  LYS A CD  1 
ATOM   3793  C  CE  . LYS A 1 495 ? 33.457  58.519  -8.408  1.00 41.63  ? 504  LYS A CE  1 
ATOM   3794  N  NZ  . LYS A 1 495 ? 34.591  59.067  -7.651  1.00 50.93  ? 504  LYS A NZ  1 
ATOM   3795  N  N   . GLY A 1 496 ? 27.517  61.663  -7.511  1.00 26.27  ? 505  GLY A N   1 
ATOM   3796  C  CA  . GLY A 1 496 ? 26.197  62.084  -7.966  1.00 28.86  ? 505  GLY A CA  1 
ATOM   3797  C  C   . GLY A 1 496 ? 25.038  61.168  -7.608  1.00 33.67  ? 505  GLY A C   1 
ATOM   3798  O  O   . GLY A 1 496 ? 23.961  61.298  -8.178  1.00 33.31  ? 505  GLY A O   1 
ATOM   3799  N  N   . ILE A 1 497 ? 25.234  60.221  -6.652  1.00 30.79  ? 506  ILE A N   1 
ATOM   3800  C  CA  . ILE A 1 497 ? 24.142  59.335  -6.240  1.00 27.15  ? 506  ILE A CA  1 
ATOM   3801  C  C   . ILE A 1 497 ? 23.493  59.933  -4.979  1.00 28.09  ? 506  ILE A C   1 
ATOM   3802  O  O   . ILE A 1 497 ? 24.220  60.372  -4.109  1.00 29.72  ? 506  ILE A O   1 
ATOM   3803  C  CB  . ILE A 1 497 ? 24.751  57.888  -6.003  1.00 27.63  ? 506  ILE A CB  1 
ATOM   3804  C  CG1 . ILE A 1 497 ? 25.149  57.262  -7.385  1.00 28.23  ? 506  ILE A CG1 1 
ATOM   3805  C  CG2 . ILE A 1 497 ? 23.718  56.971  -5.280  1.00 26.89  ? 506  ILE A CG2 1 
ATOM   3806  C  CD1 . ILE A 1 497 ? 26.290  56.199  -7.373  1.00 28.14  ? 506  ILE A CD1 1 
ATOM   3807  N  N   . ASN A 1 498 ? 22.201  59.991  -4.898  1.00 26.70  ? 507  ASN A N   1 
ATOM   3808  C  CA  . ASN A 1 498 ? 21.509  60.516  -3.738  1.00 29.93  ? 507  ASN A CA  1 
ATOM   3809  C  C   . ASN A 1 498 ? 21.559  59.501  -2.628  1.00 32.85  ? 507  ASN A C   1 
ATOM   3810  O  O   . ASN A 1 498 ? 21.270  58.340  -2.889  1.00 29.62  ? 507  ASN A O   1 
ATOM   3811  C  CB  . ASN A 1 498 ? 20.055  60.772  -4.066  1.00 38.05  ? 507  ASN A CB  1 
ATOM   3812  C  CG  . ASN A 1 498 ? 19.936  61.707  -5.233  1.00 52.90  ? 507  ASN A CG  1 
ATOM   3813  O  OD1 . ASN A 1 498 ? 19.122  61.462  -6.133  1.00 58.10  ? 507  ASN A OD1 1 
ATOM   3814  N  ND2 . ASN A 1 498 ? 20.773  62.747  -5.313  1.00 55.22  ? 507  ASN A ND2 1 
ATOM   3815  N  N   . VAL A 1 499 ? 21.882  59.929  -1.397  1.00 30.55  ? 508  VAL A N   1 
ATOM   3816  C  CA  . VAL A 1 499 ? 21.972  58.995  -0.294  1.00 28.55  ? 508  VAL A CA  1 
ATOM   3817  C  C   . VAL A 1 499 ? 21.178  59.446  0.841   1.00 28.76  ? 508  VAL A C   1 
ATOM   3818  O  O   . VAL A 1 499 ? 21.279  60.613  1.220   1.00 27.95  ? 508  VAL A O   1 
ATOM   3819  C  CB  . VAL A 1 499 ? 23.434  58.821  0.169   1.00 26.42  ? 508  VAL A CB  1 
ATOM   3820  C  CG1 . VAL A 1 499 ? 23.527  57.750  1.273   1.00 26.91  ? 508  VAL A CG1 1 
ATOM   3821  C  CG2 . VAL A 1 499 ? 24.306  58.422  -0.996  1.00 24.88  ? 508  VAL A CG2 1 
ATOM   3822  N  N   . VAL A 1 500 ? 20.358  58.561  1.401   1.00 26.64  ? 509  VAL A N   1 
ATOM   3823  C  CA  . VAL A 1 500 ? 19.650  58.903  2.632   1.00 25.57  ? 509  VAL A CA  1 
ATOM   3824  C  C   . VAL A 1 500 ? 20.240  57.972  3.706   1.00 25.63  ? 509  VAL A C   1 
ATOM   3825  O  O   . VAL A 1 500 ? 20.238  56.751  3.500   1.00 23.99  ? 509  VAL A O   1 
ATOM   3826  C  CB  . VAL A 1 500 ? 18.108  58.653  2.558   1.00 27.91  ? 509  VAL A CB  1 
ATOM   3827  C  CG1 . VAL A 1 500 ? 17.487  58.898  3.917   1.00 31.34  ? 509  VAL A CG1 1 
ATOM   3828  C  CG2 . VAL A 1 500 ? 17.430  59.563  1.499   1.00 30.21  ? 509  VAL A CG2 1 
ATOM   3829  N  N   . MET A 1 501 ? 20.713  58.489  4.833   1.00 21.42  ? 510  MET A N   1 
ATOM   3830  C  CA  . MET A 1 501 ? 21.235  57.590  5.860   1.00 20.45  ? 510  MET A CA  1 
ATOM   3831  C  C   . MET A 1 501 ? 20.126  57.321  6.877   1.00 22.48  ? 510  MET A C   1 
ATOM   3832  O  O   . MET A 1 501 ? 19.416  58.249  7.238   1.00 22.89  ? 510  MET A O   1 
ATOM   3833  C  CB  . MET A 1 501 ? 22.412  58.253  6.613   1.00 20.34  ? 510  MET A CB  1 
ATOM   3834  C  CG  . MET A 1 501 ? 23.645  58.551  5.698   1.00 19.92  ? 510  MET A CG  1 
ATOM   3835  S  SD  . MET A 1 501 ? 25.079  59.037  6.630   1.00 25.78  ? 510  MET A SD  1 
ATOM   3836  C  CE  . MET A 1 501 ? 25.487  57.441  7.449   1.00 21.86  ? 510  MET A CE  1 
ATOM   3837  N  N   . THR A 1 502 ? 19.966  56.108  7.368   1.00 22.73  ? 511  THR A N   1 
ATOM   3838  C  CA  . THR A 1 502 ? 18.907  55.890  8.366   1.00 22.37  ? 511  THR A CA  1 
ATOM   3839  C  C   . THR A 1 502 ? 19.241  56.700  9.640   1.00 19.84  ? 511  THR A C   1 
ATOM   3840  O  O   . THR A 1 502 ? 18.345  57.207  10.289  1.00 22.30  ? 511  THR A O   1 
ATOM   3841  C  CB  . THR A 1 502 ? 18.759  54.380  8.696   1.00 19.69  ? 511  THR A CB  1 
ATOM   3842  O  OG1 . THR A 1 502 ? 20.030  53.879  9.077   1.00 18.10  ? 511  THR A OG1 1 
ATOM   3843  C  CG2 . THR A 1 502 ? 18.229  53.565  7.517   1.00 20.83  ? 511  THR A CG2 1 
ATOM   3844  N  N   . ARG A 1 503 ? 20.521  56.817  9.977   1.00 21.96  ? 512  ARG A N   1 
ATOM   3845  C  CA  . ARG A 1 503 ? 20.978  57.654  11.076  1.00 23.22  ? 512  ARG A CA  1 
ATOM   3846  C  C   . ARG A 1 503 ? 22.360  58.192  10.698  1.00 25.43  ? 512  ARG A C   1 
ATOM   3847  O  O   . ARG A 1 503 ? 23.135  57.489  9.998   1.00 24.65  ? 512  ARG A O   1 
ATOM   3848  C  CB  . ARG A 1 503 ? 21.056  56.871  12.406  1.00 23.21  ? 512  ARG A CB  1 
ATOM   3849  C  CG  . ARG A 1 503 ? 22.133  55.762  12.416  1.00 25.30  ? 512  ARG A CG  1 
ATOM   3850  C  CD  . ARG A 1 503 ? 22.242  55.077  13.820  1.00 23.00  ? 512  ARG A CD  1 
ATOM   3851  N  NE  . ARG A 1 503 ? 23.217  53.962  13.814  1.00 22.40  ? 512  ARG A NE  1 
ATOM   3852  C  CZ  . ARG A 1 503 ? 24.426  54.065  14.342  1.00 19.62  ? 512  ARG A CZ  1 
ATOM   3853  N  NH1 . ARG A 1 503 ? 24.846  55.188  14.894  1.00 22.94  ? 512  ARG A NH1 1 
ATOM   3854  N  NH2 . ARG A 1 503 ? 25.233  52.996  14.336  1.00 20.41  ? 512  ARG A NH2 1 
ATOM   3855  N  N   . ASP A 1 504 ? 22.682  59.410  11.122  1.00 24.61  ? 513  ASP A N   1 
ATOM   3856  C  CA  . ASP A 1 504 ? 24.011  59.936  10.794  1.00 25.84  ? 513  ASP A CA  1 
ATOM   3857  C  C   . ASP A 1 504 ? 24.711  60.284  12.082  1.00 28.50  ? 513  ASP A C   1 
ATOM   3858  O  O   . ASP A 1 504 ? 25.766  60.922  12.073  1.00 29.57  ? 513  ASP A O   1 
ATOM   3859  C  CB  . ASP A 1 504 ? 23.923  61.166  9.895   1.00 31.48  ? 513  ASP A CB  1 
ATOM   3860  C  CG  . ASP A 1 504 ? 22.859  62.146  10.344  1.00 39.90  ? 513  ASP A CG  1 
ATOM   3861  O  OD1 . ASP A 1 504 ? 22.840  62.500  11.547  1.00 40.45  ? 513  ASP A OD1 1 
ATOM   3862  O  OD2 . ASP A 1 504 ? 22.053  62.561  9.497   1.00 44.74  ? 513  ASP A OD2 1 
ATOM   3863  N  N   . THR A 1 505 ? 24.143  59.868  13.190  1.00 28.20  ? 514  THR A N   1 
ATOM   3864  C  CA  . THR A 1 505 ? 24.753  60.080  14.475  1.00 28.83  ? 514  THR A CA  1 
ATOM   3865  C  C   . THR A 1 505 ? 24.423  58.919  15.400  1.00 28.09  ? 514  THR A C   1 
ATOM   3866  O  O   . THR A 1 505 ? 23.641  58.027  15.044  1.00 26.14  ? 514  THR A O   1 
ATOM   3867  C  CB  . THR A 1 505 ? 24.209  61.409  15.090  1.00 35.38  ? 514  THR A CB  1 
ATOM   3868  O  OG1 . THR A 1 505 ? 25.117  61.812  16.118  1.00 38.58  ? 514  THR A OG1 1 
ATOM   3869  C  CG2 . THR A 1 505 ? 22.835  61.233  15.634  1.00 35.78  ? 514  THR A CG2 1 
ATOM   3870  N  N   . ASP A 1 506 ? 24.987  58.918  16.602  1.00 27.20  ? 515  ASP A N   1 
ATOM   3871  C  CA  . ASP A 1 506 ? 24.689  57.854  17.532  1.00 31.49  ? 515  ASP A CA  1 
ATOM   3872  C  C   . ASP A 1 506 ? 23.279  58.050  18.025  1.00 37.13  ? 515  ASP A C   1 
ATOM   3873  O  O   . ASP A 1 506 ? 23.002  59.066  18.645  1.00 38.44  ? 515  ASP A O   1 
ATOM   3874  C  CB  . ASP A 1 506 ? 25.675  57.852  18.700  1.00 32.13  ? 515  ASP A CB  1 
ATOM   3875  C  CG  . ASP A 1 506 ? 25.503  56.662  19.641  1.00 39.61  ? 515  ASP A CG  1 
ATOM   3876  O  OD1 . ASP A 1 506 ? 25.020  55.611  19.196  1.00 34.98  ? 515  ASP A OD1 1 
ATOM   3877  O  OD2 . ASP A 1 506 ? 25.864  56.786  20.816  1.00 44.88  ? 515  ASP A OD2 1 
ATOM   3878  N  N   . LYS A 1 507 ? 22.361  57.139  17.692  1.00 33.47  ? 516  LYS A N   1 
ATOM   3879  C  CA  . LYS A 1 507 ? 21.008  57.208  18.218  1.00 33.51  ? 516  LYS A CA  1 
ATOM   3880  C  C   . LYS A 1 507 ? 20.345  55.852  18.157  1.00 31.24  ? 516  LYS A C   1 
ATOM   3881  O  O   . LYS A 1 507 ? 20.745  55.017  17.372  1.00 26.06  ? 516  LYS A O   1 
ATOM   3882  C  CB  . LYS A 1 507 ? 20.143  58.208  17.492  1.00 36.38  ? 516  LYS A CB  1 
ATOM   3883  C  CG  . LYS A 1 507 ? 19.835  57.863  16.090  1.00 39.58  ? 516  LYS A CG  1 
ATOM   3884  C  CD  . LYS A 1 507 ? 18.575  58.606  15.675  1.00 49.45  ? 516  LYS A CD  1 
ATOM   3885  C  CE  . LYS A 1 507 ? 17.895  57.887  14.537  1.00 59.14  ? 516  LYS A CE  1 
ATOM   3886  N  NZ  . LYS A 1 507 ? 16.663  58.578  14.096  1.00 58.60  ? 516  LYS A NZ  1 
ATOM   3887  N  N   . THR A 1 508 ? 19.352  55.630  19.018  1.00 29.46  ? 517  THR A N   1 
ATOM   3888  C  CA  . THR A 1 508 ? 18.600  54.371  19.048  1.00 27.20  ? 517  THR A CA  1 
ATOM   3889  C  C   . THR A 1 508 ? 17.645  54.334  17.851  1.00 26.33  ? 517  THR A C   1 
ATOM   3890  O  O   . THR A 1 508 ? 16.904  55.288  17.620  1.00 24.69  ? 517  THR A O   1 
ATOM   3891  C  CB  . THR A 1 508 ? 17.836  54.279  20.420  1.00 29.69  ? 517  THR A CB  1 
ATOM   3892  O  OG1 . THR A 1 508 ? 18.843  54.228  21.446  1.00 28.25  ? 517  THR A OG1 1 
ATOM   3893  C  CG2 . THR A 1 508 ? 16.967  52.965  20.518  1.00 29.49  ? 517  THR A CG2 1 
ATOM   3894  N  N   . MET A 1 509 ? 17.643  53.254  17.084  1.00 22.91  ? 518  MET A N   1 
ATOM   3895  C  CA  . MET A 1 509 ? 16.731  53.235  15.966  1.00 21.37  ? 518  MET A CA  1 
ATOM   3896  C  C   . MET A 1 509 ? 16.336  51.765  15.675  1.00 21.70  ? 518  MET A C   1 
ATOM   3897  O  O   . MET A 1 509 ? 17.235  50.943  15.455  1.00 21.88  ? 518  MET A O   1 
ATOM   3898  C  CB  . MET A 1 509 ? 17.356  53.858  14.696  1.00 23.28  ? 518  MET A CB  1 
ATOM   3899  C  CG  . MET A 1 509 ? 16.308  54.041  13.634  1.00 22.14  ? 518  MET A CG  1 
ATOM   3900  S  SD  . MET A 1 509 ? 17.107  54.977  12.268  1.00 26.57  ? 518  MET A SD  1 
ATOM   3901  C  CE  . MET A 1 509 ? 15.740  55.299  11.199  1.00 24.31  ? 518  MET A CE  1 
ATOM   3902  N  N   . ALA A 1 510 ? 15.035  51.459  15.650  1.00 21.53  ? 519  ALA A N   1 
ATOM   3903  C  CA  . ALA A 1 510 ? 14.593  50.067  15.467  1.00 23.09  ? 519  ALA A CA  1 
ATOM   3904  C  C   . ALA A 1 510 ? 14.660  49.604  14.003  1.00 23.01  ? 519  ALA A C   1 
ATOM   3905  O  O   . ALA A 1 510 ? 14.571  50.414  13.079  1.00 22.10  ? 519  ALA A O   1 
ATOM   3906  C  CB  . ALA A 1 510 ? 13.130  49.936  15.924  1.00 22.30  ? 519  ALA A CB  1 
ATOM   3907  N  N   . LEU A 1 511 ? 14.728  48.268  13.809  1.00 22.43  ? 520  LEU A N   1 
ATOM   3908  C  CA  . LEU A 1 511 ? 14.766  47.687  12.488  1.00 22.38  ? 520  LEU A CA  1 
ATOM   3909  C  C   . LEU A 1 511 ? 13.539  48.124  11.698  1.00 23.17  ? 520  LEU A C   1 
ATOM   3910  O  O   . LEU A 1 511 ? 13.617  48.418  10.504  1.00 24.09  ? 520  LEU A O   1 
ATOM   3911  C  CB  . LEU A 1 511 ? 14.823  46.120  12.657  1.00 20.89  ? 520  LEU A CB  1 
ATOM   3912  C  CG  . LEU A 1 511 ? 16.140  45.637  13.330  1.00 22.68  ? 520  LEU A CG  1 
ATOM   3913  C  CD1 . LEU A 1 511 ? 16.058  44.091  13.530  1.00 22.81  ? 520  LEU A CD1 1 
ATOM   3914  C  CD2 . LEU A 1 511 ? 17.469  45.911  12.415  1.00 22.03  ? 520  LEU A CD2 1 
ATOM   3915  N  N   . GLY A 1 512 ? 12.379  48.172  12.371  1.00 24.16  ? 521  GLY A N   1 
ATOM   3916  C  CA  . GLY A 1 512 ? 11.141  48.541  11.714  1.00 25.41  ? 521  GLY A CA  1 
ATOM   3917  C  C   . GLY A 1 512 ? 11.142  49.984  11.274  1.00 25.90  ? 521  GLY A C   1 
ATOM   3918  O  O   . GLY A 1 512 ? 10.491  50.342  10.287  1.00 27.89  ? 521  GLY A O   1 
ATOM   3919  N  N   . GLU A 1 513 ? 11.886  50.831  11.992  1.00 25.83  ? 522  GLU A N   1 
ATOM   3920  C  CA  . GLU A 1 513 ? 11.953  52.246  11.537  1.00 26.69  ? 522  GLU A CA  1 
ATOM   3921  C  C   . GLU A 1 513 ? 12.901  52.363  10.271  1.00 24.85  ? 522  GLU A C   1 
ATOM   3922  O  O   . GLU A 1 513 ? 12.596  53.061  9.297   1.00 25.81  ? 522  GLU A O   1 
ATOM   3923  C  CB  . GLU A 1 513 ? 12.503  53.144  12.665  1.00 29.40  ? 522  GLU A CB  1 
ATOM   3924  C  CG  . GLU A 1 513 ? 12.366  54.585  12.191  1.00 35.37  ? 522  GLU A CG  1 
ATOM   3925  C  CD  . GLU A 1 513 ? 12.653  55.644  13.254  1.00 42.20  ? 522  GLU A CD  1 
ATOM   3926  O  OE1 . GLU A 1 513 ? 13.032  55.294  14.414  1.00 31.22  ? 522  GLU A OE1 1 
ATOM   3927  O  OE2 . GLU A 1 513 ? 12.503  56.851  12.889  1.00 37.18  ? 522  GLU A OE2 1 
ATOM   3928  N  N   . ARG A 1 514 ? 14.034  51.641  10.303  1.00 25.60  ? 523  ARG A N   1 
ATOM   3929  C  CA  . ARG A 1 514 ? 14.979  51.646  9.173   1.00 22.11  ? 523  ARG A CA  1 
ATOM   3930  C  C   . ARG A 1 514 ? 14.285  51.127  7.976   1.00 23.78  ? 523  ARG A C   1 
ATOM   3931  O  O   . ARG A 1 514 ? 14.453  51.662  6.873   1.00 24.98  ? 523  ARG A O   1 
ATOM   3932  C  CB  . ARG A 1 514 ? 16.185  50.788  9.530   1.00 21.19  ? 523  ARG A CB  1 
ATOM   3933  C  CG  . ARG A 1 514 ? 16.907  51.334  10.768  1.00 21.77  ? 523  ARG A CG  1 
ATOM   3934  C  CD  . ARG A 1 514 ? 17.762  50.250  11.383  1.00 24.26  ? 523  ARG A CD  1 
ATOM   3935  N  NE  . ARG A 1 514 ? 18.229  50.600  12.718  1.00 23.09  ? 523  ARG A NE  1 
ATOM   3936  C  CZ  . ARG A 1 514 ? 19.493  50.871  13.027  1.00 23.64  ? 523  ARG A CZ  1 
ATOM   3937  N  NH1 . ARG A 1 514 ? 20.432  50.888  12.078  1.00 21.24  ? 523  ARG A NH1 1 
ATOM   3938  N  NH2 . ARG A 1 514 ? 19.839  51.080  14.289  1.00 22.15  ? 523  ARG A NH2 1 
ATOM   3939  N  N   . THR A 1 515 ? 13.491  50.033  8.139   1.00 24.23  ? 524  THR A N   1 
ATOM   3940  C  CA  . THR A 1 515 ? 12.794  49.491  6.979   1.00 24.77  ? 524  THR A CA  1 
ATOM   3941  C  C   . THR A 1 515 ? 11.689  50.405  6.496   1.00 27.27  ? 524  THR A C   1 
ATOM   3942  O  O   . THR A 1 515 ? 11.525  50.567  5.276   1.00 30.31  ? 524  THR A O   1 
ATOM   3943  C  CB  . THR A 1 515 ? 12.218  48.085  7.298   1.00 28.41  ? 524  THR A CB  1 
ATOM   3944  O  OG1 . THR A 1 515 ? 13.268  47.331  7.949   1.00 29.95  ? 524  THR A OG1 1 
ATOM   3945  C  CG2 . THR A 1 515 ? 11.868  47.353  6.028   1.00 31.30  ? 524  THR A CG2 1 
ATOM   3946  N  N   . ALA A 1 516 ? 10.929  51.024  7.411   1.00 31.85  ? 525  ALA A N   1 
ATOM   3947  C  CA  . ALA A 1 516 ? 9.849   51.940  6.973   1.00 33.77  ? 525  ALA A CA  1 
ATOM   3948  C  C   . ALA A 1 516 ? 10.455  53.053  6.147   1.00 33.54  ? 525  ALA A C   1 
ATOM   3949  O  O   . ALA A 1 516 ? 9.894   53.447  5.127   1.00 32.75  ? 525  ALA A O   1 
ATOM   3950  C  CB  . ALA A 1 516 ? 9.140   52.557  8.172   1.00 33.14  ? 525  ALA A CB  1 
ATOM   3951  N  N   . LEU A 1 517 ? 11.637  53.542  6.575   1.00 31.61  ? 526  LEU A N   1 
ATOM   3952  C  CA  . LEU A 1 517 ? 12.322  54.603  5.857   1.00 31.12  ? 526  LEU A CA  1 
ATOM   3953  C  C   . LEU A 1 517 ? 12.632  54.134  4.486   1.00 29.65  ? 526  LEU A C   1 
ATOM   3954  O  O   . LEU A 1 517 ? 12.398  54.862  3.507   1.00 31.46  ? 526  LEU A O   1 
ATOM   3955  C  CB  . LEU A 1 517 ? 13.627  55.017  6.565   1.00 32.27  ? 526  LEU A CB  1 
ATOM   3956  C  CG  . LEU A 1 517 ? 14.394  56.160  5.882   1.00 35.86  ? 526  LEU A CG  1 
ATOM   3957  C  CD1 . LEU A 1 517 ? 13.484  57.414  5.786   1.00 37.87  ? 526  LEU A CD1 1 
ATOM   3958  C  CD2 . LEU A 1 517 ? 15.625  56.487  6.680   1.00 39.70  ? 526  LEU A CD2 1 
ATOM   3959  N  N   . SER A 1 518 ? 13.181  52.924  4.365   1.00 29.37  ? 527  SER A N   1 
ATOM   3960  C  CA  . SER A 1 518 ? 13.515  52.391  3.024   1.00 26.43  ? 527  SER A CA  1 
ATOM   3961  C  C   . SER A 1 518 ? 12.275  52.348  2.138   1.00 28.59  ? 527  SER A C   1 
ATOM   3962  O  O   . SER A 1 518 ? 12.307  52.743  0.981   1.00 29.61  ? 527  SER A O   1 
ATOM   3963  C  CB  . SER A 1 518 ? 14.055  50.972  3.160   1.00 27.74  ? 527  SER A CB  1 
ATOM   3964  O  OG  . SER A 1 518 ? 14.581  50.528  1.923   1.00 29.61  ? 527  SER A OG  1 
ATOM   3965  N  N   . ASN A 1 519 ? 11.170  51.849  2.690   1.00 33.13  ? 528  ASN A N   1 
ATOM   3966  C  CA  . ASN A 1 519 ? 9.902   51.727  1.945   1.00 37.35  ? 528  ASN A CA  1 
ATOM   3967  C  C   . ASN A 1 519 ? 9.317   53.098  1.574   1.00 38.56  ? 528  ASN A C   1 
ATOM   3968  O  O   . ASN A 1 519 ? 8.572   53.201  0.598   1.00 38.22  ? 528  ASN A O   1 
ATOM   3969  C  CB  . ASN A 1 519 ? 8.892   50.899  2.784   1.00 37.67  ? 528  ASN A CB  1 
ATOM   3970  C  CG  . ASN A 1 519 ? 9.315   49.465  2.849   1.00 37.41  ? 528  ASN A CG  1 
ATOM   3971  O  OD1 . ASN A 1 519 ? 10.083  48.997  1.976   1.00 33.45  ? 528  ASN A OD1 1 
ATOM   3972  N  ND2 . ASN A 1 519 ? 8.946   48.711  3.864   1.00 33.52  ? 528  ASN A ND2 1 
ATOM   3973  N  N   . THR A 1 520 ? 9.643   54.134  2.336   1.00 36.02  ? 529  THR A N   1 
ATOM   3974  C  CA  . THR A 1 520 ? 9.174   55.478  2.044   1.00 35.99  ? 529  THR A CA  1 
ATOM   3975  C  C   . THR A 1 520 ? 10.050  56.085  0.948   1.00 39.63  ? 529  THR A C   1 
ATOM   3976  O  O   . THR A 1 520 ? 9.561   56.770  0.064   1.00 40.46  ? 529  THR A O   1 
ATOM   3977  C  CB  . THR A 1 520 ? 9.248   56.295  3.327   1.00 39.72  ? 529  THR A CB  1 
ATOM   3978  O  OG1 . THR A 1 520 ? 8.213   55.859  4.212   1.00 44.85  ? 529  THR A OG1 1 
ATOM   3979  C  CG2 . THR A 1 520 ? 9.103   57.776  3.080   1.00 43.41  ? 529  THR A CG2 1 
ATOM   3980  N  N   . ILE A 1 521 ? 11.365  55.824  0.988   1.00 37.46  ? 530  ILE A N   1 
ATOM   3981  C  CA  . ILE A 1 521 ? 12.305  56.396  0.033   1.00 35.83  ? 530  ILE A CA  1 
ATOM   3982  C  C   . ILE A 1 521 ? 12.259  55.698  -1.285  1.00 33.87  ? 530  ILE A C   1 
ATOM   3983  O  O   . ILE A 1 521 ? 12.517  56.348  -2.303  1.00 33.35  ? 530  ILE A O   1 
ATOM   3984  C  CB  . ILE A 1 521 ? 13.790  56.341  0.594   1.00 34.24  ? 530  ILE A CB  1 
ATOM   3985  C  CG1 . ILE A 1 521 ? 13.967  57.227  1.851   1.00 35.80  ? 530  ILE A CG1 1 
ATOM   3986  C  CG2 . ILE A 1 521 ? 14.758  56.787  -0.437  1.00 35.47  ? 530  ILE A CG2 1 
ATOM   3987  C  CD1 . ILE A 1 521 ? 13.594  58.674  1.622   1.00 42.55  ? 530  ILE A CD1 1 
ATOM   3988  N  N   . LYS A 1 522 ? 11.956  54.381  -1.299  1.00 33.74  ? 531  LYS A N   1 
ATOM   3989  C  CA  . LYS A 1 522 ? 11.909  53.554  -2.527  1.00 35.00  ? 531  LYS A CA  1 
ATOM   3990  C  C   . LYS A 1 522 ? 13.250  53.597  -3.227  1.00 37.47  ? 531  LYS A C   1 
ATOM   3991  O  O   . LYS A 1 522 ? 13.342  53.914  -4.424  1.00 35.09  ? 531  LYS A O   1 
ATOM   3992  C  CB  . LYS A 1 522 ? 10.776  54.036  -3.462  1.00 34.91  ? 531  LYS A CB  1 
ATOM   3993  C  CG  . LYS A 1 522 ? 9.530   54.411  -2.650  1.00 37.75  ? 531  LYS A CG  1 
ATOM   3994  C  CD  . LYS A 1 522 ? 8.243   54.489  -3.496  1.00 45.11  ? 531  LYS A CD  1 
ATOM   3995  C  CE  . LYS A 1 522 ? 7.132   55.166  -2.729  0.00 0.00   ? 531  LYS A CE  1 
ATOM   3996  N  NZ  . LYS A 1 522 ? 5.796   54.789  -3.261  0.00 0.00   ? 531  LYS A NZ  1 
ATOM   3997  N  N   . PRO A 1 523 ? 14.346  53.256  -2.510  1.00 35.77  ? 532  PRO A N   1 
ATOM   3998  C  CA  . PRO A 1 523 ? 15.646  53.313  -3.187  1.00 34.85  ? 532  PRO A CA  1 
ATOM   3999  C  C   . PRO A 1 523 ? 15.906  52.288  -4.228  1.00 34.24  ? 532  PRO A C   1 
ATOM   4000  O  O   . PRO A 1 523 ? 15.251  51.261  -4.305  1.00 30.61  ? 532  PRO A O   1 
ATOM   4001  C  CB  . PRO A 1 523 ? 16.648  53.091  -2.031  1.00 31.14  ? 532  PRO A CB  1 
ATOM   4002  C  CG  . PRO A 1 523 ? 15.909  52.102  -1.159  1.00 28.60  ? 532  PRO A CG  1 
ATOM   4003  C  CD  . PRO A 1 523 ? 14.498  52.732  -1.136  1.00 34.32  ? 532  PRO A CD  1 
ATOM   4004  N  N   . ASP A 1 524 ? 16.967  52.564  -5.006  1.00 31.33  ? 533  ASP A N   1 
ATOM   4005  C  CA  . ASP A 1 524 ? 17.463  51.614  -5.955  1.00 32.15  ? 533  ASP A CA  1 
ATOM   4006  C  C   . ASP A 1 524 ? 18.101  50.485  -5.129  1.00 32.93  ? 533  ASP A C   1 
ATOM   4007  O  O   . ASP A 1 524 ? 18.077  49.321  -5.526  1.00 27.94  ? 533  ASP A O   1 
ATOM   4008  C  CB  . ASP A 1 524 ? 18.528  52.273  -6.885  1.00 35.13  ? 533  ASP A CB  1 
ATOM   4009  C  CG  . ASP A 1 524 ? 17.866  53.241  -7.867  1.00 42.06  ? 533  ASP A CG  1 
ATOM   4010  O  OD1 . ASP A 1 524 ? 18.061  54.467  -7.729  1.00 40.98  ? 533  ASP A OD1 1 
ATOM   4011  O  OD2 . ASP A 1 524 ? 17.143  52.774  -8.737  1.00 44.43  ? 533  ASP A OD2 1 
ATOM   4012  N  N   . LEU A 1 525 ? 18.711  50.820  -3.957  1.00 26.92  ? 534  LEU A N   1 
ATOM   4013  C  CA  . LEU A 1 525 ? 19.343  49.770  -3.123  1.00 26.56  ? 534  LEU A CA  1 
ATOM   4014  C  C   . LEU A 1 525 ? 19.454  50.266  -1.688  1.00 26.52  ? 534  LEU A C   1 
ATOM   4015  O  O   . LEU A 1 525 ? 19.749  51.443  -1.484  1.00 26.02  ? 534  LEU A O   1 
ATOM   4016  C  CB  . LEU A 1 525 ? 20.763  49.442  -3.606  1.00 25.07  ? 534  LEU A CB  1 
ATOM   4017  C  CG  . LEU A 1 525 ? 21.497  48.372  -2.770  1.00 26.56  ? 534  LEU A CG  1 
ATOM   4018  C  CD1 . LEU A 1 525 ? 20.863  46.959  -3.105  1.00 28.61  ? 534  LEU A CD1 1 
ATOM   4019  C  CD2 . LEU A 1 525 ? 22.993  48.269  -3.079  1.00 25.21  ? 534  LEU A CD2 1 
ATOM   4020  N  N   . PHE A 1 526 ? 19.201  49.383  -0.731  1.00 25.98  ? 535  PHE A N   1 
ATOM   4021  C  CA  . PHE A 1 526 ? 19.298  49.624  0.701   1.00 21.62  ? 535  PHE A CA  1 
ATOM   4022  C  C   . PHE A 1 526 ? 20.440  48.791  1.159   1.00 23.21  ? 535  PHE A C   1 
ATOM   4023  O  O   . PHE A 1 526 ? 20.443  47.566  0.925   1.00 24.26  ? 535  PHE A O   1 
ATOM   4024  C  CB  . PHE A 1 526 ? 17.989  49.215  1.386   1.00 20.63  ? 535  PHE A CB  1 
ATOM   4025  C  CG  . PHE A 1 526 ? 18.027  49.224  2.909   1.00 23.86  ? 535  PHE A CG  1 
ATOM   4026  C  CD1 . PHE A 1 526 ? 18.642  48.203  3.613   1.00 23.83  ? 535  PHE A CD1 1 
ATOM   4027  C  CD2 . PHE A 1 526 ? 17.408  50.230  3.625   1.00 26.12  ? 535  PHE A CD2 1 
ATOM   4028  C  CE1 . PHE A 1 526 ? 18.635  48.202  5.026   1.00 21.67  ? 535  PHE A CE1 1 
ATOM   4029  C  CE2 . PHE A 1 526 ? 17.396  50.230  5.014   1.00 25.19  ? 535  PHE A CE2 1 
ATOM   4030  C  CZ  . PHE A 1 526 ? 18.015  49.209  5.703   1.00 23.49  ? 535  PHE A CZ  1 
ATOM   4031  N  N   . THR A 1 527 ? 21.448  49.398  1.831   1.00 20.27  ? 536  THR A N   1 
ATOM   4032  C  CA  . THR A 1 527 ? 22.580  48.645  2.303   1.00 17.78  ? 536  THR A CA  1 
ATOM   4033  C  C   . THR A 1 527 ? 22.742  48.826  3.821   1.00 23.40  ? 536  THR A C   1 
ATOM   4034  O  O   . THR A 1 527 ? 23.007  49.941  4.263   1.00 20.42  ? 536  THR A O   1 
ATOM   4035  C  CB  . THR A 1 527 ? 23.846  49.116  1.609   1.00 21.97  ? 536  THR A CB  1 
ATOM   4036  O  OG1 . THR A 1 527 ? 23.664  48.968  0.189   1.00 23.27  ? 536  THR A OG1 1 
ATOM   4037  C  CG2 . THR A 1 527 ? 25.051  48.295  1.950   1.00 20.04  ? 536  THR A CG2 1 
ATOM   4038  N  N   . SER A 1 528 ? 22.602  47.736  4.588   1.00 21.27  ? 537  SER A N   1 
ATOM   4039  C  CA  . SER A 1 528 ? 22.813  47.778  6.021   1.00 22.18  ? 537  SER A CA  1 
ATOM   4040  C  C   . SER A 1 528 ? 24.253  47.419  6.266   1.00 22.64  ? 537  SER A C   1 
ATOM   4041  O  O   . SER A 1 528 ? 24.776  46.493  5.632   1.00 23.80  ? 537  SER A O   1 
ATOM   4042  C  CB  . SER A 1 528 ? 21.817  46.828  6.707   1.00 23.94  ? 537  SER A CB  1 
ATOM   4043  O  OG  . SER A 1 528 ? 21.973  46.833  8.117   1.00 28.50  ? 537  SER A OG  1 
ATOM   4044  N  N   . ILE A 1 529 ? 24.954  48.129  7.167   1.00 18.11  ? 538  ILE A N   1 
ATOM   4045  C  CA  . ILE A 1 529 ? 26.358  47.900  7.387   1.00 19.20  ? 538  ILE A CA  1 
ATOM   4046  C  C   . ILE A 1 529 ? 26.539  47.468  8.813   1.00 23.08  ? 538  ILE A C   1 
ATOM   4047  O  O   . ILE A 1 529 ? 26.142  48.188  9.738   1.00 22.12  ? 538  ILE A O   1 
ATOM   4048  C  CB  . ILE A 1 529 ? 27.168  49.222  7.083   1.00 21.13  ? 538  ILE A CB  1 
ATOM   4049  C  CG1 . ILE A 1 529 ? 27.087  49.508  5.549   1.00 20.95  ? 538  ILE A CG1 1 
ATOM   4050  C  CG2 . ILE A 1 529 ? 28.661  49.071  7.454   1.00 19.97  ? 538  ILE A CG2 1 
ATOM   4051  C  CD1 . ILE A 1 529 ? 27.707  50.852  5.148   1.00 22.25  ? 538  ILE A CD1 1 
ATOM   4052  N  N   . HIS A 1 530 ? 27.152  46.311  8.990   1.00 22.47  ? 539  HIS A N   1 
ATOM   4053  C  CA  . HIS A 1 530 ? 27.352  45.688  10.293  1.00 22.18  ? 539  HIS A CA  1 
ATOM   4054  C  C   . HIS A 1 530 ? 28.765  45.108  10.439  1.00 27.53  ? 539  HIS A C   1 
ATOM   4055  O  O   . HIS A 1 530 ? 29.514  45.058  9.461   1.00 25.95  ? 539  HIS A O   1 
ATOM   4056  C  CB  . HIS A 1 530 ? 26.327  44.543  10.447  1.00 25.43  ? 539  HIS A CB  1 
ATOM   4057  C  CG  . HIS A 1 530 ? 24.934  45.032  10.732  1.00 25.32  ? 539  HIS A CG  1 
ATOM   4058  N  ND1 . HIS A 1 530 ? 24.347  44.911  11.999  1.00 25.68  ? 539  HIS A ND1 1 
ATOM   4059  C  CD2 . HIS A 1 530 ? 24.034  45.656  9.918   1.00 23.31  ? 539  HIS A CD2 1 
ATOM   4060  C  CE1 . HIS A 1 530 ? 23.147  45.473  11.893  1.00 25.41  ? 539  HIS A CE1 1 
ATOM   4061  N  NE2 . HIS A 1 530 ? 22.896  45.941  10.672  1.00 25.02  ? 539  HIS A NE2 1 
ATOM   4062  N  N   . TYR A 1 531 ? 29.147  44.703  11.671  1.00 26.96  ? 540  TYR A N   1 
ATOM   4063  C  CA  . TYR A 1 531 ? 30.435  44.043  11.917  1.00 30.06  ? 540  TYR A CA  1 
ATOM   4064  C  C   . TYR A 1 531 ? 30.113  42.690  12.596  1.00 34.68  ? 540  TYR A C   1 
ATOM   4065  O  O   . TYR A 1 531 ? 29.187  42.637  13.412  1.00 33.88  ? 540  TYR A O   1 
ATOM   4066  C  CB  . TYR A 1 531 ? 31.346  44.912  12.782  1.00 31.35  ? 540  TYR A CB  1 
ATOM   4067  C  CG  . TYR A 1 531 ? 32.066  45.932  11.929  1.00 32.54  ? 540  TYR A CG  1 
ATOM   4068  C  CD1 . TYR A 1 531 ? 33.372  45.716  11.501  1.00 29.55  ? 540  TYR A CD1 1 
ATOM   4069  C  CD2 . TYR A 1 531 ? 31.418  47.087  11.493  1.00 27.92  ? 540  TYR A CD2 1 
ATOM   4070  C  CE1 . TYR A 1 531 ? 34.009  46.610  10.647  1.00 27.31  ? 540  TYR A CE1 1 
ATOM   4071  C  CE2 . TYR A 1 531 ? 32.051  47.990  10.638  1.00 28.96  ? 540  TYR A CE2 1 
ATOM   4072  C  CZ  . TYR A 1 531 ? 33.342  47.745  10.213  1.00 29.64  ? 540  TYR A CZ  1 
ATOM   4073  O  OH  . TYR A 1 531 ? 33.965  48.634  9.361   1.00 27.79  ? 540  TYR A OH  1 
ATOM   4074  N  N   . ASN A 1 532 ? 30.815  41.601  12.217  1.00 32.75  ? 541  ASN A N   1 
ATOM   4075  C  CA  . ASN A 1 532 ? 30.551  40.245  12.741  1.00 33.96  ? 541  ASN A CA  1 
ATOM   4076  C  C   . ASN A 1 532 ? 31.269  39.991  14.037  1.00 34.73  ? 541  ASN A C   1 
ATOM   4077  O  O   . ASN A 1 532 ? 32.086  40.804  14.477  1.00 31.97  ? 541  ASN A O   1 
ATOM   4078  C  CB  . ASN A 1 532 ? 31.031  39.170  11.768  1.00 33.98  ? 541  ASN A CB  1 
ATOM   4079  C  CG  . ASN A 1 532 ? 29.908  38.359  11.249  1.00 39.43  ? 541  ASN A CG  1 
ATOM   4080  O  OD1 . ASN A 1 532 ? 29.009  38.017  12.016  1.00 39.45  ? 541  ASN A OD1 1 
ATOM   4081  N  ND2 . ASN A 1 532 ? 29.841  38.044  9.953   1.00 35.25  ? 541  ASN A ND2 1 
ATOM   4082  N  N   . ALA A 1 533 ? 30.959  38.830  14.643  1.00 34.81  ? 542  ALA A N   1 
ATOM   4083  C  CA  . ALA A 1 533 ? 31.574  38.380  15.915  1.00 41.50  ? 542  ALA A CA  1 
ATOM   4084  C  C   . ALA A 1 533 ? 31.264  36.884  16.085  1.00 39.58  ? 542  ALA A C   1 
ATOM   4085  O  O   . ALA A 1 533 ? 30.349  36.381  15.463  1.00 37.20  ? 542  ALA A O   1 
ATOM   4086  C  CB  . ALA A 1 533 ? 30.985  39.154  17.120  1.00 37.01  ? 542  ALA A CB  1 
ATOM   4087  N  N   . SER A 1 534 ? 32.023  36.211  16.902  1.00 42.94  ? 543  SER A N   1 
ATOM   4088  C  CA  . SER A 1 534 ? 31.825  34.816  17.262  1.00 49.06  ? 543  SER A CA  1 
ATOM   4089  C  C   . SER A 1 534 ? 32.684  34.731  18.543  1.00 55.45  ? 543  SER A C   1 
ATOM   4090  O  O   . SER A 1 534 ? 32.164  34.803  19.643  1.00 59.36  ? 543  SER A O   1 
ATOM   4091  C  CB  . SER A 1 534 ? 32.276  33.879  16.136  1.00 50.28  ? 543  SER A CB  1 
ATOM   4092  O  OG  . SER A 1 534 ? 33.643  33.999  15.771  1.00 51.35  ? 543  SER A OG  1 
ATOM   4093  N  N   . ASN A 1 535 ? 33.992  34.622  18.371  1.00 62.52  ? 544  ASN A N   1 
ATOM   4094  C  CA  . ASN A 1 535 ? 35.021  34.635  19.420  1.00 68.12  ? 544  ASN A CA  1 
ATOM   4095  C  C   . ASN A 1 535 ? 36.233  35.129  18.623  1.00 73.41  ? 544  ASN A C   1 
ATOM   4096  O  O   . ASN A 1 535 ? 36.001  35.729  17.595  1.00 77.87  ? 544  ASN A O   1 
ATOM   4097  C  CB  . ASN A 1 535 ? 35.238  33.261  20.101  1.00 70.14  ? 544  ASN A CB  1 
ATOM   4098  C  CG  . ASN A 1 535 ? 34.666  32.092  19.352  1.00 68.98  ? 544  ASN A CG  1 
ATOM   4099  O  OD1 . ASN A 1 535 ? 35.297  31.587  18.411  1.00 67.63  ? 544  ASN A OD1 1 
ATOM   4100  N  ND2 . ASN A 1 535 ? 33.481  31.611  19.694  1.00 69.28  ? 544  ASN A ND2 1 
ATOM   4101  N  N   . GLY A 1 536 ? 37.483  34.937  19.001  1.00 77.46  ? 545  GLY A N   1 
ATOM   4102  C  CA  . GLY A 1 536 ? 38.527  35.478  18.131  1.00 76.04  ? 545  GLY A CA  1 
ATOM   4103  C  C   . GLY A 1 536 ? 38.612  34.702  16.830  1.00 74.00  ? 545  GLY A C   1 
ATOM   4104  O  O   . GLY A 1 536 ? 39.189  35.162  15.850  1.00 71.92  ? 545  GLY A O   1 
ATOM   4105  N  N   . SER A 1 537 ? 37.995  33.493  16.845  1.00 71.46  ? 546  SER A N   1 
ATOM   4106  C  CA  . SER A 1 537 ? 37.940  32.510  15.761  1.00 66.79  ? 546  SER A CA  1 
ATOM   4107  C  C   . SER A 1 537 ? 37.461  33.043  14.375  1.00 62.83  ? 546  SER A C   1 
ATOM   4108  O  O   . SER A 1 537 ? 38.292  33.194  13.464  1.00 61.16  ? 546  SER A O   1 
ATOM   4109  C  CB  . SER A 1 537 ? 37.020  31.370  16.186  1.00 64.94  ? 546  SER A CB  1 
ATOM   4110  O  OG  . SER A 1 537 ? 37.206  30.245  15.345  1.00 70.76  ? 546  SER A OG  1 
ATOM   4111  N  N   . GLY A 1 538 ? 36.140  33.297  14.208  1.00 59.41  ? 547  GLY A N   1 
ATOM   4112  C  CA  . GLY A 1 538 ? 35.625  33.790  12.930  1.00 55.19  ? 547  GLY A CA  1 
ATOM   4113  C  C   . GLY A 1 538 ? 36.401  35.003  12.445  1.00 49.14  ? 547  GLY A C   1 
ATOM   4114  O  O   . GLY A 1 538 ? 36.911  35.797  13.226  1.00 43.54  ? 547  GLY A O   1 
ATOM   4115  N  N   . ASN A 1 539 ? 36.513  35.134  11.125  1.00 48.75  ? 548  ASN A N   1 
ATOM   4116  C  CA  . ASN A 1 539 ? 37.219  36.251  10.492  1.00 48.67  ? 548  ASN A CA  1 
ATOM   4117  C  C   . ASN A 1 539 ? 36.774  36.276  9.032   1.00 45.32  ? 548  ASN A C   1 
ATOM   4118  O  O   . ASN A 1 539 ? 36.305  35.252  8.515   1.00 42.60  ? 548  ASN A O   1 
ATOM   4119  C  CB  . ASN A 1 539 ? 38.763  36.113  10.596  1.00 49.97  ? 548  ASN A CB  1 
ATOM   4120  C  CG  . ASN A 1 539 ? 39.322  34.913  9.830   1.00 55.19  ? 548  ASN A CG  1 
ATOM   4121  O  OD1 . ASN A 1 539 ? 39.430  33.819  10.400  1.00 56.26  ? 548  ASN A OD1 1 
ATOM   4122  N  ND2 . ASN A 1 539 ? 39.632  35.016  8.532   1.00 53.82  ? 548  ASN A ND2 1 
ATOM   4123  N  N   . GLY A 1 540 ? 36.901  37.446  8.381   1.00 42.27  ? 549  GLY A N   1 
ATOM   4124  C  CA  . GLY A 1 540 ? 36.500  37.588  6.988   1.00 41.63  ? 549  GLY A CA  1 
ATOM   4125  C  C   . GLY A 1 540 ? 35.266  38.462  6.808   1.00 41.06  ? 549  GLY A C   1 
ATOM   4126  O  O   . GLY A 1 540 ? 34.718  39.009  7.772   1.00 35.37  ? 549  GLY A O   1 
ATOM   4127  N  N   . VAL A 1 541 ? 34.822  38.567  5.540   1.00 38.06  ? 550  VAL A N   1 
ATOM   4128  C  CA  . VAL A 1 541 ? 33.689  39.390  5.125   1.00 35.04  ? 550  VAL A CA  1 
ATOM   4129  C  C   . VAL A 1 541 ? 32.635  38.494  4.463   1.00 35.22  ? 550  VAL A C   1 
ATOM   4130  O  O   . VAL A 1 541 ? 32.977  37.525  3.757   1.00 32.85  ? 550  VAL A O   1 
ATOM   4131  C  CB  . VAL A 1 541 ? 34.227  40.500  4.135   1.00 35.43  ? 550  VAL A CB  1 
ATOM   4132  C  CG1 . VAL A 1 541 ? 35.015  39.873  2.987   1.00 37.00  ? 550  VAL A CG1 1 
ATOM   4133  C  CG2 . VAL A 1 541 ? 33.072  41.292  3.520   1.00 29.70  ? 550  VAL A CG2 1 
ATOM   4134  N  N   . GLU A 1 542 ? 31.348  38.799  4.698   1.00 30.01  ? 551  GLU A N   1 
ATOM   4135  C  CA  . GLU A 1 542 ? 30.227  38.090  4.081   1.00 31.36  ? 551  GLU A CA  1 
ATOM   4136  C  C   . GLU A 1 542 ? 29.118  39.074  3.915   1.00 28.67  ? 551  GLU A C   1 
ATOM   4137  O  O   . GLU A 1 542 ? 29.060  40.045  4.665   1.00 29.61  ? 551  GLU A O   1 
ATOM   4138  C  CB  . GLU A 1 542 ? 29.730  36.933  4.957   1.00 31.92  ? 551  GLU A CB  1 
ATOM   4139  C  CG  . GLU A 1 542 ? 29.401  37.389  6.384   1.00 35.79  ? 551  GLU A CG  1 
ATOM   4140  C  CD  . GLU A 1 542 ? 29.123  36.170  7.310   1.00 46.40  ? 551  GLU A CD  1 
ATOM   4141  O  OE1 . GLU A 1 542 ? 29.680  35.062  7.037   1.00 42.47  ? 551  GLU A OE1 1 
ATOM   4142  O  OE2 . GLU A 1 542 ? 28.345  36.320  8.274   1.00 43.34  ? 551  GLU A OE2 1 
ATOM   4143  N  N   . ILE A 1 543 ? 28.262  38.853  2.960   1.00 29.35  ? 552  ILE A N   1 
ATOM   4144  C  CA  . ILE A 1 543 ? 27.163  39.759  2.772   1.00 29.15  ? 552  ILE A CA  1 
ATOM   4145  C  C   . ILE A 1 543 ? 25.914  38.905  2.629   1.00 31.84  ? 552  ILE A C   1 
ATOM   4146  O  O   . ILE A 1 543 ? 25.945  37.914  1.906   1.00 32.06  ? 552  ILE A O   1 
ATOM   4147  C  CB  . ILE A 1 543 ? 27.434  40.610  1.490   1.00 27.95  ? 552  ILE A CB  1 
ATOM   4148  C  CG1 . ILE A 1 543 ? 28.816  41.392  1.650   1.00 29.22  ? 552  ILE A CG1 1 
ATOM   4149  C  CG2 . ILE A 1 543 ? 26.239  41.560  1.231   1.00 23.96  ? 552  ILE A CG2 1 
ATOM   4150  C  CD1 . ILE A 1 543 ? 29.148  42.296  0.516   1.00 31.93  ? 552  ILE A CD1 1 
ATOM   4151  N  N   . TYR A 1 544 ? 24.823  39.289  3.268   1.00 31.21  ? 553  TYR A N   1 
ATOM   4152  C  CA  . TYR A 1 544 ? 23.555  38.597  3.128   1.00 30.02  ? 553  TYR A CA  1 
ATOM   4153  C  C   . TYR A 1 544 ? 22.726  39.250  2.104   1.00 30.46  ? 553  TYR A C   1 
ATOM   4154  O  O   . TYR A 1 544 ? 22.695  40.498  2.048   1.00 27.45  ? 553  TYR A O   1 
ATOM   4155  C  CB  . TYR A 1 544 ? 22.786  38.637  4.455   1.00 32.12  ? 553  TYR A CB  1 
ATOM   4156  C  CG  . TYR A 1 544 ? 23.431  37.720  5.450   1.00 32.76  ? 553  TYR A CG  1 
ATOM   4157  C  CD1 . TYR A 1 544 ? 24.410  38.178  6.304   1.00 35.67  ? 553  TYR A CD1 1 
ATOM   4158  C  CD2 . TYR A 1 544 ? 23.113  36.357  5.481   1.00 31.29  ? 553  TYR A CD2 1 
ATOM   4159  C  CE1 . TYR A 1 544 ? 25.072  37.321  7.164   1.00 46.88  ? 553  TYR A CE1 1 
ATOM   4160  C  CE2 . TYR A 1 544 ? 23.773  35.494  6.331   1.00 34.57  ? 553  TYR A CE2 1 
ATOM   4161  C  CZ  . TYR A 1 544 ? 24.755  35.978  7.170   1.00 44.12  ? 553  TYR A CZ  1 
ATOM   4162  O  OH  . TYR A 1 544 ? 25.452  35.138  7.997   1.00 52.89  ? 553  TYR A OH  1 
ATOM   4163  N  N   . TYR A 1 545 ? 22.007  38.483  1.292   1.00 26.54  ? 554  TYR A N   1 
ATOM   4164  C  CA  . TYR A 1 545 ? 21.150  39.109  0.306   1.00 25.55  ? 554  TYR A CA  1 
ATOM   4165  C  C   . TYR A 1 545 ? 19.774  38.379  0.339   1.00 27.68  ? 554  TYR A C   1 
ATOM   4166  O  O   . TYR A 1 545 ? 19.661  37.443  1.110   1.00 28.43  ? 554  TYR A O   1 
ATOM   4167  C  CB  . TYR A 1 545 ? 21.815  39.099  -1.101  1.00 28.08  ? 554  TYR A CB  1 
ATOM   4168  C  CG  . TYR A 1 545 ? 22.064  37.698  -1.630  1.00 31.18  ? 554  TYR A CG  1 
ATOM   4169  C  CD1 . TYR A 1 545 ? 23.138  36.933  -1.165  1.00 33.53  ? 554  TYR A CD1 1 
ATOM   4170  C  CD2 . TYR A 1 545 ? 21.216  37.132  -2.573  1.00 38.33  ? 554  TYR A CD2 1 
ATOM   4171  C  CE1 . TYR A 1 545 ? 23.345  35.630  -1.625  1.00 37.93  ? 554  TYR A CE1 1 
ATOM   4172  C  CE2 . TYR A 1 545 ? 21.426  35.838  -3.048  1.00 41.35  ? 554  TYR A CE2 1 
ATOM   4173  C  CZ  . TYR A 1 545 ? 22.486  35.093  -2.570  1.00 43.69  ? 554  TYR A CZ  1 
ATOM   4174  O  OH  . TYR A 1 545 ? 22.669  33.819  -3.067  1.00 49.06  ? 554  TYR A OH  1 
ATOM   4175  N  N   . LYS A 1 546 ? 18.773  38.809  -0.433  1.00 27.58  ? 555  LYS A N   1 
ATOM   4176  C  CA  . LYS A 1 546 ? 17.436  38.217  -0.299  1.00 28.59  ? 555  LYS A CA  1 
ATOM   4177  C  C   . LYS A 1 546 ? 17.382  36.791  -0.917  1.00 35.97  ? 555  LYS A C   1 
ATOM   4178  O  O   . LYS A 1 546 ? 17.888  36.572  -2.022  1.00 34.94  ? 555  LYS A O   1 
ATOM   4179  C  CB  . LYS A 1 546 ? 16.419  39.101  -0.977  1.00 27.98  ? 555  LYS A CB  1 
ATOM   4180  C  CG  . LYS A 1 546 ? 16.221  40.461  -0.345  1.00 25.78  ? 555  LYS A CG  1 
ATOM   4181  C  CD  . LYS A 1 546 ? 15.117  41.170  -1.020  1.00 30.35  ? 555  LYS A CD  1 
ATOM   4182  C  CE  . LYS A 1 546 ? 14.803  42.465  -0.361  1.00 33.86  ? 555  LYS A CE  1 
ATOM   4183  N  NZ  . LYS A 1 546 ? 13.579  43.131  -0.959  1.00 35.15  ? 555  LYS A NZ  1 
ATOM   4184  N  N   . VAL A 1 547 ? 16.776  35.841  -0.200  1.00 40.35  ? 556  VAL A N   1 
ATOM   4185  C  CA  . VAL A 1 547 ? 16.701  34.460  -0.677  1.00 40.82  ? 556  VAL A CA  1 
ATOM   4186  C  C   . VAL A 1 547 ? 16.020  34.396  -2.041  1.00 40.69  ? 556  VAL A C   1 
ATOM   4187  O  O   . VAL A 1 547 ? 16.430  33.597  -2.855  1.00 43.68  ? 556  VAL A O   1 
ATOM   4188  C  CB  . VAL A 1 547 ? 15.974  33.601  0.405   1.00 43.56  ? 556  VAL A CB  1 
ATOM   4189  C  CG1 . VAL A 1 547 ? 14.497  33.954  0.449   1.00 43.59  ? 556  VAL A CG1 1 
ATOM   4190  C  CG2 . VAL A 1 547 ? 16.185  32.110  0.119   1.00 47.41  ? 556  VAL A CG2 1 
ATOM   4191  N  N   . LYS A 1 548 ? 15.023  35.232  -2.313  1.00 40.94  ? 557  LYS A N   1 
ATOM   4192  C  CA  . LYS A 1 548 ? 14.334  35.225  -3.595  1.00 42.77  ? 557  LYS A CA  1 
ATOM   4193  C  C   . LYS A 1 548 ? 15.292  35.386  -4.792  1.00 44.30  ? 557  LYS A C   1 
ATOM   4194  O  O   . LYS A 1 548 ? 14.949  34.995  -5.909  1.00 42.50  ? 557  LYS A O   1 
ATOM   4195  C  CB  . LYS A 1 548 ? 13.285  36.340  -3.627  1.00 44.04  ? 557  LYS A CB  1 
ATOM   4196  C  CG  . LYS A 1 548 ? 13.814  37.698  -4.080  1.00 48.26  ? 557  LYS A CG  1 
ATOM   4197  C  CD  . LYS A 1 548 ? 12.714  38.727  -4.126  1.00 50.53  ? 557  LYS A CD  1 
ATOM   4198  C  CE  . LYS A 1 548 ? 13.178  39.967  -4.844  1.00 57.04  ? 557  LYS A CE  1 
ATOM   4199  N  NZ  . LYS A 1 548 ? 12.108  40.981  -4.906  1.00 57.33  ? 557  LYS A NZ  1 
ATOM   4200  N  N   . ASP A 1 549 ? 16.488  35.977  -4.567  1.00 43.70  ? 558  ASP A N   1 
ATOM   4201  C  CA  . ASP A 1 549 ? 17.494  36.200  -5.628  1.00 44.65  ? 558  ASP A CA  1 
ATOM   4202  C  C   . ASP A 1 549 ? 18.609  35.155  -5.525  1.00 42.09  ? 558  ASP A C   1 
ATOM   4203  O  O   . ASP A 1 549 ? 19.676  35.355  -6.102  1.00 41.29  ? 558  ASP A O   1 
ATOM   4204  C  CB  . ASP A 1 549 ? 18.126  37.629  -5.492  1.00 43.19  ? 558  ASP A CB  1 
ATOM   4205  C  CG  . ASP A 1 549 ? 17.146  38.767  -5.730  1.00 46.48  ? 558  ASP A CG  1 
ATOM   4206  O  OD1 . ASP A 1 549 ? 16.129  38.541  -6.386  1.00 47.18  ? 558  ASP A OD1 1 
ATOM   4207  O  OD2 . ASP A 1 549 ? 17.411  39.913  -5.245  1.00 44.64  ? 558  ASP A OD2 1 
ATOM   4208  N  N   . LYS A 1 550 ? 18.385  34.034  -4.794  1.00 43.46  ? 559  LYS A N   1 
ATOM   4209  C  CA  . LYS A 1 550 ? 19.444  33.022  -4.629  1.00 44.80  ? 559  LYS A CA  1 
ATOM   4210  C  C   . LYS A 1 550 ? 20.029  32.527  -5.974  1.00 46.30  ? 559  LYS A C   1 
ATOM   4211  O  O   . LYS A 1 550 ? 21.203  32.139  -6.045  1.00 44.62  ? 559  LYS A O   1 
ATOM   4212  C  CB  . LYS A 1 550 ? 18.927  31.792  -3.848  1.00 46.75  ? 559  LYS A CB  1 
ATOM   4213  C  CG  . LYS A 1 550 ? 20.109  30.954  -3.292  1.00 49.68  ? 559  LYS A CG  1 
ATOM   4214  C  CD  . LYS A 1 550 ? 19.699  30.035  -2.120  1.00 53.24  ? 559  LYS A CD  1 
ATOM   4215  C  CE  . LYS A 1 550 ? 20.872  29.761  -1.213  0.00 0.00   ? 559  LYS A CE  1 
ATOM   4216  N  NZ  . LYS A 1 550 ? 20.424  29.423  0.163   0.00 0.00   ? 559  LYS A NZ  1 
ATOM   4217  N  N   . ASN A 1 551 ? 19.224  32.550  -7.024  1.00 45.91  ? 560  ASN A N   1 
ATOM   4218  C  CA  . ASN A 1 551 ? 19.700  32.070  -8.298  1.00 49.13  ? 560  ASN A CA  1 
ATOM   4219  C  C   . ASN A 1 551 ? 19.830  33.226  -9.301  1.00 50.55  ? 560  ASN A C   1 
ATOM   4220  O  O   . ASN A 1 551 ? 19.853  33.004  -10.515 1.00 48.91  ? 560  ASN A O   1 
ATOM   4221  C  CB  . ASN A 1 551 ? 18.726  30.980  -8.781  1.00 51.84  ? 560  ASN A CB  1 
ATOM   4222  C  CG  . ASN A 1 551 ? 19.370  30.058  -9.778  1.00 57.30  ? 560  ASN A CG  1 
ATOM   4223  O  OD1 . ASN A 1 551 ? 18.959  30.044  -10.948 1.00 60.74  ? 560  ASN A OD1 1 
ATOM   4224  N  ND2 . ASN A 1 551 ? 20.399  29.303  -9.418  1.00 55.81  ? 560  ASN A ND2 1 
ATOM   4225  N  N   . GLY A 1 552 ? 19.911  34.486  -8.767  1.00 48.69  ? 561  GLY A N   1 
ATOM   4226  C  CA  . GLY A 1 552 ? 20.042  35.684  -9.586  1.00 44.70  ? 561  GLY A CA  1 
ATOM   4227  C  C   . GLY A 1 552 ? 19.039  36.789  -9.262  1.00 45.66  ? 561  GLY A C   1 
ATOM   4228  O  O   . GLY A 1 552 ? 17.847  36.526  -9.110  1.00 42.92  ? 561  GLY A O   1 
ATOM   4229  N  N   . GLY A 1 553 ? 19.529  38.078  -9.161  1.00 42.06  ? 562  GLY A N   1 
ATOM   4230  C  CA  . GLY A 1 553 ? 18.658  39.237  -8.894  1.00 38.51  ? 562  GLY A CA  1 
ATOM   4231  C  C   . GLY A 1 553 ? 19.495  40.414  -8.378  1.00 34.56  ? 562  GLY A C   1 
ATOM   4232  O  O   . GLY A 1 553 ? 20.676  40.243  -8.066  1.00 32.55  ? 562  GLY A O   1 
ATOM   4233  N  N   . THR A 1 554 ? 18.883  41.600  -8.301  1.00 36.50  ? 563  THR A N   1 
ATOM   4234  C  CA  . THR A 1 554 ? 19.565  42.819  -7.864  1.00 37.51  ? 563  THR A CA  1 
ATOM   4235  C  C   . THR A 1 554 ? 20.354  42.623  -6.575  1.00 33.17  ? 563  THR A C   1 
ATOM   4236  O  O   . THR A 1 554 ? 21.496  43.046  -6.538  1.00 29.67  ? 563  THR A O   1 
ATOM   4237  C  CB  . THR A 1 554 ? 18.536  43.953  -7.687  1.00 41.90  ? 563  THR A CB  1 
ATOM   4238  O  OG1 . THR A 1 554 ? 17.814  44.104  -8.920  1.00 43.97  ? 563  THR A OG1 1 
ATOM   4239  C  CG2 . THR A 1 554 ? 19.200  45.313  -7.340  1.00 42.38  ? 563  THR A CG2 1 
ATOM   4240  N  N   . THR A 1 555 ? 19.799  41.956  -5.531  1.00 30.41  ? 564  THR A N   1 
ATOM   4241  C  CA  . THR A 1 555 ? 20.560  41.865  -4.272  1.00 29.42  ? 564  THR A CA  1 
ATOM   4242  C  C   . THR A 1 555 ? 21.684  40.913  -4.358  1.00 26.62  ? 564  THR A C   1 
ATOM   4243  O  O   . THR A 1 555 ? 22.680  41.044  -3.657  1.00 25.02  ? 564  THR A O   1 
ATOM   4244  C  CB  . THR A 1 555 ? 19.624  41.559  -3.050  1.00 27.10  ? 564  THR A CB  1 
ATOM   4245  O  OG1 . THR A 1 555 ? 19.184  40.196  -3.092  1.00 28.94  ? 564  THR A OG1 1 
ATOM   4246  C  CG2 . THR A 1 555 ? 18.411  42.445  -3.058  1.00 28.16  ? 564  THR A CG2 1 
ATOM   4247  N  N   . LYS A 1 556 ? 21.574  39.906  -5.215  1.00 30.72  ? 565  LYS A N   1 
ATOM   4248  C  CA  . LYS A 1 556 ? 22.726  39.005  -5.375  1.00 31.34  ? 565  LYS A CA  1 
ATOM   4249  C  C   . LYS A 1 556 ? 23.882  39.761  -6.140  1.00 26.92  ? 565  LYS A C   1 
ATOM   4250  O  O   . LYS A 1 556 ? 25.046  39.584  -5.824  1.00 27.08  ? 565  LYS A O   1 
ATOM   4251  C  CB  . LYS A 1 556 ? 22.297  37.750  -6.215  1.00 33.37  ? 565  LYS A CB  1 
ATOM   4252  C  CG  . LYS A 1 556 ? 23.396  36.709  -6.190  1.00 35.24  ? 565  LYS A CG  1 
ATOM   4253  C  CD  . LYS A 1 556 ? 22.995  35.468  -7.043  1.00 44.34  ? 565  LYS A CD  1 
ATOM   4254  C  CE  . LYS A 1 556 ? 23.924  34.300  -6.695  1.00 49.05  ? 565  LYS A CE  1 
ATOM   4255  N  NZ  . LYS A 1 556 ? 23.437  33.052  -7.341  1.00 49.98  ? 565  LYS A NZ  1 
ATOM   4256  N  N   . THR A 1 557 ? 23.528  40.547  -7.163  1.00 30.08  ? 566  THR A N   1 
ATOM   4257  C  CA  . THR A 1 557 ? 24.540  41.302  -7.910  1.00 29.59  ? 566  THR A CA  1 
ATOM   4258  C  C   . THR A 1 557 ? 25.185  42.333  -6.949  1.00 29.47  ? 566  THR A C   1 
ATOM   4259  O  O   . THR A 1 557 ? 26.417  42.481  -6.920  1.00 31.22  ? 566  THR A O   1 
ATOM   4260  C  CB  . THR A 1 557 ? 23.884  42.013  -9.082  1.00 34.84  ? 566  THR A CB  1 
ATOM   4261  O  OG1 . THR A 1 557 ? 23.325  41.006  -9.962  1.00 34.50  ? 566  THR A OG1 1 
ATOM   4262  C  CG2 . THR A 1 557 ? 24.873  42.872  -9.856  1.00 32.41  ? 566  THR A CG2 1 
ATOM   4263  N  N   . ALA A 1 558 ? 24.340  43.014  -6.178  1.00 29.84  ? 567  ALA A N   1 
ATOM   4264  C  CA  . ALA A 1 558 ? 24.819  44.029  -5.207  1.00 28.01  ? 567  ALA A CA  1 
ATOM   4265  C  C   . ALA A 1 558 ? 25.777  43.374  -4.253  1.00 24.39  ? 567  ALA A C   1 
ATOM   4266  O  O   . ALA A 1 558 ? 26.880  43.861  -4.053  1.00 27.87  ? 567  ALA A O   1 
ATOM   4267  C  CB  . ALA A 1 558 ? 23.619  44.608  -4.446  1.00 29.42  ? 567  ALA A CB  1 
ATOM   4268  N  N   . ALA A 1 559 ? 25.425  42.215  -3.668  1.00 26.22  ? 568  ALA A N   1 
ATOM   4269  C  CA  . ALA A 1 559 ? 26.330  41.601  -2.687  1.00 23.24  ? 568  ALA A CA  1 
ATOM   4270  C  C   . ALA A 1 559 ? 27.647  41.141  -3.308  1.00 27.75  ? 568  ALA A C   1 
ATOM   4271  O  O   . ALA A 1 559 ? 28.709  41.223  -2.678  1.00 25.63  ? 568  ALA A O   1 
ATOM   4272  C  CB  . ALA A 1 559 ? 25.608  40.391  -2.002  1.00 26.55  ? 568  ALA A CB  1 
ATOM   4273  N  N   . SER A 1 560 ? 27.586  40.628  -4.585  1.00 29.08  ? 569  SER A N   1 
ATOM   4274  C  CA  . SER A 1 560 ? 28.810  40.162  -5.280  1.00 30.24  ? 569  SER A CA  1 
ATOM   4275  C  C   . SER A 1 560 ? 29.729  41.347  -5.579  1.00 28.33  ? 569  SER A C   1 
ATOM   4276  O  O   . SER A 1 560 ? 30.929  41.258  -5.299  1.00 26.39  ? 569  SER A O   1 
ATOM   4277  C  CB  . SER A 1 560 ? 28.466  39.489  -6.611  1.00 34.74  ? 569  SER A CB  1 
ATOM   4278  O  OG  . SER A 1 560 ? 27.425  38.554  -6.353  1.00 39.79  ? 569  SER A OG  1 
ATOM   4279  N  N   . ASN A 1 561 ? 29.148  42.454  -6.104  1.00 28.84  ? 570  ASN A N   1 
ATOM   4280  C  CA  . ASN A 1 561 ? 29.952  43.671  -6.400  1.00 23.45  ? 570  ASN A CA  1 
ATOM   4281  C  C   . ASN A 1 561 ? 30.627  44.201  -5.151  1.00 25.31  ? 570  ASN A C   1 
ATOM   4282  O  O   . ASN A 1 561 ? 31.830  44.462  -5.159  1.00 26.83  ? 570  ASN A O   1 
ATOM   4283  C  CB  . ASN A 1 561 ? 29.055  44.740  -6.984  1.00 25.46  ? 570  ASN A CB  1 
ATOM   4284  C  CG  . ASN A 1 561 ? 28.614  44.443  -8.373  1.00 28.67  ? 570  ASN A CG  1 
ATOM   4285  O  OD1 . ASN A 1 561 ? 29.295  43.649  -9.015  1.00 33.39  ? 570  ASN A OD1 1 
ATOM   4286  N  ND2 . ASN A 1 561 ? 27.508  45.002  -8.882  1.00 28.76  ? 570  ASN A ND2 1 
ATOM   4287  N  N   . ILE A 1 562 ? 29.872  44.367  -4.026  1.00 25.54  ? 571  ILE A N   1 
ATOM   4288  C  CA  . ILE A 1 562 ? 30.494  44.934  -2.780  1.00 24.22  ? 571  ILE A CA  1 
ATOM   4289  C  C   . ILE A 1 562 ? 31.527  44.028  -2.232  1.00 21.17  ? 571  ILE A C   1 
ATOM   4290  O  O   . ILE A 1 562 ? 32.608  44.462  -1.804  1.00 23.93  ? 571  ILE A O   1 
ATOM   4291  C  CB  . ILE A 1 562 ? 29.342  45.207  -1.734  1.00 24.61  ? 571  ILE A CB  1 
ATOM   4292  C  CG1 . ILE A 1 562 ? 28.430  46.325  -2.294  1.00 22.75  ? 571  ILE A CG1 1 
ATOM   4293  C  CG2 . ILE A 1 562 ? 29.951  45.553  -0.351  1.00 20.83  ? 571  ILE A CG2 1 
ATOM   4294  C  CD1 . ILE A 1 562 ? 27.065  46.426  -1.609  1.00 24.65  ? 571  ILE A CD1 1 
ATOM   4295  N  N   . LEU A 1 563 ? 31.255  42.729  -2.218  1.00 21.83  ? 572  LEU A N   1 
ATOM   4296  C  CA  . LEU A 1 563 ? 32.252  41.790  -1.686  1.00 23.93  ? 572  LEU A CA  1 
ATOM   4297  C  C   . LEU A 1 563 ? 33.560  41.893  -2.530  1.00 24.58  ? 572  LEU A C   1 
ATOM   4298  O  O   . LEU A 1 563 ? 34.655  41.929  -2.014  1.00 24.79  ? 572  LEU A O   1 
ATOM   4299  C  CB  . LEU A 1 563 ? 31.614  40.341  -1.818  1.00 27.31  ? 572  LEU A CB  1 
ATOM   4300  C  CG  . LEU A 1 563 ? 32.569  39.227  -1.386  1.00 28.20  ? 572  LEU A CG  1 
ATOM   4301  C  CD1 . LEU A 1 563 ? 32.924  39.318  0.083   1.00 29.25  ? 572  LEU A CD1 1 
ATOM   4302  C  CD2 . LEU A 1 563 ? 31.884  37.888  -1.633  1.00 32.75  ? 572  LEU A CD2 1 
ATOM   4303  N  N   . LYS A 1 564 ? 33.398  41.925  -3.866  1.00 27.17  ? 573  LYS A N   1 
ATOM   4304  C  CA  . LYS A 1 564 ? 34.572  42.071  -4.752  1.00 26.97  ? 573  LYS A CA  1 
ATOM   4305  C  C   . LYS A 1 564 ? 35.326  43.366  -4.373  1.00 28.47  ? 573  LYS A C   1 
ATOM   4306  O  O   . LYS A 1 564 ? 36.537  43.322  -4.130  1.00 31.58  ? 573  LYS A O   1 
ATOM   4307  C  CB  . LYS A 1 564 ? 34.069  42.170  -6.206  1.00 32.82  ? 573  LYS A CB  1 
ATOM   4308  C  CG  . LYS A 1 564 ? 35.190  42.328  -7.230  1.00 45.07  ? 573  LYS A CG  1 
ATOM   4309  C  CD  . LYS A 1 564 ? 34.657  42.237  -8.675  1.00 55.76  ? 573  LYS A CD  1 
ATOM   4310  C  CE  . LYS A 1 564 ? 35.735  41.663  -9.653  1.00 61.77  ? 573  LYS A CE  1 
ATOM   4311  N  NZ  . LYS A 1 564 ? 35.630  42.248  -11.039 1.00 54.92  ? 573  LYS A NZ  1 
ATOM   4312  N  N   . ARG A 1 565 ? 34.597  44.526  -4.279  1.00 25.51  ? 574  ARG A N   1 
ATOM   4313  C  CA  . ARG A 1 565 ? 35.349  45.786  -3.979  1.00 24.39  ? 574  ARG A CA  1 
ATOM   4314  C  C   . ARG A 1 565 ? 36.032  45.760  -2.628  1.00 23.50  ? 574  ARG A C   1 
ATOM   4315  O  O   . ARG A 1 565 ? 37.147  46.247  -2.501  1.00 26.02  ? 574  ARG A O   1 
ATOM   4316  C  CB  . ARG A 1 565 ? 34.422  46.979  -4.108  1.00 23.83  ? 574  ARG A CB  1 
ATOM   4317  C  CG  . ARG A 1 565 ? 33.894  47.151  -5.553  1.00 23.45  ? 574  ARG A CG  1 
ATOM   4318  C  CD  . ARG A 1 565 ? 35.052  47.267  -6.590  1.00 26.61  ? 574  ARG A CD  1 
ATOM   4319  N  NE  . ARG A 1 565 ? 34.468  47.814  -7.808  1.00 33.79  ? 574  ARG A NE  1 
ATOM   4320  C  CZ  . ARG A 1 565 ? 35.179  48.297  -8.819  1.00 28.82  ? 574  ARG A CZ  1 
ATOM   4321  N  NH1 . ARG A 1 565 ? 34.567  48.811  -9.873  1.00 28.98  ? 574  ARG A NH1 1 
ATOM   4322  N  NH2 . ARG A 1 565 ? 36.502  48.252  -8.788  1.00 24.59  ? 574  ARG A NH2 1 
ATOM   4323  N  N   . ILE A 1 566 ? 35.389  45.173  -1.598  1.00 26.65  ? 575  ILE A N   1 
ATOM   4324  C  CA  . ILE A 1 566 ? 36.039  45.154  -0.304  1.00 21.29  ? 575  ILE A CA  1 
ATOM   4325  C  C   . ILE A 1 566 ? 37.334  44.370  -0.385  1.00 27.20  ? 575  ILE A C   1 
ATOM   4326  O  O   . ILE A 1 566 ? 38.394  44.797  0.108   1.00 27.34  ? 575  ILE A O   1 
ATOM   4327  C  CB  . ILE A 1 566 ? 35.097  44.507  0.749   1.00 25.45  ? 575  ILE A CB  1 
ATOM   4328  C  CG1 . ILE A 1 566 ? 33.904  45.462  1.005   1.00 24.61  ? 575  ILE A CG1 1 
ATOM   4329  C  CG2 . ILE A 1 566 ? 35.895  44.212  2.068   1.00 22.07  ? 575  ILE A CG2 1 
ATOM   4330  C  CD1 . ILE A 1 566 ? 32.897  44.832  1.995   1.00 26.11  ? 575  ILE A CD1 1 
ATOM   4331  N  N   . LEU A 1 567 ? 37.239  43.180  -1.018  1.00 30.38  ? 576  LEU A N   1 
ATOM   4332  C  CA  . LEU A 1 567 ? 38.399  42.311  -1.125  1.00 33.51  ? 576  LEU A CA  1 
ATOM   4333  C  C   . LEU A 1 567 ? 39.504  42.957  -1.982  1.00 35.94  ? 576  LEU A C   1 
ATOM   4334  O  O   . LEU A 1 567 ? 40.652  42.588  -1.804  1.00 38.70  ? 576  LEU A O   1 
ATOM   4335  C  CB  . LEU A 1 567 ? 37.942  40.956  -1.659  1.00 33.79  ? 576  LEU A CB  1 
ATOM   4336  C  CG  . LEU A 1 567 ? 37.106  40.157  -0.593  1.00 34.18  ? 576  LEU A CG  1 
ATOM   4337  C  CD1 . LEU A 1 567 ? 36.400  38.946  -1.213  1.00 31.78  ? 576  LEU A CD1 1 
ATOM   4338  C  CD2 . LEU A 1 567 ? 38.053  39.698  0.514   1.00 36.34  ? 576  LEU A CD2 1 
ATOM   4339  N  N   . GLU A 1 568 ? 39.178  43.922  -2.877  1.00 35.92  ? 577  GLU A N   1 
ATOM   4340  C  CA  . GLU A 1 568 ? 40.227  44.601  -3.665  1.00 37.83  ? 577  GLU A CA  1 
ATOM   4341  C  C   . GLU A 1 568 ? 41.170  45.393  -2.745  1.00 40.69  ? 577  GLU A C   1 
ATOM   4342  O  O   . GLU A 1 568 ? 42.302  45.635  -3.151  1.00 40.41  ? 577  GLU A O   1 
ATOM   4343  C  CB  . GLU A 1 568 ? 39.583  45.547  -4.754  1.00 38.47  ? 577  GLU A CB  1 
ATOM   4344  C  CG  . GLU A 1 568 ? 38.934  44.713  -5.858  1.00 45.45  ? 577  GLU A CG  1 
ATOM   4345  C  CD  . GLU A 1 568 ? 38.331  45.530  -7.020  1.00 51.88  ? 577  GLU A CD  1 
ATOM   4346  O  OE1 . GLU A 1 568 ? 38.306  46.780  -6.954  1.00 41.40  ? 577  GLU A OE1 1 
ATOM   4347  O  OE2 . GLU A 1 568 ? 37.876  44.876  -8.024  1.00 49.11  ? 577  GLU A OE2 1 
ATOM   4348  N  N   . LYS A 1 569 ? 40.757  45.788  -1.496  1.00 38.72  ? 578  LYS A N   1 
ATOM   4349  C  CA  . LYS A 1 569 ? 41.637  46.592  -0.608  1.00 34.89  ? 578  LYS A CA  1 
ATOM   4350  C  C   . LYS A 1 569 ? 41.909  45.941  0.694   1.00 32.90  ? 578  LYS A C   1 
ATOM   4351  O  O   . LYS A 1 569 ? 42.695  46.450  1.469   1.00 33.93  ? 578  LYS A O   1 
ATOM   4352  C  CB  . LYS A 1 569 ? 41.014  47.959  -0.226  1.00 36.22  ? 578  LYS A CB  1 
ATOM   4353  C  CG  . LYS A 1 569 ? 40.652  48.809  -1.397  1.00 44.34  ? 578  LYS A CG  1 
ATOM   4354  C  CD  . LYS A 1 569 ? 41.856  49.493  -1.981  1.00 54.96  ? 578  LYS A CD  1 
ATOM   4355  C  CE  . LYS A 1 569 ? 41.690  49.445  -3.474  1.00 61.98  ? 578  LYS A CE  1 
ATOM   4356  N  NZ  . LYS A 1 569 ? 42.571  50.413  -4.163  1.00 68.28  ? 578  LYS A NZ  1 
ATOM   4357  N  N   . PHE A 1 570 ? 41.248  44.845  0.964   1.00 34.85  ? 579  PHE A N   1 
ATOM   4358  C  CA  . PHE A 1 570 ? 41.403  44.184  2.239   1.00 35.20  ? 579  PHE A CA  1 
ATOM   4359  C  C   . PHE A 1 570 ? 41.682  42.691  2.050   1.00 38.21  ? 579  PHE A C   1 
ATOM   4360  O  O   . PHE A 1 570 ? 40.809  42.003  1.508   1.00 39.20  ? 579  PHE A O   1 
ATOM   4361  C  CB  . PHE A 1 570 ? 40.071  44.353  3.054   1.00 36.61  ? 579  PHE A CB  1 
ATOM   4362  C  CG  . PHE A 1 570 ? 39.863  45.781  3.504   1.00 35.09  ? 579  PHE A CG  1 
ATOM   4363  C  CD1 . PHE A 1 570 ? 40.497  46.268  4.633   1.00 33.54  ? 579  PHE A CD1 1 
ATOM   4364  C  CD2 . PHE A 1 570 ? 39.076  46.643  2.776   1.00 32.43  ? 579  PHE A CD2 1 
ATOM   4365  C  CE1 . PHE A 1 570 ? 40.347  47.599  5.015   1.00 32.05  ? 579  PHE A CE1 1 
ATOM   4366  C  CE2 . PHE A 1 570 ? 38.927  47.982  3.167   1.00 28.33  ? 579  PHE A CE2 1 
ATOM   4367  C  CZ  . PHE A 1 570 ? 39.570  48.437  4.285   1.00 27.73  ? 579  PHE A CZ  1 
ATOM   4368  N  N   . ASN A 1 571 ? 42.837  42.180  2.505   1.00 42.38  ? 580  ASN A N   1 
ATOM   4369  C  CA  . ASN A 1 571 ? 43.096  40.751  2.335   1.00 51.44  ? 580  ASN A CA  1 
ATOM   4370  C  C   . ASN A 1 571 ? 42.489  39.972  3.495   1.00 53.46  ? 580  ASN A C   1 
ATOM   4371  O  O   . ASN A 1 571 ? 43.216  39.513  4.367   1.00 51.84  ? 580  ASN A O   1 
ATOM   4372  C  CB  . ASN A 1 571 ? 44.620  40.432  2.260   1.00 55.67  ? 580  ASN A CB  1 
ATOM   4373  C  CG  . ASN A 1 571 ? 44.879  39.040  1.671   1.00 57.91  ? 580  ASN A CG  1 
ATOM   4374  O  OD1 . ASN A 1 571 ? 45.498  38.942  0.609   0.00 0.00   ? 580  ASN A OD1 1 
ATOM   4375  N  ND2 . ASN A 1 571 ? 44.464  37.938  2.292   0.00 0.00   ? 580  ASN A ND2 1 
ATOM   4376  N  N   . MET A 1 572 ? 41.157  39.834  3.502   1.00 50.14  ? 581  MET A N   1 
ATOM   4377  C  CA  . MET A 1 572 ? 40.421  39.094  4.533   1.00 51.10  ? 581  MET A CA  1 
ATOM   4378  C  C   . MET A 1 572 ? 39.814  37.860  3.916   1.00 50.10  ? 581  MET A C   1 
ATOM   4379  O  O   . MET A 1 572 ? 39.658  37.803  2.694   1.00 49.33  ? 581  MET A O   1 
ATOM   4380  C  CB  . MET A 1 572 ? 39.270  39.939  5.104   1.00 51.31  ? 581  MET A CB  1 
ATOM   4381  C  CG  . MET A 1 572 ? 39.733  41.098  5.939   1.00 54.39  ? 581  MET A CG  1 
ATOM   4382  S  SD  . MET A 1 572 ? 38.293  42.073  6.475   1.00 54.95  ? 581  MET A SD  1 
ATOM   4383  C  CE  . MET A 1 572 ? 39.104  43.689  7.011   1.00 53.89  ? 581  MET A CE  1 
ATOM   4384  N  N   . LYS A 1 573 ? 39.450  36.880  4.719   1.00 47.22  ? 582  LYS A N   1 
ATOM   4385  C  CA  . LYS A 1 573 ? 38.854  35.702  4.141   1.00 46.31  ? 582  LYS A CA  1 
ATOM   4386  C  C   . LYS A 1 573 ? 37.531  36.035  3.447   1.00 47.75  ? 582  LYS A C   1 
ATOM   4387  O  O   . LYS A 1 573 ? 36.687  36.784  3.971   1.00 46.60  ? 582  LYS A O   1 
ATOM   4388  C  CB  . LYS A 1 573 ? 38.629  34.632  5.216   1.00 47.97  ? 582  LYS A CB  1 
ATOM   4389  C  CG  . LYS A 1 573 ? 37.912  33.383  4.663   1.00 53.78  ? 582  LYS A CG  1 
ATOM   4390  C  CD  . LYS A 1 573 ? 37.961  32.231  5.674   1.00 58.36  ? 582  LYS A CD  1 
ATOM   4391  C  CE  . LYS A 1 573 ? 37.496  32.672  7.040   1.00 61.79  ? 582  LYS A CE  1 
ATOM   4392  N  NZ  . LYS A 1 573 ? 37.647  31.587  8.045   1.00 60.88  ? 582  LYS A NZ  1 
ATOM   4393  N  N   . ASN A 1 574 ? 37.349  35.467  2.257   1.00 44.76  ? 583  ASN A N   1 
ATOM   4394  C  CA  . ASN A 1 574 ? 36.140  35.679  1.501   1.00 42.45  ? 583  ASN A CA  1 
ATOM   4395  C  C   . ASN A 1 574 ? 35.118  34.644  1.968   1.00 44.34  ? 583  ASN A C   1 
ATOM   4396  O  O   . ASN A 1 574 ? 35.190  33.480  1.554   1.00 42.48  ? 583  ASN A O   1 
ATOM   4397  C  CB  . ASN A 1 574 ? 36.438  35.544  0.004   1.00 41.93  ? 583  ASN A CB  1 
ATOM   4398  C  CG  . ASN A 1 574 ? 35.213  35.585  -0.853  1.00 44.60  ? 583  ASN A CG  1 
ATOM   4399  O  OD1 . ASN A 1 574 ? 34.080  35.558  -0.349  1.00 43.89  ? 583  ASN A OD1 1 
ATOM   4400  N  ND2 . ASN A 1 574 ? 35.328  35.693  -2.167  1.00 47.82  ? 583  ASN A ND2 1 
ATOM   4401  N  N   . ARG A 1 575 ? 34.164  35.043  2.843   1.00 39.98  ? 584  ARG A N   1 
ATOM   4402  C  CA  . ARG A 1 575 ? 33.171  34.093  3.312   1.00 35.52  ? 584  ARG A CA  1 
ATOM   4403  C  C   . ARG A 1 575 ? 32.004  33.986  2.352   1.00 37.70  ? 584  ARG A C   1 
ATOM   4404  O  O   . ARG A 1 575 ? 31.095  33.185  2.565   1.00 38.08  ? 584  ARG A O   1 
ATOM   4405  C  CB  . ARG A 1 575 ? 32.728  34.457  4.733   1.00 39.00  ? 584  ARG A CB  1 
ATOM   4406  C  CG  . ARG A 1 575 ? 33.940  34.757  5.659   1.00 34.61  ? 584  ARG A CG  1 
ATOM   4407  C  CD  . ARG A 1 575 ? 33.498  35.382  7.004   1.00 38.84  ? 584  ARG A CD  1 
ATOM   4408  N  NE  . ARG A 1 575 ? 32.434  34.589  7.625   1.00 44.55  ? 584  ARG A NE  1 
ATOM   4409  C  CZ  . ARG A 1 575 ? 32.641  33.711  8.600   1.00 48.91  ? 584  ARG A CZ  1 
ATOM   4410  N  NH1 . ARG A 1 575 ? 33.866  33.526  9.089   1.00 45.14  ? 584  ARG A NH1 1 
ATOM   4411  N  NH2 . ARG A 1 575 ? 31.630  33.001  9.085   1.00 44.68  ? 584  ARG A NH2 1 
ATOM   4412  N  N   . GLY A 1 576 ? 32.010  34.777  1.282   1.00 35.57  ? 585  GLY A N   1 
ATOM   4413  C  CA  . GLY A 1 576 ? 30.976  34.657  0.269   1.00 34.46  ? 585  GLY A CA  1 
ATOM   4414  C  C   . GLY A 1 576 ? 29.727  35.443  0.576   1.00 33.22  ? 585  GLY A C   1 
ATOM   4415  O  O   . GLY A 1 576 ? 29.656  36.081  1.617   1.00 32.49  ? 585  GLY A O   1 
ATOM   4416  N  N   . ILE A 1 577 ? 28.755  35.399  -0.348  1.00 29.79  ? 586  ILE A N   1 
ATOM   4417  C  CA  . ILE A 1 577 ? 27.476  36.047  -0.186  1.00 31.60  ? 586  ILE A CA  1 
ATOM   4418  C  C   . ILE A 1 577 ? 26.559  34.936  0.385   1.00 39.76  ? 586  ILE A C   1 
ATOM   4419  O  O   . ILE A 1 577 ? 26.720  33.765  0.001   1.00 39.99  ? 586  ILE A O   1 
ATOM   4420  C  CB  . ILE A 1 577 ? 27.022  36.642  -1.518  1.00 37.57  ? 586  ILE A CB  1 
ATOM   4421  C  CG1 . ILE A 1 577 ? 26.933  35.591  -2.635  1.00 34.08  ? 586  ILE A CG1 1 
ATOM   4422  C  CG2 . ILE A 1 577 ? 28.051  37.707  -1.937  1.00 33.06  ? 586  ILE A CG2 1 
ATOM   4423  C  CD1 . ILE A 1 577 ? 26.134  36.100  -3.827  1.00 36.51  ? 586  ILE A CD1 1 
ATOM   4424  N  N   . LYS A 1 578 ? 25.635  35.262  1.280   1.00 37.70  ? 587  LYS A N   1 
ATOM   4425  C  CA  . LYS A 1 578 ? 24.815  34.246  1.930   1.00 35.85  ? 587  LYS A CA  1 
ATOM   4426  C  C   . LYS A 1 578 ? 23.350  34.585  2.028   1.00 38.05  ? 587  LYS A C   1 
ATOM   4427  O  O   . LYS A 1 578 ? 22.969  35.761  1.944   1.00 36.44  ? 587  LYS A O   1 
ATOM   4428  C  CB  . LYS A 1 578 ? 25.301  34.100  3.330   1.00 34.85  ? 587  LYS A CB  1 
ATOM   4429  C  CG  . LYS A 1 578 ? 26.702  33.655  3.491   1.00 41.23  ? 587  LYS A CG  1 
ATOM   4430  C  CD  . LYS A 1 578 ? 26.963  33.533  4.955   1.00 45.30  ? 587  LYS A CD  1 
ATOM   4431  C  CE  . LYS A 1 578 ? 28.104  32.610  5.261   1.00 53.06  ? 587  LYS A CE  1 
ATOM   4432  N  NZ  . LYS A 1 578 ? 29.389  33.178  4.824   1.00 65.32  ? 587  LYS A NZ  1 
ATOM   4433  N  N   . THR A 1 579 ? 22.481  33.558  2.145   1.00 38.10  ? 588  THR A N   1 
ATOM   4434  C  CA  . THR A 1 579 ? 21.083  33.823  2.389   1.00 38.07  ? 588  THR A CA  1 
ATOM   4435  C  C   . THR A 1 579 ? 20.794  33.086  3.707   1.00 41.94  ? 588  THR A C   1 
ATOM   4436  O  O   . THR A 1 579 ? 21.550  32.200  4.115   1.00 40.64  ? 588  THR A O   1 
ATOM   4437  C  CB  . THR A 1 579 ? 20.138  33.413  1.289   1.00 43.38  ? 588  THR A CB  1 
ATOM   4438  O  OG1 . THR A 1 579 ? 20.191  31.993  1.118   1.00 44.19  ? 588  THR A OG1 1 
ATOM   4439  C  CG2 . THR A 1 579 ? 20.442  34.075  0.010   1.00 43.41  ? 588  THR A CG2 1 
ATOM   4440  N  N   . ARG A 1 580 ? 19.729  33.482  4.390   1.00 42.40  ? 589  ARG A N   1 
ATOM   4441  C  CA  . ARG A 1 580 ? 19.367  32.867  5.652   1.00 41.55  ? 589  ARG A CA  1 
ATOM   4442  C  C   . ARG A 1 580 ? 17.863  33.040  5.798   1.00 40.11  ? 589  ARG A C   1 
ATOM   4443  O  O   . ARG A 1 580 ? 17.319  34.115  5.541   1.00 36.37  ? 589  ARG A O   1 
ATOM   4444  C  CB  . ARG A 1 580 ? 20.152  33.486  6.773   1.00 39.79  ? 589  ARG A CB  1 
ATOM   4445  C  CG  . ARG A 1 580 ? 20.068  32.649  8.020   1.00 42.97  ? 589  ARG A CG  1 
ATOM   4446  C  CD  . ARG A 1 580 ? 20.418  33.455  9.248   1.00 51.02  ? 589  ARG A CD  1 
ATOM   4447  N  NE  . ARG A 1 580 ? 19.820  32.840  10.434  1.00 56.87  ? 589  ARG A NE  1 
ATOM   4448  C  CZ  . ARG A 1 580 ? 20.305  32.984  11.658  1.00 55.17  ? 589  ARG A CZ  1 
ATOM   4449  N  NH1 . ARG A 1 580 ? 21.394  33.715  11.865  1.00 55.38  ? 589  ARG A NH1 1 
ATOM   4450  N  NH2 . ARG A 1 580 ? 19.700  32.405  12.690  1.00 58.81  ? 589  ARG A NH2 1 
ATOM   4451  N  N   . THR A 1 581 ? 17.170  31.948  6.181   1.00 37.85  ? 590  THR A N   1 
ATOM   4452  C  CA  . THR A 1 581 ? 15.713  32.011  6.259   1.00 40.03  ? 590  THR A CA  1 
ATOM   4453  C  C   . THR A 1 581 ? 15.148  31.585  7.605   1.00 40.77  ? 590  THR A C   1 
ATOM   4454  O  O   . THR A 1 581 ? 15.831  30.982  8.441   1.00 38.83  ? 590  THR A O   1 
ATOM   4455  C  CB  . THR A 1 581 ? 15.090  31.082  5.199   1.00 43.88  ? 590  THR A CB  1 
ATOM   4456  O  OG1 . THR A 1 581 ? 15.633  29.769  5.436   1.00 42.88  ? 590  THR A OG1 1 
ATOM   4457  C  CG2 . THR A 1 581 ? 15.391  31.532  3.775   1.00 41.49  ? 590  THR A CG2 1 
ATOM   4458  N  N   . LEU A 1 582 ? 13.899  31.966  7.816   1.00 41.57  ? 591  LEU A N   1 
ATOM   4459  C  CA  . LEU A 1 582 ? 13.126  31.557  8.999   1.00 41.71  ? 591  LEU A CA  1 
ATOM   4460  C  C   . LEU A 1 582 ? 12.469  30.214  8.562   1.00 43.91  ? 591  LEU A C   1 
ATOM   4461  O  O   . LEU A 1 582 ? 12.416  29.927  7.359   1.00 44.22  ? 591  LEU A O   1 
ATOM   4462  C  CB  . LEU A 1 582 ? 11.969  32.564  9.275   1.00 38.95  ? 591  LEU A CB  1 
ATOM   4463  C  CG  . LEU A 1 582 ? 12.363  34.065  9.418   1.00 29.40  ? 591  LEU A CG  1 
ATOM   4464  C  CD1 . LEU A 1 582 ? 11.118  34.935  9.324   1.00 29.71  ? 591  LEU A CD1 1 
ATOM   4465  C  CD2 . LEU A 1 582 ? 13.026  34.245  10.759  1.00 28.55  ? 591  LEU A CD2 1 
ATOM   4466  N  N   . ASP A 1 583 ? 11.908  29.439  9.497   1.00 49.46  ? 592  ASP A N   1 
ATOM   4467  C  CA  . ASP A 1 583 ? 11.194  28.206  9.094   1.00 52.24  ? 592  ASP A CA  1 
ATOM   4468  C  C   . ASP A 1 583 ? 10.142  28.509  8.090   1.00 50.50  ? 592  ASP A C   1 
ATOM   4469  O  O   . ASP A 1 583 ? 9.819   27.651  7.281   1.00 50.48  ? 592  ASP A O   1 
ATOM   4470  C  CB  . ASP A 1 583 ? 10.526  27.545  10.283  1.00 57.05  ? 592  ASP A CB  1 
ATOM   4471  C  CG  . ASP A 1 583 ? 11.526  26.876  11.172  1.00 66.03  ? 592  ASP A CG  1 
ATOM   4472  O  OD1 . ASP A 1 583 ? 11.374  25.664  11.416  1.00 67.51  ? 592  ASP A OD1 1 
ATOM   4473  O  OD2 . ASP A 1 583 ? 12.473  27.569  11.635  1.00 69.10  ? 592  ASP A OD2 1 
ATOM   4474  N  N   . ASN A 1 584 ? 9.587   29.705  8.077   1.00 45.60  ? 593  ASN A N   1 
ATOM   4475  C  CA  . ASN A 1 584 ? 8.565   29.884  7.070   1.00 43.15  ? 593  ASN A CA  1 
ATOM   4476  C  C   . ASN A 1 584 ? 9.082   30.152  5.666   1.00 41.07  ? 593  ASN A C   1 
ATOM   4477  O  O   . ASN A 1 584 ? 8.285   30.450  4.779   1.00 43.07  ? 593  ASN A O   1 
ATOM   4478  C  CB  . ASN A 1 584 ? 7.607   30.970  7.476   1.00 44.91  ? 593  ASN A CB  1 
ATOM   4479  C  CG  . ASN A 1 584 ? 8.203   32.361  7.568   1.00 48.93  ? 593  ASN A CG  1 
ATOM   4480  O  OD1 . ASN A 1 584 ? 9.332   32.605  7.089   1.00 44.87  ? 593  ASN A OD1 1 
ATOM   4481  N  ND2 . ASN A 1 584 ? 7.494   33.313  8.161   1.00 47.91  ? 593  ASN A ND2 1 
ATOM   4482  N  N   . GLY A 1 585 ? 10.390  30.084  5.440   1.00 42.55  ? 594  GLY A N   1 
ATOM   4483  C  CA  . GLY A 1 585 ? 10.885  30.297  4.090   1.00 43.65  ? 594  GLY A CA  1 
ATOM   4484  C  C   . GLY A 1 585 ? 11.344  31.713  3.761   1.00 46.14  ? 594  GLY A C   1 
ATOM   4485  O  O   . GLY A 1 585 ? 12.106  31.897  2.799   1.00 43.81  ? 594  GLY A O   1 
ATOM   4486  N  N   . LYS A 1 586 ? 10.894  32.727  4.550   1.00 42.48  ? 595  LYS A N   1 
ATOM   4487  C  CA  . LYS A 1 586 ? 11.257  34.135  4.304   1.00 38.66  ? 595  LYS A CA  1 
ATOM   4488  C  C   . LYS A 1 586 ? 12.629  34.449  4.870   1.00 32.96  ? 595  LYS A C   1 
ATOM   4489  O  O   . LYS A 1 586 ? 13.171  33.678  5.635   1.00 30.71  ? 595  LYS A O   1 
ATOM   4490  C  CB  . LYS A 1 586 ? 10.163  35.041  4.887   1.00 39.51  ? 595  LYS A CB  1 
ATOM   4491  C  CG  . LYS A 1 586 ? 8.787   34.614  4.354   1.00 49.22  ? 595  LYS A CG  1 
ATOM   4492  C  CD  . LYS A 1 586 ? 7.898   35.759  3.915   1.00 57.81  ? 595  LYS A CD  1 
ATOM   4493  C  CE  . LYS A 1 586 ? 6.464   35.548  4.399   1.00 68.27  ? 595  LYS A CE  1 
ATOM   4494  N  NZ  . LYS A 1 586 ? 5.624   36.770  4.197   1.00 73.03  ? 595  LYS A NZ  1 
ATOM   4495  N  N   . ASP A 1 587 ? 13.226  35.601  4.456   1.00 29.73  ? 596  ASP A N   1 
ATOM   4496  C  CA  . ASP A 1 587 ? 14.551  36.002  4.946   1.00 26.07  ? 596  ASP A CA  1 
ATOM   4497  C  C   . ASP A 1 587 ? 14.529  36.197  6.445   1.00 23.73  ? 596  ASP A C   1 
ATOM   4498  O  O   . ASP A 1 587 ? 13.544  36.727  6.989   1.00 28.05  ? 596  ASP A O   1 
ATOM   4499  C  CB  . ASP A 1 587 ? 14.967  37.354  4.302   1.00 24.45  ? 596  ASP A CB  1 
ATOM   4500  C  CG  . ASP A 1 587 ? 15.230  37.172  2.812   1.00 24.54  ? 596  ASP A CG  1 
ATOM   4501  O  OD1 . ASP A 1 587 ? 16.147  36.451  2.480   1.00 30.40  ? 596  ASP A OD1 1 
ATOM   4502  O  OD2 . ASP A 1 587 ? 14.503  37.775  2.002   1.00 31.15  ? 596  ASP A OD2 1 
ATOM   4503  N  N   . TYR A 1 588 ? 15.555  35.767  7.067   1.00 26.24  ? 597  TYR A N   1 
ATOM   4504  C  CA  . TYR A 1 588 ? 15.700  35.880  8.516   1.00 24.08  ? 597  TYR A CA  1 
ATOM   4505  C  C   . TYR A 1 588 ? 15.859  37.359  8.959   1.00 26.40  ? 597  TYR A C   1 
ATOM   4506  O  O   . TYR A 1 588 ? 15.265  37.778  9.953   1.00 26.02  ? 597  TYR A O   1 
ATOM   4507  C  CB  . TYR A 1 588 ? 16.934  35.121  8.856   1.00 25.28  ? 597  TYR A CB  1 
ATOM   4508  C  CG  . TYR A 1 588 ? 17.362  35.277  10.291  1.00 29.00  ? 597  TYR A CG  1 
ATOM   4509  C  CD1 . TYR A 1 588 ? 18.412  36.112  10.634  1.00 28.49  ? 597  TYR A CD1 1 
ATOM   4510  C  CD2 . TYR A 1 588 ? 16.726  34.577  11.306  1.00 31.98  ? 597  TYR A CD2 1 
ATOM   4511  C  CE1 . TYR A 1 588 ? 18.829  36.238  11.953  1.00 28.91  ? 597  TYR A CE1 1 
ATOM   4512  C  CE2 . TYR A 1 588 ? 17.131  34.700  12.622  1.00 28.15  ? 597  TYR A CE2 1 
ATOM   4513  C  CZ  . TYR A 1 588 ? 18.185  35.527  12.944  1.00 34.58  ? 597  TYR A CZ  1 
ATOM   4514  O  OH  . TYR A 1 588 ? 18.605  35.623  14.246  1.00 38.56  ? 597  TYR A OH  1 
ATOM   4515  N  N   . LEU A 1 589 ? 16.697  38.122  8.236   1.00 27.62  ? 598  LEU A N   1 
ATOM   4516  C  CA  . LEU A 1 589 ? 16.961  39.521  8.609   1.00 24.01  ? 598  LEU A CA  1 
ATOM   4517  C  C   . LEU A 1 589 ? 15.782  40.398  8.316   1.00 22.39  ? 598  LEU A C   1 
ATOM   4518  O  O   . LEU A 1 589 ? 15.282  40.493  7.188   1.00 24.62  ? 598  LEU A O   1 
ATOM   4519  C  CB  . LEU A 1 589 ? 18.221  40.024  7.818   1.00 24.86  ? 598  LEU A CB  1 
ATOM   4520  C  CG  . LEU A 1 589 ? 19.482  39.358  8.244   1.00 25.33  ? 598  LEU A CG  1 
ATOM   4521  C  CD1 . LEU A 1 589 ? 20.568  39.655  7.186   1.00 31.05  ? 598  LEU A CD1 1 
ATOM   4522  C  CD2 . LEU A 1 589 ? 19.959  39.845  9.619   1.00 23.41  ? 598  LEU A CD2 1 
ATOM   4523  N  N   . TYR A 1 590 ? 15.322  41.086  9.345   1.00 22.58  ? 599  TYR A N   1 
ATOM   4524  C  CA  . TYR A 1 590 ? 14.193  42.011  9.223   1.00 22.46  ? 599  TYR A CA  1 
ATOM   4525  C  C   . TYR A 1 590 ? 14.380  43.003  8.085   1.00 23.84  ? 599  TYR A C   1 
ATOM   4526  O  O   . TYR A 1 590 ? 13.444  43.242  7.296   1.00 24.41  ? 599  TYR A O   1 
ATOM   4527  C  CB  . TYR A 1 590 ? 14.046  42.791  10.572  1.00 23.53  ? 599  TYR A CB  1 
ATOM   4528  C  CG  . TYR A 1 590 ? 12.751  43.566  10.677  1.00 26.57  ? 599  TYR A CG  1 
ATOM   4529  C  CD1 . TYR A 1 590 ? 12.534  44.708  9.911   1.00 25.03  ? 599  TYR A CD1 1 
ATOM   4530  C  CD2 . TYR A 1 590 ? 11.728  43.139  11.526  1.00 25.38  ? 599  TYR A CD2 1 
ATOM   4531  C  CE1 . TYR A 1 590 ? 11.339  45.404  9.981   1.00 27.43  ? 599  TYR A CE1 1 
ATOM   4532  C  CE2 . TYR A 1 590 ? 10.523  43.828  11.599  1.00 25.81  ? 599  TYR A CE2 1 
ATOM   4533  C  CZ  . TYR A 1 590 ? 10.334  44.963  10.824  1.00 32.07  ? 599  TYR A CZ  1 
ATOM   4534  O  OH  . TYR A 1 590 ? 9.152   45.658  10.866  1.00 30.69  ? 599  TYR A OH  1 
ATOM   4535  N  N   . VAL A 1 591 ? 15.610  43.584  7.948   1.00 24.66  ? 600  VAL A N   1 
ATOM   4536  C  CA  . VAL A 1 591 ? 15.700  44.664  6.890   1.00 21.98  ? 600  VAL A CA  1 
ATOM   4537  C  C   . VAL A 1 591 ? 15.678  44.094  5.486   1.00 25.97  ? 600  VAL A C   1 
ATOM   4538  O  O   . VAL A 1 591 ? 15.539  44.862  4.520   1.00 26.83  ? 600  VAL A O   1 
ATOM   4539  C  CB  . VAL A 1 591 ? 16.934  45.572  7.112   1.00 22.55  ? 600  VAL A CB  1 
ATOM   4540  C  CG1 . VAL A 1 591 ? 16.793  46.267  8.481   1.00 20.87  ? 600  VAL A CG1 1 
ATOM   4541  C  CG2 . VAL A 1 591 ? 18.237  44.769  7.066   1.00 22.30  ? 600  VAL A CG2 1 
ATOM   4542  N  N   . LEU A 1 592 ? 15.814  42.757  5.368   1.00 25.96  ? 601  LEU A N   1 
ATOM   4543  C  CA  . LEU A 1 592 ? 15.715  42.129  4.046   1.00 27.74  ? 601  LEU A CA  1 
ATOM   4544  C  C   . LEU A 1 592 ? 14.252  41.686  3.832   1.00 29.18  ? 601  LEU A C   1 
ATOM   4545  O  O   . LEU A 1 592 ? 13.613  42.042  2.858   1.00 31.02  ? 601  LEU A O   1 
ATOM   4546  C  CB  . LEU A 1 592 ? 16.664  40.903  3.985   1.00 27.67  ? 601  LEU A CB  1 
ATOM   4547  C  CG  . LEU A 1 592 ? 18.022  41.185  3.348   1.00 32.19  ? 601  LEU A CG  1 
ATOM   4548  C  CD1 . LEU A 1 592 ? 18.724  42.319  4.060   1.00 30.40  ? 601  LEU A CD1 1 
ATOM   4549  C  CD2 . LEU A 1 592 ? 18.873  39.953  3.360   1.00 28.62  ? 601  LEU A CD2 1 
ATOM   4550  N  N   . ARG A 1 593 ? 13.712  40.957  4.802   1.00 31.22  ? 602  ARG A N   1 
ATOM   4551  C  CA  . ARG A 1 593 ? 12.359  40.395  4.684   1.00 29.66  ? 602  ARG A CA  1 
ATOM   4552  C  C   . ARG A 1 593 ? 11.302  41.432  4.538   1.00 30.55  ? 602  ARG A C   1 
ATOM   4553  O  O   . ARG A 1 593 ? 10.365  41.253  3.766   1.00 31.83  ? 602  ARG A O   1 
ATOM   4554  C  CB  . ARG A 1 593 ? 12.087  39.515  5.931   1.00 28.81  ? 602  ARG A CB  1 
ATOM   4555  C  CG  . ARG A 1 593 ? 10.649  38.874  5.939   1.00 31.43  ? 602  ARG A CG  1 
ATOM   4556  C  CD  . ARG A 1 593 ? 10.518  37.963  7.191   1.00 31.90  ? 602  ARG A CD  1 
ATOM   4557  N  NE  . ARG A 1 593 ? 10.343  38.770  8.402   1.00 29.58  ? 602  ARG A NE  1 
ATOM   4558  C  CZ  . ARG A 1 593 ? 11.274  39.013  9.322   1.00 26.68  ? 602  ARG A CZ  1 
ATOM   4559  N  NH1 . ARG A 1 593 ? 12.490  38.480  9.209   1.00 24.86  ? 602  ARG A NH1 1 
ATOM   4560  N  NH2 . ARG A 1 593 ? 11.010  39.827  10.341  1.00 22.53  ? 602  ARG A NH2 1 
ATOM   4561  N  N   . ASN A 1 594 ? 11.424  42.548  5.239   1.00 30.18  ? 603  ASN A N   1 
ATOM   4562  C  CA  . ASN A 1 594 ? 10.365  43.544  5.191   1.00 29.77  ? 603  ASN A CA  1 
ATOM   4563  C  C   . ASN A 1 594 ? 10.632  44.731  4.292   1.00 31.56  ? 603  ASN A C   1 
ATOM   4564  O  O   . ASN A 1 594 ? 9.897   45.718  4.314   1.00 29.58  ? 603  ASN A O   1 
ATOM   4565  C  CB  . ASN A 1 594 ? 10.119  44.058  6.629   1.00 31.83  ? 603  ASN A CB  1 
ATOM   4566  C  CG  . ASN A 1 594 ? 9.427   43.005  7.432   1.00 35.14  ? 603  ASN A CG  1 
ATOM   4567  O  OD1 . ASN A 1 594 ? 8.491   42.396  6.910   1.00 37.10  ? 603  ASN A OD1 1 
ATOM   4568  N  ND2 . ASN A 1 594 ? 9.854   42.672  8.645   1.00 35.15  ? 603  ASN A ND2 1 
ATOM   4569  N  N   . ASN A 1 595 ? 11.672  44.655  3.520   1.00 32.46  ? 604  ASN A N   1 
ATOM   4570  C  CA  . ASN A 1 595 ? 11.993  45.756  2.604   1.00 34.26  ? 604  ASN A CA  1 
ATOM   4571  C  C   . ASN A 1 595 ? 11.309  45.522  1.219   1.00 35.97  ? 604  ASN A C   1 
ATOM   4572  O  O   . ASN A 1 595 ? 11.506  44.456  0.641   1.00 35.98  ? 604  ASN A O   1 
ATOM   4573  C  CB  . ASN A 1 595 ? 13.513  45.761  2.399   1.00 33.10  ? 604  ASN A CB  1 
ATOM   4574  C  CG  . ASN A 1 595 ? 14.063  47.136  2.238   1.00 36.39  ? 604  ASN A CG  1 
ATOM   4575  O  OD1 . ASN A 1 595 ? 13.521  47.929  1.446   1.00 29.94  ? 604  ASN A OD1 1 
ATOM   4576  N  ND2 . ASN A 1 595 ? 15.118  47.479  2.966   1.00 30.72  ? 604  ASN A ND2 1 
ATOM   4577  N  N   . ASN A 1 596 ? 10.568  46.490  0.690   1.00 33.76  ? 605  ASN A N   1 
ATOM   4578  C  CA  . ASN A 1 596 ? 9.956   46.297  -0.636  1.00 37.05  ? 605  ASN A CA  1 
ATOM   4579  C  C   . ASN A 1 596 ? 10.977  46.628  -1.725  1.00 37.74  ? 605  ASN A C   1 
ATOM   4580  O  O   . ASN A 1 596 ? 10.640  46.554  -2.900  1.00 38.12  ? 605  ASN A O   1 
ATOM   4581  C  CB  . ASN A 1 596 ? 8.775   47.212  -0.805  1.00 39.30  ? 605  ASN A CB  1 
ATOM   4582  C  CG  . ASN A 1 596 ? 7.681   46.882  0.160   1.00 45.43  ? 605  ASN A CG  1 
ATOM   4583  O  OD1 . ASN A 1 596 ? 6.961   47.787  0.590   1.00 48.19  ? 605  ASN A OD1 1 
ATOM   4584  N  ND2 . ASN A 1 596 ? 7.490   45.634  0.537   1.00 46.37  ? 605  ASN A ND2 1 
ATOM   4585  N  N   . TYR A 1 597 ? 12.225  47.014  -1.340  1.00 34.07  ? 606  TYR A N   1 
ATOM   4586  C  CA  . TYR A 1 597 ? 13.246  47.382  -2.312  1.00 29.58  ? 606  TYR A CA  1 
ATOM   4587  C  C   . TYR A 1 597 ? 14.448  46.518  -2.149  1.00 28.25  ? 606  TYR A C   1 
ATOM   4588  O  O   . TYR A 1 597 ? 14.593  45.844  -1.120  1.00 29.27  ? 606  TYR A O   1 
ATOM   4589  C  CB  . TYR A 1 597 ? 13.563  48.896  -2.181  1.00 30.42  ? 606  TYR A CB  1 
ATOM   4590  C  CG  . TYR A 1 597 ? 12.294  49.636  -2.503  1.00 32.31  ? 606  TYR A CG  1 
ATOM   4591  C  CD1 . TYR A 1 597 ? 11.946  49.909  -3.822  1.00 37.48  ? 606  TYR A CD1 1 
ATOM   4592  C  CD2 . TYR A 1 597 ? 11.372  49.923  -1.519  1.00 35.00  ? 606  TYR A CD2 1 
ATOM   4593  C  CE1 . TYR A 1 597 ? 10.701  50.429  -4.146  1.00 43.49  ? 606  TYR A CE1 1 
ATOM   4594  C  CE2 . TYR A 1 597 ? 10.117  50.444  -1.832  1.00 43.63  ? 606  TYR A CE2 1 
ATOM   4595  C  CZ  . TYR A 1 597 ? 9.789   50.695  -3.150  1.00 48.81  ? 606  TYR A CZ  1 
ATOM   4596  O  OH  . TYR A 1 597 ? 8.555   51.213  -3.469  1.00 53.42  ? 606  TYR A OH  1 
ATOM   4597  N  N   . PRO A 1 598 ? 15.332  46.468  -3.147  1.00 28.63  ? 607  PRO A N   1 
ATOM   4598  C  CA  . PRO A 1 598 ? 16.530  45.624  -3.038  1.00 28.66  ? 607  PRO A CA  1 
ATOM   4599  C  C   . PRO A 1 598 ? 17.352  46.010  -1.761  1.00 30.24  ? 607  PRO A C   1 
ATOM   4600  O  O   . PRO A 1 598 ? 17.623  47.181  -1.542  1.00 29.36  ? 607  PRO A O   1 
ATOM   4601  C  CB  . PRO A 1 598 ? 17.290  45.919  -4.342  1.00 29.00  ? 607  PRO A CB  1 
ATOM   4602  C  CG  . PRO A 1 598 ? 16.341  46.550  -5.214  1.00 28.14  ? 607  PRO A CG  1 
ATOM   4603  C  CD  . PRO A 1 598 ? 15.411  47.341  -4.322  1.00 30.28  ? 607  PRO A CD  1 
ATOM   4604  N  N   . ALA A 1 599 ? 17.765  45.006  -0.985  1.00 29.33  ? 608  ALA A N   1 
ATOM   4605  C  CA  . ALA A 1 599 ? 18.434  45.213  0.292   1.00 29.68  ? 608  ALA A CA  1 
ATOM   4606  C  C   . ALA A 1 599 ? 19.425  44.165  0.582   1.00 27.50  ? 608  ALA A C   1 
ATOM   4607  O  O   . ALA A 1 599 ? 19.187  43.008  0.257   1.00 26.99  ? 608  ALA A O   1 
ATOM   4608  C  CB  . ALA A 1 599 ? 17.379  45.207  1.416   1.00 26.62  ? 608  ALA A CB  1 
ATOM   4609  N  N   . ILE A 1 600 ? 20.559  44.525  1.175   1.00 24.53  ? 609  ILE A N   1 
ATOM   4610  C  CA  . ILE A 1 600 ? 21.590  43.582  1.557   1.00 20.66  ? 609  ILE A CA  1 
ATOM   4611  C  C   . ILE A 1 600 ? 22.118  44.016  2.891   1.00 23.59  ? 609  ILE A C   1 
ATOM   4612  O  O   . ILE A 1 600 ? 21.889  45.168  3.321   1.00 22.90  ? 609  ILE A O   1 
ATOM   4613  C  CB  . ILE A 1 600 ? 22.794  43.532  0.603   1.00 24.85  ? 609  ILE A CB  1 
ATOM   4614  C  CG1 . ILE A 1 600 ? 23.373  44.991  0.450   1.00 28.14  ? 609  ILE A CG1 1 
ATOM   4615  C  CG2 . ILE A 1 600 ? 22.339  42.985  -0.812  1.00 22.94  ? 609  ILE A CG2 1 
ATOM   4616  C  CD1 . ILE A 1 600 ? 24.684  44.996  -0.260  1.00 28.91  ? 609  ILE A CD1 1 
ATOM   4617  N  N   . LEU A 1 601 ? 22.855  43.132  3.537   1.00 22.75  ? 610  LEU A N   1 
ATOM   4618  C  CA  . LEU A 1 601 ? 23.467  43.443  4.798   1.00 22.83  ? 610  LEU A CA  1 
ATOM   4619  C  C   . LEU A 1 601 ? 24.892  43.003  4.746   1.00 24.12  ? 610  LEU A C   1 
ATOM   4620  O  O   . LEU A 1 601 ? 25.209  41.824  4.601   1.00 24.72  ? 610  LEU A O   1 
ATOM   4621  C  CB  . LEU A 1 601 ? 22.743  42.817  5.996   1.00 23.99  ? 610  LEU A CB  1 
ATOM   4622  C  CG  . LEU A 1 601 ? 23.277  43.168  7.396   1.00 24.04  ? 610  LEU A CG  1 
ATOM   4623  C  CD1 . LEU A 1 601 ? 22.127  43.119  8.382   1.00 25.69  ? 610  LEU A CD1 1 
ATOM   4624  C  CD2 . LEU A 1 601 ? 24.377  42.258  7.886   1.00 26.00  ? 610  LEU A CD2 1 
ATOM   4625  N  N   . VAL A 1 602 ? 25.790  43.970  4.868   1.00 21.87  ? 611  VAL A N   1 
ATOM   4626  C  CA  . VAL A 1 602 ? 27.213  43.742  4.801   1.00 21.31  ? 611  VAL A CA  1 
ATOM   4627  C  C   . VAL A 1 602 ? 27.795  43.525  6.156   1.00 25.27  ? 611  VAL A C   1 
ATOM   4628  O  O   . VAL A 1 602 ? 27.608  44.364  7.025   1.00 25.17  ? 611  VAL A O   1 
ATOM   4629  C  CB  . VAL A 1 602 ? 27.921  44.983  4.169   1.00 20.27  ? 611  VAL A CB  1 
ATOM   4630  C  CG1 . VAL A 1 602 ? 29.434  44.760  4.069   1.00 19.82  ? 611  VAL A CG1 1 
ATOM   4631  C  CG2 . VAL A 1 602 ? 27.311  45.289  2.790   1.00 22.22  ? 611  VAL A CG2 1 
ATOM   4632  N  N   . GLU A 1 603 ? 28.517  42.378  6.367   1.00 25.61  ? 612  GLU A N   1 
ATOM   4633  C  CA  . GLU A 1 603 ? 29.240  42.159  7.620   1.00 26.11  ? 612  GLU A CA  1 
ATOM   4634  C  C   . GLU A 1 603 ? 30.664  42.426  7.211   1.00 29.45  ? 612  GLU A C   1 
ATOM   4635  O  O   . GLU A 1 603 ? 31.358  41.493  6.736   1.00 26.55  ? 612  GLU A O   1 
ATOM   4636  C  CB  . GLU A 1 603 ? 29.089  40.717  8.107   1.00 27.86  ? 612  GLU A CB  1 
ATOM   4637  C  CG  . GLU A 1 603 ? 27.638  40.441  8.454   1.00 32.35  ? 612  GLU A CG  1 
ATOM   4638  C  CD  . GLU A 1 603 ? 27.321  40.862  9.897   1.00 37.74  ? 612  GLU A CD  1 
ATOM   4639  O  OE1 . GLU A 1 603 ? 28.176  41.471  10.549  1.00 38.72  ? 612  GLU A OE1 1 
ATOM   4640  O  OE2 . GLU A 1 603 ? 26.212  40.573  10.359  1.00 43.27  ? 612  GLU A OE2 1 
ATOM   4641  N  N   . CYS A 1 604 ? 31.124  43.696  7.352   1.00 27.32  ? 613  CYS A N   1 
ATOM   4642  C  CA  . CYS A 1 604 ? 32.443  44.136  6.878   1.00 26.35  ? 613  CYS A CA  1 
ATOM   4643  C  C   . CYS A 1 604 ? 33.621  43.288  7.267   1.00 29.33  ? 613  CYS A C   1 
ATOM   4644  O  O   . CYS A 1 604 ? 34.525  43.065  6.467   1.00 30.47  ? 613  CYS A O   1 
ATOM   4645  C  CB  . CYS A 1 604 ? 32.699  45.570  7.348   1.00 25.43  ? 613  CYS A CB  1 
ATOM   4646  S  SG  . CYS A 1 604 ? 31.381  46.711  6.860   1.00 27.03  ? 613  CYS A SG  1 
ATOM   4647  N  N   . ALA A 1 605 ? 33.639  42.882  8.544   1.00 30.43  ? 614  ALA A N   1 
ATOM   4648  C  CA  . ALA A 1 605 ? 34.754  42.149  9.117   1.00 30.17  ? 614  ALA A CA  1 
ATOM   4649  C  C   . ALA A 1 605 ? 34.309  41.682  10.513  1.00 31.85  ? 614  ALA A C   1 
ATOM   4650  O  O   . ALA A 1 605 ? 33.235  42.094  10.983  1.00 29.65  ? 614  ALA A O   1 
ATOM   4651  C  CB  . ALA A 1 605 ? 35.938  43.091  9.262   1.00 29.95  ? 614  ALA A CB  1 
ATOM   4652  N  N   . PHE A 1 606 ? 35.111  40.803  11.156  1.00 32.74  ? 615  PHE A N   1 
ATOM   4653  C  CA  . PHE A 1 606 ? 34.809  40.321  12.507  1.00 33.89  ? 615  PHE A CA  1 
ATOM   4654  C  C   . PHE A 1 606 ? 35.457  41.296  13.400  1.00 33.60  ? 615  PHE A C   1 
ATOM   4655  O  O   . PHE A 1 606 ? 36.677  41.416  13.385  1.00 34.03  ? 615  PHE A O   1 
ATOM   4656  C  CB  . PHE A 1 606 ? 35.364  38.890  12.757  1.00 34.49  ? 615  PHE A CB  1 
ATOM   4657  C  CG  . PHE A 1 606 ? 34.401  37.840  12.253  1.00 35.68  ? 615  PHE A CG  1 
ATOM   4658  C  CD1 . PHE A 1 606 ? 34.159  37.692  10.895  1.00 35.47  ? 615  PHE A CD1 1 
ATOM   4659  C  CD2 . PHE A 1 606 ? 33.675  37.061  13.139  1.00 35.20  ? 615  PHE A CD2 1 
ATOM   4660  C  CE1 . PHE A 1 606 ? 33.213  36.791  10.435  1.00 38.24  ? 615  PHE A CE1 1 
ATOM   4661  C  CE2 . PHE A 1 606 ? 32.725  36.160  12.670  1.00 33.95  ? 615  PHE A CE2 1 
ATOM   4662  C  CZ  . PHE A 1 606 ? 32.501  36.034  11.320  1.00 38.09  ? 615  PHE A CZ  1 
ATOM   4663  N  N   . ILE A 1 607 ? 34.642  42.020  14.200  1.00 34.26  ? 616  ILE A N   1 
ATOM   4664  C  CA  . ILE A 1 607 ? 35.163  43.066  15.098  1.00 34.70  ? 616  ILE A CA  1 
ATOM   4665  C  C   . ILE A 1 607 ? 35.968  42.475  16.293  1.00 34.34  ? 616  ILE A C   1 
ATOM   4666  O  O   . ILE A 1 607 ? 36.674  43.229  16.972  1.00 33.84  ? 616  ILE A O   1 
ATOM   4667  C  CB  . ILE A 1 607 ? 33.966  43.955  15.603  1.00 34.99  ? 616  ILE A CB  1 
ATOM   4668  C  CG1 . ILE A 1 607 ? 34.497  45.357  15.972  1.00 35.07  ? 616  ILE A CG1 1 
ATOM   4669  C  CG2 . ILE A 1 607 ? 33.239  43.305  16.833  1.00 33.36  ? 616  ILE A CG2 1 
ATOM   4670  C  CD1 . ILE A 1 607 ? 33.346  46.347  16.120  1.00 37.54  ? 616  ILE A CD1 1 
ATOM   4671  N  N   . ASP A 1 608 ? 35.878  41.141  16.506  1.00 34.90  ? 617  ASP A N   1 
ATOM   4672  C  CA  . ASP A 1 608 ? 36.603  40.414  17.573  1.00 34.70  ? 617  ASP A CA  1 
ATOM   4673  C  C   . ASP A 1 608 ? 37.717  39.568  16.938  1.00 38.73  ? 617  ASP A C   1 
ATOM   4674  O  O   . ASP A 1 608 ? 38.249  38.680  17.597  1.00 40.25  ? 617  ASP A O   1 
ATOM   4675  C  CB  . ASP A 1 608 ? 35.647  39.485  18.383  1.00 38.50  ? 617  ASP A CB  1 
ATOM   4676  C  CG  . ASP A 1 608 ? 34.859  38.510  17.494  1.00 45.81  ? 617  ASP A CG  1 
ATOM   4677  O  OD1 . ASP A 1 608 ? 34.180  37.609  18.045  1.00 46.80  ? 617  ASP A OD1 1 
ATOM   4678  O  OD2 . ASP A 1 608 ? 34.921  38.651  16.234  1.00 46.38  ? 617  ASP A OD2 1 
ATOM   4679  N  N   . ASN A 1 609 ? 38.074  39.808  15.660  1.00 40.39  ? 618  ASN A N   1 
ATOM   4680  C  CA  . ASN A 1 609 ? 39.202  39.051  15.071  1.00 42.49  ? 618  ASN A CA  1 
ATOM   4681  C  C   . ASN A 1 609 ? 40.391  40.016  14.871  1.00 42.15  ? 618  ASN A C   1 
ATOM   4682  O  O   . ASN A 1 609 ? 40.278  40.989  14.129  1.00 40.80  ? 618  ASN A O   1 
ATOM   4683  C  CB  . ASN A 1 609 ? 38.834  38.389  13.746  1.00 41.40  ? 618  ASN A CB  1 
ATOM   4684  C  CG  . ASN A 1 609 ? 40.036  37.680  13.160  1.00 48.92  ? 618  ASN A CG  1 
ATOM   4685  O  OD1 . ASN A 1 609 ? 40.805  38.285  12.386  1.00 48.91  ? 618  ASN A OD1 1 
ATOM   4686  N  ND2 . ASN A 1 609 ? 40.287  36.412  13.511  1.00 49.08  ? 618  ASN A ND2 1 
ATOM   4687  N  N   . LYS A 1 610 ? 41.528  39.755  15.532  1.00 40.87  ? 619  LYS A N   1 
ATOM   4688  C  CA  . LYS A 1 610 ? 42.691  40.646  15.442  1.00 40.26  ? 619  LYS A CA  1 
ATOM   4689  C  C   . LYS A 1 610 ? 43.229  40.852  14.028  1.00 41.48  ? 619  LYS A C   1 
ATOM   4690  O  O   . LYS A 1 610 ? 43.603  41.973  13.676  1.00 41.39  ? 619  LYS A O   1 
ATOM   4691  C  CB  . LYS A 1 610 ? 43.829  40.104  16.306  1.00 47.18  ? 619  LYS A CB  1 
ATOM   4692  C  CG  . LYS A 1 610 ? 44.569  41.249  16.987  1.00 56.78  ? 619  LYS A CG  1 
ATOM   4693  C  CD  . LYS A 1 610 ? 46.060  40.992  17.120  1.00 60.72  ? 619  LYS A CD  1 
ATOM   4694  C  CE  . LYS A 1 610 ? 46.707  42.253  17.605  1.00 60.72  ? 619  LYS A CE  1 
ATOM   4695  N  NZ  . LYS A 1 610 ? 47.233  43.029  16.460  1.00 67.20  ? 619  LYS A NZ  1 
ATOM   4696  N  N   . SER A 1 611 ? 43.301  39.800  13.228  1.00 42.63  ? 620  SER A N   1 
ATOM   4697  C  CA  . SER A 1 611 ? 43.814  39.975  11.866  1.00 48.76  ? 620  SER A CA  1 
ATOM   4698  C  C   . SER A 1 611 ? 42.906  40.982  11.035  1.00 47.65  ? 620  SER A C   1 
ATOM   4699  O  O   . SER A 1 611 ? 43.432  41.866  10.362  1.00 45.29  ? 620  SER A O   1 
ATOM   4700  C  CB  . SER A 1 611 ? 43.893  38.620  11.178  1.00 51.49  ? 620  SER A CB  1 
ATOM   4701  O  OG  . SER A 1 611 ? 44.300  38.770  9.825   1.00 55.40  ? 620  SER A OG  1 
ATOM   4702  N  N   . ASP A 1 612 ? 41.559  40.835  11.125  1.00 47.53  ? 621  ASP A N   1 
ATOM   4703  C  CA  . ASP A 1 612 ? 40.587  41.711  10.447  1.00 43.50  ? 621  ASP A CA  1 
ATOM   4704  C  C   . ASP A 1 612 ? 40.706  43.125  10.978  1.00 41.32  ? 621  ASP A C   1 
ATOM   4705  O  O   . ASP A 1 612 ? 40.856  44.061  10.203  1.00 40.29  ? 621  ASP A O   1 
ATOM   4706  C  CB  . ASP A 1 612 ? 39.145  41.205  10.688  1.00 42.01  ? 621  ASP A CB  1 
ATOM   4707  C  CG  . ASP A 1 612 ? 38.738  40.005  9.868   1.00 43.38  ? 621  ASP A CG  1 
ATOM   4708  O  OD1 . ASP A 1 612 ? 37.569  39.572  9.984   1.00 42.65  ? 621  ASP A OD1 1 
ATOM   4709  O  OD2 . ASP A 1 612 ? 39.581  39.498  9.097   1.00 44.19  ? 621  ASP A OD2 1 
ATOM   4710  N  N   . MET A 1 613 ? 40.652  43.291  12.328  1.00 39.04  ? 622  MET A N   1 
ATOM   4711  C  CA  . MET A 1 613 ? 40.705  44.617  12.968  1.00 37.88  ? 622  MET A CA  1 
ATOM   4712  C  C   . MET A 1 613 ? 42.026  45.340  12.771  1.00 37.86  ? 622  MET A C   1 
ATOM   4713  O  O   . MET A 1 613 ? 42.061  46.575  12.788  1.00 35.32  ? 622  MET A O   1 
ATOM   4714  C  CB  . MET A 1 613 ? 40.399  44.481  14.468  1.00 37.91  ? 622  MET A CB  1 
ATOM   4715  C  CG  . MET A 1 613 ? 38.976  44.073  14.682  1.00 41.59  ? 622  MET A CG  1 
ATOM   4716  S  SD  . MET A 1 613 ? 37.904  45.489  14.196  1.00 46.54  ? 622  MET A SD  1 
ATOM   4717  C  CE  . MET A 1 613 ? 37.228  44.869  12.805  1.00 47.90  ? 622  MET A CE  1 
ATOM   4718  N  N   . ASP A 1 614 ? 43.135  44.579  12.584  1.00 39.09  ? 623  ASP A N   1 
ATOM   4719  C  CA  . ASP A 1 614 ? 44.431  45.222  12.315  1.00 41.79  ? 623  ASP A CA  1 
ATOM   4720  C  C   . ASP A 1 614 ? 44.346  46.016  10.942  1.00 41.52  ? 623  ASP A C   1 
ATOM   4721  O  O   . ASP A 1 614 ? 45.068  46.996  10.730  1.00 38.56  ? 623  ASP A O   1 
ATOM   4722  C  CB  . ASP A 1 614 ? 45.547  44.137  12.224  1.00 44.67  ? 623  ASP A CB  1 
ATOM   4723  C  CG  . ASP A 1 614 ? 46.063  43.686  13.587  1.00 54.30  ? 623  ASP A CG  1 
ATOM   4724  O  OD1 . ASP A 1 614 ? 45.698  44.328  14.611  1.00 56.03  ? 623  ASP A OD1 1 
ATOM   4725  O  OD2 . ASP A 1 614 ? 46.826  42.693  13.636  1.00 53.91  ? 623  ASP A OD2 1 
ATOM   4726  N  N   . LYS A 1 615 ? 43.468  45.577  10.029  1.00 38.44  ? 624  LYS A N   1 
ATOM   4727  C  CA  . LYS A 1 615 ? 43.317  46.276  8.757   1.00 42.19  ? 624  LYS A CA  1 
ATOM   4728  C  C   . LYS A 1 615 ? 42.305  47.455  8.893   1.00 40.17  ? 624  LYS A C   1 
ATOM   4729  O  O   . LYS A 1 615 ? 42.068  48.181  7.915   1.00 35.15  ? 624  LYS A O   1 
ATOM   4730  C  CB  . LYS A 1 615 ? 42.841  45.310  7.662   1.00 43.97  ? 624  LYS A CB  1 
ATOM   4731  C  CG  . LYS A 1 615 ? 43.881  44.242  7.310   1.00 47.66  ? 624  LYS A CG  1 
ATOM   4732  C  CD  . LYS A 1 615 ? 43.223  43.062  6.645   1.00 51.50  ? 624  LYS A CD  1 
ATOM   4733  C  CE  . LYS A 1 615 ? 44.205  41.936  6.447   1.00 55.35  ? 624  LYS A CE  1 
ATOM   4734  N  NZ  . LYS A 1 615 ? 44.324  41.115  7.689   1.00 55.00  ? 624  LYS A NZ  1 
ATOM   4735  N  N   . LEU A 1 616 ? 41.720  47.632  10.087  1.00 36.80  ? 625  LEU A N   1 
ATOM   4736  C  CA  . LEU A 1 616 ? 40.752  48.724  10.337  1.00 36.18  ? 625  LEU A CA  1 
ATOM   4737  C  C   . LEU A 1 616 ? 41.111  49.521  11.618  1.00 38.89  ? 625  LEU A C   1 
ATOM   4738  O  O   . LEU A 1 616 ? 40.229  50.079  12.279  1.00 33.93  ? 625  LEU A O   1 
ATOM   4739  C  CB  . LEU A 1 616 ? 39.350  48.126  10.514  1.00 35.46  ? 625  LEU A CB  1 
ATOM   4740  C  CG  . LEU A 1 616 ? 38.848  47.366  9.326   1.00 35.73  ? 625  LEU A CG  1 
ATOM   4741  C  CD1 . LEU A 1 616 ? 37.707  46.429  9.748   1.00 34.10  ? 625  LEU A CD1 1 
ATOM   4742  C  CD2 . LEU A 1 616 ? 38.408  48.364  8.291   1.00 39.27  ? 625  LEU A CD2 1 
ATOM   4743  N  N   . ASN A 1 617 ? 42.396  49.612  11.937  1.00 39.62  ? 626  ASN A N   1 
ATOM   4744  C  CA  . ASN A 1 617 ? 42.773  50.272  13.188  1.00 42.35  ? 626  ASN A CA  1 
ATOM   4745  C  C   . ASN A 1 617 ? 43.097  51.772  13.097  1.00 42.65  ? 626  ASN A C   1 
ATOM   4746  O  O   . ASN A 1 617 ? 43.717  52.290  13.995  1.00 41.89  ? 626  ASN A O   1 
ATOM   4747  C  CB  . ASN A 1 617 ? 43.943  49.514  13.815  1.00 43.48  ? 626  ASN A CB  1 
ATOM   4748  C  CG  . ASN A 1 617 ? 45.182  49.446  12.955  1.00 47.76  ? 626  ASN A CG  1 
ATOM   4749  O  OD1 . ASN A 1 617 ? 45.286  50.129  11.923  1.00 48.49  ? 626  ASN A OD1 1 
ATOM   4750  N  ND2 . ASN A 1 617 ? 46.191  48.650  13.316  1.00 49.70  ? 626  ASN A ND2 1 
ATOM   4751  N  N   . THR A 1 618 ? 42.680  52.476  12.028  1.00 41.95  ? 627  THR A N   1 
ATOM   4752  C  CA  . THR A 1 618 ? 42.851  53.933  11.932  1.00 36.45  ? 627  THR A CA  1 
ATOM   4753  C  C   . THR A 1 618 ? 41.576  54.462  11.240  1.00 35.19  ? 627  THR A C   1 
ATOM   4754  O  O   . THR A 1 618 ? 40.903  53.686  10.556  1.00 30.74  ? 627  THR A O   1 
ATOM   4755  C  CB  . THR A 1 618 ? 44.080  54.322  11.089  1.00 37.11  ? 627  THR A CB  1 
ATOM   4756  O  OG1 . THR A 1 618 ? 43.853  53.860  9.745   1.00 37.35  ? 627  THR A OG1 1 
ATOM   4757  C  CG2 . THR A 1 618 ? 45.378  53.703  11.613  1.00 39.75  ? 627  THR A CG2 1 
ATOM   4758  N  N   . ALA A 1 619 ? 41.267  55.743  11.374  1.00 32.31  ? 628  ALA A N   1 
ATOM   4759  C  CA  . ALA A 1 619 ? 40.058  56.302  10.802  1.00 32.50  ? 628  ALA A CA  1 
ATOM   4760  C  C   . ALA A 1 619 ? 40.207  56.219  9.292   1.00 34.74  ? 628  ALA A C   1 
ATOM   4761  O  O   . ALA A 1 619 ? 39.235  56.019  8.585   1.00 34.73  ? 628  ALA A O   1 
ATOM   4762  C  CB  . ALA A 1 619 ? 39.874  57.763  11.283  1.00 31.44  ? 628  ALA A CB  1 
ATOM   4763  N  N   A GLU A 1 620 ? 41.459  56.322  8.808   0.42 34.01  ? 629  GLU A N   1 
ATOM   4764  N  N   B GLU A 1 620 ? 41.386  56.348  8.776   0.58 33.11  ? 629  GLU A N   1 
ATOM   4765  C  CA  A GLU A 1 620 ? 41.772  56.247  7.379   0.42 33.15  ? 629  GLU A CA  1 
ATOM   4766  C  CA  B GLU A 1 620 ? 41.572  56.329  7.334   0.58 32.59  ? 629  GLU A CA  1 
ATOM   4767  C  C   A GLU A 1 620 ? 41.319  54.899  6.770   0.42 32.56  ? 629  GLU A C   1 
ATOM   4768  C  C   B GLU A 1 620 ? 41.290  54.923  6.747   0.58 33.31  ? 629  GLU A C   1 
ATOM   4769  O  O   A GLU A 1 620 ? 40.634  54.867  5.736   0.42 31.69  ? 629  GLU A O   1 
ATOM   4770  O  O   B GLU A 1 620 ? 40.717  54.821  5.648   0.58 31.87  ? 629  GLU A O   1 
ATOM   4771  C  CB  A GLU A 1 620 ? 43.298  56.416  7.190   0.42 34.01  ? 629  GLU A CB  1 
ATOM   4772  C  CB  B GLU A 1 620 ? 42.990  56.838  7.024   0.58 34.77  ? 629  GLU A CB  1 
ATOM   4773  C  CG  A GLU A 1 620 ? 43.726  56.358  5.737   0.42 37.17  ? 629  GLU A CG  1 
ATOM   4774  C  CG  B GLU A 1 620 ? 43.058  58.345  7.271   0.58 38.27  ? 629  GLU A CG  1 
ATOM   4775  C  CD  A GLU A 1 620 ? 42.987  57.359  4.871   0.42 42.61  ? 629  GLU A CD  1 
ATOM   4776  C  CD  B GLU A 1 620 ? 43.327  58.735  8.747   0.58 41.75  ? 629  GLU A CD  1 
ATOM   4777  O  OE1 A GLU A 1 620 ? 42.579  58.429  5.376   0.42 43.59  ? 629  GLU A OE1 1 
ATOM   4778  O  OE1 B GLU A 1 620 ? 43.223  59.939  9.043   0.58 42.28  ? 629  GLU A OE1 1 
ATOM   4779  O  OE2 A GLU A 1 620 ? 42.819  57.062  3.672   0.42 44.32  ? 629  GLU A OE2 1 
ATOM   4780  O  OE2 B GLU A 1 620 ? 43.643  57.860  9.589   0.58 39.88  ? 629  GLU A OE2 1 
ATOM   4781  N  N   . LYS A 1 621 ? 41.701  53.806  7.423   1.00 30.40  ? 630  LYS A N   1 
ATOM   4782  C  CA  . LYS A 1 621 ? 41.380  52.455  7.000   1.00 32.88  ? 630  LYS A CA  1 
ATOM   4783  C  C   . LYS A 1 621 ? 39.871  52.194  7.062   1.00 33.39  ? 630  LYS A C   1 
ATOM   4784  O  O   . LYS A 1 621 ? 39.318  51.542  6.170   1.00 28.40  ? 630  LYS A O   1 
ATOM   4785  C  CB  . LYS A 1 621 ? 42.120  51.472  7.898   1.00 36.53  ? 630  LYS A CB  1 
ATOM   4786  C  CG  . LYS A 1 621 ? 43.622  51.474  7.582   1.00 37.91  ? 630  LYS A CG  1 
ATOM   4787  C  CD  . LYS A 1 621 ? 44.341  50.619  8.592   1.00 41.67  ? 630  LYS A CD  1 
ATOM   4788  C  CE  . LYS A 1 621 ? 45.832  50.908  8.640   1.00 48.82  ? 630  LYS A CE  1 
ATOM   4789  N  NZ  . LYS A 1 621 ? 46.520  49.771  9.317   1.00 47.43  ? 630  LYS A NZ  1 
ATOM   4790  N  N   . VAL A 1 622 ? 39.193  52.711  8.117   1.00 30.55  ? 631  VAL A N   1 
ATOM   4791  C  CA  . VAL A 1 622 ? 37.741  52.538  8.184   1.00 27.65  ? 631  VAL A CA  1 
ATOM   4792  C  C   . VAL A 1 622 ? 37.117  53.310  7.045   1.00 26.05  ? 631  VAL A C   1 
ATOM   4793  O  O   . VAL A 1 622 ? 36.151  52.867  6.433   1.00 24.17  ? 631  VAL A O   1 
ATOM   4794  C  CB  . VAL A 1 622 ? 37.204  53.013  9.564   1.00 25.90  ? 631  VAL A CB  1 
ATOM   4795  C  CG1 . VAL A 1 622 ? 35.653  53.061  9.539   1.00 23.52  ? 631  VAL A CG1 1 
ATOM   4796  C  CG2 . VAL A 1 622 ? 37.692  52.072  10.640  1.00 24.52  ? 631  VAL A CG2 1 
ATOM   4797  N  N   . LYS A 1 623 ? 37.687  54.500  6.742   1.00 25.22  ? 632  LYS A N   1 
ATOM   4798  C  CA  . LYS A 1 623 ? 37.150  55.272  5.633   1.00 29.61  ? 632  LYS A CA  1 
ATOM   4799  C  C   . LYS A 1 623 ? 37.340  54.440  4.296   1.00 24.55  ? 632  LYS A C   1 
ATOM   4800  O  O   . LYS A 1 623 ? 36.460  54.431  3.456   1.00 24.75  ? 632  LYS A O   1 
ATOM   4801  C  CB  A LYS A 1 623 ? 37.869  56.612  5.544   0.62 28.90  ? 632  LYS A CB  1 
ATOM   4802  C  CB  B LYS A 1 623 ? 37.944  56.616  5.454   0.38 35.28  ? 632  LYS A CB  1 
ATOM   4803  C  CG  A LYS A 1 623 ? 37.328  57.413  4.371   0.62 37.86  ? 632  LYS A CG  1 
ATOM   4804  C  CG  B LYS A 1 623 ? 37.394  57.462  4.294   0.38 40.54  ? 632  LYS A CG  1 
ATOM   4805  C  CD  A LYS A 1 623 ? 37.965  58.801  4.270   0.62 43.25  ? 632  LYS A CD  1 
ATOM   4806  C  CD  B LYS A 1 623 ? 38.260  58.706  3.923   0.38 44.39  ? 632  LYS A CD  1 
ATOM   4807  C  CE  A LYS A 1 623 ? 37.032  59.702  3.469   0.62 51.19  ? 632  LYS A CE  1 
ATOM   4808  C  CE  B LYS A 1 623 ? 37.473  59.576  2.934   0.38 50.28  ? 632  LYS A CE  1 
ATOM   4809  N  NZ  A LYS A 1 623 ? 35.717  59.933  4.166   0.62 45.81  ? 632  LYS A NZ  1 
ATOM   4810  N  NZ  B LYS A 1 623 ? 38.259  60.699  2.347   0.38 48.22  ? 632  LYS A NZ  1 
ATOM   4811  N  N   . THR A 1 624 ? 38.452  53.722  4.149   1.00 23.18  ? 633  THR A N   1 
ATOM   4812  C  CA  . THR A 1 624 ? 38.665  52.921  2.923   1.00 27.52  ? 633  THR A CA  1 
ATOM   4813  C  C   . THR A 1 624 ? 37.599  51.813  2.834   1.00 25.31  ? 633  THR A C   1 
ATOM   4814  O  O   . THR A 1 624 ? 37.057  51.545  1.768   1.00 24.20  ? 633  THR A O   1 
ATOM   4815  C  CB  . THR A 1 624 ? 40.063  52.316  2.947   1.00 30.94  ? 633  THR A CB  1 
ATOM   4816  O  OG1 . THR A 1 624 ? 40.960  53.426  2.892   1.00 32.30  ? 633  THR A OG1 1 
ATOM   4817  C  CG2 . THR A 1 624 ? 40.324  51.376  1.743   1.00 33.04  ? 633  THR A CG2 1 
ATOM   4818  N  N   . MET A 1 625 ? 37.286  51.198  3.966   1.00 24.91  ? 634  MET A N   1 
ATOM   4819  C  CA  . MET A 1 625 ? 36.235  50.175  3.985   1.00 24.46  ? 634  MET A CA  1 
ATOM   4820  C  C   . MET A 1 625 ? 34.946  50.775  3.497   1.00 23.78  ? 634  MET A C   1 
ATOM   4821  O  O   . MET A 1 625 ? 34.277  50.176  2.644   1.00 21.42  ? 634  MET A O   1 
ATOM   4822  C  CB  . MET A 1 625 ? 36.066  49.645  5.403   1.00 24.85  ? 634  MET A CB  1 
ATOM   4823  C  CG  . MET A 1 625 ? 34.858  48.682  5.517   1.00 26.06  ? 634  MET A CG  1 
ATOM   4824  S  SD  . MET A 1 625 ? 35.070  47.125  4.556   1.00 25.77  ? 634  MET A SD  1 
ATOM   4825  C  CE  . MET A 1 625 ? 36.383  46.247  5.558   1.00 22.63  ? 634  MET A CE  1 
ATOM   4826  N  N   . GLY A 1 626 ? 34.549  52.003  3.995   1.00 18.40  ? 635  GLY A N   1 
ATOM   4827  C  CA  . GLY A 1 626 ? 33.292  52.574  3.527   1.00 18.99  ? 635  GLY A CA  1 
ATOM   4828  C  C   . GLY A 1 626 ? 33.347  52.936  2.043   1.00 18.91  ? 635  GLY A C   1 
ATOM   4829  O  O   . GLY A 1 626 ? 32.366  52.774  1.311   1.00 20.48  ? 635  GLY A O   1 
ATOM   4830  N  N   . THR A 1 627 ? 34.477  53.486  1.622   1.00 19.58  ? 636  THR A N   1 
ATOM   4831  C  CA  . THR A 1 627 ? 34.606  53.855  0.216   1.00 20.41  ? 636  THR A CA  1 
ATOM   4832  C  C   . THR A 1 627 ? 34.411  52.599  -0.716  1.00 19.18  ? 636  THR A C   1 
ATOM   4833  O  O   . THR A 1 627 ? 33.678  52.690  -1.708  1.00 23.56  ? 636  THR A O   1 
ATOM   4834  C  CB  . THR A 1 627 ? 36.035  54.368  -0.038  1.00 23.87  ? 636  THR A CB  1 
ATOM   4835  O  OG1 . THR A 1 627 ? 36.196  55.552  0.787   1.00 24.97  ? 636  THR A OG1 1 
ATOM   4836  C  CG2 . THR A 1 627 ? 36.238  54.702  -1.598  1.00 23.70  ? 636  THR A CG2 1 
ATOM   4837  N  N   . GLN A 1 628 ? 35.065  51.481  -0.393  1.00 23.05  ? 637  GLN A N   1 
ATOM   4838  C  CA  . GLN A 1 628 ? 34.920  50.265  -1.229  1.00 25.99  ? 637  GLN A CA  1 
ATOM   4839  C  C   . GLN A 1 628 ? 33.468  49.821  -1.276  1.00 26.25  ? 637  GLN A C   1 
ATOM   4840  O  O   . GLN A 1 628 ? 32.938  49.414  -2.331  1.00 23.68  ? 637  GLN A O   1 
ATOM   4841  C  CB  . GLN A 1 628 ? 35.808  49.148  -0.686  1.00 26.47  ? 637  GLN A CB  1 
ATOM   4842  C  CG  . GLN A 1 628 ? 37.312  49.451  -0.716  1.00 27.83  ? 637  GLN A CG  1 
ATOM   4843  C  CD  . GLN A 1 628 ? 37.739  49.931  -2.104  1.00 34.93  ? 637  GLN A CD  1 
ATOM   4844  O  OE1 . GLN A 1 628 ? 38.072  51.108  -2.311  1.00 28.95  ? 637  GLN A OE1 1 
ATOM   4845  N  NE2 . GLN A 1 628 ? 37.682  49.037  -3.122  1.00 27.29  ? 637  GLN A NE2 1 
ATOM   4846  N  N   . ILE A 1 629 ? 32.777  49.896  -0.110  1.00 21.29  ? 638  ILE A N   1 
ATOM   4847  C  CA  . ILE A 1 629 ? 31.398  49.534  -0.156  1.00 17.70  ? 638  ILE A CA  1 
ATOM   4848  C  C   . ILE A 1 629 ? 30.645  50.475  -1.087  1.00 21.28  ? 638  ILE A C   1 
ATOM   4849  O  O   . ILE A 1 629 ? 29.785  50.029  -1.841  1.00 21.29  ? 638  ILE A O   1 
ATOM   4850  C  CB  . ILE A 1 629 ? 30.796  49.556  1.292   1.00 19.29  ? 638  ILE A CB  1 
ATOM   4851  C  CG1 . ILE A 1 629 ? 31.457  48.431  2.130   1.00 18.39  ? 638  ILE A CG1 1 
ATOM   4852  C  CG2 . ILE A 1 629 ? 29.262  49.399  1.213   1.00 21.13  ? 638  ILE A CG2 1 
ATOM   4853  C  CD1 . ILE A 1 629 ? 31.072  48.488  3.705   1.00 21.50  ? 638  ILE A CD1 1 
ATOM   4854  N  N   . GLY A 1 630 ? 30.981  51.812  -1.038  1.00 20.52  ? 639  GLY A N   1 
ATOM   4855  C  CA  . GLY A 1 630 ? 30.287  52.753  -1.903  1.00 20.07  ? 639  GLY A CA  1 
ATOM   4856  C  C   . GLY A 1 630 ? 30.593  52.427  -3.379  1.00 20.51  ? 639  GLY A C   1 
ATOM   4857  O  O   . GLY A 1 630 ? 29.703  52.562  -4.234  1.00 19.96  ? 639  GLY A O   1 
ATOM   4858  N  N   . ILE A 1 631 ? 31.812  52.029  -3.661  1.00 20.69  ? 640  ILE A N   1 
ATOM   4859  C  CA  . ILE A 1 631 ? 32.161  51.727  -5.090  1.00 23.86  ? 640  ILE A CA  1 
ATOM   4860  C  C   . ILE A 1 631 ? 31.319  50.501  -5.538  1.00 23.56  ? 640  ILE A C   1 
ATOM   4861  O  O   . ILE A 1 631 ? 30.753  50.512  -6.640  1.00 26.19  ? 640  ILE A O   1 
ATOM   4862  C  CB  . ILE A 1 631 ? 33.672  51.438  -5.248  1.00 24.89  ? 640  ILE A CB  1 
ATOM   4863  C  CG1 . ILE A 1 631 ? 34.511  52.749  -5.033  1.00 23.08  ? 640  ILE A CG1 1 
ATOM   4864  C  CG2 . ILE A 1 631 ? 33.951  50.901  -6.748  1.00 24.76  ? 640  ILE A CG2 1 
ATOM   4865  C  CD1 . ILE A 1 631 ? 35.998  52.437  -4.739  1.00 23.37  ? 640  ILE A CD1 1 
ATOM   4866  N  N   . GLY A 1 632 ? 31.242  49.470  -4.680  1.00 24.27  ? 641  GLY A N   1 
ATOM   4867  C  CA  . GLY A 1 632 ? 30.429  48.293  -5.006  1.00 22.45  ? 641  GLY A CA  1 
ATOM   4868  C  C   . GLY A 1 632 ? 28.989  48.673  -5.230  1.00 25.10  ? 641  GLY A C   1 
ATOM   4869  O  O   . GLY A 1 632 ? 28.316  48.131  -6.093  1.00 24.92  ? 641  GLY A O   1 
ATOM   4870  N  N   . ILE A 1 633 ? 28.443  49.614  -4.416  1.00 22.21  ? 642  ILE A N   1 
ATOM   4871  C  CA  . ILE A 1 633 ? 27.066  50.046  -4.611  1.00 20.60  ? 642  ILE A CA  1 
ATOM   4872  C  C   . ILE A 1 633 ? 26.912  50.794  -5.967  1.00 21.60  ? 642  ILE A C   1 
ATOM   4873  O  O   . ILE A 1 633 ? 25.923  50.573  -6.693  1.00 26.36  ? 642  ILE A O   1 
ATOM   4874  C  CB  . ILE A 1 633 ? 26.598  50.986  -3.444  1.00 18.41  ? 642  ILE A CB  1 
ATOM   4875  C  CG1 . ILE A 1 633 ? 26.496  50.107  -2.135  1.00 21.46  ? 642  ILE A CG1 1 
ATOM   4876  C  CG2 . ILE A 1 633 ? 25.224  51.697  -3.777  1.00 19.49  ? 642  ILE A CG2 1 
ATOM   4877  C  CD1 . ILE A 1 633 ? 26.277  51.013  -0.835  1.00 20.76  ? 642  ILE A CD1 1 
ATOM   4878  N  N   . GLU A 1 634 ? 27.843  51.700  -6.253  1.00 24.44  ? 643  GLU A N   1 
ATOM   4879  C  CA  . GLU A 1 634 ? 27.815  52.459  -7.515  1.00 26.59  ? 643  GLU A CA  1 
ATOM   4880  C  C   . GLU A 1 634 ? 27.872  51.431  -8.711  1.00 28.21  ? 643  GLU A C   1 
ATOM   4881  O  O   . GLU A 1 634 ? 27.130  51.609  -9.695  1.00 31.00  ? 643  GLU A O   1 
ATOM   4882  C  CB  . GLU A 1 634 ? 29.020  53.386  -7.556  1.00 29.78  ? 643  GLU A CB  1 
ATOM   4883  C  CG  . GLU A 1 634 ? 29.185  54.031  -8.926  1.00 32.26  ? 643  GLU A CG  1 
ATOM   4884  C  CD  . GLU A 1 634 ? 30.484  54.838  -9.012  1.00 29.64  ? 643  GLU A CD  1 
ATOM   4885  O  OE1 . GLU A 1 634 ? 31.532  54.372  -8.529  1.00 31.01  ? 643  GLU A OE1 1 
ATOM   4886  O  OE2 . GLU A 1 634 ? 30.413  55.951  -9.568  1.00 35.75  ? 643  GLU A OE2 1 
ATOM   4887  N  N   . ASP A 1 635 ? 28.722  50.418  -8.618  1.00 25.44  ? 644  ASP A N   1 
ATOM   4888  C  CA  . ASP A 1 635 ? 28.776  49.355  -9.621  1.00 30.16  ? 644  ASP A CA  1 
ATOM   4889  C  C   . ASP A 1 635 ? 27.420  48.819  -9.893  1.00 32.19  ? 644  ASP A C   1 
ATOM   4890  O  O   . ASP A 1 635 ? 27.062  48.559  -11.053 1.00 30.78  ? 644  ASP A O   1 
ATOM   4891  C  CB  . ASP A 1 635 ? 29.555  48.140  -9.136  1.00 29.45  ? 644  ASP A CB  1 
ATOM   4892  C  CG  . ASP A 1 635 ? 31.029  48.360  -9.029  1.00 31.54  ? 644  ASP A CG  1 
ATOM   4893  O  OD1 . ASP A 1 635 ? 31.541  49.281  -9.688  1.00 33.48  ? 644  ASP A OD1 1 
ATOM   4894  O  OD2 . ASP A 1 635 ? 31.694  47.594  -8.297  1.00 28.74  ? 644  ASP A OD2 1 
ATOM   4895  N  N   . THR A 1 636 ? 26.657  48.636  -8.844  1.00 27.76  ? 645  THR A N   1 
ATOM   4896  C  CA  . THR A 1 636 ? 25.346  48.064  -8.925  1.00 28.48  ? 645  THR A CA  1 
ATOM   4897  C  C   . THR A 1 636 ? 24.265  48.983  -9.419  1.00 33.01  ? 645  THR A C   1 
ATOM   4898  O  O   . THR A 1 636 ? 23.493  48.551  -10.290 1.00 33.65  ? 645  THR A O   1 
ATOM   4899  C  CB  . THR A 1 636 ? 24.967  47.538  -7.510  1.00 27.57  ? 645  THR A CB  1 
ATOM   4900  O  OG1 . THR A 1 636 ? 25.996  46.673  -7.043  1.00 24.39  ? 645  THR A OG1 1 
ATOM   4901  C  CG2 . THR A 1 636 ? 23.668  46.755  -7.529  1.00 30.96  ? 645  THR A CG2 1 
ATOM   4902  N  N   . VAL A 1 637 ? 24.179  50.237  -8.950  1.00 32.07  ? 646  VAL A N   1 
ATOM   4903  C  CA  . VAL A 1 637 ? 23.030  51.056  -9.336  1.00 37.42  ? 646  VAL A CA  1 
ATOM   4904  C  C   . VAL A 1 637 ? 23.249  52.012  -10.510 1.00 38.20  ? 646  VAL A C   1 
ATOM   4905  O  O   . VAL A 1 637 ? 22.257  52.555  -11.003 1.00 40.65  ? 646  VAL A O   1 
ATOM   4906  C  CB  . VAL A 1 637 ? 22.508  51.904  -8.110  1.00 33.93  ? 646  VAL A CB  1 
ATOM   4907  C  CG1 . VAL A 1 637 ? 22.177  51.004  -6.892  1.00 31.94  ? 646  VAL A CG1 1 
ATOM   4908  C  CG2 . VAL A 1 637 ? 23.534  52.936  -7.718  1.00 31.96  ? 646  VAL A CG2 1 
ATOM   4909  N  N   . LYS A 1 638 ? 24.465  52.228  -10.964 1.00 41.06  ? 647  LYS A N   1 
ATOM   4910  C  CA  . LYS A 1 638 ? 24.602  53.286  -11.980 1.00 48.62  ? 647  LYS A CA  1 
ATOM   4911  C  C   . LYS A 1 638 ? 23.950  52.973  -13.350 1.00 53.11  ? 647  LYS A C   1 
ATOM   4912  O  O   . LYS A 1 638 ? 23.942  51.815  -13.777 1.00 53.85  ? 647  LYS A O   1 
ATOM   4913  C  CB  . LYS A 1 638 ? 26.077  53.626  -12.172 1.00 51.04  ? 647  LYS A CB  1 
ATOM   4914  C  CG  . LYS A 1 638 ? 26.870  52.431  -12.590 1.00 54.63  ? 647  LYS A CG  1 
ATOM   4915  C  CD  . LYS A 1 638 ? 28.315  52.817  -12.849 1.00 61.20  ? 647  LYS A CD  1 
ATOM   4916  C  CE  . LYS A 1 638 ? 29.193  51.588  -12.988 1.00 68.83  ? 647  LYS A CE  1 
ATOM   4917  N  NZ  . LYS A 1 638 ? 30.024  51.621  -14.219 0.00 0.00   ? 647  LYS A NZ  1 
ATOM   4918  O  OXT . LYS A 1 638 ? 23.459  53.925  -13.967 1.00 52.87  ? 647  LYS A OXT 1 
ATOM   4919  N  N   . SER B 1 1   ? -1.484  31.616  44.393  1.00 48.02  ? 10   SER B N   1 
ATOM   4920  C  CA  . SER B 1 1   ? -0.243  31.711  43.616  1.00 48.17  ? 10   SER B CA  1 
ATOM   4921  C  C   . SER B 1 1   ? 0.948   31.962  44.548  1.00 40.98  ? 10   SER B C   1 
ATOM   4922  O  O   . SER B 1 1   ? 0.879   32.791  45.443  1.00 39.71  ? 10   SER B O   1 
ATOM   4923  C  CB  . SER B 1 1   ? -0.356  32.811  42.556  1.00 49.66  ? 10   SER B CB  1 
ATOM   4924  O  OG  . SER B 1 1   ? 0.893   33.012  41.914  1.00 56.41  ? 10   SER B OG  1 
ATOM   4925  N  N   . ASP B 1 2   ? 2.042   31.259  44.324  1.00 33.86  ? 11   ASP B N   1 
ATOM   4926  C  CA  . ASP B 1 2   ? 3.208   31.389  45.197  1.00 34.64  ? 11   ASP B CA  1 
ATOM   4927  C  C   . ASP B 1 2   ? 4.207   32.456  44.722  1.00 33.85  ? 11   ASP B C   1 
ATOM   4928  O  O   . ASP B 1 2   ? 5.204   32.715  45.390  1.00 28.95  ? 11   ASP B O   1 
ATOM   4929  C  CB  . ASP B 1 2   ? 3.907   30.034  45.265  1.00 39.58  ? 11   ASP B CB  1 
ATOM   4930  C  CG  . ASP B 1 2   ? 3.057   28.999  46.027  1.00 47.59  ? 11   ASP B CG  1 
ATOM   4931  O  OD1 . ASP B 1 2   ? 2.411   29.374  47.038  1.00 50.57  ? 11   ASP B OD1 1 
ATOM   4932  O  OD2 . ASP B 1 2   ? 3.048   27.853  45.616  1.00 52.06  ? 11   ASP B OD2 1 
ATOM   4933  N  N   . ILE B 1 3   ? 3.927   33.065  43.538  1.00 30.74  ? 12   ILE B N   1 
ATOM   4934  C  CA  . ILE B 1 3   ? 4.812   34.115  43.021  1.00 27.46  ? 12   ILE B CA  1 
ATOM   4935  C  C   . ILE B 1 3   ? 3.918   35.197  42.422  1.00 27.00  ? 12   ILE B C   1 
ATOM   4936  O  O   . ILE B 1 3   ? 2.888   34.860  41.819  1.00 28.24  ? 12   ILE B O   1 
ATOM   4937  C  CB  A ILE B 1 3   ? 5.760   33.495  41.980  0.47 27.49  ? 12   ILE B CB  1 
ATOM   4938  C  CB  B ILE B 1 3   ? 5.756   33.714  41.880  0.53 26.03  ? 12   ILE B CB  1 
ATOM   4939  C  CG1 A ILE B 1 3   ? 6.647   34.602  41.354  0.47 28.40  ? 12   ILE B CG1 1 
ATOM   4940  C  CG1 B ILE B 1 3   ? 6.334   32.333  42.131  0.53 25.67  ? 12   ILE B CG1 1 
ATOM   4941  C  CG2 A ILE B 1 3   ? 4.957   32.740  40.928  0.47 26.07  ? 12   ILE B CG2 1 
ATOM   4942  C  CG2 B ILE B 1 3   ? 6.924   34.753  41.759  0.53 25.02  ? 12   ILE B CG2 1 
ATOM   4943  C  CD1 A ILE B 1 3   ? 7.663   34.048  40.396  0.47 29.57  ? 12   ILE B CD1 1 
ATOM   4944  C  CD1 B ILE B 1 3   ? 7.158   31.854  40.962  0.53 28.84  ? 12   ILE B CD1 1 
ATOM   4945  N  N   . ASN B 1 4   ? 4.270   36.457  42.615  1.00 26.23  ? 13   ASN B N   1 
ATOM   4946  C  CA  . ASN B 1 4   ? 3.555   37.582  41.986  1.00 23.81  ? 13   ASN B CA  1 
ATOM   4947  C  C   . ASN B 1 4   ? 4.648   38.353  41.171  1.00 25.53  ? 13   ASN B C   1 
ATOM   4948  O  O   . ASN B 1 4   ? 5.698   38.685  41.725  1.00 24.36  ? 13   ASN B O   1 
ATOM   4949  C  CB  . ASN B 1 4   ? 2.956   38.516  43.027  1.00 24.67  ? 13   ASN B CB  1 
ATOM   4950  C  CG  . ASN B 1 4   ? 2.116   39.580  42.347  1.00 29.62  ? 13   ASN B CG  1 
ATOM   4951  O  OD1 . ASN B 1 4   ? 2.666   40.623  41.940  1.00 27.48  ? 13   ASN B OD1 1 
ATOM   4952  N  ND2 . ASN B 1 4   ? 0.825   39.378  42.156  1.00 27.74  ? 13   ASN B ND2 1 
ATOM   4953  N  N   . ILE B 1 5   ? 4.407   38.557  39.850  1.00 22.61  ? 14   ILE B N   1 
ATOM   4954  C  CA  . ILE B 1 5   ? 5.354   39.314  38.990  1.00 21.20  ? 14   ILE B CA  1 
ATOM   4955  C  C   . ILE B 1 5   ? 4.609   40.602  38.572  1.00 20.14  ? 14   ILE B C   1 
ATOM   4956  O  O   . ILE B 1 5   ? 3.607   40.529  37.838  1.00 22.57  ? 14   ILE B O   1 
ATOM   4957  C  CB  . ILE B 1 5   ? 5.748   38.460  37.777  1.00 21.77  ? 14   ILE B CB  1 
ATOM   4958  C  CG1 . ILE B 1 5   ? 6.496   37.159  38.241  1.00 21.79  ? 14   ILE B CG1 1 
ATOM   4959  C  CG2 . ILE B 1 5   ? 6.679   39.307  36.854  1.00 20.81  ? 14   ILE B CG2 1 
ATOM   4960  C  CD1 . ILE B 1 5   ? 6.743   36.246  37.034  1.00 19.51  ? 14   ILE B CD1 1 
ATOM   4961  N  N   . ASN B 1 6   ? 5.079   41.727  39.046  1.00 19.92  ? 15   ASN B N   1 
ATOM   4962  C  CA  . ASN B 1 6   ? 4.446   43.005  38.761  1.00 22.69  ? 15   ASN B CA  1 
ATOM   4963  C  C   . ASN B 1 6   ? 5.342   43.760  37.769  1.00 20.47  ? 15   ASN B C   1 
ATOM   4964  O  O   . ASN B 1 6   ? 6.369   44.279  38.177  1.00 20.21  ? 15   ASN B O   1 
ATOM   4965  C  CB  . ASN B 1 6   ? 4.281   43.788  40.049  1.00 22.48  ? 15   ASN B CB  1 
ATOM   4966  C  CG  . ASN B 1 6   ? 3.487   45.072  39.840  1.00 25.49  ? 15   ASN B CG  1 
ATOM   4967  O  OD1 . ASN B 1 6   ? 2.695   45.173  38.882  1.00 21.68  ? 15   ASN B OD1 1 
ATOM   4968  N  ND2 . ASN B 1 6   ? 3.649   46.079  40.658  1.00 24.86  ? 15   ASN B ND2 1 
ATOM   4969  N  N   . LEU B 1 7   ? 4.983   43.715  36.466  1.00 20.56  ? 16   LEU B N   1 
ATOM   4970  C  CA  . LEU B 1 7   ? 5.743   44.444  35.427  1.00 20.67  ? 16   LEU B CA  1 
ATOM   4971  C  C   . LEU B 1 7   ? 5.082   45.782  35.236  1.00 18.97  ? 16   LEU B C   1 
ATOM   4972  O  O   . LEU B 1 7   ? 3.854   45.873  35.228  1.00 21.10  ? 16   LEU B O   1 
ATOM   4973  C  CB  . LEU B 1 7   ? 5.717   43.694  34.112  1.00 20.13  ? 16   LEU B CB  1 
ATOM   4974  C  CG  . LEU B 1 7   ? 6.280   42.257  34.223  1.00 20.70  ? 16   LEU B CG  1 
ATOM   4975  C  CD1 . LEU B 1 7   ? 6.269   41.640  32.814  1.00 21.84  ? 16   LEU B CD1 1 
ATOM   4976  C  CD2 . LEU B 1 7   ? 7.645   42.320  34.785  1.00 21.37  ? 16   LEU B CD2 1 
ATOM   4977  N  N   . GLN B 1 8   ? 5.872   46.808  35.111  1.00 18.72  ? 17   GLN B N   1 
ATOM   4978  C  CA  . GLN B 1 8   ? 5.293   48.160  34.979  1.00 17.46  ? 17   GLN B CA  1 
ATOM   4979  C  C   . GLN B 1 8   ? 4.649   48.364  33.617  1.00 18.17  ? 17   GLN B C   1 
ATOM   4980  O  O   . GLN B 1 8   ? 3.593   49.006  33.546  1.00 18.38  ? 17   GLN B O   1 
ATOM   4981  C  CB  . GLN B 1 8   ? 6.419   49.186  35.144  1.00 19.25  ? 17   GLN B CB  1 
ATOM   4982  C  CG  . GLN B 1 8   ? 5.932   50.683  35.088  1.00 18.23  ? 17   GLN B CG  1 
ATOM   4983  C  CD  . GLN B 1 8   ? 7.079   51.640  35.212  1.00 19.76  ? 17   GLN B CD  1 
ATOM   4984  O  OE1 . GLN B 1 8   ? 8.265   51.279  34.966  1.00 19.70  ? 17   GLN B OE1 1 
ATOM   4985  N  NE2 . GLN B 1 8   ? 6.759   52.849  35.637  1.00 20.52  ? 17   GLN B NE2 1 
ATOM   4986  N  N   . ARG B 1 9   ? 5.271   47.861  32.569  1.00 20.60  ? 18   ARG B N   1 
ATOM   4987  C  CA  . ARG B 1 9   ? 4.788   48.163  31.183  1.00 22.11  ? 18   ARG B CA  1 
ATOM   4988  C  C   . ARG B 1 9   ? 4.601   46.929  30.358  1.00 21.01  ? 18   ARG B C   1 
ATOM   4989  O  O   . ARG B 1 9   ? 5.432   46.029  30.432  1.00 22.87  ? 18   ARG B O   1 
ATOM   4990  C  CB  A ARG B 1 9   ? 5.861   49.085  30.477  0.68 18.81  ? 18   ARG B CB  1 
ATOM   4991  C  CB  B ARG B 1 9   ? 6.036   48.838  30.272  0.32 19.08  ? 18   ARG B CB  1 
ATOM   4992  C  CG  A ARG B 1 9   ? 6.400   50.221  31.393  0.68 19.93  ? 18   ARG B CG  1 
ATOM   4993  C  CG  B ARG B 1 9   ? 6.624   50.064  30.926  0.32 23.43  ? 18   ARG B CG  1 
ATOM   4994  C  CD  A ARG B 1 9   ? 7.288   51.240  30.634  0.68 25.67  ? 18   ARG B CD  1 
ATOM   4995  C  CD  B ARG B 1 9   ? 6.949   51.038  29.792  0.32 26.95  ? 18   ARG B CD  1 
ATOM   4996  N  NE  A ARG B 1 9   ? 7.854   52.246  31.535  0.68 30.44  ? 18   ARG B NE  1 
ATOM   4997  N  NE  B ARG B 1 9   ? 8.226   51.704  29.982  0.32 32.10  ? 18   ARG B NE  1 
ATOM   4998  C  CZ  A ARG B 1 9   ? 7.197   53.303  32.010  0.68 24.34  ? 18   ARG B CZ  1 
ATOM   4999  C  CZ  B ARG B 1 9   ? 8.742   52.534  29.090  0.32 22.30  ? 18   ARG B CZ  1 
ATOM   5000  N  NH1 A ARG B 1 9   ? 7.796   54.137  32.849  0.68 30.40  ? 18   ARG B NH1 1 
ATOM   5001  N  NH1 B ARG B 1 9   ? 9.908   53.108  29.315  0.32 25.65  ? 18   ARG B NH1 1 
ATOM   5002  N  NH2 A ARG B 1 9   ? 5.961   53.542  31.640  0.68 17.46  ? 18   ARG B NH2 1 
ATOM   5003  N  NH2 B ARG B 1 9   ? 8.085   52.807  27.964  0.32 20.01  ? 18   ARG B NH2 1 
ATOM   5004  N  N   . LYS B 1 10  ? 3.540   46.843  29.537  1.00 19.17  ? 19   LYS B N   1 
ATOM   5005  C  CA  . LYS B 1 10  ? 3.370   45.673  28.644  1.00 19.46  ? 19   LYS B CA  1 
ATOM   5006  C  C   . LYS B 1 10  ? 3.492   46.081  27.163  1.00 20.82  ? 19   LYS B C   1 
ATOM   5007  O  O   . LYS B 1 10  ? 3.388   45.245  26.304  1.00 19.99  ? 19   LYS B O   1 
ATOM   5008  C  CB  . LYS B 1 10  ? 1.987   45.015  28.842  1.00 22.83  ? 19   LYS B CB  1 
ATOM   5009  C  CG  . LYS B 1 10  ? 1.778   44.706  30.356  1.00 30.26  ? 19   LYS B CG  1 
ATOM   5010  C  CD  . LYS B 1 10  ? 2.432   43.361  30.741  1.00 38.93  ? 19   LYS B CD  1 
ATOM   5011  C  CE  . LYS B 1 10  ? 1.315   42.318  31.019  1.00 47.22  ? 19   LYS B CE  1 
ATOM   5012  N  NZ  . LYS B 1 10  ? 0.996   41.527  29.804  1.00 57.03  ? 19   LYS B NZ  1 
ATOM   5013  N  N   . SER B 1 11  ? 3.679   47.369  26.921  1.00 21.26  ? 20   SER B N   1 
ATOM   5014  C  CA  . SER B 1 11  ? 3.915   47.910  25.588  1.00 20.40  ? 20   SER B CA  1 
ATOM   5015  C  C   . SER B 1 11  ? 5.195   48.776  25.730  1.00 20.62  ? 20   SER B C   1 
ATOM   5016  O  O   . SER B 1 11  ? 5.247   49.661  26.589  1.00 20.10  ? 20   SER B O   1 
ATOM   5017  C  CB  . SER B 1 11  ? 2.727   48.748  25.147  1.00 23.14  ? 20   SER B CB  1 
ATOM   5018  O  OG  . SER B 1 11  ? 2.890   49.098  23.772  1.00 27.55  ? 20   SER B OG  1 
ATOM   5019  N  N   . VAL B 1 12  ? 6.230   48.484  24.955  1.00 19.73  ? 21   VAL B N   1 
ATOM   5020  C  CA  . VAL B 1 12  ? 7.503   49.195  25.101  1.00 17.86  ? 21   VAL B CA  1 
ATOM   5021  C  C   . VAL B 1 12  ? 8.078   49.451  23.686  1.00 17.64  ? 21   VAL B C   1 
ATOM   5022  O  O   . VAL B 1 12  ? 7.440   49.075  22.700  1.00 18.99  ? 21   VAL B O   1 
ATOM   5023  C  CB  . VAL B 1 12  ? 8.550   48.306  25.913  1.00 18.60  ? 21   VAL B CB  1 
ATOM   5024  C  CG1 . VAL B 1 12  ? 8.075   48.094  27.377  1.00 19.38  ? 21   VAL B CG1 1 
ATOM   5025  C  CG2 . VAL B 1 12  ? 8.822   46.966  25.205  1.00 17.68  ? 21   VAL B CG2 1 
ATOM   5026  N  N   . VAL B 1 13  ? 9.256   50.097  23.629  1.00 17.80  ? 22   VAL B N   1 
ATOM   5027  C  CA  . VAL B 1 13  ? 9.954   50.282  22.347  1.00 19.48  ? 22   VAL B CA  1 
ATOM   5028  C  C   . VAL B 1 13  ? 11.408  49.975  22.589  1.00 22.08  ? 22   VAL B C   1 
ATOM   5029  O  O   . VAL B 1 13  ? 11.833  49.777  23.721  1.00 19.46  ? 22   VAL B O   1 
ATOM   5030  C  CB  . VAL B 1 13  ? 9.812   51.718  21.797  1.00 18.94  ? 22   VAL B CB  1 
ATOM   5031  C  CG1 . VAL B 1 13  ? 8.335   52.057  21.542  1.00 20.80  ? 22   VAL B CG1 1 
ATOM   5032  C  CG2 . VAL B 1 13  ? 10.464  52.695  22.789  1.00 21.09  ? 22   VAL B CG2 1 
ATOM   5033  N  N   . LEU B 1 14  ? 12.212  49.919  21.516  1.00 19.64  ? 23   LEU B N   1 
ATOM   5034  C  CA  . LEU B 1 14  ? 13.634  49.707  21.740  1.00 18.80  ? 23   LEU B CA  1 
ATOM   5035  C  C   . LEU B 1 14  ? 14.139  50.832  22.637  1.00 20.71  ? 23   LEU B C   1 
ATOM   5036  O  O   . LEU B 1 14  ? 13.894  52.024  22.369  1.00 20.01  ? 23   LEU B O   1 
ATOM   5037  C  CB  . LEU B 1 14  ? 14.352  49.699  20.362  1.00 19.66  ? 23   LEU B CB  1 
ATOM   5038  C  CG  . LEU B 1 14  ? 15.873  49.420  20.424  1.00 20.64  ? 23   LEU B CG  1 
ATOM   5039  C  CD1 . LEU B 1 14  ? 16.080  47.983  20.851  1.00 19.28  ? 23   LEU B CD1 1 
ATOM   5040  C  CD2 . LEU B 1 14  ? 16.514  49.638  18.937  1.00 20.11  ? 23   LEU B CD2 1 
ATOM   5041  N  N   . GLY B 1 15  ? 14.853  50.474  23.723  1.00 22.95  ? 24   GLY B N   1 
ATOM   5042  C  CA  . GLY B 1 15  ? 15.384  51.466  24.646  1.00 25.66  ? 24   GLY B CA  1 
ATOM   5043  C  C   . GLY B 1 15  ? 14.552  51.711  25.892  1.00 26.25  ? 24   GLY B C   1 
ATOM   5044  O  O   . GLY B 1 15  ? 15.016  52.388  26.796  1.00 24.61  ? 24   GLY B O   1 
ATOM   5045  N  N   . SER B 1 16  ? 13.315  51.180  25.940  1.00 24.50  ? 25   SER B N   1 
ATOM   5046  C  CA  . SER B 1 16  ? 12.422  51.342  27.105  1.00 23.83  ? 25   SER B CA  1 
ATOM   5047  C  C   . SER B 1 16  ? 13.021  50.741  28.378  1.00 22.79  ? 25   SER B C   1 
ATOM   5048  O  O   . SER B 1 16  ? 13.817  49.795  28.320  1.00 22.07  ? 25   SER B O   1 
ATOM   5049  C  CB  . SER B 1 16  ? 11.088  50.607  26.881  1.00 20.31  ? 25   SER B CB  1 
ATOM   5050  O  OG  . SER B 1 16  ? 10.286  51.343  25.981  1.00 21.91  ? 25   SER B OG  1 
ATOM   5051  N  N   . LYS B 1 17  ? 12.599  51.295  29.510  1.00 22.31  ? 26   LYS B N   1 
ATOM   5052  C  CA  . LYS B 1 17  ? 12.960  50.775  30.831  1.00 23.90  ? 26   LYS B CA  1 
ATOM   5053  C  C   . LYS B 1 17  ? 11.624  50.483  31.482  1.00 24.37  ? 26   LYS B C   1 
ATOM   5054  O  O   . LYS B 1 17  ? 10.651  51.252  31.335  1.00 22.91  ? 26   LYS B O   1 
ATOM   5055  C  CB  . LYS B 1 17  ? 13.705  51.788  31.736  1.00 22.78  ? 26   LYS B CB  1 
ATOM   5056  C  CG  . LYS B 1 17  ? 15.076  52.230  31.189  1.00 25.88  ? 26   LYS B CG  1 
ATOM   5057  C  CD  . LYS B 1 17  ? 16.056  51.080  31.139  1.00 33.01  ? 26   LYS B CD  1 
ATOM   5058  C  CE  . LYS B 1 17  ? 17.413  51.527  30.641  1.00 35.80  ? 26   LYS B CE  1 
ATOM   5059  N  NZ  . LYS B 1 17  ? 17.739  52.860  31.180  1.00 46.26  ? 26   LYS B NZ  1 
ATOM   5060  N  N   . SER B 1 18  ? 11.540  49.376  32.199  1.00 21.54  ? 27   SER B N   1 
ATOM   5061  C  CA  . SER B 1 18  ? 10.303  49.030  32.867  1.00 20.80  ? 27   SER B CA  1 
ATOM   5062  C  C   . SER B 1 18  ? 10.659  48.512  34.259  1.00 21.89  ? 27   SER B C   1 
ATOM   5063  O  O   . SER B 1 18  ? 11.482  47.590  34.355  1.00 23.64  ? 27   SER B O   1 
ATOM   5064  C  CB  . SER B 1 18  ? 9.597   47.915  32.108  1.00 20.79  ? 27   SER B CB  1 
ATOM   5065  O  OG  . SER B 1 18  ? 8.450   47.435  32.813  1.00 22.83  ? 27   SER B OG  1 
ATOM   5066  N  N   . ASN B 1 19  ? 10.070  49.055  35.303  1.00 19.73  ? 28   ASN B N   1 
ATOM   5067  C  CA  . ASN B 1 19  ? 10.364  48.514  36.646  1.00 23.23  ? 28   ASN B CA  1 
ATOM   5068  C  C   . ASN B 1 19  ? 9.731   47.131  36.810  1.00 25.43  ? 28   ASN B C   1 
ATOM   5069  O  O   . ASN B 1 19  ? 8.601   46.907  36.340  1.00 23.66  ? 28   ASN B O   1 
ATOM   5070  C  CB  . ASN B 1 19  ? 9.756   49.416  37.707  1.00 22.65  ? 28   ASN B CB  1 
ATOM   5071  C  CG  . ASN B 1 19  ? 10.441  50.765  37.767  1.00 23.53  ? 28   ASN B CG  1 
ATOM   5072  O  OD1 . ASN B 1 19  ? 9.812   51.751  38.171  1.00 29.44  ? 28   ASN B OD1 1 
ATOM   5073  N  ND2 . ASN B 1 19  ? 11.669  50.902  37.389  1.00 20.49  ? 28   ASN B ND2 1 
ATOM   5074  N  N   . ALA B 1 20  ? 10.402  46.214  37.507  1.00 21.64  ? 29   ALA B N   1 
ATOM   5075  C  CA  . ALA B 1 20  ? 9.833   44.873  37.715  1.00 19.18  ? 29   ALA B CA  1 
ATOM   5076  C  C   . ALA B 1 20  ? 9.920   44.620  39.239  1.00 20.58  ? 29   ALA B C   1 
ATOM   5077  O  O   . ALA B 1 20  ? 10.946  44.927  39.842  1.00 21.41  ? 29   ALA B O   1 
ATOM   5078  C  CB  . ALA B 1 20  ? 10.672  43.832  36.974  1.00 20.75  ? 29   ALA B CB  1 
ATOM   5079  N  N   . SER B 1 21  ? 8.861   44.069  39.818  1.00 20.82  ? 30   SER B N   1 
ATOM   5080  C  CA  . SER B 1 21  ? 8.842   43.794  41.254  1.00 23.07  ? 30   SER B CA  1 
ATOM   5081  C  C   . SER B 1 21  ? 8.313   42.345  41.363  1.00 24.97  ? 30   SER B C   1 
ATOM   5082  O  O   . SER B 1 21  ? 7.204   42.057  40.872  1.00 22.56  ? 30   SER B O   1 
ATOM   5083  C  CB  . SER B 1 21  ? 7.927   44.820  41.912  1.00 26.05  ? 30   SER B CB  1 
ATOM   5084  O  OG  . SER B 1 21  ? 7.708   44.558  43.280  1.00 29.14  ? 30   SER B OG  1 
ATOM   5085  N  N   . VAL B 1 22  ? 9.102   41.424  41.982  1.00 22.43  ? 31   VAL B N   1 
ATOM   5086  C  CA  . VAL B 1 22  ? 8.683   40.015  42.070  1.00 21.18  ? 31   VAL B CA  1 
ATOM   5087  C  C   . VAL B 1 22  ? 8.645   39.638  43.568  1.00 22.91  ? 31   VAL B C   1 
ATOM   5088  O  O   . VAL B 1 22  ? 9.625   39.874  44.246  1.00 23.11  ? 31   VAL B O   1 
ATOM   5089  C  CB  . VAL B 1 22  ? 9.633   39.131  41.273  1.00 22.08  ? 31   VAL B CB  1 
ATOM   5090  C  CG1 . VAL B 1 22  ? 9.246   37.664  41.433  1.00 22.66  ? 31   VAL B CG1 1 
ATOM   5091  C  CG2 . VAL B 1 22  ? 9.524   39.530  39.773  1.00 20.30  ? 31   VAL B CG2 1 
ATOM   5092  N  N   A LYS B 1 23  ? 7.514   39.083  44.029  0.46 22.71  ? 32   LYS B N   1 
ATOM   5093  N  N   B LYS B 1 23  ? 7.454   39.060  43.972  0.54 21.70  ? 32   LYS B N   1 
ATOM   5094  C  CA  A LYS B 1 23  ? 7.310   38.697  45.422  0.46 24.16  ? 32   LYS B CA  1 
ATOM   5095  C  CA  B LYS B 1 23  ? 7.334   38.660  45.373  0.54 24.13  ? 32   LYS B CA  1 
ATOM   5096  C  C   A LYS B 1 23  ? 7.018   37.201  45.482  0.46 23.30  ? 32   LYS B C   1 
ATOM   5097  C  C   B LYS B 1 23  ? 7.021   37.169  45.437  0.54 23.13  ? 32   LYS B C   1 
ATOM   5098  O  O   A LYS B 1 23  ? 6.172   36.713  44.741  0.46 23.29  ? 32   LYS B O   1 
ATOM   5099  O  O   B LYS B 1 23  ? 6.217   36.659  44.663  0.54 22.51  ? 32   LYS B O   1 
ATOM   5100  C  CB  A LYS B 1 23  ? 6.125   39.478  46.023  0.46 25.45  ? 32   LYS B CB  1 
ATOM   5101  C  CB  B LYS B 1 23  ? 6.249   39.488  46.075  0.54 26.29  ? 32   LYS B CB  1 
ATOM   5102  C  CG  A LYS B 1 23  ? 6.412   40.953  46.233  0.46 26.61  ? 32   LYS B CG  1 
ATOM   5103  C  CG  B LYS B 1 23  ? 6.197   39.182  47.569  0.54 31.66  ? 32   LYS B CG  1 
ATOM   5104  C  CD  A LYS B 1 23  ? 5.331   41.619  47.061  0.46 33.56  ? 32   LYS B CD  1 
ATOM   5105  C  CD  B LYS B 1 23  ? 5.298   40.138  48.328  0.54 35.31  ? 32   LYS B CD  1 
ATOM   5106  C  CE  A LYS B 1 23  ? 5.489   43.133  47.024  0.46 41.24  ? 32   LYS B CE  1 
ATOM   5107  C  CE  B LYS B 1 23  ? 5.938   40.460  49.642  0.54 37.02  ? 32   LYS B CE  1 
ATOM   5108  N  NZ  A LYS B 1 23  ? 4.774   43.798  48.149  0.46 45.74  ? 32   LYS B NZ  1 
ATOM   5109  N  NZ  B LYS B 1 23  ? 6.331   41.872  49.705  0.54 41.78  ? 32   LYS B NZ  1 
ATOM   5110  N  N   . PHE B 1 24  ? 7.747   36.482  46.335  1.00 23.83  ? 33   PHE B N   1 
ATOM   5111  C  CA  . PHE B 1 24  ? 7.560   35.023  46.555  1.00 22.61  ? 33   PHE B CA  1 
ATOM   5112  C  C   . PHE B 1 24  ? 6.943   34.840  47.948  1.00 23.38  ? 33   PHE B C   1 
ATOM   5113  O  O   . PHE B 1 24  ? 7.354   35.515  48.900  1.00 25.52  ? 33   PHE B O   1 
ATOM   5114  C  CB  . PHE B 1 24  ? 8.927   34.317  46.533  1.00 22.47  ? 33   PHE B CB  1 
ATOM   5115  C  CG  . PHE B 1 24  ? 9.476   34.234  45.119  1.00 25.54  ? 33   PHE B CG  1 
ATOM   5116  C  CD1 . PHE B 1 24  ? 10.233  35.283  44.582  1.00 29.50  ? 33   PHE B CD1 1 
ATOM   5117  C  CD2 . PHE B 1 24  ? 9.285   33.100  44.350  1.00 29.69  ? 33   PHE B CD2 1 
ATOM   5118  C  CE1 . PHE B 1 24  ? 10.787  35.181  43.312  1.00 28.56  ? 33   PHE B CE1 1 
ATOM   5119  C  CE2 . PHE B 1 24  ? 9.857   33.003  43.061  1.00 32.54  ? 33   PHE B CE2 1 
ATOM   5120  C  CZ  . PHE B 1 24  ? 10.595  34.043  42.563  1.00 27.05  ? 33   PHE B CZ  1 
ATOM   5121  N  N   . LYS B 1 25  ? 6.000   33.944  48.085  1.00 24.79  ? 34   LYS B N   1 
ATOM   5122  C  CA  . LYS B 1 25  ? 5.433   33.656  49.416  1.00 28.37  ? 34   LYS B CA  1 
ATOM   5123  C  C   . LYS B 1 25  ? 6.481   32.906  50.300  1.00 29.88  ? 34   LYS B C   1 
ATOM   5124  O  O   . LYS B 1 25  ? 6.417   32.987  51.523  1.00 31.01  ? 34   LYS B O   1 
ATOM   5125  C  CB  . LYS B 1 25  ? 4.213   32.778  49.221  1.00 31.14  ? 34   LYS B CB  1 
ATOM   5126  C  CG  . LYS B 1 25  ? 3.055   33.541  48.592  1.00 41.41  ? 34   LYS B CG  1 
ATOM   5127  C  CD  . LYS B 1 25  ? 1.734   33.065  49.154  1.00 51.85  ? 34   LYS B CD  1 
ATOM   5128  C  CE  . LYS B 1 25  ? 0.860   34.251  49.524  1.00 61.61  ? 34   LYS B CE  1 
ATOM   5129  N  NZ  . LYS B 1 25  ? 0.183   34.815  48.326  1.00 63.94  ? 34   LYS B NZ  1 
ATOM   5130  N  N   . GLU B 1 26  ? 7.415   32.193  49.695  1.00 29.87  ? 35   GLU B N   1 
ATOM   5131  C  CA  . GLU B 1 26  ? 8.445   31.487  50.476  1.00 30.87  ? 35   GLU B CA  1 
ATOM   5132  C  C   . GLU B 1 26  ? 9.784   32.217  50.429  1.00 33.89  ? 35   GLU B C   1 
ATOM   5133  O  O   . GLU B 1 26  ? 10.052  32.972  49.482  1.00 32.50  ? 35   GLU B O   1 
ATOM   5134  C  CB  . GLU B 1 26  ? 8.620   30.069  49.889  1.00 36.86  ? 35   GLU B CB  1 
ATOM   5135  C  CG  . GLU B 1 26  ? 7.441   29.175  50.231  1.00 49.58  ? 35   GLU B CG  1 
ATOM   5136  C  CD  . GLU B 1 26  ? 7.644   27.743  49.756  1.00 60.70  ? 35   GLU B CD  1 
ATOM   5137  O  OE1 . GLU B 1 26  ? 8.773   27.217  49.929  1.00 68.66  ? 35   GLU B OE1 1 
ATOM   5138  O  OE2 . GLU B 1 26  ? 6.682   27.153  49.214  1.00 66.26  ? 35   GLU B OE2 1 
ATOM   5139  N  N   . LYS B 1 27  ? 10.632  32.023  51.428  1.00 27.99  ? 36   LYS B N   1 
ATOM   5140  C  CA  . LYS B 1 27  ? 11.947  32.626  51.425  1.00 27.96  ? 36   LYS B CA  1 
ATOM   5141  C  C   . LYS B 1 27  ? 12.813  31.832  50.426  1.00 30.33  ? 36   LYS B C   1 
ATOM   5142  O  O   . LYS B 1 27  ? 12.796  30.586  50.453  1.00 29.54  ? 36   LYS B O   1 
ATOM   5143  C  CB  . LYS B 1 27  ? 12.545  32.562  52.838  1.00 28.39  ? 36   LYS B CB  1 
ATOM   5144  C  CG  . LYS B 1 27  ? 13.948  33.178  52.896  1.00 28.04  ? 36   LYS B CG  1 
ATOM   5145  C  CD  . LYS B 1 27  ? 14.372  33.426  54.346  1.00 32.65  ? 36   LYS B CD  1 
ATOM   5146  C  CE  . LYS B 1 27  ? 15.873  33.642  54.495  1.00 36.55  ? 36   LYS B CE  1 
ATOM   5147  N  NZ  . LYS B 1 27  ? 16.198  34.232  55.832  1.00 33.51  ? 36   LYS B NZ  1 
ATOM   5148  N  N   . LEU B 1 28  ? 13.570  32.501  49.540  1.00 28.62  ? 37   LEU B N   1 
ATOM   5149  C  CA  . LEU B 1 28  ? 14.352  31.742  48.565  1.00 28.89  ? 37   LEU B CA  1 
ATOM   5150  C  C   . LEU B 1 28  ? 15.804  31.502  48.971  1.00 29.45  ? 37   LEU B C   1 
ATOM   5151  O  O   . LEU B 1 28  ? 16.426  30.693  48.301  1.00 28.74  ? 37   LEU B O   1 
ATOM   5152  C  CB  . LEU B 1 28  ? 14.425  32.473  47.176  1.00 31.59  ? 37   LEU B CB  1 
ATOM   5153  C  CG  . LEU B 1 28  ? 13.053  32.778  46.520  1.00 30.60  ? 37   LEU B CG  1 
ATOM   5154  C  CD1 . LEU B 1 28  ? 13.288  33.398  45.124  1.00 30.06  ? 37   LEU B CD1 1 
ATOM   5155  C  CD2 . LEU B 1 28  ? 12.255  31.492  46.395  1.00 30.55  ? 37   LEU B CD2 1 
ATOM   5156  N  N   . ASN B 1 29  ? 16.329  32.176  50.010  1.00 28.69  ? 38   ASN B N   1 
ATOM   5157  C  CA  . ASN B 1 29  ? 17.761  32.094  50.393  1.00 32.29  ? 38   ASN B CA  1 
ATOM   5158  C  C   . ASN B 1 29  ? 18.580  32.584  49.137  1.00 32.28  ? 38   ASN B C   1 
ATOM   5159  O  O   . ASN B 1 29  ? 19.523  31.943  48.701  1.00 31.01  ? 38   ASN B O   1 
ATOM   5160  C  CB  . ASN B 1 29  ? 18.148  30.657  50.814  1.00 33.20  ? 38   ASN B CB  1 
ATOM   5161  C  CG  . ASN B 1 29  ? 17.238  30.189  51.952  1.00 38.20  ? 38   ASN B CG  1 
ATOM   5162  O  OD1 . ASN B 1 29  ? 17.147  30.907  52.963  1.00 39.87  ? 38   ASN B OD1 1 
ATOM   5163  N  ND2 . ASN B 1 29  ? 16.498  29.077  51.828  1.00 36.66  ? 38   ASN B ND2 1 
ATOM   5164  N  N   . ALA B 1 30  ? 18.183  33.744  48.567  1.00 28.79  ? 39   ALA B N   1 
ATOM   5165  C  CA  . ALA B 1 30  ? 18.855  34.283  47.375  1.00 26.52  ? 39   ALA B CA  1 
ATOM   5166  C  C   . ALA B 1 30  ? 18.797  35.807  47.420  1.00 25.65  ? 39   ALA B C   1 
ATOM   5167  O  O   . ALA B 1 30  ? 17.726  36.377  47.644  1.00 26.36  ? 39   ALA B O   1 
ATOM   5168  C  CB  . ALA B 1 30  ? 18.165  33.767  46.132  1.00 28.79  ? 39   ALA B CB  1 
ATOM   5169  N  N   . ASP B 1 31  ? 19.948  36.464  47.257  1.00 23.74  ? 40   ASP B N   1 
ATOM   5170  C  CA  . ASP B 1 31  ? 19.956  37.921  47.257  1.00 24.24  ? 40   ASP B CA  1 
ATOM   5171  C  C   . ASP B 1 31  ? 19.434  38.476  45.907  1.00 26.43  ? 40   ASP B C   1 
ATOM   5172  O  O   . ASP B 1 31  ? 19.184  39.685  45.828  1.00 26.15  ? 40   ASP B O   1 
ATOM   5173  C  CB  . ASP B 1 31  ? 21.378  38.453  47.452  1.00 27.93  ? 40   ASP B CB  1 
ATOM   5174  C  CG  . ASP B 1 31  ? 21.880  38.360  48.893  1.00 39.67  ? 40   ASP B CG  1 
ATOM   5175  O  OD1 . ASP B 1 31  ? 21.061  38.042  49.794  1.00 43.36  ? 40   ASP B OD1 1 
ATOM   5176  O  OD2 . ASP B 1 31  ? 23.069  38.618  49.114  1.00 44.77  ? 40   ASP B OD2 1 
ATOM   5177  N  N   . SER B 1 32  ? 19.317  37.653  44.870  1.00 23.61  ? 41   SER B N   1 
ATOM   5178  C  CA  . SER B 1 32  ? 18.769  38.182  43.604  1.00 24.84  ? 41   SER B CA  1 
ATOM   5179  C  C   . SER B 1 32  ? 18.218  37.099  42.798  1.00 24.32  ? 41   SER B C   1 
ATOM   5180  O  O   . SER B 1 32  ? 18.485  35.922  43.068  1.00 23.64  ? 41   SER B O   1 
ATOM   5181  C  CB  . SER B 1 32  ? 19.854  38.908  42.801  1.00 23.25  ? 41   SER B CB  1 
ATOM   5182  O  OG  . SER B 1 32  ? 20.860  38.016  42.329  1.00 24.50  ? 41   SER B OG  1 
ATOM   5183  N  N   . ILE B 1 33  ? 17.380  37.456  41.793  1.00 20.05  ? 42   ILE B N   1 
ATOM   5184  C  CA  . ILE B 1 33  ? 16.841  36.507  40.864  1.00 21.84  ? 42   ILE B CA  1 
ATOM   5185  C  C   . ILE B 1 33  ? 17.064  37.132  39.452  1.00 23.97  ? 42   ILE B C   1 
ATOM   5186  O  O   . ILE B 1 33  ? 17.262  38.347  39.360  1.00 23.69  ? 42   ILE B O   1 
ATOM   5187  C  CB  . ILE B 1 33  ? 15.337  36.172  41.047  1.00 25.16  ? 42   ILE B CB  1 
ATOM   5188  C  CG1 . ILE B 1 33  ? 14.470  37.444  40.789  1.00 22.96  ? 42   ILE B CG1 1 
ATOM   5189  C  CG2 . ILE B 1 33  ? 15.039  35.625  42.453  1.00 21.40  ? 42   ILE B CG2 1 
ATOM   5190  C  CD1 . ILE B 1 33  ? 12.958  37.222  40.897  1.00 19.93  ? 42   ILE B CD1 1 
ATOM   5191  N  N   . THR B 1 34  ? 17.025  36.313  38.381  1.00 23.40  ? 43   THR B N   1 
ATOM   5192  C  CA  . THR B 1 34  ? 17.167  36.792  36.991  1.00 22.58  ? 43   THR B CA  1 
ATOM   5193  C  C   . THR B 1 34  ? 15.985  36.311  36.220  1.00 25.47  ? 43   THR B C   1 
ATOM   5194  O  O   . THR B 1 34  ? 15.715  35.093  36.192  1.00 26.40  ? 43   THR B O   1 
ATOM   5195  C  CB  . THR B 1 34  ? 18.440  36.203  36.342  1.00 25.93  ? 43   THR B CB  1 
ATOM   5196  O  OG1 . THR B 1 34  ? 19.566  36.706  37.086  1.00 27.44  ? 43   THR B OG1 1 
ATOM   5197  C  CG2 . THR B 1 34  ? 18.568  36.600  34.825  1.00 24.38  ? 43   THR B CG2 1 
ATOM   5198  N  N   . LEU B 1 35  ? 15.260  37.205  35.580  1.00 23.41  ? 44   LEU B N   1 
ATOM   5199  C  CA  . LEU B 1 35  ? 14.139  36.816  34.744  1.00 22.51  ? 44   LEU B CA  1 
ATOM   5200  C  C   . LEU B 1 35  ? 14.675  36.590  33.314  1.00 24.74  ? 44   LEU B C   1 
ATOM   5201  O  O   . LEU B 1 35  ? 15.457  37.434  32.846  1.00 25.47  ? 44   LEU B O   1 
ATOM   5202  C  CB  . LEU B 1 35  ? 13.115  37.967  34.687  1.00 20.96  ? 44   LEU B CB  1 
ATOM   5203  C  CG  . LEU B 1 35  ? 12.489  38.419  36.058  1.00 32.37  ? 44   LEU B CG  1 
ATOM   5204  C  CD1 . LEU B 1 35  ? 11.305  39.415  35.796  1.00 31.77  ? 44   LEU B CD1 1 
ATOM   5205  C  CD2 . LEU B 1 35  ? 11.937  37.292  36.823  1.00 31.99  ? 44   LEU B CD2 1 
ATOM   5206  N  N   . ASN B 1 36  ? 14.278  35.511  32.609  1.00 22.75  ? 45   ASN B N   1 
ATOM   5207  C  CA  . ASN B 1 36  ? 14.768  35.254  31.250  1.00 22.89  ? 45   ASN B CA  1 
ATOM   5208  C  C   . ASN B 1 36  ? 13.603  35.267  30.335  1.00 25.74  ? 45   ASN B C   1 
ATOM   5209  O  O   . ASN B 1 36  ? 12.609  34.545  30.564  1.00 23.39  ? 45   ASN B O   1 
ATOM   5210  C  CB  . ASN B 1 36  ? 15.460  33.848  31.092  1.00 24.57  ? 45   ASN B CB  1 
ATOM   5211  C  CG  . ASN B 1 36  ? 16.693  33.793  31.945  1.00 33.06  ? 45   ASN B CG  1 
ATOM   5212  O  OD1 . ASN B 1 36  ? 16.719  33.055  32.946  1.00 38.23  ? 45   ASN B OD1 1 
ATOM   5213  N  ND2 . ASN B 1 36  ? 17.714  34.578  31.654  1.00 28.86  ? 45   ASN B ND2 1 
ATOM   5214  N  N   . PHE B 1 37  ? 13.740  36.027  29.236  1.00 22.57  ? 46   PHE B N   1 
ATOM   5215  C  CA  . PHE B 1 37  ? 12.668  36.168  28.264  1.00 21.19  ? 46   PHE B CA  1 
ATOM   5216  C  C   . PHE B 1 37  ? 13.204  35.800  26.912  1.00 21.67  ? 46   PHE B C   1 
ATOM   5217  O  O   . PHE B 1 37  ? 14.420  35.724  26.712  1.00 24.84  ? 46   PHE B O   1 
ATOM   5218  C  CB  . PHE B 1 37  ? 12.186  37.631  28.161  1.00 21.58  ? 46   PHE B CB  1 
ATOM   5219  C  CG  . PHE B 1 37  ? 11.778  38.278  29.453  1.00 22.11  ? 46   PHE B CG  1 
ATOM   5220  C  CD1 . PHE B 1 37  ? 12.692  39.021  30.199  1.00 22.56  ? 46   PHE B CD1 1 
ATOM   5221  C  CD2 . PHE B 1 37  ? 10.491  38.177  29.913  1.00 23.25  ? 46   PHE B CD2 1 
ATOM   5222  C  CE1 . PHE B 1 37  ? 12.310  39.634  31.377  1.00 25.54  ? 46   PHE B CE1 1 
ATOM   5223  C  CE2 . PHE B 1 37  ? 10.109  38.786  31.111  1.00 26.37  ? 46   PHE B CE2 1 
ATOM   5224  C  CZ  . PHE B 1 37  ? 11.028  39.510  31.829  1.00 23.57  ? 46   PHE B CZ  1 
ATOM   5225  N  N   . MET B 1 38  ? 12.316  35.558  25.975  1.00 22.10  ? 47   MET B N   1 
ATOM   5226  C  CA  . MET B 1 38  ? 12.784  35.242  24.621  1.00 23.62  ? 47   MET B CA  1 
ATOM   5227  C  C   . MET B 1 38  ? 11.829  35.798  23.678  1.00 23.95  ? 47   MET B C   1 
ATOM   5228  O  O   . MET B 1 38  ? 10.606  35.774  23.931  1.00 22.72  ? 47   MET B O   1 
ATOM   5229  C  CB  . MET B 1 38  ? 12.839  33.695  24.395  1.00 28.28  ? 47   MET B CB  1 
ATOM   5230  C  CG  . MET B 1 38  ? 13.391  33.315  23.051  1.00 37.03  ? 47   MET B CG  1 
ATOM   5231  S  SD  . MET B 1 38  ? 15.208  33.190  23.053  1.00 48.23  ? 47   MET B SD  1 
ATOM   5232  C  CE  . MET B 1 38  ? 15.498  32.461  24.508  1.00 46.69  ? 47   MET B CE  1 
ATOM   5233  N  N   . CYS B 1 39  ? 12.341  36.328  22.550  1.00 22.28  ? 48   CYS B N   1 
ATOM   5234  C  CA  . CYS B 1 39  ? 11.463  36.794  21.470  1.00 23.85  ? 48   CYS B CA  1 
ATOM   5235  C  C   . CYS B 1 39  ? 12.045  36.105  20.212  1.00 26.82  ? 48   CYS B C   1 
ATOM   5236  O  O   . CYS B 1 39  ? 13.123  36.488  19.728  1.00 25.00  ? 48   CYS B O   1 
ATOM   5237  C  CB  . CYS B 1 39  ? 11.449  38.317  21.318  1.00 23.82  ? 48   CYS B CB  1 
ATOM   5238  S  SG  . CYS B 1 39  ? 10.396  38.852  19.874  1.00 23.62  ? 48   CYS B SG  1 
ATOM   5239  N  N   . TYR B 1 40  ? 11.343  35.058  19.713  1.00 26.02  ? 49   TYR B N   1 
ATOM   5240  C  CA  . TYR B 1 40  ? 11.805  34.200  18.606  1.00 25.61  ? 49   TYR B CA  1 
ATOM   5241  C  C   . TYR B 1 40  ? 13.117  33.584  19.076  1.00 29.39  ? 49   TYR B C   1 
ATOM   5242  O  O   . TYR B 1 40  ? 13.065  32.782  19.984  1.00 32.73  ? 49   TYR B O   1 
ATOM   5243  C  CB  . TYR B 1 40  ? 11.963  34.934  17.279  1.00 27.09  ? 49   TYR B CB  1 
ATOM   5244  C  CG  . TYR B 1 40  ? 12.276  33.972  16.145  1.00 33.47  ? 49   TYR B CG  1 
ATOM   5245  C  CD1 . TYR B 1 40  ? 11.426  32.908  15.854  1.00 36.34  ? 49   TYR B CD1 1 
ATOM   5246  C  CD2 . TYR B 1 40  ? 13.423  34.118  15.378  1.00 34.12  ? 49   TYR B CD2 1 
ATOM   5247  C  CE1 . TYR B 1 40  ? 11.716  32.010  14.832  1.00 36.39  ? 49   TYR B CE1 1 
ATOM   5248  C  CE2 . TYR B 1 40  ? 13.723  33.226  14.350  1.00 34.69  ? 49   TYR B CE2 1 
ATOM   5249  C  CZ  . TYR B 1 40  ? 12.864  32.170  14.081  1.00 38.81  ? 49   TYR B CZ  1 
ATOM   5250  O  OH  . TYR B 1 40  ? 13.126  31.274  13.075  1.00 37.93  ? 49   TYR B OH  1 
ATOM   5251  N  N   . ASP B 1 41  ? 14.274  33.942  18.531  1.00 27.09  ? 50   ASP B N   1 
ATOM   5252  C  CA  . ASP B 1 41  ? 15.524  33.372  18.955  1.00 26.11  ? 50   ASP B CA  1 
ATOM   5253  C  C   . ASP B 1 41  ? 16.359  34.382  19.720  1.00 26.62  ? 50   ASP B C   1 
ATOM   5254  O  O   . ASP B 1 41  ? 17.539  34.129  19.969  1.00 29.35  ? 50   ASP B O   1 
ATOM   5255  C  CB  . ASP B 1 41  ? 16.325  32.884  17.726  1.00 29.21  ? 50   ASP B CB  1 
ATOM   5256  C  CG  . ASP B 1 41  ? 16.734  33.970  16.715  1.00 35.30  ? 50   ASP B CG  1 
ATOM   5257  O  OD1 . ASP B 1 41  ? 16.266  35.127  16.841  1.00 35.01  ? 50   ASP B OD1 1 
ATOM   5258  O  OD2 . ASP B 1 41  ? 17.518  33.663  15.806  1.00 38.07  ? 50   ASP B OD2 1 
ATOM   5259  N  N   . MET B 1 42  ? 15.810  35.527  20.088  1.00 26.73  ? 51   MET B N   1 
ATOM   5260  C  CA  . MET B 1 42  ? 16.627  36.511  20.797  1.00 25.04  ? 51   MET B CA  1 
ATOM   5261  C  C   . MET B 1 42  ? 16.349  36.521  22.353  1.00 25.96  ? 51   MET B C   1 
ATOM   5262  O  O   . MET B 1 42  ? 15.181  36.688  22.761  1.00 26.49  ? 51   MET B O   1 
ATOM   5263  C  CB  A MET B 1 42  ? 16.313  37.881  20.198  0.60 26.04  ? 51   MET B CB  1 
ATOM   5264  C  CB  B MET B 1 42  ? 16.323  37.832  20.186  0.40 28.21  ? 51   MET B CB  1 
ATOM   5265  C  CG  A MET B 1 42  ? 16.825  39.030  21.009  0.60 28.98  ? 51   MET B CG  1 
ATOM   5266  C  CG  B MET B 1 42  ? 16.774  39.019  20.986  0.40 30.03  ? 51   MET B CG  1 
ATOM   5267  S  SD  A MET B 1 42  ? 18.561  39.375  20.635  0.60 29.78  ? 51   MET B SD  1 
ATOM   5268  S  SD  B MET B 1 42  ? 16.926  40.471  19.932  0.40 30.06  ? 51   MET B SD  1 
ATOM   5269  C  CE  A MET B 1 42  ? 18.344  40.148  19.064  0.60 29.09  ? 51   MET B CE  1 
ATOM   5270  C  CE  B MET B 1 42  ? 18.187  39.920  18.842  0.40 30.55  ? 51   MET B CE  1 
ATOM   5271  N  N   . PRO B 1 43  ? 17.352  36.323  23.227  1.00 24.17  ? 52   PRO B N   1 
ATOM   5272  C  CA  . PRO B 1 43  ? 17.111  36.344  24.689  1.00 24.22  ? 52   PRO B CA  1 
ATOM   5273  C  C   . PRO B 1 43  ? 17.167  37.763  25.256  1.00 26.45  ? 52   PRO B C   1 
ATOM   5274  O  O   . PRO B 1 43  ? 17.775  38.663  24.676  1.00 27.15  ? 52   PRO B O   1 
ATOM   5275  C  CB  . PRO B 1 43  ? 18.248  35.492  25.256  1.00 25.55  ? 52   PRO B CB  1 
ATOM   5276  C  CG  . PRO B 1 43  ? 19.422  35.720  24.237  1.00 28.83  ? 52   PRO B CG  1 
ATOM   5277  C  CD  . PRO B 1 43  ? 18.751  35.979  22.890  1.00 27.36  ? 52   PRO B CD  1 
ATOM   5278  N  N   . LEU B 1 44  ? 16.552  37.949  26.393  1.00 22.63  ? 53   LEU B N   1 
ATOM   5279  C  CA  . LEU B 1 44  ? 16.583  39.207  27.098  1.00 22.34  ? 53   LEU B CA  1 
ATOM   5280  C  C   . LEU B 1 44  ? 16.582  38.785  28.555  1.00 23.89  ? 53   LEU B C   1 
ATOM   5281  O  O   . LEU B 1 44  ? 15.853  37.845  28.886  1.00 24.21  ? 53   LEU B O   1 
ATOM   5282  C  CB  . LEU B 1 44  ? 15.351  40.071  26.778  1.00 21.31  ? 53   LEU B CB  1 
ATOM   5283  C  CG  . LEU B 1 44  ? 15.259  41.406  27.592  1.00 27.02  ? 53   LEU B CG  1 
ATOM   5284  C  CD1 . LEU B 1 44  ? 16.246  42.376  26.999  1.00 31.07  ? 53   LEU B CD1 1 
ATOM   5285  C  CD2 . LEU B 1 44  ? 13.828  42.023  27.490  1.00 24.00  ? 53   LEU B CD2 1 
ATOM   5286  N  N   . GLU B 1 45  ? 17.381  39.426  29.415  1.00 20.29  ? 54   GLU B N   1 
ATOM   5287  C  CA  . GLU B 1 45  ? 17.337  39.016  30.821  1.00 23.53  ? 54   GLU B CA  1 
ATOM   5288  C  C   . GLU B 1 45  ? 17.345  40.262  31.680  1.00 23.54  ? 54   GLU B C   1 
ATOM   5289  O  O   . GLU B 1 45  ? 17.673  41.368  31.209  1.00 21.07  ? 54   GLU B O   1 
ATOM   5290  C  CB  . GLU B 1 45  ? 18.542  38.104  31.142  1.00 26.25  ? 54   GLU B CB  1 
ATOM   5291  C  CG  . GLU B 1 45  ? 19.883  38.798  31.045  1.00 34.02  ? 54   GLU B CG  1 
ATOM   5292  C  CD  . GLU B 1 45  ? 21.022  37.855  31.481  1.00 45.11  ? 54   GLU B CD  1 
ATOM   5293  O  OE1 . GLU B 1 45  ? 21.397  37.874  32.689  1.00 44.61  ? 54   GLU B OE1 1 
ATOM   5294  O  OE2 . GLU B 1 45  ? 21.513  37.100  30.620  1.00 47.20  ? 54   GLU B OE2 1 
ATOM   5295  N  N   . ALA B 1 46  ? 16.970  40.123  32.946  1.00 22.67  ? 55   ALA B N   1 
ATOM   5296  C  CA  . ALA B 1 46  ? 17.040  41.247  33.866  1.00 23.13  ? 55   ALA B CA  1 
ATOM   5297  C  C   . ALA B 1 46  ? 17.225  40.653  35.250  1.00 26.09  ? 55   ALA B C   1 
ATOM   5298  O  O   . ALA B 1 46  ? 16.539  39.650  35.569  1.00 24.60  ? 55   ALA B O   1 
ATOM   5299  C  CB  . ALA B 1 46  ? 15.747  42.064  33.849  1.00 24.69  ? 55   ALA B CB  1 
ATOM   5300  N  N   . THR B 1 47  ? 18.108  41.264  36.075  1.00 24.12  ? 56   THR B N   1 
ATOM   5301  C  CA  . THR B 1 47  ? 18.341  40.760  37.413  1.00 24.34  ? 56   THR B CA  1 
ATOM   5302  C  C   . THR B 1 47  ? 17.730  41.699  38.429  1.00 25.12  ? 56   THR B C   1 
ATOM   5303  O  O   . THR B 1 47  ? 17.953  42.920  38.388  1.00 23.94  ? 56   THR B O   1 
ATOM   5304  C  CB  . THR B 1 47  ? 19.871  40.513  37.623  1.00 24.52  ? 56   THR B CB  1 
ATOM   5305  O  OG1 . THR B 1 47  ? 20.240  39.398  36.822  1.00 25.61  ? 56   THR B OG1 1 
ATOM   5306  C  CG2 . THR B 1 47  ? 20.208  40.133  39.114  1.00 23.11  ? 56   THR B CG2 1 
ATOM   5307  N  N   . LEU B 1 48  ? 16.918  41.130  39.360  1.00 22.76  ? 57   LEU B N   1 
ATOM   5308  C  CA  . LEU B 1 48  ? 16.239  41.909  40.386  1.00 22.50  ? 57   LEU B CA  1 
ATOM   5309  C  C   . LEU B 1 48  ? 16.812  41.575  41.769  1.00 24.67  ? 57   LEU B C   1 
ATOM   5310  O  O   . LEU B 1 48  ? 16.923  40.392  42.093  1.00 23.39  ? 57   LEU B O   1 
ATOM   5311  C  CB  . LEU B 1 48  ? 14.748  41.577  40.377  1.00 23.79  ? 57   LEU B CB  1 
ATOM   5312  C  CG  . LEU B 1 48  ? 14.104  41.423  38.957  1.00 26.21  ? 57   LEU B CG  1 
ATOM   5313  C  CD1 . LEU B 1 48  ? 12.566  41.136  39.140  1.00 19.69  ? 57   LEU B CD1 1 
ATOM   5314  C  CD2 . LEU B 1 48  ? 14.295  42.737  38.141  1.00 26.78  ? 57   LEU B CD2 1 
ATOM   5315  N  N   . ASN B 1 49  ? 17.184  42.593  42.527  1.00 23.89  ? 58   ASN B N   1 
ATOM   5316  C  CA  . ASN B 1 49  ? 17.822  42.431  43.840  1.00 24.67  ? 58   ASN B CA  1 
ATOM   5317  C  C   . ASN B 1 49  ? 16.816  42.386  44.956  1.00 27.04  ? 58   ASN B C   1 
ATOM   5318  O  O   . ASN B 1 49  ? 15.829  43.132  44.958  1.00 24.73  ? 58   ASN B O   1 
ATOM   5319  C  CB  . ASN B 1 49  ? 18.771  43.602  44.073  1.00 28.96  ? 58   ASN B CB  1 
ATOM   5320  C  CG  . ASN B 1 49  ? 19.939  43.466  43.122  1.00 36.99  ? 58   ASN B CG  1 
ATOM   5321  O  OD1 . ASN B 1 49  ? 20.101  44.302  42.226  1.00 39.42  ? 58   ASN B OD1 1 
ATOM   5322  N  ND2 . ASN B 1 49  ? 20.708  42.387  43.195  1.00 30.25  ? 58   ASN B ND2 1 
ATOM   5323  N  N   . TYR B 1 50  ? 17.068  41.515  45.922  1.00 25.28  ? 59   TYR B N   1 
ATOM   5324  C  CA  . TYR B 1 50  ? 16.174  41.404  47.073  1.00 25.92  ? 59   TYR B CA  1 
ATOM   5325  C  C   . TYR B 1 50  ? 16.198  42.684  47.886  1.00 27.40  ? 59   TYR B C   1 
ATOM   5326  O  O   . TYR B 1 50  ? 17.271  43.213  48.159  1.00 29.05  ? 59   TYR B O   1 
ATOM   5327  C  CB  . TYR B 1 50  ? 16.640  40.224  47.977  1.00 26.23  ? 59   TYR B CB  1 
ATOM   5328  C  CG  . TYR B 1 50  ? 15.680  39.996  49.103  1.00 28.95  ? 59   TYR B CG  1 
ATOM   5329  C  CD1 . TYR B 1 50  ? 14.378  39.565  48.861  1.00 27.98  ? 59   TYR B CD1 1 
ATOM   5330  C  CD2 . TYR B 1 50  ? 16.060  40.231  50.421  1.00 31.45  ? 59   TYR B CD2 1 
ATOM   5331  C  CE1 . TYR B 1 50  ? 13.480  39.384  49.905  1.00 34.14  ? 59   TYR B CE1 1 
ATOM   5332  C  CE2 . TYR B 1 50  ? 15.173  40.049  51.465  1.00 29.49  ? 59   TYR B CE2 1 
ATOM   5333  C  CZ  . TYR B 1 50  ? 13.890  39.634  51.209  1.00 35.22  ? 59   TYR B CZ  1 
ATOM   5334  O  OH  . TYR B 1 50  ? 13.048  39.524  52.285  1.00 39.20  ? 59   TYR B OH  1 
ATOM   5335  N  N   . ASN B 1 51  ? 15.039  43.157  48.314  1.00 27.78  ? 60   ASN B N   1 
ATOM   5336  C  CA  . ASN B 1 51  ? 14.890  44.359  49.143  1.00 28.64  ? 60   ASN B CA  1 
ATOM   5337  C  C   . ASN B 1 51  ? 14.226  43.910  50.468  1.00 29.39  ? 60   ASN B C   1 
ATOM   5338  O  O   . ASN B 1 51  ? 13.062  43.552  50.469  1.00 26.97  ? 60   ASN B O   1 
ATOM   5339  C  CB  . ASN B 1 51  ? 14.011  45.383  48.367  1.00 32.44  ? 60   ASN B CB  1 
ATOM   5340  C  CG  . ASN B 1 51  ? 13.473  46.578  49.148  1.00 47.34  ? 60   ASN B CG  1 
ATOM   5341  O  OD1 . ASN B 1 51  ? 13.371  46.560  50.394  1.00 46.54  ? 60   ASN B OD1 1 
ATOM   5342  N  ND2 . ASN B 1 51  ? 12.998  47.664  48.461  1.00 45.71  ? 60   ASN B ND2 1 
ATOM   5343  N  N   . GLU B 1 52  ? 14.975  43.926  51.591  1.00 29.32  ? 61   GLU B N   1 
ATOM   5344  C  CA  . GLU B 1 52  ? 14.462  43.458  52.889  1.00 32.57  ? 61   GLU B CA  1 
ATOM   5345  C  C   . GLU B 1 52  ? 13.242  44.184  53.328  1.00 32.97  ? 61   GLU B C   1 
ATOM   5346  O  O   . GLU B 1 52  ? 12.309  43.581  53.841  1.00 33.36  ? 61   GLU B O   1 
ATOM   5347  C  CB  . GLU B 1 52  ? 15.548  43.625  53.980  1.00 36.76  ? 61   GLU B CB  1 
ATOM   5348  C  CG  . GLU B 1 52  ? 16.649  42.600  53.852  1.00 48.87  ? 61   GLU B CG  1 
ATOM   5349  C  CD  . GLU B 1 52  ? 16.460  41.313  54.719  1.00 62.19  ? 61   GLU B CD  1 
ATOM   5350  O  OE1 . GLU B 1 52  ? 17.430  40.526  54.780  1.00 63.95  ? 61   GLU B OE1 1 
ATOM   5351  O  OE2 . GLU B 1 52  ? 15.373  41.087  55.317  1.00 60.73  ? 61   GLU B OE2 1 
ATOM   5352  N  N   . LYS B 1 53  ? 13.229  45.483  53.125  1.00 34.93  ? 62   LYS B N   1 
ATOM   5353  C  CA  . LYS B 1 53  ? 12.120  46.332  53.529  1.00 40.16  ? 62   LYS B CA  1 
ATOM   5354  C  C   . LYS B 1 53  ? 10.821  45.932  52.932  1.00 41.69  ? 62   LYS B C   1 
ATOM   5355  O  O   . LYS B 1 53  ? 9.799   46.010  53.606  1.00 39.51  ? 62   LYS B O   1 
ATOM   5356  C  CB  . LYS B 1 53  ? 12.401  47.791  53.130  1.00 45.87  ? 62   LYS B CB  1 
ATOM   5357  C  CG  . LYS B 1 53  ? 12.806  48.653  54.300  1.00 56.97  ? 62   LYS B CG  1 
ATOM   5358  C  CD  . LYS B 1 53  ? 13.714  49.781  53.867  1.00 65.72  ? 62   LYS B CD  1 
ATOM   5359  C  CE  . LYS B 1 53  ? 14.869  49.941  54.837  1.00 68.78  ? 62   LYS B CE  1 
ATOM   5360  N  NZ  . LYS B 1 53  ? 15.935  50.841  54.295  1.00 69.18  ? 62   LYS B NZ  1 
ATOM   5361  N  N   . THR B 1 54  ? 10.812  45.500  51.654  1.00 35.10  ? 63   THR B N   1 
ATOM   5362  C  CA  . THR B 1 54  ? 9.540   45.136  51.057  1.00 30.86  ? 63   THR B CA  1 
ATOM   5363  C  C   . THR B 1 54  ? 9.403   43.589  50.821  1.00 28.53  ? 63   THR B C   1 
ATOM   5364  O  O   . THR B 1 54  ? 8.385   43.145  50.315  1.00 29.42  ? 63   THR B O   1 
ATOM   5365  C  CB  . THR B 1 54  ? 9.383   45.901  49.724  1.00 30.55  ? 63   THR B CB  1 
ATOM   5366  O  OG1 . THR B 1 54  ? 10.493  45.559  48.857  1.00 29.86  ? 63   THR B OG1 1 
ATOM   5367  C  CG2 . THR B 1 54  ? 9.381   47.396  49.922  1.00 28.26  ? 63   THR B CG2 1 
ATOM   5368  N  N   . ASP B 1 55  ? 10.440  42.810  51.174  1.00 26.43  ? 64   ASP B N   1 
ATOM   5369  C  CA  . ASP B 1 55  ? 10.443  41.361  51.019  1.00 23.86  ? 64   ASP B CA  1 
ATOM   5370  C  C   . ASP B 1 55  ? 10.122  41.033  49.562  1.00 24.09  ? 64   ASP B C   1 
ATOM   5371  O  O   . ASP B 1 55  ? 9.257   40.211  49.273  1.00 24.75  ? 64   ASP B O   1 
ATOM   5372  C  CB  . ASP B 1 55  ? 9.361   40.695  51.954  1.00 26.47  ? 64   ASP B CB  1 
ATOM   5373  C  CG  . ASP B 1 55  ? 9.478   39.179  51.931  1.00 31.77  ? 64   ASP B CG  1 
ATOM   5374  O  OD1 . ASP B 1 55  ? 8.468   38.501  52.202  1.00 34.41  ? 64   ASP B OD1 1 
ATOM   5375  O  OD2 . ASP B 1 55  ? 10.587  38.659  51.614  1.00 31.48  ? 64   ASP B OD2 1 
ATOM   5376  N  N   . SER B 1 56  ? 10.846  41.697  48.634  1.00 24.36  ? 65   SER B N   1 
ATOM   5377  C  CA  . SER B 1 56  ? 10.555  41.484  47.215  1.00 25.00  ? 65   SER B CA  1 
ATOM   5378  C  C   . SER B 1 56  ? 11.842  41.697  46.392  1.00 24.30  ? 65   SER B C   1 
ATOM   5379  O  O   . SER B 1 56  ? 12.809  42.251  46.896  1.00 25.28  ? 65   SER B O   1 
ATOM   5380  C  CB  . SER B 1 56  ? 9.488   42.489  46.755  1.00 26.34  ? 65   SER B CB  1 
ATOM   5381  O  OG  . SER B 1 56  ? 9.958   43.803  46.995  1.00 32.05  ? 65   SER B OG  1 
ATOM   5382  N  N   . TYR B 1 57  ? 11.847  41.218  45.156  1.00 21.23  ? 66   TYR B N   1 
ATOM   5383  C  CA  . TYR B 1 57  ? 13.009  41.377  44.284  1.00 20.99  ? 66   TYR B CA  1 
ATOM   5384  C  C   . TYR B 1 57  ? 12.693  42.552  43.331  1.00 22.30  ? 66   TYR B C   1 
ATOM   5385  O  O   . TYR B 1 57  ? 11.652  42.482  42.655  1.00 23.37  ? 66   TYR B O   1 
ATOM   5386  C  CB  . TYR B 1 57  ? 13.200  40.095  43.509  1.00 19.85  ? 66   TYR B CB  1 
ATOM   5387  C  CG  . TYR B 1 57  ? 13.721  39.008  44.433  1.00 23.45  ? 66   TYR B CG  1 
ATOM   5388  C  CD1 . TYR B 1 57  ? 12.841  38.219  45.174  1.00 26.05  ? 66   TYR B CD1 1 
ATOM   5389  C  CD2 . TYR B 1 57  ? 15.097  38.802  44.599  1.00 21.48  ? 66   TYR B CD2 1 
ATOM   5390  C  CE1 . TYR B 1 57  ? 13.314  37.248  46.076  1.00 24.78  ? 66   TYR B CE1 1 
ATOM   5391  C  CE2 . TYR B 1 57  ? 15.583  37.820  45.481  1.00 22.94  ? 66   TYR B CE2 1 
ATOM   5392  C  CZ  . TYR B 1 57  ? 14.679  37.053  46.215  1.00 24.00  ? 66   TYR B CZ  1 
ATOM   5393  O  OH  . TYR B 1 57  ? 15.127  36.086  47.084  1.00 24.22  ? 66   TYR B OH  1 
ATOM   5394  N  N   . GLU B 1 58  ? 13.545  43.553  43.269  1.00 23.01  ? 67   GLU B N   1 
ATOM   5395  C  CA  . GLU B 1 58  ? 13.254  44.770  42.471  1.00 23.42  ? 67   GLU B CA  1 
ATOM   5396  C  C   . GLU B 1 58  ? 14.333  45.073  41.523  1.00 22.44  ? 67   GLU B C   1 
ATOM   5397  O  O   . GLU B 1 58  ? 15.489  44.940  41.845  1.00 22.28  ? 67   GLU B O   1 
ATOM   5398  C  CB  . GLU B 1 58  ? 13.177  45.984  43.397  1.00 24.76  ? 67   GLU B CB  1 
ATOM   5399  C  CG  . GLU B 1 58  ? 12.244  45.748  44.580  1.00 25.59  ? 67   GLU B CG  1 
ATOM   5400  C  CD  . GLU B 1 58  ? 10.813  45.853  44.167  1.00 37.57  ? 67   GLU B CD  1 
ATOM   5401  O  OE1 . GLU B 1 58  ? 9.935   45.222  44.784  1.00 38.64  ? 67   GLU B OE1 1 
ATOM   5402  O  OE2 . GLU B 1 58  ? 10.561  46.605  43.196  1.00 41.12  ? 67   GLU B OE2 1 
ATOM   5403  N  N   . GLY B 1 59  ? 13.970  45.546  40.339  1.00 20.75  ? 68   GLY B N   1 
ATOM   5404  C  CA  . GLY B 1 59  ? 15.004  45.919  39.373  1.00 20.05  ? 68   GLY B CA  1 
ATOM   5405  C  C   . GLY B 1 59  ? 14.315  46.526  38.159  1.00 22.00  ? 68   GLY B C   1 
ATOM   5406  O  O   . GLY B 1 59  ? 13.103  46.801  38.173  1.00 21.62  ? 68   GLY B O   1 
ATOM   5407  N  N   . VAL B 1 60  ? 15.086  46.680  37.094  1.00 22.13  ? 69   VAL B N   1 
ATOM   5408  C  CA  . VAL B 1 60  ? 14.570  47.321  35.900  1.00 23.11  ? 69   VAL B CA  1 
ATOM   5409  C  C   . VAL B 1 60  ? 14.906  46.480  34.712  1.00 22.50  ? 69   VAL B C   1 
ATOM   5410  O  O   . VAL B 1 60  ? 16.038  45.996  34.609  1.00 23.50  ? 69   VAL B O   1 
ATOM   5411  C  CB  . VAL B 1 60  ? 15.311  48.714  35.823  1.00 25.17  ? 69   VAL B CB  1 
ATOM   5412  C  CG1 . VAL B 1 60  ? 15.039  49.385  34.467  1.00 24.45  ? 69   VAL B CG1 1 
ATOM   5413  C  CG2 . VAL B 1 60  ? 14.852  49.631  36.954  1.00 22.82  ? 69   VAL B CG2 1 
ATOM   5414  N  N   . ILE B 1 61  ? 13.937  46.297  33.798  1.00 18.87  ? 70   ILE B N   1 
ATOM   5415  C  CA  . ILE B 1 61  ? 14.181  45.563  32.570  1.00 21.34  ? 70   ILE B CA  1 
ATOM   5416  C  C   . ILE B 1 61  ? 14.594  46.613  31.523  1.00 22.18  ? 70   ILE B C   1 
ATOM   5417  O  O   . ILE B 1 61  ? 13.897  47.621  31.385  1.00 22.29  ? 70   ILE B O   1 
ATOM   5418  C  CB  . ILE B 1 61  ? 12.910  44.802  32.075  1.00 20.62  ? 70   ILE B CB  1 
ATOM   5419  C  CG1 . ILE B 1 61  ? 12.439  43.786  33.181  1.00 20.37  ? 70   ILE B CG1 1 
ATOM   5420  C  CG2 . ILE B 1 61  ? 13.244  44.079  30.690  1.00 20.31  ? 70   ILE B CG2 1 
ATOM   5421  C  CD1 . ILE B 1 61  ? 10.997  43.276  32.982  1.00 22.22  ? 70   ILE B CD1 1 
ATOM   5422  N  N   . ASN B 1 62  ? 15.692  46.355  30.814  1.00 20.92  ? 71   ASN B N   1 
ATOM   5423  C  CA  . ASN B 1 62  ? 16.184  47.277  29.794  1.00 23.23  ? 71   ASN B CA  1 
ATOM   5424  C  C   . ASN B 1 62  ? 15.942  46.640  28.428  1.00 21.92  ? 71   ASN B C   1 
ATOM   5425  O  O   . ASN B 1 62  ? 16.645  45.715  28.040  1.00 21.76  ? 71   ASN B O   1 
ATOM   5426  C  CB  . ASN B 1 62  ? 17.682  47.515  30.057  1.00 24.11  ? 71   ASN B CB  1 
ATOM   5427  C  CG  . ASN B 1 62  ? 18.312  48.537  29.133  1.00 36.22  ? 71   ASN B CG  1 
ATOM   5428  O  OD1 . ASN B 1 62  ? 19.516  48.855  29.307  1.00 38.99  ? 71   ASN B OD1 1 
ATOM   5429  N  ND2 . ASN B 1 62  ? 17.630  49.057  28.133  1.00 30.98  ? 71   ASN B ND2 1 
ATOM   5430  N  N   . TYR B 1 63  ? 14.933  47.112  27.703  1.00 20.37  ? 72   TYR B N   1 
ATOM   5431  C  CA  . TYR B 1 63  ? 14.610  46.517  26.407  1.00 21.90  ? 72   TYR B CA  1 
ATOM   5432  C  C   . TYR B 1 63  ? 15.593  47.058  25.329  1.00 22.60  ? 72   TYR B C   1 
ATOM   5433  O  O   . TYR B 1 63  ? 15.195  47.885  24.513  1.00 21.58  ? 72   TYR B O   1 
ATOM   5434  C  CB  . TYR B 1 63  ? 13.170  46.892  26.067  1.00 19.60  ? 72   TYR B CB  1 
ATOM   5435  C  CG  . TYR B 1 63  ? 12.205  46.154  26.986  1.00 22.05  ? 72   TYR B CG  1 
ATOM   5436  C  CD1 . TYR B 1 63  ? 11.708  46.760  28.140  1.00 21.60  ? 72   TYR B CD1 1 
ATOM   5437  C  CD2 . TYR B 1 63  ? 11.829  44.839  26.711  1.00 21.33  ? 72   TYR B CD2 1 
ATOM   5438  C  CE1 . TYR B 1 63  ? 10.850  46.067  29.016  1.00 19.65  ? 72   TYR B CE1 1 
ATOM   5439  C  CE2 . TYR B 1 63  ? 10.992  44.135  27.574  1.00 22.18  ? 72   TYR B CE2 1 
ATOM   5440  C  CZ  . TYR B 1 63  ? 10.509  44.751  28.726  1.00 24.47  ? 72   TYR B CZ  1 
ATOM   5441  O  OH  . TYR B 1 63  ? 9.714   44.005  29.586  1.00 22.21  ? 72   TYR B OH  1 
ATOM   5442  N  N   . ASN B 1 64  ? 16.823  46.586  25.338  1.00 22.09  ? 73   ASN B N   1 
ATOM   5443  C  CA  . ASN B 1 64  ? 17.798  47.164  24.400  1.00 23.59  ? 73   ASN B CA  1 
ATOM   5444  C  C   . ASN B 1 64  ? 18.192  46.166  23.315  1.00 25.23  ? 73   ASN B C   1 
ATOM   5445  O  O   . ASN B 1 64  ? 19.263  46.289  22.724  1.00 22.51  ? 73   ASN B O   1 
ATOM   5446  C  CB  . ASN B 1 64  ? 19.018  47.633  25.218  1.00 23.46  ? 73   ASN B CB  1 
ATOM   5447  C  CG  . ASN B 1 64  ? 19.682  46.533  25.985  1.00 31.13  ? 73   ASN B CG  1 
ATOM   5448  O  OD1 . ASN B 1 64  ? 19.237  45.368  25.997  1.00 29.64  ? 73   ASN B OD1 1 
ATOM   5449  N  ND2 . ASN B 1 64  ? 20.810  46.811  26.678  1.00 32.93  ? 73   ASN B ND2 1 
ATOM   5450  N  N   . LYS B 1 65  ? 17.298  45.173  23.052  1.00 25.40  ? 74   LYS B N   1 
ATOM   5451  C  CA  . LYS B 1 65  ? 17.507  44.154  22.025  1.00 23.34  ? 74   LYS B CA  1 
ATOM   5452  C  C   . LYS B 1 65  ? 16.463  44.349  20.907  1.00 22.59  ? 74   LYS B C   1 
ATOM   5453  O  O   . LYS B 1 65  ? 15.296  44.642  21.184  1.00 22.22  ? 74   LYS B O   1 
ATOM   5454  C  CB  . LYS B 1 65  ? 17.387  42.775  22.650  1.00 24.30  ? 74   LYS B CB  1 
ATOM   5455  C  CG  . LYS B 1 65  ? 18.341  42.670  23.849  1.00 32.64  ? 74   LYS B CG  1 
ATOM   5456  C  CD  . LYS B 1 65  ? 19.666  42.143  23.431  1.00 39.96  ? 74   LYS B CD  1 
ATOM   5457  C  CE  . LYS B 1 65  ? 20.335  41.324  24.536  1.00 49.44  ? 74   LYS B CE  1 
ATOM   5458  N  NZ  . LYS B 1 65  ? 20.129  39.833  24.317  1.00 52.23  ? 74   LYS B NZ  1 
ATOM   5459  N  N   . ASP B 1 66  ? 16.901  44.222  19.649  1.00 22.88  ? 75   ASP B N   1 
ATOM   5460  C  CA  . ASP B 1 66  ? 16.002  44.422  18.530  1.00 21.88  ? 75   ASP B CA  1 
ATOM   5461  C  C   . ASP B 1 66  ? 15.853  43.081  17.760  1.00 24.64  ? 75   ASP B C   1 
ATOM   5462  O  O   . ASP B 1 66  ? 16.673  42.736  16.916  1.00 26.16  ? 75   ASP B O   1 
ATOM   5463  C  CB  . ASP B 1 66  ? 16.587  45.515  17.635  1.00 24.44  ? 75   ASP B CB  1 
ATOM   5464  C  CG  . ASP B 1 66  ? 15.501  46.333  16.957  1.00 27.93  ? 75   ASP B CG  1 
ATOM   5465  O  OD1 . ASP B 1 66  ? 14.300  46.077  17.210  1.00 27.85  ? 75   ASP B OD1 1 
ATOM   5466  O  OD2 . ASP B 1 66  ? 15.834  47.191  16.157  1.00 29.31  ? 75   ASP B OD2 1 
ATOM   5467  N  N   . PRO B 1 67  ? 14.818  42.278  18.036  1.00 28.90  ? 76   PRO B N   1 
ATOM   5468  C  CA  . PRO B 1 67  ? 14.627  40.979  17.342  1.00 28.36  ? 76   PRO B CA  1 
ATOM   5469  C  C   . PRO B 1 67  ? 14.444  41.100  15.832  1.00 21.67  ? 76   PRO B C   1 
ATOM   5470  O  O   . PRO B 1 67  ? 13.782  41.995  15.342  1.00 21.55  ? 76   PRO B O   1 
ATOM   5471  C  CB  . PRO B 1 67  ? 13.347  40.396  18.036  1.00 27.73  ? 76   PRO B CB  1 
ATOM   5472  C  CG  . PRO B 1 67  ? 13.429  40.969  19.393  1.00 34.95  ? 76   PRO B CG  1 
ATOM   5473  C  CD  . PRO B 1 67  ? 13.818  42.450  19.094  1.00 33.70  ? 76   PRO B CD  1 
ATOM   5474  N  N   . GLU B 1 68  ? 14.998  40.123  15.134  1.00 24.23  ? 77   GLU B N   1 
ATOM   5475  C  CA  . GLU B 1 68  ? 14.927  40.058  13.663  1.00 24.52  ? 77   GLU B CA  1 
ATOM   5476  C  C   . GLU B 1 68  ? 13.587  39.632  13.209  1.00 24.86  ? 77   GLU B C   1 
ATOM   5477  O  O   . GLU B 1 68  ? 13.191  39.891  12.057  1.00 23.94  ? 77   GLU B O   1 
ATOM   5478  C  CB  . GLU B 1 68  ? 15.978  39.048  13.141  1.00 24.68  ? 77   GLU B CB  1 
ATOM   5479  C  CG  . GLU B 1 68  ? 17.446  39.483  13.362  1.00 28.56  ? 77   GLU B CG  1 
ATOM   5480  C  CD  . GLU B 1 68  ? 17.833  40.765  12.583  1.00 27.58  ? 77   GLU B CD  1 
ATOM   5481  O  OE1 . GLU B 1 68  ? 17.131  41.163  11.643  1.00 24.40  ? 77   GLU B OE1 1 
ATOM   5482  O  OE2 . GLU B 1 68  ? 18.863  41.356  12.947  1.00 27.47  ? 77   GLU B OE2 1 
ATOM   5483  N  N   . TYR B 1 69  ? 12.828  38.962  14.119  1.00 24.82  ? 78   TYR B N   1 
ATOM   5484  C  CA  . TYR B 1 69  ? 11.494  38.444  13.761  1.00 25.42  ? 78   TYR B CA  1 
ATOM   5485  C  C   . TYR B 1 69  ? 10.639  38.348  15.044  1.00 24.90  ? 78   TYR B C   1 
ATOM   5486  O  O   . TYR B 1 69  ? 11.169  37.965  16.094  1.00 24.49  ? 78   TYR B O   1 
ATOM   5487  C  CB  . TYR B 1 69  ? 11.708  37.095  13.094  1.00 25.57  ? 78   TYR B CB  1 
ATOM   5488  C  CG  . TYR B 1 69  ? 10.436  36.350  12.745  1.00 27.32  ? 78   TYR B CG  1 
ATOM   5489  C  CD1 . TYR B 1 69  ? 9.466   36.930  11.955  1.00 24.56  ? 78   TYR B CD1 1 
ATOM   5490  C  CD2 . TYR B 1 69  ? 10.228  35.036  13.193  1.00 31.34  ? 78   TYR B CD2 1 
ATOM   5491  C  CE1 . TYR B 1 69  ? 8.314   36.237  11.602  1.00 29.81  ? 78   TYR B CE1 1 
ATOM   5492  C  CE2 . TYR B 1 69  ? 9.080   34.342  12.855  1.00 32.23  ? 78   TYR B CE2 1 
ATOM   5493  C  CZ  . TYR B 1 69  ? 8.130   34.944  12.055  1.00 36.92  ? 78   TYR B CZ  1 
ATOM   5494  O  OH  . TYR B 1 69  ? 7.019   34.261  11.680  1.00 36.25  ? 78   TYR B OH  1 
ATOM   5495  N  N   . LEU B 1 70  ? 9.366   38.704  14.960  1.00 23.06  ? 79   LEU B N   1 
ATOM   5496  C  CA  . LEU B 1 70  ? 8.397   38.747  16.092  1.00 23.88  ? 79   LEU B CA  1 
ATOM   5497  C  C   . LEU B 1 70  ? 8.701   39.946  16.992  1.00 25.20  ? 79   LEU B C   1 
ATOM   5498  O  O   . LEU B 1 70  ? 9.786   40.545  16.895  1.00 25.04  ? 79   LEU B O   1 
ATOM   5499  C  CB  . LEU B 1 70  ? 8.354   37.434  16.940  1.00 23.24  ? 79   LEU B CB  1 
ATOM   5500  C  CG  . LEU B 1 70  ? 8.099   36.145  16.041  1.00 28.10  ? 79   LEU B CG  1 
ATOM   5501  C  CD1 . LEU B 1 70  ? 7.928   34.918  16.945  1.00 27.69  ? 79   LEU B CD1 1 
ATOM   5502  C  CD2 . LEU B 1 70  ? 6.825   36.333  15.166  1.00 27.50  ? 79   LEU B CD2 1 
ATOM   5503  N  N   . ASN B 1 71  ? 7.771   40.305  17.870  1.00 23.17  ? 80   ASN B N   1 
ATOM   5504  C  CA  . ASN B 1 71  ? 7.974   41.483  18.734  1.00 22.66  ? 80   ASN B CA  1 
ATOM   5505  C  C   . ASN B 1 71  ? 7.297   41.306  20.080  1.00 21.61  ? 80   ASN B C   1 
ATOM   5506  O  O   . ASN B 1 71  ? 6.922   42.287  20.701  1.00 21.94  ? 80   ASN B O   1 
ATOM   5507  C  CB  . ASN B 1 71  ? 7.466   42.779  18.043  1.00 21.68  ? 80   ASN B CB  1 
ATOM   5508  C  CG  . ASN B 1 71  ? 5.967   42.904  17.944  1.00 24.47  ? 80   ASN B CG  1 
ATOM   5509  O  OD1 . ASN B 1 71  ? 5.229   41.890  17.947  1.00 25.31  ? 80   ASN B OD1 1 
ATOM   5510  N  ND2 . ASN B 1 71  ? 5.439   44.115  17.862  1.00 25.67  ? 80   ASN B ND2 1 
ATOM   5511  N  N   . VAL B 1 72  ? 7.121   40.031  20.534  1.00 20.68  ? 81   VAL B N   1 
ATOM   5512  C  CA  . VAL B 1 72  ? 6.521   39.835  21.878  1.00 19.92  ? 81   VAL B CA  1 
ATOM   5513  C  C   . VAL B 1 72  ? 7.548   39.067  22.739  1.00 21.22  ? 81   VAL B C   1 
ATOM   5514  O  O   . VAL B 1 72  ? 7.989   37.963  22.375  1.00 21.15  ? 81   VAL B O   1 
ATOM   5515  C  CB  . VAL B 1 72  ? 5.220   39.006  21.806  1.00 23.35  ? 81   VAL B CB  1 
ATOM   5516  C  CG1 . VAL B 1 72  ? 4.722   38.692  23.245  1.00 23.77  ? 81   VAL B CG1 1 
ATOM   5517  C  CG2 . VAL B 1 72  ? 4.145   39.771  21.026  1.00 22.43  ? 81   VAL B CG2 1 
ATOM   5518  N  N   . TRP B 1 73  ? 7.947   39.651  23.859  1.00 21.72  ? 82   TRP B N   1 
ATOM   5519  C  CA  . TRP B 1 73  ? 8.882   39.013  24.755  1.00 22.57  ? 82   TRP B CA  1 
ATOM   5520  C  C   . TRP B 1 73  ? 8.083   38.068  25.662  1.00 21.09  ? 82   TRP B C   1 
ATOM   5521  O  O   . TRP B 1 73  ? 7.163   38.533  26.346  1.00 23.19  ? 82   TRP B O   1 
ATOM   5522  C  CB  . TRP B 1 73  ? 9.581   40.071  25.655  1.00 19.06  ? 82   TRP B CB  1 
ATOM   5523  C  CG  . TRP B 1 73  ? 10.453  40.963  24.889  1.00 18.58  ? 82   TRP B CG  1 
ATOM   5524  C  CD1 . TRP B 1 73  ? 10.183  42.248  24.479  1.00 21.42  ? 82   TRP B CD1 1 
ATOM   5525  C  CD2 . TRP B 1 73  ? 11.727  40.622  24.339  1.00 19.24  ? 82   TRP B CD2 1 
ATOM   5526  N  NE1 . TRP B 1 73  ? 11.217  42.711  23.662  1.00 22.58  ? 82   TRP B NE1 1 
ATOM   5527  C  CE2 . TRP B 1 73  ? 12.178  41.737  23.575  1.00 18.38  ? 82   TRP B CE2 1 
ATOM   5528  C  CE3 . TRP B 1 73  ? 12.550  39.465  24.422  1.00 21.21  ? 82   TRP B CE3 1 
ATOM   5529  C  CZ2 . TRP B 1 73  ? 13.412  41.732  22.900  1.00 20.13  ? 82   TRP B CZ2 1 
ATOM   5530  C  CZ3 . TRP B 1 73  ? 13.766  39.451  23.752  1.00 27.56  ? 82   TRP B CZ3 1 
ATOM   5531  C  CH2 . TRP B 1 73  ? 14.192  40.580  22.996  1.00 22.10  ? 82   TRP B CH2 1 
ATOM   5532  N  N   . GLU B 1 74  ? 8.462   36.809  25.706  1.00 22.00  ? 83   GLU B N   1 
ATOM   5533  C  CA  . GLU B 1 74  ? 7.756   35.792  26.526  1.00 22.84  ? 83   GLU B CA  1 
ATOM   5534  C  C   . GLU B 1 74  ? 8.641   35.320  27.662  1.00 22.00  ? 83   GLU B C   1 
ATOM   5535  O  O   . GLU B 1 74  ? 9.800   34.984  27.443  1.00 22.31  ? 83   GLU B O   1 
ATOM   5536  C  CB  . GLU B 1 74  ? 7.400   34.610  25.590  1.00 23.99  ? 83   GLU B CB  1 
ATOM   5537  C  CG  . GLU B 1 74  ? 6.462   35.119  24.486  1.00 23.05  ? 83   GLU B CG  1 
ATOM   5538  C  CD  . GLU B 1 74  ? 5.917   34.010  23.601  1.00 34.06  ? 83   GLU B CD  1 
ATOM   5539  O  OE1 . GLU B 1 74  ? 5.273   34.310  22.597  1.00 41.26  ? 83   GLU B OE1 1 
ATOM   5540  O  OE2 . GLU B 1 74  ? 6.169   32.869  23.878  1.00 38.24  ? 83   GLU B OE2 1 
ATOM   5541  N  N   . LEU B 1 75  ? 8.100   35.278  28.875  1.00 22.68  ? 84   LEU B N   1 
ATOM   5542  C  CA  . LEU B 1 75  ? 8.884   34.797  30.015  1.00 22.07  ? 84   LEU B CA  1 
ATOM   5543  C  C   . LEU B 1 75  ? 9.160   33.265  29.917  1.00 24.95  ? 84   LEU B C   1 
ATOM   5544  O  O   . LEU B 1 75  ? 8.221   32.461  29.733  1.00 26.77  ? 84   LEU B O   1 
ATOM   5545  C  CB  . LEU B 1 75  ? 8.106   35.090  31.294  1.00 23.88  ? 84   LEU B CB  1 
ATOM   5546  C  CG  . LEU B 1 75  ? 8.796   34.612  32.590  1.00 24.97  ? 84   LEU B CG  1 
ATOM   5547  C  CD1 . LEU B 1 75  ? 10.126  35.359  32.894  1.00 25.77  ? 84   LEU B CD1 1 
ATOM   5548  C  CD2 . LEU B 1 75  ? 7.841   34.871  33.740  1.00 23.33  ? 84   LEU B CD2 1 
ATOM   5549  N  N   . GLN B 1 76  ? 10.407  32.892  30.036  1.00 22.86  ? 85   GLN B N   1 
ATOM   5550  C  CA  . GLN B 1 76  ? 10.854  31.497  29.910  1.00 25.65  ? 85   GLN B CA  1 
ATOM   5551  C  C   . GLN B 1 76  ? 11.163  30.876  31.206  1.00 29.15  ? 85   GLN B C   1 
ATOM   5552  O  O   . GLN B 1 76  ? 10.825  29.706  31.370  1.00 29.31  ? 85   GLN B O   1 
ATOM   5553  C  CB  . GLN B 1 76  ? 12.137  31.401  29.087  1.00 28.76  ? 85   GLN B CB  1 
ATOM   5554  C  CG  . GLN B 1 76  ? 12.002  32.083  27.714  1.00 30.85  ? 85   GLN B CG  1 
ATOM   5555  C  CD  . GLN B 1 76  ? 10.976  31.370  26.872  1.00 34.90  ? 85   GLN B CD  1 
ATOM   5556  O  OE1 . GLN B 1 76  ? 11.162  30.216  26.485  1.00 36.42  ? 85   GLN B OE1 1 
ATOM   5557  N  NE2 . GLN B 1 76  ? 9.878   32.038  26.526  1.00 28.66  ? 85   GLN B NE2 1 
ATOM   5558  N  N   . SER B 1 77  ? 11.801  31.602  32.142  1.00 25.28  ? 86   SER B N   1 
ATOM   5559  C  CA  . SER B 1 77  ? 12.236  30.981  33.393  1.00 25.02  ? 86   SER B CA  1 
ATOM   5560  C  C   . SER B 1 77  ? 12.728  32.003  34.356  1.00 26.47  ? 86   SER B C   1 
ATOM   5561  O  O   . SER B 1 77  ? 12.916  33.179  33.963  1.00 25.30  ? 86   SER B O   1 
ATOM   5562  C  CB  . SER B 1 77  ? 13.389  30.029  33.110  1.00 25.36  ? 86   SER B CB  1 
ATOM   5563  O  OG  . SER B 1 77  ? 14.513  30.731  32.598  1.00 28.88  ? 86   SER B OG  1 
ATOM   5564  N  N   . ILE B 1 78  ? 12.908  31.619  35.631  1.00 24.58  ? 87   ILE B N   1 
ATOM   5565  C  CA  . ILE B 1 78  ? 13.452  32.532  36.625  1.00 23.29  ? 87   ILE B CA  1 
ATOM   5566  C  C   . ILE B 1 78  ? 14.656  31.811  37.257  1.00 28.03  ? 87   ILE B C   1 
ATOM   5567  O  O   . ILE B 1 78  ? 14.477  30.717  37.754  1.00 24.22  ? 87   ILE B O   1 
ATOM   5568  C  CB  . ILE B 1 78  ? 12.456  32.935  37.746  1.00 25.03  ? 87   ILE B CB  1 
ATOM   5569  C  CG1 . ILE B 1 78  ? 11.237  33.716  37.165  1.00 24.93  ? 87   ILE B CG1 1 
ATOM   5570  C  CG2 . ILE B 1 78  ? 13.225  33.775  38.822  1.00 23.13  ? 87   ILE B CG2 1 
ATOM   5571  C  CD1 . ILE B 1 78  ? 10.224  34.177  38.213  1.00 26.33  ? 87   ILE B CD1 1 
ATOM   5572  N  N   . LYS B 1 79  ? 15.860  32.401  37.219  1.00 24.80  ? 88   LYS B N   1 
ATOM   5573  C  CA  . LYS B 1 79  ? 16.992  31.772  37.857  1.00 24.28  ? 88   LYS B CA  1 
ATOM   5574  C  C   . LYS B 1 79  ? 17.083  32.364  39.243  1.00 27.51  ? 88   LYS B C   1 
ATOM   5575  O  O   . LYS B 1 79  ? 16.956  33.588  39.403  1.00 27.17  ? 88   LYS B O   1 
ATOM   5576  C  CB  . LYS B 1 79  ? 18.288  32.022  37.044  1.00 29.95  ? 88   LYS B CB  1 
ATOM   5577  C  CG  . LYS B 1 79  ? 19.522  31.375  37.694  1.00 40.18  ? 88   LYS B CG  1 
ATOM   5578  C  CD  . LYS B 1 79  ? 20.672  31.079  36.645  1.00 49.21  ? 88   LYS B CD  1 
ATOM   5579  C  CE  . LYS B 1 79  ? 21.257  32.303  35.973  1.00 49.49  ? 88   LYS B CE  1 
ATOM   5580  N  NZ  . LYS B 1 79  ? 21.445  33.448  36.910  1.00 50.43  ? 88   LYS B NZ  1 
ATOM   5581  N  N   . ILE B 1 80  ? 17.274  31.522  40.277  1.00 22.66  ? 89   ILE B N   1 
ATOM   5582  C  CA  . ILE B 1 80  ? 17.407  32.002  41.670  1.00 23.75  ? 89   ILE B CA  1 
ATOM   5583  C  C   . ILE B 1 80  ? 18.887  32.029  41.956  1.00 24.37  ? 89   ILE B C   1 
ATOM   5584  O  O   . ILE B 1 80  ? 19.525  30.973  41.911  1.00 28.86  ? 89   ILE B O   1 
ATOM   5585  C  CB  . ILE B 1 80  ? 16.613  30.979  42.544  1.00 25.90  ? 89   ILE B CB  1 
ATOM   5586  C  CG1 . ILE B 1 80  ? 15.110  31.041  42.117  1.00 29.87  ? 89   ILE B CG1 1 
ATOM   5587  C  CG2 . ILE B 1 80  ? 16.837  31.309  44.012  1.00 27.93  ? 89   ILE B CG2 1 
ATOM   5588  C  CD1 . ILE B 1 80  ? 14.220  29.967  42.794  1.00 34.92  ? 89   ILE B CD1 1 
ATOM   5589  N  N   . ASN B 1 81  ? 19.447  33.182  42.203  1.00 25.75  ? 90   ASN B N   1 
ATOM   5590  C  CA  . ASN B 1 81  ? 20.890  33.267  42.362  1.00 28.08  ? 90   ASN B CA  1 
ATOM   5591  C  C   . ASN B 1 81  ? 21.310  33.128  43.835  1.00 28.37  ? 90   ASN B C   1 
ATOM   5592  O  O   . ASN B 1 81  ? 21.390  34.135  44.525  1.00 29.41  ? 90   ASN B O   1 
ATOM   5593  C  CB  . ASN B 1 81  ? 21.374  34.607  41.784  1.00 25.25  ? 90   ASN B CB  1 
ATOM   5594  C  CG  . ASN B 1 81  ? 20.866  34.836  40.362  1.00 24.12  ? 90   ASN B CG  1 
ATOM   5595  O  OD1 . ASN B 1 81  ? 20.860  33.900  39.563  1.00 24.77  ? 90   ASN B OD1 1 
ATOM   5596  N  ND2 . ASN B 1 81  ? 20.400  36.039  40.005  1.00 22.80  ? 90   ASN B ND2 1 
ATOM   5597  N  N   . GLY B 1 82  ? 21.579  31.898  44.295  1.00 33.63  ? 91   GLY B N   1 
ATOM   5598  C  CA  . GLY B 1 82  ? 21.982  31.694  45.685  1.00 36.31  ? 91   GLY B CA  1 
ATOM   5599  C  C   . GLY B 1 82  ? 23.489  31.714  45.849  1.00 39.72  ? 91   GLY B C   1 
ATOM   5600  O  O   . GLY B 1 82  ? 24.223  31.653  44.865  1.00 40.48  ? 91   GLY B O   1 
ATOM   5601  N  N   . LYS B 1 83  ? 23.967  31.821  47.093  1.00 41.00  ? 92   LYS B N   1 
ATOM   5602  C  CA  . LYS B 1 83  ? 25.412  31.816  47.387  1.00 46.29  ? 92   LYS B CA  1 
ATOM   5603  C  C   . LYS B 1 83  ? 26.030  30.415  47.294  1.00 51.31  ? 92   LYS B C   1 
ATOM   5604  O  O   . LYS B 1 83  ? 27.253  30.315  47.295  1.00 54.23  ? 92   LYS B O   1 
ATOM   5605  C  CB  . LYS B 1 83  ? 25.675  32.382  48.777  1.00 47.89  ? 92   LYS B CB  1 
ATOM   5606  C  CG  . LYS B 1 83  ? 25.395  33.857  48.815  1.00 54.70  ? 92   LYS B CG  1 
ATOM   5607  C  CD  . LYS B 1 83  ? 25.501  34.455  50.199  1.00 61.25  ? 92   LYS B CD  1 
ATOM   5608  C  CE  . LYS B 1 83  ? 24.971  35.879  50.159  1.00 63.51  ? 92   LYS B CE  1 
ATOM   5609  N  NZ  . LYS B 1 83  ? 24.467  36.318  51.484  1.00 64.46  ? 92   LYS B NZ  1 
ATOM   5610  N  N   . ASP B 1 84  ? 25.231  29.346  47.211  1.00 54.37  ? 93   ASP B N   1 
ATOM   5611  C  CA  . ASP B 1 84  ? 25.805  27.991  47.112  1.00 62.97  ? 93   ASP B CA  1 
ATOM   5612  C  C   . ASP B 1 84  ? 25.417  27.408  45.809  1.00 66.23  ? 93   ASP B C   1 
ATOM   5613  O  O   . ASP B 1 84  ? 26.255  26.977  45.027  1.00 68.22  ? 93   ASP B O   1 
ATOM   5614  C  CB  . ASP B 1 84  ? 25.275  27.014  48.184  1.00 65.61  ? 93   ASP B CB  1 
ATOM   5615  C  CG  . ASP B 1 84  ? 25.431  27.489  49.598  1.00 70.35  ? 93   ASP B CG  1 
ATOM   5616  O  OD1 . ASP B 1 84  ? 24.427  27.445  50.350  1.00 72.06  ? 93   ASP B OD1 1 
ATOM   5617  O  OD2 . ASP B 1 84  ? 26.548  27.911  49.958  1.00 71.27  ? 93   ASP B OD2 1 
ATOM   5618  N  N   . GLU B 1 85  ? 24.130  27.379  45.575  1.00 66.17  ? 94   GLU B N   1 
ATOM   5619  C  CA  . GLU B 1 85  ? 23.623  26.808  44.355  1.00 66.05  ? 94   GLU B CA  1 
ATOM   5620  C  C   . GLU B 1 85  ? 22.792  27.789  43.569  1.00 63.08  ? 94   GLU B C   1 
ATOM   5621  O  O   . GLU B 1 85  ? 22.155  28.688  44.114  1.00 61.37  ? 94   GLU B O   1 
ATOM   5622  C  CB  . GLU B 1 85  ? 22.753  25.618  44.683  1.00 67.72  ? 94   GLU B CB  1 
ATOM   5623  C  CG  . GLU B 1 85  ? 21.758  25.964  45.771  1.00 77.30  ? 94   GLU B CG  1 
ATOM   5624  C  CD  . GLU B 1 85  ? 21.157  24.737  46.414  1.00 84.63  ? 94   GLU B CD  1 
ATOM   5625  O  OE1 . GLU B 1 85  ? 20.429  24.001  45.721  1.00 86.89  ? 94   GLU B OE1 1 
ATOM   5626  O  OE2 . GLU B 1 85  ? 21.420  24.518  47.612  1.00 87.28  ? 94   GLU B OE2 1 
ATOM   5627  N  N   . GLN B 1 86  ? 22.832  27.606  42.284  1.00 57.72  ? 95   GLN B N   1 
ATOM   5628  C  CA  . GLN B 1 86  ? 22.064  28.365  41.347  1.00 53.74  ? 95   GLN B CA  1 
ATOM   5629  C  C   . GLN B 1 86  ? 20.922  27.400  41.058  1.00 54.05  ? 95   GLN B C   1 
ATOM   5630  O  O   . GLN B 1 86  ? 21.162  26.178  41.065  1.00 54.28  ? 95   GLN B O   1 
ATOM   5631  C  CB  . GLN B 1 86  ? 22.924  28.680  40.118  1.00 54.26  ? 95   GLN B CB  1 
ATOM   5632  C  CG  . GLN B 1 86  ? 24.359  29.200  40.498  1.00 51.11  ? 95   GLN B CG  1 
ATOM   5633  C  CD  . GLN B 1 86  ? 24.261  30.239  41.590  1.00 51.58  ? 95   GLN B CD  1 
ATOM   5634  O  OE1 . GLN B 1 86  ? 23.253  30.974  41.693  1.00 46.27  ? 95   GLN B OE1 1 
ATOM   5635  N  NE2 . GLN B 1 86  ? 25.267  30.299  42.475  1.00 48.31  ? 95   GLN B NE2 1 
ATOM   5636  N  N   . LYS B 1 87  ? 19.723  27.881  40.841  1.00 46.97  ? 96   LYS B N   1 
ATOM   5637  C  CA  . LYS B 1 87  ? 18.595  27.003  40.604  1.00 39.48  ? 96   LYS B CA  1 
ATOM   5638  C  C   . LYS B 1 87  ? 17.690  27.719  39.594  1.00 39.51  ? 96   LYS B C   1 
ATOM   5639  O  O   . LYS B 1 87  ? 17.603  28.933  39.671  1.00 35.92  ? 96   LYS B O   1 
ATOM   5640  C  CB  . LYS B 1 87  ? 17.811  26.786  41.902  1.00 40.72  ? 96   LYS B CB  1 
ATOM   5641  C  CG  . LYS B 1 87  ? 16.431  26.223  41.651  1.00 50.00  ? 96   LYS B CG  1 
ATOM   5642  C  CD  . LYS B 1 87  ? 15.529  26.450  42.847  1.00 59.95  ? 96   LYS B CD  1 
ATOM   5643  C  CE  . LYS B 1 87  ? 14.384  25.479  42.883  1.00 60.94  ? 96   LYS B CE  1 
ATOM   5644  N  NZ  . LYS B 1 87  ? 13.385  25.902  43.894  1.00 61.11  ? 96   LYS B NZ  1 
ATOM   5645  N  N   . VAL B 1 88  ? 17.023  26.999  38.700  1.00 34.54  ? 97   VAL B N   1 
ATOM   5646  C  CA  . VAL B 1 88  ? 16.184  27.619  37.703  1.00 33.02  ? 97   VAL B CA  1 
ATOM   5647  C  C   . VAL B 1 88  ? 14.765  27.139  37.748  1.00 34.55  ? 97   VAL B C   1 
ATOM   5648  O  O   . VAL B 1 88  ? 14.545  25.926  37.745  1.00 34.21  ? 97   VAL B O   1 
ATOM   5649  C  CB  . VAL B 1 88  ? 16.775  27.300  36.326  1.00 31.12  ? 97   VAL B CB  1 
ATOM   5650  C  CG1 . VAL B 1 88  ? 15.884  27.873  35.221  1.00 33.96  ? 97   VAL B CG1 1 
ATOM   5651  C  CG2 . VAL B 1 88  ? 18.183  27.844  36.232  1.00 32.64  ? 97   VAL B CG2 1 
ATOM   5652  N  N   . LEU B 1 89  ? 13.793  28.055  37.795  1.00 28.94  ? 98   LEU B N   1 
ATOM   5653  C  CA  . LEU B 1 89  ? 12.382  27.681  37.744  1.00 27.23  ? 98   LEU B CA  1 
ATOM   5654  C  C   . LEU B 1 89  ? 12.022  27.757  36.282  1.00 31.30  ? 98   LEU B C   1 
ATOM   5655  O  O   . LEU B 1 89  ? 12.027  28.848  35.704  1.00 31.40  ? 98   LEU B O   1 
ATOM   5656  C  CB  . LEU B 1 89  ? 11.501  28.648  38.520  1.00 22.95  ? 98   LEU B CB  1 
ATOM   5657  C  CG  . LEU B 1 89  ? 11.884  28.745  39.972  1.00 30.13  ? 98   LEU B CG  1 
ATOM   5658  C  CD1 . LEU B 1 89  ? 11.029  29.769  40.710  1.00 27.30  ? 98   LEU B CD1 1 
ATOM   5659  C  CD2 . LEU B 1 89  ? 11.668  27.338  40.623  1.00 32.03  ? 98   LEU B CD2 1 
ATOM   5660  N  N   . ASN B 1 90  ? 11.729  26.628  35.652  1.00 32.28  ? 99   ASN B N   1 
ATOM   5661  C  CA  . ASN B 1 90  ? 11.383  26.636  34.252  1.00 28.52  ? 99   ASN B CA  1 
ATOM   5662  C  C   . ASN B 1 90  ? 9.886   26.878  34.093  1.00 27.36  ? 99   ASN B C   1 
ATOM   5663  O  O   . ASN B 1 90  ? 9.172   27.106  35.076  1.00 27.88  ? 99   ASN B O   1 
ATOM   5664  C  CB  . ASN B 1 90  ? 11.779  25.273  33.581  1.00 34.28  ? 99   ASN B CB  1 
ATOM   5665  C  CG  . ASN B 1 90  ? 11.054  24.033  34.152  1.00 41.12  ? 99   ASN B CG  1 
ATOM   5666  O  OD1 . ASN B 1 90  ? 9.956   24.098  34.717  1.00 38.79  ? 99   ASN B OD1 1 
ATOM   5667  N  ND2 . ASN B 1 90  ? 11.646  22.851  34.080  1.00 45.14  ? 99   ASN B ND2 1 
ATOM   5668  N  N   . LYS B 1 91  ? 9.394   26.807  32.859  1.00 27.98  ? 100  LYS B N   1 
ATOM   5669  C  CA  . LYS B 1 91  ? 7.992   27.086  32.613  1.00 30.76  ? 100  LYS B CA  1 
ATOM   5670  C  C   . LYS B 1 91  ? 7.047   26.211  33.384  1.00 32.11  ? 100  LYS B C   1 
ATOM   5671  O  O   . LYS B 1 91  ? 6.075   26.696  33.964  1.00 33.03  ? 100  LYS B O   1 
ATOM   5672  C  CB  . LYS B 1 91  ? 7.669   26.912  31.145  1.00 34.24  ? 100  LYS B CB  1 
ATOM   5673  C  CG  . LYS B 1 91  ? 8.154   28.056  30.322  1.00 45.05  ? 100  LYS B CG  1 
ATOM   5674  C  CD  . LYS B 1 91  ? 8.134   27.652  28.877  1.00 52.10  ? 100  LYS B CD  1 
ATOM   5675  C  CE  . LYS B 1 91  ? 8.051   28.855  28.030  1.00 61.82  ? 100  LYS B CE  1 
ATOM   5676  N  NZ  . LYS B 1 91  ? 8.662   28.572  26.708  1.00 66.44  ? 100  LYS B NZ  1 
ATOM   5677  N  N   . GLU B 1 92  ? 7.315   24.907  33.414  1.00 34.42  ? 101  GLU B N   1 
ATOM   5678  C  CA  . GLU B 1 92  ? 6.393   24.027  34.144  1.00 36.47  ? 101  GLU B CA  1 
ATOM   5679  C  C   . GLU B 1 92  ? 6.461   24.338  35.616  1.00 33.80  ? 101  GLU B C   1 
ATOM   5680  O  O   . GLU B 1 92  ? 5.434   24.263  36.313  1.00 33.47  ? 101  GLU B O   1 
ATOM   5681  C  CB  . GLU B 1 92  ? 6.789   22.567  33.867  1.00 43.42  ? 101  GLU B CB  1 
ATOM   5682  C  CG  . GLU B 1 92  ? 5.650   21.572  33.950  1.00 56.00  ? 101  GLU B CG  1 
ATOM   5683  C  CD  . GLU B 1 92  ? 6.122   20.159  33.552  1.00 65.00  ? 101  GLU B CD  1 
ATOM   5684  O  OE1 . GLU B 1 92  ? 6.627   19.427  34.440  1.00 68.77  ? 101  GLU B OE1 1 
ATOM   5685  O  OE2 . GLU B 1 92  ? 5.997   19.808  32.347  1.00 69.64  ? 101  GLU B OE2 1 
ATOM   5686  N  N   . ASP B 1 93  ? 7.654   24.707  36.126  1.00 32.28  ? 102  ASP B N   1 
ATOM   5687  C  CA  . ASP B 1 93  ? 7.762   25.023  37.564  1.00 33.22  ? 102  ASP B CA  1 
ATOM   5688  C  C   . ASP B 1 93  ? 6.974   26.275  37.870  1.00 34.25  ? 102  ASP B C   1 
ATOM   5689  O  O   . ASP B 1 93  ? 6.356   26.394  38.933  1.00 32.58  ? 102  ASP B O   1 
ATOM   5690  C  CB  . ASP B 1 93  ? 9.214   25.296  37.975  1.00 34.90  ? 102  ASP B CB  1 
ATOM   5691  C  CG  . ASP B 1 93  ? 10.139  24.116  37.767  1.00 44.80  ? 102  ASP B CG  1 
ATOM   5692  O  OD1 . ASP B 1 93  ? 11.340  24.340  37.448  1.00 43.51  ? 102  ASP B OD1 1 
ATOM   5693  O  OD2 . ASP B 1 93  ? 9.682   22.975  37.941  1.00 46.25  ? 102  ASP B OD2 1 
ATOM   5694  N  N   . LEU B 1 94  ? 7.027   27.264  36.932  1.00 33.61  ? 103  LEU B N   1 
ATOM   5695  C  CA  . LEU B 1 94  ? 6.331   28.526  37.194  1.00 28.83  ? 103  LEU B CA  1 
ATOM   5696  C  C   . LEU B 1 94  ? 4.824   28.282  37.125  1.00 27.60  ? 103  LEU B C   1 
ATOM   5697  O  O   . LEU B 1 94  ? 4.070   28.827  37.959  1.00 28.30  ? 103  LEU B O   1 
ATOM   5698  C  CB  . LEU B 1 94  ? 6.815   29.612  36.184  1.00 29.25  ? 103  LEU B CB  1 
ATOM   5699  C  CG  . LEU B 1 94  ? 8.321   29.999  36.381  1.00 27.07  ? 103  LEU B CG  1 
ATOM   5700  C  CD1 . LEU B 1 94  ? 8.788   30.852  35.210  1.00 26.37  ? 103  LEU B CD1 1 
ATOM   5701  C  CD2 . LEU B 1 94  ? 8.483   30.768  37.709  1.00 26.20  ? 103  LEU B CD2 1 
ATOM   5702  N  N   . GLU B 1 95  ? 4.373   27.477  36.145  1.00 30.35  ? 104  GLU B N   1 
ATOM   5703  C  CA  . GLU B 1 95  ? 2.938   27.177  36.056  1.00 31.89  ? 104  GLU B CA  1 
ATOM   5704  C  C   . GLU B 1 95  ? 2.481   26.466  37.355  1.00 35.73  ? 104  GLU B C   1 
ATOM   5705  O  O   . GLU B 1 95  ? 1.385   26.759  37.845  1.00 35.45  ? 104  GLU B O   1 
ATOM   5706  C  CB  . GLU B 1 95  ? 2.679   26.352  34.817  1.00 36.06  ? 104  GLU B CB  1 
ATOM   5707  C  CG  . GLU B 1 95  ? 3.033   27.198  33.609  1.00 38.77  ? 104  GLU B CG  1 
ATOM   5708  C  CD  . GLU B 1 95  ? 2.852   26.502  32.297  1.00 48.70  ? 104  GLU B CD  1 
ATOM   5709  O  OE1 . GLU B 1 95  ? 3.080   25.278  32.223  1.00 49.65  ? 104  GLU B OE1 1 
ATOM   5710  O  OE2 . GLU B 1 95  ? 2.485   27.198  31.326  1.00 46.70  ? 104  GLU B OE2 1 
ATOM   5711  N  N   . SER B 1 96  ? 3.322   25.584  37.950  1.00 36.13  ? 105  SER B N   1 
ATOM   5712  C  CA  . SER B 1 96  ? 2.908   24.908  39.200  1.00 37.41  ? 105  SER B CA  1 
ATOM   5713  C  C   . SER B 1 96  ? 2.804   25.863  40.273  1.00 39.39  ? 105  SER B C   1 
ATOM   5714  O  O   . SER B 1 96  ? 2.057   25.628  41.224  1.00 39.04  ? 105  SER B O   1 
ATOM   5715  C  CB  . SER B 1 96  ? 3.921   23.852  39.624  1.00 40.81  ? 105  SER B CB  1 
ATOM   5716  O  OG  . SER B 1 96  ? 4.034   22.927  38.561  1.00 47.34  ? 105  SER B OG  1 
ATOM   5717  N  N   . MET B 1 97  ? 3.559   26.965  40.188  1.00 35.47  ? 106  MET B N   1 
ATOM   5718  C  CA  . MET B 1 97  ? 3.480   27.948  41.259  1.00 33.09  ? 106  MET B CA  1 
ATOM   5719  C  C   . MET B 1 97  ? 2.258   28.897  41.029  1.00 35.82  ? 106  MET B C   1 
ATOM   5720  O  O   . MET B 1 97  ? 2.080   29.843  41.785  1.00 37.88  ? 106  MET B O   1 
ATOM   5721  C  CB  . MET B 1 97  ? 4.821   28.710  41.352  1.00 32.90  ? 106  MET B CB  1 
ATOM   5722  C  CG  . MET B 1 97  ? 5.888   27.883  42.076  1.00 40.98  ? 106  MET B CG  1 
ATOM   5723  S  SD  . MET B 1 97  ? 7.564   28.513  41.866  1.00 46.67  ? 106  MET B SD  1 
ATOM   5724  C  CE  . MET B 1 97  ? 7.659   29.679  43.254  1.00 49.14  ? 106  MET B CE  1 
ATOM   5725  N  N   . GLY B 1 98  ? 1.439   28.618  39.998  1.00 37.65  ? 107  GLY B N   1 
ATOM   5726  C  CA  . GLY B 1 98  ? 0.224   29.392  39.782  1.00 39.74  ? 107  GLY B CA  1 
ATOM   5727  C  C   . GLY B 1 98  ? 0.278   30.479  38.714  1.00 40.17  ? 107  GLY B C   1 
ATOM   5728  O  O   . GLY B 1 98  ? -0.669  31.271  38.616  1.00 39.61  ? 107  GLY B O   1 
ATOM   5729  N  N   . LEU B 1 99  ? 1.339   30.529  37.900  1.00 35.41  ? 108  LEU B N   1 
ATOM   5730  C  CA  . LEU B 1 99  ? 1.420   31.602  36.891  1.00 33.88  ? 108  LEU B CA  1 
ATOM   5731  C  C   . LEU B 1 99  ? 0.869   31.173  35.560  1.00 33.82  ? 108  LEU B C   1 
ATOM   5732  O  O   . LEU B 1 99  ? 0.994   29.999  35.192  1.00 33.30  ? 108  LEU B O   1 
ATOM   5733  C  CB  . LEU B 1 99  ? 2.903   31.985  36.659  1.00 31.58  ? 108  LEU B CB  1 
ATOM   5734  C  CG  . LEU B 1 99  ? 3.613   32.495  37.855  1.00 32.43  ? 108  LEU B CG  1 
ATOM   5735  C  CD1 . LEU B 1 99  ? 4.988   33.142  37.488  1.00 34.58  ? 108  LEU B CD1 1 
ATOM   5736  C  CD2 . LEU B 1 99  ? 2.735   33.523  38.492  1.00 34.89  ? 108  LEU B CD2 1 
ATOM   5737  N  N   . ASN B 1 100 ? 0.263   32.097  34.828  1.00 27.39  ? 109  ASN B N   1 
ATOM   5738  C  CA  . ASN B 1 100 ? -0.162  31.821  33.458  1.00 28.51  ? 109  ASN B CA  1 
ATOM   5739  C  C   . ASN B 1 100 ? 0.848   32.687  32.673  1.00 29.80  ? 109  ASN B C   1 
ATOM   5740  O  O   . ASN B 1 100 ? 0.691   33.911  32.664  1.00 27.25  ? 109  ASN B O   1 
ATOM   5741  C  CB  . ASN B 1 100 ? -1.580  32.248  33.238  1.00 31.42  ? 109  ASN B CB  1 
ATOM   5742  C  CG  . ASN B 1 100 ? -2.398  31.695  34.394  1.00 47.12  ? 109  ASN B CG  1 
ATOM   5743  O  OD1 . ASN B 1 100 ? -2.866  32.443  35.289  1.00 50.75  ? 109  ASN B OD1 1 
ATOM   5744  N  ND2 . ASN B 1 100 ? -2.560  30.364  34.494  1.00 50.79  ? 109  ASN B ND2 1 
ATOM   5745  N  N   . LEU B 1 101 ? 1.862   32.054  32.068  1.00 28.38  ? 110  LEU B N   1 
ATOM   5746  C  CA  . LEU B 1 101 ? 2.973   32.798  31.456  1.00 30.08  ? 110  LEU B CA  1 
ATOM   5747  C  C   . LEU B 1 101 ? 2.559   33.846  30.454  1.00 29.04  ? 110  LEU B C   1 
ATOM   5748  O  O   . LEU B 1 101 ? 3.234   34.870  30.384  1.00 26.89  ? 110  LEU B O   1 
ATOM   5749  C  CB  . LEU B 1 101 ? 4.003   31.839  30.866  1.00 31.13  ? 110  LEU B CB  1 
ATOM   5750  C  CG  . LEU B 1 101 ? 4.517   30.874  31.929  1.00 31.99  ? 110  LEU B CG  1 
ATOM   5751  C  CD1 . LEU B 1 101 ? 5.559   29.966  31.296  1.00 37.89  ? 110  LEU B CD1 1 
ATOM   5752  C  CD2 . LEU B 1 101 ? 5.099   31.625  33.099  1.00 33.49  ? 110  LEU B CD2 1 
ATOM   5753  N  N   . LYS B 1 102 ? 1.497   33.639  29.697  1.00 24.52  ? 111  LYS B N   1 
ATOM   5754  C  CA  . LYS B 1 102 ? 1.095   34.685  28.772  1.00 29.46  ? 111  LYS B CA  1 
ATOM   5755  C  C   . LYS B 1 102 ? 0.731   36.008  29.456  1.00 30.42  ? 111  LYS B C   1 
ATOM   5756  O  O   . LYS B 1 102 ? 0.749   37.049  28.788  1.00 27.20  ? 111  LYS B O   1 
ATOM   5757  C  CB  . LYS B 1 102 ? -0.108  34.245  27.951  1.00 35.81  ? 111  LYS B CB  1 
ATOM   5758  C  CG  . LYS B 1 102 ? 0.254   33.254  26.896  1.00 43.15  ? 111  LYS B CG  1 
ATOM   5759  C  CD  . LYS B 1 102 ? -0.982  32.970  26.039  1.00 56.00  ? 111  LYS B CD  1 
ATOM   5760  C  CE  . LYS B 1 102 ? -0.755  33.347  24.590  1.00 66.13  ? 111  LYS B CE  1 
ATOM   5761  N  NZ  . LYS B 1 102 ? -1.537  34.563  24.200  1.00 69.16  ? 111  LYS B NZ  1 
ATOM   5762  N  N   . ASP B 1 103 ? 0.413   35.992  30.785  1.00 24.18  ? 112  ASP B N   1 
ATOM   5763  C  CA  . ASP B 1 103 ? 0.056   37.224  31.450  1.00 22.30  ? 112  ASP B CA  1 
ATOM   5764  C  C   . ASP B 1 103 ? 1.225   38.218  31.452  1.00 20.51  ? 112  ASP B C   1 
ATOM   5765  O  O   . ASP B 1 103 ? 0.993   39.414  31.654  1.00 23.79  ? 112  ASP B O   1 
ATOM   5766  C  CB  . ASP B 1 103 ? -0.328  36.974  32.926  1.00 22.40  ? 112  ASP B CB  1 
ATOM   5767  C  CG  . ASP B 1 103 ? -1.622  36.171  33.134  1.00 28.09  ? 112  ASP B CG  1 
ATOM   5768  O  OD1 . ASP B 1 103 ? -1.863  35.732  34.252  1.00 26.79  ? 112  ASP B OD1 1 
ATOM   5769  O  OD2 . ASP B 1 103 ? -2.375  35.984  32.168  1.00 25.68  ? 112  ASP B OD2 1 
ATOM   5770  N  N   . TYR B 1 104 ? 2.449   37.732  31.294  1.00 20.87  ? 113  TYR B N   1 
ATOM   5771  C  CA  . TYR B 1 104 ? 3.634   38.597  31.321  1.00 23.46  ? 113  TYR B CA  1 
ATOM   5772  C  C   . TYR B 1 104 ? 4.167   38.968  29.915  1.00 24.43  ? 113  TYR B C   1 
ATOM   5773  O  O   . TYR B 1 104 ? 5.229   39.573  29.829  1.00 23.11  ? 113  TYR B O   1 
ATOM   5774  C  CB  . TYR B 1 104 ? 4.721   37.900  32.160  1.00 22.27  ? 113  TYR B CB  1 
ATOM   5775  C  CG  . TYR B 1 104 ? 4.046   37.492  33.459  1.00 21.04  ? 113  TYR B CG  1 
ATOM   5776  C  CD1 . TYR B 1 104 ? 3.643   36.168  33.671  1.00 28.38  ? 113  TYR B CD1 1 
ATOM   5777  C  CD2 . TYR B 1 104 ? 3.701   38.437  34.414  1.00 23.89  ? 113  TYR B CD2 1 
ATOM   5778  C  CE1 . TYR B 1 104 ? 2.897   35.809  34.798  1.00 28.11  ? 113  TYR B CE1 1 
ATOM   5779  C  CE2 . TYR B 1 104 ? 2.958   38.088  35.551  1.00 25.39  ? 113  TYR B CE2 1 
ATOM   5780  C  CZ  . TYR B 1 104 ? 2.548   36.763  35.723  1.00 31.40  ? 113  TYR B CZ  1 
ATOM   5781  O  OH  . TYR B 1 104 ? 1.745   36.402  36.793  1.00 26.81  ? 113  TYR B OH  1 
ATOM   5782  N  N   . ASP B 1 105 ? 3.439   38.636  28.843  1.00 22.90  ? 114  ASP B N   1 
ATOM   5783  C  CA  . ASP B 1 105 ? 3.912   38.959  27.478  1.00 22.76  ? 114  ASP B CA  1 
ATOM   5784  C  C   . ASP B 1 105 ? 4.049   40.501  27.337  1.00 22.32  ? 114  ASP B C   1 
ATOM   5785  O  O   . ASP B 1 105 ? 3.117   41.231  27.676  1.00 23.18  ? 114  ASP B O   1 
ATOM   5786  C  CB  . ASP B 1 105 ? 2.903   38.432  26.433  1.00 19.28  ? 114  ASP B CB  1 
ATOM   5787  C  CG  . ASP B 1 105 ? 3.012   36.909  26.181  1.00 25.95  ? 114  ASP B CG  1 
ATOM   5788  O  OD1 . ASP B 1 105 ? 3.896   36.256  26.788  1.00 27.24  ? 114  ASP B OD1 1 
ATOM   5789  O  OD2 . ASP B 1 105 ? 2.229   36.386  25.367  1.00 29.16  ? 114  ASP B OD2 1 
ATOM   5790  N  N   . VAL B 1 106 ? 5.200   40.973  26.844  1.00 20.14  ? 115  VAL B N   1 
ATOM   5791  C  CA  . VAL B 1 106 ? 5.442   42.418  26.666  1.00 18.70  ? 115  VAL B CA  1 
ATOM   5792  C  C   . VAL B 1 106 ? 5.680   42.623  25.126  1.00 19.24  ? 115  VAL B C   1 
ATOM   5793  O  O   . VAL B 1 106 ? 6.515   41.922  24.539  1.00 18.91  ? 115  VAL B O   1 
ATOM   5794  C  CB  . VAL B 1 106 ? 6.679   42.855  27.466  1.00 18.76  ? 115  VAL B CB  1 
ATOM   5795  C  CG1 . VAL B 1 106 ? 7.013   44.327  27.143  1.00 17.75  ? 115  VAL B CG1 1 
ATOM   5796  C  CG2 . VAL B 1 106 ? 6.421   42.695  29.000  1.00 18.24  ? 115  VAL B CG2 1 
ATOM   5797  N  N   . THR B 1 107 ? 4.943   43.547  24.538  1.00 19.23  ? 116  THR B N   1 
ATOM   5798  C  CA  . THR B 1 107 ? 5.071   43.790  23.099  1.00 19.06  ? 116  THR B CA  1 
ATOM   5799  C  C   . THR B 1 107 ? 5.968   45.006  22.879  1.00 19.99  ? 116  THR B C   1 
ATOM   5800  O  O   . THR B 1 107 ? 5.766   46.080  23.469  1.00 18.72  ? 116  THR B O   1 
ATOM   5801  C  CB  . THR B 1 107 ? 3.649   44.067  22.507  1.00 21.17  ? 116  THR B CB  1 
ATOM   5802  O  OG1 . THR B 1 107 ? 2.823   42.946  22.831  1.00 23.00  ? 116  THR B OG1 1 
ATOM   5803  C  CG2 . THR B 1 107 ? 3.648   44.195  20.898  1.00 20.19  ? 116  THR B CG2 1 
ATOM   5804  N  N   . GLN B 1 108 ? 6.956   44.808  21.977  1.00 18.79  ? 117  GLN B N   1 
ATOM   5805  C  CA  . GLN B 1 108 ? 7.892   45.853  21.627  1.00 20.20  ? 117  GLN B CA  1 
ATOM   5806  C  C   . GLN B 1 108 ? 7.467   46.443  20.244  1.00 22.58  ? 117  GLN B C   1 
ATOM   5807  O  O   . GLN B 1 108 ? 7.647   45.813  19.221  1.00 22.15  ? 117  GLN B O   1 
ATOM   5808  C  CB  . GLN B 1 108 ? 9.324   45.276  21.582  1.00 19.20  ? 117  GLN B CB  1 
ATOM   5809  C  CG  . GLN B 1 108 ? 10.370  46.459  21.418  1.00 18.18  ? 117  GLN B CG  1 
ATOM   5810  C  CD  . GLN B 1 108 ? 11.742  45.864  21.661  1.00 26.00  ? 117  GLN B CD  1 
ATOM   5811  O  OE1 . GLN B 1 108 ? 12.011  45.268  22.731  1.00 21.39  ? 117  GLN B OE1 1 
ATOM   5812  N  NE2 . GLN B 1 108 ? 12.687  46.054  20.722  1.00 21.28  ? 117  GLN B NE2 1 
ATOM   5813  N  N   . GLU B 1 109 ? 6.875   47.671  20.252  1.00 20.33  ? 118  GLU B N   1 
ATOM   5814  C  CA  . GLU B 1 109 ? 6.439   48.364  19.021  1.00 21.05  ? 118  GLU B CA  1 
ATOM   5815  C  C   . GLU B 1 109 ? 7.581   49.260  18.533  1.00 21.84  ? 118  GLU B C   1 
ATOM   5816  O  O   . GLU B 1 109 ? 8.579   49.380  19.212  1.00 21.57  ? 118  GLU B O   1 
ATOM   5817  C  CB  . GLU B 1 109 ? 5.245   49.265  19.372  1.00 19.34  ? 118  GLU B CB  1 
ATOM   5818  C  CG  . GLU B 1 109 ? 4.149   48.466  20.066  1.00 26.48  ? 118  GLU B CG  1 
ATOM   5819  C  CD  . GLU B 1 109 ? 3.282   47.690  19.099  1.00 38.52  ? 118  GLU B CD  1 
ATOM   5820  O  OE1 . GLU B 1 109 ? 3.602   47.645  17.894  1.00 40.36  ? 118  GLU B OE1 1 
ATOM   5821  O  OE2 . GLU B 1 109 ? 2.257   47.122  19.556  1.00 39.40  ? 118  GLU B OE2 1 
ATOM   5822  N  N   . PHE B 1 110 ? 7.437   49.883  17.357  1.00 22.18  ? 119  PHE B N   1 
ATOM   5823  C  CA  . PHE B 1 110 ? 8.475   50.806  16.893  1.00 23.47  ? 119  PHE B CA  1 
ATOM   5824  C  C   . PHE B 1 110 ? 7.836   52.026  16.253  1.00 22.92  ? 119  PHE B C   1 
ATOM   5825  O  O   . PHE B 1 110 ? 6.681   51.988  15.862  1.00 21.89  ? 119  PHE B O   1 
ATOM   5826  C  CB  . PHE B 1 110 ? 9.442   50.116  15.888  1.00 22.10  ? 119  PHE B CB  1 
ATOM   5827  C  CG  . PHE B 1 110 ? 8.722   49.477  14.721  1.00 26.29  ? 119  PHE B CG  1 
ATOM   5828  C  CD1 . PHE B 1 110 ? 8.347   48.138  14.763  1.00 31.48  ? 119  PHE B CD1 1 
ATOM   5829  C  CD2 . PHE B 1 110 ? 8.403   50.224  13.577  1.00 28.20  ? 119  PHE B CD2 1 
ATOM   5830  C  CE1 . PHE B 1 110 ? 7.658   47.542  13.673  1.00 35.01  ? 119  PHE B CE1 1 
ATOM   5831  C  CE2 . PHE B 1 110 ? 7.718   49.635  12.499  1.00 32.13  ? 119  PHE B CE2 1 
ATOM   5832  C  CZ  . PHE B 1 110 ? 7.352   48.295  12.554  1.00 32.76  ? 119  PHE B CZ  1 
ATOM   5833  N  N   . ILE B 1 111 ? 8.579   53.132  16.190  1.00 24.38  ? 120  ILE B N   1 
ATOM   5834  C  CA  . ILE B 1 111 ? 8.111   54.367  15.533  1.00 26.48  ? 120  ILE B CA  1 
ATOM   5835  C  C   . ILE B 1 111 ? 7.736   54.098  14.078  1.00 31.18  ? 120  ILE B C   1 
ATOM   5836  O  O   . ILE B 1 111 ? 8.527   53.435  13.395  1.00 31.82  ? 120  ILE B O   1 
ATOM   5837  C  CB  . ILE B 1 111 ? 9.266   55.369  15.640  1.00 28.33  ? 120  ILE B CB  1 
ATOM   5838  C  CG1 . ILE B 1 111 ? 9.335   55.890  17.097  1.00 29.13  ? 120  ILE B CG1 1 
ATOM   5839  C  CG2 . ILE B 1 111 ? 9.034   56.529  14.593  1.00 29.32  ? 120  ILE B CG2 1 
ATOM   5840  C  CD1 . ILE B 1 111 ? 10.655  56.614  17.382  1.00 30.75  ? 120  ILE B CD1 1 
ATOM   5841  N  N   . ILE B 1 112 ? 6.568   54.558  13.619  1.00 35.18  ? 121  ILE B N   1 
ATOM   5842  C  CA  . ILE B 1 112 ? 6.143   54.312  12.245  1.00 47.24  ? 121  ILE B CA  1 
ATOM   5843  C  C   . ILE B 1 112 ? 6.253   55.623  11.413  1.00 57.90  ? 121  ILE B C   1 
ATOM   5844  O  O   . ILE B 1 112 ? 6.558   56.693  11.937  1.00 58.52  ? 121  ILE B O   1 
ATOM   5845  C  CB  . ILE B 1 112 ? 4.707   53.714  12.174  1.00 53.07  ? 121  ILE B CB  1 
ATOM   5846  C  CG1 . ILE B 1 112 ? 3.689   54.713  12.650  1.00 53.95  ? 121  ILE B CG1 1 
ATOM   5847  C  CG2 . ILE B 1 112 ? 4.582   52.443  13.025  1.00 54.30  ? 121  ILE B CG2 1 
ATOM   5848  C  CD1 . ILE B 1 112 ? 2.277   54.163  12.566  1.00 53.49  ? 121  ILE B CD1 1 
ATOM   5849  N  N   . SER B 1 113 ? 6.032   55.499  10.102  1.00 69.79  ? 122  SER B N   1 
ATOM   5850  C  CA  . SER B 1 113 ? 6.081   56.598  9.137   1.00 82.40  ? 122  SER B CA  1 
ATOM   5851  C  C   . SER B 1 113 ? 4.698   56.854  8.554   1.00 90.70  ? 122  SER B C   1 
ATOM   5852  O  O   . SER B 1 113 ? 4.095   55.952  7.981   1.00 94.12  ? 122  SER B O   1 
ATOM   5853  C  CB  . SER B 1 113 ? 7.051   56.265  8.007   1.00 84.33  ? 122  SER B CB  1 
ATOM   5854  O  OG  . SER B 1 113 ? 8.329   55.959  8.532   1.00 85.90  ? 122  SER B OG  1 
ATOM   5855  N  N   . ASP B 1 114 ? 4.184   58.080  8.706   1.00 99.32  ? 123  ASP B N   1 
ATOM   5856  C  CA  . ASP B 1 114 ? 2.881   58.431  8.134   1.00 110.91 ? 123  ASP B CA  1 
ATOM   5857  C  C   . ASP B 1 114 ? 3.035   58.491  6.617   1.00 117.26 ? 123  ASP B C   1 
ATOM   5858  O  O   . ASP B 1 114 ? 2.079   58.692  5.867   1.00 119.23 ? 123  ASP B O   1 
ATOM   5859  C  CB  . ASP B 1 114 ? 2.412   59.799  8.668   1.00 114.30 ? 123  ASP B CB  1 
ATOM   5860  C  CG  . ASP B 1 114 ? 0.956   59.818  9.083   0.00 0.00   ? 123  ASP B CG  1 
ATOM   5861  O  OD1 . ASP B 1 114 ? 0.511   58.848  9.735   0.00 0.00   ? 123  ASP B OD1 1 
ATOM   5862  O  OD2 . ASP B 1 114 ? 0.265   60.808  8.766   0.00 0.00   ? 123  ASP B OD2 1 
ATOM   5863  N  N   . ALA B 1 115 ? 4.286   58.301  6.191   1.00 120.92 ? 124  ALA B N   1 
ATOM   5864  C  CA  . ALA B 1 115 ? 4.761   58.333  4.824   1.00 123.69 ? 124  ALA B CA  1 
ATOM   5865  C  C   . ALA B 1 115 ? 4.415   57.104  3.986   1.00 125.71 ? 124  ALA B C   1 
ATOM   5866  O  O   . ALA B 1 115 ? 4.978   56.947  2.902   1.00 126.94 ? 124  ALA B O   1 
ATOM   5867  C  CB  . ALA B 1 115 ? 6.261   58.514  4.855   1.00 124.63 ? 124  ALA B CB  1 
ATOM   5868  N  N   . ASN B 1 116 ? 3.503   56.232  4.449   1.00 128.30 ? 125  ASN B N   1 
ATOM   5869  C  CA  . ASN B 1 116 ? 3.165   55.083  3.610   1.00 132.21 ? 125  ASN B CA  1 
ATOM   5870  C  C   . ASN B 1 116 ? 2.526   55.584  2.302   1.00 134.06 ? 125  ASN B C   1 
ATOM   5871  O  O   . ASN B 1 116 ? 2.748   54.979  1.255   1.00 135.53 ? 125  ASN B O   1 
ATOM   5872  C  CB  . ASN B 1 116 ? 2.222   54.118  4.332   1.00 133.13 ? 125  ASN B CB  1 
ATOM   5873  C  CG  . ASN B 1 116 ? 2.512   52.683  3.968   0.00 0.00   ? 125  ASN B CG  1 
ATOM   5874  O  OD1 . ASN B 1 116 ? 3.311   52.023  4.640   0.00 0.00   ? 125  ASN B OD1 1 
ATOM   5875  N  ND2 . ASN B 1 116 ? 1.924   52.127  2.908   0.00 0.00   ? 125  ASN B ND2 1 
ATOM   5876  N  N   . SER B 1 117 ? 1.740   56.683  2.366   0.00 0.00   ? 126  SER B N   1 
ATOM   5877  C  CA  . SER B 1 117 ? 1.118   57.285  1.179   0.00 0.00   ? 126  SER B CA  1 
ATOM   5878  C  C   . SER B 1 117 ? 0.214   58.487  1.505   0.00 0.00   ? 126  SER B C   1 
ATOM   5879  O  O   . SER B 1 117 ? -0.730  58.372  2.283   0.00 0.00   ? 126  SER B O   1 
ATOM   5880  C  CB  . SER B 1 117 ? 0.308   56.247  0.406   0.00 0.00   ? 126  SER B CB  1 
ATOM   5881  O  OG  . SER B 1 117 ? -0.541  55.499  1.260   0.00 0.00   ? 126  SER B OG  1 
ATOM   5882  N  N   . THR B 1 118 ? 0.524   59.639  0.893   0.00 0.00   ? 127  THR B N   1 
ATOM   5883  C  CA  . THR B 1 118 ? -0.202  60.910  1.016   0.00 0.00   ? 127  THR B CA  1 
ATOM   5884  C  C   . THR B 1 118 ? 0.018   61.637  -0.307  0.00 0.00   ? 127  THR B C   1 
ATOM   5885  O  O   . THR B 1 118 ? -0.897  61.884  -1.089  0.00 0.00   ? 127  THR B O   1 
ATOM   5886  C  CB  . THR B 1 118 ? 0.373   61.768  2.166   0.00 0.00   ? 127  THR B CB  1 
ATOM   5887  O  OG1 . THR B 1 118 ? 1.744   61.410  2.358   0.00 0.00   ? 127  THR B OG1 1 
ATOM   5888  C  CG2 . THR B 1 118 ? -0.379  61.578  3.468   0.00 0.00   ? 127  THR B CG2 1 
ATOM   5889  N  N   . LYS B 1 119 ? 1.288   61.958  -0.517  0.00 0.00   ? 128  LYS B N   1 
ATOM   5890  C  CA  . LYS B 1 119 ? 1.931   62.618  -1.644  0.00 0.00   ? 128  LYS B CA  1 
ATOM   5891  C  C   . LYS B 1 119 ? 3.371   62.609  -1.174  0.00 0.00   ? 128  LYS B C   1 
ATOM   5892  O  O   . LYS B 1 119 ? 3.631   63.055  -0.057  0.00 0.00   ? 128  LYS B O   1 
ATOM   5893  C  CB  . LYS B 1 119 ? 1.410   64.045  -1.876  0.00 0.00   ? 128  LYS B CB  1 
ATOM   5894  C  CG  . LYS B 1 119 ? 1.272   64.364  -3.363  0.00 0.00   ? 128  LYS B CG  1 
ATOM   5895  C  CD  . LYS B 1 119 ? 2.054   65.612  -3.749  0.00 0.00   ? 128  LYS B CD  1 
ATOM   5896  C  CE  . LYS B 1 119 ? 2.489   65.560  -5.194  0.00 0.00   ? 128  LYS B CE  1 
ATOM   5897  N  NZ  . LYS B 1 119 ? 3.486   66.623  -5.500  0.00 0.00   ? 128  LYS B NZ  1 
ATOM   5898  N  N   . ALA B 1 120 ? 4.307   62.115  -1.974  0.00 0.00   ? 129  ALA B N   1 
ATOM   5899  C  CA  . ALA B 1 120 ? 5.657   62.009  -1.442  0.00 0.00   ? 129  ALA B CA  1 
ATOM   5900  C  C   . ALA B 1 120 ? 6.643   63.102  -1.815  0.00 0.00   ? 129  ALA B C   1 
ATOM   5901  O  O   . ALA B 1 120 ? 7.408   62.959  -2.768  0.00 0.00   ? 129  ALA B O   1 
ATOM   5902  C  CB  . ALA B 1 120 ? 6.235   60.654  -1.815  0.00 0.00   ? 129  ALA B CB  1 
ATOM   5903  N  N   . VAL B 1 121 ? 6.614   64.204  -1.064  0.00 0.00   ? 130  VAL B N   1 
ATOM   5904  C  CA  . VAL B 1 121 ? 7.586   65.272  -1.244  0.00 0.00   ? 130  VAL B CA  1 
ATOM   5905  C  C   . VAL B 1 121 ? 8.641   64.948  -0.196  0.00 0.00   ? 130  VAL B C   1 
ATOM   5906  O  O   . VAL B 1 121 ? 8.287   64.405  0.853   0.00 0.00   ? 130  VAL B O   1 
ATOM   5907  C  CB  . VAL B 1 121 ? 6.990   66.673  -1.022  0.00 0.00   ? 130  VAL B CB  1 
ATOM   5908  C  CG1 . VAL B 1 121 ? 7.871   67.788  -0.453  0.00 0.00   ? 130  VAL B CG1 1 
ATOM   5909  C  CG2 . VAL B 1 121 ? 5.752   67.099  -1.810  0.00 0.00   ? 130  VAL B CG2 1 
ATOM   5910  N  N   . ASN B 1 122 ? 9.912   65.263  -0.442  1.00 158.51 ? 131  ASN B N   1 
ATOM   5911  C  CA  . ASN B 1 122 ? 10.945  64.931  0.536   1.00 158.55 ? 131  ASN B CA  1 
ATOM   5912  C  C   . ASN B 1 122 ? 10.856  65.728  1.853   1.00 158.39 ? 131  ASN B C   1 
ATOM   5913  O  O   . ASN B 1 122 ? 11.891  65.992  2.456   1.00 158.70 ? 131  ASN B O   1 
ATOM   5914  C  CB  . ASN B 1 122 ? 12.332  65.110  -0.082  1.00 158.72 ? 131  ASN B CB  1 
ATOM   5915  C  CG  . ASN B 1 122 ? 12.878  63.831  -0.673  0.00 0.00   ? 131  ASN B CG  1 
ATOM   5916  O  OD1 . ASN B 1 122 ? 12.351  63.342  -1.672  0.00 0.00   ? 131  ASN B OD1 1 
ATOM   5917  N  ND2 . ASN B 1 122 ? 13.940  63.242  -0.132  0.00 0.00   ? 131  ASN B ND2 1 
ATOM   5918  N  N   . GLU B 1 123 ? 9.654   66.143  2.289   1.00 156.80 ? 132  GLU B N   1 
ATOM   5919  C  CA  . GLU B 1 123 ? 9.514   66.820  3.582   1.00 152.75 ? 132  GLU B CA  1 
ATOM   5920  C  C   . GLU B 1 123 ? 8.442   66.090  4.374   1.00 149.66 ? 132  GLU B C   1 
ATOM   5921  O  O   . GLU B 1 123 ? 8.639   65.842  5.563   1.00 148.32 ? 132  GLU B O   1 
ATOM   5922  C  CB  . GLU B 1 123 ? 9.186   68.310  3.447   1.00 150.84 ? 132  GLU B CB  1 
ATOM   5923  C  CG  . GLU B 1 123 ? 10.217  69.139  4.204   0.00 0.00   ? 132  GLU B CG  1 
ATOM   5924  C  CD  . GLU B 1 123 ? 9.629   69.951  5.349   0.00 0.00   ? 132  GLU B CD  1 
ATOM   5925  O  OE1 . GLU B 1 123 ? 8.411   69.864  5.571   0.00 0.00   ? 132  GLU B OE1 1 
ATOM   5926  O  OE2 . GLU B 1 123 ? 10.402  70.682  6.032   0.00 0.00   ? 132  GLU B OE2 1 
ATOM   5927  N  N   . TYR B 1 124 ? 7.307   65.731  3.741   1.00 146.00 ? 133  TYR B N   1 
ATOM   5928  C  CA  . TYR B 1 124 ? 6.340   64.932  4.492   1.00 140.12 ? 133  TYR B CA  1 
ATOM   5929  C  C   . TYR B 1 124 ? 6.920   63.511  4.529   1.00 135.83 ? 133  TYR B C   1 
ATOM   5930  O  O   . TYR B 1 124 ? 6.351   62.608  5.137   1.00 133.48 ? 133  TYR B O   1 
ATOM   5931  C  CB  . TYR B 1 124 ? 4.945   64.932  3.845   1.00 137.75 ? 133  TYR B CB  1 
ATOM   5932  C  CG  . TYR B 1 124 ? 3.850   64.753  4.876   0.00 0.00   ? 133  TYR B CG  1 
ATOM   5933  C  CD1 . TYR B 1 124 ? 3.390   65.828  5.623   0.00 0.00   ? 133  TYR B CD1 1 
ATOM   5934  C  CD2 . TYR B 1 124 ? 3.283   63.508  5.110   0.00 0.00   ? 133  TYR B CD2 1 
ATOM   5935  C  CE1 . TYR B 1 124 ? 2.396   65.668  6.580   0.00 0.00   ? 133  TYR B CE1 1 
ATOM   5936  C  CE2 . TYR B 1 124 ? 2.288   63.337  6.064   0.00 0.00   ? 133  TYR B CE2 1 
ATOM   5937  C  CZ  . TYR B 1 124 ? 1.846   64.420  6.798   0.00 0.00   ? 133  TYR B CZ  1 
ATOM   5938  O  OH  . TYR B 1 124 ? 0.863   64.259  7.743   0.00 0.00   ? 133  TYR B OH  1 
ATOM   5939  N  N   . MET B 1 125 ? 8.078   63.342  3.848   1.00 130.67 ? 134  MET B N   1 
ATOM   5940  C  CA  . MET B 1 125 ? 8.845   62.108  3.756   1.00 121.77 ? 134  MET B CA  1 
ATOM   5941  C  C   . MET B 1 125 ? 9.197   61.568  5.153   1.00 115.17 ? 134  MET B C   1 
ATOM   5942  O  O   . MET B 1 125 ? 8.576   60.595  5.578   1.00 111.71 ? 134  MET B O   1 
ATOM   5943  C  CB  . MET B 1 125 ? 10.130  62.366  2.949   1.00 117.78 ? 134  MET B CB  1 
ATOM   5944  C  CG  . MET B 1 125 ? 10.542  61.206  2.099   0.00 0.00   ? 134  MET B CG  1 
ATOM   5945  S  SD  . MET B 1 125 ? 9.648   61.195  0.531   0.00 0.00   ? 134  MET B SD  1 
ATOM   5946  C  CE  . MET B 1 125 ? 10.524  59.913  -0.312  0.00 0.00   ? 134  MET B CE  1 
ATOM   5947  N  N   . ARG B 1 126 ? 10.171  62.170  5.876   1.00 108.66 ? 135  ARG B N   1 
ATOM   5948  C  CA  . ARG B 1 126 ? 10.471  61.626  7.203   1.00 98.46  ? 135  ARG B CA  1 
ATOM   5949  C  C   . ARG B 1 126 ? 9.503   62.097  8.300   1.00 91.34  ? 135  ARG B C   1 
ATOM   5950  O  O   . ARG B 1 126 ? 9.918   62.742  9.262   1.00 89.25  ? 135  ARG B O   1 
ATOM   5951  C  CB  . ARG B 1 126 ? 11.929  61.915  7.624   1.00 92.52  ? 135  ARG B CB  1 
ATOM   5952  C  CG  . ARG B 1 126 ? 12.640  60.618  8.057   1.00 86.50  ? 135  ARG B CG  1 
ATOM   5953  C  CD  . ARG B 1 126 ? 13.996  60.865  8.709   1.00 83.76  ? 135  ARG B CD  1 
ATOM   5954  N  NE  . ARG B 1 126 ? 15.117  60.494  7.843   1.00 80.38  ? 135  ARG B NE  1 
ATOM   5955  C  CZ  . ARG B 1 126 ? 16.138  59.728  8.225   1.00 76.62  ? 135  ARG B CZ  1 
ATOM   5956  N  NH1 . ARG B 1 126 ? 16.175  59.218  9.458   1.00 73.03  ? 135  ARG B NH1 1 
ATOM   5957  N  NH2 . ARG B 1 126 ? 17.133  59.483  7.389   1.00 75.20  ? 135  ARG B NH2 1 
ATOM   5958  N  N   . LYS B 1 127 ? 8.212   61.780  8.155   1.00 84.20  ? 136  LYS B N   1 
ATOM   5959  C  CA  . LYS B 1 127 ? 7.281   62.111  9.213   1.00 74.45  ? 136  LYS B CA  1 
ATOM   5960  C  C   . LYS B 1 127 ? 7.055   60.853  10.067  1.00 64.98  ? 136  LYS B C   1 
ATOM   5961  O  O   . LYS B 1 127 ? 6.336   59.948  9.657   1.00 63.26  ? 136  LYS B O   1 
ATOM   5962  C  CB  . LYS B 1 127 ? 5.959   62.613  8.653   1.00 71.64  ? 136  LYS B CB  1 
ATOM   5963  C  CG  . LYS B 1 127 ? 5.492   63.855  9.406   1.00 76.79  ? 136  LYS B CG  1 
ATOM   5964  C  CD  . LYS B 1 127 ? 4.624   63.503  10.618  1.00 77.52  ? 136  LYS B CD  1 
ATOM   5965  C  CE  . LYS B 1 127 ? 3.314   64.260  10.599  1.00 79.06  ? 136  LYS B CE  1 
ATOM   5966  N  NZ  . LYS B 1 127 ? 2.170   63.360  10.893  0.00 0.00   ? 136  LYS B NZ  1 
ATOM   5967  N  N   . THR B 1 128 ? 7.666   60.801  11.231  1.00 54.98  ? 137  THR B N   1 
ATOM   5968  C  CA  . THR B 1 128 ? 7.523   59.672  12.129  1.00 41.38  ? 137  THR B CA  1 
ATOM   5969  C  C   . THR B 1 128 ? 6.404   59.904  13.217  1.00 35.36  ? 137  THR B C   1 
ATOM   5970  O  O   . THR B 1 128 ? 6.019   61.028  13.518  1.00 28.31  ? 137  THR B O   1 
ATOM   5971  C  CB  . THR B 1 128 ? 8.862   59.442  12.741  1.00 38.03  ? 137  THR B CB  1 
ATOM   5972  O  OG1 . THR B 1 128 ? 9.209   60.603  13.479  1.00 38.70  ? 137  THR B OG1 1 
ATOM   5973  C  CG2 . THR B 1 128 ? 9.946   59.202  11.671  1.00 39.42  ? 137  THR B CG2 1 
ATOM   5974  N  N   . SER B 1 129 ? 5.935   58.800  13.799  1.00 30.19  ? 138  SER B N   1 
ATOM   5975  C  CA  . SER B 1 129 ? 4.880   58.769  14.795  1.00 30.59  ? 138  SER B CA  1 
ATOM   5976  C  C   . SER B 1 129 ? 5.282   57.808  15.939  1.00 28.24  ? 138  SER B C   1 
ATOM   5977  O  O   . SER B 1 129 ? 5.707   56.693  15.599  1.00 27.57  ? 138  SER B O   1 
ATOM   5978  C  CB  . SER B 1 129 ? 3.641   58.188  14.098  1.00 34.27  ? 138  SER B CB  1 
ATOM   5979  O  OG  . SER B 1 129 ? 2.488   58.937  14.401  1.00 51.19  ? 138  SER B OG  1 
ATOM   5980  N  N   . ALA B 1 130 ? 5.145   58.199  17.256  1.00 25.51  ? 139  ALA B N   1 
ATOM   5981  C  CA  . ALA B 1 130 ? 5.373   57.198  18.335  1.00 22.33  ? 139  ALA B CA  1 
ATOM   5982  C  C   . ALA B 1 130 ? 4.245   56.169  18.178  1.00 22.28  ? 139  ALA B C   1 
ATOM   5983  O  O   . ALA B 1 130 ? 3.140   56.499  17.765  1.00 21.61  ? 139  ALA B O   1 
ATOM   5984  C  CB  . ALA B 1 130 ? 5.264   57.807  19.705  1.00 21.31  ? 139  ALA B CB  1 
ATOM   5985  N  N   . PRO B 1 131 ? 4.493   54.889  18.505  1.00 20.67  ? 140  PRO B N   1 
ATOM   5986  C  CA  . PRO B 1 131 ? 3.441   53.873  18.364  1.00 21.84  ? 140  PRO B CA  1 
ATOM   5987  C  C   . PRO B 1 131 ? 2.250   54.157  19.278  1.00 22.56  ? 140  PRO B C   1 
ATOM   5988  O  O   . PRO B 1 131 ? 2.421   54.612  20.410  1.00 21.97  ? 140  PRO B O   1 
ATOM   5989  C  CB  . PRO B 1 131 ? 4.187   52.558  18.700  1.00 22.90  ? 140  PRO B CB  1 
ATOM   5990  C  CG  . PRO B 1 131 ? 5.305   52.970  19.570  1.00 22.09  ? 140  PRO B CG  1 
ATOM   5991  C  CD  . PRO B 1 131 ? 5.758   54.307  18.970  1.00 20.94  ? 140  PRO B CD  1 
ATOM   5992  N  N   . VAL B 1 132 ? 1.062   53.875  18.799  1.00 22.07  ? 141  VAL B N   1 
ATOM   5993  C  CA  . VAL B 1 132 ? -0.191  54.099  19.543  1.00 21.08  ? 141  VAL B CA  1 
ATOM   5994  C  C   . VAL B 1 132 ? -0.786  52.774  19.994  1.00 24.32  ? 141  VAL B C   1 
ATOM   5995  O  O   . VAL B 1 132 ? -0.969  51.864  19.202  1.00 23.97  ? 141  VAL B O   1 
ATOM   5996  C  CB  . VAL B 1 132 ? -1.228  54.830  18.627  1.00 21.68  ? 141  VAL B CB  1 
ATOM   5997  C  CG1 . VAL B 1 132 ? -2.599  54.929  19.331  1.00 20.24  ? 141  VAL B CG1 1 
ATOM   5998  C  CG2 . VAL B 1 132 ? -0.721  56.229  18.273  1.00 23.90  ? 141  VAL B CG2 1 
ATOM   5999  N  N   . LYS B 1 133 ? -1.090  52.662  21.285  1.00 20.82  ? 142  LYS B N   1 
ATOM   6000  C  CA  . LYS B 1 133 ? -1.768  51.475  21.809  1.00 21.49  ? 142  LYS B CA  1 
ATOM   6001  C  C   . LYS B 1 133 ? -3.192  51.972  22.132  1.00 19.77  ? 142  LYS B C   1 
ATOM   6002  O  O   . LYS B 1 133 ? -3.332  52.847  23.006  1.00 19.98  ? 142  LYS B O   1 
ATOM   6003  C  CB  . LYS B 1 133 ? -1.043  51.012  23.102  1.00 22.16  ? 142  LYS B CB  1 
ATOM   6004  C  CG  . LYS B 1 133 ? -1.813  49.920  23.878  1.00 26.09  ? 142  LYS B CG  1 
ATOM   6005  C  CD  . LYS B 1 133 ? -1.925  48.663  23.022  1.00 27.91  ? 142  LYS B CD  1 
ATOM   6006  C  CE  . LYS B 1 133 ? -2.578  47.516  23.815  1.00 33.83  ? 142  LYS B CE  1 
ATOM   6007  N  NZ  . LYS B 1 133 ? -2.826  46.346  22.886  1.00 28.59  ? 142  LYS B NZ  1 
ATOM   6008  N  N   . LYS B 1 134 ? -4.238  51.457  21.495  1.00 16.78  ? 143  LYS B N   1 
ATOM   6009  C  CA  . LYS B 1 134 ? -5.596  51.916  21.791  1.00 17.38  ? 143  LYS B CA  1 
ATOM   6010  C  C   . LYS B 1 134 ? -6.229  51.073  22.915  1.00 18.98  ? 143  LYS B C   1 
ATOM   6011  O  O   . LYS B 1 134 ? -6.165  49.843  22.863  1.00 21.36  ? 143  LYS B O   1 
ATOM   6012  C  CB  . LYS B 1 134 ? -6.467  51.834  20.540  1.00 24.04  ? 143  LYS B CB  1 
ATOM   6013  C  CG  . LYS B 1 134 ? -7.762  52.606  20.735  1.00 28.07  ? 143  LYS B CG  1 
ATOM   6014  C  CD  . LYS B 1 134 ? -8.494  52.868  19.385  1.00 28.26  ? 143  LYS B CD  1 
ATOM   6015  C  CE  . LYS B 1 134 ? -9.732  53.677  19.664  1.00 31.30  ? 143  LYS B CE  1 
ATOM   6016  N  NZ  . LYS B 1 134 ? -10.622 53.693  18.483  1.00 36.45  ? 143  LYS B NZ  1 
ATOM   6017  N  N   . LEU B 1 135 ? -6.786  51.710  23.940  1.00 18.99  ? 144  LEU B N   1 
ATOM   6018  C  CA  . LEU B 1 135 ? -7.453  50.989  25.047  1.00 20.20  ? 144  LEU B CA  1 
ATOM   6019  C  C   . LEU B 1 135 ? -8.880  51.511  24.976  1.00 18.80  ? 144  LEU B C   1 
ATOM   6020  O  O   . LEU B 1 135 ? -9.198  52.616  25.500  1.00 19.77  ? 144  LEU B O   1 
ATOM   6021  C  CB  . LEU B 1 135 ? -6.791  51.316  26.402  1.00 17.39  ? 144  LEU B CB  1 
ATOM   6022  C  CG  . LEU B 1 135 ? -5.334  50.891  26.455  1.00 17.65  ? 144  LEU B CG  1 
ATOM   6023  C  CD1 . LEU B 1 135 ? -4.777  51.374  27.883  1.00 16.74  ? 144  LEU B CD1 1 
ATOM   6024  C  CD2 . LEU B 1 135 ? -5.190  49.333  26.368  1.00 20.82  ? 144  LEU B CD2 1 
ATOM   6025  N  N   . ALA B 1 136 ? -9.749  50.763  24.330  1.00 19.77  ? 145  ALA B N   1 
ATOM   6026  C  CA  . ALA B 1 136 ? -11.085 51.280  24.094  1.00 19.38  ? 145  ALA B CA  1 
ATOM   6027  C  C   . ALA B 1 136 ? -12.086 50.154  23.832  1.00 21.67  ? 145  ALA B C   1 
ATOM   6028  O  O   . ALA B 1 136 ? -11.733 49.109  23.311  1.00 22.35  ? 145  ALA B O   1 
ATOM   6029  C  CB  . ALA B 1 136 ? -11.046 52.164  22.823  1.00 22.59  ? 145  ALA B CB  1 
ATOM   6030  N  N   . GLY B 1 137 ? -13.332 50.409  24.146  1.00 21.96  ? 146  GLY B N   1 
ATOM   6031  C  CA  . GLY B 1 137 ? -14.377 49.446  23.837  1.00 24.60  ? 146  GLY B CA  1 
ATOM   6032  C  C   . GLY B 1 137 ? -15.598 50.230  23.395  1.00 24.39  ? 146  GLY B C   1 
ATOM   6033  O  O   . GLY B 1 137 ? -15.581 51.447  23.269  1.00 25.30  ? 146  GLY B O   1 
ATOM   6034  N  N   . ALA B 1 138 ? -16.692 49.519  23.150  1.00 26.53  ? 147  ALA B N   1 
ATOM   6035  C  CA  . ALA B 1 138 ? -17.925 50.130  22.681  1.00 29.53  ? 147  ALA B CA  1 
ATOM   6036  C  C   . ALA B 1 138 ? -18.439 51.238  23.599  1.00 33.02  ? 147  ALA B C   1 
ATOM   6037  O  O   . ALA B 1 138 ? -18.945 52.243  23.107  1.00 33.50  ? 147  ALA B O   1 
ATOM   6038  C  CB  . ALA B 1 138 ? -18.975 49.040  22.541  1.00 31.72  ? 147  ALA B CB  1 
ATOM   6039  N  N   . THR B 1 139 ? -18.330 51.086  24.934  1.00 30.47  ? 148  THR B N   1 
ATOM   6040  C  CA  . THR B 1 139 ? -18.766 52.168  25.840  1.00 27.74  ? 148  THR B CA  1 
ATOM   6041  C  C   . THR B 1 139 ? -17.715 52.338  26.949  1.00 26.52  ? 148  THR B C   1 
ATOM   6042  O  O   . THR B 1 139 ? -16.774 51.549  27.021  1.00 25.55  ? 148  THR B O   1 
ATOM   6043  C  CB  . THR B 1 139 ? -20.099 51.824  26.538  1.00 31.75  ? 148  THR B CB  1 
ATOM   6044  O  OG1 . THR B 1 139 ? -19.839 50.749  27.447  1.00 32.73  ? 148  THR B OG1 1 
ATOM   6045  C  CG2 . THR B 1 139 ? -21.173 51.329  25.533  1.00 36.26  ? 148  THR B CG2 1 
ATOM   6046  N  N   . ARG B 1 140 ? -17.918 53.341  27.796  1.00 25.82  ? 149  ARG B N   1 
ATOM   6047  C  CA  . ARG B 1 140 ? -17.022 53.598  28.904  1.00 25.47  ? 149  ARG B CA  1 
ATOM   6048  C  C   . ARG B 1 140 ? -16.779 52.322  29.730  1.00 24.53  ? 149  ARG B C   1 
ATOM   6049  O  O   . ARG B 1 140 ? -15.672 52.150  30.246  1.00 22.29  ? 149  ARG B O   1 
ATOM   6050  C  CB  . ARG B 1 140 ? -17.602 54.707  29.778  1.00 21.52  ? 149  ARG B CB  1 
ATOM   6051  C  CG  . ARG B 1 140 ? -19.026 54.343  30.319  1.00 22.25  ? 149  ARG B CG  1 
ATOM   6052  C  CD  . ARG B 1 140 ? -19.773 55.554  30.901  1.00 25.86  ? 149  ARG B CD  1 
ATOM   6053  N  NE  . ARG B 1 140 ? -19.924 56.590  29.879  1.00 29.54  ? 149  ARG B NE  1 
ATOM   6054  C  CZ  . ARG B 1 140 ? -20.078 57.883  30.157  1.00 35.41  ? 149  ARG B CZ  1 
ATOM   6055  N  NH1 . ARG B 1 140 ? -20.143 58.294  31.419  1.00 32.41  ? 149  ARG B NH1 1 
ATOM   6056  N  NH2 . ARG B 1 140 ? -20.123 58.778  29.178  1.00 37.12  ? 149  ARG B NH2 1 
ATOM   6057  N  N   . PHE B 1 141 ? -17.781 51.417  29.861  1.00 23.60  ? 150  PHE B N   1 
ATOM   6058  C  CA  . PHE B 1 141 ? -17.570 50.174  30.661  1.00 23.94  ? 150  PHE B CA  1 
ATOM   6059  C  C   . PHE B 1 141 ? -16.564 49.251  30.054  1.00 22.52  ? 150  PHE B C   1 
ATOM   6060  O  O   . PHE B 1 141 ? -15.732 48.667  30.764  1.00 21.99  ? 150  PHE B O   1 
ATOM   6061  C  CB  . PHE B 1 141 ? -18.927 49.386  30.827  1.00 23.83  ? 150  PHE B CB  1 
ATOM   6062  C  CG  . PHE B 1 141 ? -19.948 50.197  31.591  1.00 25.13  ? 150  PHE B CG  1 
ATOM   6063  C  CD1 . PHE B 1 141 ? -20.021 50.122  32.974  1.00 25.69  ? 150  PHE B CD1 1 
ATOM   6064  C  CD2 . PHE B 1 141 ? -20.783 51.085  30.933  1.00 27.84  ? 150  PHE B CD2 1 
ATOM   6065  C  CE1 . PHE B 1 141 ? -20.904 50.929  33.677  1.00 25.68  ? 150  PHE B CE1 1 
ATOM   6066  C  CE2 . PHE B 1 141 ? -21.658 51.891  31.643  1.00 32.83  ? 150  PHE B CE2 1 
ATOM   6067  C  CZ  . PHE B 1 141 ? -21.708 51.808  33.017  1.00 30.06  ? 150  PHE B CZ  1 
ATOM   6068  N  N   . GLU B 1 142 ? -16.616 49.069  28.721  1.00 20.34  ? 151  GLU B N   1 
ATOM   6069  C  CA  . GLU B 1 142 ? -15.639 48.216  28.076  1.00 20.06  ? 151  GLU B CA  1 
ATOM   6070  C  C   . GLU B 1 142 ? -14.258 48.916  27.967  1.00 19.26  ? 151  GLU B C   1 
ATOM   6071  O  O   . GLU B 1 142 ? -13.254 48.221  27.916  1.00 21.09  ? 151  GLU B O   1 
ATOM   6072  C  CB  . GLU B 1 142 ? -16.100 47.897  26.653  1.00 23.94  ? 151  GLU B CB  1 
ATOM   6073  C  CG  . GLU B 1 142 ? -17.210 46.850  26.651  1.00 35.67  ? 151  GLU B CG  1 
ATOM   6074  C  CD  . GLU B 1 142 ? -18.603 47.487  26.606  1.00 52.35  ? 151  GLU B CD  1 
ATOM   6075  O  OE1 . GLU B 1 142 ? -19.589 46.711  26.556  1.00 54.83  ? 151  GLU B OE1 1 
ATOM   6076  O  OE2 . GLU B 1 142 ? -18.730 48.738  26.641  1.00 52.76  ? 151  GLU B OE2 1 
ATOM   6077  N  N   . THR B 1 143 ? -14.241 50.265  27.866  1.00 18.76  ? 152  THR B N   1 
ATOM   6078  C  CA  . THR B 1 143 ? -12.948 50.940  27.832  1.00 16.90  ? 152  THR B CA  1 
ATOM   6079  C  C   . THR B 1 143 ? -12.269 50.660  29.190  1.00 18.40  ? 152  THR B C   1 
ATOM   6080  O  O   . THR B 1 143 ? -11.083 50.346  29.220  1.00 17.44  ? 152  THR B O   1 
ATOM   6081  C  CB  . THR B 1 143 ? -13.176 52.458  27.584  1.00 17.77  ? 152  THR B CB  1 
ATOM   6082  O  OG1 . THR B 1 143 ? -13.584 52.566  26.203  1.00 20.42  ? 152  THR B OG1 1 
ATOM   6083  C  CG2 . THR B 1 143 ? -11.913 53.289  27.803  1.00 19.46  ? 152  THR B CG2 1 
ATOM   6084  N  N   . ALA B 1 144 ? -13.019 50.744  30.276  1.00 19.44  ? 153  ALA B N   1 
ATOM   6085  C  CA  . ALA B 1 144 ? -12.374 50.484  31.583  1.00 17.96  ? 153  ALA B CA  1 
ATOM   6086  C  C   . ALA B 1 144 ? -11.834 49.078  31.654  1.00 19.32  ? 153  ALA B C   1 
ATOM   6087  O  O   . ALA B 1 144 ? -10.759 48.850  32.244  1.00 19.90  ? 153  ALA B O   1 
ATOM   6088  C  CB  . ALA B 1 144 ? -13.374 50.743  32.709  1.00 19.43  ? 153  ALA B CB  1 
ATOM   6089  N  N   . VAL B 1 145 ? -12.544 48.103  31.060  1.00 17.88  ? 154  VAL B N   1 
ATOM   6090  C  CA  . VAL B 1 145 ? -12.038 46.737  31.079  1.00 18.49  ? 154  VAL B CA  1 
ATOM   6091  C  C   . VAL B 1 145 ? -10.735 46.620  30.264  1.00 21.03  ? 154  VAL B C   1 
ATOM   6092  O  O   . VAL B 1 145 ? -9.820  45.920  30.684  1.00 18.87  ? 154  VAL B O   1 
ATOM   6093  C  CB  . VAL B 1 145 ? -13.136 45.769  30.549  1.00 21.17  ? 154  VAL B CB  1 
ATOM   6094  C  CG1 . VAL B 1 145 ? -12.516 44.374  30.277  1.00 18.20  ? 154  VAL B CG1 1 
ATOM   6095  C  CG2 . VAL B 1 145 ? -14.321 45.733  31.608  1.00 21.74  ? 154  VAL B CG2 1 
ATOM   6096  N  N   . GLU B 1 146 ? -10.642 47.287  29.083  1.00 20.00  ? 155  GLU B N   1 
ATOM   6097  C  CA  . GLU B 1 146 ? -9.377  47.216  28.330  1.00 19.73  ? 155  GLU B CA  1 
ATOM   6098  C  C   . GLU B 1 146 ? -8.217  47.855  29.135  1.00 17.98  ? 155  GLU B C   1 
ATOM   6099  O  O   . GLU B 1 146 ? -7.112  47.332  29.055  1.00 19.64  ? 155  GLU B O   1 
ATOM   6100  C  CB  . GLU B 1 146 ? -9.537  47.908  26.967  1.00 19.15  ? 155  GLU B CB  1 
ATOM   6101  C  CG  . GLU B 1 146 ? -10.562 47.190  26.139  1.00 23.13  ? 155  GLU B CG  1 
ATOM   6102  C  CD  . GLU B 1 146 ? -10.178 45.726  25.912  1.00 35.84  ? 155  GLU B CD  1 
ATOM   6103  O  OE1 . GLU B 1 146 ? -11.012 44.821  26.170  1.00 40.38  ? 155  GLU B OE1 1 
ATOM   6104  O  OE2 . GLU B 1 146 ? -9.060  45.474  25.499  1.00 36.75  ? 155  GLU B OE2 1 
ATOM   6105  N  N   . ILE B 1 147 ? -8.455  48.920  29.884  1.00 17.97  ? 156  ILE B N   1 
ATOM   6106  C  CA  . ILE B 1 147 ? -7.384  49.530  30.725  1.00 19.37  ? 156  ILE B CA  1 
ATOM   6107  C  C   . ILE B 1 147 ? -6.985  48.529  31.827  1.00 20.13  ? 156  ILE B C   1 
ATOM   6108  O  O   . ILE B 1 147 ? -5.804  48.330  32.133  1.00 18.90  ? 156  ILE B O   1 
ATOM   6109  C  CB  . ILE B 1 147 ? -7.937  50.804  31.361  1.00 20.44  ? 156  ILE B CB  1 
ATOM   6110  C  CG1 . ILE B 1 147 ? -8.083  51.893  30.278  1.00 17.18  ? 156  ILE B CG1 1 
ATOM   6111  C  CG2 . ILE B 1 147 ? -7.012  51.291  32.525  1.00 19.01  ? 156  ILE B CG2 1 
ATOM   6112  C  CD1 . ILE B 1 147 ? -8.977  53.043  30.749  1.00 17.99  ? 156  ILE B CD1 1 
ATOM   6113  N  N   . SER B 1 148 ? -8.003  47.883  32.432  1.00 20.36  ? 157  SER B N   1 
ATOM   6114  C  CA  . SER B 1 148 ? -7.747  46.889  33.483  1.00 20.58  ? 157  SER B CA  1 
ATOM   6115  C  C   . SER B 1 148 ? -6.882  45.738  32.922  1.00 19.94  ? 157  SER B C   1 
ATOM   6116  O  O   . SER B 1 148 ? -5.935  45.283  33.582  1.00 19.20  ? 157  SER B O   1 
ATOM   6117  C  CB  . SER B 1 148 ? -9.111  46.338  33.998  1.00 23.65  ? 157  SER B CB  1 
ATOM   6118  O  OG  . SER B 1 148 ? -8.909  45.379  35.003  1.00 25.71  ? 157  SER B OG  1 
ATOM   6119  N  N   . LYS B 1 149 ? -7.195  45.231  31.738  1.00 19.80  ? 158  LYS B N   1 
ATOM   6120  C  CA  . LYS B 1 149 ? -6.412  44.142  31.161  1.00 20.84  ? 158  LYS B CA  1 
ATOM   6121  C  C   . LYS B 1 149 ? -4.969  44.594  30.828  1.00 22.72  ? 158  LYS B C   1 
ATOM   6122  O  O   . LYS B 1 149 ? -4.044  43.804  30.838  1.00 23.00  ? 158  LYS B O   1 
ATOM   6123  C  CB  . LYS B 1 149 ? -7.065  43.621  29.882  1.00 25.27  ? 158  LYS B CB  1 
ATOM   6124  C  CG  . LYS B 1 149 ? -8.340  42.793  30.198  1.00 24.20  ? 158  LYS B CG  1 
ATOM   6125  C  CD  . LYS B 1 149 ? -9.189  42.742  28.945  1.00 33.76  ? 158  LYS B CD  1 
ATOM   6126  C  CE  . LYS B 1 149 ? -9.772  41.391  28.710  1.00 46.78  ? 158  LYS B CE  1 
ATOM   6127  N  NZ  . LYS B 1 149 ? -10.231 41.297  27.294  1.00 58.10  ? 158  LYS B NZ  1 
ATOM   6128  N  N   . GLN B 1 150 ? -4.807  45.895  30.543  1.00 21.31  ? 159  GLN B N   1 
ATOM   6129  C  CA  . GLN B 1 150 ? -3.470  46.375  30.228  1.00 22.07  ? 159  GLN B CA  1 
ATOM   6130  C  C   . GLN B 1 150 ? -2.531  46.375  31.458  1.00 20.27  ? 159  GLN B C   1 
ATOM   6131  O  O   . GLN B 1 150 ? -1.422  45.945  31.322  1.00 22.93  ? 159  GLN B O   1 
ATOM   6132  C  CB  . GLN B 1 150 ? -3.563  47.803  29.662  1.00 20.69  ? 159  GLN B CB  1 
ATOM   6133  C  CG  . GLN B 1 150 ? -2.211  48.274  29.067  1.00 22.87  ? 159  GLN B CG  1 
ATOM   6134  C  CD  . GLN B 1 150 ? -1.843  47.500  27.781  1.00 24.44  ? 159  GLN B CD  1 
ATOM   6135  O  OE1 . GLN B 1 150 ? -2.675  46.831  27.164  1.00 22.62  ? 159  GLN B OE1 1 
ATOM   6136  N  NE2 . GLN B 1 150 ? -0.549  47.491  27.416  1.00 21.31  ? 159  GLN B NE2 1 
ATOM   6137  N  N   . GLY B 1 151 ? -2.980  46.850  32.620  1.00 20.64  ? 160  GLY B N   1 
ATOM   6138  C  CA  . GLY B 1 151 ? -2.046  46.935  33.736  1.00 22.65  ? 160  GLY B CA  1 
ATOM   6139  C  C   . GLY B 1 151 ? -2.216  45.840  34.774  1.00 23.23  ? 160  GLY B C   1 
ATOM   6140  O  O   . GLY B 1 151 ? -1.391  45.751  35.677  1.00 20.64  ? 160  GLY B O   1 
ATOM   6141  N  N   . TRP B 1 152 ? -3.290  45.049  34.649  1.00 22.32  ? 161  TRP B N   1 
ATOM   6142  C  CA  . TRP B 1 152 ? -3.619  43.984  35.643  1.00 25.20  ? 161  TRP B CA  1 
ATOM   6143  C  C   . TRP B 1 152 ? -3.989  42.684  34.918  1.00 21.90  ? 161  TRP B C   1 
ATOM   6144  O  O   . TRP B 1 152 ? -4.984  42.008  35.225  1.00 22.10  ? 161  TRP B O   1 
ATOM   6145  C  CB  . TRP B 1 152 ? -4.762  44.481  36.557  1.00 21.13  ? 161  TRP B CB  1 
ATOM   6146  C  CG  . TRP B 1 152 ? -4.361  45.679  37.354  1.00 20.90  ? 161  TRP B CG  1 
ATOM   6147  C  CD1 . TRP B 1 152 ? -3.847  45.697  38.630  1.00 21.34  ? 161  TRP B CD1 1 
ATOM   6148  C  CD2 . TRP B 1 152 ? -4.411  47.057  36.924  1.00 20.92  ? 161  TRP B CD2 1 
ATOM   6149  N  NE1 . TRP B 1 152 ? -3.579  46.985  39.018  1.00 21.97  ? 161  TRP B NE1 1 
ATOM   6150  C  CE2 . TRP B 1 152 ? -3.910  47.844  37.980  1.00 23.82  ? 161  TRP B CE2 1 
ATOM   6151  C  CE3 . TRP B 1 152 ? -4.816  47.695  35.728  1.00 19.65  ? 161  TRP B CE3 1 
ATOM   6152  C  CZ2 . TRP B 1 152 ? -3.800  49.244  37.885  1.00 23.45  ? 161  TRP B CZ2 1 
ATOM   6153  C  CZ3 . TRP B 1 152 ? -4.697  49.084  35.631  1.00 21.46  ? 161  TRP B CZ3 1 
ATOM   6154  C  CH2 . TRP B 1 152 ? -4.200  49.841  36.693  1.00 21.23  ? 161  TRP B CH2 1 
ATOM   6155  N  N   . LYS B 1 153 ? -3.160  42.333  33.935  1.00 20.04  ? 162  LYS B N   1 
ATOM   6156  C  CA  . LYS B 1 153 ? -3.383  41.137  33.175  1.00 24.01  ? 162  LYS B CA  1 
ATOM   6157  C  C   . LYS B 1 153 ? -3.313  39.889  34.090  1.00 22.78  ? 162  LYS B C   1 
ATOM   6158  O  O   . LYS B 1 153 ? -4.097  38.964  33.910  1.00 24.37  ? 162  LYS B O   1 
ATOM   6159  C  CB  . LYS B 1 153 ? -2.314  40.974  32.080  1.00 25.39  ? 162  LYS B CB  1 
ATOM   6160  C  CG  . LYS B 1 153 ? -2.651  39.845  31.099  1.00 31.29  ? 162  LYS B CG  1 
ATOM   6161  C  CD  . LYS B 1 153 ? -4.135  39.942  30.641  1.00 40.25  ? 162  LYS B CD  1 
ATOM   6162  C  CE  . LYS B 1 153 ? -4.356  39.215  29.346  1.00 50.10  ? 162  LYS B CE  1 
ATOM   6163  N  NZ  . LYS B 1 153 ? -5.470  39.807  28.560  0.00 0.00   ? 162  LYS B NZ  1 
ATOM   6164  N  N   . ASP B 1 154 ? -2.404  39.901  35.053  1.00 23.99  ? 163  ASP B N   1 
ATOM   6165  C  CA  . ASP B 1 154 ? -2.242  38.775  35.971  1.00 25.29  ? 163  ASP B CA  1 
ATOM   6166  C  C   . ASP B 1 154 ? -3.267  38.888  37.152  1.00 28.64  ? 163  ASP B C   1 
ATOM   6167  O  O   . ASP B 1 154 ? -3.157  38.106  38.089  1.00 27.38  ? 163  ASP B O   1 
ATOM   6168  C  CB  . ASP B 1 154 ? -0.776  38.730  36.518  1.00 23.30  ? 163  ASP B CB  1 
ATOM   6169  C  CG  . ASP B 1 154 ? -0.336  40.037  37.235  1.00 24.91  ? 163  ASP B CG  1 
ATOM   6170  O  OD1 . ASP B 1 154 ? 0.540   39.972  38.110  1.00 27.93  ? 163  ASP B OD1 1 
ATOM   6171  O  OD2 . ASP B 1 154 ? -0.896  41.140  36.916  1.00 23.68  ? 163  ASP B OD2 1 
ATOM   6172  N  N   . GLY B 1 155 ? -4.236  39.822  37.125  1.00 25.86  ? 164  GLY B N   1 
ATOM   6173  C  CA  . GLY B 1 155 ? -5.230  39.917  38.208  1.00 24.11  ? 164  GLY B CA  1 
ATOM   6174  C  C   . GLY B 1 155 ? -4.981  41.062  39.144  1.00 23.81  ? 164  GLY B C   1 
ATOM   6175  O  O   . GLY B 1 155 ? -4.022  41.811  38.982  1.00 25.29  ? 164  GLY B O   1 
ATOM   6176  N  N   . SER B 1 156 ? -5.875  41.255  40.167  1.00 21.46  ? 165  SER B N   1 
ATOM   6177  C  CA  . SER B 1 156 ? -5.677  42.319  41.136  1.00 22.60  ? 165  SER B CA  1 
ATOM   6178  C  C   . SER B 1 156 ? -6.411  41.893  42.441  1.00 26.20  ? 165  SER B C   1 
ATOM   6179  O  O   . SER B 1 156 ? -7.567  41.464  42.337  1.00 29.21  ? 165  SER B O   1 
ATOM   6180  C  CB  . SER B 1 156 ? -6.316  43.628  40.687  1.00 21.33  ? 165  SER B CB  1 
ATOM   6181  O  OG  . SER B 1 156 ? -5.928  44.655  41.574  1.00 24.23  ? 165  SER B OG  1 
ATOM   6182  N  N   . SER B 1 157 ? -5.785  42.039  43.596  1.00 25.95  ? 166  SER B N   1 
ATOM   6183  C  CA  . SER B 1 157 ? -6.488  41.623  44.804  1.00 29.65  ? 166  SER B CA  1 
ATOM   6184  C  C   . SER B 1 157 ? -7.582  42.616  45.170  1.00 28.74  ? 166  SER B C   1 
ATOM   6185  O  O   . SER B 1 157 ? -8.544  42.222  45.809  1.00 27.59  ? 166  SER B O   1 
ATOM   6186  C  CB  . SER B 1 157 ? -5.493  41.434  45.945  1.00 32.15  ? 166  SER B CB  1 
ATOM   6187  O  OG  . SER B 1 157 ? -5.140  42.716  46.414  1.00 39.00  ? 166  SER B OG  1 
ATOM   6188  N  N   . LYS B 1 158 ? -7.462  43.904  44.759  1.00 25.77  ? 167  LYS B N   1 
ATOM   6189  C  CA  . LYS B 1 158 ? -8.494  44.889  45.007  1.00 23.78  ? 167  LYS B CA  1 
ATOM   6190  C  C   . LYS B 1 158 ? -9.016  45.487  43.674  1.00 27.80  ? 167  LYS B C   1 
ATOM   6191  O  O   . LYS B 1 158 ? -8.273  45.501  42.682  1.00 24.62  ? 167  LYS B O   1 
ATOM   6192  C  CB  . LYS B 1 158 ? -7.970  46.032  45.882  1.00 28.00  ? 167  LYS B CB  1 
ATOM   6193  C  CG  . LYS B 1 158 ? -7.486  45.617  47.307  1.00 31.17  ? 167  LYS B CG  1 
ATOM   6194  C  CD  . LYS B 1 158 ? -7.081  46.830  48.120  1.00 33.98  ? 167  LYS B CD  1 
ATOM   6195  C  CE  . LYS B 1 158 ? -6.744  46.446  49.587  1.00 40.65  ? 167  LYS B CE  1 
ATOM   6196  N  NZ  . LYS B 1 158 ? -5.847  45.258  49.617  1.00 46.09  ? 167  LYS B NZ  1 
ATOM   6197  N  N   . VAL B 1 159 ? -10.273 45.929  43.647  1.00 25.41  ? 168  VAL B N   1 
ATOM   6198  C  CA  . VAL B 1 159 ? -10.867 46.586  42.485  1.00 26.63  ? 168  VAL B CA  1 
ATOM   6199  C  C   . VAL B 1 159 ? -11.660 47.732  43.012  1.00 26.56  ? 168  VAL B C   1 
ATOM   6200  O  O   . VAL B 1 159 ? -12.404 47.585  44.015  1.00 25.88  ? 168  VAL B O   1 
ATOM   6201  C  CB  . VAL B 1 159 ? -11.743 45.654  41.616  1.00 23.16  ? 168  VAL B CB  1 
ATOM   6202  C  CG1 . VAL B 1 159 ? -12.373 46.460  40.483  1.00 23.38  ? 168  VAL B CG1 1 
ATOM   6203  C  CG2 . VAL B 1 159 ? -10.905 44.512  41.036  1.00 24.21  ? 168  VAL B CG2 1 
ATOM   6204  N  N   . VAL B 1 160 ? -11.499 48.929  42.407  1.00 23.22  ? 169  VAL B N   1 
ATOM   6205  C  CA  . VAL B 1 160 ? -12.271 50.082  42.845  1.00 20.79  ? 169  VAL B CA  1 
ATOM   6206  C  C   . VAL B 1 160 ? -13.483 50.220  41.938  1.00 23.42  ? 169  VAL B C   1 
ATOM   6207  O  O   . VAL B 1 160 ? -13.341 49.966  40.748  1.00 21.84  ? 169  VAL B O   1 
ATOM   6208  C  CB  . VAL B 1 160 ? -11.398 51.362  42.837  1.00 21.50  ? 169  VAL B CB  1 
ATOM   6209  C  CG1 . VAL B 1 160 ? -12.263 52.578  43.105  1.00 22.39  ? 169  VAL B CG1 1 
ATOM   6210  C  CG2 . VAL B 1 160 ? -10.298 51.256  43.935  1.00 20.10  ? 169  VAL B CG2 1 
ATOM   6211  N  N   . ILE B 1 161 ? -14.649 50.579  42.459  1.00 22.22  ? 170  ILE B N   1 
ATOM   6212  C  CA  . ILE B 1 161 ? -15.842 50.680  41.605  1.00 23.11  ? 170  ILE B CA  1 
ATOM   6213  C  C   . ILE B 1 161 ? -16.428 52.036  41.713  1.00 22.75  ? 170  ILE B C   1 
ATOM   6214  O  O   . ILE B 1 161 ? -16.589 52.574  42.806  1.00 23.39  ? 170  ILE B O   1 
ATOM   6215  C  CB  . ILE B 1 161 ? -16.949 49.611  42.022  1.00 23.62  ? 170  ILE B CB  1 
ATOM   6216  C  CG1 . ILE B 1 161 ? -16.488 48.225  41.641  1.00 24.96  ? 170  ILE B CG1 1 
ATOM   6217  C  CG2 . ILE B 1 161 ? -18.326 49.967  41.371  1.00 22.28  ? 170  ILE B CG2 1 
ATOM   6218  C  CD1 . ILE B 1 161 ? -16.639 47.885  40.137  1.00 27.08  ? 170  ILE B CD1 1 
ATOM   6219  N  N   . VAL B 1 162 ? -16.770 52.640  40.572  1.00 20.12  ? 171  VAL B N   1 
ATOM   6220  C  CA  . VAL B 1 162 ? -17.398 53.951  40.544  1.00 19.94  ? 171  VAL B CA  1 
ATOM   6221  C  C   . VAL B 1 162 ? -18.646 53.878  39.646  1.00 21.44  ? 171  VAL B C   1 
ATOM   6222  O  O   . VAL B 1 162 ? -18.664 53.040  38.742  1.00 23.63  ? 171  VAL B O   1 
ATOM   6223  C  CB  . VAL B 1 162 ? -16.363 54.960  39.921  1.00 25.32  ? 171  VAL B CB  1 
ATOM   6224  C  CG1 . VAL B 1 162 ? -17.032 56.256  39.537  1.00 28.17  ? 171  VAL B CG1 1 
ATOM   6225  C  CG2 . VAL B 1 162 ? -15.219 55.216  40.931  1.00 28.64  ? 171  VAL B CG2 1 
ATOM   6226  N  N   . ASN B 1 163 ? -19.617 54.758  39.818  1.00 21.46  ? 172  ASN B N   1 
ATOM   6227  C  CA  . ASN B 1 163 ? -20.785 54.725  38.950  1.00 24.04  ? 172  ASN B CA  1 
ATOM   6228  C  C   . ASN B 1 163 ? -20.337 55.337  37.564  1.00 24.33  ? 172  ASN B C   1 
ATOM   6229  O  O   . ASN B 1 163 ? -19.932 56.476  37.545  1.00 26.08  ? 172  ASN B O   1 
ATOM   6230  C  CB  . ASN B 1 163 ? -21.914 55.545  39.578  1.00 25.65  ? 172  ASN B CB  1 
ATOM   6231  C  CG  . ASN B 1 163 ? -23.173 55.568  38.726  1.00 34.71  ? 172  ASN B CG  1 
ATOM   6232  O  OD1 . ASN B 1 163 ? -23.113 55.695  37.490  1.00 31.44  ? 172  ASN B OD1 1 
ATOM   6233  N  ND2 . ASN B 1 163 ? -24.383 55.484  39.318  1.00 30.81  ? 172  ASN B ND2 1 
ATOM   6234  N  N   . GLY B 1 164 ? -20.435 54.606  36.482  1.00 27.41  ? 173  GLY B N   1 
ATOM   6235  C  CA  . GLY B 1 164 ? -19.928 55.110  35.209  1.00 31.41  ? 173  GLY B CA  1 
ATOM   6236  C  C   . GLY B 1 164 ? -20.697 56.284  34.624  1.00 34.61  ? 173  GLY B C   1 
ATOM   6237  O  O   . GLY B 1 164 ? -20.135 57.088  33.890  1.00 32.05  ? 173  GLY B O   1 
ATOM   6238  N  N   . GLU B 1 165 ? -22.000 56.381  34.936  1.00 34.46  ? 174  GLU B N   1 
ATOM   6239  C  CA  . GLU B 1 165 ? -22.820 57.456  34.408  1.00 38.71  ? 174  GLU B CA  1 
ATOM   6240  C  C   . GLU B 1 165 ? -22.734 58.713  35.267  1.00 40.69  ? 174  GLU B C   1 
ATOM   6241  O  O   . GLU B 1 165 ? -23.078 59.774  34.784  1.00 43.81  ? 174  GLU B O   1 
ATOM   6242  C  CB  . GLU B 1 165 ? -24.295 56.969  34.267  1.00 43.76  ? 174  GLU B CB  1 
ATOM   6243  C  CG  . GLU B 1 165 ? -24.434 55.786  33.301  1.00 54.34  ? 174  GLU B CG  1 
ATOM   6244  C  CD  . GLU B 1 165 ? -23.908 56.076  31.865  1.00 62.16  ? 174  GLU B CD  1 
ATOM   6245  O  OE1 . GLU B 1 165 ? -23.867 57.271  31.456  1.00 66.44  ? 174  GLU B OE1 1 
ATOM   6246  O  OE2 . GLU B 1 165 ? -23.551 55.101  31.144  1.00 61.93  ? 174  GLU B OE2 1 
ATOM   6247  N  N   . LEU B 1 166 ? -22.310 58.610  36.519  1.00 41.42  ? 175  LEU B N   1 
ATOM   6248  C  CA  . LEU B 1 166 ? -22.085 59.730  37.436  1.00 46.26  ? 175  LEU B CA  1 
ATOM   6249  C  C   . LEU B 1 166 ? -20.555 59.793  37.724  1.00 53.71  ? 175  LEU B C   1 
ATOM   6250  O  O   . LEU B 1 166 ? -20.166 59.950  38.890  1.00 57.26  ? 175  LEU B O   1 
ATOM   6251  C  CB  . LEU B 1 166 ? -22.751 59.524  38.809  1.00 52.62  ? 175  LEU B CB  1 
ATOM   6252  C  CG  . LEU B 1 166 ? -24.262 59.447  38.864  1.00 53.74  ? 175  LEU B CG  1 
ATOM   6253  C  CD1 . LEU B 1 166 ? -24.620 59.075  40.356  1.00 54.28  ? 175  LEU B CD1 1 
ATOM   6254  C  CD2 . LEU B 1 166 ? -24.923 60.751  38.429  1.00 51.93  ? 175  LEU B CD2 1 
ATOM   6255  N  N   . ALA B 1 167 ? -19.703 59.667  36.704  1.00 55.03  ? 176  ALA B N   1 
ATOM   6256  C  CA  . ALA B 1 167 ? -18.237 59.646  36.842  1.00 59.03  ? 176  ALA B CA  1 
ATOM   6257  C  C   . ALA B 1 167 ? -17.632 60.717  37.758  1.00 60.74  ? 176  ALA B C   1 
ATOM   6258  O  O   . ALA B 1 167 ? -16.665 60.393  38.442  1.00 59.99  ? 176  ALA B O   1 
ATOM   6259  C  CB  . ALA B 1 167 ? -17.598 59.783  35.466  1.00 59.89  ? 176  ALA B CB  1 
ATOM   6260  N  N   . ALA B 1 168 ? -18.171 61.979  37.788  1.00 59.55  ? 177  ALA B N   1 
ATOM   6261  C  CA  . ALA B 1 168 ? -17.601 63.043  38.641  1.00 54.43  ? 177  ALA B CA  1 
ATOM   6262  C  C   . ALA B 1 168 ? -17.384 62.515  40.065  1.00 51.03  ? 177  ALA B C   1 
ATOM   6263  O  O   . ALA B 1 168 ? -16.566 63.034  40.814  1.00 49.55  ? 177  ALA B O   1 
ATOM   6264  C  CB  . ALA B 1 168 ? -18.494 64.273  38.643  1.00 51.50  ? 177  ALA B CB  1 
ATOM   6265  N  N   . ASP B 1 169 ? -18.094 61.454  40.403  1.00 49.69  ? 178  ASP B N   1 
ATOM   6266  C  CA  . ASP B 1 169 ? -17.947 60.727  41.661  1.00 50.74  ? 178  ASP B CA  1 
ATOM   6267  C  C   . ASP B 1 169 ? -16.489 60.258  41.914  1.00 48.84  ? 178  ASP B C   1 
ATOM   6268  O  O   . ASP B 1 169 ? -16.019 60.327  43.027  1.00 47.76  ? 178  ASP B O   1 
ATOM   6269  C  CB  . ASP B 1 169 ? -18.835 59.439  41.610  1.00 53.97  ? 178  ASP B CB  1 
ATOM   6270  C  CG  . ASP B 1 169 ? -20.254 59.636  42.121  1.00 61.59  ? 178  ASP B CG  1 
ATOM   6271  O  OD1 . ASP B 1 169 ? -21.028 58.663  42.100  1.00 61.96  ? 178  ASP B OD1 1 
ATOM   6272  O  OD2 . ASP B 1 169 ? -20.587 60.771  42.544  1.00 60.65  ? 178  ASP B OD2 1 
ATOM   6273  N  N   . GLY B 1 170 ? -15.798 59.764  40.870  1.00 45.10  ? 179  GLY B N   1 
ATOM   6274  C  CA  . GLY B 1 170 ? -14.437 59.230  40.993  1.00 38.40  ? 179  GLY B CA  1 
ATOM   6275  C  C   . GLY B 1 170 ? -13.335 60.179  40.614  1.00 32.78  ? 179  GLY B C   1 
ATOM   6276  O  O   . GLY B 1 170 ? -12.198 59.747  40.343  1.00 32.06  ? 179  GLY B O   1 
ATOM   6277  N  N   . ILE B 1 171 ? -13.621 61.479  40.605  1.00 26.82  ? 180  ILE B N   1 
ATOM   6278  C  CA  . ILE B 1 171 ? -12.542 62.377  40.189  1.00 26.72  ? 180  ILE B CA  1 
ATOM   6279  C  C   . ILE B 1 171 ? -11.460 62.398  41.246  1.00 33.56  ? 180  ILE B C   1 
ATOM   6280  O  O   . ILE B 1 171 ? -10.424 63.005  40.952  1.00 36.21  ? 180  ILE B O   1 
ATOM   6281  C  CB  . ILE B 1 171 ? -12.970 63.818  39.950  1.00 29.02  ? 180  ILE B CB  1 
ATOM   6282  C  CG1 . ILE B 1 171 ? -13.722 64.360  41.196  1.00 27.54  ? 180  ILE B CG1 1 
ATOM   6283  C  CG2 . ILE B 1 171 ? -13.854 63.898  38.705  1.00 27.24  ? 180  ILE B CG2 1 
ATOM   6284  C  CD1 . ILE B 1 171 ? -14.346 65.804  41.012  1.00 33.36  ? 180  ILE B CD1 1 
ATOM   6285  N  N   . THR B 1 172 ? -11.681 61.838  42.476  1.00 24.52  ? 181  THR B N   1 
ATOM   6286  C  CA  . THR B 1 172 ? -10.568 61.827  43.451  1.00 26.59  ? 181  THR B CA  1 
ATOM   6287  C  C   . THR B 1 172 ? -10.189 60.357  43.752  1.00 27.36  ? 181  THR B C   1 
ATOM   6288  O  O   . THR B 1 172 ? -9.349  60.110  44.634  1.00 26.18  ? 181  THR B O   1 
ATOM   6289  C  CB  . THR B 1 172 ? -10.934 62.566  44.788  1.00 27.42  ? 181  THR B CB  1 
ATOM   6290  O  OG1 . THR B 1 172 ? -12.053 61.912  45.362  1.00 30.22  ? 181  THR B OG1 1 
ATOM   6291  C  CG2 . THR B 1 172 ? -11.286 64.083  44.567  1.00 25.30  ? 181  THR B CG2 1 
ATOM   6292  N  N   . ALA B 1 173 ? -10.759 59.392  43.018  1.00 24.00  ? 182  ALA B N   1 
ATOM   6293  C  CA  . ALA B 1 173 ? -10.445 57.989  43.281  1.00 22.03  ? 182  ALA B CA  1 
ATOM   6294  C  C   . ALA B 1 173 ? -9.127  57.534  42.755  1.00 22.23  ? 182  ALA B C   1 
ATOM   6295  O  O   . ALA B 1 173 ? -8.620  56.546  43.247  1.00 23.24  ? 182  ALA B O   1 
ATOM   6296  C  CB  . ALA B 1 173 ? -11.540 57.101  42.741  1.00 21.96  ? 182  ALA B CB  1 
ATOM   6297  N  N   . THR B 1 174 ? -8.470  58.239  41.749  1.00 21.83  ? 183  THR B N   1 
ATOM   6298  C  CA  . THR B 1 174 ? -7.212  57.682  41.256  1.00 20.23  ? 183  THR B CA  1 
ATOM   6299  C  C   . THR B 1 174 ? -6.108  57.484  42.305  1.00 20.77  ? 183  THR B C   1 
ATOM   6300  O  O   . THR B 1 174 ? -5.448  56.433  42.293  1.00 22.53  ? 183  THR B O   1 
ATOM   6301  C  CB  . THR B 1 174 ? -6.653  58.536  40.053  1.00 23.65  ? 183  THR B CB  1 
ATOM   6302  O  OG1 . THR B 1 174 ? -7.554  58.310  38.960  1.00 27.12  ? 183  THR B OG1 1 
ATOM   6303  C  CG2 . THR B 1 174 ? -5.263  58.083  39.649  1.00 23.03  ? 183  THR B CG2 1 
ATOM   6304  N  N   . PRO B 1 175 ? -5.841  58.466  43.176  1.00 21.73  ? 184  PRO B N   1 
ATOM   6305  C  CA  . PRO B 1 175 ? -4.777  58.288  44.230  1.00 26.27  ? 184  PRO B CA  1 
ATOM   6306  C  C   . PRO B 1 175 ? -5.057  57.042  45.146  1.00 23.41  ? 184  PRO B C   1 
ATOM   6307  O  O   . PRO B 1 175 ? -4.125  56.357  45.574  1.00 23.20  ? 184  PRO B O   1 
ATOM   6308  C  CB  . PRO B 1 175 ? -4.819  59.630  44.994  1.00 24.88  ? 184  PRO B CB  1 
ATOM   6309  C  CG  . PRO B 1 175 ? -5.300  60.624  43.800  1.00 23.62  ? 184  PRO B CG  1 
ATOM   6310  C  CD  . PRO B 1 175 ? -6.387  59.837  43.164  1.00 21.66  ? 184  PRO B CD  1 
ATOM   6311  N  N   . LEU B 1 176 ? -6.326  56.777  45.420  1.00 24.48  ? 185  LEU B N   1 
ATOM   6312  C  CA  . LEU B 1 176 ? -6.681  55.580  46.249  1.00 23.46  ? 185  LEU B CA  1 
ATOM   6313  C  C   . LEU B 1 176 ? -6.460  54.330  45.470  1.00 22.23  ? 185  LEU B C   1 
ATOM   6314  O  O   . LEU B 1 176 ? -5.826  53.386  45.947  1.00 22.59  ? 185  LEU B O   1 
ATOM   6315  C  CB  . LEU B 1 176 ? -8.144  55.683  46.690  1.00 26.82  ? 185  LEU B CB  1 
ATOM   6316  C  CG  . LEU B 1 176 ? -8.569  54.533  47.628  1.00 30.19  ? 185  LEU B CG  1 
ATOM   6317  C  CD1 . LEU B 1 176 ? -7.636  54.474  48.918  1.00 30.98  ? 185  LEU B CD1 1 
ATOM   6318  C  CD2 . LEU B 1 176 ? -9.981  54.784  47.945  1.00 29.81  ? 185  LEU B CD2 1 
ATOM   6319  N  N   . ALA B 1 177 ? -6.962  54.279  44.197  1.00 21.41  ? 186  ALA B N   1 
ATOM   6320  C  CA  . ALA B 1 177 ? -6.726  53.099  43.415  1.00 21.51  ? 186  ALA B CA  1 
ATOM   6321  C  C   . ALA B 1 177 ? -5.227  52.832  43.270  1.00 21.95  ? 186  ALA B C   1 
ATOM   6322  O  O   . ALA B 1 177 ? -4.786  51.671  43.288  1.00 23.38  ? 186  ALA B O   1 
ATOM   6323  C  CB  . ALA B 1 177 ? -7.343  53.260  41.994  1.00 21.66  ? 186  ALA B CB  1 
ATOM   6324  N  N   A SER B 1 178 ? -4.422  53.895  43.093  0.49 22.30  ? 187  SER B N   1 
ATOM   6325  N  N   B SER B 1 178 ? -4.418  53.883  43.072  0.51 21.85  ? 187  SER B N   1 
ATOM   6326  C  CA  A SER B 1 178 ? -2.960  53.739  42.951  0.49 24.27  ? 187  SER B CA  1 
ATOM   6327  C  CA  B SER B 1 178 ? -2.963  53.721  42.972  0.51 24.13  ? 187  SER B CA  1 
ATOM   6328  C  C   A SER B 1 178 ? -2.336  53.201  44.258  0.49 26.00  ? 187  SER B C   1 
ATOM   6329  C  C   B SER B 1 178 ? -2.409  53.145  44.301  0.51 26.04  ? 187  SER B C   1 
ATOM   6330  O  O   A SER B 1 178 ? -1.449  52.347  44.223  0.49 27.83  ? 187  SER B O   1 
ATOM   6331  O  O   B SER B 1 178 ? -1.590  52.223  44.279  0.51 28.59  ? 187  SER B O   1 
ATOM   6332  C  CB  A SER B 1 178 ? -2.349  55.088  42.587  0.49 25.10  ? 187  SER B CB  1 
ATOM   6333  C  CB  B SER B 1 178 ? -2.297  55.069  42.718  0.51 25.36  ? 187  SER B CB  1 
ATOM   6334  O  OG  A SER B 1 178 ? -2.887  55.467  41.331  0.49 28.24  ? 187  SER B OG  1 
ATOM   6335  O  OG  B SER B 1 178 ? -0.926  54.832  42.463  0.51 29.69  ? 187  SER B OG  1 
ATOM   6336  N  N   . THR B 1 179 ? -2.806  53.696  45.390  1.00 26.66  ? 188  THR B N   1 
ATOM   6337  C  CA  . THR B 1 179 ? -2.355  53.202  46.704  1.00 25.15  ? 188  THR B CA  1 
ATOM   6338  C  C   . THR B 1 179 ? -2.700  51.708  46.799  1.00 27.23  ? 188  THR B C   1 
ATOM   6339  O  O   . THR B 1 179 ? -1.901  50.912  47.311  1.00 27.53  ? 188  THR B O   1 
ATOM   6340  C  CB  . THR B 1 179 ? -3.061  53.986  47.793  1.00 27.06  ? 188  THR B CB  1 
ATOM   6341  O  OG1 . THR B 1 179 ? -2.654  55.345  47.721  1.00 25.34  ? 188  THR B OG1 1 
ATOM   6342  C  CG2 . THR B 1 179 ? -2.744  53.449  49.216  1.00 26.36  ? 188  THR B CG2 1 
ATOM   6343  N  N   . TYR B 1 180 ? -3.874  51.295  46.263  1.00 24.69  ? 189  TYR B N   1 
ATOM   6344  C  CA  . TYR B 1 180 ? -4.264  49.888  46.313  1.00 24.80  ? 189  TYR B CA  1 
ATOM   6345  C  C   . TYR B 1 180 ? -3.634  49.050  45.237  1.00 28.08  ? 189  TYR B C   1 
ATOM   6346  O  O   . TYR B 1 180 ? -3.741  47.818  45.285  1.00 29.21  ? 189  TYR B O   1 
ATOM   6347  C  CB  . TYR B 1 180 ? -5.792  49.711  46.091  1.00 24.34  ? 189  TYR B CB  1 
ATOM   6348  C  CG  . TYR B 1 180 ? -6.728  50.225  47.164  1.00 26.30  ? 189  TYR B CG  1 
ATOM   6349  C  CD1 . TYR B 1 180 ? -6.332  50.271  48.508  1.00 27.22  ? 189  TYR B CD1 1 
ATOM   6350  C  CD2 . TYR B 1 180 ? -8.032  50.603  46.852  1.00 26.46  ? 189  TYR B CD2 1 
ATOM   6351  C  CE1 . TYR B 1 180 ? -7.213  50.693  49.502  1.00 26.09  ? 189  TYR B CE1 1 
ATOM   6352  C  CE2 . TYR B 1 180 ? -8.927  50.996  47.835  1.00 28.41  ? 189  TYR B CE2 1 
ATOM   6353  C  CZ  . TYR B 1 180 ? -8.512  51.048  49.158  1.00 28.80  ? 189  TYR B CZ  1 
ATOM   6354  O  OH  . TYR B 1 180 ? -9.412  51.505  50.070  1.00 31.21  ? 189  TYR B OH  1 
ATOM   6355  N  N   . ASP B 1 181 ? -2.953  49.697  44.250  1.00 27.45  ? 190  ASP B N   1 
ATOM   6356  C  CA  . ASP B 1 181 ? -2.448  49.023  43.051  1.00 26.69  ? 190  ASP B CA  1 
ATOM   6357  C  C   . ASP B 1 181 ? -3.616  48.294  42.388  1.00 23.65  ? 190  ASP B C   1 
ATOM   6358  O  O   . ASP B 1 181 ? -3.525  47.134  42.013  1.00 22.12  ? 190  ASP B O   1 
ATOM   6359  C  CB  . ASP B 1 181 ? -1.269  48.033  43.326  1.00 34.13  ? 190  ASP B CB  1 
ATOM   6360  C  CG  . ASP B 1 181 ? -0.462  47.790  42.041  1.00 42.62  ? 190  ASP B CG  1 
ATOM   6361  O  OD1 . ASP B 1 181 ? -0.980  48.086  40.933  1.00 42.94  ? 190  ASP B OD1 1 
ATOM   6362  O  OD2 . ASP B 1 181 ? 0.684   47.305  42.137  1.00 46.02  ? 190  ASP B OD2 1 
ATOM   6363  N  N   . ALA B 1 182 ? -4.712  49.001  42.192  1.00 21.43  ? 191  ALA B N   1 
ATOM   6364  C  CA  . ALA B 1 182 ? -5.936  48.427  41.620  1.00 20.03  ? 191  ALA B CA  1 
ATOM   6365  C  C   . ALA B 1 182 ? -6.500  49.248  40.435  1.00 19.56  ? 191  ALA B C   1 
ATOM   6366  O  O   . ALA B 1 182 ? -6.202  50.468  40.351  1.00 20.22  ? 191  ALA B O   1 
ATOM   6367  C  CB  . ALA B 1 182 ? -7.032  48.466  42.681  1.00 20.78  ? 191  ALA B CB  1 
ATOM   6368  N  N   . PRO B 1 183 ? -7.278  48.615  39.547  1.00 21.72  ? 192  PRO B N   1 
ATOM   6369  C  CA  . PRO B 1 183 ? -7.889  49.355  38.424  1.00 21.72  ? 192  PRO B CA  1 
ATOM   6370  C  C   . PRO B 1 183 ? -9.223  49.902  38.930  1.00 24.61  ? 192  PRO B C   1 
ATOM   6371  O  O   . PRO B 1 183 ? -9.704  49.466  40.012  1.00 22.88  ? 192  PRO B O   1 
ATOM   6372  C  CB  . PRO B 1 183 ? -8.136  48.295  37.356  1.00 21.58  ? 192  PRO B CB  1 
ATOM   6373  C  CG  . PRO B 1 183 ? -8.265  46.974  38.140  1.00 22.94  ? 192  PRO B CG  1 
ATOM   6374  C  CD  . PRO B 1 183 ? -7.362  47.149  39.364  1.00 20.19  ? 192  PRO B CD  1 
ATOM   6375  N  N   . ILE B 1 184 ? -9.855  50.790  38.156  1.00 21.40  ? 193  ILE B N   1 
ATOM   6376  C  CA  . ILE B 1 184 ? -11.199 51.302  38.474  1.00 18.72  ? 193  ILE B CA  1 
ATOM   6377  C  C   . ILE B 1 184 ? -12.116 50.685  37.444  1.00 22.81  ? 193  ILE B C   1 
ATOM   6378  O  O   . ILE B 1 184 ? -11.824 50.818  36.231  1.00 19.32  ? 193  ILE B O   1 
ATOM   6379  C  CB  . ILE B 1 184 ? -11.266 52.845  38.399  1.00 20.05  ? 193  ILE B CB  1 
ATOM   6380  C  CG1 . ILE B 1 184 ? -10.467 53.464  39.589  1.00 18.12  ? 193  ILE B CG1 1 
ATOM   6381  C  CG2 . ILE B 1 184 ? -12.737 53.331  38.430  1.00 18.09  ? 193  ILE B CG2 1 
ATOM   6382  C  CD1 . ILE B 1 184 ? -10.349 55.016  39.482  1.00 20.64  ? 193  ILE B CD1 1 
ATOM   6383  N  N   . LEU B 1 185 ? -13.190 50.001  37.868  1.00 19.70  ? 194  LEU B N   1 
ATOM   6384  C  CA  . LEU B 1 185 ? -14.169 49.447  36.927  1.00 17.76  ? 194  LEU B CA  1 
ATOM   6385  C  C   . LEU B 1 185 ? -15.457 50.170  37.169  1.00 21.55  ? 194  LEU B C   1 
ATOM   6386  O  O   . LEU B 1 185 ? -15.617 50.844  38.207  1.00 21.38  ? 194  LEU B O   1 
ATOM   6387  C  CB  . LEU B 1 185 ? -14.371 47.917  37.084  1.00 19.15  ? 194  LEU B CB  1 
ATOM   6388  C  CG  . LEU B 1 185 ? -13.160 47.066  36.769  1.00 22.46  ? 194  LEU B CG  1 
ATOM   6389  C  CD1 . LEU B 1 185 ? -13.581 45.595  36.864  1.00 20.49  ? 194  LEU B CD1 1 
ATOM   6390  C  CD2 . LEU B 1 185 ? -12.654 47.336  35.266  1.00 21.33  ? 194  LEU B CD2 1 
ATOM   6391  N  N   . LEU B 1 186 ? -16.416 50.084  36.242  1.00 22.28  ? 195  LEU B N   1 
ATOM   6392  C  CA  . LEU B 1 186 ? -17.601 50.934  36.404  1.00 21.65  ? 195  LEU B CA  1 
ATOM   6393  C  C   . LEU B 1 186 ? -18.935 50.143  36.650  1.00 20.80  ? 195  LEU B C   1 
ATOM   6394  O  O   . LEU B 1 186 ? -19.129 49.049  36.088  1.00 21.19  ? 195  LEU B O   1 
ATOM   6395  C  CB  . LEU B 1 186 ? -17.749 51.737  35.130  1.00 22.40  ? 195  LEU B CB  1 
ATOM   6396  C  CG  . LEU B 1 186 ? -16.500 52.584  34.786  1.00 21.51  ? 195  LEU B CG  1 
ATOM   6397  C  CD1 . LEU B 1 186 ? -16.812 53.284  33.407  1.00 18.82  ? 195  LEU B CD1 1 
ATOM   6398  C  CD2 . LEU B 1 186 ? -16.262 53.634  35.815  1.00 18.99  ? 195  LEU B CD2 1 
ATOM   6399  N  N   . ALA B 1 187 ? -19.800 50.743  37.433  1.00 22.87  ? 196  ALA B N   1 
ATOM   6400  C  CA  . ALA B 1 187 ? -21.126 50.158  37.698  1.00 27.10  ? 196  ALA B CA  1 
ATOM   6401  C  C   . ALA B 1 187 ? -22.229 51.104  37.267  1.00 28.03  ? 196  ALA B C   1 
ATOM   6402  O  O   . ALA B 1 187 ? -21.996 52.246  36.897  1.00 28.03  ? 196  ALA B O   1 
ATOM   6403  C  CB  . ALA B 1 187 ? -21.262 49.900  39.210  1.00 23.47  ? 196  ALA B CB  1 
ATOM   6404  N  N   . ASN B 1 188 ? -23.457 50.615  37.292  1.00 30.47  ? 197  ASN B N   1 
ATOM   6405  C  CA  . ASN B 1 188 ? -24.636 51.474  37.137  1.00 31.43  ? 197  ASN B CA  1 
ATOM   6406  C  C   . ASN B 1 188 ? -25.190 51.546  38.607  1.00 32.35  ? 197  ASN B C   1 
ATOM   6407  O  O   . ASN B 1 188 ? -24.652 50.859  39.492  1.00 30.23  ? 197  ASN B O   1 
ATOM   6408  C  CB  . ASN B 1 188 ? -25.665 50.836  36.198  1.00 31.19  ? 197  ASN B CB  1 
ATOM   6409  C  CG  . ASN B 1 188 ? -25.185 50.924  34.778  1.00 34.85  ? 197  ASN B CG  1 
ATOM   6410  O  OD1 . ASN B 1 188 ? -24.905 52.020  34.292  1.00 34.76  ? 197  ASN B OD1 1 
ATOM   6411  N  ND2 . ASN B 1 188 ? -25.061 49.841  34.061  1.00 33.99  ? 197  ASN B ND2 1 
ATOM   6412  N  N   . LYS B 1 189 ? -26.228 52.322  38.881  1.00 37.21  ? 198  LYS B N   1 
ATOM   6413  C  CA  . LYS B 1 189 ? -26.726 52.413  40.276  1.00 42.37  ? 198  LYS B CA  1 
ATOM   6414  C  C   . LYS B 1 189 ? -27.207 51.092  40.831  1.00 45.94  ? 198  LYS B C   1 
ATOM   6415  O  O   . LYS B 1 189 ? -26.855 50.750  41.957  1.00 42.94  ? 198  LYS B O   1 
ATOM   6416  C  CB  . LYS B 1 189 ? -27.883 53.414  40.367  1.00 46.64  ? 198  LYS B CB  1 
ATOM   6417  C  CG  . LYS B 1 189 ? -28.392 53.560  41.795  1.00 51.24  ? 198  LYS B CG  1 
ATOM   6418  C  CD  . LYS B 1 189 ? -29.382 54.727  41.913  1.00 58.81  ? 198  LYS B CD  1 
ATOM   6419  C  CE  . LYS B 1 189 ? -30.819 54.245  41.935  1.00 60.94  ? 198  LYS B CE  1 
ATOM   6420  N  NZ  . LYS B 1 189 ? -31.111 53.391  43.114  1.00 59.55  ? 198  LYS B NZ  1 
ATOM   6421  N  N   . ASP B 1 190 ? -27.996 50.338  40.043  1.00 45.69  ? 199  ASP B N   1 
ATOM   6422  C  CA  . ASP B 1 190 ? -28.577 49.067  40.521  1.00 45.85  ? 199  ASP B CA  1 
ATOM   6423  C  C   . ASP B 1 190 ? -28.015 47.822  39.904  1.00 46.06  ? 199  ASP B C   1 
ATOM   6424  O  O   . ASP B 1 190 ? -28.544 46.737  40.157  1.00 44.89  ? 199  ASP B O   1 
ATOM   6425  C  CB  . ASP B 1 190 ? -30.095 49.092  40.285  1.00 46.45  ? 199  ASP B CB  1 
ATOM   6426  C  CG  . ASP B 1 190 ? -30.752 50.208  41.072  1.00 49.79  ? 199  ASP B CG  1 
ATOM   6427  O  OD1 . ASP B 1 190 ? -30.347 50.432  42.259  1.00 49.19  ? 199  ASP B OD1 1 
ATOM   6428  O  OD2 . ASP B 1 190 ? -31.640 50.875  40.515  1.00 49.52  ? 199  ASP B OD2 1 
ATOM   6429  N  N   . ASP B 1 191 ? -26.947 47.913  39.106  1.00 40.94  ? 200  ASP B N   1 
ATOM   6430  C  CA  . ASP B 1 191 ? -26.411 46.685  38.500  1.00 38.39  ? 200  ASP B CA  1 
ATOM   6431  C  C   . ASP B 1 191 ? -24.992 46.918  37.972  1.00 37.47  ? 200  ASP B C   1 
ATOM   6432  O  O   . ASP B 1 191 ? -24.518 48.056  37.976  1.00 35.51  ? 200  ASP B O   1 
ATOM   6433  C  CB  . ASP B 1 191 ? -27.260 46.255  37.292  1.00 40.49  ? 200  ASP B CB  1 
ATOM   6434  C  CG  . ASP B 1 191 ? -27.276 47.317  36.201  1.00 51.05  ? 200  ASP B CG  1 
ATOM   6435  O  OD1 . ASP B 1 191 ? -28.216 48.148  36.189  1.00 54.07  ? 200  ASP B OD1 1 
ATOM   6436  O  OD2 . ASP B 1 191 ? -26.329 47.327  35.343  1.00 52.64  ? 200  ASP B OD2 1 
ATOM   6437  N  N   . ILE B 1 192 ? -24.335 45.853  37.569  1.00 35.59  ? 201  ILE B N   1 
ATOM   6438  C  CA  . ILE B 1 192 ? -23.056 45.979  36.894  1.00 34.99  ? 201  ILE B CA  1 
ATOM   6439  C  C   . ILE B 1 192 ? -23.302 45.315  35.578  1.00 35.43  ? 201  ILE B C   1 
ATOM   6440  O  O   . ILE B 1 192 ? -23.915 44.236  35.535  1.00 33.59  ? 201  ILE B O   1 
ATOM   6441  C  CB  . ILE B 1 192 ? -21.872 45.289  37.576  1.00 35.32  ? 201  ILE B CB  1 
ATOM   6442  C  CG1 . ILE B 1 192 ? -22.239 43.861  37.953  1.00 32.87  ? 201  ILE B CG1 1 
ATOM   6443  C  CG2 . ILE B 1 192 ? -21.415 46.118  38.800  1.00 33.97  ? 201  ILE B CG2 1 
ATOM   6444  C  CD1 . ILE B 1 192 ? -21.060 43.114  38.526  1.00 29.78  ? 201  ILE B CD1 1 
ATOM   6445  N  N   . PRO B 1 193 ? -22.891 45.937  34.475  1.00 35.25  ? 202  PRO B N   1 
ATOM   6446  C  CA  . PRO B 1 193 ? -23.093 45.293  33.167  1.00 31.41  ? 202  PRO B CA  1 
ATOM   6447  C  C   . PRO B 1 193 ? -22.226 44.039  33.083  1.00 31.15  ? 202  PRO B C   1 
ATOM   6448  O  O   . PRO B 1 193 ? -21.305 43.841  33.881  1.00 30.00  ? 202  PRO B O   1 
ATOM   6449  C  CB  . PRO B 1 193 ? -22.651 46.355  32.158  1.00 32.71  ? 202  PRO B CB  1 
ATOM   6450  C  CG  . PRO B 1 193 ? -22.441 47.643  32.937  1.00 35.93  ? 202  PRO B CG  1 
ATOM   6451  C  CD  . PRO B 1 193 ? -22.270 47.277  34.382  1.00 34.07  ? 202  PRO B CD  1 
ATOM   6452  N  N   . GLU B 1 194 ? -22.473 43.214  32.069  1.00 29.82  ? 203  GLU B N   1 
ATOM   6453  C  CA  . GLU B 1 194 ? -21.753 41.969  31.875  1.00 31.01  ? 203  GLU B CA  1 
ATOM   6454  C  C   . GLU B 1 194 ? -20.234 42.218  31.674  1.00 29.18  ? 203  GLU B C   1 
ATOM   6455  O  O   . GLU B 1 194 ? -19.421 41.403  32.087  1.00 30.22  ? 203  GLU B O   1 
ATOM   6456  C  CB  . GLU B 1 194 ? -22.325 41.255  30.623  1.00 34.86  ? 203  GLU B CB  1 
ATOM   6457  C  CG  . GLU B 1 194 ? -21.456 40.087  30.157  1.00 45.67  ? 203  GLU B CG  1 
ATOM   6458  C  CD  . GLU B 1 194 ? -21.327 38.987  31.231  1.00 57.48  ? 203  GLU B CD  1 
ATOM   6459  O  OE1 . GLU B 1 194 ? -22.357 38.671  31.879  1.00 61.73  ? 203  GLU B OE1 1 
ATOM   6460  O  OE2 . GLU B 1 194 ? -20.208 38.455  31.421  1.00 56.27  ? 203  GLU B OE2 1 
ATOM   6461  N  N   . SER B 1 195 ? -19.868 43.361  31.035  1.00 28.47  ? 204  SER B N   1 
ATOM   6462  C  CA  . SER B 1 195 ? -18.451 43.649  30.806  1.00 28.03  ? 204  SER B CA  1 
ATOM   6463  C  C   . SER B 1 195 ? -17.746 43.753  32.180  1.00 22.98  ? 204  SER B C   1 
ATOM   6464  O  O   . SER B 1 195 ? -16.717 43.132  32.379  1.00 23.93  ? 204  SER B O   1 
ATOM   6465  C  CB  . SER B 1 195 ? -18.302 44.964  30.052  1.00 27.06  ? 204  SER B CB  1 
ATOM   6466  O  OG  . SER B 1 195 ? -18.988 45.987  30.754  1.00 27.95  ? 204  SER B OG  1 
ATOM   6467  N  N   . THR B 1 196 ? -18.285 44.531  33.068  1.00 23.13  ? 205  THR B N   1 
ATOM   6468  C  CA  . THR B 1 196 ? -17.685 44.654  34.389  1.00 25.30  ? 205  THR B CA  1 
ATOM   6469  C  C   . THR B 1 196 ? -17.736 43.321  35.170  1.00 28.37  ? 205  THR B C   1 
ATOM   6470  O  O   . THR B 1 196 ? -16.807 42.938  35.870  1.00 25.26  ? 205  THR B O   1 
ATOM   6471  C  CB  . THR B 1 196 ? -18.456 45.701  35.171  1.00 23.43  ? 205  THR B CB  1 
ATOM   6472  O  OG1 . THR B 1 196 ? -18.271 46.975  34.520  1.00 24.53  ? 205  THR B OG1 1 
ATOM   6473  C  CG2 . THR B 1 196 ? -18.027 45.748  36.617  1.00 23.44  ? 205  THR B CG2 1 
ATOM   6474  N  N   . LYS B 1 197 ? -18.871 42.623  35.063  1.00 27.90  ? 206  LYS B N   1 
ATOM   6475  C  CA  . LYS B 1 197 ? -19.005 41.340  35.729  1.00 27.58  ? 206  LYS B CA  1 
ATOM   6476  C  C   . LYS B 1 197 ? -17.910 40.395  35.327  1.00 25.69  ? 206  LYS B C   1 
ATOM   6477  O  O   . LYS B 1 197 ? -17.216 39.812  36.153  1.00 25.93  ? 206  LYS B O   1 
ATOM   6478  C  CB  . LYS B 1 197 ? -20.411 40.747  35.343  1.00 31.17  ? 206  LYS B CB  1 
ATOM   6479  C  CG  . LYS B 1 197 ? -20.554 39.327  35.831  1.00 44.66  ? 206  LYS B CG  1 
ATOM   6480  C  CD  . LYS B 1 197 ? -22.030 38.894  35.736  1.00 54.54  ? 206  LYS B CD  1 
ATOM   6481  C  CE  . LYS B 1 197 ? -22.212 37.483  36.248  1.00 63.81  ? 206  LYS B CE  1 
ATOM   6482  N  NZ  . LYS B 1 197 ? -23.512 36.904  35.779  1.00 63.50  ? 206  LYS B NZ  1 
ATOM   6483  N  N   . ALA B 1 198 ? -17.721 40.221  34.018  1.00 25.60  ? 207  ALA B N   1 
ATOM   6484  C  CA  . ALA B 1 198 ? -16.703 39.282  33.522  1.00 25.52  ? 207  ALA B CA  1 
ATOM   6485  C  C   . ALA B 1 198 ? -15.272 39.741  33.880  1.00 26.50  ? 207  ALA B C   1 
ATOM   6486  O  O   . ALA B 1 198 ? -14.408 38.905  34.106  1.00 25.54  ? 207  ALA B O   1 
ATOM   6487  C  CB  . ALA B 1 198 ? -16.831 39.135  32.003  1.00 24.52  ? 207  ALA B CB  1 
ATOM   6488  N  N   . GLU B 1 199 ? -15.029 41.078  33.946  1.00 25.70  ? 208  GLU B N   1 
ATOM   6489  C  CA  . GLU B 1 199 ? -13.648 41.524  34.305  1.00 21.54  ? 208  GLU B CA  1 
ATOM   6490  C  C   . GLU B 1 199 ? -13.414 41.321  35.799  1.00 23.01  ? 208  GLU B C   1 
ATOM   6491  O  O   . GLU B 1 199 ? -12.294 40.965  36.214  1.00 23.33  ? 208  GLU B O   1 
ATOM   6492  C  CB  . GLU B 1 199 ? -13.441 43.001  33.861  1.00 21.99  ? 208  GLU B CB  1 
ATOM   6493  C  CG  . GLU B 1 199 ? -12.024 43.516  34.131  1.00 21.85  ? 208  GLU B CG  1 
ATOM   6494  C  CD  . GLU B 1 199 ? -10.883 42.716  33.459  1.00 26.18  ? 208  GLU B CD  1 
ATOM   6495  O  OE1 . GLU B 1 199 ? -11.099 41.829  32.581  1.00 25.37  ? 208  GLU B OE1 1 
ATOM   6496  O  OE2 . GLU B 1 199 ? -9.710  42.999  33.806  1.00 23.93  ? 208  GLU B OE2 1 
ATOM   6497  N  N   . LEU B 1 200 ? -14.450 41.522  36.639  1.00 24.36  ? 209  LEU B N   1 
ATOM   6498  C  CA  . LEU B 1 200 ? -14.231 41.225  38.052  1.00 25.65  ? 209  LEU B CA  1 
ATOM   6499  C  C   . LEU B 1 200 ? -13.821 39.751  38.220  1.00 25.19  ? 209  LEU B C   1 
ATOM   6500  O  O   . LEU B 1 200 ? -12.892 39.409  38.962  1.00 27.80  ? 209  LEU B O   1 
ATOM   6501  C  CB  . LEU B 1 200 ? -15.560 41.473  38.814  1.00 24.97  ? 209  LEU B CB  1 
ATOM   6502  C  CG  . LEU B 1 200 ? -15.873 42.917  39.021  1.00 27.81  ? 209  LEU B CG  1 
ATOM   6503  C  CD1 . LEU B 1 200 ? -17.369 43.095  39.492  1.00 28.40  ? 209  LEU B CD1 1 
ATOM   6504  C  CD2 . LEU B 1 200 ? -14.905 43.389  40.070  1.00 28.03  ? 209  LEU B CD2 1 
ATOM   6505  N  N   . LYS B 1 201 ? -14.524 38.858  37.513  1.00 27.83  ? 210  LYS B N   1 
ATOM   6506  C  CA  . LYS B 1 201 ? -14.211 37.440  37.641  1.00 30.75  ? 210  LYS B CA  1 
ATOM   6507  C  C   . LYS B 1 201 ? -12.830 37.179  37.139  1.00 31.28  ? 210  LYS B C   1 
ATOM   6508  O  O   . LYS B 1 201 ? -12.092 36.400  37.745  1.00 29.27  ? 210  LYS B O   1 
ATOM   6509  C  CB  . LYS B 1 201 ? -15.189 36.567  36.828  1.00 33.32  ? 210  LYS B CB  1 
ATOM   6510  C  CG  . LYS B 1 201 ? -16.642 36.571  37.354  1.00 38.33  ? 210  LYS B CG  1 
ATOM   6511  C  CD  . LYS B 1 201 ? -17.520 35.822  36.318  1.00 40.90  ? 210  LYS B CD  1 
ATOM   6512  C  CE  . LYS B 1 201 ? -18.969 35.705  36.717  1.00 50.32  ? 210  LYS B CE  1 
ATOM   6513  N  NZ  . LYS B 1 201 ? -19.090 34.861  37.954  1.00 57.82  ? 210  LYS B NZ  1 
ATOM   6514  N  N   . ARG B 1 202 ? -12.466 37.816  35.996  1.00 27.67  ? 211  ARG B N   1 
ATOM   6515  C  CA  . ARG B 1 202 ? -11.112 37.618  35.459  1.00 27.14  ? 211  ARG B CA  1 
ATOM   6516  C  C   . ARG B 1 202 ? -10.032 38.119  36.460  1.00 25.50  ? 211  ARG B C   1 
ATOM   6517  O  O   . ARG B 1 202 ? -9.013  37.444  36.639  1.00 26.74  ? 211  ARG B O   1 
ATOM   6518  C  CB  . ARG B 1 202 ? -10.971 38.344  34.077  1.00 26.01  ? 211  ARG B CB  1 
ATOM   6519  C  CG  . ARG B 1 202 ? -9.845  37.765  33.248  1.00 29.34  ? 211  ARG B CG  1 
ATOM   6520  C  CD  . ARG B 1 202 ? -9.461  38.683  32.076  1.00 27.09  ? 211  ARG B CD  1 
ATOM   6521  N  NE  . ARG B 1 202 ? -8.984  39.974  32.597  1.00 26.59  ? 211  ARG B NE  1 
ATOM   6522  C  CZ  . ARG B 1 202 ? -7.771  40.161  33.108  1.00 23.90  ? 211  ARG B CZ  1 
ATOM   6523  N  NH1 . ARG B 1 202 ? -7.428  41.348  33.611  1.00 23.46  ? 211  ARG B NH1 1 
ATOM   6524  N  NH2 . ARG B 1 202 ? -6.882  39.174  33.099  1.00 23.46  ? 211  ARG B NH2 1 
ATOM   6525  N  N   . LEU B 1 203 ? -10.228 39.276  37.110  1.00 24.78  ? 212  LEU B N   1 
ATOM   6526  C  CA  . LEU B 1 203 ? -9.238  39.798  38.044  1.00 23.26  ? 212  LEU B CA  1 
ATOM   6527  C  C   . LEU B 1 203 ? -9.130  38.965  39.318  1.00 27.78  ? 212  LEU B C   1 
ATOM   6528  O  O   . LEU B 1 203 ? -8.071  38.963  39.978  1.00 25.60  ? 212  LEU B O   1 
ATOM   6529  C  CB  . LEU B 1 203 ? -9.645  41.213  38.389  1.00 24.93  ? 212  LEU B CB  1 
ATOM   6530  C  CG  . LEU B 1 203 ? -9.462  42.236  37.212  1.00 22.97  ? 212  LEU B CG  1 
ATOM   6531  C  CD1 . LEU B 1 203 ? -10.119 43.518  37.550  1.00 20.52  ? 212  LEU B CD1 1 
ATOM   6532  C  CD2 . LEU B 1 203 ? -7.913  42.433  36.949  1.00 21.26  ? 212  LEU B CD2 1 
ATOM   6533  N  N   . ASN B 1 204 ? -10.226 38.263  39.664  1.00 27.15  ? 213  ASN B N   1 
ATOM   6534  C  CA  . ASN B 1 204 ? -10.254 37.408  40.868  1.00 30.73  ? 213  ASN B CA  1 
ATOM   6535  C  C   . ASN B 1 204 ? -9.859  38.182  42.104  1.00 28.17  ? 213  ASN B C   1 
ATOM   6536  O  O   . ASN B 1 204 ? -8.944  37.811  42.834  1.00 27.06  ? 213  ASN B O   1 
ATOM   6537  C  CB  . ASN B 1 204 ? -9.333  36.240  40.680  1.00 34.21  ? 213  ASN B CB  1 
ATOM   6538  C  CG  . ASN B 1 204 ? -9.477  35.195  41.778  1.00 43.20  ? 213  ASN B CG  1 
ATOM   6539  O  OD1 . ASN B 1 204 ? -10.570 34.993  42.329  1.00 43.08  ? 213  ASN B OD1 1 
ATOM   6540  N  ND2 . ASN B 1 204 ? -8.406  34.548  42.166  1.00 48.52  ? 213  ASN B ND2 1 
ATOM   6541  N  N   . PRO B 1 205 ? -10.532 39.279  42.401  1.00 26.69  ? 214  PRO B N   1 
ATOM   6542  C  CA  . PRO B 1 205 ? -10.143 40.018  43.602  1.00 27.28  ? 214  PRO B CA  1 
ATOM   6543  C  C   . PRO B 1 205 ? -10.646 39.384  44.920  1.00 32.21  ? 214  PRO B C   1 
ATOM   6544  O  O   . PRO B 1 205 ? -11.480 38.500  44.871  1.00 32.15  ? 214  PRO B O   1 
ATOM   6545  C  CB  . PRO B 1 205 ? -10.828 41.366  43.417  1.00 28.28  ? 214  PRO B CB  1 
ATOM   6546  C  CG  . PRO B 1 205 ? -12.054 41.054  42.589  1.00 27.97  ? 214  PRO B CG  1 
ATOM   6547  C  CD  . PRO B 1 205 ? -11.709 39.863  41.745  1.00 28.29  ? 214  PRO B CD  1 
ATOM   6548  N  N   . SER B 1 206 ? -10.161 39.902  46.067  1.00 31.01  ? 215  SER B N   1 
ATOM   6549  C  CA  . SER B 1 206 ? -10.605 39.514  47.419  1.00 37.13  ? 215  SER B CA  1 
ATOM   6550  C  C   . SER B 1 206 ? -11.461 40.638  47.957  1.00 38.44  ? 215  SER B C   1 
ATOM   6551  O  O   . SER B 1 206 ? -12.324 40.463  48.814  1.00 36.29  ? 215  SER B O   1 
ATOM   6552  C  CB  . SER B 1 206 ? -9.399  39.404  48.358  1.00 38.90  ? 215  SER B CB  1 
ATOM   6553  O  OG  . SER B 1 206 ? -8.506  38.445  47.831  1.00 50.19  ? 215  SER B OG  1 
ATOM   6554  N  N   . ASP B 1 207 ? -11.186 41.858  47.457  1.00 33.73  ? 216  ASP B N   1 
ATOM   6555  C  CA  . ASP B 1 207 ? -11.876 43.035  47.947  1.00 31.61  ? 216  ASP B CA  1 
ATOM   6556  C  C   . ASP B 1 207 ? -12.322 43.965  46.847  1.00 31.75  ? 216  ASP B C   1 
ATOM   6557  O  O   . ASP B 1 207 ? -11.569 44.142  45.884  1.00 27.45  ? 216  ASP B O   1 
ATOM   6558  C  CB  . ASP B 1 207 ? -10.924 43.850  48.816  1.00 34.81  ? 216  ASP B CB  1 
ATOM   6559  C  CG  . ASP B 1 207 ? -10.551 43.150  50.115  1.00 48.58  ? 216  ASP B CG  1 
ATOM   6560  O  OD1 . ASP B 1 207 ? -9.501  42.477  50.141  1.00 50.88  ? 216  ASP B OD1 1 
ATOM   6561  O  OD2 . ASP B 1 207 ? -11.315 43.289  51.107  1.00 50.24  ? 216  ASP B OD2 1 
ATOM   6562  N  N   . VAL B 1 208 ? -13.504 44.541  46.988  1.00 27.41  ? 217  VAL B N   1 
ATOM   6563  C  CA  . VAL B 1 208 ? -14.010 45.515  46.044  1.00 28.49  ? 217  VAL B CA  1 
ATOM   6564  C  C   . VAL B 1 208 ? -14.330 46.713  46.842  1.00 29.34  ? 217  VAL B C   1 
ATOM   6565  O  O   . VAL B 1 208 ? -15.030 46.597  47.871  1.00 29.89  ? 217  VAL B O   1 
ATOM   6566  C  CB  . VAL B 1 208 ? -15.247 44.983  45.309  1.00 27.93  ? 217  VAL B CB  1 
ATOM   6567  C  CG1 . VAL B 1 208 ? -15.902 46.083  44.481  1.00 27.43  ? 217  VAL B CG1 1 
ATOM   6568  C  CG2 . VAL B 1 208 ? -14.842 43.799  44.457  1.00 27.75  ? 217  VAL B CG2 1 
ATOM   6569  N  N   . ILE B 1 209 ? -13.853 47.902  46.407  1.00 23.91  ? 218  ILE B N   1 
ATOM   6570  C  CA  . ILE B 1 209 ? -14.107 49.126  47.139  1.00 23.95  ? 218  ILE B CA  1 
ATOM   6571  C  C   . ILE B 1 209 ? -15.007 49.991  46.336  1.00 28.70  ? 218  ILE B C   1 
ATOM   6572  O  O   . ILE B 1 209 ? -14.648 50.341  45.193  1.00 27.80  ? 218  ILE B O   1 
ATOM   6573  C  CB  . ILE B 1 209 ? -12.759 49.834  47.483  1.00 25.60  ? 218  ILE B CB  1 
ATOM   6574  C  CG1 . ILE B 1 209 ? -11.866 48.911  48.350  1.00 24.24  ? 218  ILE B CG1 1 
ATOM   6575  C  CG2 . ILE B 1 209 ? -13.039 51.152  48.257  1.00 25.75  ? 218  ILE B CG2 1 
ATOM   6576  C  CD1 . ILE B 1 209 ? -11.015 47.915  47.515  1.00 26.64  ? 218  ILE B CD1 1 
ATOM   6577  N  N   . ILE B 1 210 ? -16.167 50.371  46.877  1.00 25.44  ? 219  ILE B N   1 
ATOM   6578  C  CA  . ILE B 1 210 ? -17.130 51.190  46.171  1.00 25.71  ? 219  ILE B CA  1 
ATOM   6579  C  C   . ILE B 1 210 ? -16.948 52.628  46.518  1.00 29.53  ? 219  ILE B C   1 
ATOM   6580  O  O   . ILE B 1 210 ? -16.829 52.949  47.713  1.00 27.01  ? 219  ILE B O   1 
ATOM   6581  C  CB  . ILE B 1 210 ? -18.586 50.801  46.608  1.00 28.73  ? 219  ILE B CB  1 
ATOM   6582  C  CG1 . ILE B 1 210 ? -18.797 49.282  46.485  1.00 34.96  ? 219  ILE B CG1 1 
ATOM   6583  C  CG2 . ILE B 1 210 ? -19.615 51.614  45.834  1.00 28.92  ? 219  ILE B CG2 1 
ATOM   6584  C  CD1 . ILE B 1 210 ? -18.893 48.759  45.134  1.00 36.66  ? 219  ILE B CD1 1 
ATOM   6585  N  N   . ILE B 1 211 ? -16.915 53.534  45.495  1.00 25.87  ? 220  ILE B N   1 
ATOM   6586  C  CA  . ILE B 1 211 ? -16.771 54.952  45.781  1.00 26.87  ? 220  ILE B CA  1 
ATOM   6587  C  C   . ILE B 1 211 ? -18.145 55.579  45.627  1.00 30.39  ? 220  ILE B C   1 
ATOM   6588  O  O   . ILE B 1 211 ? -18.747 55.475  44.555  1.00 30.80  ? 220  ILE B O   1 
ATOM   6589  C  CB  . ILE B 1 211 ? -15.756 55.734  44.828  1.00 27.00  ? 220  ILE B CB  1 
ATOM   6590  C  CG1 . ILE B 1 211 ? -14.381 55.103  44.790  1.00 30.25  ? 220  ILE B CG1 1 
ATOM   6591  C  CG2 . ILE B 1 211 ? -15.674 57.200  45.326  1.00 27.60  ? 220  ILE B CG2 1 
ATOM   6592  C  CD1 . ILE B 1 211 ? -13.651 55.120  46.143  1.00 31.46  ? 220  ILE B CD1 1 
ATOM   6593  N  N   . GLY B 1 212 ? -18.652 56.251  46.666  1.00 29.74  ? 221  GLY B N   1 
ATOM   6594  C  CA  . GLY B 1 212 ? -19.937 56.908  46.539  1.00 29.84  ? 221  GLY B CA  1 
ATOM   6595  C  C   . GLY B 1 212 ? -20.958 56.350  47.541  1.00 35.60  ? 221  GLY B C   1 
ATOM   6596  O  O   . GLY B 1 212 ? -20.814 55.240  48.029  1.00 34.12  ? 221  GLY B O   1 
ATOM   6597  N  N   . ASP B 1 213 ? -22.005 57.140  47.812  1.00 37.84  ? 222  ASP B N   1 
ATOM   6598  C  CA  . ASP B 1 213 ? -23.050 56.737  48.733  1.00 41.20  ? 222  ASP B CA  1 
ATOM   6599  C  C   . ASP B 1 213 ? -24.032 55.847  47.968  1.00 43.08  ? 222  ASP B C   1 
ATOM   6600  O  O   . ASP B 1 213 ? -23.828 55.445  46.799  1.00 38.67  ? 222  ASP B O   1 
ATOM   6601  C  CB  . ASP B 1 213 ? -23.757 57.989  49.341  1.00 39.49  ? 222  ASP B CB  1 
ATOM   6602  C  CG  . ASP B 1 213 ? -24.706 58.747  48.422  1.00 46.44  ? 222  ASP B CG  1 
ATOM   6603  O  OD1 . ASP B 1 213 ? -24.981 58.265  47.316  1.00 51.52  ? 222  ASP B OD1 1 
ATOM   6604  O  OD2 . ASP B 1 213 ? -25.168 59.824  48.805  1.00 50.99  ? 222  ASP B OD2 1 
ATOM   6605  N  N   . ASP B 1 214 ? -25.134 55.586  48.657  1.00 43.11  ? 223  ASP B N   1 
ATOM   6606  C  CA  . ASP B 1 214 ? -26.255 54.777  48.252  1.00 43.65  ? 223  ASP B CA  1 
ATOM   6607  C  C   . ASP B 1 214 ? -26.965 55.282  47.033  1.00 38.76  ? 223  ASP B C   1 
ATOM   6608  O  O   . ASP B 1 214 ? -27.505 54.486  46.265  1.00 39.39  ? 223  ASP B O   1 
ATOM   6609  C  CB  . ASP B 1 214 ? -27.249 54.733  49.454  1.00 47.38  ? 223  ASP B CB  1 
ATOM   6610  C  CG  . ASP B 1 214 ? -27.138 53.407  50.123  1.00 55.54  ? 223  ASP B CG  1 
ATOM   6611  O  OD1 . ASP B 1 214 ? -26.023 52.835  50.114  1.00 60.00  ? 223  ASP B OD1 1 
ATOM   6612  O  OD2 . ASP B 1 214 ? -28.167 52.920  50.649  1.00 61.55  ? 223  ASP B OD2 1 
ATOM   6613  N  N   . GLY B 1 215 ? -26.999 56.575  46.873  1.00 36.39  ? 224  GLY B N   1 
ATOM   6614  C  CA  . GLY B 1 215 ? -27.601 57.164  45.693  1.00 39.71  ? 224  GLY B CA  1 
ATOM   6615  C  C   . GLY B 1 215 ? -26.756 56.912  44.446  1.00 41.75  ? 224  GLY B C   1 
ATOM   6616  O  O   . GLY B 1 215 ? -27.304 56.901  43.351  1.00 42.33  ? 224  GLY B O   1 
ATOM   6617  N  N   . SER B 1 216 ? -25.418 56.685  44.599  1.00 39.81  ? 225  SER B N   1 
ATOM   6618  C  CA  . SER B 1 216 ? -24.541 56.441  43.431  1.00 36.80  ? 225  SER B CA  1 
ATOM   6619  C  C   . SER B 1 216 ? -24.453 54.976  43.072  1.00 34.21  ? 225  SER B C   1 
ATOM   6620  O  O   . SER B 1 216 ? -24.617 54.631  41.909  1.00 35.29  ? 225  SER B O   1 
ATOM   6621  C  CB  . SER B 1 216 ? -23.119 56.931  43.703  1.00 39.58  ? 225  SER B CB  1 
ATOM   6622  O  OG  . SER B 1 216 ? -23.091 58.311  44.045  1.00 45.74  ? 225  SER B OG  1 
ATOM   6623  N  N   . VAL B 1 217 ? -24.180 54.103  44.030  1.00 31.56  ? 226  VAL B N   1 
ATOM   6624  C  CA  . VAL B 1 217 ? -24.093 52.655  43.739  1.00 34.01  ? 226  VAL B CA  1 
ATOM   6625  C  C   . VAL B 1 217 ? -24.938 51.984  44.870  1.00 37.78  ? 226  VAL B C   1 
ATOM   6626  O  O   . VAL B 1 217 ? -24.513 51.976  46.030  1.00 35.94  ? 226  VAL B O   1 
ATOM   6627  C  CB  . VAL B 1 217 ? -22.603 52.174  43.761  1.00 32.79  ? 226  VAL B CB  1 
ATOM   6628  C  CG1 . VAL B 1 217 ? -22.519 50.660  43.593  1.00 29.20  ? 226  VAL B CG1 1 
ATOM   6629  C  CG2 . VAL B 1 217 ? -21.803 52.873  42.650  1.00 28.97  ? 226  VAL B CG2 1 
ATOM   6630  N  N   . SER B 1 218 ? -26.094 51.446  44.529  1.00 38.13  ? 227  SER B N   1 
ATOM   6631  C  CA  . SER B 1 218 ? -26.996 50.905  45.568  1.00 39.66  ? 227  SER B CA  1 
ATOM   6632  C  C   . SER B 1 218 ? -26.697 49.487  46.002  1.00 40.92  ? 227  SER B C   1 
ATOM   6633  O  O   . SER B 1 218 ? -25.833 48.784  45.457  1.00 38.77  ? 227  SER B O   1 
ATOM   6634  C  CB  . SER B 1 218 ? -28.415 50.943  45.031  1.00 39.10  ? 227  SER B CB  1 
ATOM   6635  O  OG  . SER B 1 218 ? -28.602 49.829  44.165  1.00 35.37  ? 227  SER B OG  1 
ATOM   6636  N  N   . GLN B 1 219 ? -27.468 49.030  47.007  1.00 42.82  ? 228  GLN B N   1 
ATOM   6637  C  CA  . GLN B 1 219 ? -27.329 47.678  47.519  1.00 42.13  ? 228  GLN B CA  1 
ATOM   6638  C  C   . GLN B 1 219 ? -27.608 46.667  46.411  1.00 39.24  ? 228  GLN B C   1 
ATOM   6639  O  O   . GLN B 1 219 ? -27.035 45.593  46.412  1.00 40.04  ? 228  GLN B O   1 
ATOM   6640  C  CB  . GLN B 1 219 ? -28.305 47.498  48.689  1.00 49.18  ? 228  GLN B CB  1 
ATOM   6641  C  CG  . GLN B 1 219 ? -27.559 47.341  49.984  1.00 57.17  ? 228  GLN B CG  1 
ATOM   6642  C  CD  . GLN B 1 219 ? -26.436 46.330  49.857  1.00 62.58  ? 228  GLN B CD  1 
ATOM   6643  O  OE1 . GLN B 1 219 ? -25.310 46.577  50.305  1.00 63.32  ? 228  GLN B OE1 1 
ATOM   6644  N  NE2 . GLN B 1 219 ? -26.709 45.145  49.253  1.00 57.91  ? 228  GLN B NE2 1 
ATOM   6645  N  N   . LYS B 1 220 ? -28.476 47.000  45.463  1.00 40.36  ? 229  LYS B N   1 
ATOM   6646  C  CA  . LYS B 1 220 ? -28.726 46.070  44.354  1.00 43.58  ? 229  LYS B CA  1 
ATOM   6647  C  C   . LYS B 1 220 ? -27.427 45.819  43.568  1.00 45.33  ? 229  LYS B C   1 
ATOM   6648  O  O   . LYS B 1 220 ? -27.101 44.668  43.267  1.00 45.39  ? 229  LYS B O   1 
ATOM   6649  C  CB  . LYS B 1 220 ? -29.801 46.625  43.431  1.00 45.79  ? 229  LYS B CB  1 
ATOM   6650  C  CG  . LYS B 1 220 ? -31.155 46.651  44.087  1.00 51.58  ? 229  LYS B CG  1 
ATOM   6651  C  CD  . LYS B 1 220 ? -32.238 47.026  43.058  1.00 56.89  ? 229  LYS B CD  1 
ATOM   6652  C  CE  . LYS B 1 220 ? -33.611 46.571  43.513  1.00 63.64  ? 229  LYS B CE  1 
ATOM   6653  N  NZ  . LYS B 1 220 ? -34.674 47.109  42.619  1.00 68.80  ? 229  LYS B NZ  1 
ATOM   6654  N  N   . ALA B 1 221 ? -26.679 46.904  43.248  1.00 43.62  ? 230  ALA B N   1 
ATOM   6655  C  CA  . ALA B 1 221 ? -25.369 46.815  42.558  1.00 37.87  ? 230  ALA B CA  1 
ATOM   6656  C  C   . ALA B 1 221 ? -24.422 45.985  43.422  1.00 29.38  ? 230  ALA B C   1 
ATOM   6657  O  O   . ALA B 1 221 ? -23.755 45.083  42.928  1.00 30.62  ? 230  ALA B O   1 
ATOM   6658  C  CB  . ALA B 1 221 ? -24.807 48.232  42.370  1.00 35.05  ? 230  ALA B CB  1 
ATOM   6659  N  N   . VAL B 1 222 ? -24.377 46.261  44.729  1.00 33.24  ? 231  VAL B N   1 
ATOM   6660  C  CA  . VAL B 1 222 ? -23.493 45.479  45.614  1.00 33.78  ? 231  VAL B CA  1 
ATOM   6661  C  C   . VAL B 1 222 ? -23.799 43.992  45.542  1.00 35.50  ? 231  VAL B C   1 
ATOM   6662  O  O   . VAL B 1 222 ? -22.857 43.192  45.476  1.00 35.67  ? 231  VAL B O   1 
ATOM   6663  C  CB  . VAL B 1 222 ? -23.566 45.980  47.097  1.00 38.04  ? 231  VAL B CB  1 
ATOM   6664  C  CG1 . VAL B 1 222 ? -22.872 44.980  48.025  1.00 38.10  ? 231  VAL B CG1 1 
ATOM   6665  C  CG2 . VAL B 1 222 ? -22.882 47.335  47.252  1.00 38.13  ? 231  VAL B CG2 1 
ATOM   6666  N  N   . SER B 1 223 ? -25.113 43.570  45.544  1.00 39.39  ? 232  SER B N   1 
ATOM   6667  C  CA  . SER B 1 223 ? -25.387 42.108  45.496  1.00 41.92  ? 232  SER B CA  1 
ATOM   6668  C  C   . SER B 1 223 ? -24.925 41.515  44.219  1.00 42.14  ? 232  SER B C   1 
ATOM   6669  O  O   . SER B 1 223 ? -24.405 40.392  44.231  1.00 40.33  ? 232  SER B O   1 
ATOM   6670  C  CB  . SER B 1 223 ? -26.879 41.770  45.640  1.00 45.16  ? 232  SER B CB  1 
ATOM   6671  O  OG  . SER B 1 223 ? -27.637 42.855  46.137  1.00 50.86  ? 232  SER B OG  1 
ATOM   6672  N  N   . GLN B 1 224 ? -25.105 42.241  43.095  1.00 40.41  ? 233  GLN B N   1 
ATOM   6673  C  CA  . GLN B 1 224 ? -24.643 41.707  41.818  1.00 38.88  ? 233  GLN B CA  1 
ATOM   6674  C  C   . GLN B 1 224 ? -23.137 41.517  41.869  1.00 39.40  ? 233  GLN B C   1 
ATOM   6675  O  O   . GLN B 1 224 ? -22.608 40.516  41.359  1.00 37.59  ? 233  GLN B O   1 
ATOM   6676  C  CB  . GLN B 1 224 ? -24.988 42.665  40.691  1.00 44.15  ? 233  GLN B CB  1 
ATOM   6677  C  CG  . GLN B 1 224 ? -26.481 42.864  40.457  1.00 50.41  ? 233  GLN B CG  1 
ATOM   6678  C  CD  . GLN B 1 224 ? -26.694 43.089  38.981  1.00 57.57  ? 233  GLN B CD  1 
ATOM   6679  O  OE1 . GLN B 1 224 ? -25.747 43.202  38.192  1.00 55.39  ? 233  GLN B OE1 1 
ATOM   6680  N  NE2 . GLN B 1 224 ? -27.952 43.150  38.538  1.00 59.78  ? 233  GLN B NE2 1 
ATOM   6681  N  N   . ILE B 1 225 ? -22.419 42.473  42.500  1.00 34.82  ? 234  ILE B N   1 
ATOM   6682  C  CA  . ILE B 1 225 ? -20.980 42.309  42.551  1.00 31.86  ? 234  ILE B CA  1 
ATOM   6683  C  C   . ILE B 1 225 ? -20.674 41.068  43.347  1.00 34.32  ? 234  ILE B C   1 
ATOM   6684  O  O   . ILE B 1 225 ? -19.839 40.252  42.955  1.00 33.35  ? 234  ILE B O   1 
ATOM   6685  C  CB  . ILE B 1 225 ? -20.334 43.566  43.205  1.00 33.67  ? 234  ILE B CB  1 
ATOM   6686  C  CG1 . ILE B 1 225 ? -20.407 44.764  42.213  1.00 29.64  ? 234  ILE B CG1 1 
ATOM   6687  C  CG2 . ILE B 1 225 ? -18.855 43.269  43.624  1.00 28.92  ? 234  ILE B CG2 1 
ATOM   6688  C  CD1 . ILE B 1 225 ? -20.302 46.137  42.923  1.00 27.90  ? 234  ILE B CD1 1 
ATOM   6689  N  N   . LYS B 1 226 ? -21.355 40.921  44.505  1.00 36.71  ? 235  LYS B N   1 
ATOM   6690  C  CA  . LYS B 1 226 ? -21.088 39.766  45.380  1.00 39.48  ? 235  LYS B CA  1 
ATOM   6691  C  C   . LYS B 1 226 ? -21.544 38.422  44.780  1.00 40.32  ? 235  LYS B C   1 
ATOM   6692  O  O   . LYS B 1 226 ? -21.019 37.399  45.199  1.00 40.96  ? 235  LYS B O   1 
ATOM   6693  C  CB  . LYS B 1 226 ? -21.696 39.997  46.770  1.00 41.53  ? 235  LYS B CB  1 
ATOM   6694  C  CG  . LYS B 1 226 ? -20.891 41.052  47.548  1.00 42.47  ? 235  LYS B CG  1 
ATOM   6695  C  CD  . LYS B 1 226 ? -21.471 41.395  48.942  1.00 43.80  ? 235  LYS B CD  1 
ATOM   6696  C  CE  . LYS B 1 226 ? -20.975 40.484  50.070  1.00 44.82  ? 235  LYS B CE  1 
ATOM   6697  N  NZ  . LYS B 1 226 ? -19.727 39.721  49.756  1.00 51.87  ? 235  LYS B NZ  1 
ATOM   6698  N  N   . SER B 1 227 ? -22.480 38.411  43.813  1.00 40.79  ? 236  SER B N   1 
ATOM   6699  C  CA  . SER B 1 227 ? -22.829 37.160  43.149  1.00 45.87  ? 236  SER B CA  1 
ATOM   6700  C  C   . SER B 1 227 ? -21.735 36.800  42.165  1.00 47.26  ? 236  SER B C   1 
ATOM   6701  O  O   . SER B 1 227 ? -21.429 35.627  41.981  1.00 45.43  ? 236  SER B O   1 
ATOM   6702  C  CB  . SER B 1 227 ? -24.126 37.282  42.356  1.00 49.48  ? 236  SER B CB  1 
ATOM   6703  O  OG  . SER B 1 227 ? -25.236 37.338  43.230  1.00 55.94  ? 236  SER B OG  1 
ATOM   6704  N  N   . ALA B 1 228 ? -21.140 37.819  41.510  1.00 44.00  ? 237  ALA B N   1 
ATOM   6705  C  CA  . ALA B 1 228 ? -20.085 37.577  40.533  1.00 40.92  ? 237  ALA B CA  1 
ATOM   6706  C  C   . ALA B 1 228 ? -18.783 37.096  41.202  1.00 38.08  ? 237  ALA B C   1 
ATOM   6707  O  O   . ALA B 1 228 ? -18.104 36.194  40.692  1.00 35.49  ? 237  ALA B O   1 
ATOM   6708  C  CB  . ALA B 1 228 ? -19.810 38.863  39.735  1.00 39.97  ? 237  ALA B CB  1 
ATOM   6709  N  N   . VAL B 1 229 ? -18.420 37.687  42.322  1.00 35.26  ? 238  VAL B N   1 
ATOM   6710  C  CA  . VAL B 1 229 ? -17.164 37.304  42.919  1.00 36.89  ? 238  VAL B CA  1 
ATOM   6711  C  C   . VAL B 1 229 ? -17.259 37.236  44.415  1.00 37.19  ? 238  VAL B C   1 
ATOM   6712  O  O   . VAL B 1 229 ? -18.036 37.976  45.026  1.00 36.83  ? 238  VAL B O   1 
ATOM   6713  C  CB  . VAL B 1 229 ? -16.039 38.322  42.440  1.00 38.92  ? 238  VAL B CB  1 
ATOM   6714  C  CG1 . VAL B 1 229 ? -15.777 38.152  40.920  1.00 36.21  ? 238  VAL B CG1 1 
ATOM   6715  C  CG2 . VAL B 1 229 ? -16.454 39.760  42.708  1.00 37.64  ? 238  VAL B CG2 1 
ATOM   6716  N  N   . ASN B 1 230 ? -16.470 36.343  45.028  1.00 39.68  ? 239  ASN B N   1 
ATOM   6717  C  CA  . ASN B 1 230 ? -16.539 36.261  46.480  1.00 42.62  ? 239  ASN B CA  1 
ATOM   6718  C  C   . ASN B 1 230 ? -15.599 37.239  47.109  1.00 43.04  ? 239  ASN B C   1 
ATOM   6719  O  O   . ASN B 1 230 ? -14.401 36.970  47.217  1.00 41.64  ? 239  ASN B O   1 
ATOM   6720  C  CB  . ASN B 1 230 ? -16.220 34.866  46.982  1.00 48.72  ? 239  ASN B CB  1 
ATOM   6721  C  CG  . ASN B 1 230 ? -16.868 34.713  48.337  1.00 54.82  ? 239  ASN B CG  1 
ATOM   6722  O  OD1 . ASN B 1 230 ? -16.189 34.863  49.357  1.00 59.06  ? 239  ASN B OD1 1 
ATOM   6723  N  ND2 . ASN B 1 230 ? -18.201 34.520  48.430  1.00 55.04  ? 239  ASN B ND2 1 
ATOM   6724  N  N   . VAL B 1 231 ? -16.124 38.367  47.544  1.00 38.62  ? 240  VAL B N   1 
ATOM   6725  C  CA  . VAL B 1 231 ? -15.254 39.387  48.083  1.00 37.43  ? 240  VAL B CA  1 
ATOM   6726  C  C   . VAL B 1 231 ? -15.828 40.115  49.276  1.00 35.87  ? 240  VAL B C   1 
ATOM   6727  O  O   . VAL B 1 231 ? -17.027 40.078  49.533  1.00 35.51  ? 240  VAL B O   1 
ATOM   6728  C  CB  . VAL B 1 231 ? -15.044 40.471  46.951  1.00 36.62  ? 240  VAL B CB  1 
ATOM   6729  C  CG1 . VAL B 1 231 ? -14.304 39.894  45.761  1.00 34.55  ? 240  VAL B CG1 1 
ATOM   6730  C  CG2 . VAL B 1 231 ? -16.394 41.030  46.511  1.00 35.01  ? 240  VAL B CG2 1 
ATOM   6731  N  N   . ASN B 1 232 ? -14.958 40.826  49.965  1.00 35.79  ? 241  ASN B N   1 
ATOM   6732  C  CA  . ASN B 1 232 ? -15.407 41.738  51.001  1.00 37.86  ? 241  ASN B CA  1 
ATOM   6733  C  C   . ASN B 1 232 ? -15.633 43.078  50.295  1.00 38.15  ? 241  ASN B C   1 
ATOM   6734  O  O   . ASN B 1 232 ? -14.716 43.556  49.605  1.00 36.95  ? 241  ASN B O   1 
ATOM   6735  C  CB  . ASN B 1 232 ? -14.346 41.911  52.072  1.00 42.89  ? 241  ASN B CB  1 
ATOM   6736  C  CG  . ASN B 1 232 ? -14.080 40.595  52.784  1.00 56.34  ? 241  ASN B CG  1 
ATOM   6737  O  OD1 . ASN B 1 232 ? -12.911 40.239  52.985  1.00 61.30  ? 241  ASN B OD1 1 
ATOM   6738  N  ND2 . ASN B 1 232 ? -15.111 39.809  53.164  1.00 54.65  ? 241  ASN B ND2 1 
ATOM   6739  N  N   . VAL B 1 233 ? -16.803 43.672  50.448  1.00 35.27  ? 242  VAL B N   1 
ATOM   6740  C  CA  . VAL B 1 233 ? -17.126 44.941  49.852  1.00 34.92  ? 242  VAL B CA  1 
ATOM   6741  C  C   . VAL B 1 233 ? -17.004 46.033  50.863  1.00 38.25  ? 242  VAL B C   1 
ATOM   6742  O  O   . VAL B 1 233 ? -17.613 45.926  51.927  1.00 38.47  ? 242  VAL B O   1 
ATOM   6743  C  CB  . VAL B 1 233 ? -18.547 44.916  49.266  1.00 33.50  ? 242  VAL B CB  1 
ATOM   6744  C  CG1 . VAL B 1 233 ? -18.923 46.299  48.684  1.00 30.51  ? 242  VAL B CG1 1 
ATOM   6745  C  CG2 . VAL B 1 233 ? -18.628 43.836  48.202  1.00 33.23  ? 242  VAL B CG2 1 
ATOM   6746  N  N   . THR B 1 234 ? -16.212 47.077  50.566  1.00 33.37  ? 243  THR B N   1 
ATOM   6747  C  CA  . THR B 1 234 ? -16.061 48.249  51.412  1.00 31.79  ? 243  THR B CA  1 
ATOM   6748  C  C   . THR B 1 234 ? -16.638 49.462  50.668  1.00 32.90  ? 243  THR B C   1 
ATOM   6749  O  O   . THR B 1 234 ? -16.505 49.513  49.447  1.00 31.21  ? 243  THR B O   1 
ATOM   6750  C  CB  . THR B 1 234 ? -14.576 48.545  51.664  1.00 37.13  ? 243  THR B CB  1 
ATOM   6751  O  OG1 . THR B 1 234 ? -14.079 47.486  52.490  1.00 44.33  ? 243  THR B OG1 1 
ATOM   6752  C  CG2 . THR B 1 234 ? -14.359 49.904  52.371  1.00 39.70  ? 243  THR B CG2 1 
ATOM   6753  N  N   . ARG B 1 235 ? -17.258 50.421  51.354  1.00 31.66  ? 244  ARG B N   1 
ATOM   6754  C  CA  . ARG B 1 235 ? -17.766 51.607  50.702  1.00 30.07  ? 244  ARG B CA  1 
ATOM   6755  C  C   . ARG B 1 235 ? -17.114 52.830  51.304  1.00 31.25  ? 244  ARG B C   1 
ATOM   6756  O  O   . ARG B 1 235 ? -16.991 52.919  52.522  1.00 29.92  ? 244  ARG B O   1 
ATOM   6757  C  CB  . ARG B 1 235 ? -19.295 51.708  50.892  1.00 31.60  ? 244  ARG B CB  1 
ATOM   6758  C  CG  . ARG B 1 235 ? -19.895 53.018  50.404  1.00 33.66  ? 244  ARG B CG  1 
ATOM   6759  C  CD  . ARG B 1 235 ? -21.426 53.092  50.642  1.00 36.96  ? 244  ARG B CD  1 
ATOM   6760  N  NE  . ARG B 1 235 ? -22.170 51.954  50.088  1.00 36.28  ? 244  ARG B NE  1 
ATOM   6761  C  CZ  . ARG B 1 235 ? -22.698 51.935  48.865  1.00 40.02  ? 244  ARG B CZ  1 
ATOM   6762  N  NH1 . ARG B 1 235 ? -22.518 52.960  48.041  1.00 35.67  ? 244  ARG B NH1 1 
ATOM   6763  N  NH2 . ARG B 1 235 ? -23.442 50.907  48.467  1.00 42.59  ? 244  ARG B NH2 1 
ATOM   6764  N  N   . ILE B 1 236 ? -16.675 53.782  50.459  1.00 28.58  ? 245  ILE B N   1 
ATOM   6765  C  CA  . ILE B 1 236 ? -16.110 55.062  50.883  1.00 28.20  ? 245  ILE B CA  1 
ATOM   6766  C  C   . ILE B 1 236 ? -17.009 56.089  50.226  1.00 30.54  ? 245  ILE B C   1 
ATOM   6767  O  O   . ILE B 1 236 ? -16.979 56.253  48.993  1.00 30.62  ? 245  ILE B O   1 
ATOM   6768  C  CB  . ILE B 1 236 ? -14.643 55.258  50.464  1.00 28.51  ? 245  ILE B CB  1 
ATOM   6769  C  CG1 . ILE B 1 236 ? -13.776 54.152  51.060  1.00 27.78  ? 245  ILE B CG1 1 
ATOM   6770  C  CG2 . ILE B 1 236 ? -14.165 56.678  50.926  1.00 26.76  ? 245  ILE B CG2 1 
ATOM   6771  C  CD1 . ILE B 1 236 ? -12.330 54.254  50.636  1.00 33.88  ? 245  ILE B CD1 1 
ATOM   6772  N  N   . GLY B 1 237 ? -17.832 56.765  50.997  1.00 32.44  ? 246  GLY B N   1 
ATOM   6773  C  CA  . GLY B 1 237 ? -18.785 57.706  50.399  1.00 29.62  ? 246  GLY B CA  1 
ATOM   6774  C  C   . GLY B 1 237 ? -19.302 58.646  51.454  1.00 34.45  ? 246  GLY B C   1 
ATOM   6775  O  O   . GLY B 1 237 ? -19.820 58.202  52.483  1.00 32.73  ? 246  GLY B O   1 
ATOM   6776  N  N   . GLY B 1 238 ? -19.149 59.931  51.223  1.00 29.67  ? 247  GLY B N   1 
ATOM   6777  C  CA  . GLY B 1 238 ? -19.610 60.912  52.182  1.00 29.42  ? 247  GLY B CA  1 
ATOM   6778  C  C   . GLY B 1 238 ? -20.943 61.461  51.742  1.00 28.86  ? 247  GLY B C   1 
ATOM   6779  O  O   . GLY B 1 238 ? -21.553 60.963  50.788  1.00 29.02  ? 247  GLY B O   1 
ATOM   6780  N  N   . VAL B 1 239 ? -21.399 62.499  52.426  1.00 31.23  ? 248  VAL B N   1 
ATOM   6781  C  CA  . VAL B 1 239 ? -22.711 63.043  52.129  1.00 30.23  ? 248  VAL B CA  1 
ATOM   6782  C  C   . VAL B 1 239 ? -22.653 63.923  50.885  1.00 31.11  ? 248  VAL B C   1 
ATOM   6783  O  O   . VAL B 1 239 ? -23.680 64.224  50.270  1.00 28.93  ? 248  VAL B O   1 
ATOM   6784  C  CB  . VAL B 1 239 ? -23.220 63.779  53.409  1.00 30.32  ? 248  VAL B CB  1 
ATOM   6785  C  CG1 . VAL B 1 239 ? -22.584 65.155  53.544  1.00 28.48  ? 248  VAL B CG1 1 
ATOM   6786  C  CG2 . VAL B 1 239 ? -24.741 63.903  53.358  1.00 28.96  ? 248  VAL B CG2 1 
ATOM   6787  N  N   . ASP B 1 240 ? -21.425 64.345  50.496  1.00 30.23  ? 249  ASP B N   1 
ATOM   6788  C  CA  . ASP B 1 240 ? -21.263 65.129  49.267  1.00 29.83  ? 249  ASP B CA  1 
ATOM   6789  C  C   . ASP B 1 240 ? -19.866 64.808  48.712  1.00 27.58  ? 249  ASP B C   1 
ATOM   6790  O  O   . ASP B 1 240 ? -19.088 64.155  49.398  1.00 23.94  ? 249  ASP B O   1 
ATOM   6791  C  CB  . ASP B 1 240 ? -21.451 66.632  49.527  1.00 29.48  ? 249  ASP B CB  1 
ATOM   6792  C  CG  . ASP B 1 240 ? -20.484 67.241  50.542  1.00 33.41  ? 249  ASP B CG  1 
ATOM   6793  O  OD1 . ASP B 1 240 ? -19.435 66.663  50.774  1.00 34.60  ? 249  ASP B OD1 1 
ATOM   6794  O  OD2 . ASP B 1 240 ? -20.809 68.300  51.106  1.00 40.37  ? 249  ASP B OD2 1 
ATOM   6795  N  N   . ARG B 1 241 ? -19.530 65.246  47.496  1.00 27.81  ? 250  ARG B N   1 
ATOM   6796  C  CA  . ARG B 1 241 ? -18.202 64.892  46.937  1.00 26.22  ? 250  ARG B CA  1 
ATOM   6797  C  C   . ARG B 1 241 ? -17.059 65.448  47.777  1.00 18.95  ? 250  ARG B C   1 
ATOM   6798  O  O   . ARG B 1 241 ? -15.985 64.855  47.834  1.00 21.16  ? 250  ARG B O   1 
ATOM   6799  C  CB  . ARG B 1 241 ? -18.110 65.450  45.488  1.00 23.91  ? 250  ARG B CB  1 
ATOM   6800  C  CG  . ARG B 1 241 ? -18.195 67.007  45.453  1.00 25.97  ? 250  ARG B CG  1 
ATOM   6801  C  CD  . ARG B 1 241 ? -18.380 67.560  43.986  1.00 33.61  ? 250  ARG B CD  1 
ATOM   6802  N  NE  . ARG B 1 241 ? -19.488 66.901  43.262  1.00 36.59  ? 250  ARG B NE  1 
ATOM   6803  C  CZ  . ARG B 1 241 ? -19.675 66.977  41.940  1.00 40.40  ? 250  ARG B CZ  1 
ATOM   6804  N  NH1 . ARG B 1 241 ? -18.829 67.666  41.177  1.00 30.73  ? 250  ARG B NH1 1 
ATOM   6805  N  NH2 . ARG B 1 241 ? -20.716 66.371  41.372  1.00 34.87  ? 250  ARG B NH2 1 
ATOM   6806  N  N   . HIS B 1 242 ? -17.251 66.585  48.430  1.00 22.11  ? 251  HIS B N   1 
ATOM   6807  C  CA  . HIS B 1 242 ? -16.182 67.157  49.261  1.00 25.19  ? 251  HIS B CA  1 
ATOM   6808  C  C   . HIS B 1 242 ? -15.849 66.204  50.429  1.00 28.39  ? 251  HIS B C   1 
ATOM   6809  O  O   . HIS B 1 242 ? -14.660 65.911  50.702  1.00 26.90  ? 251  HIS B O   1 
ATOM   6810  C  CB  . HIS B 1 242 ? -16.657 68.518  49.806  1.00 30.08  ? 251  HIS B CB  1 
ATOM   6811  C  CG  . HIS B 1 242 ? -16.960 69.495  48.719  1.00 33.56  ? 251  HIS B CG  1 
ATOM   6812  N  ND1 . HIS B 1 242 ? -18.194 69.555  48.101  1.00 32.17  ? 251  HIS B ND1 1 
ATOM   6813  C  CD2 . HIS B 1 242 ? -16.197 70.467  48.153  1.00 29.95  ? 251  HIS B CD2 1 
ATOM   6814  C  CE1 . HIS B 1 242 ? -18.162 70.538  47.211  1.00 35.35  ? 251  HIS B CE1 1 
ATOM   6815  N  NE2 . HIS B 1 242 ? -16.978 71.109  47.221  1.00 30.68  ? 251  HIS B NE2 1 
ATOM   6816  N  N   . GLU B 1 243 ? -16.890 65.694  51.102  1.00 27.06  ? 252  GLU B N   1 
ATOM   6817  C  CA  . GLU B 1 243 ? -16.630 64.773  52.227  1.00 25.03  ? 252  GLU B CA  1 
ATOM   6818  C  C   . GLU B 1 243 ? -16.079 63.472  51.671  1.00 25.74  ? 252  GLU B C   1 
ATOM   6819  O  O   . GLU B 1 243 ? -15.207 62.856  52.290  1.00 26.22  ? 252  GLU B O   1 
ATOM   6820  C  CB  . GLU B 1 243 ? -17.946 64.475  53.057  1.00 26.98  ? 252  GLU B CB  1 
ATOM   6821  C  CG  . GLU B 1 243 ? -17.611 63.440  54.124  1.00 32.47  ? 252  GLU B CG  1 
ATOM   6822  C  CD  . GLU B 1 243 ? -18.791 63.093  55.061  1.00 43.84  ? 252  GLU B CD  1 
ATOM   6823  O  OE1 . GLU B 1 243 ? -19.959 63.351  54.715  1.00 40.71  ? 252  GLU B OE1 1 
ATOM   6824  O  OE2 . GLU B 1 243 ? -18.507 62.549  56.159  1.00 48.06  ? 252  GLU B OE2 1 
ATOM   6825  N  N   . THR B 1 244 ? -16.580 63.016  50.476  1.00 25.64  ? 253  THR B N   1 
ATOM   6826  C  CA  . THR B 1 244 ? -16.023 61.783  49.921  1.00 21.14  ? 253  THR B CA  1 
ATOM   6827  C  C   . THR B 1 244 ? -14.534 61.977  49.665  1.00 21.53  ? 253  THR B C   1 
ATOM   6828  O  O   . THR B 1 244 ? -13.781 61.034  49.909  1.00 23.65  ? 253  THR B O   1 
ATOM   6829  C  CB  . THR B 1 244 ? -16.735 61.385  48.604  1.00 26.64  ? 253  THR B CB  1 
ATOM   6830  O  OG1 . THR B 1 244 ? -18.087 61.061  48.936  1.00 26.41  ? 253  THR B OG1 1 
ATOM   6831  C  CG2 . THR B 1 244 ? -16.079 60.206  47.917  1.00 23.03  ? 253  THR B CG2 1 
ATOM   6832  N  N   . SER B 1 245 ? -14.074 63.184  49.196  1.00 24.74  ? 254  SER B N   1 
ATOM   6833  C  CA  . SER B 1 245 ? -12.605 63.316  48.976  1.00 21.71  ? 254  SER B CA  1 
ATOM   6834  C  C   . SER B 1 245 ? -11.872 63.258  50.301  1.00 20.61  ? 254  SER B C   1 
ATOM   6835  O  O   . SER B 1 245 ? -10.764 62.738  50.331  1.00 23.48  ? 254  SER B O   1 
ATOM   6836  C  CB  . SER B 1 245 ? -12.202 64.614  48.239  1.00 22.13  ? 254  SER B CB  1 
ATOM   6837  O  OG  . SER B 1 245 ? -12.562 65.819  48.876  1.00 26.69  ? 254  SER B OG  1 
ATOM   6838  N  N   . LEU B 1 246 ? -12.453 63.789  51.376  1.00 24.44  ? 255  LEU B N   1 
ATOM   6839  C  CA  . LEU B 1 246 ? -11.788 63.687  52.713  1.00 23.22  ? 255  LEU B CA  1 
ATOM   6840  C  C   . LEU B 1 246 ? -11.702 62.236  53.153  1.00 22.21  ? 255  LEU B C   1 
ATOM   6841  O  O   . LEU B 1 246 ? -10.657 61.743  53.586  1.00 23.09  ? 255  LEU B O   1 
ATOM   6842  C  CB  . LEU B 1 246 ? -12.620 64.504  53.714  1.00 26.63  ? 255  LEU B CB  1 
ATOM   6843  C  CG  . LEU B 1 246 ? -12.173 64.341  55.226  1.00 29.93  ? 255  LEU B CG  1 
ATOM   6844  C  CD1 . LEU B 1 246 ? -10.720 64.760  55.402  1.00 28.63  ? 255  LEU B CD1 1 
ATOM   6845  C  CD2 . LEU B 1 246 ? -13.128 65.229  56.088  1.00 27.86  ? 255  LEU B CD2 1 
ATOM   6846  N  N   . LEU B 1 247 ? -12.811 61.496  53.008  1.00 24.85  ? 256  LEU B N   1 
ATOM   6847  C  CA  . LEU B 1 247 ? -12.781 60.083  53.404  1.00 24.91  ? 256  LEU B CA  1 
ATOM   6848  C  C   . LEU B 1 247 ? -11.761 59.310  52.600  1.00 26.95  ? 256  LEU B C   1 
ATOM   6849  O  O   . LEU B 1 247 ? -11.111 58.391  53.107  1.00 24.36  ? 256  LEU B O   1 
ATOM   6850  C  CB  . LEU B 1 247 ? -14.175 59.481  53.241  1.00 24.78  ? 256  LEU B CB  1 
ATOM   6851  C  CG  . LEU B 1 247 ? -15.175 60.100  54.212  1.00 24.94  ? 256  LEU B CG  1 
ATOM   6852  C  CD1 . LEU B 1 247 ? -16.563 59.683  53.818  1.00 30.26  ? 256  LEU B CD1 1 
ATOM   6853  C  CD2 . LEU B 1 247 ? -14.847 59.629  55.634  1.00 28.03  ? 256  LEU B CD2 1 
ATOM   6854  N  N   . ILE B 1 248 ? -11.564 59.691  51.290  1.00 24.36  ? 257  ILE B N   1 
ATOM   6855  C  CA  . ILE B 1 248 ? -10.577 58.976  50.537  1.00 18.53  ? 257  ILE B CA  1 
ATOM   6856  C  C   . ILE B 1 248 ? -9.192  59.304  51.054  1.00 16.74  ? 257  ILE B C   1 
ATOM   6857  O  O   . ILE B 1 248 ? -8.326  58.419  51.133  1.00 22.39  ? 257  ILE B O   1 
ATOM   6858  C  CB  . ILE B 1 248 ? -10.733 59.356  48.986  1.00 19.81  ? 257  ILE B CB  1 
ATOM   6859  C  CG1 . ILE B 1 248 ? -11.954 58.580  48.426  1.00 22.48  ? 257  ILE B CG1 1 
ATOM   6860  C  CG2 . ILE B 1 248 ? -9.469  58.981  48.184  1.00 22.31  ? 257  ILE B CG2 1 
ATOM   6861  C  CD1 . ILE B 1 248 ? -12.362 58.965  46.913  1.00 22.05  ? 257  ILE B CD1 1 
ATOM   6862  N  N   . ALA B 1 249 ? -8.975  60.552  51.373  1.00 20.38  ? 258  ALA B N   1 
ATOM   6863  C  CA  . ALA B 1 249 ? -7.666  60.978  51.854  1.00 21.58  ? 258  ALA B CA  1 
ATOM   6864  C  C   . ALA B 1 249 ? -7.327  60.256  53.217  1.00 23.45  ? 258  ALA B C   1 
ATOM   6865  O  O   . ALA B 1 249 ? -6.186  59.838  53.438  1.00 22.45  ? 258  ALA B O   1 
ATOM   6866  C  CB  . ALA B 1 249 ? -7.682  62.504  52.009  1.00 19.53  ? 258  ALA B CB  1 
ATOM   6867  N  N   . LYS B 1 250 ? -8.342  60.100  54.068  1.00 26.13  ? 259  LYS B N   1 
ATOM   6868  C  CA  . LYS B 1 250 ? -8.172  59.388  55.350  1.00 27.91  ? 259  LYS B CA  1 
ATOM   6869  C  C   . LYS B 1 250 ? -7.837  57.924  55.077  1.00 31.93  ? 259  LYS B C   1 
ATOM   6870  O  O   . LYS B 1 250 ? -7.009  57.302  55.771  1.00 32.70  ? 259  LYS B O   1 
ATOM   6871  C  CB  . LYS B 1 250 ? -9.472  59.498  56.145  1.00 28.02  ? 259  LYS B CB  1 
ATOM   6872  C  CG  . LYS B 1 250 ? -9.655  60.869  56.741  1.00 31.17  ? 259  LYS B CG  1 
ATOM   6873  C  CD  . LYS B 1 250 ? -10.985 60.940  57.522  1.00 33.78  ? 259  LYS B CD  1 
ATOM   6874  C  CE  . LYS B 1 250 ? -11.139 62.317  58.123  1.00 54.02  ? 259  LYS B CE  1 
ATOM   6875  N  NZ  . LYS B 1 250 ? -11.287 62.307  59.629  1.00 63.35  ? 259  LYS B NZ  1 
ATOM   6876  N  N   . GLU B 1 251 ? -8.453  57.358  54.026  1.00 29.95  ? 260  GLU B N   1 
ATOM   6877  C  CA  . GLU B 1 251 ? -8.159  55.969  53.692  1.00 27.54  ? 260  GLU B CA  1 
ATOM   6878  C  C   . GLU B 1 251 ? -6.713  55.852  53.206  1.00 30.84  ? 260  GLU B C   1 
ATOM   6879  O  O   . GLU B 1 251 ? -5.971  54.949  53.619  1.00 29.47  ? 260  GLU B O   1 
ATOM   6880  C  CB  . GLU B 1 251 ? -9.136  55.491  52.644  1.00 29.71  ? 260  GLU B CB  1 
ATOM   6881  C  CG  . GLU B 1 251 ? -8.892  54.068  52.191  1.00 35.44  ? 260  GLU B CG  1 
ATOM   6882  C  CD  . GLU B 1 251 ? -9.389  52.997  53.207  1.00 51.45  ? 260  GLU B CD  1 
ATOM   6883  O  OE1 . GLU B 1 251 ? -10.033 53.364  54.209  1.00 51.08  ? 260  GLU B OE1 1 
ATOM   6884  O  OE2 . GLU B 1 251 ? -9.120  51.781  52.971  1.00 53.74  ? 260  GLU B OE2 1 
ATOM   6885  N  N   . ILE B 1 252 ? -6.281  56.776  52.333  1.00 26.15  ? 261  ILE B N   1 
ATOM   6886  C  CA  . ILE B 1 252 ? -4.892  56.696  51.869  1.00 27.77  ? 261  ILE B CA  1 
ATOM   6887  C  C   . ILE B 1 252 ? -3.915  56.789  53.091  1.00 26.37  ? 261  ILE B C   1 
ATOM   6888  O  O   . ILE B 1 252 ? -2.912  56.073  53.111  1.00 28.21  ? 261  ILE B O   1 
ATOM   6889  C  CB  . ILE B 1 252 ? -4.623  57.869  50.879  1.00 27.79  ? 261  ILE B CB  1 
ATOM   6890  C  CG1 . ILE B 1 252 ? -5.453  57.587  49.579  1.00 27.11  ? 261  ILE B CG1 1 
ATOM   6891  C  CG2 . ILE B 1 252 ? -3.098  57.968  50.571  1.00 27.82  ? 261  ILE B CG2 1 
ATOM   6892  C  CD1 . ILE B 1 252 ? -5.321  58.750  48.541  1.00 28.46  ? 261  ILE B CD1 1 
ATOM   6893  N  N   . ASP B 1 253 ? -4.225  57.639  54.036  1.00 28.67  ? 262  ASP B N   1 
ATOM   6894  C  CA  . ASP B 1 253 ? -3.357  57.849  55.209  1.00 31.98  ? 262  ASP B CA  1 
ATOM   6895  C  C   . ASP B 1 253 ? -3.217  56.568  56.048  1.00 35.81  ? 262  ASP B C   1 
ATOM   6896  O  O   . ASP B 1 253 ? -2.247  56.447  56.777  1.00 37.92  ? 262  ASP B O   1 
ATOM   6897  C  CB  . ASP B 1 253 ? -3.879  58.980  56.036  1.00 31.94  ? 262  ASP B CB  1 
ATOM   6898  C  CG  . ASP B 1 253 ? -2.859  59.489  57.070  1.00 42.01  ? 262  ASP B CG  1 
ATOM   6899  O  OD1 . ASP B 1 253 ? -1.759  59.944  56.662  1.00 39.50  ? 262  ASP B OD1 1 
ATOM   6900  O  OD2 . ASP B 1 253 ? -3.173  59.437  58.281  1.00 40.42  ? 262  ASP B OD2 1 
ATOM   6901  N  N   . LYS B 1 254 ? -4.129  55.624  55.933  1.00 36.45  ? 263  LYS B N   1 
ATOM   6902  C  CA  . LYS B 1 254 ? -3.994  54.368  56.658  1.00 40.16  ? 263  LYS B CA  1 
ATOM   6903  C  C   . LYS B 1 254 ? -2.850  53.551  56.080  1.00 42.61  ? 263  LYS B C   1 
ATOM   6904  O  O   . LYS B 1 254 ? -2.295  52.707  56.778  1.00 42.08  ? 263  LYS B O   1 
ATOM   6905  C  CB  . LYS B 1 254 ? -5.273  53.529  56.559  1.00 39.16  ? 263  LYS B CB  1 
ATOM   6906  C  CG  . LYS B 1 254 ? -6.487  54.187  57.199  1.00 43.22  ? 263  LYS B CG  1 
ATOM   6907  C  CD  . LYS B 1 254 ? -7.554  53.168  57.384  1.00 53.49  ? 263  LYS B CD  1 
ATOM   6908  C  CE  . LYS B 1 254 ? -8.923  53.680  57.023  1.00 67.42  ? 263  LYS B CE  1 
ATOM   6909  N  NZ  . LYS B 1 254 ? -9.560  54.494  58.101  1.00 73.32  ? 263  LYS B NZ  1 
ATOM   6910  N  N   . TYR B 1 255 ? -2.486  53.780  54.793  1.00 39.90  ? 264  TYR B N   1 
ATOM   6911  C  CA  . TYR B 1 255 ? -1.427  53.000  54.146  1.00 35.94  ? 264  TYR B CA  1 
ATOM   6912  C  C   . TYR B 1 255 ? -0.112  53.689  54.164  1.00 37.97  ? 264  TYR B C   1 
ATOM   6913  O  O   . TYR B 1 255 ? 0.913   53.013  54.250  1.00 38.32  ? 264  TYR B O   1 
ATOM   6914  C  CB  . TYR B 1 255 ? -1.773  52.688  52.689  1.00 36.59  ? 264  TYR B CB  1 
ATOM   6915  C  CG  . TYR B 1 255 ? -2.978  51.795  52.605  1.00 38.56  ? 264  TYR B CG  1 
ATOM   6916  C  CD1 . TYR B 1 255 ? -4.256  52.300  52.794  1.00 36.51  ? 264  TYR B CD1 1 
ATOM   6917  C  CD2 . TYR B 1 255 ? -2.845  50.439  52.344  1.00 42.55  ? 264  TYR B CD2 1 
ATOM   6918  C  CE1 . TYR B 1 255 ? -5.368  51.479  52.743  1.00 39.41  ? 264  TYR B CE1 1 
ATOM   6919  C  CE2 . TYR B 1 255 ? -3.962  49.606  52.287  1.00 45.54  ? 264  TYR B CE2 1 
ATOM   6920  C  CZ  . TYR B 1 255 ? -5.217  50.129  52.500  1.00 46.63  ? 264  TYR B CZ  1 
ATOM   6921  O  OH  . TYR B 1 255 ? -6.317  49.303  52.543  1.00 51.88  ? 264  TYR B OH  1 
ATOM   6922  N  N   . HIS B 1 256 ? -0.093  55.009  54.053  1.00 35.11  ? 265  HIS B N   1 
ATOM   6923  C  CA  . HIS B 1 256 ? 1.164   55.706  54.113  1.00 34.92  ? 265  HIS B CA  1 
ATOM   6924  C  C   . HIS B 1 256 ? 0.847   57.140  54.463  1.00 33.18  ? 265  HIS B C   1 
ATOM   6925  O  O   . HIS B 1 256 ? -0.306  57.565  54.343  1.00 32.46  ? 265  HIS B O   1 
ATOM   6926  C  CB  . HIS B 1 256 ? 1.989   55.553  52.825  1.00 36.72  ? 265  HIS B CB  1 
ATOM   6927  C  CG  . HIS B 1 256 ? 1.289   56.020  51.590  1.00 37.14  ? 265  HIS B CG  1 
ATOM   6928  N  ND1 . HIS B 1 256 ? 0.705   55.145  50.696  1.00 41.07  ? 265  HIS B ND1 1 
ATOM   6929  C  CD2 . HIS B 1 256 ? 1.087   57.264  51.101  1.00 37.17  ? 265  HIS B CD2 1 
ATOM   6930  C  CE1 . HIS B 1 256 ? 0.161   55.857  49.715  1.00 36.36  ? 265  HIS B CE1 1 
ATOM   6931  N  NE2 . HIS B 1 256 ? 0.378   57.134  49.929  1.00 36.34  ? 265  HIS B NE2 1 
ATOM   6932  N  N   . ASP B 1 257 ? 1.812   57.894  54.908  1.00 30.56  ? 266  ASP B N   1 
ATOM   6933  C  CA  . ASP B 1 257 ? 1.555   59.263  55.303  1.00 33.85  ? 266  ASP B CA  1 
ATOM   6934  C  C   . ASP B 1 257 ? 1.116   60.204  54.177  1.00 35.93  ? 266  ASP B C   1 
ATOM   6935  O  O   . ASP B 1 257 ? 1.713   60.216  53.108  1.00 34.79  ? 266  ASP B O   1 
ATOM   6936  C  CB  . ASP B 1 257 ? 2.832   59.935  55.879  1.00 40.03  ? 266  ASP B CB  1 
ATOM   6937  C  CG  . ASP B 1 257 ? 3.233   59.491  57.288  1.00 51.53  ? 266  ASP B CG  1 
ATOM   6938  O  OD1 . ASP B 1 257 ? 2.511   58.655  57.884  1.00 53.12  ? 266  ASP B OD1 1 
ATOM   6939  O  OD2 . ASP B 1 257 ? 4.265   59.980  57.787  1.00 56.01  ? 266  ASP B OD2 1 
ATOM   6940  N  N   . VAL B 1 258 ? 0.123   61.009  54.466  1.00 32.82  ? 267  VAL B N   1 
ATOM   6941  C  CA  . VAL B 1 258 ? -0.317  62.039  53.563  1.00 30.99  ? 267  VAL B CA  1 
ATOM   6942  C  C   . VAL B 1 258 ? 0.416   63.299  53.937  1.00 32.53  ? 267  VAL B C   1 
ATOM   6943  O  O   . VAL B 1 258 ? 0.200   63.811  55.044  1.00 33.44  ? 267  VAL B O   1 
ATOM   6944  C  CB  . VAL B 1 258 ? -1.852  62.234  53.692  1.00 28.66  ? 267  VAL B CB  1 
ATOM   6945  C  CG1 . VAL B 1 258 ? -2.300  63.545  53.015  1.00 26.10  ? 267  VAL B CG1 1 
ATOM   6946  C  CG2 . VAL B 1 258 ? -2.541  61.029  53.071  1.00 29.47  ? 267  VAL B CG2 1 
ATOM   6947  N  N   . ASN B 1 259 ? 1.273   63.831  53.051  1.00 30.31  ? 268  ASN B N   1 
ATOM   6948  C  CA  . ASN B 1 259 ? 1.970   65.071  53.396  1.00 32.47  ? 268  ASN B CA  1 
ATOM   6949  C  C   . ASN B 1 259 ? 1.880   66.095  52.274  1.00 33.61  ? 268  ASN B C   1 
ATOM   6950  O  O   . ASN B 1 259 ? 2.486   67.169  52.351  1.00 31.63  ? 268  ASN B O   1 
ATOM   6951  C  CB  . ASN B 1 259 ? 3.439   64.781  53.693  1.00 37.70  ? 268  ASN B CB  1 
ATOM   6952  C  CG  . ASN B 1 259 ? 3.990   63.775  52.769  1.00 47.61  ? 268  ASN B CG  1 
ATOM   6953  O  OD1 . ASN B 1 259 ? 4.454   62.732  53.234  1.00 54.47  ? 268  ASN B OD1 1 
ATOM   6954  N  ND2 . ASN B 1 259 ? 3.959   63.977  51.450  1.00 50.27  ? 268  ASN B ND2 1 
ATOM   6955  N  N   . LYS B 1 260 ? 1.106   65.769  51.230  1.00 30.40  ? 269  LYS B N   1 
ATOM   6956  C  CA  . LYS B 1 260 ? 0.948   66.679  50.095  1.00 28.47  ? 269  LYS B CA  1 
ATOM   6957  C  C   . LYS B 1 260 ? -0.503  66.589  49.614  1.00 26.85  ? 269  LYS B C   1 
ATOM   6958  O  O   . LYS B 1 260 ? -1.070  65.485  49.624  1.00 26.72  ? 269  LYS B O   1 
ATOM   6959  C  CB  . LYS B 1 260 ? 1.943   66.256  49.014  1.00 29.92  ? 269  LYS B CB  1 
ATOM   6960  C  CG  . LYS B 1 260 ? 1.524   66.682  47.636  1.00 39.95  ? 269  LYS B CG  1 
ATOM   6961  C  CD  . LYS B 1 260 ? 2.695   66.745  46.650  1.00 45.53  ? 269  LYS B CD  1 
ATOM   6962  C  CE  . LYS B 1 260 ? 3.565   65.535  46.728  1.00 50.21  ? 269  LYS B CE  1 
ATOM   6963  N  NZ  . LYS B 1 260 ? 4.547   65.537  45.602  1.00 51.22  ? 269  LYS B NZ  1 
ATOM   6964  N  N   . ILE B 1 261 ? -1.120  67.718  49.257  1.00 26.85  ? 270  ILE B N   1 
ATOM   6965  C  CA  . ILE B 1 261 ? -2.490  67.653  48.722  1.00 26.81  ? 270  ILE B CA  1 
ATOM   6966  C  C   . ILE B 1 261 ? -2.553  68.452  47.427  1.00 28.87  ? 270  ILE B C   1 
ATOM   6967  O  O   . ILE B 1 261 ? -1.774  69.389  47.204  1.00 27.98  ? 270  ILE B O   1 
ATOM   6968  C  CB  . ILE B 1 261 ? -3.552  68.172  49.713  1.00 27.45  ? 270  ILE B CB  1 
ATOM   6969  C  CG1 . ILE B 1 261 ? -3.229  69.610  50.162  1.00 27.76  ? 270  ILE B CG1 1 
ATOM   6970  C  CG2 . ILE B 1 261 ? -3.607  67.198  50.924  1.00 21.93  ? 270  ILE B CG2 1 
ATOM   6971  C  CD1 . ILE B 1 261 ? -4.348  70.256  50.949  1.00 25.65  ? 270  ILE B CD1 1 
ATOM   6972  N  N   . TYR B 1 262 ? -3.485  68.072  46.574  1.00 26.32  ? 271  TYR B N   1 
ATOM   6973  C  CA  . TYR B 1 262 ? -3.760  68.786  45.329  1.00 24.24  ? 271  TYR B CA  1 
ATOM   6974  C  C   . TYR B 1 262 ? -5.202  69.224  45.459  1.00 20.02  ? 271  TYR B C   1 
ATOM   6975  O  O   . TYR B 1 262 ? -6.092  68.353  45.608  1.00 22.90  ? 271  TYR B O   1 
ATOM   6976  C  CB  . TYR B 1 262 ? -3.581  67.824  44.149  1.00 21.68  ? 271  TYR B CB  1 
ATOM   6977  C  CG  . TYR B 1 262 ? -2.152  67.408  43.953  1.00 23.66  ? 271  TYR B CG  1 
ATOM   6978  C  CD1 . TYR B 1 262 ? -1.263  68.211  43.252  1.00 24.55  ? 271  TYR B CD1 1 
ATOM   6979  C  CD2 . TYR B 1 262 ? -1.685  66.216  44.455  1.00 19.57  ? 271  TYR B CD2 1 
ATOM   6980  C  CE1 . TYR B 1 262 ? 0.051   67.814  43.048  1.00 22.12  ? 271  TYR B CE1 1 
ATOM   6981  C  CE2 . TYR B 1 262 ? -0.362  65.821  44.277  1.00 24.46  ? 271  TYR B CE2 1 
ATOM   6982  C  CZ  . TYR B 1 262 ? 0.497   66.628  43.556  1.00 23.77  ? 271  TYR B CZ  1 
ATOM   6983  O  OH  . TYR B 1 262 ? 1.785   66.237  43.313  1.00 27.09  ? 271  TYR B OH  1 
ATOM   6984  N  N   . ILE B 1 263 ? -5.497  70.507  45.438  1.00 20.16  ? 272  ILE B N   1 
ATOM   6985  C  CA  . ILE B 1 263 ? -6.871  70.934  45.681  1.00 24.38  ? 272  ILE B CA  1 
ATOM   6986  C  C   . ILE B 1 263 ? -7.580  71.393  44.417  1.00 28.51  ? 272  ILE B C   1 
ATOM   6987  O  O   . ILE B 1 263 ? -6.936  72.031  43.563  1.00 27.79  ? 272  ILE B O   1 
ATOM   6988  C  CB  . ILE B 1 263 ? -6.782  72.127  46.682  1.00 25.96  ? 272  ILE B CB  1 
ATOM   6989  C  CG1 . ILE B 1 263 ? -6.265  71.610  48.059  1.00 26.70  ? 272  ILE B CG1 1 
ATOM   6990  C  CG2 . ILE B 1 263 ? -8.145  72.873  46.835  1.00 24.69  ? 272  ILE B CG2 1 
ATOM   6991  C  CD1 . ILE B 1 263 ? -5.861  72.832  48.864  1.00 29.09  ? 272  ILE B CD1 1 
ATOM   6992  N  N   . ALA B 1 264 ? -8.873  71.059  44.292  1.00 26.36  ? 273  ALA B N   1 
ATOM   6993  C  CA  . ALA B 1 264 ? -9.682  71.529  43.185  1.00 24.02  ? 273  ALA B CA  1 
ATOM   6994  C  C   . ALA B 1 264 ? -11.011 71.897  43.717  1.00 24.38  ? 273  ALA B C   1 
ATOM   6995  O  O   . ALA B 1 264 ? -11.432 71.394  44.763  1.00 25.19  ? 273  ALA B O   1 
ATOM   6996  C  CB  . ALA B 1 264 ? -9.861  70.432  42.098  1.00 23.96  ? 273  ALA B CB  1 
ATOM   6997  N  N   . ASN B 1 265 ? -11.737 72.753  42.990  1.00 25.75  ? 274  ASN B N   1 
ATOM   6998  C  CA  . ASN B 1 265 ? -13.071 73.151  43.412  1.00 26.22  ? 274  ASN B CA  1 
ATOM   6999  C  C   . ASN B 1 265 ? -13.983 71.963  43.089  1.00 27.04  ? 274  ASN B C   1 
ATOM   7000  O  O   . ASN B 1 265 ? -13.992 71.506  41.951  1.00 24.54  ? 274  ASN B O   1 
ATOM   7001  C  CB  . ASN B 1 265 ? -13.486 74.433  42.645  1.00 28.14  ? 274  ASN B CB  1 
ATOM   7002  C  CG  . ASN B 1 265 ? -14.812 74.948  43.117  1.00 31.29  ? 274  ASN B CG  1 
ATOM   7003  O  OD1 . ASN B 1 265 ? -15.812 74.186  43.126  1.00 27.35  ? 274  ASN B OD1 1 
ATOM   7004  N  ND2 . ASN B 1 265 ? -14.914 76.205  43.537  1.00 31.44  ? 274  ASN B ND2 1 
ATOM   7005  N  N   . GLY B 1 266 ? -14.745 71.443  44.058  1.00 25.66  ? 275  GLY B N   1 
ATOM   7006  C  CA  . GLY B 1 266 ? -15.557 70.250  43.783  1.00 25.16  ? 275  GLY B CA  1 
ATOM   7007  C  C   . GLY B 1 266 ? -16.618 70.405  42.681  1.00 25.71  ? 275  GLY B C   1 
ATOM   7008  O  O   . GLY B 1 266 ? -16.699 69.588  41.787  1.00 24.74  ? 275  GLY B O   1 
ATOM   7009  N  N   . TYR B 1 267 ? -17.461 71.432  42.764  1.00 27.82  ? 276  TYR B N   1 
ATOM   7010  C  CA  . TYR B 1 267 ? -18.540 71.585  41.760  1.00 26.98  ? 276  TYR B CA  1 
ATOM   7011  C  C   . TYR B 1 267 ? -18.079 72.384  40.519  1.00 29.44  ? 276  TYR B C   1 
ATOM   7012  O  O   . TYR B 1 267 ? -18.542 72.093  39.419  1.00 27.86  ? 276  TYR B O   1 
ATOM   7013  C  CB  . TYR B 1 267 ? -19.748 72.295  42.390  1.00 29.25  ? 276  TYR B CB  1 
ATOM   7014  C  CG  . TYR B 1 267 ? -20.464 71.433  43.396  1.00 30.91  ? 276  TYR B CG  1 
ATOM   7015  C  CD1 . TYR B 1 267 ? -20.935 70.176  43.052  1.00 30.33  ? 276  TYR B CD1 1 
ATOM   7016  C  CD2 . TYR B 1 267 ? -20.666 71.876  44.705  1.00 35.22  ? 276  TYR B CD2 1 
ATOM   7017  C  CE1 . TYR B 1 267 ? -21.586 69.373  43.981  1.00 33.66  ? 276  TYR B CE1 1 
ATOM   7018  C  CE2 . TYR B 1 267 ? -21.304 71.073  45.649  1.00 35.52  ? 276  TYR B CE2 1 
ATOM   7019  C  CZ  . TYR B 1 267 ? -21.758 69.823  45.286  1.00 36.21  ? 276  TYR B CZ  1 
ATOM   7020  O  OH  . TYR B 1 267 ? -22.360 69.025  46.235  1.00 37.64  ? 276  TYR B OH  1 
ATOM   7021  N  N   . ALA B 1 268 ? -17.167 73.326  40.705  1.00 29.05  ? 277  ALA B N   1 
ATOM   7022  C  CA  . ALA B 1 268 ? -16.627 74.191  39.641  1.00 32.20  ? 277  ALA B CA  1 
ATOM   7023  C  C   . ALA B 1 268 ? -15.354 73.718  39.018  1.00 32.47  ? 277  ALA B C   1 
ATOM   7024  O  O   . ALA B 1 268 ? -15.017 74.208  37.954  1.00 35.69  ? 277  ALA B O   1 
ATOM   7025  C  CB  . ALA B 1 268 ? -16.377 75.610  40.204  1.00 37.14  ? 277  ALA B CB  1 
ATOM   7026  N  N   . GLY B 1 269 ? -14.632 72.762  39.612  1.00 30.28  ? 278  GLY B N   1 
ATOM   7027  C  CA  . GLY B 1 269 ? -13.359 72.329  39.046  1.00 26.70  ? 278  GLY B CA  1 
ATOM   7028  C  C   . GLY B 1 269 ? -13.254 70.837  38.801  1.00 22.71  ? 278  GLY B C   1 
ATOM   7029  O  O   . GLY B 1 269 ? -12.239 70.198  39.074  1.00 24.07  ? 278  GLY B O   1 
ATOM   7030  N  N   . GLU B 1 270 ? -14.329 70.232  38.258  1.00 21.85  ? 279  GLU B N   1 
ATOM   7031  C  CA  . GLU B 1 270 ? -14.232 68.804  37.975  1.00 22.29  ? 279  GLU B CA  1 
ATOM   7032  C  C   . GLU B 1 270 ? -13.084 68.539  37.026  1.00 24.80  ? 279  GLU B C   1 
ATOM   7033  O  O   . GLU B 1 270 ? -12.378 67.530  37.178  1.00 23.58  ? 279  GLU B O   1 
ATOM   7034  C  CB  . GLU B 1 270 ? -15.550 68.317  37.342  1.00 25.12  ? 279  GLU B CB  1 
ATOM   7035  C  CG  . GLU B 1 270 ? -16.679 68.293  38.367  1.00 35.34  ? 279  GLU B CG  1 
ATOM   7036  C  CD  . GLU B 1 270 ? -18.033 67.976  37.733  1.00 47.60  ? 279  GLU B CD  1 
ATOM   7037  O  OE1 . GLU B 1 270 ? -19.071 67.970  38.455  1.00 39.51  ? 279  GLU B OE1 1 
ATOM   7038  O  OE2 . GLU B 1 270 ? -18.055 67.734  36.505  1.00 48.17  ? 279  GLU B OE2 1 
ATOM   7039  N  N   . TYR B 1 271 ? -12.845 69.452  36.019  1.00 22.89  ? 280  TYR B N   1 
ATOM   7040  C  CA  . TYR B 1 271 ? -11.706 69.138  35.131  1.00 24.32  ? 280  TYR B CA  1 
ATOM   7041  C  C   . TYR B 1 271 ? -10.364 69.482  35.810  1.00 22.71  ? 280  TYR B C   1 
ATOM   7042  O  O   . TYR B 1 271 ? -9.372  68.930  35.455  1.00 23.96  ? 280  TYR B O   1 
ATOM   7043  C  CB  . TYR B 1 271 ? -11.856 69.886  33.754  1.00 24.02  ? 280  TYR B CB  1 
ATOM   7044  C  CG  . TYR B 1 271 ? -12.831 69.102  32.898  1.00 25.36  ? 280  TYR B CG  1 
ATOM   7045  C  CD1 . TYR B 1 271 ? -14.201 69.396  32.912  1.00 27.46  ? 280  TYR B CD1 1 
ATOM   7046  C  CD2 . TYR B 1 271 ? -12.392 68.051  32.105  1.00 27.37  ? 280  TYR B CD2 1 
ATOM   7047  C  CE1 . TYR B 1 271 ? -15.105 68.661  32.151  1.00 31.03  ? 280  TYR B CE1 1 
ATOM   7048  C  CE2 . TYR B 1 271 ? -13.287 67.301  31.340  1.00 31.01  ? 280  TYR B CE2 1 
ATOM   7049  C  CZ  . TYR B 1 271 ? -14.640 67.611  31.360  1.00 34.12  ? 280  TYR B CZ  1 
ATOM   7050  O  OH  . TYR B 1 271 ? -15.473 66.879  30.560  1.00 32.45  ? 280  TYR B OH  1 
ATOM   7051  N  N   . ASP B 1 272 ? -10.351 70.383  36.789  1.00 24.59  ? 281  ASP B N   1 
ATOM   7052  C  CA  . ASP B 1 272 ? -9.088  70.614  37.521  1.00 26.76  ? 281  ASP B CA  1 
ATOM   7053  C  C   . ASP B 1 272 ? -8.672  69.303  38.276  1.00 24.03  ? 281  ASP B C   1 
ATOM   7054  O  O   . ASP B 1 272 ? -7.506  68.880  38.253  1.00 21.80  ? 281  ASP B O   1 
ATOM   7055  C  CB  . ASP B 1 272 ? -9.320  71.781  38.485  1.00 25.75  ? 281  ASP B CB  1 
ATOM   7056  C  CG  . ASP B 1 272 ? -9.554  73.080  37.714  1.00 28.52  ? 281  ASP B CG  1 
ATOM   7057  O  OD1 . ASP B 1 272 ? -8.829  73.319  36.718  1.00 28.66  ? 281  ASP B OD1 1 
ATOM   7058  O  OD2 . ASP B 1 272 ? -10.462 73.849  38.098  1.00 28.40  ? 281  ASP B OD2 1 
ATOM   7059  N  N   . ALA B 1 273 ? -9.667  68.638  38.951  1.00 24.98  ? 282  ALA B N   1 
ATOM   7060  C  CA  . ALA B 1 273 ? -9.380  67.369  39.644  1.00 23.76  ? 282  ALA B CA  1 
ATOM   7061  C  C   . ALA B 1 273 ? -8.929  66.309  38.631  1.00 21.29  ? 282  ALA B C   1 
ATOM   7062  O  O   . ALA B 1 273 ? -7.963  65.612  38.811  1.00 22.48  ? 282  ALA B O   1 
ATOM   7063  C  CB  . ALA B 1 273 ? -10.659 66.896  40.350  1.00 24.14  ? 282  ALA B CB  1 
ATOM   7064  N  N   . LEU B 1 274 ? -9.660  66.208  37.517  1.00 24.10  ? 283  LEU B N   1 
ATOM   7065  C  CA  . LEU B 1 274 ? -9.277  65.239  36.470  1.00 22.02  ? 283  LEU B CA  1 
ATOM   7066  C  C   . LEU B 1 274 ? -7.842  65.498  35.982  1.00 19.24  ? 283  LEU B C   1 
ATOM   7067  O  O   . LEU B 1 274 ? -7.046  64.585  35.829  1.00 20.31  ? 283  LEU B O   1 
ATOM   7068  C  CB  . LEU B 1 274 ? -10.303 65.456  35.306  1.00 23.48  ? 283  LEU B CB  1 
ATOM   7069  C  CG  . LEU B 1 274 ? -10.137 64.597  34.078  1.00 34.45  ? 283  LEU B CG  1 
ATOM   7070  C  CD1 . LEU B 1 274 ? -11.468 64.567  33.303  1.00 29.46  ? 283  LEU B CD1 1 
ATOM   7071  C  CD2 . LEU B 1 274 ? -9.065  65.203  33.154  1.00 35.70  ? 283  LEU B CD2 1 
ATOM   7072  N  N   . ASN B 1 275 ? -7.535  66.787  35.724  1.00 22.62  ? 284  ASN B N   1 
ATOM   7073  C  CA  . ASN B 1 275 ? -6.217  67.167  35.159  1.00 19.96  ? 284  ASN B CA  1 
ATOM   7074  C  C   . ASN B 1 275 ? -5.095  66.828  36.073  1.00 23.05  ? 284  ASN B C   1 
ATOM   7075  O  O   . ASN B 1 275 ? -4.007  66.493  35.604  1.00 22.01  ? 284  ASN B O   1 
ATOM   7076  C  CB  . ASN B 1 275 ? -6.241  68.707  34.845  1.00 19.81  ? 284  ASN B CB  1 
ATOM   7077  C  CG  . ASN B 1 275 ? -6.767  69.001  33.465  1.00 19.83  ? 284  ASN B CG  1 
ATOM   7078  O  OD1 . ASN B 1 275 ? -6.508  68.185  32.582  1.00 19.35  ? 284  ASN B OD1 1 
ATOM   7079  N  ND2 . ASN B 1 275 ? -7.532  70.094  33.225  1.00 21.92  ? 284  ASN B ND2 1 
ATOM   7080  N  N   . ILE B 1 276 ? -5.304  66.906  37.416  1.00 22.87  ? 285  ILE B N   1 
ATOM   7081  C  CA  . ILE B 1 276 ? -4.185  66.530  38.283  1.00 20.74  ? 285  ILE B CA  1 
ATOM   7082  C  C   . ILE B 1 276 ? -4.240  65.015  38.666  1.00 23.57  ? 285  ILE B C   1 
ATOM   7083  O  O   . ILE B 1 276 ? -3.364  64.507  39.362  1.00 22.75  ? 285  ILE B O   1 
ATOM   7084  C  CB  . ILE B 1 276 ? -4.266  67.453  39.543  1.00 21.80  ? 285  ILE B CB  1 
ATOM   7085  C  CG1 . ILE B 1 276 ? -2.901  67.461  40.267  1.00 23.92  ? 285  ILE B CG1 1 
ATOM   7086  C  CG2 . ILE B 1 276 ? -5.420  66.968  40.480  1.00 22.98  ? 285  ILE B CG2 1 
ATOM   7087  C  CD1 . ILE B 1 276 ? -1.687  67.891  39.358  1.00 26.84  ? 285  ILE B CD1 1 
ATOM   7088  N  N   . SER B 1 277 ? -5.255  64.267  38.209  1.00 24.94  ? 286  SER B N   1 
ATOM   7089  C  CA  . SER B 1 277 ? -5.360  62.843  38.645  1.00 22.86  ? 286  SER B CA  1 
ATOM   7090  C  C   . SER B 1 277 ? -4.188  61.981  38.418  1.00 24.40  ? 286  SER B C   1 
ATOM   7091  O  O   . SER B 1 277 ? -3.803  61.219  39.304  1.00 22.07  ? 286  SER B O   1 
ATOM   7092  C  CB  . SER B 1 277 ? -6.554  62.169  37.939  1.00 24.84  ? 286  SER B CB  1 
ATOM   7093  O  OG  . SER B 1 277 ? -7.706  62.583  38.638  1.00 32.57  ? 286  SER B OG  1 
ATOM   7094  N  N   . SER B 1 278 ? -3.553  61.996  37.203  1.00 22.91  ? 287  SER B N   1 
ATOM   7095  C  CA  . SER B 1 278 ? -2.441  61.070  37.069  1.00 18.88  ? 287  SER B CA  1 
ATOM   7096  C  C   . SER B 1 278 ? -1.285  61.423  37.980  1.00 22.41  ? 287  SER B C   1 
ATOM   7097  O  O   . SER B 1 278 ? -0.582  60.512  38.436  1.00 25.12  ? 287  SER B O   1 
ATOM   7098  C  CB  . SER B 1 278 ? -1.906  61.012  35.613  1.00 20.97  ? 287  SER B CB  1 
ATOM   7099  O  OG  . SER B 1 278 ? -1.453  62.296  35.205  1.00 26.28  ? 287  SER B OG  1 
ATOM   7100  N  N   . LYS B 1 279 ? -1.053  62.700  38.248  1.00 22.70  ? 288  LYS B N   1 
ATOM   7101  C  CA  . LYS B 1 279 ? 0.093   63.081  39.096  1.00 20.83  ? 288  LYS B CA  1 
ATOM   7102  C  C   . LYS B 1 279 ? -0.201  62.747  40.597  1.00 20.70  ? 288  LYS B C   1 
ATOM   7103  O  O   . LYS B 1 279 ? 0.666   62.188  41.251  1.00 24.28  ? 288  LYS B O   1 
ATOM   7104  C  CB  . LYS B 1 279 ? 0.380   64.574  38.926  1.00 20.50  ? 288  LYS B CB  1 
ATOM   7105  C  CG  . LYS B 1 279 ? 1.555   65.129  39.806  1.00 25.45  ? 288  LYS B CG  1 
ATOM   7106  C  CD  . LYS B 1 279 ? 2.837   64.359  39.648  1.00 30.30  ? 288  LYS B CD  1 
ATOM   7107  C  CE  . LYS B 1 279 ? 3.910   64.997  40.543  1.00 34.57  ? 288  LYS B CE  1 
ATOM   7108  N  NZ  . LYS B 1 279 ? 5.045   64.048  40.744  1.00 34.27  ? 288  LYS B NZ  1 
ATOM   7109  N  N   . ALA B 1 280 ? -1.389  63.056  41.059  1.00 23.32  ? 289  ALA B N   1 
ATOM   7110  C  CA  . ALA B 1 280 ? -1.779  62.737  42.440  1.00 21.94  ? 289  ALA B CA  1 
ATOM   7111  C  C   . ALA B 1 280 ? -1.724  61.189  42.515  1.00 23.12  ? 289  ALA B C   1 
ATOM   7112  O  O   . ALA B 1 280 ? -1.279  60.623  43.530  1.00 22.95  ? 289  ALA B O   1 
ATOM   7113  C  CB  . ALA B 1 280 ? -3.153  63.290  42.713  1.00 20.88  ? 289  ALA B CB  1 
ATOM   7114  N  N   . GLY B 1 281 ? -2.107  60.483  41.426  1.00 21.94  ? 290  GLY B N   1 
ATOM   7115  C  CA  . GLY B 1 281 ? -2.058  59.020  41.418  1.00 22.20  ? 290  GLY B CA  1 
ATOM   7116  C  C   . GLY B 1 281 ? -0.616  58.489  41.531  1.00 26.00  ? 290  GLY B C   1 
ATOM   7117  O  O   . GLY B 1 281 ? -0.324  57.587  42.308  1.00 22.73  ? 290  GLY B O   1 
ATOM   7118  N  N   . GLU B 1 282 ? 0.312   59.040  40.732  1.00 23.01  ? 291  GLU B N   1 
ATOM   7119  C  CA  . GLU B 1 282 ? 1.700   58.597  40.789  1.00 23.12  ? 291  GLU B CA  1 
ATOM   7120  C  C   . GLU B 1 282 ? 2.248   58.854  42.217  1.00 26.74  ? 291  GLU B C   1 
ATOM   7121  O  O   . GLU B 1 282 ? 2.921   58.008  42.772  1.00 28.08  ? 291  GLU B O   1 
ATOM   7122  C  CB  . GLU B 1 282 ? 2.514   59.423  39.759  1.00 28.51  ? 291  GLU B CB  1 
ATOM   7123  C  CG  . GLU B 1 282 ? 3.902   58.858  39.621  1.00 36.70  ? 291  GLU B CG  1 
ATOM   7124  C  CD  . GLU B 1 282 ? 4.811   59.711  38.732  1.00 43.06  ? 291  GLU B CD  1 
ATOM   7125  O  OE1 . GLU B 1 282 ? 4.349   60.209  37.670  1.00 45.19  ? 291  GLU B OE1 1 
ATOM   7126  O  OE2 . GLU B 1 282 ? 5.977   59.849  39.112  1.00 48.25  ? 291  GLU B OE2 1 
ATOM   7127  N  N   . ASP B 1 283 ? 1.958   60.008  42.778  1.00 25.89  ? 292  ASP B N   1 
ATOM   7128  C  CA  . ASP B 1 283 ? 2.459   60.345  44.123  1.00 26.21  ? 292  ASP B CA  1 
ATOM   7129  C  C   . ASP B 1 283 ? 1.723   59.575  45.213  1.00 29.82  ? 292  ASP B C   1 
ATOM   7130  O  O   . ASP B 1 283 ? 2.231   59.474  46.322  1.00 28.74  ? 292  ASP B O   1 
ATOM   7131  C  CB  . ASP B 1 283 ? 2.194   61.847  44.390  1.00 28.51  ? 292  ASP B CB  1 
ATOM   7132  C  CG  . ASP B 1 283 ? 3.080   62.794  43.600  1.00 29.86  ? 292  ASP B CG  1 
ATOM   7133  O  OD1 . ASP B 1 283 ? 3.960   62.312  42.862  1.00 32.49  ? 292  ASP B OD1 1 
ATOM   7134  O  OD2 . ASP B 1 283 ? 2.891   64.003  43.720  1.00 34.07  ? 292  ASP B OD2 1 
ATOM   7135  N  N   . GLN B 1 284 ? 0.508   59.032  44.915  1.00 27.12  ? 293  GLN B N   1 
ATOM   7136  C  CA  . GLN B 1 284 ? -0.352  58.393  45.936  1.00 25.78  ? 293  GLN B CA  1 
ATOM   7137  C  C   . GLN B 1 284 ? -0.628  59.385  47.033  1.00 26.46  ? 293  GLN B C   1 
ATOM   7138  O  O   . GLN B 1 284 ? -0.553  59.053  48.218  1.00 28.05  ? 293  GLN B O   1 
ATOM   7139  C  CB  . GLN B 1 284 ? 0.257   57.094  46.489  1.00 27.06  ? 293  GLN B CB  1 
ATOM   7140  C  CG  . GLN B 1 284 ? 0.502   56.085  45.358  1.00 26.94  ? 293  GLN B CG  1 
ATOM   7141  C  CD  . GLN B 1 284 ? 1.072   54.768  45.834  1.00 32.06  ? 293  GLN B CD  1 
ATOM   7142  O  OE1 . GLN B 1 284 ? 1.079   54.464  47.022  1.00 32.46  ? 293  GLN B OE1 1 
ATOM   7143  N  NE2 . GLN B 1 284 ? 1.486   53.927  44.921  1.00 30.55  ? 293  GLN B NE2 1 
ATOM   7144  N  N   . GLN B 1 285 ? -0.906  60.635  46.671  1.00 27.10  ? 294  GLN B N   1 
ATOM   7145  C  CA  . GLN B 1 285 ? -1.271  61.697  47.642  1.00 25.95  ? 294  GLN B CA  1 
ATOM   7146  C  C   . GLN B 1 285 ? -2.635  62.187  47.178  1.00 25.21  ? 294  GLN B C   1 
ATOM   7147  O  O   . GLN B 1 285 ? -2.935  62.231  45.965  1.00 23.09  ? 294  GLN B O   1 
ATOM   7148  C  CB  . GLN B 1 285 ? -0.188  62.798  47.719  1.00 23.72  ? 294  GLN B CB  1 
ATOM   7149  C  CG  . GLN B 1 285 ? 1.121   62.163  48.277  1.00 26.24  ? 294  GLN B CG  1 
ATOM   7150  C  CD  . GLN B 1 285 ? 1.054   61.961  49.798  1.00 24.67  ? 294  GLN B CD  1 
ATOM   7151  O  OE1 . GLN B 1 285 ? 0.505   62.777  50.524  1.00 27.88  ? 294  GLN B OE1 1 
ATOM   7152  N  NE2 . GLN B 1 285 ? 1.586   60.850  50.275  1.00 29.29  ? 294  GLN B NE2 1 
ATOM   7153  N  N   . PRO B 1 286 ? -3.492  62.582  48.098  1.00 23.31  ? 295  PRO B N   1 
ATOM   7154  C  CA  . PRO B 1 286 ? -4.835  63.009  47.704  1.00 23.45  ? 295  PRO B CA  1 
ATOM   7155  C  C   . PRO B 1 286 ? -5.184  64.271  46.982  1.00 24.00  ? 295  PRO B C   1 
ATOM   7156  O  O   . PRO B 1 286 ? -4.536  65.312  47.064  1.00 22.75  ? 295  PRO B O   1 
ATOM   7157  C  CB  . PRO B 1 286 ? -5.609  62.991  49.038  1.00 26.51  ? 295  PRO B CB  1 
ATOM   7158  C  CG  . PRO B 1 286 ? -4.566  63.301  50.062  1.00 26.02  ? 295  PRO B CG  1 
ATOM   7159  C  CD  . PRO B 1 286 ? -3.267  62.720  49.565  1.00 24.15  ? 295  PRO B CD  1 
ATOM   7160  N  N   . ILE B 1 287 ? -6.323  64.136  46.273  1.00 21.71  ? 296  ILE B N   1 
ATOM   7161  C  CA  . ILE B 1 287 ? -6.935  65.295  45.673  1.00 23.20  ? 296  ILE B CA  1 
ATOM   7162  C  C   . ILE B 1 287 ? -7.996  65.710  46.653  1.00 23.06  ? 296  ILE B C   1 
ATOM   7163  O  O   . ILE B 1 287 ? -8.853  64.892  46.968  1.00 23.90  ? 296  ILE B O   1 
ATOM   7164  C  CB  . ILE B 1 287 ? -7.586  64.975  44.304  1.00 23.19  ? 296  ILE B CB  1 
ATOM   7165  C  CG1 . ILE B 1 287 ? -6.477  64.591  43.307  1.00 25.45  ? 296  ILE B CG1 1 
ATOM   7166  C  CG2 . ILE B 1 287 ? -8.464  66.220  43.873  1.00 23.67  ? 296  ILE B CG2 1 
ATOM   7167  C  CD1 . ILE B 1 287 ? -7.012  63.753  42.114  1.00 23.13  ? 296  ILE B CD1 1 
ATOM   7168  N  N   . ILE B 1 288 ? -7.968  66.936  47.139  1.00 23.18  ? 297  ILE B N   1 
ATOM   7169  C  CA  . ILE B 1 288 ? -8.933  67.449  48.113  1.00 24.95  ? 297  ILE B CA  1 
ATOM   7170  C  C   . ILE B 1 288 ? -9.878  68.391  47.423  1.00 24.54  ? 297  ILE B C   1 
ATOM   7171  O  O   . ILE B 1 288 ? -9.423  69.313  46.752  1.00 25.09  ? 297  ILE B O   1 
ATOM   7172  C  CB  . ILE B 1 288 ? -8.160  68.188  49.287  1.00 24.33  ? 297  ILE B CB  1 
ATOM   7173  C  CG1 . ILE B 1 288 ? -7.333  67.141  50.073  1.00 25.01  ? 297  ILE B CG1 1 
ATOM   7174  C  CG2 . ILE B 1 288 ? -9.131  68.907  50.213  1.00 25.54  ? 297  ILE B CG2 1 
ATOM   7175  C  CD1 . ILE B 1 288 ? -8.238  66.109  50.732  1.00 26.87  ? 297  ILE B CD1 1 
ATOM   7176  N  N   . LEU B 1 289 ? -11.201 68.175  47.557  1.00 22.59  ? 298  LEU B N   1 
ATOM   7177  C  CA  . LEU B 1 289 ? -12.145 69.063  46.904  1.00 21.64  ? 298  LEU B CA  1 
ATOM   7178  C  C   . LEU B 1 289 ? -12.544 70.166  47.855  1.00 27.57  ? 298  LEU B C   1 
ATOM   7179  O  O   . LEU B 1 289 ? -12.814 69.929  49.040  1.00 27.04  ? 298  LEU B O   1 
ATOM   7180  C  CB  . LEU B 1 289 ? -13.390 68.352  46.390  1.00 22.27  ? 298  LEU B CB  1 
ATOM   7181  C  CG  . LEU B 1 289 ? -13.081 67.183  45.435  1.00 20.97  ? 298  LEU B CG  1 
ATOM   7182  C  CD1 . LEU B 1 289 ? -14.467 66.529  44.937  1.00 24.12  ? 298  LEU B CD1 1 
ATOM   7183  C  CD2 . LEU B 1 289 ? -12.256 67.681  44.160  1.00 20.35  ? 298  LEU B CD2 1 
ATOM   7184  N  N   . ALA B 1 290 ? -12.656 71.381  47.321  1.00 27.14  ? 299  ALA B N   1 
ATOM   7185  C  CA  . ALA B 1 290 ? -12.936 72.565  48.114  1.00 26.42  ? 299  ALA B CA  1 
ATOM   7186  C  C   . ALA B 1 290 ? -14.037 73.414  47.563  1.00 28.99  ? 299  ALA B C   1 
ATOM   7187  O  O   . ALA B 1 290 ? -14.540 73.164  46.468  1.00 28.20  ? 299  ALA B O   1 
ATOM   7188  C  CB  . ALA B 1 290 ? -11.657 73.417  48.126  1.00 26.02  ? 299  ALA B CB  1 
ATOM   7189  N  N   . ASN B 1 291 ? -14.428 74.424  48.332  1.00 29.68  ? 300  ASN B N   1 
ATOM   7190  C  CA  . ASN B 1 291 ? -15.345 75.449  47.833  1.00 32.36  ? 300  ASN B CA  1 
ATOM   7191  C  C   . ASN B 1 291 ? -14.386 76.563  47.319  1.00 35.25  ? 300  ASN B C   1 
ATOM   7192  O  O   . ASN B 1 291 ? -13.172 76.471  47.491  1.00 33.35  ? 300  ASN B O   1 
ATOM   7193  C  CB  . ASN B 1 291 ? -16.267 75.976  48.922  1.00 36.80  ? 300  ASN B CB  1 
ATOM   7194  C  CG  . ASN B 1 291 ? -17.038 74.853  49.579  1.00 41.60  ? 300  ASN B CG  1 
ATOM   7195  O  OD1 . ASN B 1 291 ? -17.842 74.172  48.918  1.00 42.04  ? 300  ASN B OD1 1 
ATOM   7196  N  ND2 . ASN B 1 291 ? -16.788 74.557  50.841  1.00 43.91  ? 300  ASN B ND2 1 
ATOM   7197  N  N   . LYS B 1 292 ? -14.913 77.593  46.688  1.00 38.94  ? 301  LYS B N   1 
ATOM   7198  C  CA  . LYS B 1 292 ? -14.088 78.675  46.150  1.00 42.94  ? 301  LYS B CA  1 
ATOM   7199  C  C   . LYS B 1 292 ? -13.184 79.383  47.187  1.00 43.79  ? 301  LYS B C   1 
ATOM   7200  O  O   . LYS B 1 292 ? -11.998 79.636  46.921  1.00 41.69  ? 301  LYS B O   1 
ATOM   7201  C  CB  . LYS B 1 292 ? -15.038 79.720  45.529  1.00 47.89  ? 301  LYS B CB  1 
ATOM   7202  C  CG  . LYS B 1 292 ? -14.318 80.783  44.678  1.00 55.12  ? 301  LYS B CG  1 
ATOM   7203  C  CD  . LYS B 1 292 ? -15.347 81.663  43.964  1.00 59.19  ? 301  LYS B CD  1 
ATOM   7204  C  CE  . LYS B 1 292 ? -14.812 83.038  43.673  1.00 62.63  ? 301  LYS B CE  1 
ATOM   7205  N  NZ  . LYS B 1 292 ? -14.216 83.092  42.304  1.00 64.22  ? 301  LYS B NZ  1 
ATOM   7206  N  N   . ASP B 1 293 ? -13.750 79.681  48.362  1.00 45.75  ? 302  ASP B N   1 
ATOM   7207  C  CA  . ASP B 1 293 ? -13.048 80.451  49.388  1.00 48.56  ? 302  ASP B CA  1 
ATOM   7208  C  C   . ASP B 1 293 ? -12.483 79.656  50.503  1.00 50.95  ? 302  ASP B C   1 
ATOM   7209  O  O   . ASP B 1 293 ? -11.823 80.235  51.366  1.00 50.65  ? 302  ASP B O   1 
ATOM   7210  C  CB  . ASP B 1 293 ? -14.003 81.500  49.959  1.00 50.40  ? 302  ASP B CB  1 
ATOM   7211  C  CG  . ASP B 1 293 ? -14.329 82.595  48.958  1.00 52.76  ? 302  ASP B CG  1 
ATOM   7212  O  OD1 . ASP B 1 293 ? -13.498 82.851  48.053  1.00 49.22  ? 302  ASP B OD1 1 
ATOM   7213  O  OD2 . ASP B 1 293 ? -15.411 83.193  49.073  1.00 54.25  ? 302  ASP B OD2 1 
ATOM   7214  N  N   . SER B 1 294 ? -12.680 78.336  50.509  1.00 48.24  ? 303  SER B N   1 
ATOM   7215  C  CA  . SER B 1 294 ? -12.157 77.539  51.606  1.00 42.92  ? 303  SER B CA  1 
ATOM   7216  C  C   . SER B 1 294 ? -12.452 76.081  51.432  1.00 41.42  ? 303  SER B C   1 
ATOM   7217  O  O   . SER B 1 294 ? -13.359 75.740  50.659  1.00 38.56  ? 303  SER B O   1 
ATOM   7218  C  CB  . SER B 1 294 ? -12.841 77.965  52.907  1.00 43.82  ? 303  SER B CB  1 
ATOM   7219  O  OG  . SER B 1 294 ? -14.241 77.721  52.858  1.00 42.69  ? 303  SER B OG  1 
ATOM   7220  N  N   . VAL B 1 295 ? -11.696 75.203  52.133  1.00 40.92  ? 304  VAL B N   1 
ATOM   7221  C  CA  . VAL B 1 295 ? -12.040 73.777  52.125  1.00 42.64  ? 304  VAL B CA  1 
ATOM   7222  C  C   . VAL B 1 295 ? -13.081 73.666  53.217  1.00 46.85  ? 304  VAL B C   1 
ATOM   7223  O  O   . VAL B 1 295 ? -13.029 74.472  54.178  1.00 48.03  ? 304  VAL B O   1 
ATOM   7224  C  CB  . VAL B 1 295 ? -10.860 72.818  52.408  1.00 45.41  ? 304  VAL B CB  1 
ATOM   7225  C  CG1 . VAL B 1 295 ? -9.726  73.080  51.411  1.00 45.90  ? 304  VAL B CG1 1 
ATOM   7226  C  CG2 . VAL B 1 295 ? -10.363 72.990  53.847  1.00 45.52  ? 304  VAL B CG2 1 
ATOM   7227  N  N   . PRO B 1 296 ? -14.045 72.735  53.149  1.00 47.64  ? 305  PRO B N   1 
ATOM   7228  C  CA  . PRO B 1 296 ? -15.021 72.691  54.251  1.00 47.46  ? 305  PRO B CA  1 
ATOM   7229  C  C   . PRO B 1 296 ? -14.325 72.522  55.630  1.00 44.25  ? 305  PRO B C   1 
ATOM   7230  O  O   . PRO B 1 296 ? -13.180 72.033  55.683  1.00 41.97  ? 305  PRO B O   1 
ATOM   7231  C  CB  . PRO B 1 296 ? -15.940 71.509  53.875  1.00 48.26  ? 305  PRO B CB  1 
ATOM   7232  C  CG  . PRO B 1 296 ? -15.410 70.938  52.567  1.00 49.81  ? 305  PRO B CG  1 
ATOM   7233  C  CD  . PRO B 1 296 ? -14.491 71.967  51.979  1.00 49.27  ? 305  PRO B CD  1 
ATOM   7234  N  N   . GLN B 1 297 ? -15.019 72.896  56.739  1.00 44.47  ? 306  GLN B N   1 
ATOM   7235  C  CA  . GLN B 1 297 ? -14.420 72.819  58.074  1.00 47.17  ? 306  GLN B CA  1 
ATOM   7236  C  C   . GLN B 1 297 ? -13.933 71.422  58.408  1.00 43.31  ? 306  GLN B C   1 
ATOM   7237  O  O   . GLN B 1 297 ? -12.840 71.270  58.964  1.00 38.73  ? 306  GLN B O   1 
ATOM   7238  C  CB  . GLN B 1 297 ? -15.431 73.260  59.197  1.00 51.17  ? 306  GLN B CB  1 
ATOM   7239  C  CG  . GLN B 1 297 ? -15.220 74.697  59.764  1.00 60.59  ? 306  GLN B CG  1 
ATOM   7240  C  CD  . GLN B 1 297 ? -13.764 75.015  60.122  1.00 69.96  ? 306  GLN B CD  1 
ATOM   7241  O  OE1 . GLN B 1 297 ? -13.188 74.465  61.077  1.00 72.10  ? 306  GLN B OE1 1 
ATOM   7242  N  NE2 . GLN B 1 297 ? -13.126 75.920  59.341  1.00 70.77  ? 306  GLN B NE2 1 
ATOM   7243  N  N   . GLY B 1 298 ? -14.741 70.397  58.070  1.00 37.25  ? 307  GLY B N   1 
ATOM   7244  C  CA  . GLY B 1 298 ? -14.358 69.040  58.397  1.00 33.75  ? 307  GLY B CA  1 
ATOM   7245  C  C   . GLY B 1 298 ? -13.038 68.646  57.790  1.00 34.24  ? 307  GLY B C   1 
ATOM   7246  O  O   . GLY B 1 298 ? -12.181 68.023  58.412  1.00 33.58  ? 307  GLY B O   1 
ATOM   7247  N  N   . THR B 1 299 ? -12.871 69.037  56.518  1.00 34.57  ? 308  THR B N   1 
ATOM   7248  C  CA  . THR B 1 299 ? -11.646 68.726  55.820  1.00 32.52  ? 308  THR B CA  1 
ATOM   7249  C  C   . THR B 1 299 ? -10.503 69.527  56.387  1.00 31.37  ? 308  THR B C   1 
ATOM   7250  O  O   . THR B 1 299 ? -9.402  68.995  56.608  1.00 33.94  ? 308  THR B O   1 
ATOM   7251  C  CB  . THR B 1 299 ? -11.805 69.077  54.325  1.00 30.84  ? 308  THR B CB  1 
ATOM   7252  O  OG1 . THR B 1 299 ? -12.896 68.305  53.822  1.00 29.93  ? 308  THR B OG1 1 
ATOM   7253  C  CG2 . THR B 1 299 ? -10.528 68.800  53.547  1.00 31.15  ? 308  THR B CG2 1 
ATOM   7254  N  N   . TYR B 1 300 ? -10.743 70.794  56.600  1.00 34.25  ? 309  TYR B N   1 
ATOM   7255  C  CA  . TYR B 1 300 ? -9.697  71.664  57.123  1.00 42.00  ? 309  TYR B CA  1 
ATOM   7256  C  C   . TYR B 1 300 ? -9.209  71.157  58.497  1.00 44.22  ? 309  TYR B C   1 
ATOM   7257  O  O   . TYR B 1 300 ? -7.999  71.139  58.782  1.00 43.46  ? 309  TYR B O   1 
ATOM   7258  C  CB  . TYR B 1 300 ? -10.250 73.090  57.245  1.00 45.83  ? 309  TYR B CB  1 
ATOM   7259  C  CG  . TYR B 1 300 ? -9.258  74.017  57.911  1.00 50.92  ? 309  TYR B CG  1 
ATOM   7260  C  CD1 . TYR B 1 300 ? -8.218  74.586  57.188  1.00 50.78  ? 309  TYR B CD1 1 
ATOM   7261  C  CD2 . TYR B 1 300 ? -9.345  74.298  59.270  1.00 53.60  ? 309  TYR B CD2 1 
ATOM   7262  C  CE1 . TYR B 1 300 ? -7.278  75.405  57.799  1.00 55.46  ? 309  TYR B CE1 1 
ATOM   7263  C  CE2 . TYR B 1 300 ? -8.414  75.121  59.893  1.00 60.27  ? 309  TYR B CE2 1 
ATOM   7264  C  CZ  . TYR B 1 300 ? -7.375  75.670  59.155  1.00 59.37  ? 309  TYR B CZ  1 
ATOM   7265  O  OH  . TYR B 1 300 ? -6.427  76.470  59.765  1.00 61.97  ? 309  TYR B OH  1 
ATOM   7266  N  N   . ASN B 1 301 ? -10.144 70.727  59.324  1.00 44.69  ? 310  ASN B N   1 
ATOM   7267  C  CA  . ASN B 1 301 ? -9.776  70.200  60.624  1.00 46.20  ? 310  ASN B CA  1 
ATOM   7268  C  C   . ASN B 1 301 ? -8.814  69.020  60.464  1.00 44.89  ? 310  ASN B C   1 
ATOM   7269  O  O   . ASN B 1 301 ? -7.777  68.968  61.131  1.00 40.82  ? 310  ASN B O   1 
ATOM   7270  C  CB  . ASN B 1 301 ? -11.025 69.815  61.342  1.00 48.34  ? 310  ASN B CB  1 
ATOM   7271  C  CG  . ASN B 1 301 ? -11.781 71.034  61.869  1.00 54.70  ? 310  ASN B CG  1 
ATOM   7272  O  OD1 . ASN B 1 301 ? -12.939 70.907  62.256  1.00 57.04  ? 310  ASN B OD1 1 
ATOM   7273  N  ND2 . ASN B 1 301 ? -11.205 72.239  61.910  1.00 53.61  ? 310  ASN B ND2 1 
ATOM   7274  N  N   . TRP B 1 302 ? -9.126  68.076  59.567  1.00 40.52  ? 311  TRP B N   1 
ATOM   7275  C  CA  . TRP B 1 302 ? -8.242  66.927  59.356  1.00 38.86  ? 311  TRP B CA  1 
ATOM   7276  C  C   . TRP B 1 302 ? -6.905  67.378  58.747  1.00 39.43  ? 311  TRP B C   1 
ATOM   7277  O  O   . TRP B 1 302 ? -5.849  66.890  59.167  1.00 40.10  ? 311  TRP B O   1 
ATOM   7278  C  CB  . TRP B 1 302 ? -8.904  65.908  58.422  1.00 36.68  ? 311  TRP B CB  1 
ATOM   7279  C  CG  . TRP B 1 302 ? -8.103  64.674  58.189  1.00 35.20  ? 311  TRP B CG  1 
ATOM   7280  C  CD1 . TRP B 1 302 ? -7.962  63.622  59.026  1.00 39.38  ? 311  TRP B CD1 1 
ATOM   7281  C  CD2 . TRP B 1 302 ? -7.325  64.364  57.027  1.00 37.53  ? 311  TRP B CD2 1 
ATOM   7282  N  NE1 . TRP B 1 302 ? -7.141  62.672  58.474  1.00 44.39  ? 311  TRP B NE1 1 
ATOM   7283  C  CE2 . TRP B 1 302 ? -6.736  63.099  57.240  1.00 40.22  ? 311  TRP B CE2 1 
ATOM   7284  C  CE3 . TRP B 1 302 ? -7.065  65.036  55.822  1.00 38.42  ? 311  TRP B CE3 1 
ATOM   7285  C  CZ2 . TRP B 1 302 ? -5.902  62.490  56.299  1.00 40.10  ? 311  TRP B CZ2 1 
ATOM   7286  C  CZ3 . TRP B 1 302 ? -6.232  64.429  54.893  1.00 40.31  ? 311  TRP B CZ3 1 
ATOM   7287  C  CH2 . TRP B 1 302 ? -5.660  63.170  55.137  1.00 36.25  ? 311  TRP B CH2 1 
ATOM   7288  N  N   . LEU B 1 303 ? -6.932  68.310  57.761  1.00 38.99  ? 312  LEU B N   1 
ATOM   7289  C  CA  . LEU B 1 303 ? -5.680  68.735  57.137  1.00 37.76  ? 312  LEU B CA  1 
ATOM   7290  C  C   . LEU B 1 303 ? -4.723  69.382  58.175  1.00 39.17  ? 312  LEU B C   1 
ATOM   7291  O  O   . LEU B 1 303 ? -3.526  69.101  58.136  1.00 40.35  ? 312  LEU B O   1 
ATOM   7292  C  CB  . LEU B 1 303 ? -5.949  69.682  55.969  1.00 38.63  ? 312  LEU B CB  1 
ATOM   7293  C  CG  . LEU B 1 303 ? -6.648  68.986  54.742  1.00 33.76  ? 312  LEU B CG  1 
ATOM   7294  C  CD1 . LEU B 1 303 ? -6.961  69.998  53.720  1.00 35.23  ? 312  LEU B CD1 1 
ATOM   7295  C  CD2 . LEU B 1 303 ? -5.773  67.931  54.131  1.00 35.28  ? 312  LEU B CD2 1 
ATOM   7296  N  N   . SER B 1 304 ? -5.249  70.209  59.070  1.00 44.32  ? 313  SER B N   1 
ATOM   7297  C  CA  . SER B 1 304 ? -4.476  70.846  60.154  1.00 51.99  ? 313  SER B CA  1 
ATOM   7298  C  C   . SER B 1 304 ? -3.561  69.859  60.934  1.00 52.31  ? 313  SER B C   1 
ATOM   7299  O  O   . SER B 1 304 ? -2.454  70.238  61.314  1.00 52.23  ? 313  SER B O   1 
ATOM   7300  C  CB  . SER B 1 304 ? -5.439  71.462  61.156  1.00 53.50  ? 313  SER B CB  1 
ATOM   7301  O  OG  . SER B 1 304 ? -6.102  72.566  60.564  1.00 55.70  ? 313  SER B OG  1 
ATOM   7302  N  N   . SER B 1 305 ? -3.998  68.623  61.151  1.00 50.76  ? 314  SER B N   1 
ATOM   7303  C  CA  . SER B 1 305 ? -3.241  67.612  61.906  1.00 51.04  ? 314  SER B CA  1 
ATOM   7304  C  C   . SER B 1 305 ? -2.233  66.825  61.104  1.00 50.84  ? 314  SER B C   1 
ATOM   7305  O  O   . SER B 1 305 ? -1.452  66.063  61.683  1.00 47.50  ? 314  SER B O   1 
ATOM   7306  C  CB  . SER B 1 305 ? -4.209  66.579  62.465  1.00 53.15  ? 314  SER B CB  1 
ATOM   7307  O  OG  . SER B 1 305 ? -4.469  65.559  61.504  1.00 58.05  ? 314  SER B OG  1 
ATOM   7308  N  N   . GLN B 1 306 ? -2.228  66.980  59.776  1.00 46.81  ? 315  GLN B N   1 
ATOM   7309  C  CA  . GLN B 1 306 ? -1.360  66.132  58.978  1.00 41.84  ? 315  GLN B CA  1 
ATOM   7310  C  C   . GLN B 1 306 ? 0.060   66.636  58.782  1.00 40.18  ? 315  GLN B C   1 
ATOM   7311  O  O   . GLN B 1 306 ? 0.853   65.890  58.181  1.00 41.94  ? 315  GLN B O   1 
ATOM   7312  C  CB  . GLN B 1 306 ? -2.021  65.922  57.602  1.00 41.94  ? 315  GLN B CB  1 
ATOM   7313  C  CG  . GLN B 1 306 ? -3.253  65.051  57.679  1.00 43.45  ? 315  GLN B CG  1 
ATOM   7314  C  CD  . GLN B 1 306 ? -2.934  63.648  58.127  1.00 45.11  ? 315  GLN B CD  1 
ATOM   7315  O  OE1 . GLN B 1 306 ? -3.618  63.104  58.987  1.00 47.82  ? 315  GLN B OE1 1 
ATOM   7316  N  NE2 . GLN B 1 306 ? -1.903  63.037  57.559  1.00 43.27  ? 315  GLN B NE2 1 
ATOM   7317  N  N   . GLY B 1 307 ? 0.414   67.848  59.240  1.00 37.75  ? 316  GLY B N   1 
ATOM   7318  C  CA  . GLY B 1 307 ? 1.790   68.310  59.061  1.00 36.14  ? 316  GLY B CA  1 
ATOM   7319  C  C   . GLY B 1 307 ? 2.133   68.285  57.584  1.00 38.61  ? 316  GLY B C   1 
ATOM   7320  O  O   . GLY B 1 307 ? 3.145   67.715  57.167  1.00 39.72  ? 316  GLY B O   1 
ATOM   7321  N  N   . LEU B 1 308 ? 1.249   68.865  56.775  1.00 38.99  ? 317  LEU B N   1 
ATOM   7322  C  CA  . LEU B 1 308 ? 1.440   68.905  55.317  1.00 38.74  ? 317  LEU B CA  1 
ATOM   7323  C  C   . LEU B 1 308 ? 2.733   69.602  54.911  1.00 37.58  ? 317  LEU B C   1 
ATOM   7324  O  O   . LEU B 1 308 ? 3.008   70.718  55.367  1.00 35.68  ? 317  LEU B O   1 
ATOM   7325  C  CB  . LEU B 1 308 ? 0.271   69.683  54.669  1.00 37.05  ? 317  LEU B CB  1 
ATOM   7326  C  CG  . LEU B 1 308 ? -1.077  68.996  54.877  1.00 33.61  ? 317  LEU B CG  1 
ATOM   7327  C  CD1 . LEU B 1 308 ? -2.132  69.817  54.251  1.00 35.72  ? 317  LEU B CD1 1 
ATOM   7328  C  CD2 . LEU B 1 308 ? -1.011  67.581  54.305  1.00 31.67  ? 317  LEU B CD2 1 
ATOM   7329  N  N   . GLU B 1 309 ? 3.520   68.938  54.084  1.00 36.01  ? 318  GLU B N   1 
ATOM   7330  C  CA  . GLU B 1 309 ? 4.725   69.542  53.547  1.00 40.51  ? 318  GLU B CA  1 
ATOM   7331  C  C   . GLU B 1 309 ? 4.366   70.446  52.374  1.00 42.61  ? 318  GLU B C   1 
ATOM   7332  O  O   . GLU B 1 309 ? 4.962   71.507  52.218  1.00 39.83  ? 318  GLU B O   1 
ATOM   7333  C  CB  . GLU B 1 309 ? 5.690   68.445  53.079  1.00 45.73  ? 318  GLU B CB  1 
ATOM   7334  C  CG  . GLU B 1 309 ? 6.236   67.682  54.282  1.00 58.53  ? 318  GLU B CG  1 
ATOM   7335  C  CD  . GLU B 1 309 ? 6.861   66.331  53.913  1.00 67.21  ? 318  GLU B CD  1 
ATOM   7336  O  OE1 . GLU B 1 309 ? 7.143   65.557  54.854  1.00 69.59  ? 318  GLU B OE1 1 
ATOM   7337  O  OE2 . GLU B 1 309 ? 7.067   66.040  52.713  1.00 68.21  ? 318  GLU B OE2 1 
ATOM   7338  N  N   . GLU B 1 310 ? 3.362   70.029  51.535  1.00 38.58  ? 319  GLU B N   1 
ATOM   7339  C  CA  . GLU B 1 310 ? 3.009   70.805  50.347  1.00 35.62  ? 319  GLU B CA  1 
ATOM   7340  C  C   . GLU B 1 310 ? 1.532   70.830  50.005  1.00 34.45  ? 319  GLU B C   1 
ATOM   7341  O  O   . GLU B 1 310 ? 0.802   69.863  50.247  1.00 32.45  ? 319  GLU B O   1 
ATOM   7342  C  CB  . GLU B 1 310 ? 3.711   70.214  49.128  1.00 37.51  ? 319  GLU B CB  1 
ATOM   7343  C  CG  . GLU B 1 310 ? 5.231   70.200  49.240  1.00 44.93  ? 319  GLU B CG  1 
ATOM   7344  C  CD  . GLU B 1 310 ? 5.852   69.293  48.222  1.00 56.72  ? 319  GLU B CD  1 
ATOM   7345  O  OE1 . GLU B 1 310 ? 6.488   68.300  48.604  1.00 64.25  ? 319  GLU B OE1 1 
ATOM   7346  O  OE2 . GLU B 1 310 ? 5.705   69.567  47.026  1.00 60.19  ? 319  GLU B OE2 1 
ATOM   7347  N  N   . ALA B 1 311 ? 1.090   71.934  49.456  1.00 32.81  ? 320  ALA B N   1 
ATOM   7348  C  CA  . ALA B 1 311 ? -0.281  72.043  48.979  1.00 31.87  ? 320  ALA B CA  1 
ATOM   7349  C  C   . ALA B 1 311 ? -0.220  72.732  47.608  1.00 32.60  ? 320  ALA B C   1 
ATOM   7350  O  O   . ALA B 1 311 ? 0.523   73.707  47.452  1.00 33.11  ? 320  ALA B O   1 
ATOM   7351  C  CB  . ALA B 1 311 ? -1.146  72.853  49.944  1.00 31.22  ? 320  ALA B CB  1 
ATOM   7352  N  N   . TYR B 1 312 ? -0.968  72.216  46.621  1.00 30.57  ? 321  TYR B N   1 
ATOM   7353  C  CA  . TYR B 1 312 ? -1.072  72.788  45.266  1.00 28.22  ? 321  TYR B CA  1 
ATOM   7354  C  C   . TYR B 1 312 ? -2.517  73.143  45.014  1.00 28.02  ? 321  TYR B C   1 
ATOM   7355  O  O   . TYR B 1 312 ? -3.414  72.438  45.496  1.00 25.65  ? 321  TYR B O   1 
ATOM   7356  C  CB  . TYR B 1 312 ? -0.620  71.773  44.219  1.00 24.93  ? 321  TYR B CB  1 
ATOM   7357  C  CG  . TYR B 1 312 ? 0.853   71.492  44.363  1.00 28.79  ? 321  TYR B CG  1 
ATOM   7358  C  CD1 . TYR B 1 312 ? 1.306   70.417  45.132  1.00 32.03  ? 321  TYR B CD1 1 
ATOM   7359  C  CD2 . TYR B 1 312 ? 1.799   72.321  43.777  1.00 27.66  ? 321  TYR B CD2 1 
ATOM   7360  C  CE1 . TYR B 1 312 ? 2.668   70.183  45.308  1.00 34.98  ? 321  TYR B CE1 1 
ATOM   7361  C  CE2 . TYR B 1 312 ? 3.159   72.100  43.955  1.00 32.26  ? 321  TYR B CE2 1 
ATOM   7362  C  CZ  . TYR B 1 312 ? 3.590   71.037  44.718  1.00 39.63  ? 321  TYR B CZ  1 
ATOM   7363  O  OH  . TYR B 1 312 ? 4.947   70.862  44.864  1.00 42.43  ? 321  TYR B OH  1 
ATOM   7364  N  N   . TYR B 1 313 ? -2.757  74.198  44.253  1.00 24.52  ? 322  TYR B N   1 
ATOM   7365  C  CA  . TYR B 1 313 ? -4.099  74.637  43.954  1.00 22.13  ? 322  TYR B CA  1 
ATOM   7366  C  C   . TYR B 1 313 ? -4.286  74.510  42.436  1.00 27.16  ? 322  TYR B C   1 
ATOM   7367  O  O   . TYR B 1 313 ? -3.611  75.211  41.688  1.00 25.93  ? 322  TYR B O   1 
ATOM   7368  C  CB  . TYR B 1 313 ? -4.288  76.098  44.390  1.00 24.13  ? 322  TYR B CB  1 
ATOM   7369  C  CG  . TYR B 1 313 ? -3.801  76.288  45.804  1.00 29.27  ? 322  TYR B CG  1 
ATOM   7370  C  CD1 . TYR B 1 313 ? -4.634  76.028  46.879  1.00 30.11  ? 322  TYR B CD1 1 
ATOM   7371  C  CD2 . TYR B 1 313 ? -2.501  76.730  46.067  1.00 30.49  ? 322  TYR B CD2 1 
ATOM   7372  C  CE1 . TYR B 1 313 ? -4.193  76.199  48.192  1.00 35.36  ? 322  TYR B CE1 1 
ATOM   7373  C  CE2 . TYR B 1 313 ? -2.047  76.899  47.378  1.00 34.26  ? 322  TYR B CE2 1 
ATOM   7374  C  CZ  . TYR B 1 313 ? -2.898  76.626  48.434  1.00 32.88  ? 322  TYR B CZ  1 
ATOM   7375  O  OH  . TYR B 1 313 ? -2.490  76.750  49.743  1.00 36.25  ? 322  TYR B OH  1 
ATOM   7376  N  N   . ILE B 1 314 ? -5.162  73.606  41.996  1.00 26.13  ? 323  ILE B N   1 
ATOM   7377  C  CA  . ILE B 1 314 ? -5.404  73.421  40.553  1.00 27.30  ? 323  ILE B CA  1 
ATOM   7378  C  C   . ILE B 1 314 ? -6.668  74.193  40.215  1.00 28.47  ? 323  ILE B C   1 
ATOM   7379  O  O   . ILE B 1 314 ? -7.796  73.824  40.610  1.00 27.27  ? 323  ILE B O   1 
ATOM   7380  C  CB  . ILE B 1 314 ? -5.536  71.907  40.227  1.00 26.43  ? 323  ILE B CB  1 
ATOM   7381  C  CG1 . ILE B 1 314 ? -4.444  71.063  40.921  1.00 24.85  ? 323  ILE B CG1 1 
ATOM   7382  C  CG2 . ILE B 1 314 ? -5.444  71.737  38.677  1.00 24.43  ? 323  ILE B CG2 1 
ATOM   7383  C  CD1 . ILE B 1 314 ? -2.992  71.542  40.652  1.00 23.07  ? 323  ILE B CD1 1 
ATOM   7384  N  N   . GLY B 1 315 ? -6.520  75.307  39.506  1.00 28.22  ? 324  GLY B N   1 
ATOM   7385  C  CA  . GLY B 1 315 ? -7.697  76.117  39.198  1.00 28.50  ? 324  GLY B CA  1 
ATOM   7386  C  C   . GLY B 1 315 ? -7.294  77.580  39.254  1.00 33.16  ? 324  GLY B C   1 
ATOM   7387  O  O   . GLY B 1 315 ? -6.281  77.922  39.888  1.00 34.53  ? 324  GLY B O   1 
ATOM   7388  N  N   . GLY B 1 316 ? -8.079  78.448  38.610  1.00 34.75  ? 325  GLY B N   1 
ATOM   7389  C  CA  . GLY B 1 316 ? -7.770  79.870  38.618  1.00 39.33  ? 325  GLY B CA  1 
ATOM   7390  C  C   . GLY B 1 316 ? -8.512  80.546  39.741  1.00 43.82  ? 325  GLY B C   1 
ATOM   7391  O  O   . GLY B 1 316 ? -9.272  79.897  40.481  1.00 39.96  ? 325  GLY B O   1 
ATOM   7392  N  N   . SER B 1 317 ? -8.334  81.879  39.868  1.00 39.04  ? 326  SER B N   1 
ATOM   7393  C  CA  . SER B 1 317 ? -8.962  82.586  40.983  1.00 42.60  ? 326  SER B CA  1 
ATOM   7394  C  C   . SER B 1 317 ? -10.486 82.526  40.930  1.00 42.68  ? 326  SER B C   1 
ATOM   7395  O  O   . SER B 1 317 ? -11.129 82.680  41.957  1.00 47.95  ? 326  SER B O   1 
ATOM   7396  C  CB  . SER B 1 317 ? -8.488  84.038  41.028  1.00 45.12  ? 326  SER B CB  1 
ATOM   7397  O  OG  . SER B 1 317 ? -8.623  84.584  39.722  1.00 50.89  ? 326  SER B OG  1 
ATOM   7398  N  N   . GLN B 1 318 ? -11.060 82.307  39.796  1.00 44.92  ? 327  GLN B N   1 
ATOM   7399  C  CA  . GLN B 1 318 ? -12.516 82.201  39.737  1.00 47.12  ? 327  GLN B CA  1 
ATOM   7400  C  C   . GLN B 1 318 ? -12.996 80.889  40.424  1.00 47.35  ? 327  GLN B C   1 
ATOM   7401  O  O   . GLN B 1 318 ? -14.122 80.850  40.898  1.00 45.97  ? 327  GLN B O   1 
ATOM   7402  C  CB  . GLN B 1 318 ? -12.995 82.194  38.267  1.00 50.64  ? 327  GLN B CB  1 
ATOM   7403  C  CG  . GLN B 1 318 ? -12.678 80.875  37.524  1.00 53.85  ? 327  GLN B CG  1 
ATOM   7404  C  CD  . GLN B 1 318 ? -11.237 80.811  37.025  1.00 57.88  ? 327  GLN B CD  1 
ATOM   7405  O  OE1 . GLN B 1 318 ? -10.392 81.644  37.383  1.00 59.25  ? 327  GLN B OE1 1 
ATOM   7406  N  NE2 . GLN B 1 318 ? -10.911 79.794  36.189  1.00 61.65  ? 327  GLN B NE2 1 
ATOM   7407  N  N   . SER B 1 319 ? -12.133 79.835  40.464  1.00 44.95  ? 328  SER B N   1 
ATOM   7408  C  CA  . SER B 1 319 ? -12.460 78.533  41.068  1.00 42.89  ? 328  SER B CA  1 
ATOM   7409  C  C   . SER B 1 319 ? -11.912 78.383  42.491  1.00 41.48  ? 328  SER B C   1 
ATOM   7410  O  O   . SER B 1 319 ? -12.580 77.813  43.360  1.00 37.51  ? 328  SER B O   1 
ATOM   7411  C  CB  . SER B 1 319 ? -11.880 77.421  40.208  1.00 42.27  ? 328  SER B CB  1 
ATOM   7412  O  OG  . SER B 1 319 ? -12.522 77.417  38.946  1.00 46.75  ? 328  SER B OG  1 
ATOM   7413  N  N   . LEU B 1 320 ? -10.687 78.895  42.727  1.00 37.16  ? 329  LEU B N   1 
ATOM   7414  C  CA  . LEU B 1 320 ? -10.049 78.824  44.022  1.00 32.57  ? 329  LEU B CA  1 
ATOM   7415  C  C   . LEU B 1 320 ? -9.480  80.254  44.264  1.00 38.36  ? 329  LEU B C   1 
ATOM   7416  O  O   . LEU B 1 320 ? -8.458  80.626  43.678  1.00 40.06  ? 329  LEU B O   1 
ATOM   7417  C  CB  . LEU B 1 320 ? -8.889  77.771  44.032  1.00 29.59  ? 329  LEU B CB  1 
ATOM   7418  C  CG  . LEU B 1 320 ? -9.358  76.302  43.742  1.00 27.58  ? 329  LEU B CG  1 
ATOM   7419  C  CD1 . LEU B 1 320 ? -8.144  75.386  43.625  1.00 26.84  ? 329  LEU B CD1 1 
ATOM   7420  C  CD2 . LEU B 1 320 ? -10.298 75.864  44.886  1.00 27.34  ? 329  LEU B CD2 1 
ATOM   7421  N  N   . SER B 1 321 ? -10.162 81.035  45.108  1.00 40.09  ? 330  SER B N   1 
ATOM   7422  C  CA  . SER B 1 321 ? -9.762  82.413  45.399  1.00 41.72  ? 330  SER B CA  1 
ATOM   7423  C  C   . SER B 1 321 ? -8.549  82.449  46.312  1.00 42.05  ? 330  SER B C   1 
ATOM   7424  O  O   . SER B 1 321 ? -8.144  81.436  46.869  1.00 40.57  ? 330  SER B O   1 
ATOM   7425  C  CB  . SER B 1 321 ? -10.903 83.142  46.096  1.00 40.16  ? 330  SER B CB  1 
ATOM   7426  O  OG  . SER B 1 321 ? -10.923 82.745  47.463  1.00 39.96  ? 330  SER B OG  1 
ATOM   7427  N  N   . SER B 1 322 ? -7.978  83.645  46.488  1.00 41.51  ? 331  SER B N   1 
ATOM   7428  C  CA  . SER B 1 322 ? -6.832  83.823  47.348  1.00 41.67  ? 331  SER B CA  1 
ATOM   7429  C  C   . SER B 1 322 ? -7.184  83.469  48.788  1.00 42.75  ? 331  SER B C   1 
ATOM   7430  O  O   . SER B 1 322 ? -6.291  83.183  49.581  1.00 41.94  ? 331  SER B O   1 
ATOM   7431  C  CB  . SER B 1 322 ? -6.356  85.281  47.287  1.00 44.89  ? 331  SER B CB  1 
ATOM   7432  O  OG  . SER B 1 322 ? -7.364  86.168  47.740  1.00 46.42  ? 331  SER B OG  1 
ATOM   7433  N  N   . LYS B 1 323 ? -8.477  83.491  49.130  1.00 41.59  ? 332  LYS B N   1 
ATOM   7434  C  CA  . LYS B 1 323 ? -8.922  83.167  50.482  1.00 43.25  ? 332  LYS B CA  1 
ATOM   7435  C  C   . LYS B 1 323 ? -8.611  81.688  50.800  1.00 44.90  ? 332  LYS B C   1 
ATOM   7436  O  O   . LYS B 1 323 ? -8.220  81.378  51.918  1.00 42.43  ? 332  LYS B O   1 
ATOM   7437  C  CB  . LYS B 1 323 ? -10.425 83.457  50.627  1.00 45.74  ? 332  LYS B CB  1 
ATOM   7438  C  CG  . LYS B 1 323 ? -10.733 84.952  50.638  1.00 53.24  ? 332  LYS B CG  1 
ATOM   7439  C  CD  . LYS B 1 323 ? -12.115 85.220  51.216  1.00 60.14  ? 332  LYS B CD  1 
ATOM   7440  C  CE  . LYS B 1 323 ? -12.750 86.462  50.613  1.00 65.45  ? 332  LYS B CE  1 
ATOM   7441  N  NZ  . LYS B 1 323 ? -14.218 86.266  50.356  1.00 73.12  ? 332  LYS B NZ  1 
ATOM   7442  N  N   . ILE B 1 324 ? -8.750  80.762  49.808  1.00 44.17  ? 333  ILE B N   1 
ATOM   7443  C  CA  . ILE B 1 324 ? -8.420  79.374  50.133  1.00 40.83  ? 333  ILE B CA  1 
ATOM   7444  C  C   . ILE B 1 324 ? -6.923  79.223  50.219  1.00 37.53  ? 333  ILE B C   1 
ATOM   7445  O  O   . ILE B 1 324 ? -6.419  78.447  51.035  1.00 35.01  ? 333  ILE B O   1 
ATOM   7446  C  CB  . ILE B 1 324 ? -9.064  78.383  49.114  1.00 43.01  ? 333  ILE B CB  1 
ATOM   7447  C  CG1 . ILE B 1 324 ? -8.999  76.971  49.695  1.00 45.60  ? 333  ILE B CG1 1 
ATOM   7448  C  CG2 . ILE B 1 324 ? -8.358  78.419  47.764  1.00 42.32  ? 333  ILE B CG2 1 
ATOM   7449  C  CD1 . ILE B 1 324 ? -9.895  76.030  48.916  1.00 48.52  ? 333  ILE B CD1 1 
ATOM   7450  N  N   . ILE B 1 325 ? -6.173  79.976  49.390  1.00 36.80  ? 334  ILE B N   1 
ATOM   7451  C  CA  . ILE B 1 325 ? -4.719  79.883  49.467  1.00 38.76  ? 334  ILE B CA  1 
ATOM   7452  C  C   . ILE B 1 325 ? -4.267  80.415  50.863  1.00 40.81  ? 334  ILE B C   1 
ATOM   7453  O  O   . ILE B 1 325 ? -3.381  79.841  51.493  1.00 39.82  ? 334  ILE B O   1 
ATOM   7454  C  CB  . ILE B 1 325 ? -4.069  80.711  48.335  1.00 40.44  ? 334  ILE B CB  1 
ATOM   7455  C  CG1 . ILE B 1 325 ? -4.438  80.070  46.955  1.00 38.66  ? 334  ILE B CG1 1 
ATOM   7456  C  CG2 . ILE B 1 325 ? -2.561  80.789  48.583  1.00 34.18  ? 334  ILE B CG2 1 
ATOM   7457  C  CD1 . ILE B 1 325 ? -3.490  80.458  45.821  1.00 41.56  ? 334  ILE B CD1 1 
ATOM   7458  N  N   . ASP B 1 326 ? -4.891  81.499  51.317  1.00 42.16  ? 335  ASP B N   1 
ATOM   7459  C  CA  . ASP B 1 326 ? -4.581  82.079  52.622  1.00 45.41  ? 335  ASP B CA  1 
ATOM   7460  C  C   . ASP B 1 326 ? -4.844  81.026  53.712  1.00 44.78  ? 335  ASP B C   1 
ATOM   7461  O  O   . ASP B 1 326 ? -4.013  80.808  54.590  1.00 43.63  ? 335  ASP B O   1 
ATOM   7462  C  CB  . ASP B 1 326 ? -5.459  83.326  52.845  1.00 48.19  ? 335  ASP B CB  1 
ATOM   7463  C  CG  . ASP B 1 326 ? -4.934  84.560  52.119  1.00 54.65  ? 335  ASP B CG  1 
ATOM   7464  O  OD1 . ASP B 1 326 ? -3.740  84.558  51.732  1.00 58.40  ? 335  ASP B OD1 1 
ATOM   7465  O  OD2 . ASP B 1 326 ? -5.720  85.522  51.932  1.00 58.29  ? 335  ASP B OD2 1 
ATOM   7466  N  N   . GLN B 1 327 ? -5.984  80.339  53.629  1.00 43.05  ? 336  GLN B N   1 
ATOM   7467  C  CA  . GLN B 1 327 ? -6.356  79.330  54.624  1.00 42.38  ? 336  GLN B CA  1 
ATOM   7468  C  C   . GLN B 1 327 ? -5.409  78.134  54.698  1.00 42.19  ? 336  GLN B C   1 
ATOM   7469  O  O   . GLN B 1 327 ? -5.024  77.721  55.777  1.00 41.54  ? 336  GLN B O   1 
ATOM   7470  C  CB  . GLN B 1 327 ? -7.754  78.802  54.298  1.00 42.99  ? 336  GLN B CB  1 
ATOM   7471  C  CG  . GLN B 1 327 ? -8.211  77.693  55.222  1.00 44.92  ? 336  GLN B CG  1 
ATOM   7472  C  CD  . GLN B 1 327 ? -9.495  77.100  54.683  1.00 53.80  ? 336  GLN B CD  1 
ATOM   7473  O  OE1 . GLN B 1 327 ? -9.648  76.852  53.477  1.00 53.96  ? 336  GLN B OE1 1 
ATOM   7474  N  NE2 . GLN B 1 327 ? -10.463 76.879  55.562  1.00 57.33  ? 336  GLN B NE2 1 
ATOM   7475  N  N   . ILE B 1 328 ? -5.057  77.559  53.553  1.00 39.47  ? 337  ILE B N   1 
ATOM   7476  C  CA  . ILE B 1 328 ? -4.222  76.368  53.526  1.00 36.96  ? 337  ILE B CA  1 
ATOM   7477  C  C   . ILE B 1 328 ? -2.738  76.680  53.673  1.00 34.97  ? 337  ILE B C   1 
ATOM   7478  O  O   . ILE B 1 328 ? -1.998  75.836  54.170  1.00 35.08  ? 337  ILE B O   1 
ATOM   7479  C  CB  . ILE B 1 328 ? -4.524  75.629  52.184  1.00 33.99  ? 337  ILE B CB  1 
ATOM   7480  C  CG1 . ILE B 1 328 ? -6.015  75.250  52.167  1.00 32.62  ? 337  ILE B CG1 1 
ATOM   7481  C  CG2 . ILE B 1 328 ? -3.601  74.425  52.012  1.00 31.26  ? 337  ILE B CG2 1 
ATOM   7482  C  CD1 . ILE B 1 328 ? -6.482  74.242  53.254  1.00 32.47  ? 337  ILE B CD1 1 
ATOM   7483  N  N   . SER B 1 329 ? -2.308  77.876  53.216  1.00 36.57  ? 338  SER B N   1 
ATOM   7484  C  CA  . SER B 1 329 ? -0.926  78.319  53.345  1.00 38.28  ? 338  SER B CA  1 
ATOM   7485  C  C   . SER B 1 329 ? -0.514  78.240  54.843  1.00 40.05  ? 338  SER B C   1 
ATOM   7486  O  O   . SER B 1 329 ? 0.606   77.841  55.144  1.00 39.86  ? 338  SER B O   1 
ATOM   7487  C  CB  . SER B 1 329 ? -0.781  79.772  52.897  1.00 41.51  ? 338  SER B CB  1 
ATOM   7488  O  OG  . SER B 1 329 ? 0.578   79.963  52.537  1.00 47.53  ? 338  SER B OG  1 
ATOM   7489  N  N   . LYS B 1 330 ? -1.445  78.600  55.742  1.00 39.86  ? 339  LYS B N   1 
ATOM   7490  C  CA  . LYS B 1 330 ? -1.231  78.539  57.202  1.00 46.95  ? 339  LYS B CA  1 
ATOM   7491  C  C   . LYS B 1 330 ? -0.876  77.142  57.631  1.00 48.68  ? 339  LYS B C   1 
ATOM   7492  O  O   . LYS B 1 330 ? -0.105  76.992  58.564  1.00 49.09  ? 339  LYS B O   1 
ATOM   7493  C  CB  . LYS B 1 330 ? -2.511  78.913  58.000  1.00 47.66  ? 339  LYS B CB  1 
ATOM   7494  C  CG  . LYS B 1 330 ? -3.083  80.306  57.766  1.00 55.07  ? 339  LYS B CG  1 
ATOM   7495  C  CD  . LYS B 1 330 ? -4.238  80.596  58.822  1.00 62.22  ? 339  LYS B CD  1 
ATOM   7496  C  CE  . LYS B 1 330 ? -5.588  80.945  58.193  1.00 62.75  ? 339  LYS B CE  1 
ATOM   7497  N  NZ  . LYS B 1 330 ? -6.528  79.766  58.163  1.00 63.17  ? 339  LYS B NZ  1 
ATOM   7498  N  N   . ILE B 1 331 ? -1.436  76.089  56.973  1.00 47.83  ? 340  ILE B N   1 
ATOM   7499  C  CA  . ILE B 1 331 ? -1.165  74.724  57.437  1.00 45.55  ? 340  ILE B CA  1 
ATOM   7500  C  C   . ILE B 1 331 ? -0.325  73.847  56.538  1.00 45.64  ? 340  ILE B C   1 
ATOM   7501  O  O   . ILE B 1 331 ? -0.374  72.630  56.661  1.00 45.87  ? 340  ILE B O   1 
ATOM   7502  C  CB  . ILE B 1 331 ? -2.507  74.053  57.751  1.00 45.80  ? 340  ILE B CB  1 
ATOM   7503  C  CG1 . ILE B 1 331 ? -3.392  73.990  56.466  1.00 43.02  ? 340  ILE B CG1 1 
ATOM   7504  C  CG2 . ILE B 1 331 ? -3.230  74.848  58.866  1.00 44.20  ? 340  ILE B CG2 1 
ATOM   7505  C  CD1 . ILE B 1 331 ? -4.614  73.113  56.682  1.00 46.90  ? 340  ILE B CD1 1 
ATOM   7506  N  N   . ALA B 1 332 ? 0.460   74.422  55.646  1.00 44.36  ? 341  ALA B N   1 
ATOM   7507  C  CA  . ALA B 1 332 ? 1.324   73.608  54.804  1.00 39.33  ? 341  ALA B CA  1 
ATOM   7508  C  C   . ALA B 1 332 ? 2.674   74.291  54.736  1.00 41.17  ? 341  ALA B C   1 
ATOM   7509  O  O   . ALA B 1 332 ? 2.721   75.515  54.589  1.00 41.74  ? 341  ALA B O   1 
ATOM   7510  C  CB  . ALA B 1 332 ? 0.730   73.477  53.389  1.00 38.64  ? 341  ALA B CB  1 
ATOM   7511  N  N   . LYS B 1 333 ? 3.770   73.530  54.847  1.00 42.87  ? 342  LYS B N   1 
ATOM   7512  C  CA  . LYS B 1 333 ? 5.094   74.142  54.803  1.00 46.43  ? 342  LYS B CA  1 
ATOM   7513  C  C   . LYS B 1 333 ? 5.246   74.923  53.501  1.00 49.50  ? 342  LYS B C   1 
ATOM   7514  O  O   . LYS B 1 333 ? 5.761   76.034  53.515  1.00 48.92  ? 342  LYS B O   1 
ATOM   7515  C  CB  . LYS B 1 333 ? 6.182   73.075  54.892  1.00 49.00  ? 342  LYS B CB  1 
ATOM   7516  C  CG  . LYS B 1 333 ? 6.580   72.828  56.329  1.00 56.48  ? 342  LYS B CG  1 
ATOM   7517  C  CD  . LYS B 1 333 ? 6.377   71.414  56.715  1.00 61.65  ? 342  LYS B CD  1 
ATOM   7518  C  CE  . LYS B 1 333 ? 7.605   70.851  57.402  1.00 65.63  ? 342  LYS B CE  1 
ATOM   7519  N  NZ  . LYS B 1 333 ? 8.660   70.479  56.430  0.00 0.00   ? 342  LYS B NZ  1 
ATOM   7520  N  N   . ASN B 1 334 ? 4.795   74.347  52.374  1.00 44.66  ? 343  ASN B N   1 
ATOM   7521  C  CA  . ASN B 1 334 ? 4.885   75.036  51.102  1.00 40.56  ? 343  ASN B CA  1 
ATOM   7522  C  C   . ASN B 1 334 ? 3.497   75.044  50.434  1.00 39.31  ? 343  ASN B C   1 
ATOM   7523  O  O   . ASN B 1 334 ? 3.149   74.092  49.731  1.00 34.64  ? 343  ASN B O   1 
ATOM   7524  C  CB  . ASN B 1 334 ? 5.912   74.347  50.263  1.00 42.27  ? 343  ASN B CB  1 
ATOM   7525  C  CG  . ASN B 1 334 ? 7.298   74.608  50.822  1.00 56.21  ? 343  ASN B CG  1 
ATOM   7526  O  OD1 . ASN B 1 334 ? 7.795   75.751  50.778  1.00 61.47  ? 343  ASN B OD1 1 
ATOM   7527  N  ND2 . ASN B 1 334 ? 7.997   73.609  51.385  1.00 63.49  ? 343  ASN B ND2 1 
ATOM   7528  N  N   . GLY B 1 335 ? 2.733   76.105  50.670  1.00 35.08  ? 344  GLY B N   1 
ATOM   7529  C  CA  . GLY B 1 335 ? 1.379   76.218  50.152  1.00 36.02  ? 344  GLY B CA  1 
ATOM   7530  C  C   . GLY B 1 335 ? 0.990   77.622  49.755  1.00 35.38  ? 344  GLY B C   1 
ATOM   7531  O  O   . GLY B 1 335 ? -0.160  78.022  49.932  1.00 36.90  ? 344  GLY B O   1 
ATOM   7532  N  N   . THR B 1 336 ? 1.943   78.391  49.218  1.00 35.95  ? 345  THR B N   1 
ATOM   7533  C  CA  . THR B 1 336 ? 1.659   79.782  48.810  1.00 38.11  ? 345  THR B CA  1 
ATOM   7534  C  C   . THR B 1 336 ? 1.122   79.790  47.382  1.00 40.31  ? 345  THR B C   1 
ATOM   7535  O  O   . THR B 1 336 ? 1.085   78.722  46.747  1.00 39.50  ? 345  THR B O   1 
ATOM   7536  C  CB  . THR B 1 336 ? 2.960   80.634  48.841  1.00 39.82  ? 345  THR B CB  1 
ATOM   7537  O  OG1 . THR B 1 336 ? 3.822   80.193  47.797  1.00 39.42  ? 345  THR B OG1 1 
ATOM   7538  C  CG2 . THR B 1 336 ? 3.727   80.484  50.152  1.00 40.34  ? 345  THR B CG2 1 
ATOM   7539  N  N   . SER B 1 337 ? 0.726   80.985  46.872  1.00 42.58  ? 346  SER B N   1 
ATOM   7540  C  CA  . SER B 1 337 ? 0.193   81.166  45.516  1.00 41.12  ? 346  SER B CA  1 
ATOM   7541  C  C   . SER B 1 337 ? 1.159   80.685  44.462  1.00 42.15  ? 346  SER B C   1 
ATOM   7542  O  O   . SER B 1 337 ? 0.759   80.525  43.313  1.00 42.01  ? 346  SER B O   1 
ATOM   7543  C  CB  . SER B 1 337 ? -0.141  82.633  45.269  1.00 42.51  ? 346  SER B CB  1 
ATOM   7544  O  OG  . SER B 1 337 ? 1.038   83.380  45.474  1.00 46.15  ? 346  SER B OG  1 
ATOM   7545  N  N   . LYS B 1 338 ? 2.422   80.423  44.815  1.00 39.45  ? 347  LYS B N   1 
ATOM   7546  C  CA  . LYS B 1 338 ? 3.357   79.924  43.827  1.00 42.59  ? 347  LYS B CA  1 
ATOM   7547  C  C   . LYS B 1 338 ? 2.958   78.515  43.386  1.00 43.39  ? 347  LYS B C   1 
ATOM   7548  O  O   . LYS B 1 338 ? 3.386   78.039  42.332  1.00 39.90  ? 347  LYS B O   1 
ATOM   7549  C  CB  . LYS B 1 338 ? 4.782   79.820  44.424  1.00 48.19  ? 347  LYS B CB  1 
ATOM   7550  C  CG  . LYS B 1 338 ? 5.352   81.174  44.839  1.00 57.47  ? 347  LYS B CG  1 
ATOM   7551  C  CD  . LYS B 1 338 ? 6.566   81.002  45.736  1.00 58.98  ? 347  LYS B CD  1 
ATOM   7552  C  CE  . LYS B 1 338 ? 6.492   81.960  46.898  0.00 0.00   ? 347  LYS B CE  1 
ATOM   7553  N  NZ  . LYS B 1 338 ? 7.584   81.720  47.876  0.00 0.00   ? 347  LYS B NZ  1 
ATOM   7554  N  N   . ASN B 1 339 ? 2.169   77.832  44.222  1.00 38.49  ? 348  ASN B N   1 
ATOM   7555  C  CA  . ASN B 1 339 ? 1.766   76.457  43.941  1.00 34.77  ? 348  ASN B CA  1 
ATOM   7556  C  C   . ASN B 1 339 ? 0.408   76.394  43.203  1.00 33.59  ? 348  ASN B C   1 
ATOM   7557  O  O   . ASN B 1 339 ? -0.218  75.325  43.151  1.00 31.15  ? 348  ASN B O   1 
ATOM   7558  C  CB  . ASN B 1 339 ? 1.688   75.710  45.279  1.00 33.10  ? 348  ASN B CB  1 
ATOM   7559  C  CG  . ASN B 1 339 ? 3.063   75.264  45.740  1.00 38.56  ? 348  ASN B CG  1 
ATOM   7560  O  OD1 . ASN B 1 339 ? 4.065   75.521  45.047  1.00 36.08  ? 348  ASN B OD1 1 
ATOM   7561  N  ND2 . ASN B 1 339 ? 3.189   74.552  46.852  1.00 33.68  ? 348  ASN B ND2 1 
ATOM   7562  N  N   . ARG B 1 340 ? -0.065  77.522  42.666  1.00 30.42  ? 349  ARG B N   1 
ATOM   7563  C  CA  . ARG B 1 340 ? -1.289  77.507  41.878  1.00 28.36  ? 349  ARG B CA  1 
ATOM   7564  C  C   . ARG B 1 340 ? -0.933  77.087  40.436  1.00 31.13  ? 349  ARG B C   1 
ATOM   7565  O  O   . ARG B 1 340 ? 0.070   77.546  39.905  1.00 28.36  ? 349  ARG B O   1 
ATOM   7566  C  CB  . ARG B 1 340 ? -1.928  78.901  41.812  1.00 27.84  ? 349  ARG B CB  1 
ATOM   7567  C  CG  . ARG B 1 340 ? -3.168  78.916  40.946  1.00 26.99  ? 349  ARG B CG  1 
ATOM   7568  C  CD  . ARG B 1 340 ? -3.776  80.319  40.752  1.00 30.28  ? 349  ARG B CD  1 
ATOM   7569  N  NE  . ARG B 1 340 ? -4.271  80.992  41.961  1.00 31.57  ? 349  ARG B NE  1 
ATOM   7570  C  CZ  . ARG B 1 340 ? -5.491  80.861  42.461  1.00 32.58  ? 349  ARG B CZ  1 
ATOM   7571  N  NH1 . ARG B 1 340 ? -6.362  80.032  41.899  1.00 36.16  ? 349  ARG B NH1 1 
ATOM   7572  N  NH2 . ARG B 1 340 ? -5.866  81.581  43.503  1.00 31.33  ? 349  ARG B NH2 1 
ATOM   7573  N  N   . VAL B 1 341 ? -1.715  76.204  39.827  1.00 28.29  ? 350  VAL B N   1 
ATOM   7574  C  CA  . VAL B 1 341 ? -1.479  75.774  38.444  1.00 25.39  ? 350  VAL B CA  1 
ATOM   7575  C  C   . VAL B 1 341 ? -2.827  76.104  37.812  1.00 28.73  ? 350  VAL B C   1 
ATOM   7576  O  O   . VAL B 1 341 ? -3.846  75.561  38.266  1.00 28.33  ? 350  VAL B O   1 
ATOM   7577  C  CB  . VAL B 1 341 ? -1.163  74.294  38.297  1.00 27.89  ? 350  VAL B CB  1 
ATOM   7578  C  CG1 . VAL B 1 341 ? -1.054  73.928  36.783  1.00 28.97  ? 350  VAL B CG1 1 
ATOM   7579  C  CG2 . VAL B 1 341 ? 0.126   73.959  39.014  1.00 26.55  ? 350  VAL B CG2 1 
ATOM   7580  N  N   . SER B 1 342 ? -2.900  77.005  36.830  1.00 27.64  ? 351  SER B N   1 
ATOM   7581  C  CA  . SER B 1 342 ? -4.240  77.289  36.331  1.00 26.73  ? 351  SER B CA  1 
ATOM   7582  C  C   . SER B 1 342 ? -4.222  77.263  34.829  1.00 28.29  ? 351  SER B C   1 
ATOM   7583  O  O   . SER B 1 342 ? -3.330  76.669  34.266  1.00 31.44  ? 351  SER B O   1 
ATOM   7584  C  CB  . SER B 1 342 ? -4.725  78.641  36.823  1.00 32.86  ? 351  SER B CB  1 
ATOM   7585  O  OG  . SER B 1 342 ? -3.740  79.629  36.570  1.00 39.97  ? 351  SER B OG  1 
ATOM   7586  N  N   . GLY B 1 343 ? -5.211  77.884  34.195  1.00 28.04  ? 352  GLY B N   1 
ATOM   7587  C  CA  . GLY B 1 343 ? -5.300  77.882  32.752  1.00 28.02  ? 352  GLY B CA  1 
ATOM   7588  C  C   . GLY B 1 343 ? -6.624  78.538  32.424  1.00 29.49  ? 352  GLY B C   1 
ATOM   7589  O  O   . GLY B 1 343 ? -7.527  78.608  33.252  1.00 28.64  ? 352  GLY B O   1 
ATOM   7590  N  N   . ALA B 1 344 ? -6.761  79.001  31.177  1.00 28.18  ? 353  ALA B N   1 
ATOM   7591  C  CA  . ALA B 1 344 ? -7.979  79.690  30.755  1.00 29.37  ? 353  ALA B CA  1 
ATOM   7592  C  C   . ALA B 1 344 ? -9.141  78.732  30.601  1.00 27.31  ? 353  ALA B C   1 
ATOM   7593  O  O   . ALA B 1 344 ? -10.289 79.151  30.646  1.00 24.61  ? 353  ALA B O   1 
ATOM   7594  C  CB  . ALA B 1 344 ? -7.713  80.384  29.419  1.00 30.16  ? 353  ALA B CB  1 
ATOM   7595  N  N   . ASP B 1 345 ? -8.847  77.434  30.368  1.00 24.79  ? 354  ASP B N   1 
ATOM   7596  C  CA  . ASP B 1 345 ? -9.910  76.443  30.236  1.00 19.32  ? 354  ASP B CA  1 
ATOM   7597  C  C   . ASP B 1 345 ? -9.282  75.062  30.574  1.00 18.85  ? 354  ASP B C   1 
ATOM   7598  O  O   . ASP B 1 345 ? -8.108  75.018  30.899  1.00 19.82  ? 354  ASP B O   1 
ATOM   7599  C  CB  . ASP B 1 345 ? -10.546 76.426  28.797  1.00 20.36  ? 354  ASP B CB  1 
ATOM   7600  C  CG  . ASP B 1 345 ? -9.583  76.154  27.665  1.00 25.90  ? 354  ASP B CG  1 
ATOM   7601  O  OD1 . ASP B 1 345 ? -8.570  75.459  27.893  1.00 25.32  ? 354  ASP B OD1 1 
ATOM   7602  O  OD2 . ASP B 1 345 ? -9.828  76.652  26.539  1.00 29.37  ? 354  ASP B OD2 1 
ATOM   7603  N  N   . ARG B 1 346 ? -10.060 73.959  30.461  1.00 20.84  ? 355  ARG B N   1 
ATOM   7604  C  CA  . ARG B 1 346 ? -9.552  72.623  30.838  1.00 21.62  ? 355  ARG B CA  1 
ATOM   7605  C  C   . ARG B 1 346 ? -8.324  72.219  30.029  1.00 23.12  ? 355  ARG B C   1 
ATOM   7606  O  O   . ARG B 1 346 ? -7.488  71.458  30.547  1.00 20.69  ? 355  ARG B O   1 
ATOM   7607  C  CB  . ARG B 1 346 ? -10.675 71.568  30.671  1.00 21.79  ? 355  ARG B CB  1 
ATOM   7608  C  CG  . ARG B 1 346 ? -11.069 71.296  29.181  1.00 19.47  ? 355  ARG B CG  1 
ATOM   7609  C  CD  . ARG B 1 346 ? -12.424 70.480  29.021  1.00 23.65  ? 355  ARG B CD  1 
ATOM   7610  N  NE  . ARG B 1 346 ? -13.550 71.273  29.508  1.00 30.29  ? 355  ARG B NE  1 
ATOM   7611  C  CZ  . ARG B 1 346 ? -14.821 70.903  29.392  1.00 32.08  ? 355  ARG B CZ  1 
ATOM   7612  N  NH1 . ARG B 1 346 ? -15.140 69.742  28.813  1.00 26.78  ? 355  ARG B NH1 1 
ATOM   7613  N  NH2 . ARG B 1 346 ? -15.784 71.685  29.850  1.00 31.31  ? 355  ARG B NH2 1 
ATOM   7614  N  N   . HIS B 1 347 ? -8.183  72.730  28.777  1.00 19.49  ? 356  HIS B N   1 
ATOM   7615  C  CA  . HIS B 1 347 ? -6.996  72.334  28.016  1.00 16.24  ? 356  HIS B CA  1 
ATOM   7616  C  C   . HIS B 1 347 ? -5.739  73.092  28.422  1.00 18.96  ? 356  HIS B C   1 
ATOM   7617  O  O   . HIS B 1 347 ? -4.656  72.475  28.515  1.00 19.54  ? 356  HIS B O   1 
ATOM   7618  C  CB  . HIS B 1 347 ? -7.258  72.501  26.507  1.00 19.82  ? 356  HIS B CB  1 
ATOM   7619  C  CG  . HIS B 1 347 ? -8.512  71.790  26.113  1.00 18.38  ? 356  HIS B CG  1 
ATOM   7620  N  ND1 . HIS B 1 347 ? -9.609  72.466  25.619  1.00 18.96  ? 356  HIS B ND1 1 
ATOM   7621  C  CD2 . HIS B 1 347 ? -8.857  70.481  26.166  1.00 17.23  ? 356  HIS B CD2 1 
ATOM   7622  C  CE1 . HIS B 1 347 ? -10.568 71.579  25.374  1.00 21.86  ? 356  HIS B CE1 1 
ATOM   7623  N  NE2 . HIS B 1 347 ? -10.140 70.377  25.694  1.00 20.95  ? 356  HIS B NE2 1 
ATOM   7624  N  N   . GLU B 1 348 ? -5.836  74.412  28.671  1.00 19.06  ? 357  GLU B N   1 
ATOM   7625  C  CA  . GLU B 1 348 ? -4.644  75.099  29.115  1.00 19.86  ? 357  GLU B CA  1 
ATOM   7626  C  C   . GLU B 1 348 ? -4.243  74.583  30.523  1.00 19.85  ? 357  GLU B C   1 
ATOM   7627  O  O   . GLU B 1 348 ? -3.059  74.427  30.817  1.00 21.92  ? 357  GLU B O   1 
ATOM   7628  C  CB  . GLU B 1 348 ? -4.869  76.609  29.174  1.00 20.15  ? 357  GLU B CB  1 
ATOM   7629  C  CG  . GLU B 1 348 ? -3.479  77.242  29.396  1.00 19.71  ? 357  GLU B CG  1 
ATOM   7630  C  CD  . GLU B 1 348 ? -3.511  78.792  29.424  1.00 23.38  ? 357  GLU B CD  1 
ATOM   7631  O  OE1 . GLU B 1 348 ? -4.523  79.392  29.734  1.00 24.74  ? 357  GLU B OE1 1 
ATOM   7632  O  OE2 . GLU B 1 348 ? -2.474  79.364  29.084  1.00 25.48  ? 357  GLU B OE2 1 
ATOM   7633  N  N   . THR B 1 349 ? -5.232  74.235  31.347  1.00 20.78  ? 358  THR B N   1 
ATOM   7634  C  CA  . THR B 1 349 ? -4.879  73.734  32.673  1.00 20.63  ? 358  THR B CA  1 
ATOM   7635  C  C   . THR B 1 349 ? -4.197  72.377  32.521  1.00 19.30  ? 358  THR B C   1 
ATOM   7636  O  O   . THR B 1 349 ? -3.210  72.090  33.169  1.00 19.40  ? 358  THR B O   1 
ATOM   7637  C  CB  . THR B 1 349 ? -6.141  73.642  33.569  1.00 24.02  ? 358  THR B CB  1 
ATOM   7638  O  OG1 . THR B 1 349 ? -6.671  74.968  33.738  1.00 27.49  ? 358  THR B OG1 1 
ATOM   7639  C  CG2 . THR B 1 349 ? -5.822  73.025  34.943  1.00 24.18  ? 358  THR B CG2 1 
ATOM   7640  N  N   . ASN B 1 350 ? -4.697  71.536  31.621  1.00 20.28  ? 359  ASN B N   1 
ATOM   7641  C  CA  . ASN B 1 350 ? -4.066  70.242  31.380  1.00 15.09  ? 359  ASN B CA  1 
ATOM   7642  C  C   . ASN B 1 350 ? -2.613  70.474  30.916  1.00 18.75  ? 359  ASN B C   1 
ATOM   7643  O  O   . ASN B 1 350 ? -1.691  69.808  31.376  1.00 19.04  ? 359  ASN B O   1 
ATOM   7644  C  CB  . ASN B 1 350 ? -4.850  69.488  30.275  1.00 17.01  ? 359  ASN B CB  1 
ATOM   7645  C  CG  . ASN B 1 350 ? -4.302  68.119  29.984  1.00 21.19  ? 359  ASN B CG  1 
ATOM   7646  O  OD1 . ASN B 1 350 ? -3.754  67.819  28.902  1.00 18.45  ? 359  ASN B OD1 1 
ATOM   7647  N  ND2 . ASN B 1 350 ? -4.438  67.161  30.898  1.00 18.69  ? 359  ASN B ND2 1 
ATOM   7648  N  N   . ALA B 1 351 ? -2.420  71.413  29.953  1.00 19.06  ? 360  ALA B N   1 
ATOM   7649  C  CA  . ALA B 1 351 ? -1.054  71.652  29.481  1.00 20.30  ? 360  ALA B CA  1 
ATOM   7650  C  C   . ALA B 1 351 ? -0.148  72.220  30.616  1.00 20.78  ? 360  ALA B C   1 
ATOM   7651  O  O   . ALA B 1 351 ? 1.017   71.808  30.705  1.00 19.96  ? 360  ALA B O   1 
ATOM   7652  C  CB  . ALA B 1 351 ? -1.114  72.619  28.295  1.00 23.79  ? 360  ALA B CB  1 
ATOM   7653  N  N   . ASN B 1 352 ? -0.664  73.109  31.469  1.00 19.83  ? 361  ASN B N   1 
ATOM   7654  C  CA  . ASN B 1 352 ? 0.141   73.659  32.567  1.00 21.64  ? 361  ASN B CA  1 
ATOM   7655  C  C   . ASN B 1 352 ? 0.454   72.566  33.603  1.00 22.84  ? 361  ASN B C   1 
ATOM   7656  O  O   . ASN B 1 352 ? 1.551   72.578  34.206  1.00 23.13  ? 361  ASN B O   1 
ATOM   7657  C  CB  . ASN B 1 352 ? -0.581  74.818  33.236  1.00 20.83  ? 361  ASN B CB  1 
ATOM   7658  C  CG  . ASN B 1 352 ? -0.397  76.066  32.444  1.00 24.11  ? 361  ASN B CG  1 
ATOM   7659  O  OD1 . ASN B 1 352 ? 0.553   76.129  31.656  1.00 27.02  ? 361  ASN B OD1 1 
ATOM   7660  N  ND2 . ASN B 1 352 ? -1.276  77.018  32.475  1.00 23.06  ? 361  ASN B ND2 1 
ATOM   7661  N  N   . VAL B 1 353 ? -0.505  71.617  33.810  1.00 22.44  ? 362  VAL B N   1 
ATOM   7662  C  CA  . VAL B 1 353 ? -0.172  70.491  34.694  1.00 20.92  ? 362  VAL B CA  1 
ATOM   7663  C  C   . VAL B 1 353 ? 0.951   69.658  34.143  1.00 19.89  ? 362  VAL B C   1 
ATOM   7664  O  O   . VAL B 1 353 ? 1.891   69.284  34.844  1.00 20.44  ? 362  VAL B O   1 
ATOM   7665  C  CB  . VAL B 1 353 ? -1.430  69.619  34.932  1.00 22.17  ? 362  VAL B CB  1 
ATOM   7666  C  CG1 . VAL B 1 353 ? -1.012  68.226  35.494  1.00 21.08  ? 362  VAL B CG1 1 
ATOM   7667  C  CG2 . VAL B 1 353 ? -2.373  70.339  35.868  1.00 23.90  ? 362  VAL B CG2 1 
ATOM   7668  N  N   . ILE B 1 354 ? 0.894   69.335  32.838  1.00 17.60  ? 363  ILE B N   1 
ATOM   7669  C  CA  . ILE B 1 354 ? 1.938   68.527  32.269  1.00 17.93  ? 363  ILE B CA  1 
ATOM   7670  C  C   . ILE B 1 354 ? 3.271   69.291  32.297  1.00 21.83  ? 363  ILE B C   1 
ATOM   7671  O  O   . ILE B 1 354 ? 4.310   68.697  32.607  1.00 22.89  ? 363  ILE B O   1 
ATOM   7672  C  CB  . ILE B 1 354 ? 1.509   68.185  30.820  1.00 19.36  ? 363  ILE B CB  1 
ATOM   7673  C  CG1 . ILE B 1 354 ? 0.300   67.112  30.881  1.00 19.68  ? 363  ILE B CG1 1 
ATOM   7674  C  CG2 . ILE B 1 354 ? 2.713   67.594  30.021  1.00 21.38  ? 363  ILE B CG2 1 
ATOM   7675  C  CD1 . ILE B 1 354 ? -0.350  66.774  29.481  1.00 20.16  ? 363  ILE B CD1 1 
ATOM   7676  N  N   . LYS B 1 355 ? 3.238   70.582  31.974  1.00 21.79  ? 364  LYS B N   1 
ATOM   7677  C  CA  . LYS B 1 355 ? 4.470   71.387  31.980  1.00 20.58  ? 364  LYS B CA  1 
ATOM   7678  C  C   . LYS B 1 355 ? 5.099   71.421  33.399  1.00 25.15  ? 364  LYS B C   1 
ATOM   7679  O  O   . LYS B 1 355 ? 6.312   71.276  33.549  1.00 25.83  ? 364  LYS B O   1 
ATOM   7680  C  CB  . LYS B 1 355 ? 4.084   72.827  31.563  1.00 21.72  ? 364  LYS B CB  1 
ATOM   7681  C  CG  . LYS B 1 355 ? 5.251   73.803  31.652  1.00 27.46  ? 364  LYS B CG  1 
ATOM   7682  C  CD  . LYS B 1 355 ? 4.754   75.224  31.555  1.00 34.83  ? 364  LYS B CD  1 
ATOM   7683  C  CE  . LYS B 1 355 ? 5.942   76.148  31.419  1.00 49.68  ? 364  LYS B CE  1 
ATOM   7684  N  NZ  . LYS B 1 355 ? 5.565   77.570  31.671  1.00 62.09  ? 364  LYS B NZ  1 
ATOM   7685  N  N   . THR B 1 356 ? 4.286   71.611  34.407  1.00 25.12  ? 365  THR B N   1 
ATOM   7686  C  CA  . THR B 1 356 ? 4.759   71.750  35.813  1.00 24.73  ? 365  THR B CA  1 
ATOM   7687  C  C   . THR B 1 356 ? 5.130   70.450  36.444  1.00 27.69  ? 365  THR B C   1 
ATOM   7688  O  O   . THR B 1 356 ? 6.187   70.340  37.060  1.00 24.82  ? 365  THR B O   1 
ATOM   7689  C  CB  . THR B 1 356 ? 3.646   72.385  36.628  1.00 25.46  ? 365  THR B CB  1 
ATOM   7690  O  OG1 . THR B 1 356 ? 3.316   73.642  36.063  1.00 27.96  ? 365  THR B OG1 1 
ATOM   7691  C  CG2 . THR B 1 356 ? 4.001   72.593  38.142  1.00 26.34  ? 365  THR B CG2 1 
ATOM   7692  N  N   . PHE B 1 357 ? 4.269   69.419  36.289  1.00 25.96  ? 366  PHE B N   1 
ATOM   7693  C  CA  . PHE B 1 357 ? 4.496   68.158  37.035  1.00 26.48  ? 366  PHE B CA  1 
ATOM   7694  C  C   . PHE B 1 357 ? 5.153   67.063  36.275  1.00 25.91  ? 366  PHE B C   1 
ATOM   7695  O  O   . PHE B 1 357 ? 5.517   66.058  36.868  1.00 24.62  ? 366  PHE B O   1 
ATOM   7696  C  CB  . PHE B 1 357 ? 3.121   67.714  37.644  1.00 25.26  ? 366  PHE B CB  1 
ATOM   7697  C  CG  . PHE B 1 357 ? 2.581   68.718  38.644  1.00 26.98  ? 366  PHE B CG  1 
ATOM   7698  C  CD1 . PHE B 1 357 ? 1.479   69.508  38.342  1.00 27.22  ? 366  PHE B CD1 1 
ATOM   7699  C  CD2 . PHE B 1 357 ? 3.180   68.875  39.893  1.00 29.16  ? 366  PHE B CD2 1 
ATOM   7700  C  CE1 . PHE B 1 357 ? 0.985   70.443  39.263  1.00 31.54  ? 366  PHE B CE1 1 
ATOM   7701  C  CE2 . PHE B 1 357 ? 2.685   69.803  40.804  1.00 24.64  ? 366  PHE B CE2 1 
ATOM   7702  C  CZ  . PHE B 1 357 ? 1.603   70.586  40.497  1.00 25.97  ? 366  PHE B CZ  1 
ATOM   7703  N  N   . TYR B 1 358 ? 5.320   67.206  34.937  1.00 23.33  ? 367  TYR B N   1 
ATOM   7704  C  CA  . TYR B 1 358 ? 6.054   66.239  34.166  1.00 22.33  ? 367  TYR B CA  1 
ATOM   7705  C  C   . TYR B 1 358 ? 7.122   67.007  33.378  1.00 28.40  ? 367  TYR B C   1 
ATOM   7706  O  O   . TYR B 1 358 ? 7.106   67.113  32.153  1.00 26.47  ? 367  TYR B O   1 
ATOM   7707  C  CB  . TYR B 1 358 ? 5.172   65.418  33.226  1.00 24.11  ? 367  TYR B CB  1 
ATOM   7708  C  CG  . TYR B 1 358 ? 4.126   64.618  33.995  1.00 20.95  ? 367  TYR B CG  1 
ATOM   7709  C  CD1 . TYR B 1 358 ? 4.312   63.258  34.256  1.00 24.15  ? 367  TYR B CD1 1 
ATOM   7710  C  CD2 . TYR B 1 358 ? 2.967   65.222  34.470  1.00 21.99  ? 367  TYR B CD2 1 
ATOM   7711  C  CE1 . TYR B 1 358 ? 3.358   62.517  34.974  1.00 22.18  ? 367  TYR B CE1 1 
ATOM   7712  C  CE2 . TYR B 1 358 ? 2.007   64.491  35.172  1.00 24.99  ? 367  TYR B CE2 1 
ATOM   7713  C  CZ  . TYR B 1 358 ? 2.214   63.140  35.419  1.00 21.21  ? 367  TYR B CZ  1 
ATOM   7714  O  OH  . TYR B 1 358 ? 1.223   62.439  36.059  1.00 21.65  ? 367  TYR B OH  1 
ATOM   7715  N  N   . PRO B 1 359 ? 8.113   67.540  34.115  1.00 31.91  ? 368  PRO B N   1 
ATOM   7716  C  CA  . PRO B 1 359 ? 9.211   68.322  33.516  1.00 32.26  ? 368  PRO B CA  1 
ATOM   7717  C  C   . PRO B 1 359 ? 10.136  67.599  32.598  1.00 29.67  ? 368  PRO B C   1 
ATOM   7718  O  O   . PRO B 1 359 ? 10.779  68.281  31.814  1.00 31.05  ? 368  PRO B O   1 
ATOM   7719  C  CB  . PRO B 1 359 ? 9.952   68.879  34.756  1.00 32.00  ? 368  PRO B CB  1 
ATOM   7720  C  CG  . PRO B 1 359 ? 9.766   67.744  35.763  1.00 32.49  ? 368  PRO B CG  1 
ATOM   7721  C  CD  . PRO B 1 359 ? 8.286   67.415  35.587  1.00 31.08  ? 368  PRO B CD  1 
ATOM   7722  N  N   . ASP B 1 360 ? 10.263  66.284  32.631  1.00 28.02  ? 369  ASP B N   1 
ATOM   7723  C  CA  . ASP B 1 360 ? 11.250  65.667  31.749  1.00 28.83  ? 369  ASP B CA  1 
ATOM   7724  C  C   . ASP B 1 360 ? 10.936  65.875  30.285  1.00 31.91  ? 369  ASP B C   1 
ATOM   7725  O  O   . ASP B 1 360 ? 9.764   65.929  29.901  1.00 29.48  ? 369  ASP B O   1 
ATOM   7726  C  CB  . ASP B 1 360 ? 11.330  64.157  32.000  1.00 33.65  ? 369  ASP B CB  1 
ATOM   7727  C  CG  . ASP B 1 360 ? 11.883  63.805  33.395  1.00 41.58  ? 369  ASP B CG  1 
ATOM   7728  O  OD1 . ASP B 1 360 ? 12.307  64.727  34.116  1.00 40.89  ? 369  ASP B OD1 1 
ATOM   7729  O  OD2 . ASP B 1 360 ? 11.871  62.602  33.753  1.00 39.42  ? 369  ASP B OD2 1 
ATOM   7730  N  N   . LYS B 1 361 ? 11.967  65.970  29.456  1.00 28.19  ? 370  LYS B N   1 
ATOM   7731  C  CA  . LYS B 1 361 ? 11.760  66.133  28.027  1.00 27.43  ? 370  LYS B CA  1 
ATOM   7732  C  C   . LYS B 1 361 ? 11.397  64.768  27.379  1.00 27.33  ? 370  LYS B C   1 
ATOM   7733  O  O   . LYS B 1 361 ? 10.814  64.737  26.290  1.00 27.61  ? 370  LYS B O   1 
ATOM   7734  C  CB  . LYS B 1 361 ? 13.086  66.627  27.373  1.00 32.77  ? 370  LYS B CB  1 
ATOM   7735  C  CG  . LYS B 1 361 ? 13.436  68.047  27.770  1.00 45.21  ? 370  LYS B CG  1 
ATOM   7736  C  CD  . LYS B 1 361 ? 12.413  69.026  27.173  1.00 56.54  ? 370  LYS B CD  1 
ATOM   7737  C  CE  . LYS B 1 361 ? 12.591  70.465  27.624  1.00 65.01  ? 370  LYS B CE  1 
ATOM   7738  N  NZ  . LYS B 1 361 ? 13.393  70.580  28.882  1.00 66.99  ? 370  LYS B NZ  1 
ATOM   7739  N  N   . GLU B 1 362 ? 11.815  63.641  28.014  1.00 24.45  ? 371  GLU B N   1 
ATOM   7740  C  CA  . GLU B 1 362 ? 11.558  62.318  27.470  1.00 26.35  ? 371  GLU B CA  1 
ATOM   7741  C  C   . GLU B 1 362 ? 10.596  61.584  28.406  1.00 29.61  ? 371  GLU B C   1 
ATOM   7742  O  O   . GLU B 1 362 ? 10.955  61.187  29.526  1.00 30.28  ? 371  GLU B O   1 
ATOM   7743  C  CB  . GLU B 1 362 ? 12.877  61.549  27.248  1.00 30.88  ? 371  GLU B CB  1 
ATOM   7744  C  CG  . GLU B 1 362 ? 13.749  62.355  26.300  1.00 34.92  ? 371  GLU B CG  1 
ATOM   7745  C  CD  . GLU B 1 362 ? 14.883  61.579  25.649  1.00 45.29  ? 371  GLU B CD  1 
ATOM   7746  O  OE1 . GLU B 1 362 ? 15.318  60.553  26.207  1.00 46.85  ? 371  GLU B OE1 1 
ATOM   7747  O  OE2 . GLU B 1 362 ? 15.327  62.016  24.551  1.00 44.94  ? 371  GLU B OE2 1 
ATOM   7748  N  N   . LEU B 1 363 ? 9.360   61.467  27.992  1.00 24.75  ? 372  LEU B N   1 
ATOM   7749  C  CA  . LEU B 1 363 ? 8.375   60.772  28.832  1.00 23.91  ? 372  LEU B CA  1 
ATOM   7750  C  C   . LEU B 1 363 ? 8.369   59.318  28.477  1.00 24.33  ? 372  LEU B C   1 
ATOM   7751  O  O   . LEU B 1 363 ? 8.680   58.961  27.338  1.00 23.30  ? 372  LEU B O   1 
ATOM   7752  C  CB  . LEU B 1 363 ? 6.970   61.314  28.556  1.00 21.38  ? 372  LEU B CB  1 
ATOM   7753  C  CG  . LEU B 1 363 ? 6.852   62.841  28.780  1.00 22.31  ? 372  LEU B CG  1 
ATOM   7754  C  CD1 . LEU B 1 363 ? 5.528   63.268  28.241  1.00 22.39  ? 372  LEU B CD1 1 
ATOM   7755  C  CD2 . LEU B 1 363 ? 6.902   63.180  30.303  1.00 24.74  ? 372  LEU B CD2 1 
ATOM   7756  N  N   . SER B 1 364 ? 7.954   58.461  29.429  1.00 21.57  ? 373  SER B N   1 
ATOM   7757  C  CA  . SER B 1 364 ? 7.879   57.057  29.082  1.00 22.42  ? 373  SER B CA  1 
ATOM   7758  C  C   . SER B 1 364 ? 6.585   56.809  28.265  1.00 22.50  ? 373  SER B C   1 
ATOM   7759  O  O   . SER B 1 364 ? 6.491   55.833  27.540  1.00 24.24  ? 373  SER B O   1 
ATOM   7760  C  CB  . SER B 1 364 ? 7.834   56.199  30.349  1.00 27.66  ? 373  SER B CB  1 
ATOM   7761  O  OG  . SER B 1 364 ? 6.745   56.611  31.163  1.00 32.88  ? 373  SER B OG  1 
ATOM   7762  N  N   . ALA B 1 365 ? 5.622   57.694  28.392  1.00 20.19  ? 374  ALA B N   1 
ATOM   7763  C  CA  . ALA B 1 365 ? 4.347   57.510  27.716  1.00 19.43  ? 374  ALA B CA  1 
ATOM   7764  C  C   . ALA B 1 365 ? 3.496   58.725  27.843  1.00 17.94  ? 374  ALA B C   1 
ATOM   7765  O  O   . ALA B 1 365 ? 3.764   59.609  28.643  1.00 18.36  ? 374  ALA B O   1 
ATOM   7766  C  CB  . ALA B 1 365 ? 3.586   56.314  28.345  1.00 20.94  ? 374  ALA B CB  1 
ATOM   7767  N  N   . MET B 1 366 ? 2.427   58.782  27.043  1.00 19.13  ? 375  MET B N   1 
ATOM   7768  C  CA  . MET B 1 366 ? 1.442   59.834  27.177  1.00 18.61  ? 375  MET B CA  1 
ATOM   7769  C  C   . MET B 1 366 ? 0.109   59.163  26.982  1.00 20.20  ? 375  MET B C   1 
ATOM   7770  O  O   . MET B 1 366 ? -0.030  58.446  25.992  1.00 18.80  ? 375  MET B O   1 
ATOM   7771  C  CB  . MET B 1 366 ? 1.643   60.914  26.069  1.00 23.46  ? 375  MET B CB  1 
ATOM   7772  C  CG  A MET B 1 366 ? 0.603   61.989  26.081  0.67 27.07  ? 375  MET B CG  1 
ATOM   7773  C  CG  B MET B 1 366 ? 0.570   62.030  26.358  0.33 26.09  ? 375  MET B CG  1 
ATOM   7774  S  SD  A MET B 1 366 ? 0.907   63.220  27.369  0.67 24.09  ? 375  MET B SD  1 
ATOM   7775  S  SD  B MET B 1 366 ? 0.988   63.635  25.629  0.33 24.09  ? 375  MET B SD  1 
ATOM   7776  C  CE  A MET B 1 366 ? 2.178   64.297  26.580  0.67 19.97  ? 375  MET B CE  1 
ATOM   7777  C  CE  B MET B 1 366 ? 2.429   64.086  26.564  0.33 21.96  ? 375  MET B CE  1 
ATOM   7778  N  N   . LEU B 1 367 ? -0.880  59.339  27.856  1.00 15.13  ? 376  LEU B N   1 
ATOM   7779  C  CA  . LEU B 1 367 ? -2.172  58.693  27.639  1.00 14.52  ? 376  LEU B CA  1 
ATOM   7780  C  C   . LEU B 1 367 ? -3.080  59.821  27.166  1.00 20.02  ? 376  LEU B C   1 
ATOM   7781  O  O   . LEU B 1 367 ? -3.099  60.893  27.764  1.00 22.36  ? 376  LEU B O   1 
ATOM   7782  C  CB  . LEU B 1 367 ? -2.680  58.123  29.042  1.00 16.63  ? 376  LEU B CB  1 
ATOM   7783  C  CG  . LEU B 1 367 ? -1.922  56.806  29.478  1.00 19.22  ? 376  LEU B CG  1 
ATOM   7784  C  CD1 . LEU B 1 367 ? -0.603  57.183  30.128  1.00 18.35  ? 376  LEU B CD1 1 
ATOM   7785  C  CD2 . LEU B 1 367 ? -2.843  55.962  30.438  1.00 20.91  ? 376  LEU B CD2 1 
ATOM   7786  N  N   . VAL B 1 368 ? -3.840  59.606  26.102  1.00 18.16  ? 377  VAL B N   1 
ATOM   7787  C  CA  . VAL B 1 368 ? -4.651  60.685  25.558  1.00 15.45  ? 377  VAL B CA  1 
ATOM   7788  C  C   . VAL B 1 368 ? -6.111  60.355  25.634  1.00 17.11  ? 377  VAL B C   1 
ATOM   7789  O  O   . VAL B 1 368 ? -6.540  59.341  25.059  1.00 20.25  ? 377  VAL B O   1 
ATOM   7790  C  CB  . VAL B 1 368 ? -4.279  60.841  24.044  1.00 12.98  ? 377  VAL B CB  1 
ATOM   7791  C  CG1 . VAL B 1 368 ? -5.131  61.945  23.401  1.00 14.95  ? 377  VAL B CG1 1 
ATOM   7792  C  CG2 . VAL B 1 368 ? -2.775  61.178  23.955  1.00 15.56  ? 377  VAL B CG2 1 
ATOM   7793  N  N   . ALA B 1 369 ? -6.897  61.225  26.283  1.00 15.26  ? 378  ALA B N   1 
ATOM   7794  C  CA  . ALA B 1 369 ? -8.311  60.985  26.392  1.00 16.91  ? 378  ALA B CA  1 
ATOM   7795  C  C   . ALA B 1 369 ? -9.102  62.188  25.841  1.00 18.45  ? 378  ALA B C   1 
ATOM   7796  O  O   . ALA B 1 369 ? -8.584  63.318  25.763  1.00 17.19  ? 378  ALA B O   1 
ATOM   7797  C  CB  . ALA B 1 369 ? -8.687  60.851  27.927  1.00 15.83  ? 378  ALA B CB  1 
ATOM   7798  N  N   . LYS B 1 370 ? -10.370 61.969  25.524  1.00 17.64  ? 379  LYS B N   1 
ATOM   7799  C  CA  . LYS B 1 370 ? -11.233 63.060  25.086  1.00 18.06  ? 379  LYS B CA  1 
ATOM   7800  C  C   . LYS B 1 370 ? -11.557 63.990  26.191  1.00 21.25  ? 379  LYS B C   1 
ATOM   7801  O  O   . LYS B 1 370 ? -11.807 63.548  27.315  1.00 21.60  ? 379  LYS B O   1 
ATOM   7802  C  CB  . LYS B 1 370 ? -12.541 62.513  24.537  1.00 20.77  ? 379  LYS B CB  1 
ATOM   7803  C  CG  . LYS B 1 370 ? -12.320 61.629  23.345  1.00 22.71  ? 379  LYS B CG  1 
ATOM   7804  C  CD  . LYS B 1 370 ? -13.738 61.005  22.953  1.00 22.53  ? 379  LYS B CD  1 
ATOM   7805  C  CE  . LYS B 1 370 ? -14.019 59.832  23.849  1.00 24.28  ? 379  LYS B CE  1 
ATOM   7806  N  NZ  . LYS B 1 370 ? -15.454 59.325  23.653  1.00 28.53  ? 379  LYS B NZ  1 
ATOM   7807  N  N   . SER B 1 371 ? -11.601 65.297  25.924  1.00 18.61  ? 380  SER B N   1 
ATOM   7808  C  CA  . SER B 1 371 ? -11.835 66.204  27.036  1.00 17.59  ? 380  SER B CA  1 
ATOM   7809  C  C   . SER B 1 371 ? -13.293 66.521  27.207  1.00 21.16  ? 380  SER B C   1 
ATOM   7810  O  O   . SER B 1 371 ? -13.633 67.339  28.046  1.00 22.81  ? 380  SER B O   1 
ATOM   7811  C  CB  . SER B 1 371 ? -11.068 67.509  26.815  1.00 20.12  ? 380  SER B CB  1 
ATOM   7812  O  OG  . SER B 1 371 ? -11.589 68.063  25.608  1.00 21.47  ? 380  SER B OG  1 
ATOM   7813  N  N   . ASP B 1 372 ? -14.168 65.902  26.401  1.00 21.96  ? 381  ASP B N   1 
ATOM   7814  C  CA  . ASP B 1 372 ? -15.582 66.249  26.548  1.00 26.82  ? 381  ASP B CA  1 
ATOM   7815  C  C   . ASP B 1 372 ? -16.297 65.369  27.544  1.00 28.73  ? 381  ASP B C   1 
ATOM   7816  O  O   . ASP B 1 372 ? -17.450 65.628  27.829  1.00 32.43  ? 381  ASP B O   1 
ATOM   7817  C  CB  . ASP B 1 372 ? -16.300 66.224  25.184  1.00 28.47  ? 381  ASP B CB  1 
ATOM   7818  C  CG  . ASP B 1 372 ? -16.270 64.849  24.587  1.00 35.86  ? 381  ASP B CG  1 
ATOM   7819  O  OD1 . ASP B 1 372 ? -17.345 64.236  24.453  1.00 42.21  ? 381  ASP B OD1 1 
ATOM   7820  O  OD2 . ASP B 1 372 ? -15.194 64.381  24.257  1.00 38.88  ? 381  ASP B OD2 1 
ATOM   7821  N  N   . ILE B 1 373 ? -15.644 64.355  28.103  1.00 26.55  ? 382  ILE B N   1 
ATOM   7822  C  CA  . ILE B 1 373 ? -16.278 63.548  29.156  1.00 29.20  ? 382  ILE B CA  1 
ATOM   7823  C  C   . ILE B 1 373 ? -15.281 63.412  30.295  1.00 28.89  ? 382  ILE B C   1 
ATOM   7824  O  O   . ILE B 1 373 ? -14.082 63.697  30.103  1.00 29.33  ? 382  ILE B O   1 
ATOM   7825  C  CB  . ILE B 1 373 ? -16.651 62.157  28.672  1.00 28.33  ? 382  ILE B CB  1 
ATOM   7826  C  CG1 . ILE B 1 373 ? -15.400 61.514  28.056  1.00 30.23  ? 382  ILE B CG1 1 
ATOM   7827  C  CG2 . ILE B 1 373 ? -17.835 62.287  27.621  1.00 30.42  ? 382  ILE B CG2 1 
ATOM   7828  C  CD1 . ILE B 1 373 ? -15.698 60.112  27.555  1.00 41.68  ? 382  ILE B CD1 1 
ATOM   7829  N  N   . ILE B 1 374 ? -15.734 63.012  31.444  1.00 26.43  ? 383  ILE B N   1 
ATOM   7830  C  CA  . ILE B 1 374 ? -14.813 62.846  32.564  1.00 23.55  ? 383  ILE B CA  1 
ATOM   7831  C  C   . ILE B 1 374 ? -14.385 61.401  32.760  1.00 22.58  ? 383  ILE B C   1 
ATOM   7832  O  O   . ILE B 1 374 ? -13.229 61.141  33.083  1.00 20.80  ? 383  ILE B O   1 
ATOM   7833  C  CB  . ILE B 1 374 ? -15.566 63.318  33.832  1.00 27.34  ? 383  ILE B CB  1 
ATOM   7834  C  CG1 . ILE B 1 374 ? -15.862 64.825  33.781  1.00 35.26  ? 383  ILE B CG1 1 
ATOM   7835  C  CG2 . ILE B 1 374 ? -14.732 62.980  35.007  1.00 32.03  ? 383  ILE B CG2 1 
ATOM   7836  C  CD1 . ILE B 1 374 ? -14.708 65.677  34.167  1.00 43.72  ? 383  ILE B CD1 1 
ATOM   7837  N  N   . VAL B 1 375 ? -15.300 60.452  32.542  1.00 21.88  ? 384  VAL B N   1 
ATOM   7838  C  CA  . VAL B 1 375 ? -15.029 59.063  32.942  1.00 23.90  ? 384  VAL B CA  1 
ATOM   7839  C  C   . VAL B 1 375 ? -13.791 58.383  32.367  1.00 23.14  ? 384  VAL B C   1 
ATOM   7840  O  O   . VAL B 1 375 ? -13.106 57.670  33.097  1.00 22.65  ? 384  VAL B O   1 
ATOM   7841  C  CB  . VAL B 1 375 ? -16.297 58.198  32.652  1.00 26.17  ? 384  VAL B CB  1 
ATOM   7842  C  CG1 . VAL B 1 375 ? -16.511 58.009  31.159  1.00 24.69  ? 384  VAL B CG1 1 
ATOM   7843  C  CG2 . VAL B 1 375 ? -16.136 56.857  33.344  1.00 29.94  ? 384  VAL B CG2 1 
ATOM   7844  N  N   . ASP B 1 376 ? -13.505 58.570  31.065  1.00 20.07  ? 385  ASP B N   1 
ATOM   7845  C  CA  . ASP B 1 376 ? -12.345 57.921  30.508  1.00 18.98  ? 385  ASP B CA  1 
ATOM   7846  C  C   . ASP B 1 376 ? -11.033 58.379  31.214  1.00 18.18  ? 385  ASP B C   1 
ATOM   7847  O  O   . ASP B 1 376 ? -10.167 57.525  31.369  1.00 20.23  ? 385  ASP B O   1 
ATOM   7848  C  CB  . ASP B 1 376 ? -12.259 58.223  29.024  1.00 21.93  ? 385  ASP B CB  1 
ATOM   7849  C  CG  . ASP B 1 376 ? -13.265 57.465  28.153  1.00 30.19  ? 385  ASP B CG  1 
ATOM   7850  O  OD1 . ASP B 1 376 ? -13.885 56.475  28.645  1.00 26.81  ? 385  ASP B OD1 1 
ATOM   7851  O  OD2 . ASP B 1 376 ? -13.419 57.837  26.982  1.00 28.91  ? 385  ASP B OD2 1 
ATOM   7852  N  N   . SER B 1 377 ? -10.873 59.636  31.585  1.00 19.47  ? 386  SER B N   1 
ATOM   7853  C  CA  . SER B 1 377 ? -9.624  60.039  32.280  1.00 22.34  ? 386  SER B CA  1 
ATOM   7854  C  C   . SER B 1 377 ? -9.610  59.426  33.689  1.00 22.14  ? 386  SER B C   1 
ATOM   7855  O  O   . SER B 1 377 ? -8.540  59.109  34.200  1.00 20.93  ? 386  SER B O   1 
ATOM   7856  C  CB  . SER B 1 377 ? -9.534  61.561  32.435  1.00 21.82  ? 386  SER B CB  1 
ATOM   7857  O  OG  . SER B 1 377 ? -9.350  62.112  31.146  1.00 22.73  ? 386  SER B OG  1 
ATOM   7858  N  N   . ILE B 1 378 ? -10.798 59.240  34.294  1.00 22.31  ? 387  ILE B N   1 
ATOM   7859  C  CA  . ILE B 1 378 ? -10.831 58.612  35.640  1.00 22.18  ? 387  ILE B CA  1 
ATOM   7860  C  C   . ILE B 1 378 ? -10.373 57.184  35.530  1.00 22.12  ? 387  ILE B C   1 
ATOM   7861  O  O   . ILE B 1 378 ? -9.514  56.732  36.314  1.00 21.45  ? 387  ILE B O   1 
ATOM   7862  C  CB  A ILE B 1 378 ? -12.266 58.637  36.223  0.55 24.72  ? 387  ILE B CB  1 
ATOM   7863  C  CB  B ILE B 1 378 ? -12.211 58.879  36.298  0.45 26.75  ? 387  ILE B CB  1 
ATOM   7864  C  CG1 A ILE B 1 378 ? -12.652 60.037  36.632  0.55 24.58  ? 387  ILE B CG1 1 
ATOM   7865  C  CG1 B ILE B 1 378 ? -12.563 60.379  36.521  0.45 25.03  ? 387  ILE B CG1 1 
ATOM   7866  C  CG2 A ILE B 1 378 ? -12.378 57.698  37.468  0.55 26.79  ? 387  ILE B CG2 1 
ATOM   7867  C  CG2 B ILE B 1 378 ? -12.300 58.103  37.642  0.45 27.92  ? 387  ILE B CG2 1 
ATOM   7868  C  CD1 A ILE B 1 378 ? -14.081 60.018  37.163  0.55 23.68  ? 387  ILE B CD1 1 
ATOM   7869  C  CD1 B ILE B 1 378 ? -11.420 61.401  36.656  0.45 23.50  ? 387  ILE B CD1 1 
ATOM   7870  N  N   . THR B 1 379 ? -10.905 56.434  34.557  1.00 18.75  ? 388  THR B N   1 
ATOM   7871  C  CA  . THR B 1 379 ? -10.471 55.042  34.503  1.00 16.93  ? 388  THR B CA  1 
ATOM   7872  C  C   . THR B 1 379 ? -9.023  54.888  34.020  1.00 20.31  ? 388  THR B C   1 
ATOM   7873  O  O   . THR B 1 379 ? -8.357  53.901  34.351  1.00 19.97  ? 388  THR B O   1 
ATOM   7874  C  CB  . THR B 1 379 ? -11.426 54.181  33.638  1.00 21.59  ? 388  THR B CB  1 
ATOM   7875  O  OG1 . THR B 1 379 ? -11.481 54.734  32.307  1.00 22.05  ? 388  THR B OG1 1 
ATOM   7876  C  CG2 . THR B 1 379 ? -12.831 54.144  34.222  1.00 21.18  ? 388  THR B CG2 1 
ATOM   7877  N  N   . ALA B 1 380 ? -8.531  55.868  33.188  1.00 20.21  ? 389  ALA B N   1 
ATOM   7878  C  CA  . ALA B 1 380 ? -7.133  55.788  32.771  1.00 18.91  ? 389  ALA B CA  1 
ATOM   7879  C  C   . ALA B 1 380 ? -6.182  56.175  33.925  1.00 17.90  ? 389  ALA B C   1 
ATOM   7880  O  O   . ALA B 1 380 ? -5.023  55.782  33.865  1.00 20.37  ? 389  ALA B O   1 
ATOM   7881  C  CB  . ALA B 1 380 ? -6.913  56.771  31.582  1.00 18.70  ? 389  ALA B CB  1 
ATOM   7882  N  N   . GLY B 1 381 ? -6.670  56.921  34.941  1.00 18.82  ? 390  GLY B N   1 
ATOM   7883  C  CA  . GLY B 1 381 ? -5.816  57.451  36.027  1.00 16.85  ? 390  GLY B CA  1 
ATOM   7884  C  C   . GLY B 1 381 ? -4.905  56.421  36.665  1.00 20.22  ? 390  GLY B C   1 
ATOM   7885  O  O   . GLY B 1 381 ? -3.698  56.604  36.792  1.00 19.26  ? 390  GLY B O   1 
ATOM   7886  N  N   . PRO B 1 382 ? -5.465  55.274  37.090  1.00 20.99  ? 391  PRO B N   1 
ATOM   7887  C  CA  . PRO B 1 382 ? -4.645  54.201  37.720  1.00 20.61  ? 391  PRO B CA  1 
ATOM   7888  C  C   . PRO B 1 382 ? -3.561  53.650  36.839  1.00 19.52  ? 391  PRO B C   1 
ATOM   7889  O  O   . PRO B 1 382 ? -2.475  53.328  37.328  1.00 20.21  ? 391  PRO B O   1 
ATOM   7890  C  CB  . PRO B 1 382 ? -5.708  53.135  38.132  1.00 19.98  ? 391  PRO B CB  1 
ATOM   7891  C  CG  . PRO B 1 382 ? -6.906  53.936  38.385  1.00 21.07  ? 391  PRO B CG  1 
ATOM   7892  C  CD  . PRO B 1 382 ? -6.905  54.997  37.236  1.00 22.73  ? 391  PRO B CD  1 
ATOM   7893  N  N   . LEU B 1 383 ? -3.814  53.515  35.520  1.00 16.39  ? 392  LEU B N   1 
ATOM   7894  C  CA  . LEU B 1 383 ? -2.781  53.014  34.627  1.00 17.78  ? 392  LEU B CA  1 
ATOM   7895  C  C   . LEU B 1 383 ? -1.718  54.135  34.389  1.00 19.59  ? 392  LEU B C   1 
ATOM   7896  O  O   . LEU B 1 383 ? -0.509  53.860  34.414  1.00 19.32  ? 392  LEU B O   1 
ATOM   7897  C  CB  . LEU B 1 383 ? -3.440  52.627  33.296  1.00 17.97  ? 392  LEU B CB  1 
ATOM   7898  C  CG  . LEU B 1 383 ? -2.406  52.179  32.261  1.00 19.94  ? 392  LEU B CG  1 
ATOM   7899  C  CD1 . LEU B 1 383 ? -1.667  50.909  32.718  1.00 21.84  ? 392  LEU B CD1 1 
ATOM   7900  C  CD2 . LEU B 1 383 ? -3.128  51.905  30.910  1.00 18.19  ? 392  LEU B CD2 1 
ATOM   7901  N  N   . ALA B 1 384 ? -2.169  55.397  34.196  1.00 18.16  ? 393  ALA B N   1 
ATOM   7902  C  CA  . ALA B 1 384 ? -1.215  56.487  34.032  1.00 18.59  ? 393  ALA B CA  1 
ATOM   7903  C  C   . ALA B 1 384 ? -0.257  56.541  35.274  1.00 19.99  ? 393  ALA B C   1 
ATOM   7904  O  O   . ALA B 1 384 ? 0.947   56.773  35.132  1.00 19.58  ? 393  ALA B O   1 
ATOM   7905  C  CB  . ALA B 1 384 ? -1.976  57.818  33.918  1.00 18.07  ? 393  ALA B CB  1 
ATOM   7906  N  N   . ALA B 1 385 ? -0.814  56.367  36.483  1.00 19.12  ? 394  ALA B N   1 
ATOM   7907  C  CA  . ALA B 1 385 ? 0.009   56.417  37.672  1.00 21.00  ? 394  ALA B CA  1 
ATOM   7908  C  C   . ALA B 1 385 ? 1.020   55.258  37.663  1.00 19.57  ? 394  ALA B C   1 
ATOM   7909  O  O   . ALA B 1 385 ? 2.199   55.460  37.990  1.00 20.97  ? 394  ALA B O   1 
ATOM   7910  C  CB  . ALA B 1 385 ? -0.888  56.314  38.897  1.00 19.27  ? 394  ALA B CB  1 
ATOM   7911  N  N   . LYS B 1 386 ? 0.578   54.054  37.290  1.00 17.51  ? 395  LYS B N   1 
ATOM   7912  C  CA  . LYS B 1 386 ? 1.448   52.901  37.243  1.00 17.15  ? 395  LYS B CA  1 
ATOM   7913  C  C   . LYS B 1 386 ? 2.577   53.134  36.264  1.00 19.20  ? 395  LYS B C   1 
ATOM   7914  O  O   . LYS B 1 386 ? 3.744   52.813  36.503  1.00 18.46  ? 395  LYS B O   1 
ATOM   7915  C  CB  . LYS B 1 386 ? 0.603   51.665  36.829  1.00 15.98  ? 395  LYS B CB  1 
ATOM   7916  C  CG  . LYS B 1 386 ? 1.470   50.338  36.736  1.00 20.35  ? 395  LYS B CG  1 
ATOM   7917  C  CD  . LYS B 1 386 ? 0.495   49.176  36.380  1.00 21.40  ? 395  LYS B CD  1 
ATOM   7918  C  CE  . LYS B 1 386 ? 1.195   47.878  35.974  1.00 24.70  ? 395  LYS B CE  1 
ATOM   7919  N  NZ  . LYS B 1 386 ? 1.983   47.341  37.125  1.00 23.75  ? 395  LYS B NZ  1 
ATOM   7920  N  N   . LEU B 1 387 ? 2.224   53.721  35.122  1.00 20.23  ? 396  LEU B N   1 
ATOM   7921  C  CA  . LEU B 1 387 ? 3.222   53.978  34.094  1.00 21.46  ? 396  LEU B CA  1 
ATOM   7922  C  C   . LEU B 1 387 ? 4.052   55.202  34.385  1.00 21.60  ? 396  LEU B C   1 
ATOM   7923  O  O   . LEU B 1 387 ? 5.037   55.427  33.689  1.00 21.41  ? 396  LEU B O   1 
ATOM   7924  C  CB  . LEU B 1 387 ? 2.476   54.235  32.747  1.00 20.45  ? 396  LEU B CB  1 
ATOM   7925  C  CG  . LEU B 1 387 ? 1.776   52.992  32.207  1.00 19.65  ? 396  LEU B CG  1 
ATOM   7926  C  CD1 . LEU B 1 387 ? 1.052   53.400  30.853  1.00 16.40  ? 396  LEU B CD1 1 
ATOM   7927  C  CD2 . LEU B 1 387 ? 2.751   51.833  31.919  1.00 22.60  ? 396  LEU B CD2 1 
ATOM   7928  N  N   . LYS B 1 388 ? 3.676   55.981  35.408  1.00 19.53  ? 397  LYS B N   1 
ATOM   7929  C  CA  . LYS B 1 388 ? 4.341   57.260  35.796  1.00 18.75  ? 397  LYS B CA  1 
ATOM   7930  C  C   . LYS B 1 388 ? 4.337   58.168  34.563  1.00 22.37  ? 397  LYS B C   1 
ATOM   7931  O  O   . LYS B 1 388 ? 5.373   58.741  34.179  1.00 22.94  ? 397  LYS B O   1 
ATOM   7932  C  CB  . LYS B 1 388 ? 5.775   57.002  36.298  1.00 21.12  ? 397  LYS B CB  1 
ATOM   7933  C  CG  . LYS B 1 388 ? 5.759   56.127  37.570  1.00 26.28  ? 397  LYS B CG  1 
ATOM   7934  C  CD  . LYS B 1 388 ? 7.223   56.018  38.117  1.00 35.25  ? 397  LYS B CD  1 
ATOM   7935  C  CE  . LYS B 1 388 ? 7.448   54.848  39.069  1.00 39.60  ? 397  LYS B CE  1 
ATOM   7936  N  NZ  . LYS B 1 388 ? 6.535   54.940  40.236  1.00 38.15  ? 397  LYS B NZ  1 
ATOM   7937  N  N   . ALA B 1 389 ? 3.170   58.272  33.940  1.00 19.96  ? 398  ALA B N   1 
ATOM   7938  C  CA  . ALA B 1 389 ? 3.029   59.091  32.729  1.00 20.40  ? 398  ALA B CA  1 
ATOM   7939  C  C   . ALA B 1 389 ? 1.817   59.994  32.853  1.00 20.07  ? 398  ALA B C   1 
ATOM   7940  O  O   . ALA B 1 389 ? 0.902   59.745  33.635  1.00 18.55  ? 398  ALA B O   1 
ATOM   7941  C  CB  . ALA B 1 389 ? 2.868   58.170  31.540  1.00 21.15  ? 398  ALA B CB  1 
ATOM   7942  N  N   . PRO B 1 390 ? 1.791   61.101  32.111  1.00 17.81  ? 399  PRO B N   1 
ATOM   7943  C  CA  . PRO B 1 390 ? 0.628   61.993  32.208  1.00 14.98  ? 399  PRO B CA  1 
ATOM   7944  C  C   . PRO B 1 390 ? -0.534  61.633  31.342  1.00 18.44  ? 399  PRO B C   1 
ATOM   7945  O  O   . PRO B 1 390 ? -0.376  60.911  30.359  1.00 16.55  ? 399  PRO B O   1 
ATOM   7946  C  CB  . PRO B 1 390 ? 1.196   63.359  31.744  1.00 18.02  ? 399  PRO B CB  1 
ATOM   7947  C  CG  . PRO B 1 390 ? 2.298   62.942  30.744  1.00 19.10  ? 399  PRO B CG  1 
ATOM   7948  C  CD  . PRO B 1 390 ? 2.893   61.629  31.251  1.00 17.96  ? 399  PRO B CD  1 
ATOM   7949  N  N   . ILE B 1 391 ? -1.659  62.203  31.646  1.00 17.43  ? 400  ILE B N   1 
ATOM   7950  C  CA  . ILE B 1 391 ? -2.856  62.100  30.783  1.00 19.06  ? 400  ILE B CA  1 
ATOM   7951  C  C   . ILE B 1 391 ? -3.037  63.476  30.094  1.00 17.91  ? 400  ILE B C   1 
ATOM   7952  O  O   . ILE B 1 391 ? -3.122  64.514  30.765  1.00 17.65  ? 400  ILE B O   1 
ATOM   7953  C  CB  . ILE B 1 391 ? -4.124  61.787  31.653  1.00 17.11  ? 400  ILE B CB  1 
ATOM   7954  C  CG1 . ILE B 1 391 ? -4.052  60.322  32.122  1.00 16.47  ? 400  ILE B CG1 1 
ATOM   7955  C  CG2 . ILE B 1 391 ? -5.408  62.045  30.838  1.00 18.46  ? 400  ILE B CG2 1 
ATOM   7956  C  CD1 . ILE B 1 391 ? -5.124  60.142  33.275  1.00 17.22  ? 400  ILE B CD1 1 
ATOM   7957  N  N   . LEU B 1 392 ? -3.127  63.460  28.753  1.00 15.19  ? 401  LEU B N   1 
ATOM   7958  C  CA  . LEU B 1 392 ? -3.352  64.668  27.966  1.00 16.28  ? 401  LEU B CA  1 
ATOM   7959  C  C   . LEU B 1 392 ? -4.842  64.622  27.538  1.00 15.22  ? 401  LEU B C   1 
ATOM   7960  O  O   . LEU B 1 392 ? -5.279  63.533  27.128  1.00 16.48  ? 401  LEU B O   1 
ATOM   7961  C  CB  . LEU B 1 392 ? -2.486  64.572  26.693  1.00 17.99  ? 401  LEU B CB  1 
ATOM   7962  C  CG  . LEU B 1 392 ? -2.574  65.913  25.851  1.00 24.53  ? 401  LEU B CG  1 
ATOM   7963  C  CD1 . LEU B 1 392 ? -1.204  66.352  25.294  1.00 24.47  ? 401  LEU B CD1 1 
ATOM   7964  C  CD2 . LEU B 1 392 ? -3.538  65.661  24.684  1.00 27.16  ? 401  LEU B CD2 1 
ATOM   7965  N  N   . ILE B 1 393 ? -5.607  65.708  27.684  1.00 15.42  ? 402  ILE B N   1 
ATOM   7966  C  CA  . ILE B 1 393 ? -6.982  65.697  27.228  1.00 15.73  ? 402  ILE B CA  1 
ATOM   7967  C  C   . ILE B 1 393 ? -7.099  66.729  26.115  1.00 20.23  ? 402  ILE B C   1 
ATOM   7968  O  O   . ILE B 1 393 ? -6.475  67.798  26.195  1.00 19.38  ? 402  ILE B O   1 
ATOM   7969  C  CB  . ILE B 1 393 ? -8.040  66.014  28.342  1.00 18.85  ? 402  ILE B CB  1 
ATOM   7970  C  CG1 . ILE B 1 393 ? -7.791  67.407  29.011  1.00 21.07  ? 402  ILE B CG1 1 
ATOM   7971  C  CG2 . ILE B 1 393 ? -7.986  64.862  29.384  1.00 20.65  ? 402  ILE B CG2 1 
ATOM   7972  C  CD1 . ILE B 1 393 ? -8.959  67.847  29.983  1.00 19.12  ? 402  ILE B CD1 1 
ATOM   7973  N  N   . THR B 1 394 ? -7.883  66.415  25.089  1.00 18.74  ? 403  THR B N   1 
ATOM   7974  C  CA  . THR B 1 394 ? -8.095  67.376  23.969  1.00 19.84  ? 403  THR B CA  1 
ATOM   7975  C  C   . THR B 1 394 ? -9.388  66.993  23.323  1.00 18.90  ? 403  THR B C   1 
ATOM   7976  O  O   . THR B 1 394 ? -9.889  65.859  23.519  1.00 17.78  ? 403  THR B O   1 
ATOM   7977  C  CB  . THR B 1 394 ? -6.850  67.314  22.974  1.00 22.13  ? 403  THR B CB  1 
ATOM   7978  O  OG1 . THR B 1 394 ? -6.976  68.402  22.072  1.00 20.60  ? 403  THR B OG1 1 
ATOM   7979  C  CG2 . THR B 1 394 ? -6.800  66.064  22.129  1.00 19.83  ? 403  THR B CG2 1 
ATOM   7980  N  N   . PRO B 1 395 ? -10.032 67.910  22.592  1.00 16.63  ? 404  PRO B N   1 
ATOM   7981  C  CA  . PRO B 1 395 ? -11.309 67.529  21.947  1.00 18.45  ? 404  PRO B CA  1 
ATOM   7982  C  C   . PRO B 1 395 ? -11.165 66.449  20.926  1.00 18.13  ? 404  PRO B C   1 
ATOM   7983  O  O   . PRO B 1 395 ? -10.073 66.182  20.429  1.00 19.08  ? 404  PRO B O   1 
ATOM   7984  C  CB  . PRO B 1 395 ? -11.765 68.851  21.288  1.00 20.46  ? 404  PRO B CB  1 
ATOM   7985  C  CG  . PRO B 1 395 ? -11.209 69.904  22.276  1.00 20.31  ? 404  PRO B CG  1 
ATOM   7986  C  CD  . PRO B 1 395 ? -9.791  69.362  22.522  1.00 17.71  ? 404  PRO B CD  1 
ATOM   7987  N  N   . LYS B 1 396 ? -12.295 65.845  20.558  1.00 19.82  ? 405  LYS B N   1 
ATOM   7988  C  CA  . LYS B 1 396 ? -12.250 64.790  19.557  1.00 21.28  ? 405  LYS B CA  1 
ATOM   7989  C  C   . LYS B 1 396 ? -11.740 65.228  18.200  1.00 23.44  ? 405  LYS B C   1 
ATOM   7990  O  O   . LYS B 1 396 ? -11.090 64.412  17.521  1.00 22.89  ? 405  LYS B O   1 
ATOM   7991  C  CB  . LYS B 1 396 ? -13.687 64.238  19.287  1.00 23.31  ? 405  LYS B CB  1 
ATOM   7992  C  CG  . LYS B 1 396 ? -14.124 63.193  20.291  1.00 31.81  ? 405  LYS B CG  1 
ATOM   7993  C  CD  . LYS B 1 396 ? -15.549 62.668  19.905  1.00 37.64  ? 405  LYS B CD  1 
ATOM   7994  C  CE  . LYS B 1 396 ? -16.621 63.494  20.528  1.00 44.50  ? 405  LYS B CE  1 
ATOM   7995  N  NZ  . LYS B 1 396 ? -17.645 62.618  21.139  1.00 50.18  ? 405  LYS B NZ  1 
ATOM   7996  N  N   . THR B 1 397 ? -12.015 66.501  17.787  1.00 22.20  ? 406  THR B N   1 
ATOM   7997  C  CA  . THR B 1 397 ? -11.657 66.868  16.405  1.00 25.85  ? 406  THR B CA  1 
ATOM   7998  C  C   . THR B 1 397 ? -10.438 67.757  16.294  1.00 27.08  ? 406  THR B C   1 
ATOM   7999  O  O   . THR B 1 397 ? -10.105 68.131  15.198  1.00 27.07  ? 406  THR B O   1 
ATOM   8000  C  CB  . THR B 1 397 ? -12.892 67.541  15.743  1.00 28.70  ? 406  THR B CB  1 
ATOM   8001  O  OG1 . THR B 1 397 ? -13.242 68.661  16.537  1.00 30.33  ? 406  THR B OG1 1 
ATOM   8002  C  CG2 . THR B 1 397 ? -14.084 66.596  15.663  1.00 32.01  ? 406  THR B CG2 1 
ATOM   8003  N  N   . TYR B 1 398 ? -9.765  68.125  17.388  1.00 22.29  ? 407  TYR B N   1 
ATOM   8004  C  CA  . TYR B 1 398 ? -8.540  68.923  17.217  1.00 18.97  ? 407  TYR B CA  1 
ATOM   8005  C  C   . TYR B 1 398 ? -7.621  68.849  18.455  1.00 20.12  ? 407  TYR B C   1 
ATOM   8006  O  O   . TYR B 1 398 ? -8.078  68.615  19.557  1.00 19.39  ? 407  TYR B O   1 
ATOM   8007  C  CB  . TYR B 1 398 ? -8.874  70.427  16.931  1.00 18.91  ? 407  TYR B CB  1 
ATOM   8008  C  CG  . TYR B 1 398 ? -9.699  71.119  17.991  1.00 21.25  ? 407  TYR B CG  1 
ATOM   8009  C  CD1 . TYR B 1 398 ? -11.091 71.078  17.948  1.00 19.71  ? 407  TYR B CD1 1 
ATOM   8010  C  CD2 . TYR B 1 398 ? -9.094  71.869  19.005  1.00 20.02  ? 407  TYR B CD2 1 
ATOM   8011  C  CE1 . TYR B 1 398 ? -11.868 71.769  18.874  1.00 20.95  ? 407  TYR B CE1 1 
ATOM   8012  C  CE2 . TYR B 1 398 ? -9.879  72.573  19.951  1.00 21.43  ? 407  TYR B CE2 1 
ATOM   8013  C  CZ  . TYR B 1 398 ? -11.268 72.505  19.867  1.00 23.88  ? 407  TYR B CZ  1 
ATOM   8014  O  OH  . TYR B 1 398 ? -12.123 73.129  20.752  1.00 24.14  ? 407  TYR B OH  1 
ATOM   8015  N  N   . VAL B 1 399 ? -6.326  69.046  18.230  1.00 19.58  ? 408  VAL B N   1 
ATOM   8016  C  CA  . VAL B 1 399 ? -5.356  69.142  19.295  1.00 18.11  ? 408  VAL B CA  1 
ATOM   8017  C  C   . VAL B 1 399 ? -5.438  70.563  19.751  1.00 22.42  ? 408  VAL B C   1 
ATOM   8018  O  O   . VAL B 1 399 ? -5.243  71.488  18.951  1.00 20.09  ? 408  VAL B O   1 
ATOM   8019  C  CB  . VAL B 1 399 ? -3.909  68.864  18.800  1.00 19.34  ? 408  VAL B CB  1 
ATOM   8020  C  CG1 . VAL B 1 399 ? -2.921  68.923  20.037  1.00 17.79  ? 408  VAL B CG1 1 
ATOM   8021  C  CG2 . VAL B 1 399 ? -3.857  67.501  18.101  1.00 21.64  ? 408  VAL B CG2 1 
ATOM   8022  N  N   . SER B 1 400 ? -5.704  70.788  21.032  1.00 18.18  ? 409  SER B N   1 
ATOM   8023  C  CA  . SER B 1 400 ? -5.767  72.156  21.521  1.00 21.63  ? 409  SER B CA  1 
ATOM   8024  C  C   . SER B 1 400 ? -4.445  72.879  21.288  1.00 19.05  ? 409  SER B C   1 
ATOM   8025  O  O   . SER B 1 400 ? -3.367  72.293  21.490  1.00 18.73  ? 409  SER B O   1 
ATOM   8026  C  CB  . SER B 1 400 ? -6.040  72.133  23.037  1.00 20.28  ? 409  SER B CB  1 
ATOM   8027  O  OG  . SER B 1 400 ? -5.942  73.446  23.560  1.00 21.69  ? 409  SER B OG  1 
ATOM   8028  N  N   . ALA B 1 401 ? -4.515  74.160  20.874  1.00 18.12  ? 410  ALA B N   1 
ATOM   8029  C  CA  . ALA B 1 401 ? -3.302  74.973  20.671  1.00 18.98  ? 410  ALA B CA  1 
ATOM   8030  C  C   . ALA B 1 401 ? -2.537  75.118  21.982  1.00 17.39  ? 410  ALA B C   1 
ATOM   8031  O  O   . ALA B 1 401 ? -1.339  75.365  21.979  1.00 18.36  ? 410  ALA B O   1 
ATOM   8032  C  CB  . ALA B 1 401 ? -3.708  76.384  20.186  1.00 19.98  ? 410  ALA B CB  1 
ATOM   8033  N  N   . TYR B 1 402 ? -3.236  74.955  23.147  1.00 18.01  ? 411  TYR B N   1 
ATOM   8034  C  CA  . TYR B 1 402 ? -2.466  75.089  24.372  1.00 17.70  ? 411  TYR B CA  1 
ATOM   8035  C  C   . TYR B 1 402 ? -1.424  73.989  24.582  1.00 18.47  ? 411  TYR B C   1 
ATOM   8036  O  O   . TYR B 1 402 ? -0.549  74.168  25.444  1.00 19.04  ? 411  TYR B O   1 
ATOM   8037  C  CB  . TYR B 1 402 ? -3.417  75.098  25.574  1.00 19.43  ? 411  TYR B CB  1 
ATOM   8038  C  CG  . TYR B 1 402 ? -4.294  76.338  25.642  1.00 20.04  ? 411  TYR B CG  1 
ATOM   8039  C  CD1 . TYR B 1 402 ? -3.735  77.603  25.858  1.00 22.41  ? 411  TYR B CD1 1 
ATOM   8040  C  CD2 . TYR B 1 402 ? -5.674  76.248  25.497  1.00 18.19  ? 411  TYR B CD2 1 
ATOM   8041  C  CE1 . TYR B 1 402 ? -4.531  78.736  25.935  1.00 19.12  ? 411  TYR B CE1 1 
ATOM   8042  C  CE2 . TYR B 1 402 ? -6.474  77.374  25.544  1.00 21.72  ? 411  TYR B CE2 1 
ATOM   8043  C  CZ  . TYR B 1 402 ? -5.893  78.621  25.769  1.00 21.29  ? 411  TYR B CZ  1 
ATOM   8044  O  OH  . TYR B 1 402 ? -6.659  79.754  25.852  1.00 21.86  ? 411  TYR B OH  1 
ATOM   8045  N  N   . HIS B 1 403 ? -1.510  72.877  23.859  1.00 16.78  ? 412  HIS B N   1 
ATOM   8046  C  CA  . HIS B 1 403 ? -0.583  71.734  24.013  1.00 17.04  ? 412  HIS B CA  1 
ATOM   8047  C  C   . HIS B 1 403 ? 0.686   71.896  23.158  1.00 21.50  ? 412  HIS B C   1 
ATOM   8048  O  O   . HIS B 1 403 ? 1.572   71.063  23.234  1.00 18.75  ? 412  HIS B O   1 
ATOM   8049  C  CB  . HIS B 1 403 ? -1.305  70.404  23.558  1.00 17.12  ? 412  HIS B CB  1 
ATOM   8050  C  CG  . HIS B 1 403 ? -2.413  69.999  24.469  1.00 17.85  ? 412  HIS B CG  1 
ATOM   8051  N  ND1 . HIS B 1 403 ? -2.279  70.061  25.844  1.00 18.66  ? 412  HIS B ND1 1 
ATOM   8052  C  CD2 . HIS B 1 403 ? -3.655  69.516  24.219  1.00 19.56  ? 412  HIS B CD2 1 
ATOM   8053  C  CE1 . HIS B 1 403 ? -3.419  69.661  26.387  1.00 21.51  ? 412  HIS B CE1 1 
ATOM   8054  N  NE2 . HIS B 1 403 ? -4.267  69.312  25.432  1.00 21.24  ? 412  HIS B NE2 1 
ATOM   8055  N  N   . SER B 1 404 ? 0.782   73.002  22.352  1.00 21.28  ? 413  SER B N   1 
ATOM   8056  C  CA  . SER B 1 404 ? 1.923   73.083  21.386  1.00 23.45  ? 413  SER B CA  1 
ATOM   8057  C  C   . SER B 1 404 ? 3.301   73.012  21.956  1.00 24.25  ? 413  SER B C   1 
ATOM   8058  O  O   . SER B 1 404 ? 4.096   72.265  21.403  1.00 24.15  ? 413  SER B O   1 
ATOM   8059  C  CB  . SER B 1 404 ? 1.826   74.359  20.545  1.00 26.52  ? 413  SER B CB  1 
ATOM   8060  O  OG  . SER B 1 404 ? 0.584   74.282  19.864  1.00 30.35  ? 413  SER B OG  1 
ATOM   8061  N  N   . THR B 1 405 ? 3.599   73.738  23.025  1.00 24.21  ? 414  THR B N   1 
ATOM   8062  C  CA  . THR B 1 405 ? 4.978   73.706  23.553  1.00 28.64  ? 414  THR B CA  1 
ATOM   8063  C  C   . THR B 1 405 ? 5.316   72.353  24.077  1.00 24.66  ? 414  THR B C   1 
ATOM   8064  O  O   . THR B 1 405 ? 6.360   71.804  23.776  1.00 23.99  ? 414  THR B O   1 
ATOM   8065  C  CB  . THR B 1 405 ? 5.140   74.768  24.658  1.00 31.91  ? 414  THR B CB  1 
ATOM   8066  O  OG1 . THR B 1 405 ? 4.833   76.033  24.088  1.00 33.97  ? 414  THR B OG1 1 
ATOM   8067  C  CG2 . THR B 1 405 ? 6.532   74.769  25.265  1.00 35.36  ? 414  THR B CG2 1 
ATOM   8068  N  N   . ASN B 1 406 ? 4.403   71.761  24.868  1.00 24.55  ? 415  ASN B N   1 
ATOM   8069  C  CA  . ASN B 1 406 ? 4.717   70.453  25.431  1.00 22.75  ? 415  ASN B CA  1 
ATOM   8070  C  C   . ASN B 1 406 ? 4.871   69.431  24.384  1.00 20.21  ? 415  ASN B C   1 
ATOM   8071  O  O   . ASN B 1 406 ? 5.803   68.625  24.474  1.00 21.11  ? 415  ASN B O   1 
ATOM   8072  C  CB  . ASN B 1 406 ? 3.577   69.945  26.413  1.00 21.54  ? 415  ASN B CB  1 
ATOM   8073  C  CG  . ASN B 1 406 ? 3.422   70.751  27.669  1.00 26.51  ? 415  ASN B CG  1 
ATOM   8074  O  OD1 . ASN B 1 406 ? 4.390   71.418  28.108  1.00 27.25  ? 415  ASN B OD1 1 
ATOM   8075  N  ND2 . ASN B 1 406 ? 2.228   70.835  28.292  1.00 23.06  ? 415  ASN B ND2 1 
ATOM   8076  N  N   . LEU B 1 407 ? 3.957   69.367  23.390  1.00 18.94  ? 416  LEU B N   1 
ATOM   8077  C  CA  . LEU B 1 407 ? 4.059   68.309  22.397  1.00 21.43  ? 416  LEU B CA  1 
ATOM   8078  C  C   . LEU B 1 407 ? 5.262   68.497  21.501  1.00 23.04  ? 416  LEU B C   1 
ATOM   8079  O  O   . LEU B 1 407 ? 5.904   67.524  21.092  1.00 19.93  ? 416  LEU B O   1 
ATOM   8080  C  CB  . LEU B 1 407 ? 2.783   68.259  21.489  1.00 21.40  ? 416  LEU B CB  1 
ATOM   8081  C  CG  . LEU B 1 407 ? 1.518   67.869  22.290  1.00 17.89  ? 416  LEU B CG  1 
ATOM   8082  C  CD1 . LEU B 1 407 ? 0.229   68.003  21.370  1.00 18.21  ? 416  LEU B CD1 1 
ATOM   8083  C  CD2 . LEU B 1 407 ? 1.730   66.361  22.745  1.00 20.19  ? 416  LEU B CD2 1 
ATOM   8084  N  N   . SER B 1 408 ? 5.565   69.743  21.208  1.00 21.28  ? 417  SER B N   1 
ATOM   8085  C  CA  . SER B 1 408 ? 6.735   70.022  20.362  1.00 21.23  ? 417  SER B CA  1 
ATOM   8086  C  C   . SER B 1 408 ? 8.003   69.606  21.065  1.00 22.63  ? 417  SER B C   1 
ATOM   8087  O  O   . SER B 1 408 ? 8.796   68.839  20.493  1.00 25.09  ? 417  SER B O   1 
ATOM   8088  C  CB  . SER B 1 408 ? 6.808   71.529  20.082  1.00 23.39  ? 417  SER B CB  1 
ATOM   8089  O  OG  . SER B 1 408 ? 7.966   71.740  19.285  1.00 30.83  ? 417  SER B OG  1 
ATOM   8090  N  N   . GLU B 1 409 ? 8.195   70.077  22.301  1.00 23.48  ? 418  GLU B N   1 
ATOM   8091  C  CA  . GLU B 1 409 ? 9.426   69.845  23.038  1.00 27.93  ? 418  GLU B CA  1 
ATOM   8092  C  C   . GLU B 1 409 ? 9.658   68.420  23.504  1.00 31.95  ? 418  GLU B C   1 
ATOM   8093  O  O   . GLU B 1 409 ? 10.795  67.943  23.471  1.00 29.99  ? 418  GLU B O   1 
ATOM   8094  C  CB  . GLU B 1 409 ? 9.458   70.684  24.321  1.00 31.34  ? 418  GLU B CB  1 
ATOM   8095  C  CG  . GLU B 1 409 ? 9.623   72.178  24.081  1.00 39.39  ? 418  GLU B CG  1 
ATOM   8096  C  CD  . GLU B 1 409 ? 9.637   72.948  25.422  1.00 52.24  ? 418  GLU B CD  1 
ATOM   8097  O  OE1 . GLU B 1 409 ? 9.951   74.150  25.405  1.00 57.06  ? 418  GLU B OE1 1 
ATOM   8098  O  OE2 . GLU B 1 409 ? 9.319   72.345  26.493  1.00 57.72  ? 418  GLU B OE2 1 
ATOM   8099  N  N   . LYS B 1 410 ? 8.603   67.756  23.978  1.00 26.15  ? 419  LYS B N   1 
ATOM   8100  C  CA  . LYS B 1 410 ? 8.765   66.414  24.529  1.00 22.29  ? 419  LYS B CA  1 
ATOM   8101  C  C   . LYS B 1 410 ? 8.665   65.289  23.563  1.00 22.00  ? 419  LYS B C   1 
ATOM   8102  O  O   . LYS B 1 410 ? 8.226   65.458  22.415  1.00 23.96  ? 419  LYS B O   1 
ATOM   8103  C  CB  . LYS B 1 410 ? 7.688   66.194  25.643  1.00 22.59  ? 419  LYS B CB  1 
ATOM   8104  C  CG  . LYS B 1 410 ? 7.829   67.212  26.752  1.00 23.56  ? 419  LYS B CG  1 
ATOM   8105  C  CD  . LYS B 1 410 ? 6.907   66.851  27.973  1.00 22.85  ? 419  LYS B CD  1 
ATOM   8106  C  CE  . LYS B 1 410 ? 6.807   68.022  28.921  1.00 25.95  ? 419  LYS B CE  1 
ATOM   8107  N  NZ  . LYS B 1 410 ? 8.059   68.207  29.739  1.00 25.72  ? 419  LYS B NZ  1 
ATOM   8108  N  N   . THR B 1 411 ? 9.139   64.095  24.003  1.00 22.24  ? 420  THR B N   1 
ATOM   8109  C  CA  . THR B 1 411 ? 8.920   62.874  23.284  1.00 21.09  ? 420  THR B CA  1 
ATOM   8110  C  C   . THR B 1 411 ? 8.204   61.929  24.258  1.00 22.14  ? 420  THR B C   1 
ATOM   8111  O  O   . THR B 1 411 ? 8.291   62.151  25.487  1.00 21.53  ? 420  THR B O   1 
ATOM   8112  C  CB  . THR B 1 411 ? 10.215  62.170  22.799  1.00 26.26  ? 420  THR B CB  1 
ATOM   8113  O  OG1 . THR B 1 411 ? 11.121  62.030  23.900  1.00 25.26  ? 420  THR B OG1 1 
ATOM   8114  C  CG2 . THR B 1 411 ? 10.881  62.954  21.670  1.00 23.60  ? 420  THR B CG2 1 
ATOM   8115  N  N   . ALA B 1 412 ? 7.526   60.917  23.739  1.00 21.36  ? 421  ALA B N   1 
ATOM   8116  C  CA  . ALA B 1 412 ? 6.890   59.888  24.594  1.00 21.91  ? 421  ALA B CA  1 
ATOM   8117  C  C   . ALA B 1 412 ? 7.173   58.609  23.881  1.00 23.42  ? 421  ALA B C   1 
ATOM   8118  O  O   . ALA B 1 412 ? 7.034   58.528  22.655  1.00 22.18  ? 421  ALA B O   1 
ATOM   8119  C  CB  . ALA B 1 412 ? 5.378   60.109  24.717  1.00 20.75  ? 421  ALA B CB  1 
ATOM   8120  N  N   . GLU B 1 413 ? 7.571   57.565  24.597  1.00 20.56  ? 422  GLU B N   1 
ATOM   8121  C  CA  . GLU B 1 413 ? 7.897   56.321  23.892  1.00 20.38  ? 422  GLU B CA  1 
ATOM   8122  C  C   . GLU B 1 413 ? 6.668   55.664  23.342  1.00 21.66  ? 422  GLU B C   1 
ATOM   8123  O  O   . GLU B 1 413 ? 6.667   55.151  22.229  1.00 19.42  ? 422  GLU B O   1 
ATOM   8124  C  CB  . GLU B 1 413 ? 8.593   55.359  24.884  1.00 22.18  ? 422  GLU B CB  1 
ATOM   8125  C  CG  . GLU B 1 413 ? 9.912   55.965  25.396  1.00 25.96  ? 422  GLU B CG  1 
ATOM   8126  C  CD  . GLU B 1 413 ? 10.581  55.065  26.442  1.00 35.34  ? 422  GLU B CD  1 
ATOM   8127  O  OE1 . GLU B 1 413 ? 11.687  55.377  26.869  1.00 35.08  ? 422  GLU B OE1 1 
ATOM   8128  O  OE2 . GLU B 1 413 ? 9.965   54.042  26.838  1.00 39.19  ? 422  GLU B OE2 1 
ATOM   8129  N  N   . THR B 1 414 ? 5.564   55.645  24.146  1.00 20.20  ? 423  THR B N   1 
ATOM   8130  C  CA  . THR B 1 414 ? 4.316   55.015  23.667  1.00 19.67  ? 423  THR B CA  1 
ATOM   8131  C  C   . THR B 1 414 ? 3.139   55.994  23.934  1.00 21.94  ? 423  THR B C   1 
ATOM   8132  O  O   . THR B 1 414 ? 3.077   56.638  24.983  1.00 20.64  ? 423  THR B O   1 
ATOM   8133  C  CB  . THR B 1 414 ? 4.046   53.726  24.475  1.00 24.30  ? 423  THR B CB  1 
ATOM   8134  O  OG1 . THR B 1 414 ? 5.170   52.860  24.365  1.00 27.82  ? 423  THR B OG1 1 
ATOM   8135  C  CG2 . THR B 1 414 ? 2.803   53.000  24.017  1.00 26.23  ? 423  THR B CG2 1 
ATOM   8136  N  N   . VAL B 1 415 ? 2.217   56.088  22.983  1.00 18.98  ? 424  VAL B N   1 
ATOM   8137  C  CA  . VAL B 1 415 ? 1.062   56.887  23.183  1.00 17.57  ? 424  VAL B CA  1 
ATOM   8138  C  C   . VAL B 1 415 ? -0.093  55.931  23.385  1.00 19.35  ? 424  VAL B C   1 
ATOM   8139  O  O   . VAL B 1 415 ? -0.256  55.010  22.584  1.00 20.30  ? 424  VAL B O   1 
ATOM   8140  C  CB  . VAL B 1 415 ? 0.845   57.776  21.934  1.00 18.56  ? 424  VAL B CB  1 
ATOM   8141  C  CG1 . VAL B 1 415 ? -0.582  58.421  21.972  1.00 17.86  ? 424  VAL B CG1 1 
ATOM   8142  C  CG2 . VAL B 1 415 ? 1.966   58.857  21.884  1.00 18.92  ? 424  VAL B CG2 1 
ATOM   8143  N  N   . TYR B 1 416 ? -0.902  56.136  24.427  1.00 18.67  ? 425  TYR B N   1 
ATOM   8144  C  CA  . TYR B 1 416 ? -2.089  55.269  24.672  1.00 18.44  ? 425  TYR B CA  1 
ATOM   8145  C  C   . TYR B 1 416 ? -3.296  56.090  24.328  1.00 16.47  ? 425  TYR B C   1 
ATOM   8146  O  O   . TYR B 1 416 ? -3.438  57.183  24.828  1.00 21.64  ? 425  TYR B O   1 
ATOM   8147  C  CB  . TYR B 1 416 ? -2.172  54.871  26.198  1.00 16.31  ? 425  TYR B CB  1 
ATOM   8148  C  CG  . TYR B 1 416 ? -1.042  53.918  26.575  1.00 18.29  ? 425  TYR B CG  1 
ATOM   8149  C  CD1 . TYR B 1 416 ? -1.249  52.542  26.620  1.00 23.04  ? 425  TYR B CD1 1 
ATOM   8150  C  CD2 . TYR B 1 416 ? 0.211   54.399  26.929  1.00 17.41  ? 425  TYR B CD2 1 
ATOM   8151  C  CE1 . TYR B 1 416 ? -0.247  51.671  27.038  1.00 23.72  ? 425  TYR B CE1 1 
ATOM   8152  C  CE2 . TYR B 1 416 ? 1.229   53.534  27.334  1.00 21.81  ? 425  TYR B CE2 1 
ATOM   8153  C  CZ  . TYR B 1 416 ? 0.984   52.170  27.405  1.00 23.25  ? 425  TYR B CZ  1 
ATOM   8154  O  OH  . TYR B 1 416 ? 1.967   51.326  27.911  1.00 21.42  ? 425  TYR B OH  1 
ATOM   8155  N  N   . GLN B 1 417 ? -4.163  55.583  23.455  1.00 17.14  ? 426  GLN B N   1 
ATOM   8156  C  CA  . GLN B 1 417 ? -5.375  56.313  23.077  1.00 14.93  ? 426  GLN B CA  1 
ATOM   8157  C  C   . GLN B 1 417 ? -6.487  55.736  23.934  1.00 16.91  ? 426  GLN B C   1 
ATOM   8158  O  O   . GLN B 1 417 ? -6.802  54.545  23.819  1.00 19.91  ? 426  GLN B O   1 
ATOM   8159  C  CB  . GLN B 1 417 ? -5.629  56.085  21.549  1.00 17.54  ? 426  GLN B CB  1 
ATOM   8160  C  CG  . GLN B 1 417 ? -6.989  56.700  21.104  1.00 18.93  ? 426  GLN B CG  1 
ATOM   8161  C  CD  . GLN B 1 417 ? -7.179  56.515  19.612  1.00 24.49  ? 426  GLN B CD  1 
ATOM   8162  O  OE1 . GLN B 1 417 ? -6.348  55.898  18.924  1.00 24.28  ? 426  GLN B OE1 1 
ATOM   8163  N  NE2 . GLN B 1 417 ? -8.274  57.037  19.075  1.00 23.99  ? 426  GLN B NE2 1 
ATOM   8164  N  N   . ILE B 1 418 ? -7.081  56.561  24.777  1.00 16.09  ? 427  ILE B N   1 
ATOM   8165  C  CA  . ILE B 1 418 ? -8.098  56.050  25.650  1.00 17.41  ? 427  ILE B CA  1 
ATOM   8166  C  C   . ILE B 1 418 ? -9.487  56.278  25.100  1.00 17.21  ? 427  ILE B C   1 
ATOM   8167  O  O   . ILE B 1 418 ? -9.850  57.406  24.813  1.00 20.72  ? 427  ILE B O   1 
ATOM   8168  C  CB  . ILE B 1 418 ? -7.973  56.720  27.070  1.00 17.55  ? 427  ILE B CB  1 
ATOM   8169  C  CG1 . ILE B 1 418 ? -6.509  56.598  27.631  1.00 18.42  ? 427  ILE B CG1 1 
ATOM   8170  C  CG2 . ILE B 1 418 ? -9.017  56.072  28.035  1.00 19.90  ? 427  ILE B CG2 1 
ATOM   8171  C  CD1 . ILE B 1 418 ? -6.014  55.139  27.829  1.00 17.51  ? 427  ILE B CD1 1 
ATOM   8172  N  N   . GLY B 1 419 ? -10.271 55.189  24.971  1.00 17.15  ? 428  GLY B N   1 
ATOM   8173  C  CA  . GLY B 1 419 ? -11.659 55.327  24.524  1.00 18.13  ? 428  GLY B CA  1 
ATOM   8174  C  C   . GLY B 1 419 ? -11.704 55.512  23.002  1.00 22.12  ? 428  GLY B C   1 
ATOM   8175  O  O   . GLY B 1 419 ? -10.694 55.670  22.333  1.00 20.76  ? 428  GLY B O   1 
ATOM   8176  N  N   . ASP B 1 420 ? -12.902 55.472  22.488  1.00 24.67  ? 429  ASP B N   1 
ATOM   8177  C  CA  . ASP B 1 420 ? -13.184 55.607  21.066  1.00 23.73  ? 429  ASP B CA  1 
ATOM   8178  C  C   . ASP B 1 420 ? -13.801 56.977  20.767  1.00 24.66  ? 429  ASP B C   1 
ATOM   8179  O  O   . ASP B 1 420 ? -14.495 57.527  21.604  1.00 26.10  ? 429  ASP B O   1 
ATOM   8180  C  CB  . ASP B 1 420 ? -14.233 54.530  20.714  1.00 28.53  ? 429  ASP B CB  1 
ATOM   8181  C  CG  . ASP B 1 420 ? -14.316 54.375  19.238  1.00 45.29  ? 429  ASP B CG  1 
ATOM   8182  O  OD1 . ASP B 1 420 ? -15.432 54.545  18.682  1.00 51.00  ? 429  ASP B OD1 1 
ATOM   8183  O  OD2 . ASP B 1 420 ? -13.273 54.087  18.623  1.00 49.09  ? 429  ASP B OD2 1 
ATOM   8184  N  N   . GLY B 1 421 ? -13.580 57.524  19.589  1.00 24.10  ? 430  GLY B N   1 
ATOM   8185  C  CA  . GLY B 1 421 ? -14.216 58.792  19.235  1.00 23.67  ? 430  GLY B CA  1 
ATOM   8186  C  C   . GLY B 1 421 ? -13.222 59.864  18.827  1.00 25.11  ? 430  GLY B C   1 
ATOM   8187  O  O   . GLY B 1 421 ? -13.532 60.696  17.985  1.00 23.72  ? 430  GLY B O   1 
ATOM   8188  N  N   . MET B 1 422 ? -12.008 59.874  19.408  1.00 22.81  ? 431  MET B N   1 
ATOM   8189  C  CA  . MET B 1 422 ? -11.049 60.884  18.960  1.00 23.25  ? 431  MET B CA  1 
ATOM   8190  C  C   . MET B 1 422 ? -10.677 60.568  17.446  1.00 25.32  ? 431  MET B C   1 
ATOM   8191  O  O   . MET B 1 422 ? -10.482 59.411  17.085  1.00 24.13  ? 431  MET B O   1 
ATOM   8192  C  CB  . MET B 1 422 ? -9.811  60.878  19.859  1.00 23.09  ? 431  MET B CB  1 
ATOM   8193  C  CG  . MET B 1 422 ? -8.843  62.023  19.520  1.00 21.06  ? 431  MET B CG  1 
ATOM   8194  S  SD  . MET B 1 422 ? -7.575  62.182  20.801  1.00 21.97  ? 431  MET B SD  1 
ATOM   8195  C  CE  . MET B 1 422 ? -8.583  62.800  22.140  1.00 16.90  ? 431  MET B CE  1 
ATOM   8196  N  N   . LYS B 1 423 ? -10.614 61.602  16.591  1.00 24.55  ? 432  LYS B N   1 
ATOM   8197  C  CA  . LYS B 1 423 ? -10.318 61.420  15.152  1.00 23.98  ? 432  LYS B CA  1 
ATOM   8198  C  C   . LYS B 1 423 ? -8.922  60.938  14.967  1.00 25.70  ? 432  LYS B C   1 
ATOM   8199  O  O   . LYS B 1 423 ? -8.012  61.336  15.688  1.00 23.25  ? 432  LYS B O   1 
ATOM   8200  C  CB  . LYS B 1 423 ? -10.453 62.790  14.433  1.00 25.52  ? 432  LYS B CB  1 
ATOM   8201  C  CG  . LYS B 1 423 ? -11.914 63.335  14.429  1.00 29.12  ? 432  LYS B CG  1 
ATOM   8202  C  CD  . LYS B 1 423 ? -12.906 62.280  14.021  1.00 43.04  ? 432  LYS B CD  1 
ATOM   8203  C  CE  . LYS B 1 423 ? -14.327 62.841  14.034  1.00 60.50  ? 432  LYS B CE  1 
ATOM   8204  N  NZ  . LYS B 1 423 ? -15.242 62.047  14.905  1.00 69.31  ? 432  LYS B NZ  1 
ATOM   8205  N  N   . ASP B 1 424 ? -8.710  60.087  13.968  1.00 24.80  ? 433  ASP B N   1 
ATOM   8206  C  CA  . ASP B 1 424 ? -7.391  59.584  13.648  1.00 23.34  ? 433  ASP B CA  1 
ATOM   8207  C  C   . ASP B 1 424 ? -6.392  60.675  13.456  1.00 26.55  ? 433  ASP B C   1 
ATOM   8208  O  O   . ASP B 1 424 ? -5.244  60.538  13.867  1.00 27.19  ? 433  ASP B O   1 
ATOM   8209  C  CB  . ASP B 1 424 ? -7.438  58.823  12.325  1.00 27.73  ? 433  ASP B CB  1 
ATOM   8210  C  CG  . ASP B 1 424 ? -8.093  57.463  12.395  1.00 37.00  ? 433  ASP B CG  1 
ATOM   8211  O  OD1 . ASP B 1 424 ? -8.286  56.945  13.527  1.00 38.79  ? 433  ASP B OD1 1 
ATOM   8212  O  OD2 . ASP B 1 424 ? -8.426  56.910  11.324  1.00 35.96  ? 433  ASP B OD2 1 
ATOM   8213  N  N   . SER B 1 425 ? -6.794  61.787  12.849  1.00 25.11  ? 434  SER B N   1 
ATOM   8214  C  CA  . SER B 1 425 ? -5.813  62.818  12.566  1.00 26.50  ? 434  SER B CA  1 
ATOM   8215  C  C   . SER B 1 425 ? -5.304  63.499  13.816  1.00 25.19  ? 434  SER B C   1 
ATOM   8216  O  O   . SER B 1 425 ? -4.174  63.953  13.843  1.00 23.64  ? 434  SER B O   1 
ATOM   8217  C  CB  . SER B 1 425 ? -6.423  63.875  11.635  1.00 27.96  ? 434  SER B CB  1 
ATOM   8218  O  OG  . SER B 1 425 ? -7.512  64.536  12.270  1.00 31.42  ? 434  SER B OG  1 
ATOM   8219  N  N   . VAL B 1 426 ? -6.156  63.568  14.871  1.00 22.33  ? 435  VAL B N   1 
ATOM   8220  C  CA  . VAL B 1 426 ? -5.795  64.218  16.149  1.00 19.27  ? 435  VAL B CA  1 
ATOM   8221  C  C   . VAL B 1 426 ? -4.847  63.293  16.906  1.00 19.15  ? 435  VAL B C   1 
ATOM   8222  O  O   . VAL B 1 426 ? -3.793  63.753  17.302  1.00 22.63  ? 435  VAL B O   1 
ATOM   8223  C  CB  . VAL B 1 426 ? -7.122  64.457  16.911  1.00 23.22  ? 435  VAL B CB  1 
ATOM   8224  C  CG1 . VAL B 1 426 ? -6.866  64.971  18.328  1.00 19.87  ? 435  VAL B CG1 1 
ATOM   8225  C  CG2 . VAL B 1 426 ? -8.009  65.464  16.117  1.00 22.90  ? 435  VAL B CG2 1 
ATOM   8226  N  N   . ILE B 1 427 ? -5.178  61.986  17.066  1.00 17.60  ? 436  ILE B N   1 
ATOM   8227  C  CA  . ILE B 1 427 ? -4.266  61.138  17.813  1.00 20.03  ? 436  ILE B CA  1 
ATOM   8228  C  C   . ILE B 1 427 ? -2.952  60.996  17.014  1.00 22.41  ? 436  ILE B C   1 
ATOM   8229  O  O   . ILE B 1 427 ? -1.874  60.986  17.604  1.00 22.40  ? 436  ILE B O   1 
ATOM   8230  C  CB  . ILE B 1 427 ? -4.988  59.779  18.188  1.00 21.72  ? 436  ILE B CB  1 
ATOM   8231  C  CG1 . ILE B 1 427 ? -4.065  58.902  19.047  1.00 25.52  ? 436  ILE B CG1 1 
ATOM   8232  C  CG2 . ILE B 1 427 ? -5.477  59.053  16.935  1.00 23.15  ? 436  ILE B CG2 1 
ATOM   8233  C  CD1 . ILE B 1 427 ? -4.084  59.492  20.484  1.00 23.90  ? 436  ILE B CD1 1 
ATOM   8234  N  N   A ASN B 1 428 ? -3.014  60.934  15.646  0.58 21.66  ? 437  ASN B N   1 
ATOM   8235  N  N   B ASN B 1 428 ? -3.030  60.911  15.686  0.42 23.22  ? 437  ASN B N   1 
ATOM   8236  C  CA  A ASN B 1 428 ? -1.769  60.830  14.876  0.58 21.35  ? 437  ASN B CA  1 
ATOM   8237  C  CA  B ASN B 1 428 ? -1.803  60.730  14.923  0.42 23.41  ? 437  ASN B CA  1 
ATOM   8238  C  C   A ASN B 1 428 ? -0.912  62.108  14.999  0.58 19.81  ? 437  ASN B C   1 
ATOM   8239  C  C   B ASN B 1 428 ? -0.974  62.028  14.956  0.42 22.50  ? 437  ASN B C   1 
ATOM   8240  O  O   A ASN B 1 428 ? 0.315   62.033  15.051  0.58 20.72  ? 437  ASN B O   1 
ATOM   8241  O  O   B ASN B 1 428 ? 0.247   61.968  14.887  0.42 23.48  ? 437  ASN B O   1 
ATOM   8242  C  CB  A ASN B 1 428 ? -2.050  60.597  13.393  0.58 22.28  ? 437  ASN B CB  1 
ATOM   8243  C  CB  B ASN B 1 428 ? -2.138  60.279  13.489  0.42 24.95  ? 437  ASN B CB  1 
ATOM   8244  C  CG  A ASN B 1 428 ? -0.757  60.531  12.629  0.58 30.32  ? 437  ASN B CG  1 
ATOM   8245  C  CG  B ASN B 1 428 ? -2.754  58.888  13.489  0.42 31.17  ? 437  ASN B CG  1 
ATOM   8246  O  OD1 A ASN B 1 428 ? 0.027   59.590  12.807  0.58 34.06  ? 437  ASN B OD1 1 
ATOM   8247  O  OD1 B ASN B 1 428 ? -3.517  58.526  12.578  0.42 33.28  ? 437  ASN B OD1 1 
ATOM   8248  N  ND2 A ASN B 1 428 ? -0.422  61.526  11.802  0.58 34.33  ? 437  ASN B ND2 1 
ATOM   8249  N  ND2 B ASN B 1 428 ? -2.509  58.031  14.502  0.42 33.75  ? 437  ASN B ND2 1 
ATOM   8250  N  N   . SER B 1 429 ? -1.551  63.278  15.060  1.00 19.73  ? 438  SER B N   1 
ATOM   8251  C  CA  . SER B 1 429 ? -0.822  64.522  15.222  1.00 23.21  ? 438  SER B CA  1 
ATOM   8252  C  C   . SER B 1 429 ? -0.035  64.461  16.551  1.00 23.40  ? 438  SER B C   1 
ATOM   8253  O  O   . SER B 1 429 ? 1.160   64.766  16.574  1.00 21.79  ? 438  SER B O   1 
ATOM   8254  C  CB  . SER B 1 429 ? -1.793  65.711  15.259  1.00 22.29  ? 438  SER B CB  1 
ATOM   8255  O  OG  . SER B 1 429 ? -1.071  66.874  15.612  1.00 23.33  ? 438  SER B OG  1 
ATOM   8256  N  N   . ILE B 1 430 ? -0.710  64.078  17.634  1.00 21.39  ? 439  ILE B N   1 
ATOM   8257  C  CA  . ILE B 1 430 ? -0.034  63.996  18.948  1.00 18.86  ? 439  ILE B CA  1 
ATOM   8258  C  C   . ILE B 1 430 ? 1.090   62.982  18.882  1.00 19.60  ? 439  ILE B C   1 
ATOM   8259  O  O   . ILE B 1 430 ? 2.200   63.268  19.372  1.00 19.54  ? 439  ILE B O   1 
ATOM   8260  C  CB  . ILE B 1 430 ? -1.114  63.616  20.004  1.00 18.10  ? 439  ILE B CB  1 
ATOM   8261  C  CG1 . ILE B 1 430 ? -2.060  64.818  20.217  1.00 17.67  ? 439  ILE B CG1 1 
ATOM   8262  C  CG2 . ILE B 1 430 ? -0.395  63.248  21.374  1.00 16.22  ? 439  ILE B CG2 1 
ATOM   8263  C  CD1 . ILE B 1 430 ? -3.399  64.366  20.827  1.00 18.59  ? 439  ILE B CD1 1 
ATOM   8264  N  N   . ALA B 1 431 ? 0.835   61.794  18.260  1.00 19.61  ? 440  ALA B N   1 
ATOM   8265  C  CA  . ALA B 1 431 ? 1.901   60.764  18.230  1.00 19.92  ? 440  ALA B CA  1 
ATOM   8266  C  C   . ALA B 1 431 ? 3.091   61.212  17.374  1.00 21.01  ? 440  ALA B C   1 
ATOM   8267  O  O   . ALA B 1 431 ? 4.240   60.878  17.681  1.00 21.76  ? 440  ALA B O   1 
ATOM   8268  C  CB  . ALA B 1 431 ? 1.369   59.448  17.714  1.00 19.53  ? 440  ALA B CB  1 
ATOM   8269  N  N   . SER B 1 432 ? 2.817   61.976  16.300  1.00 22.25  ? 441  SER B N   1 
ATOM   8270  C  CA  . SER B 1 432 ? 3.919   62.506  15.481  1.00 22.21  ? 441  SER B CA  1 
ATOM   8271  C  C   . SER B 1 432 ? 4.693   63.519  16.251  1.00 20.44  ? 441  SER B C   1 
ATOM   8272  O  O   . SER B 1 432 ? 5.913   63.452  16.267  1.00 20.97  ? 441  SER B O   1 
ATOM   8273  C  CB  . SER B 1 432 ? 3.379   63.196  14.215  1.00 25.42  ? 441  SER B CB  1 
ATOM   8274  O  OG  . SER B 1 432 ? 2.631   62.269  13.453  1.00 33.05  ? 441  SER B OG  1 
ATOM   8275  N  N   . SER B 1 433 ? 4.026   64.470  16.923  1.00 21.85  ? 442  SER B N   1 
ATOM   8276  C  CA  . SER B 1 433 ? 4.790   65.433  17.730  1.00 21.75  ? 442  SER B CA  1 
ATOM   8277  C  C   . SER B 1 433 ? 5.667   64.768  18.765  1.00 21.16  ? 442  SER B C   1 
ATOM   8278  O  O   . SER B 1 433 ? 6.792   65.227  19.063  1.00 20.69  ? 442  SER B O   1 
ATOM   8279  C  CB  . SER B 1 433 ? 3.845   66.370  18.487  1.00 22.78  ? 442  SER B CB  1 
ATOM   8280  O  OG  . SER B 1 433 ? 3.025   67.150  17.624  1.00 23.39  ? 442  SER B OG  1 
ATOM   8281  N  N   . LEU B 1 434 ? 5.148   63.655  19.356  1.00 21.69  ? 443  LEU B N   1 
ATOM   8282  C  CA  . LEU B 1 434 ? 5.891   63.034  20.455  1.00 17.48  ? 443  LEU B CA  1 
ATOM   8283  C  C   . LEU B 1 434 ? 6.961   62.091  19.968  1.00 20.85  ? 443  LEU B C   1 
ATOM   8284  O  O   . LEU B 1 434 ? 7.597   61.451  20.784  1.00 21.10  ? 443  LEU B O   1 
ATOM   8285  C  CB  . LEU B 1 434 ? 4.886   62.292  21.390  1.00 17.33  ? 443  LEU B CB  1 
ATOM   8286  C  CG  . LEU B 1 434 ? 4.003   63.285  22.227  1.00 18.46  ? 443  LEU B CG  1 
ATOM   8287  C  CD1 . LEU B 1 434 ? 2.850   62.454  22.894  1.00 19.61  ? 443  LEU B CD1 1 
ATOM   8288  C  CD2 . LEU B 1 434 ? 4.863   64.052  23.309  1.00 20.02  ? 443  LEU B CD2 1 
ATOM   8289  N  N   . SER B 1 435 ? 7.188   61.976  18.628  1.00 19.60  ? 444  SER B N   1 
ATOM   8290  C  CA  . SER B 1 435 ? 8.283   61.116  18.200  1.00 23.56  ? 444  SER B CA  1 
ATOM   8291  C  C   . SER B 1 435 ? 9.595   61.867  18.116  1.00 27.06  ? 444  SER B C   1 
ATOM   8292  O  O   . SER B 1 435 ? 10.630  61.226  17.877  1.00 26.37  ? 444  SER B O   1 
ATOM   8293  C  CB  . SER B 1 435 ? 7.977   60.464  16.851  1.00 27.97  ? 444  SER B CB  1 
ATOM   8294  O  OG  . SER B 1 435 ? 7.918   61.462  15.848  1.00 30.87  ? 444  SER B OG  1 
ATOM   8295  N  N   . LYS B 1 436 ? 9.608   63.196  18.266  1.00 26.40  ? 445  LYS B N   1 
ATOM   8296  C  CA  . LYS B 1 436 ? 10.901  63.893  18.230  1.00 31.18  ? 445  LYS B CA  1 
ATOM   8297  C  C   . LYS B 1 436 ? 10.891  65.183  18.970  1.00 30.40  ? 445  LYS B C   1 
ATOM   8298  O  O   . LYS B 1 436 ? 9.832   65.783  19.197  1.00 27.41  ? 445  LYS B O   1 
ATOM   8299  C  CB  . LYS B 1 436 ? 11.388  64.149  16.797  1.00 39.05  ? 445  LYS B CB  1 
ATOM   8300  C  CG  . LYS B 1 436 ? 10.425  64.962  15.961  1.00 44.77  ? 445  LYS B CG  1 
ATOM   8301  C  CD  . LYS B 1 436 ? 11.035  65.159  14.549  1.00 52.81  ? 445  LYS B CD  1 
ATOM   8302  C  CE  . LYS B 1 436 ? 10.389  66.322  13.843  0.00 0.00   ? 445  LYS B CE  1 
ATOM   8303  N  NZ  . LYS B 1 436 ? 10.971  66.524  12.491  0.00 0.00   ? 445  LYS B NZ  1 
ATOM   8304  N  N   . HIS B 1 437 ? 12.066  65.614  19.390  1.00 28.37  ? 446  HIS B N   1 
ATOM   8305  C  CA  . HIS B 1 437 ? 12.222  66.883  20.104  1.00 31.04  ? 446  HIS B CA  1 
ATOM   8306  C  C   . HIS B 1 437 ? 12.139  68.047  19.107  1.00 33.92  ? 446  HIS B C   1 
ATOM   8307  O  O   . HIS B 1 437 ? 12.576  67.896  17.965  1.00 34.18  ? 446  HIS B O   1 
ATOM   8308  C  CB  . HIS B 1 437 ? 13.554  66.910  20.806  1.00 32.38  ? 446  HIS B CB  1 
ATOM   8309  C  CG  . HIS B 1 437 ? 13.620  65.884  21.882  1.00 35.76  ? 446  HIS B CG  1 
ATOM   8310  N  ND1 . HIS B 1 437 ? 12.853  65.974  23.031  1.00 33.51  ? 446  HIS B ND1 1 
ATOM   8311  C  CD2 . HIS B 1 437 ? 14.336  64.737  21.977  1.00 36.08  ? 446  HIS B CD2 1 
ATOM   8312  C  CE1 . HIS B 1 437 ? 13.117  64.915  23.783  1.00 32.18  ? 446  HIS B CE1 1 
ATOM   8313  N  NE2 . HIS B 1 437 ? 14.005  64.149  23.175  1.00 36.62  ? 446  HIS B NE2 1 
ATOM   8314  N  N   . ASN B 1 438 ? 11.584  69.191  19.545  1.00 36.27  ? 447  ASN B N   1 
ATOM   8315  C  CA  . ASN B 1 438 ? 11.365  70.372  18.693  1.00 43.21  ? 447  ASN B CA  1 
ATOM   8316  C  C   . ASN B 1 438 ? 10.664  69.962  17.446  1.00 42.76  ? 447  ASN B C   1 
ATOM   8317  O  O   . ASN B 1 438 ? 11.034  70.345  16.322  1.00 37.97  ? 447  ASN B O   1 
ATOM   8318  C  CB  . ASN B 1 438 ? 12.658  71.093  18.375  1.00 49.44  ? 447  ASN B CB  1 
ATOM   8319  C  CG  . ASN B 1 438 ? 13.445  71.330  19.635  1.00 60.56  ? 447  ASN B CG  1 
ATOM   8320  O  OD1 . ASN B 1 438 ? 14.679  71.306  19.566  1.00 65.66  ? 447  ASN B OD1 1 
ATOM   8321  N  ND2 . ASN B 1 438 ? 12.814  71.511  20.843  1.00 59.08  ? 447  ASN B ND2 1 
ATOM   8322  N  N   . ALA B 1 439 ? 9.629   69.153  17.632  1.00 34.34  ? 448  ALA B N   1 
ATOM   8323  C  CA  . ALA B 1 439 ? 8.832   68.736  16.494  1.00 34.78  ? 448  ALA B CA  1 
ATOM   8324  C  C   . ALA B 1 439 ? 8.091   69.993  15.949  1.00 34.88  ? 448  ALA B C   1 
ATOM   8325  O  O   . ALA B 1 439 ? 7.710   70.865  16.739  1.00 32.91  ? 448  ALA B O   1 
ATOM   8326  C  CB  . ALA B 1 439 ? 7.790   67.660  16.922  1.00 32.65  ? 448  ALA B CB  1 
ATOM   8327  N  N   . PRO B 1 440 ? 7.876   70.097  14.626  1.00 38.43  ? 449  PRO B N   1 
ATOM   8328  C  CA  . PRO B 1 440 ? 7.170   71.293  14.132  1.00 43.98  ? 449  PRO B CA  1 
ATOM   8329  C  C   . PRO B 1 440 ? 5.712   71.243  14.558  1.00 48.27  ? 449  PRO B C   1 
ATOM   8330  O  O   . PRO B 1 440 ? 5.139   70.174  14.766  1.00 46.73  ? 449  PRO B O   1 
ATOM   8331  C  CB  . PRO B 1 440 ? 7.353   71.191  12.611  1.00 45.98  ? 449  PRO B CB  1 
ATOM   8332  C  CG  . PRO B 1 440 ? 7.398   69.713  12.378  1.00 43.38  ? 449  PRO B CG  1 
ATOM   8333  C  CD  . PRO B 1 440 ? 8.218   69.182  13.521  1.00 39.70  ? 449  PRO B CD  1 
ATOM   8334  N  N   . THR B 1 441 ? 5.124   72.415  14.699  1.00 54.50  ? 450  THR B N   1 
ATOM   8335  C  CA  . THR B 1 441 ? 3.729   72.522  15.049  1.00 62.80  ? 450  THR B CA  1 
ATOM   8336  C  C   . THR B 1 441 ? 3.047   72.749  13.744  1.00 68.06  ? 450  THR B C   1 
ATOM   8337  O  O   . THR B 1 441 ? 2.761   73.896  13.401  1.00 71.87  ? 450  THR B O   1 
ATOM   8338  C  CB  . THR B 1 441 ? 3.462   73.708  16.005  1.00 65.05  ? 450  THR B CB  1 
ATOM   8339  O  OG1 . THR B 1 441 ? 4.413   73.682  17.072  1.00 66.36  ? 450  THR B OG1 1 
ATOM   8340  C  CG2 . THR B 1 441 ? 2.082   73.649  16.573  1.00 63.40  ? 450  THR B CG2 1 
ATOM   8341  N  N   . GLU B 1 442 ? 2.809   71.708  12.972  1.00 69.50  ? 451  GLU B N   1 
ATOM   8342  C  CA  . GLU B 1 442 ? 2.127   72.007  11.738  1.00 74.26  ? 451  GLU B CA  1 
ATOM   8343  C  C   . GLU B 1 442 ? 1.040   70.971  11.496  1.00 76.74  ? 451  GLU B C   1 
ATOM   8344  O  O   . GLU B 1 442 ? -0.103  71.401  11.447  1.00 77.71  ? 451  GLU B O   1 
ATOM   8345  C  CB  . GLU B 1 442 ? 3.104   72.144  10.537  1.00 75.20  ? 451  GLU B CB  1 
ATOM   8346  C  CG  . GLU B 1 442 ? 3.867   73.461  10.537  0.00 0.00   ? 451  GLU B CG  1 
ATOM   8347  C  CD  . GLU B 1 442 ? 4.820   73.599  9.356   0.00 0.00   ? 451  GLU B CD  1 
ATOM   8348  O  OE1 . GLU B 1 442 ? 5.979   73.156  9.480   0.00 0.00   ? 451  GLU B OE1 1 
ATOM   8349  O  OE2 . GLU B 1 442 ? 4.414   74.156  8.311   0.00 0.00   ? 451  GLU B OE2 1 
ATOM   8350  N  N   . PRO B 1 443 ? 1.299   69.645  11.376  0.00 0.00   ? 452  PRO B N   1 
ATOM   8351  C  CA  . PRO B 1 443 ? 0.293   68.590  11.141  0.00 0.00   ? 452  PRO B CA  1 
ATOM   8352  C  C   . PRO B 1 443 ? -1.094  68.901  11.709  0.00 0.00   ? 452  PRO B C   1 
ATOM   8353  O  O   . PRO B 1 443 ? -2.099  68.474  11.141  0.00 0.00   ? 452  PRO B O   1 
ATOM   8354  C  CB  . PRO B 1 443 ? 0.947   67.347  11.759  0.00 0.00   ? 452  PRO B CB  1 
ATOM   8355  C  CG  . PRO B 1 443 ? 2.443   67.752  12.009  0.00 0.00   ? 452  PRO B CG  1 
ATOM   8356  C  CD  . PRO B 1 443 ? 2.640   69.053  11.312  0.00 0.00   ? 452  PRO B CD  1 
ATOM   8357  N  N   . ASP B 1 444 ? -1.149  69.625  12.834  0.00 0.00   ? 453  ASP B N   1 
ATOM   8358  C  CA  . ASP B 1 444 ? -2.404  70.085  13.427  0.00 0.00   ? 453  ASP B CA  1 
ATOM   8359  C  C   . ASP B 1 444 ? -3.035  71.148  12.516  0.00 0.00   ? 453  ASP B C   1 
ATOM   8360  O  O   . ASP B 1 444 ? -3.993  71.801  12.910  0.00 0.00   ? 453  ASP B O   1 
ATOM   8361  C  CB  . ASP B 1 444 ? -2.142  70.747  14.782  0.00 0.00   ? 453  ASP B CB  1 
ATOM   8362  C  CG  . ASP B 1 444 ? -1.340  69.907  15.732  0.00 0.00   ? 453  ASP B CG  1 
ATOM   8363  O  OD1 . ASP B 1 444 ? -0.101  69.946  15.654  0.00 0.00   ? 453  ASP B OD1 1 
ATOM   8364  O  OD2 . ASP B 1 444 ? -1.948  69.216  16.559  0.00 0.00   ? 453  ASP B OD2 1 
ATOM   8365  N  N   . ASN B 1 445 ? -2.477  71.331  11.313  1.00 158.79 ? 454  ASN B N   1 
ATOM   8366  C  CA  . ASN B 1 445 ? -2.919  72.309  10.331  1.00 157.75 ? 454  ASN B CA  1 
ATOM   8367  C  C   . ASN B 1 445 ? -4.198  71.872  9.641   1.00 157.49 ? 454  ASN B C   1 
ATOM   8368  O  O   . ASN B 1 445 ? -5.093  72.688  9.419   1.00 156.57 ? 454  ASN B O   1 
ATOM   8369  C  CB  . ASN B 1 445 ? -1.808  72.509  9.300   1.00 156.59 ? 454  ASN B CB  1 
ATOM   8370  C  CG  . ASN B 1 445 ? -0.941  73.705  9.599   0.00 0.00   ? 454  ASN B CG  1 
ATOM   8371  O  OD1 . ASN B 1 445 ? -0.338  74.275  8.689   0.00 0.00   ? 454  ASN B OD1 1 
ATOM   8372  N  ND2 . ASN B 1 445 ? -0.812  74.146  10.848  0.00 0.00   ? 454  ASN B ND2 1 
ATOM   8373  N  N   . SER B 1 446 ? -4.285  70.583  9.287   1.00 156.87 ? 455  SER B N   1 
ATOM   8374  C  CA  . SER B 1 446 ? -5.470  70.039  8.632   1.00 154.60 ? 455  SER B CA  1 
ATOM   8375  C  C   . SER B 1 446 ? -6.388  69.386  9.681   1.00 152.26 ? 455  SER B C   1 
ATOM   8376  O  O   . SER B 1 446 ? -5.896  68.753  10.620  1.00 151.15 ? 455  SER B O   1 
ATOM   8377  C  CB  . SER B 1 446 ? -5.062  69.014  7.575   1.00 153.25 ? 455  SER B CB  1 
ATOM   8378  O  OG  . SER B 1 446 ? -3.948  68.251  8.009   0.00 0.00   ? 455  SER B OG  1 
ATOM   8379  N  N   . GLY B 1 447 ? -7.711  69.544  9.530   1.00 148.24 ? 456  GLY B N   1 
ATOM   8380  C  CA  . GLY B 1 447 ? -8.646  68.948  10.475  1.00 141.94 ? 456  GLY B CA  1 
ATOM   8381  C  C   . GLY B 1 447 ? -10.009 68.783  9.843   1.00 136.40 ? 456  GLY B C   1 
ATOM   8382  O  O   . GLY B 1 447 ? -10.369 67.696  9.396   1.00 134.31 ? 456  GLY B O   1 
ATOM   8383  N  N   . SER B 1 448 ? -10.781 69.875  9.809   1.00 132.11 ? 457  SER B N   1 
ATOM   8384  C  CA  . SER B 1 448 ? -12.106 69.891  9.201   1.00 125.11 ? 457  SER B CA  1 
ATOM   8385  C  C   . SER B 1 448 ? -11.952 70.365  7.753   1.00 119.95 ? 457  SER B C   1 
ATOM   8386  O  O   . SER B 1 448 ? -12.170 71.536  7.459   1.00 118.23 ? 457  SER B O   1 
ATOM   8387  C  CB  . SER B 1 448 ? -13.036 70.825  9.972   1.00 122.79 ? 457  SER B CB  1 
ATOM   8388  O  OG  . SER B 1 448 ? -14.393 70.613  9.614   1.00 123.03 ? 457  SER B OG  1 
ATOM   8389  N  N   . ALA B 1 449 ? -11.579 69.454  6.847   1.00 113.53 ? 458  ALA B N   1 
ATOM   8390  C  CA  . ALA B 1 449 ? -11.382 69.779  5.434   1.00 103.11 ? 458  ALA B CA  1 
ATOM   8391  C  C   . ALA B 1 449 ? -12.592 70.520  4.821   1.00 94.14  ? 458  ALA B C   1 
ATOM   8392  O  O   . ALA B 1 449 ? -12.456 71.140  3.776   1.00 90.19  ? 458  ALA B O   1 
ATOM   8393  C  CB  . ALA B 1 449 ? -11.100 68.502  4.653   1.00 99.76  ? 458  ALA B CB  1 
ATOM   8394  N  N   . ALA B 1 450 ? -13.755 70.454  5.477   1.00 86.41  ? 459  ALA B N   1 
ATOM   8395  C  CA  . ALA B 1 450 ? -14.968 71.113  5.013   1.00 78.74  ? 459  ALA B CA  1 
ATOM   8396  C  C   . ALA B 1 450 ? -15.082 72.571  5.521   1.00 72.08  ? 459  ALA B C   1 
ATOM   8397  O  O   . ALA B 1 450 ? -15.497 73.454  4.781   1.00 69.53  ? 459  ALA B O   1 
ATOM   8398  C  CB  . ALA B 1 450 ? -16.178 70.338  5.483   1.00 75.36  ? 459  ALA B CB  1 
ATOM   8399  N  N   . GLY B 1 451 ? -14.709 72.803  6.774   1.00 62.90  ? 460  GLY B N   1 
ATOM   8400  C  CA  . GLY B 1 451 ? -14.842 74.133  7.342   1.00 50.79  ? 460  GLY B CA  1 
ATOM   8401  C  C   . GLY B 1 451 ? -14.004 75.221  6.697   1.00 36.87  ? 460  GLY B C   1 
ATOM   8402  O  O   . GLY B 1 451 ? -13.147 75.007  5.851   1.00 32.71  ? 460  GLY B O   1 
ATOM   8403  N  N   . LYS B 1 452 ? -14.311 76.433  7.089   1.00 28.64  ? 461  LYS B N   1 
ATOM   8404  C  CA  . LYS B 1 452 ? -13.537 77.567  6.677   1.00 26.98  ? 461  LYS B CA  1 
ATOM   8405  C  C   . LYS B 1 452 ? -12.121 77.455  7.331   1.00 23.25  ? 461  LYS B C   1 
ATOM   8406  O  O   . LYS B 1 452 ? -11.949 76.696  8.277   1.00 21.72  ? 461  LYS B O   1 
ATOM   8407  C  CB  . LYS B 1 452 ? -14.258 78.823  7.191   1.00 24.16  ? 461  LYS B CB  1 
ATOM   8408  C  CG  . LYS B 1 452 ? -15.663 78.877  6.554   1.00 26.25  ? 461  LYS B CG  1 
ATOM   8409  C  CD  . LYS B 1 452 ? -15.461 79.176  5.055   1.00 27.27  ? 461  LYS B CD  1 
ATOM   8410  C  CE  . LYS B 1 452 ? -16.782 79.150  4.297   1.00 39.88  ? 461  LYS B CE  1 
ATOM   8411  N  NZ  . LYS B 1 452 ? -16.641 79.943  3.038   1.00 50.50  ? 461  LYS B NZ  1 
ATOM   8412  N  N   . THR B 1 453 ? -11.125 78.241  6.831   1.00 22.42  ? 462  THR B N   1 
ATOM   8413  C  CA  . THR B 1 453 ? -9.799  78.221  7.436   1.00 20.90  ? 462  THR B CA  1 
ATOM   8414  C  C   . THR B 1 453 ? -9.364  79.648  7.713   1.00 18.82  ? 462  THR B C   1 
ATOM   8415  O  O   . THR B 1 453 ? -9.487  80.518  6.854   1.00 18.10  ? 462  THR B O   1 
ATOM   8416  C  CB  . THR B 1 453 ? -8.770  77.578  6.498   1.00 26.14  ? 462  THR B CB  1 
ATOM   8417  O  OG1 . THR B 1 453 ? -9.181  76.216  6.339   1.00 29.37  ? 462  THR B OG1 1 
ATOM   8418  C  CG2 . THR B 1 453 ? -7.313  77.612  7.102   1.00 25.50  ? 462  THR B CG2 1 
ATOM   8419  N  N   . VAL B 1 454 ? -8.860  79.890  8.912   1.00 16.83  ? 463  VAL B N   1 
ATOM   8420  C  CA  . VAL B 1 454 ? -8.421  81.235  9.319   1.00 16.78  ? 463  VAL B CA  1 
ATOM   8421  C  C   . VAL B 1 454 ? -6.973  81.126  9.819   1.00 18.18  ? 463  VAL B C   1 
ATOM   8422  O  O   . VAL B 1 454 ? -6.625  80.094  10.411  1.00 18.72  ? 463  VAL B O   1 
ATOM   8423  C  CB  . VAL B 1 454 ? -9.369  81.633  10.490  1.00 18.29  ? 463  VAL B CB  1 
ATOM   8424  C  CG1 . VAL B 1 454 ? -8.779  82.820  11.299  1.00 24.04  ? 463  VAL B CG1 1 
ATOM   8425  C  CG2 . VAL B 1 454 ? -10.737 82.011  9.906   1.00 17.13  ? 463  VAL B CG2 1 
ATOM   8426  N  N   . VAL B 1 455 ? -6.145  82.110  9.539   1.00 17.44  ? 464  VAL B N   1 
ATOM   8427  C  CA  . VAL B 1 455 ? -4.784  82.144  10.126  1.00 17.42  ? 464  VAL B CA  1 
ATOM   8428  C  C   . VAL B 1 455 ? -4.846  83.192  11.207  1.00 18.74  ? 464  VAL B C   1 
ATOM   8429  O  O   . VAL B 1 455 ? -5.342  84.315  10.940  1.00 16.11  ? 464  VAL B O   1 
ATOM   8430  C  CB  . VAL B 1 455 ? -3.702  82.494  9.090   1.00 19.02  ? 464  VAL B CB  1 
ATOM   8431  C  CG1 . VAL B 1 455 ? -2.371  82.787  9.812   1.00 17.79  ? 464  VAL B CG1 1 
ATOM   8432  C  CG2 . VAL B 1 455 ? -3.538  81.322  8.089   1.00 18.23  ? 464  VAL B CG2 1 
ATOM   8433  N  N   . ILE B 1 456 ? -4.408  82.853  12.427  1.00 16.17  ? 465  ILE B N   1 
ATOM   8434  C  CA  . ILE B 1 456 ? -4.364  83.782  13.562  1.00 17.15  ? 465  ILE B CA  1 
ATOM   8435  C  C   . ILE B 1 456 ? -2.892  84.147  13.789  1.00 16.19  ? 465  ILE B C   1 
ATOM   8436  O  O   . ILE B 1 456 ? -2.062  83.235  13.912  1.00 16.33  ? 465  ILE B O   1 
ATOM   8437  C  CB  . ILE B 1 456 ? -4.989  83.111  14.803  1.00 15.73  ? 465  ILE B CB  1 
ATOM   8438  C  CG1 . ILE B 1 456 ? -6.521  82.912  14.574  1.00 17.38  ? 465  ILE B CG1 1 
ATOM   8439  C  CG2 . ILE B 1 456 ? -4.737  83.979  16.106  1.00 18.21  ? 465  ILE B CG2 1 
ATOM   8440  C  CD1 . ILE B 1 456 ? -7.318  84.250  14.331  1.00 16.45  ? 465  ILE B CD1 1 
ATOM   8441  N  N   . ASP B 1 457 ? -2.568  85.441  13.839  1.00 14.94  ? 466  ASP B N   1 
ATOM   8442  C  CA  . ASP B 1 457 ? -1.164  85.860  13.968  1.00 14.76  ? 466  ASP B CA  1 
ATOM   8443  C  C   . ASP B 1 457 ? -0.940  86.692  15.211  1.00 17.63  ? 466  ASP B C   1 
ATOM   8444  O  O   . ASP B 1 457 ? -1.268  87.901  15.231  1.00 17.05  ? 466  ASP B O   1 
ATOM   8445  C  CB  . ASP B 1 457 ? -0.814  86.692  12.721  1.00 17.59  ? 466  ASP B CB  1 
ATOM   8446  C  CG  . ASP B 1 457 ? 0.549   87.316  12.824  1.00 21.34  ? 466  ASP B CG  1 
ATOM   8447  O  OD1 . ASP B 1 457 ? 0.670   88.530  12.515  1.00 20.60  ? 466  ASP B OD1 1 
ATOM   8448  O  OD2 . ASP B 1 457 ? 1.509   86.601  13.241  1.00 18.71  ? 466  ASP B OD2 1 
ATOM   8449  N  N   . PRO B 1 458 ? -0.460  86.089  16.302  1.00 17.65  ? 467  PRO B N   1 
ATOM   8450  C  CA  . PRO B 1 458 ? -0.199  86.895  17.519  1.00 18.82  ? 467  PRO B CA  1 
ATOM   8451  C  C   . PRO B 1 458 ? 1.074   87.740  17.296  1.00 18.04  ? 467  PRO B C   1 
ATOM   8452  O  O   . PRO B 1 458 ? 2.158   87.173  17.106  1.00 17.35  ? 467  PRO B O   1 
ATOM   8453  C  CB  . PRO B 1 458 ? -0.004  85.865  18.628  1.00 18.48  ? 467  PRO B CB  1 
ATOM   8454  C  CG  . PRO B 1 458 ? 0.110   84.534  17.987  1.00 18.62  ? 467  PRO B CG  1 
ATOM   8455  C  CD  . PRO B 1 458 ? -0.169  84.663  16.480  1.00 20.32  ? 467  PRO B CD  1 
ATOM   8456  N  N   . GLY B 1 459 ? 0.929   89.073  17.331  1.00 16.05  ? 468  GLY B N   1 
ATOM   8457  C  CA  . GLY B 1 459 ? 2.044   89.957  17.041  1.00 15.49  ? 468  GLY B CA  1 
ATOM   8458  C  C   . GLY B 1 459 ? 3.275   89.750  17.905  1.00 21.18  ? 468  GLY B C   1 
ATOM   8459  O  O   . GLY B 1 459 ? 3.193   89.388  19.081  1.00 16.90  ? 468  GLY B O   1 
ATOM   8460  N  N   . HIS B 1 460 ? 4.412   89.996  17.285  1.00 19.59  ? 469  HIS B N   1 
ATOM   8461  C  CA  . HIS B 1 460 ? 5.692   89.955  18.000  1.00 21.59  ? 469  HIS B CA  1 
ATOM   8462  C  C   . HIS B 1 460 ? 5.994   88.553  18.500  1.00 21.79  ? 469  HIS B C   1 
ATOM   8463  O  O   . HIS B 1 460 ? 5.444   87.582  17.993  1.00 18.57  ? 469  HIS B O   1 
ATOM   8464  C  CB  . HIS B 1 460 ? 5.680   90.984  19.147  1.00 21.94  ? 469  HIS B CB  1 
ATOM   8465  C  CG  . HIS B 1 460 ? 5.259   92.336  18.669  1.00 23.92  ? 469  HIS B CG  1 
ATOM   8466  N  ND1 . HIS B 1 460 ? 6.084   93.158  17.941  1.00 26.41  ? 469  HIS B ND1 1 
ATOM   8467  C  CD2 . HIS B 1 460 ? 4.072   92.994  18.731  1.00 23.53  ? 469  HIS B CD2 1 
ATOM   8468  C  CE1 . HIS B 1 460 ? 5.388   94.255  17.619  1.00 30.09  ? 469  HIS B CE1 1 
ATOM   8469  N  NE2 . HIS B 1 460 ? 4.181   94.226  18.065  1.00 27.29  ? 469  HIS B NE2 1 
ATOM   8470  N  N   . GLY B 1 461 ? 6.948   88.421  19.466  1.00 19.79  ? 470  GLY B N   1 
ATOM   8471  C  CA  . GLY B 1 461 ? 7.313   87.077  19.919  1.00 21.62  ? 470  GLY B CA  1 
ATOM   8472  C  C   . GLY B 1 461 ? 8.848   86.990  20.083  1.00 26.56  ? 470  GLY B C   1 
ATOM   8473  O  O   . GLY B 1 461 ? 9.582   87.655  19.350  1.00 22.80  ? 470  GLY B O   1 
ATOM   8474  N  N   . GLY B 1 462 ? 9.310   86.170  21.046  1.00 24.37  ? 471  GLY B N   1 
ATOM   8475  C  CA  . GLY B 1 462 ? 10.748  85.901  21.227  1.00 26.92  ? 471  GLY B CA  1 
ATOM   8476  C  C   . GLY B 1 462 ? 11.523  87.145  21.530  1.00 26.72  ? 471  GLY B C   1 
ATOM   8477  O  O   . GLY B 1 462 ? 11.248  87.853  22.485  1.00 28.32  ? 471  GLY B O   1 
ATOM   8478  N  N   . SER B 1 463 ? 12.526  87.449  20.664  1.00 29.27  ? 472  SER B N   1 
ATOM   8479  C  CA  . SER B 1 463 ? 13.313  88.645  20.904  1.00 27.44  ? 472  SER B CA  1 
ATOM   8480  C  C   . SER B 1 463 ? 12.588  89.905  20.763  1.00 28.52  ? 472  SER B C   1 
ATOM   8481  O  O   . SER B 1 463 ? 13.070  90.930  21.245  1.00 30.18  ? 472  SER B O   1 
ATOM   8482  C  CB  . SER B 1 463 ? 14.504  88.707  19.952  1.00 30.94  ? 472  SER B CB  1 
ATOM   8483  O  OG  . SER B 1 463 ? 15.217  87.493  20.062  1.00 33.88  ? 472  SER B OG  1 
ATOM   8484  N  N   . ASP B 1 464 ? 11.441  89.914  20.080  1.00 27.93  ? 473  ASP B N   1 
ATOM   8485  C  CA  . ASP B 1 464 ? 10.694  91.167  19.948  1.00 25.38  ? 473  ASP B CA  1 
ATOM   8486  C  C   . ASP B 1 464 ? 9.533   91.110  20.973  1.00 27.12  ? 473  ASP B C   1 
ATOM   8487  O  O   . ASP B 1 464 ? 8.565   90.366  20.791  1.00 24.02  ? 473  ASP B O   1 
ATOM   8488  C  CB  . ASP B 1 464 ? 10.150  91.293  18.539  1.00 23.67  ? 473  ASP B CB  1 
ATOM   8489  C  CG  . ASP B 1 464 ? 9.310   92.551  18.334  1.00 27.93  ? 473  ASP B CG  1 
ATOM   8490  O  OD1 . ASP B 1 464 ? 9.246   93.392  19.254  1.00 29.76  ? 473  ASP B OD1 1 
ATOM   8491  O  OD2 . ASP B 1 464 ? 8.748   92.710  17.243  1.00 30.12  ? 473  ASP B OD2 1 
ATOM   8492  N  N   . SER B 1 465 ? 9.669   91.829  22.089  1.00 29.60  ? 474  SER B N   1 
ATOM   8493  C  CA  . SER B 1 465 ? 8.632   91.759  23.112  1.00 33.75  ? 474  SER B CA  1 
ATOM   8494  C  C   . SER B 1 465 ? 7.401   92.671  22.726  1.00 33.91  ? 474  SER B C   1 
ATOM   8495  O  O   . SER B 1 465 ? 6.327   92.544  23.331  1.00 34.12  ? 474  SER B O   1 
ATOM   8496  C  CB  . SER B 1 465 ? 9.223   92.196  24.450  1.00 37.62  ? 474  SER B CB  1 
ATOM   8497  O  OG  . SER B 1 465 ? 9.573   93.562  24.280  1.00 46.50  ? 474  SER B OG  1 
ATOM   8498  N  N   . GLY B 1 466 ? 7.583   93.532  21.701  1.00 32.47  ? 475  GLY B N   1 
ATOM   8499  C  CA  . GLY B 1 466 ? 6.549   94.471  21.295  1.00 35.84  ? 475  GLY B CA  1 
ATOM   8500  C  C   . GLY B 1 466 ? 6.487   95.533  22.365  1.00 40.68  ? 475  GLY B C   1 
ATOM   8501  O  O   . GLY B 1 466 ? 7.422   95.658  23.169  1.00 39.05  ? 475  GLY B O   1 
ATOM   8502  N  N   . ALA B 1 467 ? 5.400   96.302  22.406  1.00 40.81  ? 476  ALA B N   1 
ATOM   8503  C  CA  . ALA B 1 467 ? 5.255   97.357  23.431  1.00 43.52  ? 476  ALA B CA  1 
ATOM   8504  C  C   . ALA B 1 467 ? 5.217   96.764  24.850  1.00 45.70  ? 476  ALA B C   1 
ATOM   8505  O  O   . ALA B 1 467 ? 4.689   95.669  25.079  1.00 44.42  ? 476  ALA B O   1 
ATOM   8506  C  CB  . ALA B 1 467 ? 3.974   98.161  23.167  1.00 42.49  ? 476  ALA B CB  1 
ATOM   8507  N  N   . THR B 1 468 ? 5.806   97.470  25.815  1.00 48.05  ? 477  THR B N   1 
ATOM   8508  C  CA  . THR B 1 468 ? 5.801   96.968  27.200  1.00 50.95  ? 477  THR B CA  1 
ATOM   8509  C  C   . THR B 1 468 ? 5.400   98.102  28.175  1.00 52.08  ? 477  THR B C   1 
ATOM   8510  O  O   . THR B 1 468 ? 5.433   99.270  27.809  1.00 52.55  ? 477  THR B O   1 
ATOM   8511  C  CB  . THR B 1 468 ? 7.190   96.389  27.604  1.00 49.68  ? 477  THR B CB  1 
ATOM   8512  O  OG1 . THR B 1 468 ? 8.165   97.440  27.542  1.00 45.90  ? 477  THR B OG1 1 
ATOM   8513  C  CG2 . THR B 1 468 ? 7.624   95.236  26.710  1.00 47.80  ? 477  THR B CG2 1 
ATOM   8514  N  N   . SER B 1 469 ? 5.032   97.738  29.388  1.00 54.91  ? 478  SER B N   1 
ATOM   8515  C  CA  . SER B 1 469 ? 4.641   98.690  30.414  1.00 60.03  ? 478  SER B CA  1 
ATOM   8516  C  C   . SER B 1 469 ? 4.710   97.966  31.778  1.00 59.38  ? 478  SER B C   1 
ATOM   8517  O  O   . SER B 1 469 ? 4.879   96.749  31.805  1.00 56.37  ? 478  SER B O   1 
ATOM   8518  C  CB  . SER B 1 469 ? 3.220   99.210  30.147  1.00 60.13  ? 478  SER B CB  1 
ATOM   8519  O  OG  . SER B 1 469 ? 2.230   98.348  30.685  1.00 59.45  ? 478  SER B OG  1 
ATOM   8520  N  N   . GLY B 1 470 ? 4.589   98.716  32.897  1.00 59.13  ? 479  GLY B N   1 
ATOM   8521  C  CA  . GLY B 1 470 ? 4.627   98.106  34.221  1.00 59.70  ? 479  GLY B CA  1 
ATOM   8522  C  C   . GLY B 1 470 ? 3.217   97.810  34.705  1.00 60.68  ? 479  GLY B C   1 
ATOM   8523  O  O   . GLY B 1 470 ? 3.029   97.371  35.836  1.00 60.81  ? 479  GLY B O   1 
ATOM   8524  N  N   . LEU B 1 471 ? 2.197   98.057  33.836  1.00 59.78  ? 480  LEU B N   1 
ATOM   8525  C  CA  . LEU B 1 471 ? 0.800   97.784  34.211  1.00 56.99  ? 480  LEU B CA  1 
ATOM   8526  C  C   . LEU B 1 471 ? 0.595   96.289  34.416  1.00 55.62  ? 480  LEU B C   1 
ATOM   8527  O  O   . LEU B 1 471 ? 1.321   95.470  33.841  1.00 55.83  ? 480  LEU B O   1 
ATOM   8528  C  CB  . LEU B 1 471 ? -0.212  98.297  33.144  1.00 54.86  ? 480  LEU B CB  1 
ATOM   8529  C  CG  . LEU B 1 471 ? -0.245  99.809  33.016  1.00 57.74  ? 480  LEU B CG  1 
ATOM   8530  C  CD1 . LEU B 1 471 ? -1.153  100.286 31.894  1.00 56.92  ? 480  LEU B CD1 1 
ATOM   8531  C  CD2 . LEU B 1 471 ? -0.724  100.399 34.365  1.00 58.43  ? 480  LEU B CD2 1 
ATOM   8532  N  N   . ASN B 1 472 ? -0.392  95.930  35.236  1.00 56.89  ? 481  ASN B N   1 
ATOM   8533  C  CA  . ASN B 1 472 ? -0.740  94.533  35.499  1.00 60.92  ? 481  ASN B CA  1 
ATOM   8534  C  C   . ASN B 1 472 ? 0.487   93.698  35.986  1.00 62.51  ? 481  ASN B C   1 
ATOM   8535  O  O   . ASN B 1 472 ? 0.613   92.506  35.676  1.00 59.94  ? 481  ASN B O   1 
ATOM   8536  C  CB  . ASN B 1 472 ? -1.375  93.927  34.221  1.00 61.74  ? 481  ASN B CB  1 
ATOM   8537  C  CG  . ASN B 1 472 ? -2.741  94.537  33.848  1.00 60.24  ? 481  ASN B CG  1 
ATOM   8538  O  OD1 . ASN B 1 472 ? -3.425  94.007  32.942  1.00 57.03  ? 481  ASN B OD1 1 
ATOM   8539  N  ND2 . ASN B 1 472 ? -3.211  95.647  34.450  1.00 52.81  ? 481  ASN B ND2 1 
ATOM   8540  N  N   . GLY B 1 473 ? 1.376   94.373  36.772  1.00 64.17  ? 482  GLY B N   1 
ATOM   8541  C  CA  . GLY B 1 473 ? 2.579   93.753  37.319  1.00 64.16  ? 482  GLY B CA  1 
ATOM   8542  C  C   . GLY B 1 473 ? 3.566   93.457  36.215  1.00 63.63  ? 482  GLY B C   1 
ATOM   8543  O  O   . GLY B 1 473 ? 4.211   92.415  36.220  1.00 65.33  ? 482  GLY B O   1 
ATOM   8544  N  N   . GLY B 1 474 ? 3.691   94.388  35.268  1.00 62.33  ? 483  GLY B N   1 
ATOM   8545  C  CA  . GLY B 1 474 ? 4.576   94.170  34.137  1.00 62.14  ? 483  GLY B CA  1 
ATOM   8546  C  C   . GLY B 1 474 ? 3.777   93.515  33.024  1.00 60.00  ? 483  GLY B C   1 
ATOM   8547  O  O   . GLY B 1 474 ? 3.142   92.461  33.187  1.00 56.42  ? 483  GLY B O   1 
ATOM   8548  N  N   . ALA B 1 475 ? 3.817   94.152  31.872  1.00 56.64  ? 484  ALA B N   1 
ATOM   8549  C  CA  . ALA B 1 475 ? 3.083   93.687  30.724  1.00 50.96  ? 484  ALA B CA  1 
ATOM   8550  C  C   . ALA B 1 475 ? 3.953   93.684  29.470  1.00 46.89  ? 484  ALA B C   1 
ATOM   8551  O  O   . ALA B 1 475 ? 4.673   94.658  29.220  1.00 42.40  ? 484  ALA B O   1 
ATOM   8552  C  CB  . ALA B 1 475 ? 1.900   94.603  30.512  1.00 47.93  ? 484  ALA B CB  1 
ATOM   8553  N  N   . GLN B 1 476 ? 3.895   92.602  28.684  1.00 40.91  ? 485  GLN B N   1 
ATOM   8554  C  CA  . GLN B 1 476 ? 4.634   92.583  27.427  1.00 41.09  ? 485  GLN B CA  1 
ATOM   8555  C  C   . GLN B 1 476 ? 3.666   92.230  26.310  1.00 36.13  ? 485  GLN B C   1 
ATOM   8556  O  O   . GLN B 1 476 ? 2.986   91.192  26.391  1.00 31.63  ? 485  GLN B O   1 
ATOM   8557  C  CB  . GLN B 1 476 ? 5.764   91.546  27.398  1.00 38.70  ? 485  GLN B CB  1 
ATOM   8558  C  CG  . GLN B 1 476 ? 6.783   91.716  28.519  1.00 45.59  ? 485  GLN B CG  1 
ATOM   8559  C  CD  . GLN B 1 476 ? 7.899   90.741  28.287  1.00 53.72  ? 485  GLN B CD  1 
ATOM   8560  O  OE1 . GLN B 1 476 ? 7.872   89.611  28.747  1.00 61.42  ? 485  GLN B OE1 1 
ATOM   8561  N  NE2 . GLN B 1 476 ? 8.890   91.134  27.503  1.00 62.32  ? 485  GLN B NE2 1 
ATOM   8562  N  N   . GLU B 1 477 ? 3.634   93.071  25.269  1.00 32.69  ? 486  GLU B N   1 
ATOM   8563  C  CA  . GLU B 1 477 ? 2.723   92.828  24.164  1.00 32.45  ? 486  GLU B CA  1 
ATOM   8564  C  C   . GLU B 1 477 ? 2.803   91.366  23.672  1.00 33.02  ? 486  GLU B C   1 
ATOM   8565  O  O   . GLU B 1 477 ? 1.765   90.730  23.507  1.00 32.32  ? 486  GLU B O   1 
ATOM   8566  C  CB  . GLU B 1 477 ? 3.018   93.780  22.993  1.00 32.57  ? 486  GLU B CB  1 
ATOM   8567  C  CG  . GLU B 1 477 ? 2.029   93.623  21.836  1.00 29.83  ? 486  GLU B CG  1 
ATOM   8568  C  CD  . GLU B 1 477 ? 2.273   94.619  20.736  1.00 41.91  ? 486  GLU B CD  1 
ATOM   8569  O  OE1 . GLU B 1 477 ? 1.573   94.556  19.668  1.00 33.14  ? 486  GLU B OE1 1 
ATOM   8570  O  OE2 . GLU B 1 477 ? 3.181   95.471  20.924  1.00 37.33  ? 486  GLU B OE2 1 
ATOM   8571  N  N   . LYS B 1 478 ? 4.026   90.810  23.451  1.00 30.54  ? 487  LYS B N   1 
ATOM   8572  C  CA  . LYS B 1 478 ? 4.086   89.463  22.858  1.00 25.88  ? 487  LYS B CA  1 
ATOM   8573  C  C   . LYS B 1 478 ? 3.365   88.425  23.698  1.00 23.17  ? 487  LYS B C   1 
ATOM   8574  O  O   . LYS B 1 478 ? 2.898   87.439  23.145  1.00 21.79  ? 487  LYS B O   1 
ATOM   8575  C  CB  . LYS B 1 478 ? 5.549   89.012  22.642  1.00 22.05  ? 487  LYS B CB  1 
ATOM   8576  C  CG  . LYS B 1 478 ? 6.321   88.969  23.991  1.00 23.99  ? 487  LYS B CG  1 
ATOM   8577  C  CD  . LYS B 1 478 ? 7.691   88.161  23.742  1.00 26.00  ? 487  LYS B CD  1 
ATOM   8578  C  CE  . LYS B 1 478 ? 8.553   88.020  25.011  1.00 29.09  ? 487  LYS B CE  1 
ATOM   8579  N  NZ  . LYS B 1 478 ? 9.698   87.105  24.693  1.00 26.56  ? 487  LYS B NZ  1 
ATOM   8580  N  N   . LYS B 1 479 ? 3.290   88.617  25.045  1.00 23.21  ? 488  LYS B N   1 
ATOM   8581  C  CA  . LYS B 1 479 ? 2.558   87.660  25.861  1.00 26.05  ? 488  LYS B CA  1 
ATOM   8582  C  C   . LYS B 1 479 ? 1.023   87.840  25.763  1.00 26.02  ? 488  LYS B C   1 
ATOM   8583  O  O   . LYS B 1 479 ? 0.290   86.852  25.725  1.00 24.61  ? 488  LYS B O   1 
ATOM   8584  C  CB  . LYS B 1 479 ? 2.940   87.827  27.364  1.00 31.50  ? 488  LYS B CB  1 
ATOM   8585  C  CG  . LYS B 1 479 ? 4.466   87.712  27.531  1.00 46.07  ? 488  LYS B CG  1 
ATOM   8586  C  CD  . LYS B 1 479 ? 4.826   87.010  28.817  1.00 56.62  ? 488  LYS B CD  1 
ATOM   8587  C  CE  . LYS B 1 479 ? 6.312   87.053  29.056  1.00 61.02  ? 488  LYS B CE  1 
ATOM   8588  N  NZ  . LYS B 1 479 ? 6.614   87.634  30.388  1.00 67.19  ? 488  LYS B NZ  1 
ATOM   8589  N  N   . TYR B 1 480 ? 0.549   89.104  25.791  1.00 26.08  ? 489  TYR B N   1 
ATOM   8590  C  CA  . TYR B 1 480 ? -0.888  89.383  25.705  1.00 22.06  ? 489  TYR B CA  1 
ATOM   8591  C  C   . TYR B 1 480 ? -1.386  88.966  24.362  1.00 20.24  ? 489  TYR B C   1 
ATOM   8592  O  O   . TYR B 1 480 ? -2.483  88.399  24.303  1.00 21.58  ? 489  TYR B O   1 
ATOM   8593  C  CB  . TYR B 1 480 ? -1.109  90.889  25.918  1.00 25.86  ? 489  TYR B CB  1 
ATOM   8594  C  CG  . TYR B 1 480 ? -1.239  91.215  27.396  1.00 33.78  ? 489  TYR B CG  1 
ATOM   8595  C  CD1 . TYR B 1 480 ? -0.110  91.354  28.207  1.00 35.89  ? 489  TYR B CD1 1 
ATOM   8596  C  CD2 . TYR B 1 480 ? -2.488  91.348  27.986  1.00 32.47  ? 489  TYR B CD2 1 
ATOM   8597  C  CE1 . TYR B 1 480 ? -0.238  91.618  29.578  1.00 35.57  ? 489  TYR B CE1 1 
ATOM   8598  C  CE2 . TYR B 1 480 ? -2.623  91.602  29.343  1.00 39.66  ? 489  TYR B CE2 1 
ATOM   8599  C  CZ  . TYR B 1 480 ? -1.501  91.744  30.135  1.00 39.06  ? 489  TYR B CZ  1 
ATOM   8600  O  OH  . TYR B 1 480 ? -1.713  92.054  31.453  1.00 38.24  ? 489  TYR B OH  1 
ATOM   8601  N  N   . THR B 1 481 ? -0.613  89.206  23.272  1.00 21.63  ? 490  THR B N   1 
ATOM   8602  C  CA  . THR B 1 481 ? -1.103  88.805  21.960  1.00 22.88  ? 490  THR B CA  1 
ATOM   8603  C  C   . THR B 1 481 ? -1.179  87.300  21.897  1.00 20.80  ? 490  THR B C   1 
ATOM   8604  O  O   . THR B 1 481 ? -2.136  86.762  21.358  1.00 20.77  ? 490  THR B O   1 
ATOM   8605  C  CB  . THR B 1 481 ? -0.223  89.282  20.776  1.00 18.76  ? 490  THR B CB  1 
ATOM   8606  O  OG1 . THR B 1 481 ? 1.085   88.728  20.913  1.00 25.09  ? 490  THR B OG1 1 
ATOM   8607  C  CG2 . THR B 1 481 ? -0.122  90.754  20.728  1.00 20.69  ? 490  THR B CG2 1 
ATOM   8608  N  N   . LEU B 1 482 ? -0.167  86.581  22.461  1.00 19.50  ? 491  LEU B N   1 
ATOM   8609  C  CA  . LEU B 1 482 ? -0.262  85.131  22.377  1.00 18.14  ? 491  LEU B CA  1 
ATOM   8610  C  C   . LEU B 1 482 ? -1.458  84.569  23.191  1.00 16.17  ? 491  LEU B C   1 
ATOM   8611  O  O   . LEU B 1 482 ? -2.197  83.724  22.696  1.00 18.06  ? 491  LEU B O   1 
ATOM   8612  C  CB  . LEU B 1 482 ? 1.050   84.476  22.913  1.00 18.31  ? 491  LEU B CB  1 
ATOM   8613  C  CG  . LEU B 1 482 ? 0.993   82.969  22.874  1.00 17.77  ? 491  LEU B CG  1 
ATOM   8614  C  CD1 . LEU B 1 482 ? 0.841   82.437  21.437  1.00 18.62  ? 491  LEU B CD1 1 
ATOM   8615  C  CD2 . LEU B 1 482 ? 2.386   82.460  23.480  1.00 23.00  ? 491  LEU B CD2 1 
ATOM   8616  N  N   . ASN B 1 483 ? -1.656  85.045  24.420  1.00 17.82  ? 492  ASN B N   1 
ATOM   8617  C  CA  . ASN B 1 483 ? -2.773  84.489  25.194  1.00 18.98  ? 492  ASN B CA  1 
ATOM   8618  C  C   . ASN B 1 483 ? -4.140  84.862  24.572  1.00 18.88  ? 492  ASN B C   1 
ATOM   8619  O  O   . ASN B 1 483 ? -5.058  84.051  24.590  1.00 17.59  ? 492  ASN B O   1 
ATOM   8620  C  CB  . ASN B 1 483 ? -2.692  85.003  26.621  1.00 22.45  ? 492  ASN B CB  1 
ATOM   8621  C  CG  . ASN B 1 483 ? -1.496  84.376  27.343  1.00 28.60  ? 492  ASN B CG  1 
ATOM   8622  O  OD1 . ASN B 1 483 ? -1.120  83.263  27.024  1.00 27.28  ? 492  ASN B OD1 1 
ATOM   8623  N  ND2 . ASN B 1 483 ? -0.863  85.077  28.285  1.00 28.25  ? 492  ASN B ND2 1 
ATOM   8624  N  N   . THR B 1 484 ? -4.235  86.060  24.006  1.00 19.28  ? 493  THR B N   1 
ATOM   8625  C  CA  . THR B 1 484 ? -5.495  86.463  23.372  1.00 18.35  ? 493  THR B CA  1 
ATOM   8626  C  C   . THR B 1 484 ? -5.707  85.577  22.135  1.00 18.59  ? 493  THR B C   1 
ATOM   8627  O  O   . THR B 1 484 ? -6.789  85.008  21.902  1.00 16.12  ? 493  THR B O   1 
ATOM   8628  C  CB  . THR B 1 484 ? -5.393  87.953  22.920  1.00 18.83  ? 493  THR B CB  1 
ATOM   8629  O  OG1 . THR B 1 484 ? -5.196  88.797  24.049  1.00 19.57  ? 493  THR B OG1 1 
ATOM   8630  C  CG2 . THR B 1 484 ? -6.725  88.435  22.246  1.00 17.59  ? 493  THR B CG2 1 
ATOM   8631  N  N   . ALA B 1 485 ? -4.644  85.436  21.332  1.00 18.19  ? 494  ALA B N   1 
ATOM   8632  C  CA  . ALA B 1 485 ? -4.709  84.644  20.103  1.00 16.94  ? 494  ALA B CA  1 
ATOM   8633  C  C   . ALA B 1 485 ? -5.012  83.204  20.368  1.00 19.12  ? 494  ALA B C   1 
ATOM   8634  O  O   . ALA B 1 485 ? -5.733  82.573  19.593  1.00 18.43  ? 494  ALA B O   1 
ATOM   8635  C  CB  . ALA B 1 485 ? -3.367  84.753  19.337  1.00 16.76  ? 494  ALA B CB  1 
ATOM   8636  N  N   . LEU B 1 486 ? -4.485  82.630  21.478  1.00 15.30  ? 495  LEU B N   1 
ATOM   8637  C  CA  . LEU B 1 486 ? -4.806  81.237  21.780  1.00 15.30  ? 495  LEU B CA  1 
ATOM   8638  C  C   . LEU B 1 486 ? -6.305  81.089  22.069  1.00 16.06  ? 495  LEU B C   1 
ATOM   8639  O  O   . LEU B 1 486 ? -6.932  80.110  21.652  1.00 16.80  ? 495  LEU B O   1 
ATOM   8640  C  CB  . LEU B 1 486 ? -4.002  80.762  23.019  1.00 15.89  ? 495  LEU B CB  1 
ATOM   8641  C  CG  . LEU B 1 486 ? -2.469  80.498  22.653  1.00 17.93  ? 495  LEU B CG  1 
ATOM   8642  C  CD1 . LEU B 1 486 ? -1.662  80.364  24.008  1.00 17.52  ? 495  LEU B CD1 1 
ATOM   8643  C  CD2 . LEU B 1 486 ? -2.287  79.237  21.806  1.00 17.66  ? 495  LEU B CD2 1 
ATOM   8644  N  N   . ALA B 1 487 ? -6.871  82.052  22.768  1.00 17.22  ? 496  ALA B N   1 
ATOM   8645  C  CA  . ALA B 1 487 ? -8.306  81.956  23.096  1.00 19.03  ? 496  ALA B CA  1 
ATOM   8646  C  C   . ALA B 1 487 ? -9.124  82.096  21.799  1.00 18.21  ? 496  ALA B C   1 
ATOM   8647  O  O   . ALA B 1 487 ? -10.103 81.372  21.616  1.00 18.10  ? 496  ALA B O   1 
ATOM   8648  C  CB  . ALA B 1 487 ? -8.665  83.054  24.070  1.00 17.02  ? 496  ALA B CB  1 
ATOM   8649  N  N   . THR B 1 488 ? -8.704  83.007  20.902  1.00 16.83  ? 497  THR B N   1 
ATOM   8650  C  CA  . THR B 1 488 ? -9.395  83.176  19.618  1.00 15.88  ? 497  THR B CA  1 
ATOM   8651  C  C   . THR B 1 488 ? -9.349  81.870  18.833  1.00 17.84  ? 497  THR B C   1 
ATOM   8652  O  O   . THR B 1 488 ? -10.375 81.397  18.338  1.00 16.42  ? 497  THR B O   1 
ATOM   8653  C  CB  . THR B 1 488 ? -8.732  84.253  18.732  1.00 17.96  ? 497  THR B CB  1 
ATOM   8654  O  OG1 . THR B 1 488 ? -8.767  85.469  19.459  1.00 18.85  ? 497  THR B OG1 1 
ATOM   8655  C  CG2 . THR B 1 488 ? -9.443  84.376  17.383  1.00 15.14  ? 497  THR B CG2 1 
ATOM   8656  N  N   . THR B 1 489 ? -8.130  81.241  18.746  1.00 17.13  ? 498  THR B N   1 
ATOM   8657  C  CA  . THR B 1 489 ? -7.963  79.982  18.032  1.00 15.86  ? 498  THR B CA  1 
ATOM   8658  C  C   . THR B 1 489 ? -8.839  78.864  18.577  1.00 18.14  ? 498  THR B C   1 
ATOM   8659  O  O   . THR B 1 489 ? -9.469  78.131  17.821  1.00 16.90  ? 498  THR B O   1 
ATOM   8660  C  CB  . THR B 1 489 ? -6.448  79.558  18.114  1.00 15.66  ? 498  THR B CB  1 
ATOM   8661  O  OG1 . THR B 1 489 ? -5.656  80.565  17.431  1.00 17.04  ? 498  THR B OG1 1 
ATOM   8662  C  CG2 . THR B 1 489 ? -6.204  78.207  17.550  1.00 16.56  ? 498  THR B CG2 1 
ATOM   8663  N  N   . GLU B 1 490 ? -8.889  78.713  19.915  1.00 15.68  ? 499  GLU B N   1 
ATOM   8664  C  CA  . GLU B 1 490 ? -9.633  77.586  20.511  1.00 19.00  ? 499  GLU B CA  1 
ATOM   8665  C  C   . GLU B 1 490 ? -11.156 77.783  20.303  1.00 18.94  ? 499  GLU B C   1 
ATOM   8666  O  O   . GLU B 1 490 ? -11.912 76.832  20.048  1.00 19.06  ? 499  GLU B O   1 
ATOM   8667  C  CB  . GLU B 1 490 ? -9.212  77.518  22.011  1.00 21.11  ? 499  GLU B CB  1 
ATOM   8668  C  CG  . GLU B 1 490 ? -7.701  77.145  22.077  1.00 23.31  ? 499  GLU B CG  1 
ATOM   8669  C  CD  . GLU B 1 490 ? -7.469  75.664  21.622  1.00 28.94  ? 499  GLU B CD  1 
ATOM   8670  O  OE1 . GLU B 1 490 ? -6.958  75.369  20.481  1.00 22.32  ? 499  GLU B OE1 1 
ATOM   8671  O  OE2 . GLU B 1 490 ? -7.857  74.789  22.425  1.00 29.68  ? 499  GLU B OE2 1 
ATOM   8672  N  N   . TYR B 1 491 ? -11.586 79.052  20.360  1.00 17.92  ? 500  TYR B N   1 
ATOM   8673  C  CA  . TYR B 1 491 ? -12.992 79.363  20.139  1.00 16.97  ? 500  TYR B CA  1 
ATOM   8674  C  C   . TYR B 1 491 ? -13.335 78.978  18.706  1.00 17.45  ? 500  TYR B C   1 
ATOM   8675  O  O   . TYR B 1 491 ? -14.311 78.243  18.475  1.00 19.60  ? 500  TYR B O   1 
ATOM   8676  C  CB  . TYR B 1 491 ? -13.280 80.881  20.353  1.00 16.89  ? 500  TYR B CB  1 
ATOM   8677  C  CG  . TYR B 1 491 ? -14.699 81.179  19.920  1.00 19.41  ? 500  TYR B CG  1 
ATOM   8678  C  CD1 . TYR B 1 491 ? -15.766 80.934  20.773  1.00 24.55  ? 500  TYR B CD1 1 
ATOM   8679  C  CD2 . TYR B 1 491 ? -14.979 81.640  18.625  1.00 20.94  ? 500  TYR B CD2 1 
ATOM   8680  C  CE1 . TYR B 1 491 ? -17.094 81.128  20.356  1.00 23.02  ? 500  TYR B CE1 1 
ATOM   8681  C  CE2 . TYR B 1 491 ? -16.297 81.831  18.200  1.00 24.04  ? 500  TYR B CE2 1 
ATOM   8682  C  CZ  . TYR B 1 491 ? -17.345 81.565  19.075  1.00 27.48  ? 500  TYR B CZ  1 
ATOM   8683  O  OH  . TYR B 1 491 ? -18.659 81.702  18.699  1.00 22.81  ? 500  TYR B OH  1 
ATOM   8684  N  N   . LEU B 1 492 ? -12.565 79.431  17.755  1.00 17.06  ? 501  LEU B N   1 
ATOM   8685  C  CA  . LEU B 1 492 ? -12.895 79.110  16.361  1.00 16.93  ? 501  LEU B CA  1 
ATOM   8686  C  C   . LEU B 1 492 ? -12.878 77.571  16.099  1.00 16.73  ? 501  LEU B C   1 
ATOM   8687  O  O   . LEU B 1 492 ? -13.768 77.032  15.442  1.00 18.95  ? 501  LEU B O   1 
ATOM   8688  C  CB  . LEU B 1 492 ? -11.863 79.787  15.404  1.00 17.22  ? 501  LEU B CB  1 
ATOM   8689  C  CG  . LEU B 1 492 ? -12.024 81.308  15.379  1.00 17.15  ? 501  LEU B CG  1 
ATOM   8690  C  CD1 . LEU B 1 492 ? -10.818 81.934  14.610  1.00 17.77  ? 501  LEU B CD1 1 
ATOM   8691  C  CD2 . LEU B 1 492 ? -13.364 81.677  14.644  1.00 18.48  ? 501  LEU B CD2 1 
ATOM   8692  N  N   . ARG B 1 493 ? -11.829 76.874  16.610  1.00 15.80  ? 502  ARG B N   1 
ATOM   8693  C  CA  . ARG B 1 493 ? -11.801 75.416  16.439  1.00 18.14  ? 502  ARG B CA  1 
ATOM   8694  C  C   . ARG B 1 493 ? -13.027 74.775  17.084  1.00 19.01  ? 502  ARG B C   1 
ATOM   8695  O  O   . ARG B 1 493 ? -13.549 73.793  16.515  1.00 20.86  ? 502  ARG B O   1 
ATOM   8696  C  CB  . ARG B 1 493 ? -10.517 74.837  17.101  1.00 18.56  ? 502  ARG B CB  1 
ATOM   8697  C  CG  . ARG B 1 493 ? -9.277  75.266  16.263  1.00 19.87  ? 502  ARG B CG  1 
ATOM   8698  C  CD  . ARG B 1 493 ? -8.006  74.643  16.834  1.00 21.30  ? 502  ARG B CD  1 
ATOM   8699  N  NE  . ARG B 1 493 ? -6.870  74.895  15.945  1.00 23.55  ? 502  ARG B NE  1 
ATOM   8700  C  CZ  . ARG B 1 493 ? -5.610  74.845  16.359  1.00 25.46  ? 502  ARG B CZ  1 
ATOM   8701  N  NH1 . ARG B 1 493 ? -5.331  74.554  17.628  1.00 22.02  ? 502  ARG B NH1 1 
ATOM   8702  N  NH2 . ARG B 1 493 ? -4.616  75.068  15.507  1.00 21.58  ? 502  ARG B NH2 1 
ATOM   8703  N  N   . SER B 1 494 ? -13.467 75.256  18.231  1.00 19.97  ? 503  SER B N   1 
ATOM   8704  C  CA  . SER B 1 494 ? -14.642 74.676  18.908  1.00 20.72  ? 503  SER B CA  1 
ATOM   8705  C  C   . SER B 1 494 ? -15.912 74.858  18.083  1.00 24.41  ? 503  SER B C   1 
ATOM   8706  O  O   . SER B 1 494 ? -16.898 74.147  18.299  1.00 22.94  ? 503  SER B O   1 
ATOM   8707  C  CB  . SER B 1 494 ? -14.809 75.293  20.297  1.00 17.43  ? 503  SER B CB  1 
ATOM   8708  O  OG  . SER B 1 494 ? -15.420 76.581  20.230  1.00 19.59  ? 503  SER B OG  1 
ATOM   8709  N  N   . LYS B 1 495 ? -15.895 75.793  17.115  1.00 24.40  ? 504  LYS B N   1 
ATOM   8710  C  CA  . LYS B 1 495 ? -17.044 76.042  16.247  1.00 25.27  ? 504  LYS B CA  1 
ATOM   8711  C  C   . LYS B 1 495 ? -16.830 75.397  14.885  1.00 26.37  ? 504  LYS B C   1 
ATOM   8712  O  O   . LYS B 1 495 ? -17.563 75.706  13.940  1.00 26.05  ? 504  LYS B O   1 
ATOM   8713  C  CB  . LYS B 1 495 ? -17.251 77.556  16.068  1.00 23.72  ? 504  LYS B CB  1 
ATOM   8714  C  CG  . LYS B 1 495 ? -17.598 78.250  17.387  1.00 25.34  ? 504  LYS B CG  1 
ATOM   8715  C  CD  . LYS B 1 495 ? -18.748 77.533  18.085  1.00 30.29  ? 504  LYS B CD  1 
ATOM   8716  C  CE  . LYS B 1 495 ? -19.714 78.488  18.685  1.00 43.38  ? 504  LYS B CE  1 
ATOM   8717  N  NZ  . LYS B 1 495 ? -20.563 79.117  17.602  1.00 53.37  ? 504  LYS B NZ  1 
ATOM   8718  N  N   . GLY B 1 496 ? -15.824 74.510  14.756  1.00 22.39  ? 505  GLY B N   1 
ATOM   8719  C  CA  . GLY B 1 496 ? -15.573 73.842  13.477  1.00 23.75  ? 505  GLY B CA  1 
ATOM   8720  C  C   . GLY B 1 496 ? -14.846 74.627  12.414  1.00 27.78  ? 505  GLY B C   1 
ATOM   8721  O  O   . GLY B 1 496 ? -14.888 74.261  11.240  1.00 28.83  ? 505  GLY B O   1 
ATOM   8722  N  N   . ILE B 1 497 ? -14.176 75.742  12.791  1.00 23.40  ? 506  ILE B N   1 
ATOM   8723  C  CA  . ILE B 1 497 ? -13.399 76.498  11.797  1.00 24.45  ? 506  ILE B CA  1 
ATOM   8724  C  C   . ILE B 1 497 ? -11.957 76.072  11.970  1.00 24.56  ? 506  ILE B C   1 
ATOM   8725  O  O   . ILE B 1 497 ? -11.466 76.019  13.097  1.00 25.32  ? 506  ILE B O   1 
ATOM   8726  C  CB  . ILE B 1 497 ? -13.599 78.033  12.048  1.00 23.23  ? 506  ILE B CB  1 
ATOM   8727  C  CG1 . ILE B 1 497 ? -15.056 78.413  11.628  1.00 26.37  ? 506  ILE B CG1 1 
ATOM   8728  C  CG2 . ILE B 1 497 ? -12.532 78.852  11.241  1.00 21.51  ? 506  ILE B CG2 1 
ATOM   8729  C  CD1 . ILE B 1 497 ? -15.490 79.790  12.223  1.00 27.46  ? 506  ILE B CD1 1 
ATOM   8730  N  N   A ASN B 1 498 ? -11.278 75.757  10.906  0.72 20.80  ? 507  ASN B N   1 
ATOM   8731  N  N   B ASN B 1 498 ? -11.294 75.756  10.952  0.28 23.18  ? 507  ASN B N   1 
ATOM   8732  C  CA  A ASN B 1 498 ? -9.880  75.358  10.994  0.72 20.61  ? 507  ASN B CA  1 
ATOM   8733  C  CA  B ASN B 1 498 ? -9.890  75.380  11.016  0.28 25.10  ? 507  ASN B CA  1 
ATOM   8734  C  C   A ASN B 1 498 ? -9.002  76.559  11.278  0.72 22.93  ? 507  ASN B C   1 
ATOM   8735  C  C   B ASN B 1 498 ? -9.026  76.602  11.256  0.28 26.68  ? 507  ASN B C   1 
ATOM   8736  O  O   A ASN B 1 498 ? -9.221  77.598  10.651  0.72 21.57  ? 507  ASN B O   1 
ATOM   8737  O  O   B ASN B 1 498 ? -9.247  77.641  10.626  0.28 25.90  ? 507  ASN B O   1 
ATOM   8738  C  CB  A ASN B 1 498 ? -9.466  74.789  9.688   0.72 24.64  ? 507  ASN B CB  1 
ATOM   8739  C  CB  B ASN B 1 498 ? -9.444  74.731  9.718   0.28 28.00  ? 507  ASN B CB  1 
ATOM   8740  C  CG  A ASN B 1 498 ? -10.332 73.618  9.387   0.72 32.38  ? 507  ASN B CG  1 
ATOM   8741  C  CG  B ASN B 1 498 ? -8.063  74.144  9.841   0.28 33.53  ? 507  ASN B CG  1 
ATOM   8742  O  OD1 A ASN B 1 498 ? -10.266 72.617  10.148  0.72 33.43  ? 507  ASN B OD1 1 
ATOM   8743  O  OD1 B ASN B 1 498 ? -7.090  74.765  9.419   0.28 36.75  ? 507  ASN B OD1 1 
ATOM   8744  N  ND2 A ASN B 1 498 ? -11.201 73.684  8.365   0.72 33.23  ? 507  ASN B ND2 1 
ATOM   8745  N  ND2 B ASN B 1 498 ? -7.886  72.961  10.422  0.28 36.58  ? 507  ASN B ND2 1 
ATOM   8746  N  N   . VAL B 1 499 ? -8.012  76.442  12.194  1.00 20.31  ? 508  VAL B N   1 
ATOM   8747  C  CA  . VAL B 1 499 ? -7.124  77.596  12.433  1.00 17.60  ? 508  VAL B CA  1 
ATOM   8748  C  C   . VAL B 1 499 ? -5.696  77.181  12.328  1.00 20.52  ? 508  VAL B C   1 
ATOM   8749  O  O   . VAL B 1 499 ? -5.311  76.133  12.879  1.00 22.40  ? 508  VAL B O   1 
ATOM   8750  C  CB  . VAL B 1 499 ? -7.348  78.218  13.860  1.00 19.46  ? 508  VAL B CB  1 
ATOM   8751  C  CG1 . VAL B 1 499 ? -6.310  79.319  14.125  1.00 19.33  ? 508  VAL B CG1 1 
ATOM   8752  C  CG2 . VAL B 1 499 ? -8.767  78.762  13.986  1.00 19.71  ? 508  VAL B CG2 1 
ATOM   8753  N  N   . VAL B 1 500 ? -4.905  77.947  11.611  1.00 16.68  ? 509  VAL B N   1 
ATOM   8754  C  CA  . VAL B 1 500 ? -3.475  77.736  11.636  1.00 17.10  ? 509  VAL B CA  1 
ATOM   8755  C  C   . VAL B 1 500 ? -2.888  79.013  12.322  1.00 22.52  ? 509  VAL B C   1 
ATOM   8756  O  O   . VAL B 1 500 ? -3.195  80.142  11.918  1.00 18.83  ? 509  VAL B O   1 
ATOM   8757  C  CB  . VAL B 1 500 ? -2.860  77.539  10.237  1.00 21.79  ? 509  VAL B CB  1 
ATOM   8758  C  CG1 . VAL B 1 500 ? -1.348  77.431  10.388  1.00 22.85  ? 509  VAL B CG1 1 
ATOM   8759  C  CG2 . VAL B 1 500 ? -3.443  76.292  9.595   1.00 20.88  ? 509  VAL B CG2 1 
ATOM   8760  N  N   . MET B 1 501 ? -2.095  78.853  13.409  1.00 17.78  ? 510  MET B N   1 
ATOM   8761  C  CA  . MET B 1 501 ? -1.474  80.029  14.015  1.00 17.53  ? 510  MET B CA  1 
ATOM   8762  C  C   . MET B 1 501 ? -0.095  80.238  13.372  1.00 19.83  ? 510  MET B C   1 
ATOM   8763  O  O   . MET B 1 501 ? 0.592   79.262  13.076  1.00 17.86  ? 510  MET B O   1 
ATOM   8764  C  CB  . MET B 1 501 ? -1.270  79.825  15.552  1.00 17.98  ? 510  MET B CB  1 
ATOM   8765  C  CG  . MET B 1 501 ? -2.652  79.462  16.230  1.00 17.59  ? 510  MET B CG  1 
ATOM   8766  S  SD  . MET B 1 501 ? -2.500  79.475  18.035  1.00 20.73  ? 510  MET B SD  1 
ATOM   8767  C  CE  . MET B 1 501 ? -2.241  81.189  18.341  1.00 17.58  ? 510  MET B CE  1 
ATOM   8768  N  N   . THR B 1 502 ? 0.322   81.471  13.204  1.00 17.16  ? 511  THR B N   1 
ATOM   8769  C  CA  . THR B 1 502 ? 1.677   81.726  12.671  1.00 16.59  ? 511  THR B CA  1 
ATOM   8770  C  C   . THR B 1 502 ? 2.659   81.285  13.755  1.00 20.47  ? 511  THR B C   1 
ATOM   8771  O  O   . THR B 1 502 ? 3.743   80.797  13.433  1.00 19.51  ? 511  THR B O   1 
ATOM   8772  C  CB  . THR B 1 502 ? 1.852   83.237  12.371  1.00 16.58  ? 511  THR B CB  1 
ATOM   8773  O  OG1 . THR B 1 502 ? 1.493   83.945  13.560  1.00 17.66  ? 511  THR B OG1 1 
ATOM   8774  C  CG2 . THR B 1 502 ? 1.010   83.683  11.136  1.00 18.06  ? 511  THR B CG2 1 
ATOM   8775  N  N   . ARG B 1 503 ? 2.341   81.514  15.007  1.00 17.50  ? 512  ARG B N   1 
ATOM   8776  C  CA  . ARG B 1 503 ? 3.159   80.981  16.097  1.00 22.39  ? 512  ARG B CA  1 
ATOM   8777  C  C   . ARG B 1 503 ? 2.200   80.629  17.218  1.00 24.39  ? 512  ARG B C   1 
ATOM   8778  O  O   . ARG B 1 503 ? 1.166   81.304  17.411  1.00 21.74  ? 512  ARG B O   1 
ATOM   8779  C  CB  . ARG B 1 503 ? 4.203   81.980  16.684  1.00 22.30  ? 512  ARG B CB  1 
ATOM   8780  C  CG  . ARG B 1 503 ? 3.540   83.164  17.327  1.00 19.41  ? 512  ARG B CG  1 
ATOM   8781  C  CD  . ARG B 1 503 ? 4.606   84.176  17.821  1.00 20.01  ? 512  ARG B CD  1 
ATOM   8782  N  NE  . ARG B 1 503 ? 4.002   85.344  18.504  1.00 21.72  ? 512  ARG B NE  1 
ATOM   8783  C  CZ  . ARG B 1 503 ? 3.949   85.512  19.828  1.00 21.62  ? 512  ARG B CZ  1 
ATOM   8784  N  NH1 . ARG B 1 503 ? 4.404   84.566  20.646  1.00 20.95  ? 512  ARG B NH1 1 
ATOM   8785  N  NH2 . ARG B 1 503 ? 3.495   86.638  20.338  1.00 19.91  ? 512  ARG B NH2 1 
ATOM   8786  N  N   . ASP B 1 504 ? 2.507   79.555  17.972  1.00 24.12  ? 513  ASP B N   1 
ATOM   8787  C  CA  . ASP B 1 504 ? 1.626   79.264  19.119  1.00 27.83  ? 513  ASP B CA  1 
ATOM   8788  C  C   . ASP B 1 504 ? 2.442   79.165  20.400  1.00 28.32  ? 513  ASP B C   1 
ATOM   8789  O  O   . ASP B 1 504 ? 1.951   78.678  21.426  1.00 29.37  ? 513  ASP B O   1 
ATOM   8790  C  CB  . ASP B 1 504 ? 0.794   78.027  18.916  1.00 30.51  ? 513  ASP B CB  1 
ATOM   8791  C  CG  . ASP B 1 504 ? 1.504   76.878  18.270  1.00 41.90  ? 513  ASP B CG  1 
ATOM   8792  O  OD1 . ASP B 1 504 ? 2.725   76.714  18.511  1.00 43.33  ? 513  ASP B OD1 1 
ATOM   8793  O  OD2 . ASP B 1 504 ? 0.850   76.139  17.526  1.00 46.66  ? 513  ASP B OD2 1 
ATOM   8794  N  N   . THR B 1 505 ? 3.669   79.662  20.340  1.00 25.13  ? 514  THR B N   1 
ATOM   8795  C  CA  . THR B 1 505 ? 4.594   79.702  21.454  1.00 26.45  ? 514  THR B CA  1 
ATOM   8796  C  C   . THR B 1 505 ? 5.348   81.002  21.398  1.00 28.15  ? 514  THR B C   1 
ATOM   8797  O  O   . THR B 1 505 ? 5.225   81.737  20.425  1.00 25.78  ? 514  THR B O   1 
ATOM   8798  C  CB  . THR B 1 505 ? 5.622   78.515  21.350  1.00 29.91  ? 514  THR B CB  1 
ATOM   8799  O  OG1 . THR B 1 505 ? 6.427   78.716  20.177  1.00 30.63  ? 514  THR B OG1 1 
ATOM   8800  C  CG2 . THR B 1 505 ? 4.966   77.188  21.146  1.00 32.92  ? 514  THR B CG2 1 
ATOM   8801  N  N   . ASP B 1 506 ? 6.140   81.301  22.446  1.00 28.06  ? 515  ASP B N   1 
ATOM   8802  C  CA  . ASP B 1 506 ? 6.948   82.487  22.462  1.00 28.99  ? 515  ASP B CA  1 
ATOM   8803  C  C   . ASP B 1 506 ? 8.214   82.237  21.588  1.00 35.87  ? 515  ASP B C   1 
ATOM   8804  O  O   . ASP B 1 506 ? 9.157   81.570  22.045  1.00 38.28  ? 515  ASP B O   1 
ATOM   8805  C  CB  . ASP B 1 506 ? 7.374   82.818  23.859  1.00 32.05  ? 515  ASP B CB  1 
ATOM   8806  C  CG  . ASP B 1 506 ? 8.200   84.089  23.901  1.00 39.30  ? 515  ASP B CG  1 
ATOM   8807  O  OD1 . ASP B 1 506 ? 7.969   84.973  23.074  1.00 38.10  ? 515  ASP B OD1 1 
ATOM   8808  O  OD2 . ASP B 1 506 ? 9.070   84.201  24.784  1.00 44.48  ? 515  ASP B OD2 1 
ATOM   8809  N  N   . LYS B 1 507 ? 8.240   82.721  20.371  1.00 31.69  ? 516  LYS B N   1 
ATOM   8810  C  CA  . LYS B 1 507 ? 9.402   82.519  19.500  1.00 28.89  ? 516  LYS B CA  1 
ATOM   8811  C  C   . LYS B 1 507 ? 9.484   83.694  18.572  1.00 27.22  ? 516  LYS B C   1 
ATOM   8812  O  O   . LYS B 1 507 ? 8.462   84.328  18.265  1.00 21.94  ? 516  LYS B O   1 
ATOM   8813  C  CB  . LYS B 1 507 ? 9.284   81.246  18.684  1.00 27.70  ? 516  LYS B CB  1 
ATOM   8814  C  CG  . LYS B 1 507 ? 8.093   81.196  17.749  1.00 30.45  ? 516  LYS B CG  1 
ATOM   8815  C  CD  . LYS B 1 507 ? 8.191   80.008  16.807  1.00 42.02  ? 516  LYS B CD  1 
ATOM   8816  C  CE  . LYS B 1 507 ? 7.324   80.171  15.565  1.00 52.29  ? 516  LYS B CE  1 
ATOM   8817  N  NZ  . LYS B 1 507 ? 8.114   79.998  14.312  1.00 59.48  ? 516  LYS B NZ  1 
ATOM   8818  N  N   . THR B 1 508 ? 10.697  83.993  18.119  1.00 23.65  ? 517  THR B N   1 
ATOM   8819  C  CA  . THR B 1 508 ? 10.929  85.094  17.209  1.00 21.48  ? 517  THR B CA  1 
ATOM   8820  C  C   . THR B 1 508 ? 10.422  84.722  15.856  1.00 19.60  ? 517  THR B C   1 
ATOM   8821  O  O   . THR B 1 508 ? 10.707  83.622  15.358  1.00 22.50  ? 517  THR B O   1 
ATOM   8822  C  CB  . THR B 1 508 ? 12.446  85.354  17.153  1.00 23.56  ? 517  THR B CB  1 
ATOM   8823  O  OG1 . THR B 1 508 ? 12.879  85.620  18.504  1.00 21.85  ? 517  THR B OG1 1 
ATOM   8824  C  CG2 . THR B 1 508 ? 12.787  86.593  16.298  1.00 19.89  ? 517  THR B CG2 1 
ATOM   8825  N  N   . MET B 1 509 ? 9.718   85.619  15.181  1.00 18.92  ? 518  MET B N   1 
ATOM   8826  C  CA  . MET B 1 509 ? 9.210   85.254  13.858  1.00 18.02  ? 518  MET B CA  1 
ATOM   8827  C  C   . MET B 1 509 ? 8.968   86.536  13.051  1.00 19.85  ? 518  MET B C   1 
ATOM   8828  O  O   . MET B 1 509 ? 8.144   87.365  13.440  1.00 19.28  ? 518  MET B O   1 
ATOM   8829  C  CB  . MET B 1 509 ? 7.842   84.458  13.962  1.00 20.04  ? 518  MET B CB  1 
ATOM   8830  C  CG  . MET B 1 509 ? 7.354   84.010  12.620  1.00 20.20  ? 518  MET B CG  1 
ATOM   8831  S  SD  . MET B 1 509 ? 5.906   82.915  12.831  1.00 21.75  ? 518  MET B SD  1 
ATOM   8832  C  CE  . MET B 1 509 ? 5.729   82.317  11.168  1.00 18.29  ? 518  MET B CE  1 
ATOM   8833  N  N   . ALA B 1 510 ? 9.655   86.669  11.888  1.00 19.38  ? 519  ALA B N   1 
ATOM   8834  C  CA  . ALA B 1 510 ? 9.575   87.920  11.100  1.00 20.11  ? 519  ALA B CA  1 
ATOM   8835  C  C   . ALA B 1 510 ? 8.234   88.025  10.340  1.00 19.10  ? 519  ALA B C   1 
ATOM   8836  O  O   . ALA B 1 510 ? 7.610   87.022  10.070  1.00 18.72  ? 519  ALA B O   1 
ATOM   8837  C  CB  . ALA B 1 510 ? 10.695  87.953  10.065  1.00 18.85  ? 519  ALA B CB  1 
ATOM   8838  N  N   . LEU B 1 511 ? 7.853   89.235  9.975   1.00 18.41  ? 520  LEU B N   1 
ATOM   8839  C  CA  . LEU B 1 511 ? 6.609   89.479  9.213   1.00 17.06  ? 520  LEU B CA  1 
ATOM   8840  C  C   . LEU B 1 511 ? 6.638   88.696  7.957   1.00 18.78  ? 520  LEU B C   1 
ATOM   8841  O  O   . LEU B 1 511 ? 5.631   88.147  7.534   1.00 18.59  ? 520  LEU B O   1 
ATOM   8842  C  CB  . LEU B 1 511 ? 6.554   91.008  8.929   1.00 15.63  ? 520  LEU B CB  1 
ATOM   8843  C  CG  . LEU B 1 511 ? 6.464   91.863  10.211  1.00 19.62  ? 520  LEU B CG  1 
ATOM   8844  C  CD1 . LEU B 1 511 ? 6.418   93.388  9.856   1.00 17.56  ? 520  LEU B CD1 1 
ATOM   8845  C  CD2 . LEU B 1 511 ? 5.222   91.525  10.988  1.00 21.83  ? 520  LEU B CD2 1 
ATOM   8846  N  N   . GLY B 1 512 ? 7.817   88.644  7.304   1.00 18.53  ? 521  GLY B N   1 
ATOM   8847  C  CA  . GLY B 1 512 ? 7.886   87.909  6.049   1.00 16.67  ? 521  GLY B CA  1 
ATOM   8848  C  C   . GLY B 1 512 ? 7.650   86.402  6.206   1.00 20.14  ? 521  GLY B C   1 
ATOM   8849  O  O   . GLY B 1 512 ? 7.256   85.711  5.280   1.00 19.29  ? 521  GLY B O   1 
ATOM   8850  N  N   . GLU B 1 513 ? 7.919   85.867  7.403   1.00 19.72  ? 522  GLU B N   1 
ATOM   8851  C  CA  . GLU B 1 513 ? 7.635   84.431  7.599   1.00 17.51  ? 522  GLU B CA  1 
ATOM   8852  C  C   . GLU B 1 513 ? 6.134   84.257  7.796   1.00 19.12  ? 522  GLU B C   1 
ATOM   8853  O  O   . GLU B 1 513 ? 5.579   83.249  7.386   1.00 18.73  ? 522  GLU B O   1 
ATOM   8854  C  CB  . GLU B 1 513 ? 8.339   83.955  8.867   1.00 22.94  ? 522  GLU B CB  1 
ATOM   8855  C  CG  . GLU B 1 513 ? 9.871   84.122  8.787   1.00 25.17  ? 522  GLU B CG  1 
ATOM   8856  C  CD  . GLU B 1 513 ? 10.538  83.701  10.122  1.00 26.25  ? 522  GLU B CD  1 
ATOM   8857  O  OE1 . GLU B 1 513 ? 10.389  82.491  10.479  1.00 26.01  ? 522  GLU B OE1 1 
ATOM   8858  O  OE2 . GLU B 1 513 ? 11.211  84.537  10.837  1.00 22.47  ? 522  GLU B OE2 1 
ATOM   8859  N  N   . ARG B 1 514 ? 5.493   85.212  8.483   1.00 17.47  ? 523  ARG B N   1 
ATOM   8860  C  CA  . ARG B 1 514 ? 4.043   85.109  8.758   1.00 16.51  ? 523  ARG B CA  1 
ATOM   8861  C  C   . ARG B 1 514 ? 3.251   85.214  7.476   1.00 17.31  ? 523  ARG B C   1 
ATOM   8862  O  O   . ARG B 1 514 ? 2.282   84.480  7.324   1.00 17.01  ? 523  ARG B O   1 
ATOM   8863  C  CB  . ARG B 1 514 ? 3.638   86.227  9.690   1.00 17.10  ? 523  ARG B CB  1 
ATOM   8864  C  CG  . ARG B 1 514 ? 4.450   86.197  11.028  1.00 16.91  ? 523  ARG B CG  1 
ATOM   8865  C  CD  . ARG B 1 514 ? 4.358   87.494  11.856  1.00 18.26  ? 523  ARG B CD  1 
ATOM   8866  N  NE  . ARG B 1 514 ? 5.307   87.423  12.979  1.00 19.18  ? 523  ARG B NE  1 
ATOM   8867  C  CZ  . ARG B 1 514 ? 4.961   87.405  14.264  1.00 20.57  ? 523  ARG B CZ  1 
ATOM   8868  N  NH1 . ARG B 1 514 ? 3.672   87.413  14.619  1.00 18.63  ? 523  ARG B NH1 1 
ATOM   8869  N  NH2 . ARG B 1 514 ? 5.903   87.400  15.214  1.00 19.22  ? 523  ARG B NH2 1 
ATOM   8870  N  N   . THR B 1 515 ? 3.653   86.105  6.530   1.00 15.93  ? 524  THR B N   1 
ATOM   8871  C  CA  . THR B 1 515 ? 2.886   86.193  5.283   1.00 19.45  ? 524  THR B CA  1 
ATOM   8872  C  C   . THR B 1 515 ? 3.178   84.958  4.381   1.00 21.86  ? 524  THR B C   1 
ATOM   8873  O  O   . THR B 1 515 ? 2.303   84.498  3.651   1.00 20.36  ? 524  THR B O   1 
ATOM   8874  C  CB  . THR B 1 515 ? 3.204   87.530  4.527   1.00 21.56  ? 524  THR B CB  1 
ATOM   8875  O  OG1 . THR B 1 515 ? 4.590   87.553  4.178   1.00 26.79  ? 524  THR B OG1 1 
ATOM   8876  C  CG2 . THR B 1 515 ? 3.015   88.737  5.425   1.00 22.46  ? 524  THR B CG2 1 
ATOM   8877  N  N   . ALA B 1 516 ? 4.417   84.436  4.403   1.00 21.46  ? 525  ALA B N   1 
ATOM   8878  C  CA  . ALA B 1 516 ? 4.706   83.255  3.569   1.00 18.87  ? 525  ALA B CA  1 
ATOM   8879  C  C   . ALA B 1 516 ? 3.787   82.106  4.049   1.00 21.51  ? 525  ALA B C   1 
ATOM   8880  O  O   . ALA B 1 516 ? 3.225   81.361  3.235   1.00 22.87  ? 525  ALA B O   1 
ATOM   8881  C  CB  . ALA B 1 516 ? 6.192   82.847  3.721   1.00 19.91  ? 525  ALA B CB  1 
ATOM   8882  N  N   . LEU B 1 517 ? 3.615   81.983  5.362   1.00 20.26  ? 526  LEU B N   1 
ATOM   8883  C  CA  . LEU B 1 517 ? 2.752   80.946  5.870   1.00 19.72  ? 526  LEU B CA  1 
ATOM   8884  C  C   . LEU B 1 517 ? 1.319   81.191  5.413   1.00 22.28  ? 526  LEU B C   1 
ATOM   8885  O  O   . LEU B 1 517 ? 0.634   80.258  4.983   1.00 24.28  ? 526  LEU B O   1 
ATOM   8886  C  CB  A LEU B 1 517 ? 2.795   80.888  7.420   0.58 20.48  ? 526  LEU B CB  1 
ATOM   8887  C  CB  B LEU B 1 517 ? 2.730   81.070  7.497   0.42 22.03  ? 526  LEU B CB  1 
ATOM   8888  C  CG  A LEU B 1 517 ? 1.812   79.885  8.054   0.58 25.35  ? 526  LEU B CG  1 
ATOM   8889  C  CG  B LEU B 1 517 ? 1.908   79.993  8.178   0.42 26.43  ? 526  LEU B CG  1 
ATOM   8890  C  CD1 A LEU B 1 517 ? 2.163   78.447  7.759   0.58 26.09  ? 526  LEU B CD1 1 
ATOM   8891  C  CD1 B LEU B 1 517 ? 2.651   79.601  9.422   0.42 28.08  ? 526  LEU B CD1 1 
ATOM   8892  C  CD2 A LEU B 1 517 ? 1.837   80.084  9.557   0.58 27.63  ? 526  LEU B CD2 1 
ATOM   8893  C  CD2 B LEU B 1 517 ? 0.487   80.490  8.541   0.42 26.47  ? 526  LEU B CD2 1 
ATOM   8894  N  N   . SER B 1 518 ? 0.836   82.451  5.500   1.00 21.44  ? 527  SER B N   1 
ATOM   8895  C  CA  . SER B 1 518 ? -0.533  82.745  5.072   1.00 16.37  ? 527  SER B CA  1 
ATOM   8896  C  C   . SER B 1 518 ? -0.680  82.414  3.597   1.00 19.81  ? 527  SER B C   1 
ATOM   8897  O  O   . SER B 1 518 ? -1.699  81.873  3.179   1.00 21.22  ? 527  SER B O   1 
ATOM   8898  C  CB  . SER B 1 518 ? -0.810  84.249  5.269   1.00 18.77  ? 527  SER B CB  1 
ATOM   8899  O  OG  . SER B 1 518 ? -2.166  84.543  4.968   1.00 20.08  ? 527  SER B OG  1 
ATOM   8900  N  N   . ASN B 1 519 ? 0.314   82.762  2.812   1.00 20.71  ? 528  ASN B N   1 
ATOM   8901  C  CA  . ASN B 1 519 ? 0.184   82.519  1.385   1.00 19.33  ? 528  ASN B CA  1 
ATOM   8902  C  C   . ASN B 1 519 ? 0.226   80.971  1.069   1.00 22.56  ? 528  ASN B C   1 
ATOM   8903  O  O   . ASN B 1 519 ? -0.245  80.591  -0.001  1.00 23.23  ? 528  ASN B O   1 
ATOM   8904  C  CB  . ASN B 1 519 ? 1.290   83.270  0.594   1.00 20.86  ? 528  ASN B CB  1 
ATOM   8905  C  CG  . ASN B 1 519 ? 1.010   84.786  0.600   1.00 22.05  ? 528  ASN B CG  1 
ATOM   8906  O  OD1 . ASN B 1 519 ? -0.164  85.181  0.723   1.00 21.67  ? 528  ASN B OD1 1 
ATOM   8907  N  ND2 . ASN B 1 519 ? 2.024   85.640  0.520   1.00 21.78  ? 528  ASN B ND2 1 
ATOM   8908  N  N   . THR B 1 520 ? 0.766   80.161  1.960   1.00 21.86  ? 529  THR B N   1 
ATOM   8909  C  CA  . THR B 1 520 ? 0.764   78.701  1.717   1.00 25.57  ? 529  THR B CA  1 
ATOM   8910  C  C   . THR B 1 520 ? -0.604  78.108  2.151   1.00 28.49  ? 529  THR B C   1 
ATOM   8911  O  O   . THR B 1 520 ? -1.135  77.198  1.524   1.00 25.39  ? 529  THR B O   1 
ATOM   8912  C  CB  . THR B 1 520 ? 1.862   78.040  2.613   1.00 30.65  ? 529  THR B CB  1 
ATOM   8913  O  OG1 . THR B 1 520 ? 3.125   78.572  2.200   1.00 32.94  ? 529  THR B OG1 1 
ATOM   8914  C  CG2 . THR B 1 520 ? 1.866   76.566  2.488   1.00 31.51  ? 529  THR B CG2 1 
ATOM   8915  N  N   . ILE B 1 521 ? -1.150  78.643  3.265   1.00 22.23  ? 530  ILE B N   1 
ATOM   8916  C  CA  . ILE B 1 521 ? -2.390  78.130  3.796   1.00 24.45  ? 530  ILE B CA  1 
ATOM   8917  C  C   . ILE B 1 521 ? -3.582  78.557  2.954   1.00 25.18  ? 530  ILE B C   1 
ATOM   8918  O  O   . ILE B 1 521 ? -4.567  77.799  2.829   1.00 23.34  ? 530  ILE B O   1 
ATOM   8919  C  CB  . ILE B 1 521 ? -2.558  78.591  5.276   1.00 25.53  ? 530  ILE B CB  1 
ATOM   8920  C  CG1 . ILE B 1 521 ? -1.436  77.981  6.189   1.00 25.35  ? 530  ILE B CG1 1 
ATOM   8921  C  CG2 . ILE B 1 521 ? -3.937  78.215  5.832   1.00 22.68  ? 530  ILE B CG2 1 
ATOM   8922  C  CD1 . ILE B 1 521 ? -1.276  76.453  6.021   1.00 26.04  ? 530  ILE B CD1 1 
ATOM   8923  N  N   . LYS B 1 522 ? -3.527  79.758  2.398   1.00 21.89  ? 531  LYS B N   1 
ATOM   8924  C  CA  . LYS B 1 522 ? -4.615  80.323  1.585   1.00 24.83  ? 531  LYS B CA  1 
ATOM   8925  C  C   . LYS B 1 522 ? -5.900  80.421  2.380   1.00 25.25  ? 531  LYS B C   1 
ATOM   8926  O  O   . LYS B 1 522 ? -6.972  79.952  1.955   1.00 21.39  ? 531  LYS B O   1 
ATOM   8927  C  CB  . LYS B 1 522 ? -4.843  79.477  0.341   1.00 26.86  ? 531  LYS B CB  1 
ATOM   8928  C  CG  . LYS B 1 522 ? -3.505  79.214  -0.316  1.00 26.79  ? 531  LYS B CG  1 
ATOM   8929  C  CD  . LYS B 1 522 ? -3.658  78.348  -1.589  1.00 28.66  ? 531  LYS B CD  1 
ATOM   8930  C  CE  . LYS B 1 522 ? -2.306  78.346  -2.250  1.00 46.24  ? 531  LYS B CE  1 
ATOM   8931  N  NZ  . LYS B 1 522 ? -2.416  78.049  -3.701  1.00 57.81  ? 531  LYS B NZ  1 
ATOM   8932  N  N   . PRO B 1 523 ? -5.854  81.105  3.531   1.00 21.57  ? 532  PRO B N   1 
ATOM   8933  C  CA  . PRO B 1 523 ? -7.067  81.199  4.340   1.00 20.02  ? 532  PRO B CA  1 
ATOM   8934  C  C   . PRO B 1 523 ? -8.207  82.109  3.832   1.00 20.86  ? 532  PRO B C   1 
ATOM   8935  O  O   . PRO B 1 523 ? -7.993  82.966  2.975   1.00 21.39  ? 532  PRO B O   1 
ATOM   8936  C  CB  . PRO B 1 523 ? -6.522  81.733  5.675   1.00 16.09  ? 532  PRO B CB  1 
ATOM   8937  C  CG  . PRO B 1 523 ? -5.484  82.745  5.187   1.00 17.61  ? 532  PRO B CG  1 
ATOM   8938  C  CD  . PRO B 1 523 ? -4.778  81.978  4.053   1.00 21.05  ? 532  PRO B CD  1 
ATOM   8939  N  N   . ASP B 1 524 ? -9.371  81.929  4.432   1.00 21.71  ? 533  ASP B N   1 
ATOM   8940  C  CA  . ASP B 1 524 ? -10.533 82.793  4.173   1.00 22.68  ? 533  ASP B CA  1 
ATOM   8941  C  C   . ASP B 1 524 ? -10.246 84.120  4.848   1.00 23.15  ? 533  ASP B C   1 
ATOM   8942  O  O   . ASP B 1 524 ? -10.727 85.173  4.390   1.00 21.04  ? 533  ASP B O   1 
ATOM   8943  C  CB  . ASP B 1 524 ? -11.793 82.139  4.757   1.00 24.86  ? 533  ASP B CB  1 
ATOM   8944  C  CG  . ASP B 1 524 ? -12.084 80.833  4.001   1.00 33.19  ? 533  ASP B CG  1 
ATOM   8945  O  OD1 . ASP B 1 524 ? -11.926 79.746  4.600   1.00 28.33  ? 533  ASP B OD1 1 
ATOM   8946  O  OD2 . ASP B 1 524 ? -12.435 80.907  2.802   1.00 28.52  ? 533  ASP B OD2 1 
ATOM   8947  N  N   . LEU B 1 525 ? -9.471  84.095  5.948   1.00 21.45  ? 534  LEU B N   1 
ATOM   8948  C  CA  . LEU B 1 525 ? -9.110  85.351  6.605   1.00 20.87  ? 534  LEU B CA  1 
ATOM   8949  C  C   . LEU B 1 525 ? -7.853  85.149  7.437   1.00 20.47  ? 534  LEU B C   1 
ATOM   8950  O  O   . LEU B 1 525 ? -7.695  84.118  8.062   1.00 17.76  ? 534  LEU B O   1 
ATOM   8951  C  CB  . LEU B 1 525 ? -10.266 85.827  7.535   1.00 18.22  ? 534  LEU B CB  1 
ATOM   8952  C  CG  . LEU B 1 525 ? -10.029 87.199  8.254   1.00 18.60  ? 534  LEU B CG  1 
ATOM   8953  C  CD1 . LEU B 1 525 ? -10.020 88.398  7.305   1.00 21.10  ? 534  LEU B CD1 1 
ATOM   8954  C  CD2 . LEU B 1 525 ? -11.155 87.408  9.282   1.00 18.18  ? 534  LEU B CD2 1 
ATOM   8955  N  N   . PHE B 1 526 ? -6.979  86.139  7.417   1.00 17.29  ? 535  PHE B N   1 
ATOM   8956  C  CA  . PHE B 1 526 ? -5.762  86.201  8.244   1.00 19.04  ? 535  PHE B CA  1 
ATOM   8957  C  C   . PHE B 1 526 ? -5.989  87.346  9.248   1.00 18.71  ? 535  PHE B C   1 
ATOM   8958  O  O   . PHE B 1 526 ? -6.273  88.480  8.828   1.00 16.37  ? 535  PHE B O   1 
ATOM   8959  C  CB  . PHE B 1 526 ? -4.558  86.525  7.333   1.00 17.94  ? 535  PHE B CB  1 
ATOM   8960  C  CG  . PHE B 1 526 ? -3.257  86.784  8.051   1.00 16.04  ? 535  PHE B CG  1 
ATOM   8961  C  CD1 . PHE B 1 526 ? -2.987  88.031  8.620   1.00 16.11  ? 535  PHE B CD1 1 
ATOM   8962  C  CD2 . PHE B 1 526 ? -2.246  85.816  8.063   1.00 19.95  ? 535  PHE B CD2 1 
ATOM   8963  C  CE1 . PHE B 1 526 ? -1.724  88.299  9.195   1.00 15.58  ? 535  PHE B CE1 1 
ATOM   8964  C  CE2 . PHE B 1 526 ? -0.989  86.093  8.632   1.00 20.63  ? 535  PHE B CE2 1 
ATOM   8965  C  CZ  . PHE B 1 526 ? -0.739  87.322  9.186   1.00 18.12  ? 535  PHE B CZ  1 
ATOM   8966  N  N   . THR B 1 527 ? -5.871  87.098  10.553  1.00 17.60  ? 536  THR B N   1 
ATOM   8967  C  CA  . THR B 1 527 ? -6.094  88.153  11.467  1.00 16.53  ? 536  THR B CA  1 
ATOM   8968  C  C   . THR B 1 527 ? -4.829  88.273  12.377  1.00 20.42  ? 536  THR B C   1 
ATOM   8969  O  O   . THR B 1 527 ? -4.493  87.339  13.093  1.00 17.55  ? 536  THR B O   1 
ATOM   8970  C  CB  . THR B 1 527 ? -7.313  87.849  12.410  1.00 18.26  ? 536  THR B CB  1 
ATOM   8971  O  OG1 . THR B 1 527 ? -8.479  87.682  11.577  1.00 18.21  ? 536  THR B OG1 1 
ATOM   8972  C  CG2 . THR B 1 527 ? -7.533  88.968  13.439  1.00 17.58  ? 536  THR B CG2 1 
ATOM   8973  N  N   . SER B 1 528 ? -4.191  89.444  12.341  1.00 18.18  ? 537  SER B N   1 
ATOM   8974  C  CA  . SER B 1 528 ? -3.054  89.740  13.182  1.00 17.06  ? 537  SER B CA  1 
ATOM   8975  C  C   . SER B 1 528 ? -3.609  90.418  14.434  1.00 17.72  ? 537  SER B C   1 
ATOM   8976  O  O   . SER B 1 528 ? -4.527  91.278  14.398  1.00 18.19  ? 537  SER B O   1 
ATOM   8977  C  CB  . SER B 1 528 ? -2.043  90.590  12.406  1.00 18.06  ? 537  SER B CB  1 
ATOM   8978  O  OG  . SER B 1 528 ? -0.850  90.739  13.149  1.00 21.87  ? 537  SER B OG  1 
ATOM   8979  N  N   . ILE B 1 529 ? -3.095  90.003  15.590  1.00 16.17  ? 538  ILE B N   1 
ATOM   8980  C  CA  . ILE B 1 529 ? -3.554  90.527  16.879  1.00 16.52  ? 538  ILE B CA  1 
ATOM   8981  C  C   . ILE B 1 529 ? -2.414  91.225  17.594  1.00 19.23  ? 538  ILE B C   1 
ATOM   8982  O  O   . ILE B 1 529 ? -1.343  90.618  17.799  1.00 19.89  ? 538  ILE B O   1 
ATOM   8983  C  CB  . ILE B 1 529 ? -4.098  89.329  17.688  1.00 19.57  ? 538  ILE B CB  1 
ATOM   8984  C  CG1 . ILE B 1 529 ? -5.354  88.744  16.954  1.00 17.46  ? 538  ILE B CG1 1 
ATOM   8985  C  CG2 . ILE B 1 529 ? -4.487  89.828  19.121  1.00 19.25  ? 538  ILE B CG2 1 
ATOM   8986  C  CD1 . ILE B 1 529 ? -5.985  87.547  17.681  1.00 21.63  ? 538  ILE B CD1 1 
ATOM   8987  N  N   . HIS B 1 530 ? -2.614  92.498  17.961  1.00 17.10  ? 539  HIS B N   1 
ATOM   8988  C  CA  . HIS B 1 530 ? -1.581  93.336  18.589  1.00 20.93  ? 539  HIS B CA  1 
ATOM   8989  C  C   . HIS B 1 530 ? -2.144  94.173  19.709  1.00 24.69  ? 539  HIS B C   1 
ATOM   8990  O  O   . HIS B 1 530 ? -3.367  94.285  19.898  1.00 21.31  ? 539  HIS B O   1 
ATOM   8991  C  CB  . HIS B 1 530 ? -0.996  94.366  17.566  1.00 21.33  ? 539  HIS B CB  1 
ATOM   8992  C  CG  . HIS B 1 530 ? -0.113  93.736  16.554  1.00 23.47  ? 539  HIS B CG  1 
ATOM   8993  N  ND1 . HIS B 1 530 ? 1.255   93.979  16.524  1.00 22.60  ? 539  HIS B ND1 1 
ATOM   8994  C  CD2 . HIS B 1 530 ? -0.384  92.776  15.625  1.00 21.86  ? 539  HIS B CD2 1 
ATOM   8995  C  CE1 . HIS B 1 530 ? 1.743   93.165  15.599  1.00 25.90  ? 539  HIS B CE1 1 
ATOM   8996  N  NE2 . HIS B 1 530 ? 0.822   92.419  15.022  1.00 25.09  ? 539  HIS B NE2 1 
ATOM   8997  N  N   . TYR B 1 531 ? -1.256  94.788  20.459  1.00 25.51  ? 540  TYR B N   1 
ATOM   8998  C  CA  . TYR B 1 531 ? -1.727  95.716  21.508  1.00 29.62  ? 540  TYR B CA  1 
ATOM   8999  C  C   . TYR B 1 531 ? -1.041  97.070  21.168  1.00 38.04  ? 540  TYR B C   1 
ATOM   9000  O  O   . TYR B 1 531 ? 0.102   97.086  20.690  1.00 39.09  ? 540  TYR B O   1 
ATOM   9001  C  CB  . TYR B 1 531 ? -1.432  95.161  22.931  1.00 30.24  ? 540  TYR B CB  1 
ATOM   9002  C  CG  . TYR B 1 531 ? -2.492  94.158  23.357  1.00 32.13  ? 540  TYR B CG  1 
ATOM   9003  C  CD1 . TYR B 1 531 ? -3.495  94.512  24.262  1.00 37.10  ? 540  TYR B CD1 1 
ATOM   9004  C  CD2 . TYR B 1 531 ? -2.513  92.874  22.835  1.00 33.70  ? 540  TYR B CD2 1 
ATOM   9005  C  CE1 . TYR B 1 531 ? -4.489  93.609  24.631  1.00 37.80  ? 540  TYR B CE1 1 
ATOM   9006  C  CE2 . TYR B 1 531 ? -3.514  91.955  23.194  1.00 32.96  ? 540  TYR B CE2 1 
ATOM   9007  C  CZ  . TYR B 1 531 ? -4.501  92.337  24.092  1.00 33.21  ? 540  TYR B CZ  1 
ATOM   9008  O  OH  . TYR B 1 531 ? -5.524  91.486  24.430  1.00 32.05  ? 540  TYR B OH  1 
ATOM   9009  N  N   . ASN B 1 532 ? -1.762  98.180  21.343  1.00 42.71  ? 541  ASN B N   1 
ATOM   9010  C  CA  . ASN B 1 532 ? -1.252  99.509  21.001  1.00 49.18  ? 541  ASN B CA  1 
ATOM   9011  C  C   . ASN B 1 532 ? -0.410  100.096 22.124  1.00 53.68  ? 541  ASN B C   1 
ATOM   9012  O  O   . ASN B 1 532 ? -0.215  99.453  23.159  1.00 53.79  ? 541  ASN B O   1 
ATOM   9013  C  CB  . ASN B 1 532 ? -2.424  100.467 20.677  1.00 51.28  ? 541  ASN B CB  1 
ATOM   9014  C  CG  . ASN B 1 532 ? -2.291  101.027 19.281  1.00 55.36  ? 541  ASN B CG  1 
ATOM   9015  O  OD1 . ASN B 1 532 ? -1.172  101.095 18.773  1.00 55.60  ? 541  ASN B OD1 1 
ATOM   9016  N  ND2 . ASN B 1 532 ? -3.365  101.429 18.580  1.00 54.53  ? 541  ASN B ND2 1 
ATOM   9017  N  N   . ALA B 1 533 ? 0.064   101.335 21.884  1.00 59.46  ? 542  ALA B N   1 
ATOM   9018  C  CA  . ALA B 1 533 ? 0.883   102.151 22.774  1.00 65.27  ? 542  ALA B CA  1 
ATOM   9019  C  C   . ALA B 1 533 ? 1.855   102.901 21.939  1.00 69.35  ? 542  ALA B C   1 
ATOM   9020  O  O   . ALA B 1 533 ? 1.828   104.129 21.850  1.00 70.04  ? 542  ALA B O   1 
ATOM   9021  C  CB  . ALA B 1 533 ? 1.681   101.268 23.733  1.00 66.79  ? 542  ALA B CB  1 
ATOM   9022  N  N   . SER B 1 534 ? 2.724   102.069 21.306  0.00 0.00   ? 543  SER B N   1 
ATOM   9023  C  CA  . SER B 1 534 ? 3.900   102.372 20.494  0.00 0.00   ? 543  SER B CA  1 
ATOM   9024  C  C   . SER B 1 534 ? 4.947   102.684 21.552  0.00 0.00   ? 543  SER B C   1 
ATOM   9025  O  O   . SER B 1 534 ? 5.793   103.562 21.392  0.00 0.00   ? 543  SER B O   1 
ATOM   9026  C  CB  . SER B 1 534 ? 3.664   103.547 19.551  0.00 0.00   ? 543  SER B CB  1 
ATOM   9027  O  OG  . SER B 1 534 ? 2.574   103.280 18.683  0.00 0.00   ? 543  SER B OG  1 
ATOM   9028  N  N   . ASN B 1 535 ? 4.862   101.909 22.658  0.00 0.00   ? 544  ASN B N   1 
ATOM   9029  C  CA  . ASN B 1 535 ? 5.677   102.052 23.860  0.00 0.00   ? 544  ASN B CA  1 
ATOM   9030  C  C   . ASN B 1 535 ? 5.234   103.379 24.490  0.00 0.00   ? 544  ASN B C   1 
ATOM   9031  O  O   . ASN B 1 535 ? 6.049   104.219 24.860  0.00 0.00   ? 544  ASN B O   1 
ATOM   9032  C  CB  . ASN B 1 535 ? 7.179   102.026 23.535  0.00 0.00   ? 544  ASN B CB  1 
ATOM   9033  C  CG  . ASN B 1 535 ? 7.752   100.627 23.560  0.00 0.00   ? 544  ASN B CG  1 
ATOM   9034  O  OD1 . ASN B 1 535 ? 7.145   99.703  23.014  0.00 0.00   ? 544  ASN B OD1 1 
ATOM   9035  N  ND2 . ASN B 1 535 ? 8.913   100.378 24.169  0.00 0.00   ? 544  ASN B ND2 1 
ATOM   9036  N  N   . GLY B 1 536 ? 3.901   103.534 24.598  0.00 0.00   ? 545  GLY B N   1 
ATOM   9037  C  CA  . GLY B 1 536 ? 3.274   104.737 25.138  0.00 0.00   ? 545  GLY B CA  1 
ATOM   9038  C  C   . GLY B 1 536 ? 1.841   104.391 25.489  0.00 0.00   ? 545  GLY B C   1 
ATOM   9039  O  O   . GLY B 1 536 ? 1.548   103.214 25.615  0.00 0.00   ? 545  GLY B O   1 
ATOM   9040  N  N   . SER B 1 537 ? 0.909   105.354 25.620  0.00 0.00   ? 546  SER B N   1 
ATOM   9041  C  CA  . SER B 1 537 ? -0.414  104.872 26.035  1.00 68.24  ? 546  SER B CA  1 
ATOM   9042  C  C   . SER B 1 537 ? -1.643  105.738 25.837  1.00 68.31  ? 546  SER B C   1 
ATOM   9043  O  O   . SER B 1 537 ? -2.208  106.137 26.863  1.00 70.92  ? 546  SER B O   1 
ATOM   9044  C  CB  . SER B 1 537 ? -0.364  104.574 27.525  0.00 0.00   ? 546  SER B CB  1 
ATOM   9045  O  OG  . SER B 1 537 ? 0.535   105.436 28.203  0.00 0.00   ? 546  SER B OG  1 
ATOM   9046  N  N   . GLY B 1 538 ? -2.085  106.073 24.590  1.00 66.49  ? 547  GLY B N   1 
ATOM   9047  C  CA  . GLY B 1 538 ? -3.367  106.768 24.444  1.00 58.52  ? 547  GLY B CA  1 
ATOM   9048  C  C   . GLY B 1 538 ? -4.376  105.672 24.809  1.00 59.04  ? 547  GLY B C   1 
ATOM   9049  O  O   . GLY B 1 538 ? -4.113  104.917 25.762  1.00 58.67  ? 547  GLY B O   1 
ATOM   9050  N  N   . ASN B 1 539 ? -5.530  105.511 24.111  1.00 53.49  ? 548  ASN B N   1 
ATOM   9051  C  CA  . ASN B 1 539 ? -6.369  104.383 24.548  1.00 49.67  ? 548  ASN B CA  1 
ATOM   9052  C  C   . ASN B 1 539 ? -7.463  103.971 23.537  1.00 46.63  ? 548  ASN B C   1 
ATOM   9053  O  O   . ASN B 1 539 ? -7.875  104.781 22.701  1.00 43.12  ? 548  ASN B O   1 
ATOM   9054  C  CB  . ASN B 1 539 ? -7.023  104.681 25.911  1.00 47.51  ? 548  ASN B CB  1 
ATOM   9055  C  CG  . ASN B 1 539 ? -8.025  105.825 25.846  1.00 48.99  ? 548  ASN B CG  1 
ATOM   9056  O  OD1 . ASN B 1 539 ? -7.647  106.986 26.074  1.00 50.15  ? 548  ASN B OD1 1 
ATOM   9057  N  ND2 . ASN B 1 539 ? -9.279  105.609 25.480  1.00 43.24  ? 548  ASN B ND2 1 
ATOM   9058  N  N   . GLY B 1 540 ? -7.919  102.690 23.614  1.00 39.42  ? 549  GLY B N   1 
ATOM   9059  C  CA  . GLY B 1 540 ? -8.977  102.235 22.729  1.00 32.53  ? 549  GLY B CA  1 
ATOM   9060  C  C   . GLY B 1 540 ? -8.632  101.071 21.822  1.00 27.25  ? 549  GLY B C   1 
ATOM   9061  O  O   . GLY B 1 540 ? -7.591  100.447 21.951  1.00 24.38  ? 549  GLY B O   1 
ATOM   9062  N  N   . VAL B 1 541 ? -9.543  100.789 20.879  1.00 22.65  ? 550  VAL B N   1 
ATOM   9063  C  CA  . VAL B 1 541 ? -9.388  99.692  19.958  1.00 22.20  ? 550  VAL B CA  1 
ATOM   9064  C  C   . VAL B 1 541 ? -9.505  100.223 18.531  1.00 21.21  ? 550  VAL B C   1 
ATOM   9065  O  O   . VAL B 1 541 ? -10.324 101.113 18.273  1.00 21.28  ? 550  VAL B O   1 
ATOM   9066  C  CB  . VAL B 1 541 ? -10.510 98.621  20.226  1.00 24.08  ? 550  VAL B CB  1 
ATOM   9067  C  CG1 . VAL B 1 541 ? -11.885 99.281  20.270  1.00 26.52  ? 550  VAL B CG1 1 
ATOM   9068  C  CG2 . VAL B 1 541 ? -10.480 97.553  19.137  1.00 21.43  ? 550  VAL B CG2 1 
ATOM   9069  N  N   . GLU B 1 542 ? -8.671  99.737  17.612  1.00 19.86  ? 551  GLU B N   1 
ATOM   9070  C  CA  . GLU B 1 542 ? -8.799  100.129 16.208  1.00 21.60  ? 551  GLU B CA  1 
ATOM   9071  C  C   . GLU B 1 542 ? -8.437  98.935  15.371  1.00 19.56  ? 551  GLU B C   1 
ATOM   9072  O  O   . GLU B 1 542 ? -7.714  98.039  15.843  1.00 19.97  ? 551  GLU B O   1 
ATOM   9073  C  CB  . GLU B 1 542 ? -7.900  101.326 15.812  1.00 22.05  ? 551  GLU B CB  1 
ATOM   9074  C  CG  . GLU B 1 542 ? -6.416  101.067 16.069  1.00 22.97  ? 551  GLU B CG  1 
ATOM   9075  C  CD  . GLU B 1 542 ? -5.589  102.364 15.925  1.00 35.95  ? 551  GLU B CD  1 
ATOM   9076  O  OE1 . GLU B 1 542 ? -4.354  102.247 15.821  1.00 37.02  ? 551  GLU B OE1 1 
ATOM   9077  O  OE2 . GLU B 1 542 ? -6.162  103.479 15.903  1.00 35.48  ? 551  GLU B OE2 1 
ATOM   9078  N  N   . ILE B 1 543 ? -8.901  98.909  14.133  1.00 16.25  ? 552  ILE B N   1 
ATOM   9079  C  CA  . ILE B 1 543 ? -8.569  97.757  13.297  1.00 16.39  ? 552  ILE B CA  1 
ATOM   9080  C  C   . ILE B 1 543 ? -8.164  98.231  11.895  1.00 19.71  ? 552  ILE B C   1 
ATOM   9081  O  O   . ILE B 1 543 ? -8.836  99.102  11.332  1.00 19.53  ? 552  ILE B O   1 
ATOM   9082  C  CB  . ILE B 1 543 ? -9.790  96.807  13.200  1.00 15.85  ? 552  ILE B CB  1 
ATOM   9083  C  CG1 . ILE B 1 543 ? -10.193 96.315  14.646  1.00 17.02  ? 552  ILE B CG1 1 
ATOM   9084  C  CG2 . ILE B 1 543 ? -9.418  95.576  12.305  1.00 14.84  ? 552  ILE B CG2 1 
ATOM   9085  C  CD1 . ILE B 1 543 ? -11.369 95.347  14.644  1.00 21.15  ? 552  ILE B CD1 1 
ATOM   9086  N  N   . TYR B 1 544 ? -7.072  97.690  11.353  1.00 15.62  ? 553  TYR B N   1 
ATOM   9087  C  CA  . TYR B 1 544 ? -6.691  98.057  9.989   1.00 15.49  ? 553  TYR B CA  1 
ATOM   9088  C  C   . TYR B 1 544 ? -7.104  97.018  9.018   1.00 17.73  ? 553  TYR B C   1 
ATOM   9089  O  O   . TYR B 1 544 ? -6.996  95.822  9.308   1.00 16.70  ? 553  TYR B O   1 
ATOM   9090  C  CB  . TYR B 1 544 ? -5.123  98.204  9.883   1.00 18.55  ? 553  TYR B CB  1 
ATOM   9091  C  CG  . TYR B 1 544 ? -4.641  99.404  10.644  1.00 20.32  ? 553  TYR B CG  1 
ATOM   9092  C  CD1 . TYR B 1 544 ? -4.307  99.309  11.992  1.00 25.59  ? 553  TYR B CD1 1 
ATOM   9093  C  CD2 . TYR B 1 544 ? -4.559  100.652 10.037  1.00 26.77  ? 553  TYR B CD2 1 
ATOM   9094  C  CE1 . TYR B 1 544 ? -3.909  100.419 12.710  1.00 29.41  ? 553  TYR B CE1 1 
ATOM   9095  C  CE2 . TYR B 1 544 ? -4.157  101.771 10.760  1.00 28.93  ? 553  TYR B CE2 1 
ATOM   9096  C  CZ  . TYR B 1 544 ? -3.838  101.640 12.090  1.00 30.37  ? 553  TYR B CZ  1 
ATOM   9097  O  OH  . TYR B 1 544 ? -3.447  102.741 12.819  1.00 40.02  ? 553  TYR B OH  1 
ATOM   9098  N  N   . TYR B 1 545 ? -7.512  97.446  7.809   1.00 14.66  ? 554  TYR B N   1 
ATOM   9099  C  CA  . TYR B 1 545 ? -7.969  96.500  6.806   1.00 13.95  ? 554  TYR B CA  1 
ATOM   9100  C  C   . TYR B 1 545 ? -7.312  96.915  5.469   1.00 17.65  ? 554  TYR B C   1 
ATOM   9101  O  O   . TYR B 1 545 ? -6.584  97.942  5.441   1.00 15.86  ? 554  TYR B O   1 
ATOM   9102  C  CB  . TYR B 1 545 ? -9.512  96.385  6.727   1.00 12.87  ? 554  TYR B CB  1 
ATOM   9103  C  CG  . TYR B 1 545 ? -10.184 97.653  6.257   1.00 16.23  ? 554  TYR B CG  1 
ATOM   9104  C  CD1 . TYR B 1 545 ? -10.531 98.659  7.140   1.00 16.69  ? 554  TYR B CD1 1 
ATOM   9105  C  CD2 . TYR B 1 545 ? -10.461 97.848  4.915   1.00 16.89  ? 554  TYR B CD2 1 
ATOM   9106  C  CE1 . TYR B 1 545 ? -11.137 99.851  6.691   1.00 17.18  ? 554  TYR B CE1 1 
ATOM   9107  C  CE2 . TYR B 1 545 ? -11.072 99.024  4.456   1.00 22.62  ? 554  TYR B CE2 1 
ATOM   9108  C  CZ  . TYR B 1 545 ? -11.405 100.010 5.341   1.00 25.61  ? 554  TYR B CZ  1 
ATOM   9109  O  OH  . TYR B 1 545 ? -11.997 101.127 4.815   1.00 24.84  ? 554  TYR B OH  1 
ATOM   9110  N  N   . LYS B 1 546 ? -7.513  96.106  4.423   1.00 17.20  ? 555  LYS B N   1 
ATOM   9111  C  CA  . LYS B 1 546 ? -6.835  96.323  3.150   1.00 16.55  ? 555  LYS B CA  1 
ATOM   9112  C  C   . LYS B 1 546 ? -7.400  97.480  2.330   1.00 19.68  ? 555  LYS B C   1 
ATOM   9113  O  O   . LYS B 1 546 ? -8.616  97.588  2.191   1.00 18.82  ? 555  LYS B O   1 
ATOM   9114  C  CB  . LYS B 1 546 ? -6.919  95.064  2.328   1.00 18.34  ? 555  LYS B CB  1 
ATOM   9115  C  CG  . LYS B 1 546 ? -5.896  93.996  2.762   1.00 17.70  ? 555  LYS B CG  1 
ATOM   9116  C  CD  . LYS B 1 546 ? -6.028  92.785  1.828   1.00 21.65  ? 555  LYS B CD  1 
ATOM   9117  C  CE  . LYS B 1 546 ? -4.866  91.806  1.905   1.00 24.34  ? 555  LYS B CE  1 
ATOM   9118  N  NZ  . LYS B 1 546 ? -4.874  90.838  0.706   1.00 21.90  ? 555  LYS B NZ  1 
ATOM   9119  N  N   . VAL B 1 547 ? -6.530  98.352  1.822   1.00 17.93  ? 556  VAL B N   1 
ATOM   9120  C  CA  . VAL B 1 547 ? -7.064  99.527  1.123   1.00 19.58  ? 556  VAL B CA  1 
ATOM   9121  C  C   . VAL B 1 547 ? -7.844  99.059  -0.148  1.00 19.25  ? 556  VAL B C   1 
ATOM   9122  O  O   . VAL B 1 547 ? -8.696  99.803  -0.604  1.00 21.28  ? 556  VAL B O   1 
ATOM   9123  C  CB  . VAL B 1 547 ? -5.889  100.491 0.794   1.00 20.18  ? 556  VAL B CB  1 
ATOM   9124  C  CG1 . VAL B 1 547 ? -5.010  99.927  -0.369  1.00 21.73  ? 556  VAL B CG1 1 
ATOM   9125  C  CG2 . VAL B 1 547 ? -6.423  101.924 0.512   1.00 20.09  ? 556  VAL B CG2 1 
ATOM   9126  N  N   . LYS B 1 548 ? -7.583  97.885  -0.681  1.00 20.63  ? 557  LYS B N   1 
ATOM   9127  C  CA  . LYS B 1 548 ? -8.384  97.510  -1.865  1.00 22.40  ? 557  LYS B CA  1 
ATOM   9128  C  C   . LYS B 1 548 ? -9.840  97.348  -1.494  1.00 25.16  ? 557  LYS B C   1 
ATOM   9129  O  O   . LYS B 1 548 ? -10.702 97.372  -2.379  1.00 23.43  ? 557  LYS B O   1 
ATOM   9130  C  CB  . LYS B 1 548 ? -7.846  96.260  -2.557  1.00 25.35  ? 557  LYS B CB  1 
ATOM   9131  C  CG  . LYS B 1 548 ? -8.068  95.016  -1.764  1.00 28.22  ? 557  LYS B CG  1 
ATOM   9132  C  CD  . LYS B 1 548 ? -7.774  93.856  -2.639  1.00 42.10  ? 557  LYS B CD  1 
ATOM   9133  C  CE  . LYS B 1 548 ? -7.649  92.628  -1.798  1.00 48.48  ? 557  LYS B CE  1 
ATOM   9134  N  NZ  . LYS B 1 548 ? -7.740  91.395  -2.616  1.00 52.12  ? 557  LYS B NZ  1 
ATOM   9135  N  N   . ASP B 1 549 ? -10.159 97.195  -0.199  1.00 19.29  ? 558  ASP B N   1 
ATOM   9136  C  CA  . ASP B 1 549 ? -11.565 97.027  0.216   1.00 20.36  ? 558  ASP B CA  1 
ATOM   9137  C  C   . ASP B 1 549 ? -12.156 98.332  0.771   1.00 20.37  ? 558  ASP B C   1 
ATOM   9138  O  O   . ASP B 1 549 ? -13.180 98.268  1.447   1.00 21.54  ? 558  ASP B O   1 
ATOM   9139  C  CB  . ASP B 1 549 ? -11.651 95.934  1.353   1.00 20.70  ? 558  ASP B CB  1 
ATOM   9140  C  CG  . ASP B 1 549 ? -11.361 94.548  0.828   1.00 26.90  ? 558  ASP B CG  1 
ATOM   9141  O  OD1 . ASP B 1 549 ? -11.521 94.325  -0.418  1.00 22.38  ? 558  ASP B OD1 1 
ATOM   9142  O  OD2 . ASP B 1 549 ? -10.950 93.652  1.645   1.00 23.25  ? 558  ASP B OD2 1 
ATOM   9143  N  N   . LYS B 1 550 ? -11.515 99.498  0.527   1.00 19.84  ? 559  LYS B N   1 
ATOM   9144  C  CA  . LYS B 1 550 ? -11.974 100.731 1.161   1.00 22.03  ? 559  LYS B CA  1 
ATOM   9145  C  C   . LYS B 1 550 ? -13.430 101.043 0.762   1.00 25.19  ? 559  LYS B C   1 
ATOM   9146  O  O   . LYS B 1 550 ? -14.117 101.686 1.511   1.00 26.67  ? 559  LYS B O   1 
ATOM   9147  C  CB  . LYS B 1 550 ? -11.066 101.933 0.823   1.00 24.25  ? 559  LYS B CB  1 
ATOM   9148  C  CG  . LYS B 1 550 ? -11.125 102.302 -0.648  1.00 29.18  ? 559  LYS B CG  1 
ATOM   9149  C  CD  . LYS B 1 550 ? -10.110 103.420 -0.958  1.00 36.40  ? 559  LYS B CD  1 
ATOM   9150  C  CE  . LYS B 1 550 ? -10.518 104.235 -2.141  1.00 49.35  ? 559  LYS B CE  1 
ATOM   9151  N  NZ  . LYS B 1 550 ? -9.504  105.295 -2.382  1.00 62.07  ? 559  LYS B NZ  1 
ATOM   9152  N  N   . ASN B 1 551 ? -13.871 100.576 -0.385  1.00 23.38  ? 560  ASN B N   1 
ATOM   9153  C  CA  . ASN B 1 551 ? -15.278 100.846 -0.742  1.00 28.91  ? 560  ASN B CA  1 
ATOM   9154  C  C   . ASN B 1 551 ? -16.116 99.597  -0.533  1.00 30.61  ? 560  ASN B C   1 
ATOM   9155  O  O   . ASN B 1 551 ? -17.174 99.432  -1.161  1.00 28.12  ? 560  ASN B O   1 
ATOM   9156  C  CB  . ASN B 1 551 ? -15.362 101.320 -2.207  1.00 29.64  ? 560  ASN B CB  1 
ATOM   9157  C  CG  . ASN B 1 551 ? -14.699 102.672 -2.343  1.00 33.63  ? 560  ASN B CG  1 
ATOM   9158  O  OD1 . ASN B 1 551 ? -13.895 102.865 -3.248  1.00 38.80  ? 560  ASN B OD1 1 
ATOM   9159  N  ND2 . ASN B 1 551 ? -14.962 103.626 -1.479  1.00 34.60  ? 560  ASN B ND2 1 
ATOM   9160  N  N   . GLY B 1 552 ? -15.662 98.702  0.354   1.00 24.16  ? 561  GLY B N   1 
ATOM   9161  C  CA  . GLY B 1 552 ? -16.408 97.487  0.622   1.00 21.52  ? 561  GLY B CA  1 
ATOM   9162  C  C   . GLY B 1 552 ? -15.612 96.270  0.212   1.00 23.23  ? 561  GLY B C   1 
ATOM   9163  O  O   . GLY B 1 552 ? -14.962 96.236  -0.842  1.00 22.32  ? 561  GLY B O   1 
ATOM   9164  N  N   . GLY B 1 553 ? -15.623 95.262  1.069   1.00 21.34  ? 562  GLY B N   1 
ATOM   9165  C  CA  . GLY B 1 553 ? -14.891 94.045  0.731   1.00 21.55  ? 562  GLY B CA  1 
ATOM   9166  C  C   . GLY B 1 553 ? -14.697 93.242  1.991   1.00 19.45  ? 562  GLY B C   1 
ATOM   9167  O  O   . GLY B 1 553 ? -15.007 93.720  3.102   1.00 19.77  ? 562  GLY B O   1 
ATOM   9168  N  N   . THR B 1 554 ? -14.166 92.018  1.831   1.00 19.03  ? 563  THR B N   1 
ATOM   9169  C  CA  . THR B 1 554 ? -14.032 91.144  2.996   1.00 22.30  ? 563  THR B CA  1 
ATOM   9170  C  C   . THR B 1 554 ? -13.315 91.694  4.193   1.00 19.46  ? 563  THR B C   1 
ATOM   9171  O  O   . THR B 1 554 ? -13.799 91.531  5.318   1.00 18.40  ? 563  THR B O   1 
ATOM   9172  C  CB  . THR B 1 554 ? -13.320 89.867  2.510   1.00 23.00  ? 563  THR B CB  1 
ATOM   9173  O  OG1 . THR B 1 554 ? -14.168 89.334  1.469   1.00 21.17  ? 563  THR B OG1 1 
ATOM   9174  C  CG2 . THR B 1 554 ? -13.158 88.864  3.585   1.00 17.85  ? 563  THR B CG2 1 
ATOM   9175  N  N   . THR B 1 555 ? -12.145 92.368  3.992   1.00 17.42  ? 564  THR B N   1 
ATOM   9176  C  CA  . THR B 1 555 ? -11.440 92.832  5.202   1.00 16.60  ? 564  THR B CA  1 
ATOM   9177  C  C   . THR B 1 555 ? -12.144 93.945  5.853   1.00 17.75  ? 564  THR B C   1 
ATOM   9178  O  O   . THR B 1 555 ? -12.071 94.057  7.081   1.00 15.97  ? 564  THR B O   1 
ATOM   9179  C  CB  . THR B 1 555 ? -9.990  93.179  4.895   1.00 16.48  ? 564  THR B CB  1 
ATOM   9180  O  OG1 . THR B 1 555 ? -9.933  94.325  4.030   1.00 16.85  ? 564  THR B OG1 1 
ATOM   9181  C  CG2 . THR B 1 555 ? -9.295  92.044  4.233   1.00 18.60  ? 564  THR B CG2 1 
ATOM   9182  N  N   . LYS B 1 556 ? -12.869 94.789  5.098   1.00 16.86  ? 565  LYS B N   1 
ATOM   9183  C  CA  . LYS B 1 556 ? -13.607 95.889  5.739   1.00 19.79  ? 565  LYS B CA  1 
ATOM   9184  C  C   . LYS B 1 556 ? -14.743 95.329  6.578   1.00 19.64  ? 565  LYS B C   1 
ATOM   9185  O  O   . LYS B 1 556 ? -14.968 95.742  7.731   1.00 17.28  ? 565  LYS B O   1 
ATOM   9186  C  CB  . LYS B 1 556 ? -14.139 96.844  4.641   1.00 19.47  ? 565  LYS B CB  1 
ATOM   9187  C  CG  . LYS B 1 556 ? -14.665 98.116  5.327   1.00 20.05  ? 565  LYS B CG  1 
ATOM   9188  C  CD  . LYS B 1 556 ? -15.159 99.074  4.218   1.00 19.63  ? 565  LYS B CD  1 
ATOM   9189  C  CE  . LYS B 1 556 ? -15.440 100.485 4.752   1.00 27.55  ? 565  LYS B CE  1 
ATOM   9190  N  NZ  . LYS B 1 556 ? -15.882 101.343 3.602   1.00 33.35  ? 565  LYS B NZ  1 
ATOM   9191  N  N   . THR B 1 557 ? -15.467 94.334  6.013   1.00 17.22  ? 566  THR B N   1 
ATOM   9192  C  CA  . THR B 1 557 ? -16.517 93.688  6.775   1.00 17.15  ? 566  THR B CA  1 
ATOM   9193  C  C   . THR B 1 557 ? -15.954 93.010  8.055   1.00 17.36  ? 566  THR B C   1 
ATOM   9194  O  O   . THR B 1 557 ? -16.526 93.094  9.153   1.00 18.01  ? 566  THR B O   1 
ATOM   9195  C  CB  . THR B 1 557 ? -17.172 92.592  5.919   1.00 22.64  ? 566  THR B CB  1 
ATOM   9196  O  OG1 . THR B 1 557 ? -17.825 93.256  4.839   1.00 22.00  ? 566  THR B OG1 1 
ATOM   9197  C  CG2 . THR B 1 557 ? -18.161 91.732  6.714   1.00 19.61  ? 566  THR B CG2 1 
ATOM   9198  N  N   . ALA B 1 558 ? -14.822 92.290  7.878   1.00 17.25  ? 567  ALA B N   1 
ATOM   9199  C  CA  . ALA B 1 558 ? -14.218 91.589  9.050   1.00 16.29  ? 567  ALA B CA  1 
ATOM   9200  C  C   . ALA B 1 558 ? -13.885 92.587  10.120  1.00 15.66  ? 567  ALA B C   1 
ATOM   9201  O  O   . ALA B 1 558 ? -14.170 92.364  11.307  1.00 15.83  ? 567  ALA B O   1 
ATOM   9202  C  CB  . ALA B 1 558 ? -12.912 90.869  8.615   1.00 16.66  ? 567  ALA B CB  1 
ATOM   9203  N  N   . ALA B 1 559 ? -13.258 93.726  9.711   1.00 16.20  ? 568  ALA B N   1 
ATOM   9204  C  CA  . ALA B 1 559 ? -12.889 94.742  10.704  1.00 16.52  ? 568  ALA B CA  1 
ATOM   9205  C  C   . ALA B 1 559 ? -14.135 95.294  11.435  1.00 16.69  ? 568  ALA B C   1 
ATOM   9206  O  O   . ALA B 1 559 ? -14.150 95.415  12.654  1.00 16.08  ? 568  ALA B O   1 
ATOM   9207  C  CB  . ALA B 1 559 ? -12.160 95.888  10.010  1.00 16.77  ? 568  ALA B CB  1 
ATOM   9208  N  N   . SER B 1 560 ? -15.173 95.612  10.655  1.00 16.36  ? 569  SER B N   1 
ATOM   9209  C  CA  . SER B 1 560 ? -16.399 96.130  11.279  1.00 17.34  ? 569  SER B CA  1 
ATOM   9210  C  C   . SER B 1 560 ? -17.013 95.097  12.241  1.00 16.94  ? 569  SER B C   1 
ATOM   9211  O  O   . SER B 1 560 ? -17.479 95.490  13.321  1.00 17.22  ? 569  SER B O   1 
ATOM   9212  C  CB  . SER B 1 560 ? -17.379 96.517  10.152  1.00 19.67  ? 569  SER B CB  1 
ATOM   9213  O  OG  . SER B 1 560 ? -18.585 96.915  10.779  1.00 22.08  ? 569  SER B OG  1 
ATOM   9214  N  N   . ASN B 1 561 ? -17.012 93.800  11.880  1.00 16.43  ? 570  ASN B N   1 
ATOM   9215  C  CA  . ASN B 1 561 ? -17.599 92.743  12.752  1.00 16.59  ? 570  ASN B CA  1 
ATOM   9216  C  C   . ASN B 1 561 ? -16.796 92.545  14.041  1.00 17.80  ? 570  ASN B C   1 
ATOM   9217  O  O   . ASN B 1 561 ? -17.359 92.418  15.131  1.00 18.53  ? 570  ASN B O   1 
ATOM   9218  C  CB  . ASN B 1 561 ? -17.655 91.411  11.984  1.00 17.76  ? 570  ASN B CB  1 
ATOM   9219  C  CG  . ASN B 1 561 ? -18.782 91.368  11.003  1.00 22.49  ? 570  ASN B CG  1 
ATOM   9220  O  OD1 . ASN B 1 561 ? -19.739 92.164  11.134  1.00 20.66  ? 570  ASN B OD1 1 
ATOM   9221  N  ND2 . ASN B 1 561 ? -18.737 90.542  9.987   1.00 16.42  ? 570  ASN B ND2 1 
ATOM   9222  N  N   . ILE B 1 562 ? -15.451 92.531  13.931  1.00 16.49  ? 571  ILE B N   1 
ATOM   9223  C  CA  . ILE B 1 562 ? -14.648 92.338  15.157  1.00 17.12  ? 571  ILE B CA  1 
ATOM   9224  C  C   . ILE B 1 562 ? -14.686 93.520  16.044  1.00 16.95  ? 571  ILE B C   1 
ATOM   9225  O  O   . ILE B 1 562 ? -14.766 93.378  17.247  1.00 18.40  ? 571  ILE B O   1 
ATOM   9226  C  CB  . ILE B 1 562 ? -13.201 92.008  14.647  1.00 15.44  ? 571  ILE B CB  1 
ATOM   9227  C  CG1 . ILE B 1 562 ? -13.246 90.597  13.962  1.00 17.80  ? 571  ILE B CG1 1 
ATOM   9228  C  CG2 . ILE B 1 562 ? -12.193 92.042  15.868  1.00 17.01  ? 571  ILE B CG2 1 
ATOM   9229  C  CD1 . ILE B 1 562 ? -11.983 90.444  13.082  1.00 21.37  ? 571  ILE B CD1 1 
ATOM   9230  N  N   . LEU B 1 563 ? -14.665 94.749  15.478  1.00 15.99  ? 572  LEU B N   1 
ATOM   9231  C  CA  . LEU B 1 563 ? -14.739 95.935  16.336  1.00 16.38  ? 572  LEU B CA  1 
ATOM   9232  C  C   . LEU B 1 563 ? -16.070 95.868  17.114  1.00 15.66  ? 572  LEU B C   1 
ATOM   9233  O  O   . LEU B 1 563 ? -16.097 96.139  18.324  1.00 18.90  ? 572  LEU B O   1 
ATOM   9234  C  CB  . LEU B 1 563 ? -14.708 97.185  15.427  1.00 17.61  ? 572  LEU B CB  1 
ATOM   9235  C  CG  . LEU B 1 563 ? -14.780 98.539  16.139  1.00 19.50  ? 572  LEU B CG  1 
ATOM   9236  C  CD1 . LEU B 1 563 ? -13.657 98.689  17.166  1.00 18.67  ? 572  LEU B CD1 1 
ATOM   9237  C  CD2 . LEU B 1 563 ? -14.640 99.610  15.035  1.00 18.65  ? 572  LEU B CD2 1 
ATOM   9238  N  N   . LYS B 1 564 ? -17.159 95.536  16.397  1.00 16.45  ? 573  LYS B N   1 
ATOM   9239  C  CA  . LYS B 1 564 ? -18.469 95.411  17.054  1.00 15.81  ? 573  LYS B CA  1 
ATOM   9240  C  C   . LYS B 1 564 ? -18.374 94.449  18.231  1.00 18.97  ? 573  LYS B C   1 
ATOM   9241  O  O   . LYS B 1 564 ? -18.794 94.770  19.332  1.00 19.17  ? 573  LYS B O   1 
ATOM   9242  C  CB  . LYS B 1 564 ? -19.509 94.904  15.998  1.00 17.98  ? 573  LYS B CB  1 
ATOM   9243  C  CG  . LYS B 1 564 ? -20.741 94.200  16.615  1.00 19.58  ? 573  LYS B CG  1 
ATOM   9244  C  CD  . LYS B 1 564 ? -21.624 93.722  15.495  1.00 19.19  ? 573  LYS B CD  1 
ATOM   9245  C  CE  . LYS B 1 564 ? -22.741 92.822  16.015  1.00 18.82  ? 573  LYS B CE  1 
ATOM   9246  N  NZ  . LYS B 1 564 ? -23.610 92.434  14.870  1.00 22.71  ? 573  LYS B NZ  1 
ATOM   9247  N  N   . ARG B 1 565 ? -17.765 93.259  18.020  1.00 18.10  ? 574  ARG B N   1 
ATOM   9248  C  CA  . ARG B 1 565 ? -17.755 92.237  19.082  1.00 17.82  ? 574  ARG B CA  1 
ATOM   9249  C  C   . ARG B 1 565 ? -16.885 92.610  20.192  1.00 18.15  ? 574  ARG B C   1 
ATOM   9250  O  O   . ARG B 1 565 ? -17.265 92.366  21.360  1.00 19.18  ? 574  ARG B O   1 
ATOM   9251  C  CB  . ARG B 1 565 ? -17.363 90.845  18.486  1.00 17.44  ? 574  ARG B CB  1 
ATOM   9252  C  CG  . ARG B 1 565 ? -18.412 90.380  17.465  1.00 18.11  ? 574  ARG B CG  1 
ATOM   9253  C  CD  . ARG B 1 565 ? -19.817 90.190  18.118  1.00 17.69  ? 574  ARG B CD  1 
ATOM   9254  N  NE  . ARG B 1 565 ? -20.650 89.482  17.134  1.00 22.33  ? 574  ARG B NE  1 
ATOM   9255  C  CZ  . ARG B 1 565 ? -21.927 89.151  17.331  1.00 26.70  ? 574  ARG B CZ  1 
ATOM   9256  N  NH1 . ARG B 1 565 ? -22.556 89.521  18.439  1.00 22.03  ? 574  ARG B NH1 1 
ATOM   9257  N  NH2 . ARG B 1 565 ? -22.567 88.406  16.436  1.00 22.34  ? 574  ARG B NH2 1 
ATOM   9258  N  N   . ILE B 1 566 ? -15.740 93.210  19.927  1.00 14.83  ? 575  ILE B N   1 
ATOM   9259  C  CA  . ILE B 1 566 ? -14.940 93.655  21.091  1.00 14.66  ? 575  ILE B CA  1 
ATOM   9260  C  C   . ILE B 1 566 ? -15.690 94.660  21.920  1.00 19.91  ? 575  ILE B C   1 
ATOM   9261  O  O   . ILE B 1 566 ? -15.688 94.579  23.162  1.00 20.02  ? 575  ILE B O   1 
ATOM   9262  C  CB  . ILE B 1 566 ? -13.627 94.317  20.544  1.00 17.36  ? 575  ILE B CB  1 
ATOM   9263  C  CG1 . ILE B 1 566 ? -12.776 93.186  19.839  1.00 17.99  ? 575  ILE B CG1 1 
ATOM   9264  C  CG2 . ILE B 1 566 ? -12.869 94.970  21.711  1.00 19.73  ? 575  ILE B CG2 1 
ATOM   9265  C  CD1 . ILE B 1 566 ? -11.438 93.737  19.200  1.00 18.70  ? 575  ILE B CD1 1 
ATOM   9266  N  N   . LEU B 1 567 ? -16.343 95.627  21.277  1.00 19.88  ? 576  LEU B N   1 
ATOM   9267  C  CA  . LEU B 1 567 ? -17.016 96.650  22.056  1.00 19.98  ? 576  LEU B CA  1 
ATOM   9268  C  C   . LEU B 1 567 ? -18.268 96.142  22.743  1.00 19.94  ? 576  LEU B C   1 
ATOM   9269  O  O   . LEU B 1 567 ? -18.761 96.841  23.652  1.00 22.21  ? 576  LEU B O   1 
ATOM   9270  C  CB  . LEU B 1 567 ? -17.367 97.880  21.184  1.00 19.35  ? 576  LEU B CB  1 
ATOM   9271  C  CG  . LEU B 1 567 ? -16.110 98.648  20.664  1.00 21.07  ? 576  LEU B CG  1 
ATOM   9272  C  CD1 . LEU B 1 567 ? -16.584 99.692  19.659  1.00 24.56  ? 576  LEU B CD1 1 
ATOM   9273  C  CD2 . LEU B 1 567 ? -15.413 99.297  21.809  1.00 26.55  ? 576  LEU B CD2 1 
ATOM   9274  N  N   . GLU B 1 568 ? -18.771 94.971  22.380  1.00 19.91  ? 577  GLU B N   1 
ATOM   9275  C  CA  . GLU B 1 568 ? -19.938 94.431  23.119  1.00 19.45  ? 577  GLU B CA  1 
ATOM   9276  C  C   . GLU B 1 568 ? -19.479 93.929  24.482  1.00 23.80  ? 577  GLU B C   1 
ATOM   9277  O  O   . GLU B 1 568 ? -20.325 93.745  25.365  1.00 25.99  ? 577  GLU B O   1 
ATOM   9278  C  CB  . GLU B 1 568 ? -20.587 93.305  22.337  1.00 21.78  ? 577  GLU B CB  1 
ATOM   9279  C  CG  . GLU B 1 568 ? -21.369 93.918  21.210  1.00 22.27  ? 577  GLU B CG  1 
ATOM   9280  C  CD  . GLU B 1 568 ? -22.210 92.908  20.421  1.00 27.37  ? 577  GLU B CD  1 
ATOM   9281  O  OE1 . GLU B 1 568 ? -21.858 91.703  20.353  1.00 22.90  ? 577  GLU B OE1 1 
ATOM   9282  O  OE2 . GLU B 1 568 ? -23.242 93.353  19.835  1.00 25.42  ? 577  GLU B OE2 1 
ATOM   9283  N  N   . LYS B 1 569 ? -18.164 93.724  24.708  1.00 21.47  ? 578  LYS B N   1 
ATOM   9284  C  CA  . LYS B 1 569 ? -17.754 93.256  26.055  1.00 19.54  ? 578  LYS B CA  1 
ATOM   9285  C  C   . LYS B 1 569 ? -16.860 94.209  26.728  1.00 23.78  ? 578  LYS B C   1 
ATOM   9286  O  O   . LYS B 1 569 ? -16.684 94.100  27.927  1.00 25.59  ? 578  LYS B O   1 
ATOM   9287  C  CB  . LYS B 1 569 ? -16.963 91.966  25.927  1.00 21.94  ? 578  LYS B CB  1 
ATOM   9288  C  CG  . LYS B 1 569 ? -17.840 90.768  25.570  1.00 23.99  ? 578  LYS B CG  1 
ATOM   9289  C  CD  . LYS B 1 569 ? -18.916 90.516  26.596  1.00 32.36  ? 578  LYS B CD  1 
ATOM   9290  C  CE  . LYS B 1 569 ? -19.718 89.324  26.180  1.00 39.66  ? 578  LYS B CE  1 
ATOM   9291  N  NZ  . LYS B 1 569 ? -20.497 88.770  27.324  1.00 49.80  ? 578  LYS B NZ  1 
ATOM   9292  N  N   . PHE B 1 570 ? -16.221 95.153  25.972  1.00 21.57  ? 579  PHE B N   1 
ATOM   9293  C  CA  . PHE B 1 570 ? -15.288 96.084  26.598  1.00 23.17  ? 579  PHE B CA  1 
ATOM   9294  C  C   . PHE B 1 570 ? -15.667 97.533  26.407  1.00 24.85  ? 579  PHE B C   1 
ATOM   9295  O  O   . PHE B 1 570 ? -16.069 97.897  25.326  1.00 25.24  ? 579  PHE B O   1 
ATOM   9296  C  CB  . PHE B 1 570 ? -13.859 95.892  25.992  1.00 22.37  ? 579  PHE B CB  1 
ATOM   9297  C  CG  . PHE B 1 570 ? -13.313 94.526  26.359  1.00 23.63  ? 579  PHE B CG  1 
ATOM   9298  C  CD1 . PHE B 1 570 ? -12.577 94.347  27.519  1.00 28.80  ? 579  PHE B CD1 1 
ATOM   9299  C  CD2 . PHE B 1 570 ? -13.559 93.423  25.555  1.00 24.97  ? 579  PHE B CD2 1 
ATOM   9300  C  CE1 . PHE B 1 570 ? -12.100 93.076  27.878  1.00 28.96  ? 579  PHE B CE1 1 
ATOM   9301  C  CE2 . PHE B 1 570 ? -13.088 92.159  25.905  1.00 28.23  ? 579  PHE B CE2 1 
ATOM   9302  C  CZ  . PHE B 1 570 ? -12.355 91.995  27.080  1.00 29.40  ? 579  PHE B CZ  1 
ATOM   9303  N  N   . ASN B 1 571 ? -15.573 98.365  27.460  1.00 26.46  ? 580  ASN B N   1 
ATOM   9304  C  CA  . ASN B 1 571 ? -15.850 99.795  27.305  1.00 31.45  ? 580  ASN B CA  1 
ATOM   9305  C  C   . ASN B 1 571 ? -14.542 100.512 26.947  1.00 33.57  ? 580  ASN B C   1 
ATOM   9306  O  O   . ASN B 1 571 ? -14.000 101.292 27.702  1.00 38.72  ? 580  ASN B O   1 
ATOM   9307  C  CB  . ASN B 1 571 ? -16.506 100.399 28.567  1.00 36.48  ? 580  ASN B CB  1 
ATOM   9308  C  CG  . ASN B 1 571 ? -17.950 99.952  28.683  1.00 54.43  ? 580  ASN B CG  1 
ATOM   9309  O  OD1 . ASN B 1 571 ? -18.607 99.593  27.652  1.00 56.80  ? 580  ASN B OD1 1 
ATOM   9310  N  ND2 . ASN B 1 571 ? -18.532 99.858  29.885  1.00 59.98  ? 580  ASN B ND2 1 
ATOM   9311  N  N   . MET B 1 572 ? -14.040 100.221 25.813  1.00 33.12  ? 581  MET B N   1 
ATOM   9312  C  CA  . MET B 1 572 ? -12.836 100.826 25.336  1.00 31.58  ? 581  MET B CA  1 
ATOM   9313  C  C   . MET B 1 572 ? -13.234 101.919 24.298  1.00 29.53  ? 581  MET B C   1 
ATOM   9314  O  O   . MET B 1 572 ? -14.322 101.855 23.706  1.00 27.00  ? 581  MET B O   1 
ATOM   9315  C  CB  . MET B 1 572 ? -11.959 99.740  24.713  1.00 35.08  ? 581  MET B CB  1 
ATOM   9316  C  CG  . MET B 1 572 ? -10.994 99.022  25.801  1.00 47.22  ? 581  MET B CG  1 
ATOM   9317  S  SD  . MET B 1 572 ? -10.239 97.550  25.114  1.00 57.31  ? 581  MET B SD  1 
ATOM   9318  C  CE  . MET B 1 572 ? -9.676  96.622  26.696  1.00 60.72  ? 581  MET B CE  1 
ATOM   9319  N  N   . LYS B 1 573 ? -12.396 102.919 24.112  1.00 23.57  ? 582  LYS B N   1 
ATOM   9320  C  CA  . LYS B 1 573 ? -12.669 103.978 23.138  1.00 25.78  ? 582  LYS B CA  1 
ATOM   9321  C  C   . LYS B 1 573 ? -12.736 103.382 21.727  1.00 25.66  ? 582  LYS B C   1 
ATOM   9322  O  O   . LYS B 1 573 ? -11.835 102.638 21.359  1.00 23.34  ? 582  LYS B O   1 
ATOM   9323  C  CB  . LYS B 1 573 ? -11.537 104.994 23.142  1.00 27.76  ? 582  LYS B CB  1 
ATOM   9324  C  CG  . LYS B 1 573 ? -11.828 106.138 22.200  1.00 39.90  ? 582  LYS B CG  1 
ATOM   9325  C  CD  . LYS B 1 573 ? -11.345 107.479 22.785  1.00 53.21  ? 582  LYS B CD  1 
ATOM   9326  C  CE  . LYS B 1 573 ? -9.839  107.615 22.787  1.00 58.51  ? 582  LYS B CE  1 
ATOM   9327  N  NZ  . LYS B 1 573 ? -9.379  108.616 21.791  1.00 66.26  ? 582  LYS B NZ  1 
ATOM   9328  N  N   . ASN B 1 574 ? -13.779 103.692 20.973  1.00 21.15  ? 583  ASN B N   1 
ATOM   9329  C  CA  . ASN B 1 574 ? -13.908 103.198 19.614  1.00 20.14  ? 583  ASN B CA  1 
ATOM   9330  C  C   . ASN B 1 574 ? -13.110 104.110 18.683  1.00 21.18  ? 583  ASN B C   1 
ATOM   9331  O  O   . ASN B 1 574 ? -13.524 105.249 18.402  1.00 21.27  ? 583  ASN B O   1 
ATOM   9332  C  CB  . ASN B 1 574 ? -15.379 103.147 19.276  1.00 17.50  ? 583  ASN B CB  1 
ATOM   9333  C  CG  . ASN B 1 574 ? -15.673 102.609 17.910  1.00 18.16  ? 583  ASN B CG  1 
ATOM   9334  O  OD1 . ASN B 1 574 ? -16.855 102.224 17.665  1.00 24.35  ? 583  ASN B OD1 1 
ATOM   9335  N  ND2 . ASN B 1 574 ? -14.732 102.487 17.027  1.00 16.26  ? 583  ASN B ND2 1 
ATOM   9336  N  N   . ARG B 1 575 ? -11.949 103.613 18.191  1.00 17.66  ? 584  ARG B N   1 
ATOM   9337  C  CA  . ARG B 1 575 ? -11.134 104.423 17.293  1.00 17.95  ? 584  ARG B CA  1 
ATOM   9338  C  C   . ARG B 1 575 ? -11.403 104.097 15.858  1.00 22.68  ? 584  ARG B C   1 
ATOM   9339  O  O   . ARG B 1 575 ? -10.780 104.736 14.985  1.00 21.13  ? 584  ARG B O   1 
ATOM   9340  C  CB  . ARG B 1 575 ? -9.640  104.246 17.613  1.00 21.70  ? 584  ARG B CB  1 
ATOM   9341  C  CG  . ARG B 1 575 ? -9.344  104.480 19.090  1.00 25.42  ? 584  ARG B CG  1 
ATOM   9342  C  CD  . ARG B 1 575 ? -7.984  103.843 19.413  1.00 36.49  ? 584  ARG B CD  1 
ATOM   9343  N  NE  . ARG B 1 575 ? -6.913  104.452 18.613  1.00 44.38  ? 584  ARG B NE  1 
ATOM   9344  C  CZ  . ARG B 1 575 ? -6.203  105.513 18.995  1.00 57.79  ? 584  ARG B CZ  1 
ATOM   9345  N  NH1 . ARG B 1 575 ? -6.432  106.085 20.177  1.00 54.93  ? 584  ARG B NH1 1 
ATOM   9346  N  NH2 . ARG B 1 575 ? -5.260  106.011 18.198  1.00 55.52  ? 584  ARG B NH2 1 
ATOM   9347  N  N   . GLY B 1 576 ? -12.271 103.104 15.584  1.00 18.84  ? 585  GLY B N   1 
ATOM   9348  C  CA  . GLY B 1 576 ? -12.670 102.836 14.198  1.00 19.63  ? 585  GLY B CA  1 
ATOM   9349  C  C   . GLY B 1 576 ? -11.808 101.874 13.389  1.00 19.10  ? 585  GLY B C   1 
ATOM   9350  O  O   . GLY B 1 576 ? -10.799 101.363 13.850  1.00 19.09  ? 585  GLY B O   1 
ATOM   9351  N  N   . ILE B 1 577 ? -12.244 101.628 12.146  1.00 17.93  ? 586  ILE B N   1 
ATOM   9352  C  CA  . ILE B 1 577 ? -11.543 100.767 11.203  1.00 17.02  ? 586  ILE B CA  1 
ATOM   9353  C  C   . ILE B 1 577 ? -10.882 101.675 10.256  1.00 18.77  ? 586  ILE B C   1 
ATOM   9354  O  O   . ILE B 1 577 ? -11.456 102.728 9.944   1.00 18.77  ? 586  ILE B O   1 
ATOM   9355  C  CB  . ILE B 1 577 ? -12.486 99.736  10.530  1.00 18.73  ? 586  ILE B CB  1 
ATOM   9356  C  CG1 . ILE B 1 577 ? -13.552 100.362 9.587   1.00 22.54  ? 586  ILE B CG1 1 
ATOM   9357  C  CG2 . ILE B 1 577 ? -13.184 98.947  11.683  1.00 19.24  ? 586  ILE B CG2 1 
ATOM   9358  C  CD1 . ILE B 1 577 ? -14.328 99.153  8.783   1.00 24.65  ? 586  ILE B CD1 1 
ATOM   9359  N  N   . LYS B 1 578 ? -9.701  101.333 9.782   1.00 17.49  ? 587  LYS B N   1 
ATOM   9360  C  CA  . LYS B 1 578 ? -8.987  102.266 8.914   1.00 24.03  ? 587  LYS B CA  1 
ATOM   9361  C  C   . LYS B 1 578 ? -7.973  101.601 8.049   1.00 21.24  ? 587  LYS B C   1 
ATOM   9362  O  O   . LYS B 1 578 ? -7.710  100.413 8.209   1.00 18.36  ? 587  LYS B O   1 
ATOM   9363  C  CB  . LYS B 1 578 ? -8.233  103.270 9.741   1.00 26.28  ? 587  LYS B CB  1 
ATOM   9364  C  CG  . LYS B 1 578 ? -7.530  102.667 10.891  1.00 30.79  ? 587  LYS B CG  1 
ATOM   9365  C  CD  . LYS B 1 578 ? -7.156  103.777 11.947  1.00 38.46  ? 587  LYS B CD  1 
ATOM   9366  C  CE  . LYS B 1 578 ? -8.330  104.187 12.744  1.00 49.01  ? 587  LYS B CE  1 
ATOM   9367  N  NZ  . LYS B 1 578 ? -7.958  105.190 13.785  1.00 56.95  ? 587  LYS B NZ  1 
ATOM   9368  N  N   . THR B 1 579 ? -7.450  102.364 7.083   1.00 19.36  ? 588  THR B N   1 
ATOM   9369  C  CA  . THR B 1 579 ? -6.413  101.850 6.188   1.00 18.02  ? 588  THR B CA  1 
ATOM   9370  C  C   . THR B 1 579 ? -5.203  102.789 6.293   1.00 20.37  ? 588  THR B C   1 
ATOM   9371  O  O   . THR B 1 579 ? -5.292  103.911 6.794   1.00 20.04  ? 588  THR B O   1 
ATOM   9372  C  CB  . THR B 1 579 ? -6.926  101.815 4.742   1.00 21.48  ? 588  THR B CB  1 
ATOM   9373  O  OG1 . THR B 1 579 ? -7.191  103.186 4.370   1.00 22.15  ? 588  THR B OG1 1 
ATOM   9374  C  CG2 . THR B 1 579 ? -8.178  100.959 4.616   1.00 23.38  ? 588  THR B CG2 1 
ATOM   9375  N  N   . ARG B 1 580 ? -4.065  102.331 5.835   1.00 19.82  ? 589  ARG B N   1 
ATOM   9376  C  CA  . ARG B 1 580 ? -2.879  103.174 5.789   1.00 22.64  ? 589  ARG B CA  1 
ATOM   9377  C  C   . ARG B 1 580 ? -2.067  102.683 4.585   1.00 21.20  ? 589  ARG B C   1 
ATOM   9378  O  O   . ARG B 1 580 ? -1.965  101.477 4.385   1.00 21.42  ? 589  ARG B O   1 
ATOM   9379  C  CB  . ARG B 1 580 ? -2.048  103.049 7.101   1.00 24.11  ? 589  ARG B CB  1 
ATOM   9380  C  CG  . ARG B 1 580 ? -1.099  104.212 7.133   1.00 34.31  ? 589  ARG B CG  1 
ATOM   9381  C  CD  . ARG B 1 580 ? -0.223  104.288 8.389   1.00 40.50  ? 589  ARG B CD  1 
ATOM   9382  N  NE  . ARG B 1 580 ? 1.113   104.756 8.017   1.00 50.52  ? 589  ARG B NE  1 
ATOM   9383  C  CZ  . ARG B 1 580 ? 2.129   104.832 8.868   1.00 57.87  ? 589  ARG B CZ  1 
ATOM   9384  N  NH1 . ARG B 1 580 ? 1.957   104.504 10.146  1.00 54.87  ? 589  ARG B NH1 1 
ATOM   9385  N  NH2 . ARG B 1 580 ? 3.331   105.208 8.443   1.00 60.47  ? 589  ARG B NH2 1 
ATOM   9386  N  N   . THR B 1 581 ? -1.514  103.576 3.786   1.00 18.98  ? 590  THR B N   1 
ATOM   9387  C  CA  . THR B 1 581 ? -0.766  103.147 2.626   1.00 16.99  ? 590  THR B CA  1 
ATOM   9388  C  C   . THR B 1 581 ? 0.567   103.854 2.473   1.00 14.96  ? 590  THR B C   1 
ATOM   9389  O  O   . THR B 1 581 ? 0.793   104.962 2.958   1.00 17.73  ? 590  THR B O   1 
ATOM   9390  C  CB  . THR B 1 581 ? -1.554  103.463 1.304   1.00 15.60  ? 590  THR B CB  1 
ATOM   9391  O  OG1 . THR B 1 581 ? -1.873  104.858 1.271   1.00 16.66  ? 590  THR B OG1 1 
ATOM   9392  C  CG2 . THR B 1 581 ? -2.892  102.704 1.199   1.00 18.61  ? 590  THR B CG2 1 
ATOM   9393  N  N   . LEU B 1 582 ? 1.478   103.129 1.760   1.00 17.77  ? 591  LEU B N   1 
ATOM   9394  C  CA  . LEU B 1 582 ? 2.765   103.652 1.355   1.00 18.61  ? 591  LEU B CA  1 
ATOM   9395  C  C   . LEU B 1 582 ? 2.487   104.706 0.258   1.00 18.93  ? 591  LEU B C   1 
ATOM   9396  O  O   . LEU B 1 582 ? 1.337   104.878 -0.159  1.00 16.80  ? 591  LEU B O   1 
ATOM   9397  C  CB  . LEU B 1 582 ? 3.601   102.519 0.692   1.00 19.50  ? 591  LEU B CB  1 
ATOM   9398  C  CG  . LEU B 1 582 ? 3.722   101.274 1.585   1.00 19.12  ? 591  LEU B CG  1 
ATOM   9399  C  CD1 . LEU B 1 582 ? 4.514   100.227 0.779   1.00 18.79  ? 591  LEU B CD1 1 
ATOM   9400  C  CD2 . LEU B 1 582 ? 4.411   101.709 2.873   1.00 22.53  ? 591  LEU B CD2 1 
ATOM   9401  N  N   . ASP B 1 583 ? 3.530   105.379 -0.214  1.00 19.63  ? 592  ASP B N   1 
ATOM   9402  C  CA  . ASP B 1 583 ? 3.386   106.404 -1.282  1.00 20.86  ? 592  ASP B CA  1 
ATOM   9403  C  C   . ASP B 1 583 ? 2.860   105.865 -2.572  1.00 24.29  ? 592  ASP B C   1 
ATOM   9404  O  O   . ASP B 1 583 ? 2.278   106.624 -3.369  1.00 22.57  ? 592  ASP B O   1 
ATOM   9405  C  CB  . ASP B 1 583 ? 4.766   107.058 -1.566  1.00 26.43  ? 592  ASP B CB  1 
ATOM   9406  C  CG  . ASP B 1 583 ? 5.432   107.615 -0.338  1.00 38.84  ? 592  ASP B CG  1 
ATOM   9407  O  OD1 . ASP B 1 583 ? 6.677   107.843 -0.376  1.00 40.06  ? 592  ASP B OD1 1 
ATOM   9408  O  OD2 . ASP B 1 583 ? 4.736   107.815 0.678   1.00 37.91  ? 592  ASP B OD2 1 
ATOM   9409  N  N   . ASN B 1 584 ? 3.054   104.570 -2.841  1.00 22.49  ? 593  ASN B N   1 
ATOM   9410  C  CA  . ASN B 1 584 ? 2.534   104.024 -4.100  1.00 23.84  ? 593  ASN B CA  1 
ATOM   9411  C  C   . ASN B 1 584 ? 1.144   103.489 -3.947  1.00 24.04  ? 593  ASN B C   1 
ATOM   9412  O  O   . ASN B 1 584 ? 0.639   102.866 -4.871  1.00 26.34  ? 593  ASN B O   1 
ATOM   9413  C  CB  . ASN B 1 584 ? 3.439   102.892 -4.628  1.00 27.45  ? 593  ASN B CB  1 
ATOM   9414  C  CG  . ASN B 1 584 ? 3.569   101.716 -3.701  1.00 29.65  ? 593  ASN B CG  1 
ATOM   9415  O  OD1 . ASN B 1 584 ? 2.858   101.615 -2.686  1.00 23.97  ? 593  ASN B OD1 1 
ATOM   9416  N  ND2 . ASN B 1 584 ? 4.455   100.777 -3.943  1.00 29.10  ? 593  ASN B ND2 1 
ATOM   9417  N  N   . GLY B 1 585 ? 0.476   103.699 -2.809  1.00 19.53  ? 594  GLY B N   1 
ATOM   9418  C  CA  . GLY B 1 585 ? -0.903  103.241 -2.709  1.00 18.76  ? 594  GLY B CA  1 
ATOM   9419  C  C   . GLY B 1 585 ? -1.063  101.831 -2.148  1.00 20.09  ? 594  GLY B C   1 
ATOM   9420  O  O   . GLY B 1 585 ? -2.193  101.418 -1.916  1.00 20.38  ? 594  GLY B O   1 
ATOM   9421  N  N   . LYS B 1 586 ? 0.042   101.096 -1.924  1.00 17.68  ? 595  LYS B N   1 
ATOM   9422  C  CA  . LYS B 1 586 ? -0.109  99.731  -1.342  1.00 17.90  ? 595  LYS B CA  1 
ATOM   9423  C  C   . LYS B 1 586 ? -0.210  99.832  0.160   1.00 16.50  ? 595  LYS B C   1 
ATOM   9424  O  O   . LYS B 1 586 ? 0.220   100.816 0.727   1.00 17.34  ? 595  LYS B O   1 
ATOM   9425  C  CB  . LYS B 1 586 ? 1.083   98.866  -1.672  1.00 19.42  ? 595  LYS B CB  1 
ATOM   9426  C  CG  . LYS B 1 586 ? 1.075   98.566  -3.162  1.00 27.09  ? 595  LYS B CG  1 
ATOM   9427  C  CD  . LYS B 1 586 ? 2.203   97.636  -3.471  1.00 42.46  ? 595  LYS B CD  1 
ATOM   9428  C  CE  . LYS B 1 586 ? 2.693   97.837  -4.881  1.00 54.88  ? 595  LYS B CE  1 
ATOM   9429  N  NZ  . LYS B 1 586 ? 2.991   96.524  -5.499  1.00 58.27  ? 595  LYS B NZ  1 
ATOM   9430  N  N   . ASP B 1 587 ? -0.754  98.792  0.795   1.00 16.82  ? 596  ASP B N   1 
ATOM   9431  C  CA  . ASP B 1 587 ? -0.943  98.837  2.261   1.00 15.03  ? 596  ASP B CA  1 
ATOM   9432  C  C   . ASP B 1 587 ? 0.404   99.034  2.967   1.00 16.87  ? 596  ASP B C   1 
ATOM   9433  O  O   . ASP B 1 587 ? 1.426   98.493  2.519   1.00 17.00  ? 596  ASP B O   1 
ATOM   9434  C  CB  . ASP B 1 587 ? -1.580  97.504  2.747   1.00 15.20  ? 596  ASP B CB  1 
ATOM   9435  C  CG  . ASP B 1 587 ? -3.059  97.422  2.297   1.00 19.69  ? 596  ASP B CG  1 
ATOM   9436  O  OD1 . ASP B 1 587 ? -3.845  98.326  2.656   1.00 19.31  ? 596  ASP B OD1 1 
ATOM   9437  O  OD2 . ASP B 1 587 ? -3.402  96.484  1.563   1.00 21.18  ? 596  ASP B OD2 1 
ATOM   9438  N  N   . TYR B 1 588 ? 0.370   99.794  4.076   1.00 16.45  ? 597  TYR B N   1 
ATOM   9439  C  CA  . TYR B 1 588 ? 1.553   100.063 4.882   1.00 17.42  ? 597  TYR B CA  1 
ATOM   9440  C  C   . TYR B 1 588 ? 1.948   98.822  5.695   1.00 17.65  ? 597  TYR B C   1 
ATOM   9441  O  O   . TYR B 1 588 ? 3.142   98.481  5.767   1.00 16.31  ? 597  TYR B O   1 
ATOM   9442  C  CB  . TYR B 1 588 ? 1.206   101.251 5.806   1.00 17.06  ? 597  TYR B CB  1 
ATOM   9443  C  CG  . TYR B 1 588 ? 2.232   101.371 6.907   1.00 22.85  ? 597  TYR B CG  1 
ATOM   9444  C  CD1 . TYR B 1 588 ? 1.946   100.942 8.204   1.00 23.45  ? 597  TYR B CD1 1 
ATOM   9445  C  CD2 . TYR B 1 588 ? 3.485   101.934 6.657   1.00 28.13  ? 597  TYR B CD2 1 
ATOM   9446  C  CE1 . TYR B 1 588 ? 2.872   101.095 9.227   1.00 26.98  ? 597  TYR B CE1 1 
ATOM   9447  C  CE2 . TYR B 1 588 ? 4.432   102.069 7.678   1.00 32.28  ? 597  TYR B CE2 1 
ATOM   9448  C  CZ  . TYR B 1 588 ? 4.115   101.659 8.957   1.00 36.98  ? 597  TYR B CZ  1 
ATOM   9449  O  OH  . TYR B 1 588 ? 5.051   101.780 9.962   1.00 41.30  ? 597  TYR B OH  1 
ATOM   9450  N  N   . LEU B 1 589 ? 0.988   98.132  6.295   1.00 15.22  ? 598  LEU B N   1 
ATOM   9451  C  CA  . LEU B 1 589 ? 1.333   96.943  7.100   1.00 18.01  ? 598  LEU B CA  1 
ATOM   9452  C  C   . LEU B 1 589 ? 1.787   95.809  6.237   1.00 18.84  ? 598  LEU B C   1 
ATOM   9453  O  O   . LEU B 1 589 ? 1.086   95.396  5.303   1.00 18.11  ? 598  LEU B O   1 
ATOM   9454  C  CB  . LEU B 1 589 ? 0.105   96.504  7.902   1.00 17.05  ? 598  LEU B CB  1 
ATOM   9455  C  CG  . LEU B 1 589 ? -0.244  97.531  8.982   1.00 18.48  ? 598  LEU B CG  1 
ATOM   9456  C  CD1 . LEU B 1 589 ? -1.663  97.099  9.605   1.00 17.69  ? 598  LEU B CD1 1 
ATOM   9457  C  CD2 . LEU B 1 589 ? 0.803   97.501  10.186  1.00 20.47  ? 598  LEU B CD2 1 
ATOM   9458  N  N   . TYR B 1 590 ? 2.947   95.258  6.544   1.00 17.96  ? 599  TYR B N   1 
ATOM   9459  C  CA  . TYR B 1 590 ? 3.541   94.170  5.742   1.00 16.06  ? 599  TYR B CA  1 
ATOM   9460  C  C   . TYR B 1 590 ? 2.567   92.931  5.568   1.00 15.32  ? 599  TYR B C   1 
ATOM   9461  O  O   . TYR B 1 590 ? 2.433   92.399  4.460   1.00 18.58  ? 599  TYR B O   1 
ATOM   9462  C  CB  . TYR B 1 590 ? 4.822   93.721  6.513   1.00 16.15  ? 599  TYR B CB  1 
ATOM   9463  C  CG  . TYR B 1 590 ? 5.714   92.778  5.734   1.00 17.11  ? 599  TYR B CG  1 
ATOM   9464  C  CD1 . TYR B 1 590 ? 5.295   91.474  5.424   1.00 16.85  ? 599  TYR B CD1 1 
ATOM   9465  C  CD2 . TYR B 1 590 ? 6.969   93.195  5.280   1.00 18.47  ? 599  TYR B CD2 1 
ATOM   9466  C  CE1 . TYR B 1 590 ? 6.118   90.612  4.704   1.00 16.87  ? 599  TYR B CE1 1 
ATOM   9467  C  CE2 . TYR B 1 590 ? 7.760   92.368  4.507   1.00 19.97  ? 599  TYR B CE2 1 
ATOM   9468  C  CZ  . TYR B 1 590 ? 7.340   91.080  4.230   1.00 23.11  ? 599  TYR B CZ  1 
ATOM   9469  O  OH  . TYR B 1 590 ? 8.166   90.303  3.443   1.00 23.00  ? 599  TYR B OH  1 
ATOM   9470  N  N   . VAL B 1 591 ? 1.909   92.514  6.667   1.00 16.80  ? 600  VAL B N   1 
ATOM   9471  C  CA  . VAL B 1 591 ? 1.045   91.336  6.637   1.00 18.66  ? 600  VAL B CA  1 
ATOM   9472  C  C   . VAL B 1 591 ? -0.239  91.615  5.844   1.00 17.94  ? 600  VAL B C   1 
ATOM   9473  O  O   . VAL B 1 591 ? -0.964  90.675  5.588   1.00 18.09  ? 600  VAL B O   1 
ATOM   9474  C  CB  . VAL B 1 591 ? 0.705   90.739  8.046   1.00 18.16  ? 600  VAL B CB  1 
ATOM   9475  C  CG1 . VAL B 1 591 ? 2.022   90.423  8.739   1.00 18.70  ? 600  VAL B CG1 1 
ATOM   9476  C  CG2 . VAL B 1 591 ? -0.142  91.677  8.913   1.00 17.70  ? 600  VAL B CG2 1 
ATOM   9477  N  N   . LEU B 1 592 ? -0.524  92.900  5.498   1.00 16.21  ? 601  LEU B N   1 
ATOM   9478  C  CA  . LEU B 1 592 ? -1.653  93.157  4.590   1.00 15.63  ? 601  LEU B CA  1 
ATOM   9479  C  C   . LEU B 1 592 ? -1.053  93.252  3.143   1.00 17.86  ? 601  LEU B C   1 
ATOM   9480  O  O   . LEU B 1 592 ? -1.514  92.569  2.218   1.00 19.88  ? 601  LEU B O   1 
ATOM   9481  C  CB  . LEU B 1 592 ? -2.341  94.485  4.909   1.00 15.82  ? 601  LEU B CB  1 
ATOM   9482  C  CG  . LEU B 1 592 ? -3.528  94.313  5.927   1.00 20.26  ? 601  LEU B CG  1 
ATOM   9483  C  CD1 . LEU B 1 592 ? -3.084  93.648  7.269   1.00 19.78  ? 601  LEU B CD1 1 
ATOM   9484  C  CD2 . LEU B 1 592 ? -4.107  95.793  6.287   1.00 20.74  ? 601  LEU B CD2 1 
ATOM   9485  N  N   . ARG B 1 593 ? 0.004   94.065  2.956   1.00 15.72  ? 602  ARG B N   1 
ATOM   9486  C  CA  . ARG B 1 593 ? 0.553   94.299  1.611   1.00 18.11  ? 602  ARG B CA  1 
ATOM   9487  C  C   . ARG B 1 593 ? 1.022   93.023  0.958   1.00 18.72  ? 602  ARG B C   1 
ATOM   9488  O  O   . ARG B 1 593 ? 0.770   92.827  -0.222  1.00 20.88  ? 602  ARG B O   1 
ATOM   9489  C  CB  . ARG B 1 593 ? 1.803   95.229  1.697   1.00 16.30  ? 602  ARG B CB  1 
ATOM   9490  C  CG  . ARG B 1 593 ? 2.401   95.659  0.297   1.00 16.51  ? 602  ARG B CG  1 
ATOM   9491  C  CD  . ARG B 1 593 ? 3.401   96.814  0.491   1.00 16.88  ? 602  ARG B CD  1 
ATOM   9492  N  NE  . ARG B 1 593 ? 4.602   96.337  1.222   1.00 15.41  ? 602  ARG B NE  1 
ATOM   9493  C  CZ  . ARG B 1 593 ? 4.866   96.534  2.520   1.00 19.29  ? 602  ARG B CZ  1 
ATOM   9494  N  NH1 . ARG B 1 593 ? 4.035   97.253  3.280   1.00 14.66  ? 602  ARG B NH1 1 
ATOM   9495  N  NH2 . ARG B 1 593 ? 5.955   96.003  3.070   1.00 15.50  ? 602  ARG B NH2 1 
ATOM   9496  N  N   . ASN B 1 594 ? 1.684   92.159  1.723   1.00 18.23  ? 603  ASN B N   1 
ATOM   9497  C  CA  . ASN B 1 594 ? 2.294   90.970  1.101   1.00 19.29  ? 603  ASN B CA  1 
ATOM   9498  C  C   . ASN B 1 594 ? 1.458   89.722  1.262   1.00 21.84  ? 603  ASN B C   1 
ATOM   9499  O  O   . ASN B 1 594 ? 1.929   88.599  1.018   1.00 20.13  ? 603  ASN B O   1 
ATOM   9500  C  CB  . ASN B 1 594 ? 3.692   90.777  1.708   1.00 21.43  ? 603  ASN B CB  1 
ATOM   9501  C  CG  . ASN B 1 594 ? 4.622   91.860  1.204   1.00 24.40  ? 603  ASN B CG  1 
ATOM   9502  O  OD1 . ASN B 1 594 ? 4.627   92.150  0.011   1.00 22.86  ? 603  ASN B OD1 1 
ATOM   9503  N  ND2 . ASN B 1 594 ? 5.365   92.560  2.050   1.00 19.29  ? 603  ASN B ND2 1 
ATOM   9504  N  N   . ASN B 1 595 ? 0.201   89.911  1.673   1.00 18.58  ? 604  ASN B N   1 
ATOM   9505  C  CA  . ASN B 1 595 ? -0.682  88.761  1.801   1.00 17.65  ? 604  ASN B CA  1 
ATOM   9506  C  C   . ASN B 1 595 ? -1.552  88.639  0.567   1.00 19.43  ? 604  ASN B C   1 
ATOM   9507  O  O   . ASN B 1 595 ? -2.173  89.626  0.173   1.00 21.16  ? 604  ASN B O   1 
ATOM   9508  C  CB  . ASN B 1 595 ? -1.596  88.998  2.999   1.00 19.57  ? 604  ASN B CB  1 
ATOM   9509  C  CG  . ASN B 1 595 ? -1.893  87.747  3.778   1.00 22.59  ? 604  ASN B CG  1 
ATOM   9510  O  OD1 . ASN B 1 595 ? -2.285  86.718  3.192   1.00 21.08  ? 604  ASN B OD1 1 
ATOM   9511  N  ND2 . ASN B 1 595 ? -1.761  87.763  5.120   1.00 17.82  ? 604  ASN B ND2 1 
ATOM   9512  N  N   . ASN B 1 596 ? -1.641  87.447  -0.013  1.00 19.31  ? 605  ASN B N   1 
ATOM   9513  C  CA  . ASN B 1 596 ? -2.522  87.260  -1.144  1.00 22.07  ? 605  ASN B CA  1 
ATOM   9514  C  C   . ASN B 1 596 ? -3.920  86.921  -0.687  1.00 23.15  ? 605  ASN B C   1 
ATOM   9515  O  O   . ASN B 1 596 ? -4.789  86.746  -1.542  1.00 23.70  ? 605  ASN B O   1 
ATOM   9516  C  CB  . ASN B 1 596 ? -2.010  86.148  -2.092  1.00 23.27  ? 605  ASN B CB  1 
ATOM   9517  C  CG  . ASN B 1 596 ? -0.652  86.485  -2.687  1.00 30.79  ? 605  ASN B CG  1 
ATOM   9518  O  OD1 . ASN B 1 596 ? -0.405  87.641  -2.990  1.00 31.16  ? 605  ASN B OD1 1 
ATOM   9519  N  ND2 . ASN B 1 596 ? 0.295   85.551  -2.786  1.00 33.46  ? 605  ASN B ND2 1 
ATOM   9520  N  N   . TYR B 1 597 ? -4.177  86.877  0.614   1.00 20.38  ? 606  TYR B N   1 
ATOM   9521  C  CA  . TYR B 1 597 ? -5.498  86.518  1.153   1.00 20.39  ? 606  TYR B CA  1 
ATOM   9522  C  C   . TYR B 1 597 ? -6.040  87.653  2.026   1.00 20.52  ? 606  TYR B C   1 
ATOM   9523  O  O   . TYR B 1 597 ? -5.262  88.518  2.450   1.00 19.68  ? 606  TYR B O   1 
ATOM   9524  C  CB  . TYR B 1 597 ? -5.359  85.154  1.863   1.00 19.32  ? 606  TYR B CB  1 
ATOM   9525  C  CG  . TYR B 1 597 ? -4.967  84.131  0.799   1.00 21.56  ? 606  TYR B CG  1 
ATOM   9526  C  CD1 . TYR B 1 597 ? -5.926  83.591  -0.063  1.00 25.65  ? 606  TYR B CD1 1 
ATOM   9527  C  CD2 . TYR B 1 597 ? -3.634  83.831  0.551   1.00 21.70  ? 606  TYR B CD2 1 
ATOM   9528  C  CE1 . TYR B 1 597 ? -5.563  82.810  -1.154  1.00 24.11  ? 606  TYR B CE1 1 
ATOM   9529  C  CE2 . TYR B 1 597 ? -3.256  83.056  -0.556  1.00 23.23  ? 606  TYR B CE2 1 
ATOM   9530  C  CZ  . TYR B 1 597 ? -4.226  82.564  -1.406  1.00 27.44  ? 606  TYR B CZ  1 
ATOM   9531  O  OH  . TYR B 1 597 ? -3.858  81.873  -2.532  1.00 30.46  ? 606  TYR B OH  1 
ATOM   9532  N  N   . PRO B 1 598 ? -7.340  87.710  2.305   1.00 20.21  ? 607  PRO B N   1 
ATOM   9533  C  CA  . PRO B 1 598 ? -7.926  88.793  3.128   1.00 19.17  ? 607  PRO B CA  1 
ATOM   9534  C  C   . PRO B 1 598 ? -7.192  88.836  4.475   1.00 19.82  ? 607  PRO B C   1 
ATOM   9535  O  O   . PRO B 1 598 ? -7.025  87.783  5.090   1.00 17.85  ? 607  PRO B O   1 
ATOM   9536  C  CB  . PRO B 1 598 ? -9.368  88.352  3.288   1.00 19.25  ? 607  PRO B CB  1 
ATOM   9537  C  CG  . PRO B 1 598 ? -9.619  87.564  1.943   1.00 18.60  ? 607  PRO B CG  1 
ATOM   9538  C  CD  . PRO B 1 598 ? -8.362  86.726  1.877   1.00 19.76  ? 607  PRO B CD  1 
ATOM   9539  N  N   . ALA B 1 599 ? -6.716  90.001  4.857   1.00 17.41  ? 608  ALA B N   1 
ATOM   9540  C  CA  . ALA B 1 599 ? -5.939  90.168  6.105   1.00 18.08  ? 608  ALA B CA  1 
ATOM   9541  C  C   . ALA B 1 599 ? -6.338  91.455  6.821   1.00 17.29  ? 608  ALA B C   1 
ATOM   9542  O  O   . ALA B 1 599 ? -6.589  92.468  6.169   1.00 15.26  ? 608  ALA B O   1 
ATOM   9543  C  CB  . ALA B 1 599 ? -4.434  90.246  5.737   1.00 16.57  ? 608  ALA B CB  1 
ATOM   9544  N  N   . ILE B 1 600 ? -6.307  91.454  8.187   1.00 15.62  ? 609  ILE B N   1 
ATOM   9545  C  CA  . ILE B 1 600 ? -6.609  92.648  8.994   1.00 16.31  ? 609  ILE B CA  1 
ATOM   9546  C  C   . ILE B 1 600 ? -5.664  92.599  10.183  1.00 18.30  ? 609  ILE B C   1 
ATOM   9547  O  O   . ILE B 1 600 ? -5.078  91.535  10.445  1.00 16.40  ? 609  ILE B O   1 
ATOM   9548  C  CB  . ILE B 1 600 ? -8.066  92.712  9.556   1.00 16.35  ? 609  ILE B CB  1 
ATOM   9549  C  CG1 . ILE B 1 600 ? -8.341  91.404  10.367  1.00 19.73  ? 609  ILE B CG1 1 
ATOM   9550  C  CG2 . ILE B 1 600 ? -9.040  92.884  8.364   1.00 15.54  ? 609  ILE B CG2 1 
ATOM   9551  C  CD1 . ILE B 1 600 ? -9.627  91.389  11.162  1.00 21.01  ? 609  ILE B CD1 1 
ATOM   9552  N  N   . LEU B 1 601 ? -5.485  93.727  10.850  1.00 15.99  ? 610  LEU B N   1 
ATOM   9553  C  CA  . LEU B 1 601 ? -4.681  93.755  12.060  1.00 15.17  ? 610  LEU B CA  1 
ATOM   9554  C  C   . LEU B 1 601 ? -5.501  94.442  13.118  1.00 16.56  ? 610  LEU B C   1 
ATOM   9555  O  O   . LEU B 1 601 ? -5.927  95.610  12.957  1.00 15.73  ? 610  LEU B O   1 
ATOM   9556  C  CB  . LEU B 1 601 ? -3.388  94.524  11.782  1.00 15.19  ? 610  LEU B CB  1 
ATOM   9557  C  CG  . LEU B 1 601 ? -2.402  94.519  12.989  1.00 22.31  ? 610  LEU B CG  1 
ATOM   9558  C  CD1 . LEU B 1 601 ? -0.921  94.628  12.429  1.00 25.80  ? 610  LEU B CD1 1 
ATOM   9559  C  CD2 . LEU B 1 601 ? -2.683  95.679  13.880  1.00 21.83  ? 610  LEU B CD2 1 
ATOM   9560  N  N   . VAL B 1 602 ? -5.728  93.754  14.241  1.00 15.21  ? 611  VAL B N   1 
ATOM   9561  C  CA  . VAL B 1 602 ? -6.539  94.269  15.341  1.00 15.04  ? 611  VAL B CA  1 
ATOM   9562  C  C   . VAL B 1 602 ? -5.609  94.830  16.429  1.00 18.72  ? 611  VAL B C   1 
ATOM   9563  O  O   . VAL B 1 602 ? -4.731  94.090  16.879  1.00 20.40  ? 611  VAL B O   1 
ATOM   9564  C  CB  . VAL B 1 602 ? -7.356  93.068  15.962  1.00 18.03  ? 611  VAL B CB  1 
ATOM   9565  C  CG1 . VAL B 1 602 ? -8.184  93.563  17.178  1.00 15.92  ? 611  VAL B CG1 1 
ATOM   9566  C  CG2 . VAL B 1 602 ? -8.307  92.431  14.934  1.00 18.53  ? 611  VAL B CG2 1 
ATOM   9567  N  N   . GLU B 1 603 ? -5.761  96.118  16.819  1.00 15.98  ? 612  GLU B N   1 
ATOM   9568  C  CA  . GLU B 1 603 ? -4.970  96.671  17.953  1.00 21.82  ? 612  GLU B CA  1 
ATOM   9569  C  C   . GLU B 1 603 ? -6.030  96.654  19.062  1.00 29.34  ? 612  GLU B C   1 
ATOM   9570  O  O   . GLU B 1 603 ? -6.892  97.570  19.077  1.00 26.67  ? 612  GLU B O   1 
ATOM   9571  C  CB  . GLU B 1 603 ? -4.485  98.093  17.662  1.00 25.01  ? 612  GLU B CB  1 
ATOM   9572  C  CG  . GLU B 1 603 ? -3.594  98.165  16.462  1.00 34.40  ? 612  GLU B CG  1 
ATOM   9573  C  CD  . GLU B 1 603 ? -2.118  97.925  16.853  1.00 47.51  ? 612  GLU B CD  1 
ATOM   9574  O  OE1 . GLU B 1 603 ? -1.857  97.578  18.029  1.00 46.09  ? 612  GLU B OE1 1 
ATOM   9575  O  OE2 . GLU B 1 603 ? -1.238  98.088  15.985  1.00 51.58  ? 612  GLU B OE2 1 
ATOM   9576  N  N   . CYS B 1 604 ? -6.007  95.621  19.946  1.00 30.85  ? 613  CYS B N   1 
ATOM   9577  C  CA  . CYS B 1 604 ? -7.025  95.336  20.997  1.00 34.17  ? 613  CYS B CA  1 
ATOM   9578  C  C   . CYS B 1 604 ? -7.201  96.376  22.021  1.00 34.75  ? 613  CYS B C   1 
ATOM   9579  O  O   . CYS B 1 604 ? -8.326  96.558  22.507  1.00 31.55  ? 613  CYS B O   1 
ATOM   9580  C  CB  . CYS B 1 604 ? -6.700  94.035  21.720  1.00 32.10  ? 613  CYS B CB  1 
ATOM   9581  S  SG  . CYS B 1 604 ? -6.454  92.631  20.625  1.00 34.36  ? 613  CYS B SG  1 
ATOM   9582  N  N   . ALA B 1 605 ? -6.108  97.016  22.413  1.00 33.73  ? 614  ALA B N   1 
ATOM   9583  C  CA  . ALA B 1 605 ? -6.177  97.952  23.519  1.00 34.88  ? 614  ALA B CA  1 
ATOM   9584  C  C   . ALA B 1 605 ? -4.825  98.583  23.641  1.00 41.61  ? 614  ALA B C   1 
ATOM   9585  O  O   . ALA B 1 605 ? -3.912  98.111  22.937  1.00 41.46  ? 614  ALA B O   1 
ATOM   9586  C  CB  . ALA B 1 605 ? -6.495  97.210  24.797  1.00 37.56  ? 614  ALA B CB  1 
ATOM   9587  N  N   . PHE B 1 606 ? -4.661  99.637  24.490  1.00 42.54  ? 615  PHE B N   1 
ATOM   9588  C  CA  . PHE B 1 606 ? -3.326  100.236 24.629  1.00 48.89  ? 615  PHE B CA  1 
ATOM   9589  C  C   . PHE B 1 606 ? -2.698  99.566  25.847  1.00 51.27  ? 615  PHE B C   1 
ATOM   9590  O  O   . PHE B 1 606 ? -3.217  99.698  26.970  1.00 48.32  ? 615  PHE B O   1 
ATOM   9591  C  CB  . PHE B 1 606 ? -3.396  101.772 24.811  1.00 52.50  ? 615  PHE B CB  1 
ATOM   9592  C  CG  . PHE B 1 606 ? -3.436  102.553 23.509  1.00 54.42  ? 615  PHE B CG  1 
ATOM   9593  C  CD1 . PHE B 1 606 ? -4.565  102.521 22.691  1.00 56.40  ? 615  PHE B CD1 1 
ATOM   9594  C  CD2 . PHE B 1 606 ? -2.359  103.330 23.114  1.00 53.84  ? 615  PHE B CD2 1 
ATOM   9595  C  CE1 . PHE B 1 606 ? -4.610  103.256 21.506  1.00 57.40  ? 615  PHE B CE1 1 
ATOM   9596  C  CE2 . PHE B 1 606 ? -2.404  104.068 21.926  1.00 52.75  ? 615  PHE B CE2 1 
ATOM   9597  C  CZ  . PHE B 1 606 ? -3.527  104.028 21.127  1.00 52.88  ? 615  PHE B CZ  1 
ATOM   9598  N  N   . ILE B 1 607 ? -1.598  98.815  25.623  1.00 51.17  ? 616  ILE B N   1 
ATOM   9599  C  CA  . ILE B 1 607 ? -0.942  98.092  26.710  1.00 51.83  ? 616  ILE B CA  1 
ATOM   9600  C  C   . ILE B 1 607 ? -0.286  99.017  27.787  1.00 53.28  ? 616  ILE B C   1 
ATOM   9601  O  O   . ILE B 1 607 ? -0.022  98.538  28.880  1.00 54.97  ? 616  ILE B O   1 
ATOM   9602  C  CB  . ILE B 1 607 ? 0.084   97.125  26.102  1.00 51.46  ? 616  ILE B CB  1 
ATOM   9603  C  CG1 . ILE B 1 607 ? 0.305   95.953  27.063  1.00 51.77  ? 616  ILE B CG1 1 
ATOM   9604  C  CG2 . ILE B 1 607 ? 1.384   97.866  25.796  1.00 49.35  ? 616  ILE B CG2 1 
ATOM   9605  C  CD1 . ILE B 1 607 ? 0.931   94.758  26.402  1.00 52.46  ? 616  ILE B CD1 1 
ATOM   9606  N  N   . ASP B 1 608 ? -0.012  100.295 27.493  1.00 53.68  ? 617  ASP B N   1 
ATOM   9607  C  CA  . ASP B 1 608 ? 0.521   101.159 28.559  1.00 54.93  ? 617  ASP B CA  1 
ATOM   9608  C  C   . ASP B 1 608 ? -0.630  102.051 29.137  1.00 54.53  ? 617  ASP B C   1 
ATOM   9609  O  O   . ASP B 1 608 ? -0.348  102.976 29.896  1.00 54.15  ? 617  ASP B O   1 
ATOM   9610  C  CB  . ASP B 1 608 ? 1.669   102.068 28.056  1.00 52.63  ? 617  ASP B CB  1 
ATOM   9611  C  CG  . ASP B 1 608 ? 2.943   101.356 27.669  0.00 0.00   ? 617  ASP B CG  1 
ATOM   9612  O  OD1 . ASP B 1 608 ? 4.003   101.690 28.240  0.00 0.00   ? 617  ASP B OD1 1 
ATOM   9613  O  OD2 . ASP B 1 608 ? 2.885   100.475 26.789  0.00 0.00   ? 617  ASP B OD2 1 
ATOM   9614  N  N   . ASN B 1 609 ? -1.907  101.785 28.765  1.00 53.52  ? 618  ASN B N   1 
ATOM   9615  C  CA  . ASN B 1 609 ? -3.040  102.579 29.258  1.00 53.06  ? 618  ASN B CA  1 
ATOM   9616  C  C   . ASN B 1 609 ? -3.671  101.858 30.400  1.00 51.39  ? 618  ASN B C   1 
ATOM   9617  O  O   . ASN B 1 609 ? -4.164  100.741 30.224  1.00 49.96  ? 618  ASN B O   1 
ATOM   9618  C  CB  . ASN B 1 609 ? -4.118  102.824 28.185  1.00 51.53  ? 618  ASN B CB  1 
ATOM   9619  C  CG  . ASN B 1 609 ? -5.235  103.715 28.728  1.00 50.30  ? 618  ASN B CG  1 
ATOM   9620  O  OD1 . ASN B 1 609 ? -6.243  103.215 29.244  1.00 47.52  ? 618  ASN B OD1 1 
ATOM   9621  N  ND2 . ASN B 1 609 ? -5.101  105.034 28.682  1.00 45.50  ? 618  ASN B ND2 1 
ATOM   9622  N  N   . LYS B 1 610 ? -3.680  102.484 31.574  1.00 49.65  ? 619  LYS B N   1 
ATOM   9623  C  CA  . LYS B 1 610 ? -4.221  101.825 32.740  1.00 48.70  ? 619  LYS B CA  1 
ATOM   9624  C  C   . LYS B 1 610 ? -5.709  101.484 32.620  1.00 48.55  ? 619  LYS B C   1 
ATOM   9625  O  O   . LYS B 1 610 ? -6.110  100.375 32.973  1.00 48.45  ? 619  LYS B O   1 
ATOM   9626  C  CB  . LYS B 1 610 ? -3.980  102.673 34.016  1.00 48.99  ? 619  LYS B CB  1 
ATOM   9627  C  CG  . LYS B 1 610 ? -4.465  101.916 35.229  1.00 49.78  ? 619  LYS B CG  1 
ATOM   9628  C  CD  . LYS B 1 610 ? -4.007  102.547 36.521  1.00 56.26  ? 619  LYS B CD  1 
ATOM   9629  C  CE  . LYS B 1 610 ? -4.065  101.486 37.588  1.00 61.26  ? 619  LYS B CE  1 
ATOM   9630  N  NZ  . LYS B 1 610 ? -5.458  100.997 37.743  1.00 66.81  ? 619  LYS B NZ  1 
ATOM   9631  N  N   . SER B 1 611 ? -6.521  102.393 32.131  1.00 49.05  ? 620  SER B N   1 
ATOM   9632  C  CA  . SER B 1 611 ? -7.946  102.058 32.052  1.00 51.73  ? 620  SER B CA  1 
ATOM   9633  C  C   . SER B 1 611 ? -8.159  100.822 31.117  1.00 49.17  ? 620  SER B C   1 
ATOM   9634  O  O   . SER B 1 611 ? -8.931  99.920  31.449  1.00 48.41  ? 620  SER B O   1 
ATOM   9635  C  CB  . SER B 1 611 ? -8.736  103.266 31.559  1.00 49.07  ? 620  SER B CB  1 
ATOM   9636  O  OG  . SER B 1 611 ? -10.115 102.952 31.557  1.00 48.64  ? 620  SER B OG  1 
ATOM   9637  N  N   . ASP B 1 612 ? -7.457  100.792 29.978  1.00 46.62  ? 621  ASP B N   1 
ATOM   9638  C  CA  . ASP B 1 612 ? -7.573  99.674  29.062  1.00 46.74  ? 621  ASP B CA  1 
ATOM   9639  C  C   . ASP B 1 612 ? -7.076  98.384  29.731  1.00 45.80  ? 621  ASP B C   1 
ATOM   9640  O  O   . ASP B 1 612 ? -7.764  97.357  29.694  1.00 44.31  ? 621  ASP B O   1 
ATOM   9641  C  CB  . ASP B 1 612 ? -6.758  99.960  27.789  1.00 45.28  ? 621  ASP B CB  1 
ATOM   9642  C  CG  . ASP B 1 612 ? -7.473  100.923 26.839  1.00 46.48  ? 621  ASP B CG  1 
ATOM   9643  O  OD1 . ASP B 1 612 ? -6.909  101.226 25.766  1.00 46.92  ? 621  ASP B OD1 1 
ATOM   9644  O  OD2 . ASP B 1 612 ? -8.587  101.370 27.174  1.00 41.18  ? 621  ASP B OD2 1 
ATOM   9645  N  N   . MET B 1 613 ? -5.894  98.449  30.364  1.00 45.57  ? 622  MET B N   1 
ATOM   9646  C  CA  . MET B 1 613 ? -5.299  97.265  30.978  1.00 48.22  ? 622  MET B CA  1 
ATOM   9647  C  C   . MET B 1 613 ? -6.080  96.757  32.207  1.00 48.13  ? 622  MET B C   1 
ATOM   9648  O  O   . MET B 1 613 ? -6.044  95.539  32.475  1.00 46.93  ? 622  MET B O   1 
ATOM   9649  C  CB  . MET B 1 613 ? -3.835  97.563  31.281  1.00 46.46  ? 622  MET B CB  1 
ATOM   9650  C  CG  . MET B 1 613 ? -3.063  97.709  29.990  1.00 48.38  ? 622  MET B CG  1 
ATOM   9651  S  SD  . MET B 1 613 ? -3.097  96.108  29.107  1.00 54.15  ? 622  MET B SD  1 
ATOM   9652  C  CE  . MET B 1 613 ? -3.890  96.567  27.690  1.00 48.60  ? 622  MET B CE  1 
ATOM   9653  N  N   . ASP B 1 614 ? -6.798  97.630  32.928  1.00 46.25  ? 623  ASP B N   1 
ATOM   9654  C  CA  . ASP B 1 614 ? -7.599  97.144  34.068  1.00 47.60  ? 623  ASP B CA  1 
ATOM   9655  C  C   . ASP B 1 614 ? -8.681  96.149  33.561  1.00 48.17  ? 623  ASP B C   1 
ATOM   9656  O  O   . ASP B 1 614 ? -9.122  95.240  34.288  1.00 46.39  ? 623  ASP B O   1 
ATOM   9657  C  CB  . ASP B 1 614 ? -8.306  98.311  34.780  1.00 50.38  ? 623  ASP B CB  1 
ATOM   9658  C  CG  . ASP B 1 614 ? -7.376  99.159  35.647  1.00 59.89  ? 623  ASP B CG  1 
ATOM   9659  O  OD1 . ASP B 1 614 ? -6.266  98.681  35.978  1.00 59.53  ? 623  ASP B OD1 1 
ATOM   9660  O  OD2 . ASP B 1 614 ? -7.763  100.301 35.996  1.00 60.21  ? 623  ASP B OD2 1 
ATOM   9661  N  N   . LYS B 1 615 ? -9.115  96.332  32.287  1.00 44.98  ? 624  LYS B N   1 
ATOM   9662  C  CA  . LYS B 1 615 ? -10.136 95.456  31.722  1.00 41.42  ? 624  LYS B CA  1 
ATOM   9663  C  C   . LYS B 1 615 ? -9.529  94.155  31.212  1.00 38.78  ? 624  LYS B C   1 
ATOM   9664  O  O   . LYS B 1 615 ? -10.260 93.237  30.844  1.00 37.80  ? 624  LYS B O   1 
ATOM   9665  C  CB  . LYS B 1 615 ? -10.872 96.184  30.589  1.00 41.10  ? 624  LYS B CB  1 
ATOM   9666  C  CG  . LYS B 1 615 ? -11.525 97.447  31.105  1.00 45.10  ? 624  LYS B CG  1 
ATOM   9667  C  CD  . LYS B 1 615 ? -12.105 98.298  30.009  1.00 48.70  ? 624  LYS B CD  1 
ATOM   9668  C  CE  . LYS B 1 615 ? -12.951 99.382  30.670  1.00 52.07  ? 624  LYS B CE  1 
ATOM   9669  N  NZ  . LYS B 1 615 ? -12.170 100.621 30.908  1.00 49.57  ? 624  LYS B NZ  1 
ATOM   9670  N  N   . LEU B 1 616 ? -8.195  94.076  31.191  1.00 38.35  ? 625  LEU B N   1 
ATOM   9671  C  CA  . LEU B 1 616 ? -7.492  92.879  30.714  1.00 42.62  ? 625  LEU B CA  1 
ATOM   9672  C  C   . LEU B 1 616 ? -6.552  92.314  31.820  1.00 45.87  ? 625  LEU B C   1 
ATOM   9673  O  O   . LEU B 1 616 ? -5.531  91.689  31.537  1.00 44.89  ? 625  LEU B O   1 
ATOM   9674  C  CB  . LEU B 1 616 ? -6.726  93.282  29.447  1.00 42.08  ? 625  LEU B CB  1 
ATOM   9675  C  CG  . LEU B 1 616 ? -7.683  93.647  28.273  1.00 42.24  ? 625  LEU B CG  1 
ATOM   9676  C  CD1 . LEU B 1 616 ? -6.908  94.314  27.174  1.00 45.11  ? 625  LEU B CD1 1 
ATOM   9677  C  CD2 . LEU B 1 616 ? -8.383  92.359  27.715  1.00 36.80  ? 625  LEU B CD2 1 
ATOM   9678  N  N   . ASN B 1 617 ? -6.968  92.585  33.074  1.00 47.08  ? 626  ASN B N   1 
ATOM   9679  C  CA  . ASN B 1 617 ? -6.417  92.271  34.400  1.00 50.34  ? 626  ASN B CA  1 
ATOM   9680  C  C   . ASN B 1 617 ? -6.162  90.788  34.661  1.00 50.30  ? 626  ASN B C   1 
ATOM   9681  O  O   . ASN B 1 617 ? -5.263  90.456  35.423  1.00 49.87  ? 626  ASN B O   1 
ATOM   9682  C  CB  . ASN B 1 617 ? -7.522  92.670  35.489  1.00 52.07  ? 626  ASN B CB  1 
ATOM   9683  C  CG  . ASN B 1 617 ? -7.128  93.799  36.369  1.00 59.13  ? 626  ASN B CG  1 
ATOM   9684  O  OD1 . ASN B 1 617 ? -7.510  93.826  37.539  1.00 62.95  ? 626  ASN B OD1 1 
ATOM   9685  N  ND2 . ASN B 1 617 ? -6.400  94.814  35.885  1.00 64.57  ? 626  ASN B ND2 1 
ATOM   9686  N  N   . THR B 1 618 ? -6.970  89.902  34.083  1.00 44.53  ? 627  THR B N   1 
ATOM   9687  C  CA  . THR B 1 618 ? -6.852  88.489  34.411  1.00 37.56  ? 627  THR B CA  1 
ATOM   9688  C  C   . THR B 1 618 ? -6.860  87.655  33.160  1.00 35.92  ? 627  THR B C   1 
ATOM   9689  O  O   . THR B 1 618 ? -7.125  88.173  32.061  1.00 33.37  ? 627  THR B O   1 
ATOM   9690  C  CB  . THR B 1 618 ? -8.087  88.069  35.267  1.00 37.61  ? 627  THR B CB  1 
ATOM   9691  O  OG1 . THR B 1 618 ? -9.252  88.203  34.431  1.00 35.91  ? 627  THR B OG1 1 
ATOM   9692  C  CG2 . THR B 1 618 ? -8.311  88.981  36.512  1.00 35.32  ? 627  THR B CG2 1 
ATOM   9693  N  N   . ALA B 1 619 ? -6.612  86.355  33.326  1.00 33.56  ? 628  ALA B N   1 
ATOM   9694  C  CA  . ALA B 1 619 ? -6.599  85.445  32.204  1.00 31.57  ? 628  ALA B CA  1 
ATOM   9695  C  C   . ALA B 1 619 ? -7.992  85.360  31.639  1.00 34.14  ? 628  ALA B C   1 
ATOM   9696  O  O   . ALA B 1 619 ? -8.162  85.201  30.435  1.00 33.57  ? 628  ALA B O   1 
ATOM   9697  C  CB  . ALA B 1 619 ? -6.133  84.052  32.642  1.00 35.05  ? 628  ALA B CB  1 
ATOM   9698  N  N   . GLU B 1 620 ? -8.999  85.471  32.499  1.00 33.91  ? 629  GLU B N   1 
ATOM   9699  C  CA  . GLU B 1 620 ? -10.376 85.343  32.038  1.00 36.25  ? 629  GLU B CA  1 
ATOM   9700  C  C   . GLU B 1 620 ? -10.726 86.563  31.150  1.00 33.82  ? 629  GLU B C   1 
ATOM   9701  O  O   . GLU B 1 620 ? -11.427 86.392  30.149  1.00 32.39  ? 629  GLU B O   1 
ATOM   9702  C  CB  . GLU B 1 620 ? -11.309 85.200  33.282  1.00 38.89  ? 629  GLU B CB  1 
ATOM   9703  C  CG  . GLU B 1 620 ? -12.768 84.986  32.948  1.00 50.23  ? 629  GLU B CG  1 
ATOM   9704  C  CD  . GLU B 1 620 ? -13.017 83.758  32.067  1.00 62.81  ? 629  GLU B CD  1 
ATOM   9705  O  OE1 . GLU B 1 620 ? -13.550 83.945  30.970  1.00 66.99  ? 629  GLU B OE1 1 
ATOM   9706  O  OE2 . GLU B 1 620 ? -12.697 82.621  32.466  1.00 63.94  ? 629  GLU B OE2 1 
ATOM   9707  N  N   . LYS B 1 621 ? -10.243 87.766  31.487  1.00 29.86  ? 630  LYS B N   1 
ATOM   9708  C  CA  . LYS B 1 621 ? -10.555 88.913  30.630  1.00 30.85  ? 630  LYS B CA  1 
ATOM   9709  C  C   . LYS B 1 621 ? -9.836  88.816  29.263  1.00 30.34  ? 630  LYS B C   1 
ATOM   9710  O  O   . LYS B 1 621 ? -10.388 89.179  28.203  1.00 26.21  ? 630  LYS B O   1 
ATOM   9711  C  CB  . LYS B 1 621 ? -10.168 90.186  31.353  1.00 32.00  ? 630  LYS B CB  1 
ATOM   9712  C  CG  . LYS B 1 621 ? -11.050 90.319  32.644  1.00 36.24  ? 630  LYS B CG  1 
ATOM   9713  C  CD  . LYS B 1 621 ? -10.666 91.513  33.436  1.00 42.79  ? 630  LYS B CD  1 
ATOM   9714  C  CE  . LYS B 1 621 ? -11.432 91.555  34.765  1.00 50.06  ? 630  LYS B CE  1 
ATOM   9715  N  NZ  . LYS B 1 621 ? -11.156 92.835  35.492  1.00 50.15  ? 630  LYS B NZ  1 
ATOM   9716  N  N   . VAL B 1 622 ? -8.574  88.352  29.289  1.00 25.34  ? 631  VAL B N   1 
ATOM   9717  C  CA  . VAL B 1 622 ? -7.839  88.131  28.039  1.00 23.78  ? 631  VAL B CA  1 
ATOM   9718  C  C   . VAL B 1 622 ? -8.610  87.076  27.258  1.00 23.29  ? 631  VAL B C   1 
ATOM   9719  O  O   . VAL B 1 622 ? -8.728  87.155  26.026  1.00 22.50  ? 631  VAL B O   1 
ATOM   9720  C  CB  . VAL B 1 622 ? -6.387  87.685  28.376  1.00 26.98  ? 631  VAL B CB  1 
ATOM   9721  C  CG1 . VAL B 1 622 ? -5.739  87.035  27.139  1.00 26.10  ? 631  VAL B CG1 1 
ATOM   9722  C  CG2 . VAL B 1 622 ? -5.571  88.887  28.846  1.00 28.31  ? 631  VAL B CG2 1 
ATOM   9723  N  N   . LYS B 1 623 ? -9.173  86.082  27.936  1.00 23.34  ? 632  LYS B N   1 
ATOM   9724  C  CA  . LYS B 1 623 ? -9.904  85.055  27.191  1.00 25.49  ? 632  LYS B CA  1 
ATOM   9725  C  C   . LYS B 1 623 ? -11.177 85.682  26.548  1.00 26.60  ? 632  LYS B C   1 
ATOM   9726  O  O   . LYS B 1 623 ? -11.543 85.329  25.436  1.00 23.91  ? 632  LYS B O   1 
ATOM   9727  C  CB  . LYS B 1 623 ? -10.296 83.893  28.136  1.00 24.88  ? 632  LYS B CB  1 
ATOM   9728  C  CG  . LYS B 1 623 ? -11.102 82.788  27.455  1.00 24.11  ? 632  LYS B CG  1 
ATOM   9729  C  CD  . LYS B 1 623 ? -11.435 81.665  28.483  1.00 29.18  ? 632  LYS B CD  1 
ATOM   9730  C  CE  . LYS B 1 623 ? -12.062 80.526  27.735  1.00 35.95  ? 632  LYS B CE  1 
ATOM   9731  N  NZ  . LYS B 1 623 ? -13.189 79.961  28.503  1.00 52.39  ? 632  LYS B NZ  1 
ATOM   9732  N  N   . THR B 1 624 ? -11.819 86.591  27.255  1.00 23.05  ? 633  THR B N   1 
ATOM   9733  C  CA  . THR B 1 624 ? -13.003 87.251  26.709  1.00 24.97  ? 633  THR B CA  1 
ATOM   9734  C  C   . THR B 1 624 ? -12.627 88.040  25.472  1.00 22.07  ? 633  THR B C   1 
ATOM   9735  O  O   . THR B 1 624 ? -13.325 87.998  24.447  1.00 24.37  ? 633  THR B O   1 
ATOM   9736  C  CB  . THR B 1 624 ? -13.581 88.190  27.761  1.00 28.06  ? 633  THR B CB  1 
ATOM   9737  O  OG1 . THR B 1 624 ? -13.964 87.361  28.865  1.00 25.80  ? 633  THR B OG1 1 
ATOM   9738  C  CG2 . THR B 1 624 ? -14.791 88.996  27.178  1.00 25.89  ? 633  THR B CG2 1 
ATOM   9739  N  N   . MET B 1 625 ? -11.477 88.745  25.553  1.00 21.29  ? 634  MET B N   1 
ATOM   9740  C  CA  . MET B 1 625 ? -11.060 89.488  24.388  1.00 19.26  ? 634  MET B CA  1 
ATOM   9741  C  C   . MET B 1 625 ? -10.833 88.532  23.234  1.00 19.48  ? 634  MET B C   1 
ATOM   9742  O  O   . MET B 1 625 ? -11.327 88.793  22.113  1.00 17.70  ? 634  MET B O   1 
ATOM   9743  C  CB  . MET B 1 625 ? -9.773  90.323  24.678  1.00 20.97  ? 634  MET B CB  1 
ATOM   9744  C  CG  . MET B 1 625 ? -9.147  90.932  23.406  1.00 21.03  ? 634  MET B CG  1 
ATOM   9745  S  SD  . MET B 1 625 ? -10.210 92.349  22.837  1.00 22.10  ? 634  MET B SD  1 
ATOM   9746  C  CE  . MET B 1 625 ? -9.886  93.569  24.229  1.00 21.03  ? 634  MET B CE  1 
ATOM   9747  N  N   . GLY B 1 626 ? -10.095 87.418  23.429  1.00 19.54  ? 635  GLY B N   1 
ATOM   9748  C  CA  . GLY B 1 626 ? -9.854  86.506  22.294  1.00 16.25  ? 635  GLY B CA  1 
ATOM   9749  C  C   . GLY B 1 626 ? -11.169 85.906  21.805  1.00 18.11  ? 635  GLY B C   1 
ATOM   9750  O  O   . GLY B 1 626 ? -11.366 85.681  20.602  1.00 18.04  ? 635  GLY B O   1 
ATOM   9751  N  N   . THR B 1 627 ? -12.083 85.626  22.711  1.00 15.59  ? 636  THR B N   1 
ATOM   9752  C  CA  . THR B 1 627 ? -13.382 85.056  22.251  1.00 17.87  ? 636  THR B CA  1 
ATOM   9753  C  C   . THR B 1 627 ? -14.154 86.022  21.376  1.00 17.05  ? 636  THR B C   1 
ATOM   9754  O  O   . THR B 1 627 ? -14.674 85.581  20.349  1.00 18.60  ? 636  THR B O   1 
ATOM   9755  C  CB  . THR B 1 627 ? -14.268 84.722  23.482  1.00 22.54  ? 636  THR B CB  1 
ATOM   9756  O  OG1 . THR B 1 627 ? -13.538 83.714  24.216  1.00 23.18  ? 636  THR B OG1 1 
ATOM   9757  C  CG2 . THR B 1 627 ? -15.654 84.132  23.073  1.00 22.03  ? 636  THR B CG2 1 
ATOM   9758  N  N   . GLN B 1 628 ? -14.208 87.340  21.755  1.00 17.23  ? 637  GLN B N   1 
ATOM   9759  C  CA  . GLN B 1 628 ? -14.965 88.324  20.952  1.00 15.26  ? 637  GLN B CA  1 
ATOM   9760  C  C   . GLN B 1 628 ? -14.331 88.400  19.580  1.00 17.37  ? 637  GLN B C   1 
ATOM   9761  O  O   . GLN B 1 628 ? -15.030 88.452  18.544  1.00 19.47  ? 637  GLN B O   1 
ATOM   9762  C  CB  . GLN B 1 628 ? -14.977 89.705  21.655  1.00 17.80  ? 637  GLN B CB  1 
ATOM   9763  C  CG  . GLN B 1 628 ? -15.773 89.619  23.013  1.00 18.48  ? 637  GLN B CG  1 
ATOM   9764  C  CD  . GLN B 1 628 ? -17.142 88.999  22.887  1.00 20.68  ? 637  GLN B CD  1 
ATOM   9765  O  OE1 . GLN B 1 628 ? -17.397 87.873  23.391  1.00 21.34  ? 637  GLN B OE1 1 
ATOM   9766  N  NE2 . GLN B 1 628 ? -18.055 89.625  22.132  1.00 17.55  ? 637  GLN B NE2 1 
ATOM   9767  N  N   . ILE B 1 629 ? -12.975 88.416  19.532  1.00 16.42  ? 638  ILE B N   1 
ATOM   9768  C  CA  . ILE B 1 629 ? -12.392 88.460  18.200  1.00 15.66  ? 638  ILE B CA  1 
ATOM   9769  C  C   . ILE B 1 629 ? -12.808 87.222  17.431  1.00 17.17  ? 638  ILE B C   1 
ATOM   9770  O  O   . ILE B 1 629 ? -13.106 87.340  16.217  1.00 17.73  ? 638  ILE B O   1 
ATOM   9771  C  CB  . ILE B 1 629 ? -10.829 88.569  18.346  1.00 15.18  ? 638  ILE B CB  1 
ATOM   9772  C  CG1 . ILE B 1 629 ? -10.466 89.972  18.940  1.00 15.66  ? 638  ILE B CG1 1 
ATOM   9773  C  CG2 . ILE B 1 629 ? -10.154 88.353  16.911  1.00 14.51  ? 638  ILE B CG2 1 
ATOM   9774  C  CD1 . ILE B 1 629 ? -9.013  90.072  19.349  1.00 16.58  ? 638  ILE B CD1 1 
ATOM   9775  N  N   . GLY B 1 630 ? -12.822 86.005  18.055  1.00 18.27  ? 639  GLY B N   1 
ATOM   9776  C  CA  . GLY B 1 630 ? -13.221 84.816  17.326  1.00 15.67  ? 639  GLY B CA  1 
ATOM   9777  C  C   . GLY B 1 630 ? -14.671 84.910  16.809  1.00 17.53  ? 639  GLY B C   1 
ATOM   9778  O  O   . GLY B 1 630 ? -14.968 84.470  15.715  1.00 17.84  ? 639  GLY B O   1 
ATOM   9779  N  N   . ILE B 1 631 ? -15.555 85.497  17.620  1.00 18.91  ? 640  ILE B N   1 
ATOM   9780  C  CA  . ILE B 1 631 ? -16.976 85.644  17.193  1.00 18.68  ? 640  ILE B CA  1 
ATOM   9781  C  C   . ILE B 1 631 ? -17.051 86.539  15.983  1.00 18.45  ? 640  ILE B C   1 
ATOM   9782  O  O   . ILE B 1 631 ? -17.792 86.238  15.036  1.00 18.14  ? 640  ILE B O   1 
ATOM   9783  C  CB  . ILE B 1 631 ? -17.804 86.204  18.369  1.00 21.27  ? 640  ILE B CB  1 
ATOM   9784  C  CG1 . ILE B 1 631 ? -17.872 85.117  19.460  1.00 21.11  ? 640  ILE B CG1 1 
ATOM   9785  C  CG2 . ILE B 1 631 ? -19.232 86.566  17.908  1.00 19.55  ? 640  ILE B CG2 1 
ATOM   9786  C  CD1 . ILE B 1 631 ? -18.339 85.593  20.799  1.00 20.25  ? 640  ILE B CD1 1 
ATOM   9787  N  N   . GLY B 1 632 ? -16.257 87.653  16.033  1.00 16.68  ? 641  GLY B N   1 
ATOM   9788  C  CA  . GLY B 1 632 ? -16.213 88.594  14.932  1.00 16.37  ? 641  GLY B CA  1 
ATOM   9789  C  C   . GLY B 1 632 ? -15.739 87.912  13.653  1.00 18.82  ? 641  GLY B C   1 
ATOM   9790  O  O   . GLY B 1 632 ? -16.228 88.157  12.552  1.00 19.19  ? 641  GLY B O   1 
ATOM   9791  N  N   . ILE B 1 633 ? -14.690 87.038  13.782  1.00 17.38  ? 642  ILE B N   1 
ATOM   9792  C  CA  . ILE B 1 633 ? -14.188 86.322  12.595  1.00 15.05  ? 642  ILE B CA  1 
ATOM   9793  C  C   . ILE B 1 633 ? -15.254 85.336  12.106  1.00 15.81  ? 642  ILE B C   1 
ATOM   9794  O  O   . ILE B 1 633 ? -15.510 85.219  10.904  1.00 16.81  ? 642  ILE B O   1 
ATOM   9795  C  CB  . ILE B 1 633 ? -12.895 85.548  12.990  1.00 15.69  ? 642  ILE B CB  1 
ATOM   9796  C  CG1 . ILE B 1 633 ? -11.756 86.594  13.116  1.00 13.53  ? 642  ILE B CG1 1 
ATOM   9797  C  CG2 . ILE B 1 633 ? -12.508 84.491  11.932  1.00 17.35  ? 642  ILE B CG2 1 
ATOM   9798  C  CD1 . ILE B 1 633 ? -10.463 86.016  13.820  1.00 16.09  ? 642  ILE B CD1 1 
ATOM   9799  N  N   . GLU B 1 634 ? -15.850 84.614  13.046  1.00 16.47  ? 643  GLU B N   1 
ATOM   9800  C  CA  . GLU B 1 634 ? -16.885 83.636  12.693  1.00 18.28  ? 643  GLU B CA  1 
ATOM   9801  C  C   . GLU B 1 634 ? -18.057 84.362  11.951  1.00 21.11  ? 643  GLU B C   1 
ATOM   9802  O  O   . GLU B 1 634 ? -18.542 83.843  10.942  1.00 21.67  ? 643  GLU B O   1 
ATOM   9803  C  CB  . GLU B 1 634 ? -17.340 82.979  14.003  1.00 19.71  ? 643  GLU B CB  1 
ATOM   9804  C  CG  . GLU B 1 634 ? -18.502 81.991  13.827  1.00 22.78  ? 643  GLU B CG  1 
ATOM   9805  C  CD  . GLU B 1 634 ? -19.010 81.499  15.171  1.00 28.48  ? 643  GLU B CD  1 
ATOM   9806  O  OE1 . GLU B 1 634 ? -19.030 82.279  16.170  1.00 26.96  ? 643  GLU B OE1 1 
ATOM   9807  O  OE2 . GLU B 1 634 ? -19.382 80.317  15.239  1.00 29.48  ? 643  GLU B OE2 1 
ATOM   9808  N  N   . ASP B 1 635 ? -18.454 85.571  12.440  1.00 18.19  ? 644  ASP B N   1 
ATOM   9809  C  CA  . ASP B 1 635 ? -19.560 86.362  11.825  1.00 18.87  ? 644  ASP B CA  1 
ATOM   9810  C  C   . ASP B 1 635 ? -19.200 86.592  10.383  1.00 21.01  ? 644  ASP B C   1 
ATOM   9811  O  O   . ASP B 1 635 ? -20.053 86.589  9.529   1.00 21.76  ? 644  ASP B O   1 
ATOM   9812  C  CB  . ASP B 1 635 ? -19.680 87.783  12.398  1.00 17.70  ? 644  ASP B CB  1 
ATOM   9813  C  CG  . ASP B 1 635 ? -20.160 87.918  13.824  1.00 24.15  ? 644  ASP B CG  1 
ATOM   9814  O  OD1 . ASP B 1 635 ? -20.845 87.003  14.313  1.00 26.18  ? 644  ASP B OD1 1 
ATOM   9815  O  OD2 . ASP B 1 635 ? -19.859 88.962  14.449  1.00 25.17  ? 644  ASP B OD2 1 
ATOM   9816  N  N   . THR B 1 636 ? -17.916 86.835  10.110  1.00 18.52  ? 645  THR B N   1 
ATOM   9817  C  CA  . THR B 1 636 ? -17.493 87.151  8.755   1.00 19.52  ? 645  THR B CA  1 
ATOM   9818  C  C   . THR B 1 636 ? -17.324 85.970  7.832   1.00 24.28  ? 645  THR B C   1 
ATOM   9819  O  O   . THR B 1 636 ? -17.769 86.025  6.686   1.00 23.50  ? 645  THR B O   1 
ATOM   9820  C  CB  . THR B 1 636 ? -16.095 87.850  8.838   1.00 20.24  ? 645  THR B CB  1 
ATOM   9821  O  OG1 . THR B 1 636 ? -16.199 88.947  9.742   1.00 18.87  ? 645  THR B OG1 1 
ATOM   9822  C  CG2 . THR B 1 636 ? -15.628 88.316  7.505   1.00 22.08  ? 645  THR B CG2 1 
ATOM   9823  N  N   . VAL B 1 637 ? -16.659 84.890  8.277   1.00 22.50  ? 646  VAL B N   1 
ATOM   9824  C  CA  . VAL B 1 637 ? -16.345 83.844  7.300   1.00 22.55  ? 646  VAL B CA  1 
ATOM   9825  C  C   . VAL B 1 637 ? -17.380 82.737  7.230   1.00 28.15  ? 646  VAL B C   1 
ATOM   9826  O  O   . VAL B 1 637 ? -17.320 81.958  6.273   1.00 29.38  ? 646  VAL B O   1 
ATOM   9827  C  CB  . VAL B 1 637 ? -14.961 83.167  7.579   1.00 25.23  ? 646  VAL B CB  1 
ATOM   9828  C  CG1 . VAL B 1 637 ? -13.844 84.192  7.596   1.00 27.48  ? 646  VAL B CG1 1 
ATOM   9829  C  CG2 . VAL B 1 637 ? -14.972 82.409  8.888   1.00 21.95  ? 646  VAL B CG2 1 
ATOM   9830  N  N   . LYS B 1 638 ? -18.267 82.615  8.205   1.00 31.55  ? 647  LYS B N   1 
ATOM   9831  C  CA  . LYS B 1 638 ? -19.196 81.472  8.126   1.00 39.85  ? 647  LYS B CA  1 
ATOM   9832  C  C   . LYS B 1 638 ? -20.059 81.514  6.860   1.00 45.50  ? 647  LYS B C   1 
ATOM   9833  O  O   . LYS B 1 638 ? -20.318 82.585  6.305   1.00 47.68  ? 647  LYS B O   1 
ATOM   9834  C  CB  . LYS B 1 638 ? -20.100 81.428  9.324   1.00 40.01  ? 647  LYS B CB  1 
ATOM   9835  C  CG  . LYS B 1 638 ? -21.096 82.585  9.287   1.00 49.39  ? 647  LYS B CG  1 
ATOM   9836  C  CD  . LYS B 1 638 ? -21.806 82.643  10.612  1.00 56.42  ? 647  LYS B CD  1 
ATOM   9837  C  CE  . LYS B 1 638 ? -22.338 83.978  10.945  1.00 59.31  ? 647  LYS B CE  1 
ATOM   9838  N  NZ  . LYS B 1 638 ? -22.592 84.040  12.419  1.00 68.86  ? 647  LYS B NZ  1 
ATOM   9839  O  OXT . LYS B 1 638 ? -20.423 80.425  6.429   1.00 48.76  ? 647  LYS B OXT 1 
HETATM 9840  CA CA  A CA  C 2 .   ? 35.774  98.258  10.929  0.70 45.58  ? 701  CA  A CA  1 
HETATM 9841  CA CA  B CA  C 2 .   ? 37.369  98.284  11.566  0.30 57.10  ? 701  CA  A CA  1 
HETATM 9842  CA CA  . CA  D 2 .   ? 52.088  71.471  31.589  1.00 60.14  ? 702  CA  A CA  1 
HETATM 9843  NA NA  . NA  E 3 .   ? 19.557  72.810  11.862  1.00 26.00  ? 703  NA  A NA  1 
HETATM 9844  CL CL  . CL  F 4 .   ? 28.307  91.225  7.654   1.00 25.58  ? 704  CL  A CL  1 
HETATM 9845  CL CL  . CL  G 4 .   ? 8.073   40.680  10.310  1.00 55.51  ? 705  CL  A CL  1 
HETATM 9846  CL CL  . CL  H 4 .   ? 27.196  89.719  18.444  1.00 56.35  ? 706  CL  A CL  1 
HETATM 9847  ZN ZN  . ZN  I 5 .   ? 25.073  43.740  13.711  0.69 36.08  ? 707  ZN  A ZN  1 
HETATM 9848  CA CA  . CA  J 2 .   ? 0.463   44.093  39.046  1.00 39.38  ? 701  CA  B CA  1 
HETATM 9849  CA CA  . CA  K 2 .   ? -3.644  34.438  35.110  1.00 61.35  ? 702  CA  B CA  1 
HETATM 9850  CA CA  . CA  L 2 .   ? -0.022  106.481 1.184   0.50 33.35  ? 703  CA  B CA  1 
HETATM 9851  NA NA  . NA  M 3 .   ? 7.937   66.503  20.478  1.00 22.05  ? 704  NA  B NA  1 
HETATM 9852  NA NA  . NA  N 3 .   ? -0.026  106.455 -4.903  0.50 44.37  ? 705  NA  B NA  1 
HETATM 9853  CL CL  . CL  O 4 .   ? 1.353   48.983  29.498  1.00 25.46  ? 706  CL  B CL  1 
HETATM 9854  CL CL  . CL  P 4 .   ? -18.440 61.304  31.935  1.00 37.52  ? 707  CL  B CL  1 
HETATM 9855  C  C1  . CIT Q 6 .   ? 7.972   94.349  0.518   1.00 49.34  ? 708  CIT B C1  1 
HETATM 9856  O  O1  . CIT Q 6 .   ? 8.709   93.477  -0.056  1.00 53.75  ? 708  CIT B O1  1 
HETATM 9857  O  O2  . CIT Q 6 .   ? 7.487   94.264  1.604   1.00 44.92  ? 708  CIT B O2  1 
HETATM 9858  C  C2  . CIT Q 6 .   ? 7.721   95.593  -0.239  1.00 54.82  ? 708  CIT B C2  1 
HETATM 9859  C  C3  . CIT Q 6 .   ? 6.797   95.384  -1.392  1.00 59.04  ? 708  CIT B C3  1 
HETATM 9860  O  O7  . CIT Q 6 .   ? 5.606   94.792  -0.887  1.00 55.76  ? 708  CIT B O7  1 
HETATM 9861  C  C4  . CIT Q 6 .   ? 6.594   96.790  -1.930  1.00 59.94  ? 708  CIT B C4  1 
HETATM 9862  C  C5  . CIT Q 6 .   ? 5.625   96.985  -3.048  1.00 66.60  ? 708  CIT B C5  1 
HETATM 9863  O  O3  . CIT Q 6 .   ? 5.124   95.952  -3.605  1.00 67.38  ? 708  CIT B O3  1 
HETATM 9864  O  O4  . CIT Q 6 .   ? 5.382   98.187  -3.342  1.00 66.54  ? 708  CIT B O4  1 
HETATM 9865  C  C6  . CIT Q 6 .   ? 7.458   94.395  -2.442  1.00 61.59  ? 708  CIT B C6  1 
HETATM 9866  O  O5  . CIT Q 6 .   ? 8.509   94.769  -3.018  1.00 65.46  ? 708  CIT B O5  1 
HETATM 9867  O  O6  . CIT Q 6 .   ? 6.942   93.248  -2.594  1.00 61.22  ? 708  CIT B O6  1 
HETATM 9868  C  C1  . CIT R 6 .   ? -11.775 74.370  33.335  1.00 53.80  ? 709  CIT B C1  1 
HETATM 9869  O  O1  . CIT R 6 .   ? -10.723 75.062  33.332  1.00 53.31  ? 709  CIT B O1  1 
HETATM 9870  O  O2  . CIT R 6 .   ? -11.777 73.155  33.483  1.00 51.34  ? 709  CIT B O2  1 
HETATM 9871  C  C2  . CIT R 6 .   ? -13.119 75.087  33.190  1.00 56.00  ? 709  CIT B C2  1 
HETATM 9872  C  C3  . CIT R 6 .   ? -14.090 74.581  32.085  1.00 53.35  ? 709  CIT B C3  1 
HETATM 9873  O  O7  . CIT R 6 .   ? -14.266 73.162  32.211  1.00 53.33  ? 709  CIT B O7  1 
HETATM 9874  C  C4  . CIT R 6 .   ? -15.480 75.275  32.203  1.00 55.34  ? 709  CIT B C4  1 
HETATM 9875  C  C5  . CIT R 6 .   ? -16.387 75.147  30.989  1.00 58.79  ? 709  CIT B C5  1 
HETATM 9876  O  O3  . CIT R 6 .   ? -16.075 74.373  30.053  1.00 57.11  ? 709  CIT B O3  1 
HETATM 9877  O  O4  . CIT R 6 .   ? -17.429 75.839  30.962  1.00 60.28  ? 709  CIT B O4  1 
HETATM 9878  C  C6  . CIT R 6 .   ? -13.476 74.918  30.674  1.00 50.60  ? 709  CIT B C6  1 
HETATM 9879  O  O5  . CIT R 6 .   ? -12.861 74.040  30.075  1.00 42.16  ? 709  CIT B O5  1 
HETATM 9880  O  O6  . CIT R 6 .   ? -13.693 76.102  30.230  1.00 51.65  ? 709  CIT B O6  1 
HETATM 9881  ZN ZN  . ZN  S 5 .   ? 2.376   95.384  17.745  0.70 47.07  ? 710  ZN  B ZN  1 
HETATM 9882  O  O   . HOH T 7 .   ? 40.657  113.704 13.820  1.00 38.32  ? 801  HOH A O   1 
HETATM 9883  O  O   . HOH T 7 .   ? 36.129  115.999 11.611  1.00 60.17  ? 802  HOH A O   1 
HETATM 9884  O  O   . HOH T 7 .   ? 44.823  115.148 14.424  1.00 52.53  ? 803  HOH A O   1 
HETATM 9885  O  O   . HOH T 7 .   ? 35.462  35.964  15.341  1.00 51.85  ? 804  HOH A O   1 
HETATM 9886  O  O   . HOH T 7 .   ? 13.124  53.485  16.033  1.00 25.94  ? 805  HOH A O   1 
HETATM 9887  O  O   . HOH T 7 .   ? 38.902  113.331 10.880  1.00 47.34  ? 806  HOH A O   1 
HETATM 9888  O  O   . HOH T 7 .   ? 16.074  108.067 22.468  1.00 27.32  ? 807  HOH A O   1 
HETATM 9889  O  O   . HOH T 7 .   ? 11.316  32.709  0.609   1.00 47.26  ? 808  HOH A O   1 
HETATM 9890  O  O   . HOH T 7 .   ? 23.791  87.918  13.225  1.00 48.72  ? 809  HOH A O   1 
HETATM 9891  O  O   . HOH T 7 .   ? 23.177  65.545  -6.382  1.00 58.07  ? 810  HOH A O   1 
HETATM 9892  O  O   . HOH T 7 .   ? 7.477   90.078  13.523  1.00 28.03  ? 811  HOH A O   1 
HETATM 9893  O  O   . HOH T 7 .   ? 16.175  109.866 14.343  1.00 24.12  ? 812  HOH A O   1 
HETATM 9894  O  O   . HOH T 7 .   ? 39.701  69.920  25.118  1.00 58.13  ? 813  HOH A O   1 
HETATM 9895  O  O   . HOH T 7 .   ? 26.719  100.559 1.776   1.00 49.82  ? 814  HOH A O   1 
HETATM 9896  O  O   . HOH T 7 .   ? 58.092  84.201  24.587  1.00 45.74  ? 815  HOH A O   1 
HETATM 9897  O  O   . HOH T 7 .   ? 44.850  69.190  28.606  1.00 41.12  ? 816  HOH A O   1 
HETATM 9898  O  O   . HOH T 7 .   ? 17.441  54.895  23.892  1.00 39.99  ? 817  HOH A O   1 
HETATM 9899  O  O   . HOH T 7 .   ? 33.881  105.933 3.299   1.00 35.95  ? 818  HOH A O   1 
HETATM 9900  O  O   . HOH T 7 .   ? 41.509  89.942  -10.670 1.00 33.72  ? 819  HOH A O   1 
HETATM 9901  O  O   . HOH T 7 .   ? 51.794  70.805  1.766   1.00 53.51  ? 820  HOH A O   1 
HETATM 9902  O  O   . HOH T 7 .   ? 24.457  66.900  -1.151  1.00 39.95  ? 821  HOH A O   1 
HETATM 9903  O  O   . HOH T 7 .   ? 23.490  63.199  5.311   1.00 58.48  ? 822  HOH A O   1 
HETATM 9904  O  O   . HOH T 7 .   ? 40.649  55.965  2.699   1.00 53.88  ? 823  HOH A O   1 
HETATM 9905  O  O   . HOH T 7 .   ? 61.356  77.290  2.599   1.00 51.31  ? 824  HOH A O   1 
HETATM 9906  O  O   . HOH T 7 .   ? 43.325  52.838  3.706   1.00 51.19  ? 825  HOH A O   1 
HETATM 9907  O  O   . HOH T 7 .   ? 44.579  81.663  8.714   1.00 47.42  ? 826  HOH A O   1 
HETATM 9908  O  O   . HOH T 7 .   ? 56.854  91.480  14.484  1.00 58.03  ? 827  HOH A O   1 
HETATM 9909  O  O   . HOH T 7 .   ? 6.694   95.416  13.507  1.00 35.66  ? 828  HOH A O   1 
HETATM 9910  O  O   . HOH T 7 .   ? 33.929  104.542 10.427  1.00 25.12  ? 829  HOH A O   1 
HETATM 9911  O  O   . HOH T 7 .   ? 18.701  90.995  19.868  1.00 43.85  ? 830  HOH A O   1 
HETATM 9912  O  O   . HOH T 7 .   ? 53.640  106.187 3.220   1.00 38.23  ? 831  HOH A O   1 
HETATM 9913  O  O   . HOH T 7 .   ? 39.792  72.807  -7.538  1.00 54.85  ? 832  HOH A O   1 
HETATM 9914  O  O   . HOH T 7 .   ? 11.527  95.026  20.283  1.00 33.59  ? 833  HOH A O   1 
HETATM 9915  O  O   . HOH T 7 .   ? 35.090  63.595  2.297   1.00 46.68  ? 834  HOH A O   1 
HETATM 9916  O  O   . HOH T 7 .   ? 45.415  97.369  -13.311 1.00 51.27  ? 835  HOH A O   1 
HETATM 9917  O  O   . HOH T 7 .   ? 56.866  80.465  30.514  1.00 44.48  ? 836  HOH A O   1 
HETATM 9918  O  O   . HOH T 7 .   ? 34.500  57.904  1.219   1.00 27.58  ? 837  HOH A O   1 
HETATM 9919  O  O   . HOH T 7 .   ? 43.877  46.277  3.791   1.00 40.53  ? 838  HOH A O   1 
HETATM 9920  O  O   . HOH T 7 .   ? 26.646  81.423  19.147  1.00 39.40  ? 839  HOH A O   1 
HETATM 9921  O  O   . HOH T 7 .   ? 19.735  62.339  2.871   1.00 52.75  ? 840  HOH A O   1 
HETATM 9922  O  O   . HOH T 7 .   ? 34.158  115.560 18.074  1.00 31.23  ? 841  HOH A O   1 
HETATM 9923  O  O   . HOH T 7 .   ? 25.662  87.718  17.654  1.00 44.23  ? 842  HOH A O   1 
HETATM 9924  O  O   . HOH T 7 .   ? 36.040  88.635  16.787  1.00 30.06  ? 843  HOH A O   1 
HETATM 9925  O  O   . HOH T 7 .   ? 26.768  91.252  20.535  1.00 47.54  ? 844  HOH A O   1 
HETATM 9926  O  O   . HOH T 7 .   ? -4.228  68.745  -0.698  1.00 60.42  ? 845  HOH A O   1 
HETATM 9927  O  O   . HOH T 7 .   ? 7.061   44.232  11.605  1.00 39.81  ? 846  HOH A O   1 
HETATM 9928  O  O   . HOH T 7 .   ? 17.309  48.659  -7.960  1.00 45.60  ? 847  HOH A O   1 
HETATM 9929  O  O   . HOH T 7 .   ? 51.038  81.996  13.915  1.00 27.12  ? 848  HOH A O   1 
HETATM 9930  O  O   . HOH T 7 .   ? 31.536  65.960  14.085  1.00 44.62  ? 849  HOH A O   1 
HETATM 9931  O  O   . HOH T 7 .   ? 22.075  90.742  3.472   1.00 32.28  ? 850  HOH A O   1 
HETATM 9932  O  O   . HOH T 7 .   ? 19.508  102.958 23.576  1.00 37.45  ? 851  HOH A O   1 
HETATM 9933  O  O   . HOH T 7 .   ? 52.289  85.162  0.435   1.00 29.72  ? 852  HOH A O   1 
HETATM 9934  O  O   . HOH T 7 .   ? 17.942  106.254 25.317  1.00 54.94  ? 853  HOH A O   1 
HETATM 9935  O  O   . HOH T 7 .   ? 23.704  103.892 7.666   1.00 20.64  ? 854  HOH A O   1 
HETATM 9936  O  O   . HOH T 7 .   ? 13.348  97.268  20.710  1.00 61.82  ? 855  HOH A O   1 
HETATM 9937  O  O   . HOH T 7 .   ? 45.883  65.426  9.816   1.00 46.70  ? 856  HOH A O   1 
HETATM 9938  O  O   . HOH T 7 .   ? 23.763  100.689 1.482   1.00 52.26  ? 857  HOH A O   1 
HETATM 9939  O  O   . HOH T 7 .   ? 56.597  89.736  20.237  1.00 38.20  ? 858  HOH A O   1 
HETATM 9940  O  O   . HOH T 7 .   ? 32.977  71.750  22.996  1.00 52.01  ? 859  HOH A O   1 
HETATM 9941  O  O   . HOH T 7 .   ? 20.622  119.203 8.836   1.00 31.90  ? 860  HOH A O   1 
HETATM 9942  O  O   . HOH T 7 .   ? 2.645   94.786  12.808  1.00 30.53  ? 861  HOH A O   1 
HETATM 9943  O  O   . HOH T 7 .   ? 20.372  95.874  1.369   1.00 30.14  ? 862  HOH A O   1 
HETATM 9944  O  O   . HOH T 7 .   ? 13.911  106.907 7.399   1.00 30.73  ? 863  HOH A O   1 
HETATM 9945  O  O   . HOH T 7 .   ? 60.736  70.513  14.790  1.00 52.31  ? 864  HOH A O   1 
HETATM 9946  O  O   . HOH T 7 .   ? 2.383   93.852  9.301   1.00 16.99  ? 865  HOH A O   1 
HETATM 9947  O  O   . HOH T 7 .   ? 19.747  48.422  17.337  1.00 29.79  ? 866  HOH A O   1 
HETATM 9948  O  O   . HOH T 7 .   ? 22.009  99.315  12.377  1.00 19.48  ? 867  HOH A O   1 
HETATM 9949  O  O   . HOH T 7 .   ? 42.959  105.699 -1.402  1.00 21.74  ? 868  HOH A O   1 
HETATM 9950  O  O   . HOH T 7 .   ? 27.230  69.745  17.046  1.00 43.44  ? 869  HOH A O   1 
HETATM 9951  O  O   . HOH T 7 .   ? 32.320  106.564 6.610   1.00 22.37  ? 870  HOH A O   1 
HETATM 9952  O  O   . HOH T 7 .   ? 34.963  82.580  14.479  1.00 21.47  ? 871  HOH A O   1 
HETATM 9953  O  O   . HOH T 7 .   ? 33.741  79.811  19.340  1.00 33.97  ? 872  HOH A O   1 
HETATM 9954  O  O   . HOH T 7 .   ? 22.792  100.775 10.201  1.00 20.75  ? 873  HOH A O   1 
HETATM 9955  O  O   . HOH T 7 .   ? 26.649  110.365 3.845   1.00 35.25  ? 874  HOH A O   1 
HETATM 9956  O  O   . HOH T 7 .   ? 58.752  69.985  26.660  1.00 29.36  ? 875  HOH A O   1 
HETATM 9957  O  O   . HOH T 7 .   ? 36.675  75.571  -7.004  1.00 48.58  ? 876  HOH A O   1 
HETATM 9958  O  O   . HOH T 7 .   ? 21.146  88.250  7.201   1.00 20.78  ? 877  HOH A O   1 
HETATM 9959  O  O   . HOH T 7 .   ? 42.049  39.512  8.047   1.00 53.56  ? 878  HOH A O   1 
HETATM 9960  O  O   . HOH T 7 .   ? 31.902  117.444 20.390  1.00 46.48  ? 879  HOH A O   1 
HETATM 9961  O  O   . HOH T 7 .   ? 31.954  62.295  12.527  1.00 39.33  ? 880  HOH A O   1 
HETATM 9962  O  O   . HOH T 7 .   ? 39.307  53.226  -1.214  1.00 41.31  ? 881  HOH A O   1 
HETATM 9963  O  O   . HOH T 7 .   ? 38.220  76.942  0.728   1.00 30.65  ? 882  HOH A O   1 
HETATM 9964  O  O   . HOH T 7 .   ? 19.164  66.948  15.823  1.00 56.95  ? 883  HOH A O   1 
HETATM 9965  O  O   . HOH T 7 .   ? 17.922  81.088  1.807   1.00 29.23  ? 884  HOH A O   1 
HETATM 9966  O  O   . HOH T 7 .   ? 53.133  98.500  7.336   1.00 40.49  ? 885  HOH A O   1 
HETATM 9967  O  O   . HOH T 7 .   ? 29.940  79.058  -4.125  1.00 27.29  ? 886  HOH A O   1 
HETATM 9968  O  O   . HOH T 7 .   ? 34.839  60.276  -3.393  1.00 62.87  ? 887  HOH A O   1 
HETATM 9969  O  O   . HOH T 7 .   ? 28.185  66.953  11.997  1.00 24.50  ? 888  HOH A O   1 
HETATM 9970  O  O   . HOH T 7 .   ? 34.401  57.828  8.287   1.00 25.30  ? 889  HOH A O   1 
HETATM 9971  O  O   . HOH T 7 .   ? 47.918  68.758  11.390  1.00 24.26  ? 890  HOH A O   1 
HETATM 9972  O  O   . HOH T 7 .   ? 35.965  111.328 10.443  1.00 52.68  ? 891  HOH A O   1 
HETATM 9973  O  O   . HOH T 7 .   ? 42.501  66.009  10.777  1.00 28.44  ? 892  HOH A O   1 
HETATM 9974  O  O   . HOH T 7 .   ? 28.590  102.763 1.163   1.00 41.62  ? 893  HOH A O   1 
HETATM 9975  O  O   . HOH T 7 .   ? 28.367  117.584 30.759  1.00 52.56  ? 894  HOH A O   1 
HETATM 9976  O  O   . HOH T 7 .   ? 41.252  84.860  23.110  1.00 52.21  ? 895  HOH A O   1 
HETATM 9977  O  O   . HOH T 7 .   ? 22.096  70.248  4.677   1.00 29.35  ? 896  HOH A O   1 
HETATM 9978  O  O   . HOH T 7 .   ? 43.131  61.562  24.839  1.00 59.44  ? 897  HOH A O   1 
HETATM 9979  O  O   . HOH T 7 .   ? 19.253  116.267 26.677  1.00 34.54  ? 898  HOH A O   1 
HETATM 9980  O  O   . HOH T 7 .   ? 39.968  37.403  7.319   1.00 39.05  ? 899  HOH A O   1 
HETATM 9981  O  O   . HOH T 7 .   ? 38.759  98.592  -11.274 1.00 57.10  ? 900  HOH A O   1 
HETATM 9982  O  O   . HOH T 7 .   ? 41.681  69.998  28.307  1.00 53.23  ? 901  HOH A O   1 
HETATM 9983  O  O   . HOH T 7 .   ? 25.213  66.053  5.188   1.00 31.96  ? 902  HOH A O   1 
HETATM 9984  O  O   . HOH T 7 .   ? 56.422  87.831  25.068  1.00 43.91  ? 903  HOH A O   1 
HETATM 9985  O  O   . HOH T 7 .   ? 34.119  58.783  10.855  1.00 47.45  ? 904  HOH A O   1 
HETATM 9986  O  O   . HOH T 7 .   ? 14.252  88.391  10.137  1.00 16.75  ? 905  HOH A O   1 
HETATM 9987  O  O   . HOH T 7 .   ? 9.401   83.141  4.571   1.00 37.24  ? 906  HOH A O   1 
HETATM 9988  O  O   . HOH T 7 .   ? 19.743  98.066  20.219  1.00 24.00  ? 907  HOH A O   1 
HETATM 9989  O  O   . HOH T 7 .   ? 51.655  96.320  23.454  1.00 41.33  ? 908  HOH A O   1 
HETATM 9990  O  O   . HOH T 7 .   ? 3.524   98.655  12.706  1.00 53.78  ? 909  HOH A O   1 
HETATM 9991  O  O   . HOH T 7 .   ? 12.889  90.893  9.855   1.00 17.74  ? 910  HOH A O   1 
HETATM 9992  O  O   . HOH T 7 .   ? 57.301  89.063  13.943  1.00 30.67  ? 911  HOH A O   1 
HETATM 9993  O  O   . HOH T 7 .   ? 25.514  42.440  15.615  1.00 46.50  ? 912  HOH A O   1 
HETATM 9994  O  O   . HOH T 7 .   ? 56.560  76.874  14.265  1.00 34.41  ? 913  HOH A O   1 
HETATM 9995  O  O   . HOH T 7 .   ? 49.251  99.733  -8.895  1.00 46.56  ? 914  HOH A O   1 
HETATM 9996  O  O   . HOH T 7 .   ? 48.398  82.697  13.432  1.00 19.32  ? 915  HOH A O   1 
HETATM 9997  O  O   . HOH T 7 .   ? 38.497  51.009  18.104  1.00 38.59  ? 916  HOH A O   1 
HETATM 9998  O  O   . HOH T 7 .   ? 28.435  65.053  -6.832  1.00 36.82  ? 917  HOH A O   1 
HETATM 9999  O  O   . HOH T 7 .   ? 38.888  49.205  -5.876  1.00 51.09  ? 918  HOH A O   1 
HETATM 10000 O  O   . HOH T 7 .   ? 18.654  36.061  3.452   1.00 32.36  ? 919  HOH A O   1 
HETATM 10001 O  O   . HOH T 7 .   ? 17.977  111.791 15.050  1.00 24.86  ? 920  HOH A O   1 
HETATM 10002 O  O   . HOH T 7 .   ? 38.716  88.457  16.679  1.00 33.88  ? 921  HOH A O   1 
HETATM 10003 O  O   . HOH T 7 .   ? 16.152  101.875 4.395   1.00 27.91  ? 922  HOH A O   1 
HETATM 10004 O  O   . HOH T 7 .   ? 25.578  96.266  13.096  1.00 18.34  ? 923  HOH A O   1 
HETATM 10005 O  O   . HOH T 7 .   ? 43.393  44.562  16.034  1.00 45.14  ? 924  HOH A O   1 
HETATM 10006 O  O   . HOH T 7 .   ? 34.133  91.440  15.986  1.00 23.97  ? 925  HOH A O   1 
HETATM 10007 O  O   . HOH T 7 .   ? 16.020  79.719  12.802  1.00 40.79  ? 926  HOH A O   1 
HETATM 10008 O  O   . HOH T 7 .   ? 10.002  92.868  8.395   1.00 27.18  ? 927  HOH A O   1 
HETATM 10009 O  O   . HOH T 7 .   ? 32.009  51.953  -9.912  1.00 35.67  ? 928  HOH A O   1 
HETATM 10010 O  O   . HOH T 7 .   ? 40.919  63.326  17.723  1.00 49.85  ? 929  HOH A O   1 
HETATM 10011 O  O   . HOH T 7 .   ? 36.597  44.782  -10.783 1.00 37.07  ? 930  HOH A O   1 
HETATM 10012 O  O   . HOH T 7 .   ? 25.234  78.764  -6.003  1.00 35.86  ? 931  HOH A O   1 
HETATM 10013 O  O   . HOH T 7 .   ? 32.144  68.478  -6.109  1.00 41.22  ? 932  HOH A O   1 
HETATM 10014 O  O   . HOH T 7 .   ? 23.293  81.526  -3.907  1.00 50.91  ? 933  HOH A O   1 
HETATM 10015 O  O   . HOH T 7 .   ? 17.041  111.461 24.333  1.00 26.68  ? 934  HOH A O   1 
HETATM 10016 O  O   . HOH T 7 .   ? 36.902  97.670  -5.020  1.00 24.01  ? 935  HOH A O   1 
HETATM 10017 O  O   . HOH T 7 .   ? 62.769  79.694  26.619  1.00 50.79  ? 936  HOH A O   1 
HETATM 10018 O  O   . HOH T 7 .   ? 17.291  85.735  15.884  1.00 34.54  ? 937  HOH A O   1 
HETATM 10019 O  O   . HOH T 7 .   ? 38.793  102.240 -5.890  1.00 22.95  ? 938  HOH A O   1 
HETATM 10020 O  O   . HOH T 7 .   ? 51.717  58.876  15.688  1.00 45.15  ? 939  HOH A O   1 
HETATM 10021 O  O   . HOH T 7 .   ? 26.911  98.998  4.669   1.00 31.79  ? 940  HOH A O   1 
HETATM 10022 O  O   . HOH T 7 .   ? 43.289  93.264  18.481  1.00 36.15  ? 941  HOH A O   1 
HETATM 10023 O  O   . HOH T 7 .   ? 41.289  81.529  7.178   1.00 37.31  ? 942  HOH A O   1 
HETATM 10024 O  O   . HOH T 7 .   ? 39.185  90.182  1.955   1.00 22.20  ? 943  HOH A O   1 
HETATM 10025 O  O   . HOH T 7 .   ? 47.733  101.269 10.454  1.00 35.32  ? 944  HOH A O   1 
HETATM 10026 O  O   . HOH T 7 .   ? 8.848   48.433  9.216   1.00 53.14  ? 945  HOH A O   1 
HETATM 10027 O  O   . HOH T 7 .   ? 51.215  91.663  24.834  1.00 38.81  ? 946  HOH A O   1 
HETATM 10028 O  O   . HOH T 7 .   ? 34.674  78.956  -1.840  1.00 25.58  ? 947  HOH A O   1 
HETATM 10029 O  O   . HOH T 7 .   ? 32.714  45.054  -8.389  1.00 53.83  ? 948  HOH A O   1 
HETATM 10030 O  O   . HOH T 7 .   ? 54.683  60.055  23.281  1.00 56.52  ? 949  HOH A O   1 
HETATM 10031 O  O   . HOH T 7 .   ? 54.739  78.301  27.995  1.00 30.09  ? 950  HOH A O   1 
HETATM 10032 O  O   . HOH T 7 .   ? 20.933  80.809  15.079  1.00 24.57  ? 951  HOH A O   1 
HETATM 10033 O  O   . HOH T 7 .   ? 12.560  77.883  11.760  1.00 49.39  ? 952  HOH A O   1 
HETATM 10034 O  O   . HOH T 7 .   ? 34.893  92.002  -6.611  1.00 28.86  ? 953  HOH A O   1 
HETATM 10035 O  O   . HOH T 7 .   ? 26.882  55.122  16.730  1.00 31.12  ? 954  HOH A O   1 
HETATM 10036 O  O   . HOH T 7 .   ? 23.479  43.831  20.035  1.00 52.47  ? 955  HOH A O   1 
HETATM 10037 O  O   . HOH T 7 .   ? 27.072  71.484  21.413  1.00 60.68  ? 956  HOH A O   1 
HETATM 10038 O  O   . HOH T 7 .   ? 23.236  120.095 11.422  1.00 33.89  ? 957  HOH A O   1 
HETATM 10039 O  O   . HOH T 7 .   ? 41.808  33.647  7.566   1.00 66.86  ? 958  HOH A O   1 
HETATM 10040 O  O   . HOH T 7 .   ? 14.948  85.733  13.068  1.00 28.68  ? 959  HOH A O   1 
HETATM 10041 O  O   . HOH T 7 .   ? 30.720  92.794  8.964   1.00 23.33  ? 960  HOH A O   1 
HETATM 10042 O  O   . HOH T 7 .   ? 15.977  110.534 7.641   1.00 49.86  ? 961  HOH A O   1 
HETATM 10043 O  O   . HOH T 7 .   ? 14.325  50.092  -6.617  1.00 48.05  ? 962  HOH A O   1 
HETATM 10044 O  O   . HOH T 7 .   ? 23.725  87.904  10.934  1.00 34.67  ? 963  HOH A O   1 
HETATM 10045 O  O   . HOH T 7 .   ? 23.538  76.404  23.009  1.00 47.74  ? 964  HOH A O   1 
HETATM 10046 O  O   . HOH T 7 .   ? 18.611  109.700 20.025  1.00 28.26  ? 965  HOH A O   1 
HETATM 10047 O  O   . HOH T 7 .   ? 28.871  85.004  16.999  1.00 33.82  ? 966  HOH A O   1 
HETATM 10048 O  O   . HOH T 7 .   ? 22.672  62.642  -1.042  1.00 29.87  ? 967  HOH A O   1 
HETATM 10049 O  O   . HOH T 7 .   ? 59.135  96.247  4.154   1.00 45.09  ? 968  HOH A O   1 
HETATM 10050 O  O   . HOH T 7 .   ? 49.171  69.752  29.782  1.00 27.95  ? 969  HOH A O   1 
HETATM 10051 O  O   . HOH T 7 .   ? 37.780  77.389  13.034  1.00 18.89  ? 970  HOH A O   1 
HETATM 10052 O  O   . HOH T 7 .   ? 36.079  76.458  10.546  1.00 20.94  ? 971  HOH A O   1 
HETATM 10053 O  O   . HOH T 7 .   ? 17.569  95.430  0.814   1.00 35.07  ? 972  HOH A O   1 
HETATM 10054 O  O   . HOH T 7 .   ? 37.547  104.018 2.796   1.00 25.05  ? 973  HOH A O   1 
HETATM 10055 O  O   . HOH T 7 .   ? 49.674  73.812  7.370   1.00 46.97  ? 974  HOH A O   1 
HETATM 10056 O  O   . HOH T 7 .   ? 22.435  38.393  -9.890  1.00 36.46  ? 975  HOH A O   1 
HETATM 10057 O  O   . HOH T 7 .   ? 26.622  93.957  0.802   1.00 56.81  ? 976  HOH A O   1 
HETATM 10058 O  O   . HOH T 7 .   ? 19.725  92.333  0.546   1.00 56.17  ? 977  HOH A O   1 
HETATM 10059 O  O   . HOH T 7 .   ? 21.483  67.111  8.314   1.00 35.09  ? 978  HOH A O   1 
HETATM 10060 O  O   . HOH T 7 .   ? 36.766  99.288  9.392   1.00 48.80  ? 979  HOH A O   1 
HETATM 10061 O  O   . HOH T 7 .   ? 16.691  97.470  20.240  1.00 28.26  ? 980  HOH A O   1 
HETATM 10062 O  O   . HOH T 7 .   ? 20.882  41.630  -11.100 1.00 55.32  ? 981  HOH A O   1 
HETATM 10063 O  O   . HOH T 7 .   ? 28.645  71.426  19.086  1.00 30.69  ? 982  HOH A O   1 
HETATM 10064 O  O   . HOH T 7 .   ? 29.734  70.830  10.262  1.00 25.26  ? 983  HOH A O   1 
HETATM 10065 O  O   . HOH T 7 .   ? 57.227  100.865 3.210   1.00 30.90  ? 984  HOH A O   1 
HETATM 10066 O  O   . HOH T 7 .   ? 31.084  104.044 30.929  1.00 53.36  ? 985  HOH A O   1 
HETATM 10067 O  O   . HOH T 7 .   ? 29.502  114.522 31.914  1.00 53.07  ? 986  HOH A O   1 
HETATM 10068 O  O   . HOH T 7 .   ? 31.346  49.526  -12.442 1.00 52.29  ? 987  HOH A O   1 
HETATM 10069 O  O   . HOH T 7 .   ? 54.161  65.373  29.021  1.00 58.06  ? 988  HOH A O   1 
HETATM 10070 O  O   . HOH T 7 .   ? 21.423  49.690  26.728  1.00 39.45  ? 989  HOH A O   1 
HETATM 10071 O  O   . HOH T 7 .   ? 51.506  106.312 -4.906  1.00 32.38  ? 990  HOH A O   1 
HETATM 10072 O  O   . HOH T 7 .   ? 30.256  92.654  0.030   1.00 34.23  ? 991  HOH A O   1 
HETATM 10073 O  O   . HOH T 7 .   ? 38.652  90.441  11.689  1.00 35.15  ? 992  HOH A O   1 
HETATM 10074 O  O   . HOH T 7 .   ? 42.230  90.546  -3.939  1.00 19.21  ? 993  HOH A O   1 
HETATM 10075 O  O   . HOH T 7 .   ? 36.361  113.927 17.471  1.00 26.76  ? 994  HOH A O   1 
HETATM 10076 O  O   . HOH T 7 .   ? 13.629  36.987  -0.516  1.00 34.97  ? 995  HOH A O   1 
HETATM 10077 O  O   . HOH T 7 .   ? 51.511  85.037  27.628  1.00 44.70  ? 996  HOH A O   1 
HETATM 10078 O  O   . HOH T 7 .   ? 50.195  70.818  32.456  1.00 31.70  ? 997  HOH A O   1 
HETATM 10079 O  O   . HOH T 7 .   ? 47.864  61.046  20.796  1.00 51.24  ? 998  HOH A O   1 
HETATM 10080 O  O   . HOH T 7 .   ? 26.126  89.995  -1.913  1.00 51.32  ? 999  HOH A O   1 
HETATM 10081 O  O   . HOH T 7 .   ? 14.263  54.919  18.409  1.00 39.35  ? 1000 HOH A O   1 
HETATM 10082 O  O   . HOH T 7 .   ? 27.646  62.610  15.278  1.00 53.43  ? 1001 HOH A O   1 
HETATM 10083 O  O   . HOH T 7 .   ? 44.030  96.259  16.147  1.00 52.30  ? 1002 HOH A O   1 
HETATM 10084 O  O   . HOH T 7 .   ? 20.555  97.630  22.594  1.00 57.22  ? 1003 HOH A O   1 
HETATM 10085 O  O   . HOH T 7 .   ? 53.337  88.911  26.222  1.00 61.32  ? 1004 HOH A O   1 
HETATM 10086 O  O   . HOH T 7 .   ? 26.909  36.587  -8.256  1.00 48.67  ? 1005 HOH A O   1 
HETATM 10087 O  O   . HOH T 7 .   ? 20.698  119.878 29.249  1.00 45.05  ? 1006 HOH A O   1 
HETATM 10088 O  O   . HOH T 7 .   ? 35.329  100.547 11.503  1.00 26.22  ? 1007 HOH A O   1 
HETATM 10089 O  O   . HOH T 7 .   ? 23.740  96.569  4.223   1.00 21.26  ? 1008 HOH A O   1 
HETATM 10090 O  O   . HOH T 7 .   ? 19.764  44.029  19.049  1.00 32.14  ? 1009 HOH A O   1 
HETATM 10091 O  O   . HOH T 7 .   ? 14.025  43.389  -3.699  1.00 37.34  ? 1010 HOH A O   1 
HETATM 10092 O  O   . HOH T 7 .   ? 50.806  105.477 5.080   1.00 44.79  ? 1011 HOH A O   1 
HETATM 10093 O  O   . HOH T 7 .   ? 43.880  48.159  5.793   1.00 37.75  ? 1012 HOH A O   1 
HETATM 10094 O  O   . HOH T 7 .   ? 62.083  88.205  2.185   1.00 49.04  ? 1013 HOH A O   1 
HETATM 10095 O  O   . HOH T 7 .   ? 58.035  76.722  29.854  1.00 46.88  ? 1014 HOH A O   1 
HETATM 10096 O  O   . HOH T 7 .   ? 14.638  103.898 5.195   1.00 23.18  ? 1015 HOH A O   1 
HETATM 10097 O  O   . HOH T 7 .   ? 30.338  116.370 24.862  1.00 42.77  ? 1016 HOH A O   1 
HETATM 10098 O  O   . HOH T 7 .   ? 31.956  39.261  8.311   1.00 34.57  ? 1017 HOH A O   1 
HETATM 10099 O  O   . HOH T 7 .   ? 20.678  61.261  5.203   1.00 29.17  ? 1018 HOH A O   1 
HETATM 10100 O  O   . HOH T 7 .   ? 45.114  67.806  7.105   1.00 53.28  ? 1019 HOH A O   1 
HETATM 10101 O  O   . HOH T 7 .   ? 55.233  91.407  23.965  1.00 59.37  ? 1020 HOH A O   1 
HETATM 10102 O  O   . HOH T 7 .   ? 30.717  99.801  8.110   1.00 36.31  ? 1021 HOH A O   1 
HETATM 10103 O  O   . HOH T 7 .   ? 39.467  89.172  4.439   1.00 17.21  ? 1022 HOH A O   1 
HETATM 10104 O  O   . HOH T 7 .   ? 43.896  45.367  18.638  1.00 42.16  ? 1023 HOH A O   1 
HETATM 10105 O  O   . HOH T 7 .   ? 17.776  83.100  10.072  1.00 25.72  ? 1024 HOH A O   1 
HETATM 10106 O  O   . HOH T 7 .   ? 39.816  52.297  13.936  1.00 42.14  ? 1025 HOH A O   1 
HETATM 10107 O  O   . HOH T 7 .   ? 60.597  78.640  14.211  1.00 49.94  ? 1026 HOH A O   1 
HETATM 10108 O  O   . HOH T 7 .   ? 34.774  65.027  -3.249  1.00 38.25  ? 1027 HOH A O   1 
HETATM 10109 O  O   . HOH T 7 .   ? 41.710  68.856  8.126   1.00 23.27  ? 1028 HOH A O   1 
HETATM 10110 O  O   . HOH T 7 .   ? 21.381  99.848  23.994  1.00 33.97  ? 1029 HOH A O   1 
HETATM 10111 O  O   . HOH T 7 .   ? 22.900  112.793 29.628  1.00 54.05  ? 1030 HOH A O   1 
HETATM 10112 O  O   . HOH T 7 .   ? 38.936  56.162  0.747   1.00 42.03  ? 1031 HOH A O   1 
HETATM 10113 O  O   . HOH T 7 .   ? 52.569  77.615  31.103  1.00 39.74  ? 1032 HOH A O   1 
HETATM 10114 O  O   . HOH T 7 .   ? 27.485  118.099 5.811   1.00 46.78  ? 1033 HOH A O   1 
HETATM 10115 O  O   . HOH T 7 .   ? 15.899  42.277  -5.359  1.00 40.76  ? 1034 HOH A O   1 
HETATM 10116 O  O   . HOH T 7 .   ? 30.989  90.009  -7.946  1.00 37.41  ? 1035 HOH A O   1 
HETATM 10117 O  O   . HOH T 7 .   ? 23.751  33.933  -9.990  1.00 61.50  ? 1036 HOH A O   1 
HETATM 10118 O  O   . HOH T 7 .   ? 40.752  64.280  21.691  1.00 50.14  ? 1037 HOH A O   1 
HETATM 10119 O  O   . HOH T 7 .   ? 36.182  107.828 22.042  1.00 26.30  ? 1038 HOH A O   1 
HETATM 10120 O  O   . HOH T 7 .   ? 20.389  47.422  10.985  1.00 22.08  ? 1039 HOH A O   1 
HETATM 10121 O  O   . HOH T 7 .   ? 64.121  76.625  14.882  1.00 46.87  ? 1040 HOH A O   1 
HETATM 10122 O  O   . HOH T 7 .   ? 19.678  113.310 11.564  1.00 27.77  ? 1041 HOH A O   1 
HETATM 10123 O  O   . HOH T 7 .   ? 36.705  56.758  9.575   1.00 34.96  ? 1042 HOH A O   1 
HETATM 10124 O  O   . HOH T 7 .   ? 39.407  84.385  -2.224  1.00 23.00  ? 1043 HOH A O   1 
HETATM 10125 O  O   . HOH T 7 .   ? 23.353  92.712  2.081   1.00 34.09  ? 1044 HOH A O   1 
HETATM 10126 O  O   . HOH T 7 .   ? 62.387  70.713  18.440  1.00 47.71  ? 1045 HOH A O   1 
HETATM 10127 O  O   . HOH T 7 .   ? 16.166  70.249  6.751   1.00 58.91  ? 1046 HOH A O   1 
HETATM 10128 O  O   . HOH T 7 .   ? 58.318  64.552  23.271  1.00 51.41  ? 1047 HOH A O   1 
HETATM 10129 O  O   . HOH T 7 .   ? 46.817  84.969  -10.913 1.00 59.79  ? 1048 HOH A O   1 
HETATM 10130 O  O   . HOH T 7 .   ? 23.310  87.594  16.570  1.00 27.68  ? 1049 HOH A O   1 
HETATM 10131 O  O   . HOH T 7 .   ? 30.701  89.439  21.435  1.00 50.90  ? 1050 HOH A O   1 
HETATM 10132 O  O   . HOH T 7 .   ? 19.513  68.896  8.324   1.00 28.29  ? 1051 HOH A O   1 
HETATM 10133 O  O   . HOH T 7 .   ? 45.887  54.627  7.948   1.00 38.59  ? 1052 HOH A O   1 
HETATM 10134 O  O   . HOH T 7 .   ? 38.348  108.141 15.920  1.00 37.43  ? 1053 HOH A O   1 
HETATM 10135 O  O   . HOH T 7 .   ? 30.716  78.456  -1.730  1.00 27.11  ? 1054 HOH A O   1 
HETATM 10136 O  O   . HOH T 7 .   ? 22.380  105.688 4.878   1.00 25.92  ? 1055 HOH A O   1 
HETATM 10137 O  O   . HOH T 7 .   ? 56.346  81.412  4.691   1.00 40.75  ? 1056 HOH A O   1 
HETATM 10138 O  O   . HOH T 7 .   ? 53.435  87.919  -10.755 1.00 51.82  ? 1057 HOH A O   1 
HETATM 10139 O  O   . HOH T 7 .   ? 25.989  119.174 16.886  1.00 28.45  ? 1058 HOH A O   1 
HETATM 10140 O  O   . HOH T 7 .   ? 36.900  82.651  -5.380  1.00 35.52  ? 1059 HOH A O   1 
HETATM 10141 O  O   . HOH T 7 .   ? 7.574   39.265  8.667   1.00 53.34  ? 1060 HOH A O   1 
HETATM 10142 O  O   . HOH T 7 .   ? 20.961  109.818 18.390  1.00 26.03  ? 1061 HOH A O   1 
HETATM 10143 O  O   . HOH T 7 .   ? 9.997   95.139  5.674   1.00 21.41  ? 1062 HOH A O   1 
HETATM 10144 O  O   . HOH T 7 .   ? 36.336  94.512  15.103  1.00 52.33  ? 1063 HOH A O   1 
HETATM 10145 O  O   . HOH T 7 .   ? 24.878  51.086  24.111  1.00 56.46  ? 1064 HOH A O   1 
HETATM 10146 O  O   . HOH T 7 .   ? 24.648  98.358  24.344  1.00 30.28  ? 1065 HOH A O   1 
HETATM 10147 O  O   . HOH T 7 .   ? 44.754  93.543  20.657  1.00 31.05  ? 1066 HOH A O   1 
HETATM 10148 O  O   . HOH T 7 .   ? 60.881  88.379  5.322   1.00 53.34  ? 1067 HOH A O   1 
HETATM 10149 O  O   . HOH T 7 .   ? 27.870  111.223 31.187  1.00 40.66  ? 1068 HOH A O   1 
HETATM 10150 O  O   . HOH T 7 .   ? 9.680   100.267 8.422   1.00 27.25  ? 1069 HOH A O   1 
HETATM 10151 O  O   . HOH T 7 .   ? 27.929  98.885  27.058  1.00 40.82  ? 1070 HOH A O   1 
HETATM 10152 O  O   . HOH T 7 .   ? 22.324  114.806 4.700   1.00 45.71  ? 1071 HOH A O   1 
HETATM 10153 O  O   . HOH T 7 .   ? 25.796  108.675 30.135  1.00 35.01  ? 1072 HOH A O   1 
HETATM 10154 O  O   . HOH T 7 .   ? 31.029  32.687  21.153  1.00 67.34  ? 1073 HOH A O   1 
HETATM 10155 O  O   . HOH T 7 .   ? 19.133  108.073 6.182   1.00 33.13  ? 1074 HOH A O   1 
HETATM 10156 O  O   . HOH T 7 .   ? 31.283  31.279  5.749   1.00 70.28  ? 1075 HOH A O   1 
HETATM 10157 O  O   . HOH T 7 .   ? 18.680  71.902  -1.834  1.00 39.00  ? 1076 HOH A O   1 
HETATM 10158 O  O   . HOH T 7 .   ? 36.178  55.108  -7.736  1.00 46.78  ? 1077 HOH A O   1 
HETATM 10159 O  O   . HOH T 7 .   ? 53.280  60.036  9.346   1.00 58.79  ? 1078 HOH A O   1 
HETATM 10160 O  O   . HOH T 7 .   ? 15.818  100.287 19.835  1.00 26.38  ? 1079 HOH A O   1 
HETATM 10161 O  O   . HOH T 7 .   ? 58.466  92.332  10.530  1.00 51.27  ? 1080 HOH A O   1 
HETATM 10162 O  O   . HOH T 7 .   ? 28.228  62.135  12.807  1.00 63.33  ? 1081 HOH A O   1 
HETATM 10163 O  O   . HOH T 7 .   ? 40.995  100.422 10.497  1.00 29.71  ? 1082 HOH A O   1 
HETATM 10164 O  O   . HOH T 7 .   ? 45.564  87.964  25.527  1.00 58.60  ? 1083 HOH A O   1 
HETATM 10165 O  O   . HOH T 7 .   ? 35.452  61.794  14.385  1.00 47.60  ? 1084 HOH A O   1 
HETATM 10166 O  O   . HOH T 7 .   ? 37.986  52.972  21.195  1.00 68.67  ? 1085 HOH A O   1 
HETATM 10167 O  O   . HOH T 7 .   ? 56.883  107.979 0.033   1.00 45.03  ? 1086 HOH A O   1 
HETATM 10168 O  O   . HOH T 7 .   ? 42.770  56.823  13.534  1.00 44.48  ? 1087 HOH A O   1 
HETATM 10169 O  O   . HOH T 7 .   ? 22.809  59.029  -9.878  1.00 49.24  ? 1088 HOH A O   1 
HETATM 10170 O  O   . HOH T 7 .   ? 35.928  31.779  10.304  1.00 57.76  ? 1089 HOH A O   1 
HETATM 10171 O  O   . HOH T 7 .   ? 55.839  102.329 -6.438  1.00 34.36  ? 1090 HOH A O   1 
HETATM 10172 O  O   . HOH T 7 .   ? 35.130  110.788 25.478  1.00 32.53  ? 1091 HOH A O   1 
HETATM 10173 O  O   . HOH T 7 .   ? 31.769  99.884  27.850  1.00 51.25  ? 1092 HOH A O   1 
HETATM 10174 O  O   . HOH T 7 .   ? 37.276  103.045 9.147   1.00 66.48  ? 1093 HOH A O   1 
HETATM 10175 O  O   . HOH T 7 .   ? 27.953  79.344  -7.361  1.00 49.63  ? 1094 HOH A O   1 
HETATM 10176 O  O   . HOH T 7 .   ? 43.416  87.215  22.699  1.00 36.23  ? 1095 HOH A O   1 
HETATM 10177 O  O   . HOH T 7 .   ? 55.607  104.180 0.992   1.00 40.93  ? 1096 HOH A O   1 
HETATM 10178 O  O   . HOH T 7 .   ? 34.107  89.420  -10.653 1.00 39.38  ? 1097 HOH A O   1 
HETATM 10179 O  O   . HOH T 7 .   ? 38.034  95.902  -6.912  1.00 25.54  ? 1098 HOH A O   1 
HETATM 10180 O  O   . HOH T 7 .   ? 13.298  91.721  7.290   1.00 28.29  ? 1099 HOH A O   1 
HETATM 10181 O  O   . HOH T 7 .   ? 46.989  104.730 -9.500  1.00 66.19  ? 1100 HOH A O   1 
HETATM 10182 O  O   . HOH T 7 .   ? 39.497  77.321  22.595  1.00 29.91  ? 1101 HOH A O   1 
HETATM 10183 O  O   . HOH T 7 .   ? 29.389  89.026  -3.992  1.00 34.52  ? 1102 HOH A O   1 
HETATM 10184 O  O   . HOH T 7 .   ? 34.697  77.624  21.990  1.00 45.79  ? 1103 HOH A O   1 
HETATM 10185 O  O   . HOH T 7 .   ? 13.510  77.914  1.431   1.00 49.61  ? 1104 HOH A O   1 
HETATM 10186 O  O   . HOH T 7 .   ? 31.681  82.078  18.327  1.00 29.69  ? 1105 HOH A O   1 
HETATM 10187 O  O   . HOH T 7 .   ? 35.644  109.061 9.690   1.00 55.59  ? 1106 HOH A O   1 
HETATM 10188 O  O   . HOH T 7 .   ? 23.766  87.537  -2.122  1.00 37.23  ? 1107 HOH A O   1 
HETATM 10189 O  O   . HOH T 7 .   ? 9.107   31.242  10.439  1.00 52.72  ? 1108 HOH A O   1 
HETATM 10190 O  O   . HOH T 7 .   ? 55.921  106.901 5.773   1.00 43.40  ? 1109 HOH A O   1 
HETATM 10191 O  O   . HOH T 7 .   ? 21.342  64.233  13.263  1.00 54.63  ? 1110 HOH A O   1 
HETATM 10192 O  O   . HOH T 7 .   ? 45.331  38.784  6.368   1.00 57.21  ? 1111 HOH A O   1 
HETATM 10193 O  O   . HOH T 7 .   ? 18.531  29.430  6.165   1.00 52.01  ? 1112 HOH A O   1 
HETATM 10194 O  O   . HOH T 7 .   ? 19.461  51.493  -10.764 1.00 49.92  ? 1113 HOH A O   1 
HETATM 10195 O  O   . HOH T 7 .   ? 29.853  63.535  11.535  1.00 53.09  ? 1114 HOH A O   1 
HETATM 10196 O  O   . HOH T 7 .   ? 56.141  105.375 -3.332  1.00 41.41  ? 1115 HOH A O   1 
HETATM 10197 O  O   . HOH T 7 .   ? 19.664  51.258  17.460  1.00 22.49  ? 1116 HOH A O   1 
HETATM 10198 O  O   . HOH T 7 .   ? 36.635  69.347  -2.537  1.00 41.62  ? 1117 HOH A O   1 
HETATM 10199 O  O   . HOH T 7 .   ? 34.847  82.754  -7.096  1.00 33.78  ? 1118 HOH A O   1 
HETATM 10200 O  O   . HOH T 7 .   ? 34.601  30.210  14.136  1.00 67.67  ? 1119 HOH A O   1 
HETATM 10201 O  O   . HOH T 7 .   ? 15.015  56.735  15.911  1.00 60.52  ? 1120 HOH A O   1 
HETATM 10202 O  O   . HOH T 7 .   ? 20.372  105.757 26.762  1.00 53.01  ? 1121 HOH A O   1 
HETATM 10203 O  O   . HOH T 7 .   ? 46.327  57.089  8.915   1.00 58.71  ? 1122 HOH A O   1 
HETATM 10204 O  O   . HOH T 7 .   ? 25.282  81.075  -7.239  1.00 51.13  ? 1123 HOH A O   1 
HETATM 10205 O  O   . HOH T 7 .   ? 43.213  83.333  25.048  1.00 57.30  ? 1124 HOH A O   1 
HETATM 10206 O  O   . HOH T 7 .   ? 51.549  58.950  18.286  1.00 40.28  ? 1125 HOH A O   1 
HETATM 10207 O  O   . HOH T 7 .   ? 40.706  93.393  16.331  1.00 40.78  ? 1126 HOH A O   1 
HETATM 10208 O  O   . HOH T 7 .   ? 29.128  66.685  14.367  1.00 37.98  ? 1127 HOH A O   1 
HETATM 10209 O  O   . HOH T 7 .   ? 34.550  51.519  18.774  1.00 35.48  ? 1128 HOH A O   1 
HETATM 10210 O  O   . HOH T 7 .   ? 24.889  71.725  18.516  1.00 43.22  ? 1129 HOH A O   1 
HETATM 10211 O  O   . HOH T 7 .   ? 59.691  101.049 -7.183  1.00 58.31  ? 1130 HOH A O   1 
HETATM 10212 O  O   . HOH T 7 .   ? 20.364  47.669  13.649  1.00 22.22  ? 1131 HOH A O   1 
HETATM 10213 O  O   . HOH T 7 .   ? 8.559   43.294  -0.749  1.00 76.41  ? 1132 HOH A O   1 
HETATM 10214 O  O   . HOH T 7 .   ? 45.213  61.406  20.845  1.00 56.67  ? 1133 HOH A O   1 
HETATM 10215 O  O   . HOH T 7 .   ? 16.177  105.347 6.937   1.00 31.56  ? 1134 HOH A O   1 
HETATM 10216 O  O   . HOH T 7 .   ? 39.180  68.062  21.864  1.00 44.08  ? 1135 HOH A O   1 
HETATM 10217 O  O   . HOH T 7 .   ? 63.661  84.735  9.276   1.00 58.10  ? 1136 HOH A O   1 
HETATM 10218 O  O   . HOH T 7 .   ? 57.151  66.125  10.125  1.00 59.53  ? 1137 HOH A O   1 
HETATM 10219 O  O   . HOH T 7 .   ? 32.297  96.024  16.375  1.00 24.12  ? 1138 HOH A O   1 
HETATM 10220 O  O   . HOH T 7 .   ? 7.088   49.821  5.765   1.00 45.92  ? 1139 HOH A O   1 
HETATM 10221 O  O   . HOH T 7 .   ? 22.763  50.749  -16.180 1.00 62.54  ? 1140 HOH A O   1 
HETATM 10222 O  O   . HOH T 7 .   ? 18.455  83.751  0.890   1.00 39.28  ? 1141 HOH A O   1 
HETATM 10223 O  O   . HOH T 7 .   ? 20.897  86.622  18.551  1.00 45.49  ? 1142 HOH A O   1 
HETATM 10224 O  O   . HOH T 7 .   ? 36.963  80.282  -6.061  1.00 57.77  ? 1143 HOH A O   1 
HETATM 10225 O  O   . HOH T 7 .   ? 23.707  75.678  -9.288  1.00 51.16  ? 1144 HOH A O   1 
HETATM 10226 O  O   . HOH T 7 .   ? 25.213  63.432  -4.685  1.00 58.88  ? 1145 HOH A O   1 
HETATM 10227 O  O   . HOH T 7 .   ? 38.206  41.384  -5.465  1.00 52.40  ? 1146 HOH A O   1 
HETATM 10228 O  O   . HOH T 7 .   ? 41.379  37.199  16.863  1.00 37.66  ? 1147 HOH A O   1 
HETATM 10229 O  O   . HOH T 7 .   ? 38.160  78.168  9.617   1.00 19.76  ? 1148 HOH A O   1 
HETATM 10230 O  O   . HOH T 7 .   ? 11.713  37.173  2.566   1.00 31.51  ? 1149 HOH A O   1 
HETATM 10231 O  O   . HOH T 7 .   ? 34.920  103.685 2.461   1.00 30.16  ? 1150 HOH A O   1 
HETATM 10232 O  O   . HOH T 7 .   ? 31.159  95.701  9.250   1.00 27.11  ? 1151 HOH A O   1 
HETATM 10233 O  O   . HOH T 7 .   ? 50.242  65.089  28.096  1.00 46.59  ? 1152 HOH A O   1 
HETATM 10234 O  O   . HOH T 7 .   ? 9.412   42.525  1.354   1.00 56.62  ? 1153 HOH A O   1 
HETATM 10235 O  O   . HOH T 7 .   ? 18.794  79.210  -0.260  1.00 41.12  ? 1154 HOH A O   1 
HETATM 10236 O  O   . HOH T 7 .   ? 39.343  98.119  10.384  1.00 50.14  ? 1155 HOH A O   1 
HETATM 10237 O  O   . HOH T 7 .   ? 23.609  62.433  -10.811 1.00 55.44  ? 1156 HOH A O   1 
HETATM 10238 O  O   . HOH T 7 .   ? 31.381  113.041 4.304   1.00 34.07  ? 1157 HOH A O   1 
HETATM 10239 O  O   . HOH T 7 .   ? 41.010  103.779 6.009   1.00 35.46  ? 1158 HOH A O   1 
HETATM 10240 O  O   . HOH T 7 .   ? 65.775  80.173  20.004  1.00 67.34  ? 1159 HOH A O   1 
HETATM 10241 O  O   . HOH T 7 .   ? 19.033  84.980  17.927  1.00 76.62  ? 1160 HOH A O   1 
HETATM 10242 O  O   . HOH T 7 .   ? 31.473  96.942  6.808   1.00 23.43  ? 1161 HOH A O   1 
HETATM 10243 O  O   . HOH T 7 .   ? 10.444  96.636  1.397   1.00 54.74  ? 1162 HOH A O   1 
HETATM 10244 O  O   . HOH T 7 .   ? 38.332  64.557  17.003  1.00 32.30  ? 1163 HOH A O   1 
HETATM 10245 O  O   . HOH T 7 .   ? 63.259  82.875  17.453  1.00 60.33  ? 1164 HOH A O   1 
HETATM 10246 O  O   . HOH T 7 .   ? 26.139  108.268 2.498   1.00 45.51  ? 1165 HOH A O   1 
HETATM 10247 O  O   . HOH T 7 .   ? 33.155  92.350  18.200  1.00 30.24  ? 1166 HOH A O   1 
HETATM 10248 O  O   . HOH T 7 .   ? 37.269  79.091  23.444  1.00 49.59  ? 1167 HOH A O   1 
HETATM 10249 O  O   . HOH T 7 .   ? 54.475  58.143  19.043  1.00 53.00  ? 1168 HOH A O   1 
HETATM 10250 O  O   . HOH T 7 .   ? 33.948  117.962 24.587  1.00 53.07  ? 1169 HOH A O   1 
HETATM 10251 O  O   . HOH T 7 .   ? 29.020  96.171  4.216   1.00 34.42  ? 1170 HOH A O   1 
HETATM 10252 O  O   . HOH T 7 .   ? 47.510  91.239  26.954  1.00 52.68  ? 1171 HOH A O   1 
HETATM 10253 O  O   . HOH T 7 .   ? 17.196  92.368  1.090   1.00 43.53  ? 1172 HOH A O   1 
HETATM 10254 O  O   . HOH T 7 .   ? 31.800  99.610  10.590  1.00 24.40  ? 1173 HOH A O   1 
HETATM 10255 O  O   . HOH T 7 .   ? 36.090  106.759 10.172  1.00 50.05  ? 1174 HOH A O   1 
HETATM 10256 O  O   . HOH T 7 .   ? 26.512  45.171  -11.609 1.00 35.30  ? 1175 HOH A O   1 
HETATM 10257 O  O   . HOH T 7 .   ? 43.939  76.660  -6.196  1.00 58.63  ? 1176 HOH A O   1 
HETATM 10258 O  O   . HOH T 7 .   ? 36.692  110.077 23.422  1.00 30.50  ? 1177 HOH A O   1 
HETATM 10259 O  O   . HOH T 7 .   ? 35.614  102.034 31.512  1.00 64.98  ? 1178 HOH A O   1 
HETATM 10260 O  O   . HOH T 7 .   ? 44.894  76.770  31.481  1.00 45.22  ? 1179 HOH A O   1 
HETATM 10261 O  O   . HOH T 7 .   ? 10.438  103.413 -1.735  1.00 65.71  ? 1180 HOH A O   1 
HETATM 10262 O  O   . HOH T 7 .   ? 36.104  96.029  10.465  1.00 38.63  ? 1181 HOH A O   1 
HETATM 10263 O  O   . HOH T 7 .   ? 21.819  107.576 6.708   1.00 25.89  ? 1182 HOH A O   1 
HETATM 10264 O  O   . HOH T 7 .   ? 26.564  87.674  11.040  1.00 33.05  ? 1183 HOH A O   1 
HETATM 10265 O  O   . HOH T 7 .   ? 57.354  88.096  21.986  1.00 59.31  ? 1184 HOH A O   1 
HETATM 10266 O  O   . HOH T 7 .   ? 23.904  47.162  23.864  1.00 33.92  ? 1185 HOH A O   1 
HETATM 10267 O  O   . HOH T 7 .   ? 11.802  41.344  0.684   1.00 53.42  ? 1186 HOH A O   1 
HETATM 10268 O  O   . HOH T 7 .   ? 35.651  102.335 16.485  1.00 30.77  ? 1187 HOH A O   1 
HETATM 10269 O  O   . HOH T 7 .   ? 11.784  46.614  14.764  1.00 34.62  ? 1188 HOH A O   1 
HETATM 10270 O  O   . HOH T 7 .   ? 55.530  70.307  8.588   1.00 29.68  ? 1189 HOH A O   1 
HETATM 10271 O  O   . HOH T 7 .   ? 15.774  95.541  14.333  1.00 17.81  ? 1190 HOH A O   1 
HETATM 10272 O  O   . HOH T 7 .   ? 33.761  109.173 3.870   1.00 62.02  ? 1191 HOH A O   1 
HETATM 10273 O  O   . HOH T 7 .   ? 34.065  110.769 28.481  1.00 47.97  ? 1192 HOH A O   1 
HETATM 10274 O  O   . HOH T 7 .   ? 19.821  56.786  22.460  1.00 60.28  ? 1193 HOH A O   1 
HETATM 10275 O  O   . HOH T 7 .   ? 15.045  98.098  1.777   1.00 23.11  ? 1194 HOH A O   1 
HETATM 10276 O  O   . HOH T 7 .   ? 15.269  88.009  3.295   1.00 57.12  ? 1195 HOH A O   1 
HETATM 10277 O  O   . HOH T 7 .   ? 21.274  112.050 27.843  1.00 39.53  ? 1196 HOH A O   1 
HETATM 10278 O  O   . HOH T 7 .   ? 58.933  65.251  13.324  1.00 39.96  ? 1197 HOH A O   1 
HETATM 10279 O  O   . HOH T 7 .   ? 29.722  92.821  23.494  1.00 53.83  ? 1198 HOH A O   1 
HETATM 10280 O  O   . HOH T 7 .   ? 48.390  63.732  26.857  1.00 37.58  ? 1199 HOH A O   1 
HETATM 10281 O  O   . HOH T 7 .   ? 21.870  117.963 31.873  1.00 58.48  ? 1200 HOH A O   1 
HETATM 10282 O  O   . HOH T 7 .   ? 34.639  70.977  -4.966  1.00 34.19  ? 1201 HOH A O   1 
HETATM 10283 O  O   . HOH T 7 .   ? 41.554  92.270  -11.771 1.00 39.34  ? 1202 HOH A O   1 
HETATM 10284 O  O   . HOH T 7 .   ? 29.376  88.012  18.382  1.00 32.15  ? 1203 HOH A O   1 
HETATM 10285 O  O   . HOH T 7 .   ? 33.895  97.917  9.601   1.00 34.71  ? 1204 HOH A O   1 
HETATM 10286 O  O   . HOH T 7 .   ? 35.520  53.258  13.946  1.00 33.48  ? 1205 HOH A O   1 
HETATM 10287 O  O   . HOH T 7 .   ? 46.146  100.952 12.638  1.00 76.57  ? 1206 HOH A O   1 
HETATM 10288 O  O   . HOH T 7 .   ? 45.747  87.680  -11.212 1.00 58.60  ? 1207 HOH A O   1 
HETATM 10289 O  O   . HOH T 7 .   ? 17.983  80.501  10.860  1.00 26.50  ? 1208 HOH A O   1 
HETATM 10290 O  O   . HOH T 7 .   ? 7.778   100.054 10.223  1.00 32.67  ? 1209 HOH A O   1 
HETATM 10291 O  O   . HOH T 7 .   ? 20.179  109.215 24.706  1.00 29.06  ? 1210 HOH A O   1 
HETATM 10292 O  O   . HOH T 7 .   ? 52.632  62.448  25.271  1.00 51.62  ? 1211 HOH A O   1 
HETATM 10293 O  O   . HOH T 7 .   ? 18.358  57.864  20.670  1.00 50.44  ? 1212 HOH A O   1 
HETATM 10294 O  O   . HOH T 7 .   ? 40.351  31.236  9.175   1.00 59.09  ? 1213 HOH A O   1 
HETATM 10295 O  O   . HOH T 7 .   ? 22.939  106.225 28.918  1.00 60.42  ? 1214 HOH A O   1 
HETATM 10296 O  O   . HOH T 7 .   ? 57.330  82.845  2.039   1.00 60.19  ? 1215 HOH A O   1 
HETATM 10297 O  O   . HOH T 7 .   ? 23.069  78.718  21.363  1.00 40.88  ? 1216 HOH A O   1 
HETATM 10298 O  O   . HOH T 7 .   ? 56.415  94.537  12.933  1.00 51.04  ? 1217 HOH A O   1 
HETATM 10299 O  O   . HOH T 7 .   ? 31.148  70.143  21.935  1.00 51.52  ? 1218 HOH A O   1 
HETATM 10300 O  O   . HOH T 7 .   ? 20.579  60.567  12.846  1.00 39.92  ? 1219 HOH A O   1 
HETATM 10301 O  O   . HOH T 7 .   ? 51.065  96.593  18.995  1.00 50.73  ? 1220 HOH A O   1 
HETATM 10302 O  O   . HOH T 7 .   ? 28.441  81.864  15.592  1.00 26.91  ? 1221 HOH A O   1 
HETATM 10303 O  O   . HOH T 7 .   ? 48.567  69.505  3.833   1.00 46.77  ? 1222 HOH A O   1 
HETATM 10304 O  O   . HOH T 7 .   ? 61.977  70.183  22.904  1.00 56.83  ? 1223 HOH A O   1 
HETATM 10305 O  O   . HOH T 7 .   ? 42.870  62.199  21.876  1.00 55.21  ? 1224 HOH A O   1 
HETATM 10306 O  O   . HOH T 7 .   ? 46.042  68.989  4.779   1.00 41.41  ? 1225 HOH A O   1 
HETATM 10307 O  O   . HOH T 7 .   ? 17.260  79.885  15.882  1.00 41.26  ? 1226 HOH A O   1 
HETATM 10308 O  O   . HOH T 7 .   ? 60.270  93.938  -0.445  1.00 47.84  ? 1227 HOH A O   1 
HETATM 10309 O  O   . HOH T 7 .   ? 9.725   38.695  2.418   1.00 51.39  ? 1228 HOH A O   1 
HETATM 10310 O  O   . HOH T 7 .   ? 27.012  63.562  10.463  1.00 37.36  ? 1229 HOH A O   1 
HETATM 10311 O  O   . HOH T 7 .   ? 59.488  94.166  2.289   1.00 53.33  ? 1230 HOH A O   1 
HETATM 10312 O  O   . HOH T 7 .   ? 38.040  41.002  22.104  1.00 52.53  ? 1231 HOH A O   1 
HETATM 10313 O  O   . HOH T 7 .   ? 33.368  102.682 -0.759  1.00 38.48  ? 1232 HOH A O   1 
HETATM 10314 O  O   . HOH T 7 .   ? 21.855  73.269  -8.129  1.00 48.95  ? 1233 HOH A O   1 
HETATM 10315 O  O   . HOH T 7 .   ? 42.409  48.415  -6.347  1.00 70.09  ? 1234 HOH A O   1 
HETATM 10316 O  O   . HOH T 7 .   ? 29.539  78.387  19.783  1.00 29.11  ? 1235 HOH A O   1 
HETATM 10317 O  O   . HOH T 7 .   ? 24.715  32.131  -1.728  1.00 51.77  ? 1236 HOH A O   1 
HETATM 10318 O  O   . HOH T 7 .   ? 62.090  90.966  -4.284  1.00 50.91  ? 1237 HOH A O   1 
HETATM 10319 O  O   . HOH T 7 .   ? 18.309  37.046  5.982   1.00 29.47  ? 1238 HOH A O   1 
HETATM 10320 O  O   . HOH T 7 .   ? 27.722  116.780 25.211  1.00 41.85  ? 1239 HOH A O   1 
HETATM 10321 O  O   . HOH T 7 .   ? 26.178  42.051  12.945  1.00 49.90  ? 1240 HOH A O   1 
HETATM 10322 O  O   . HOH T 7 .   ? 27.399  54.379  24.381  1.00 72.74  ? 1241 HOH A O   1 
HETATM 10323 O  O   . HOH T 7 .   ? 44.562  60.232  16.041  1.00 50.64  ? 1242 HOH A O   1 
HETATM 10324 O  O   . HOH T 7 .   ? 30.305  95.312  22.593  1.00 44.24  ? 1243 HOH A O   1 
HETATM 10325 O  O   . HOH T 7 .   ? 24.976  93.363  4.048   1.00 30.12  ? 1244 HOH A O   1 
HETATM 10326 O  O   . HOH T 7 .   ? 44.262  98.398  12.483  1.00 58.17  ? 1245 HOH A O   1 
HETATM 10327 O  O   . HOH T 7 .   ? 39.638  33.858  1.209   1.00 42.17  ? 1246 HOH A O   1 
HETATM 10328 O  O   . HOH T 7 .   ? 46.238  47.632  7.250   1.00 51.64  ? 1247 HOH A O   1 
HETATM 10329 O  O   . HOH T 7 .   ? 41.823  39.907  -1.193  1.00 62.37  ? 1248 HOH A O   1 
HETATM 10330 O  O   . HOH T 7 .   ? 44.347  93.009  -13.737 1.00 44.68  ? 1249 HOH A O   1 
HETATM 10331 O  O   . HOH T 7 .   ? 64.511  72.995  14.845  1.00 55.23  ? 1250 HOH A O   1 
HETATM 10332 O  O   . HOH T 7 .   ? 23.279  30.878  1.084   1.00 45.25  ? 1251 HOH A O   1 
HETATM 10333 O  O   . HOH T 7 .   ? 46.915  78.582  -3.608  1.00 45.23  ? 1252 HOH A O   1 
HETATM 10334 O  O   . HOH T 7 .   ? 63.554  76.627  26.047  1.00 59.56  ? 1253 HOH A O   1 
HETATM 10335 O  O   . HOH T 7 .   ? 40.899  65.507  2.905   1.00 29.16  ? 1254 HOH A O   1 
HETATM 10336 O  O   . HOH T 7 .   ? 33.576  94.045  14.790  1.00 30.83  ? 1255 HOH A O   1 
HETATM 10337 O  O   . HOH T 7 .   ? 40.165  45.845  -9.717  1.00 65.49  ? 1256 HOH A O   1 
HETATM 10338 O  O   . HOH T 7 .   ? 59.679  88.740  9.130   1.00 40.75  ? 1257 HOH A O   1 
HETATM 10339 O  O   . HOH T 7 .   ? 22.448  96.189  24.685  1.00 55.49  ? 1258 HOH A O   1 
HETATM 10340 O  O   . HOH T 7 .   ? 14.047  75.610  15.470  1.00 38.77  ? 1259 HOH A O   1 
HETATM 10341 O  O   . HOH T 7 .   ? 60.894  66.283  14.769  1.00 69.13  ? 1260 HOH A O   1 
HETATM 10342 O  O   . HOH T 7 .   ? 48.499  106.468 -5.509  1.00 43.90  ? 1261 HOH A O   1 
HETATM 10343 O  O   . HOH T 7 .   ? 42.213  101.366 -9.539  1.00 42.29  ? 1262 HOH A O   1 
HETATM 10344 O  O   . HOH T 7 .   ? 34.356  47.618  23.609  1.00 51.50  ? 1263 HOH A O   1 
HETATM 10345 O  O   . HOH T 7 .   ? 38.565  90.406  14.538  1.00 27.90  ? 1264 HOH A O   1 
HETATM 10346 O  O   . HOH T 7 .   ? 29.506  59.923  -11.630 1.00 57.49  ? 1265 HOH A O   1 
HETATM 10347 O  O   . HOH T 7 .   ? 15.960  30.471  -11.056 1.00 45.88  ? 1266 HOH A O   1 
HETATM 10348 O  O   . HOH T 7 .   ? 29.917  81.660  21.966  1.00 56.12  ? 1267 HOH A O   1 
HETATM 10349 O  O   . HOH T 7 .   ? 43.039  97.766  10.262  1.00 30.28  ? 1268 HOH A O   1 
HETATM 10350 O  O   . HOH T 7 .   ? 46.624  78.281  -6.683  1.00 61.66  ? 1269 HOH A O   1 
HETATM 10351 O  O   . HOH T 7 .   ? 23.826  100.404 28.034  1.00 62.76  ? 1270 HOH A O   1 
HETATM 10352 O  O   . HOH T 7 .   ? 15.937  63.304  9.835   1.00 59.65  ? 1271 HOH A O   1 
HETATM 10353 O  O   . HOH T 7 .   ? 44.091  64.921  30.392  1.00 54.06  ? 1272 HOH A O   1 
HETATM 10354 O  O   . HOH T 7 .   ? 28.666  91.591  -2.059  1.00 51.63  ? 1273 HOH A O   1 
HETATM 10355 O  O   . HOH T 7 .   ? 40.595  81.767  -8.920  1.00 48.68  ? 1274 HOH A O   1 
HETATM 10356 O  O   . HOH T 7 .   ? 28.345  85.698  -7.957  1.00 55.15  ? 1275 HOH A O   1 
HETATM 10357 O  O   . HOH T 7 .   ? 28.339  105.089 -0.736  1.00 61.82  ? 1276 HOH A O   1 
HETATM 10358 O  O   . HOH T 7 .   ? 27.819  59.963  17.174  1.00 53.89  ? 1277 HOH A O   1 
HETATM 10359 O  O   . HOH T 7 .   ? 23.296  42.522  13.623  1.00 46.68  ? 1278 HOH A O   1 
HETATM 10360 O  O   . HOH T 7 .   ? 31.832  96.659  21.238  1.00 48.00  ? 1279 HOH A O   1 
HETATM 10361 O  O   . HOH T 7 .   ? 4.720   32.470  9.205   1.00 56.43  ? 1280 HOH A O   1 
HETATM 10362 O  O   . HOH T 7 .   ? 21.215  88.502  0.604   1.00 59.27  ? 1281 HOH A O   1 
HETATM 10363 O  O   . HOH T 7 .   ? 42.541  89.908  21.794  1.00 49.86  ? 1282 HOH A O   1 
HETATM 10364 O  O   . HOH T 7 .   ? 34.246  56.238  16.925  1.00 47.50  ? 1283 HOH A O   1 
HETATM 10365 O  O   . HOH T 7 .   ? 63.204  81.836  20.023  1.00 54.92  ? 1284 HOH A O   1 
HETATM 10366 O  O   . HOH T 7 .   ? 44.081  77.677  -3.165  1.00 24.19  ? 1285 HOH A O   1 
HETATM 10367 O  O   . HOH T 7 .   ? 63.021  84.524  4.442   1.00 51.80  ? 1286 HOH A O   1 
HETATM 10368 O  O   . HOH T 7 .   ? 24.003  45.872  -11.810 1.00 54.96  ? 1287 HOH A O   1 
HETATM 10369 O  O   . HOH T 7 .   ? 9.457   83.725  1.627   1.00 35.44  ? 1288 HOH A O   1 
HETATM 10370 O  O   . HOH T 7 .   ? 53.973  93.635  23.588  1.00 60.36  ? 1289 HOH A O   1 
HETATM 10371 O  O   . HOH T 7 .   ? 8.327   101.370 16.282  1.00 63.61  ? 1290 HOH A O   1 
HETATM 10372 O  O   . HOH T 7 .   ? 44.894  69.276  31.108  1.00 50.10  ? 1291 HOH A O   1 
HETATM 10373 O  O   . HOH T 7 .   ? 19.580  38.033  16.009  1.00 57.54  ? 1292 HOH A O   1 
HETATM 10374 O  O   . HOH T 7 .   ? 38.302  116.085 16.828  1.00 52.44  ? 1293 HOH A O   1 
HETATM 10375 O  O   . HOH T 7 .   ? 44.042  74.762  -3.181  1.00 56.09  ? 1294 HOH A O   1 
HETATM 10376 O  O   . HOH T 7 .   ? 43.052  83.243  -10.311 1.00 51.56  ? 1295 HOH A O   1 
HETATM 10377 O  O   . HOH T 7 .   ? 17.114  88.867  -0.055  1.00 81.85  ? 1296 HOH A O   1 
HETATM 10378 O  O   . HOH T 7 .   ? 25.766  65.776  -6.946  1.00 56.31  ? 1297 HOH A O   1 
HETATM 10379 O  O   . HOH T 7 .   ? 34.801  91.392  20.259  1.00 57.87  ? 1298 HOH A O   1 
HETATM 10380 O  O   . HOH T 7 .   ? 34.570  52.316  21.499  1.00 60.20  ? 1299 HOH A O   1 
HETATM 10381 O  O   . HOH T 7 .   ? 41.695  115.175 22.229  1.00 62.66  ? 1300 HOH A O   1 
HETATM 10382 O  O   . HOH T 7 .   ? 35.745  70.027  24.377  1.00 57.79  ? 1301 HOH A O   1 
HETATM 10383 O  O   . HOH T 7 .   ? 23.121  31.114  -9.912  1.00 60.27  ? 1302 HOH A O   1 
HETATM 10384 O  O   . HOH T 7 .   ? 15.693  46.558  -8.757  1.00 56.66  ? 1303 HOH A O   1 
HETATM 10385 O  O   . HOH T 7 .   ? 16.279  107.014 3.223   1.00 49.25  ? 1304 HOH A O   1 
HETATM 10386 O  O   . HOH T 7 .   ? 33.287  32.363  -0.836  1.00 54.60  ? 1305 HOH A O   1 
HETATM 10387 O  O   . HOH T 7 .   ? 14.143  91.186  1.798   1.00 50.92  ? 1306 HOH A O   1 
HETATM 10388 O  O   . HOH T 7 .   ? 18.643  87.792  23.971  1.00 64.16  ? 1307 HOH A O   1 
HETATM 10389 O  O   . HOH T 7 .   ? 36.424  66.038  18.096  1.00 56.02  ? 1308 HOH A O   1 
HETATM 10390 O  O   . HOH T 7 .   ? 38.842  104.859 5.337   1.00 53.81  ? 1309 HOH A O   1 
HETATM 10391 O  O   . HOH T 7 .   ? 38.148  81.621  24.268  1.00 70.30  ? 1310 HOH A O   1 
HETATM 10392 O  O   . HOH T 7 .   ? 19.817  44.926  10.156  1.00 27.59  ? 1311 HOH A O   1 
HETATM 10393 O  O   . HOH T 7 .   ? 37.854  62.216  15.167  1.00 49.80  ? 1312 HOH A O   1 
HETATM 10394 O  O   . HOH T 7 .   ? 42.265  64.674  7.733   1.00 66.39  ? 1313 HOH A O   1 
HETATM 10395 O  O   . HOH T 7 .   ? 62.351  87.194  9.392   1.00 45.88  ? 1314 HOH A O   1 
HETATM 10396 O  O   . HOH T 7 .   ? 43.403  102.217 23.978  1.00 63.00  ? 1315 HOH A O   1 
HETATM 10397 O  O   . HOH T 7 .   ? 36.795  55.746  12.298  1.00 47.16  ? 1316 HOH A O   1 
HETATM 10398 O  O   . HOH T 7 .   ? 46.843  107.027 -3.643  1.00 35.95  ? 1317 HOH A O   1 
HETATM 10399 O  O   . HOH T 7 .   ? 42.536  66.908  6.306   1.00 38.55  ? 1318 HOH A O   1 
HETATM 10400 O  O   . HOH T 7 .   ? 48.342  97.369  -10.727 1.00 53.16  ? 1319 HOH A O   1 
HETATM 10401 O  O   . HOH T 7 .   ? 51.475  106.721 -7.650  1.00 62.10  ? 1320 HOH A O   1 
HETATM 10402 O  O   . HOH T 7 .   ? 18.950  100.561 23.439  1.00 56.69  ? 1321 HOH A O   1 
HETATM 10403 O  O   . HOH T 7 .   ? 6.016   78.888  5.691   1.00 57.79  ? 1322 HOH A O   1 
HETATM 10404 O  O   . HOH T 7 .   ? 57.289  68.345  7.819   1.00 39.37  ? 1323 HOH A O   1 
HETATM 10405 O  O   . HOH T 7 .   ? 27.814  119.808 15.337  1.00 51.54  ? 1324 HOH A O   1 
HETATM 10406 O  O   . HOH T 7 .   ? 28.640  81.909  -12.810 1.00 60.44  ? 1325 HOH A O   1 
HETATM 10407 O  O   . HOH T 7 .   ? 39.798  102.829 8.398   1.00 55.83  ? 1326 HOH A O   1 
HETATM 10408 O  O   . HOH T 7 .   ? 29.449  120.991 10.761  1.00 58.63  ? 1327 HOH A O   1 
HETATM 10409 O  O   . HOH T 7 .   ? 40.535  34.921  20.528  1.00 55.76  ? 1328 HOH A O   1 
HETATM 10410 O  O   . HOH T 7 .   ? 39.770  60.687  13.236  1.00 40.07  ? 1329 HOH A O   1 
HETATM 10411 O  O   . HOH T 7 .   ? 66.926  77.479  25.478  1.00 63.96  ? 1330 HOH A O   1 
HETATM 10412 O  O   . HOH T 7 .   ? 27.989  87.533  -6.278  1.00 45.29  ? 1331 HOH A O   1 
HETATM 10413 O  O   . HOH T 7 .   ? 22.621  30.718  10.728  1.00 71.61  ? 1332 HOH A O   1 
HETATM 10414 O  O   . HOH T 7 .   ? 29.127  117.012 4.007   1.00 53.50  ? 1333 HOH A O   1 
HETATM 10415 O  O   . HOH T 7 .   ? 7.514   102.650 13.811  1.00 51.53  ? 1334 HOH A O   1 
HETATM 10416 O  O   . HOH T 7 .   ? 19.475  82.481  16.548  1.00 49.70  ? 1335 HOH A O   1 
HETATM 10417 O  O   . HOH T 7 .   ? 61.842  79.142  28.916  1.00 55.74  ? 1336 HOH A O   1 
HETATM 10418 O  O   . HOH T 7 .   ? 57.558  61.644  24.199  1.00 62.78  ? 1337 HOH A O   1 
HETATM 10419 O  O   . HOH T 7 .   ? 34.744  52.217  -10.470 1.00 48.15  ? 1338 HOH A O   1 
HETATM 10420 O  O   . HOH T 7 .   ? 31.905  30.127  11.037  1.00 62.47  ? 1339 HOH A O   1 
HETATM 10421 O  O   . HOH T 7 .   ? 30.655  62.200  -10.509 1.00 62.87  ? 1340 HOH A O   1 
HETATM 10422 O  O   . HOH T 7 .   ? 18.747  100.877 0.767   1.00 39.71  ? 1341 HOH A O   1 
HETATM 10423 O  O   . HOH T 7 .   ? 38.341  104.369 -4.275  1.00 25.92  ? 1342 HOH A O   1 
HETATM 10424 O  O   . HOH T 7 .   ? 17.821  113.383 7.577   1.00 47.73  ? 1343 HOH A O   1 
HETATM 10425 O  O   . HOH T 7 .   ? 12.354  95.119  2.063   1.00 44.19  ? 1344 HOH A O   1 
HETATM 10426 O  O   . HOH T 7 .   ? 17.959  41.538  -11.727 1.00 71.80  ? 1345 HOH A O   1 
HETATM 10427 O  O   . HOH T 7 .   ? 23.838  81.569  21.463  1.00 54.47  ? 1346 HOH A O   1 
HETATM 10428 O  O   . HOH T 7 .   ? 35.069  50.302  23.658  1.00 42.31  ? 1347 HOH A O   1 
HETATM 10429 O  O   . HOH T 7 .   ? 63.013  87.835  19.069  1.00 56.10  ? 1348 HOH A O   1 
HETATM 10430 O  O   . HOH T 7 .   ? 38.108  51.135  -7.405  1.00 54.94  ? 1349 HOH A O   1 
HETATM 10431 O  O   . HOH T 7 .   ? 41.085  52.413  16.417  1.00 58.99  ? 1350 HOH A O   1 
HETATM 10432 O  O   . HOH T 7 .   ? 52.204  63.642  27.606  1.00 50.68  ? 1351 HOH A O   1 
HETATM 10433 O  O   . HOH T 7 .   ? 30.024  96.068  25.040  1.00 54.92  ? 1352 HOH A O   1 
HETATM 10434 O  O   . HOH T 7 .   ? 36.630  100.267 -5.873  1.00 28.45  ? 1353 HOH A O   1 
HETATM 10435 O  O   . HOH T 7 .   ? 58.353  101.655 -4.632  1.00 55.40  ? 1354 HOH A O   1 
HETATM 10436 O  O   . HOH T 7 .   ? 27.884  59.766  21.386  1.00 66.57  ? 1355 HOH A O   1 
HETATM 10437 O  O   . HOH T 7 .   ? 23.059  67.735  5.101   1.00 41.24  ? 1356 HOH A O   1 
HETATM 10438 O  O   . HOH T 7 .   ? 38.436  65.187  0.688   1.00 59.80  ? 1357 HOH A O   1 
HETATM 10439 O  O   . HOH T 7 .   ? 16.946  112.651 11.425  1.00 52.19  ? 1358 HOH A O   1 
HETATM 10440 O  O   . HOH T 7 .   ? 42.401  60.500  12.713  1.00 53.88  ? 1359 HOH A O   1 
HETATM 10441 O  O   . HOH T 7 .   ? 14.413  43.317  -7.603  1.00 62.82  ? 1360 HOH A O   1 
HETATM 10442 O  O   . HOH T 7 .   ? 38.767  100.115 13.233  1.00 71.70  ? 1361 HOH A O   1 
HETATM 10443 O  O   . HOH T 7 .   ? 31.397  117.584 22.872  1.00 60.71  ? 1362 HOH A O   1 
HETATM 10444 O  O   . HOH T 7 .   ? 20.422  45.023  14.139  1.00 29.08  ? 1363 HOH A O   1 
HETATM 10445 O  O   . HOH T 7 .   ? 30.589  83.639  20.117  1.00 52.42  ? 1364 HOH A O   1 
HETATM 10446 O  O   . HOH T 7 .   ? 61.970  91.441  -7.287  1.00 57.90  ? 1365 HOH A O   1 
HETATM 10447 O  O   . HOH T 7 .   ? 34.953  59.957  -0.804  1.00 44.15  ? 1366 HOH A O   1 
HETATM 10448 O  O   . HOH T 7 .   ? 45.454  47.279  19.955  1.00 58.98  ? 1367 HOH A O   1 
HETATM 10449 O  O   . HOH T 7 .   ? 61.733  67.414  12.052  1.00 58.76  ? 1368 HOH A O   1 
HETATM 10450 O  O   . HOH T 7 .   ? 26.216  106.617 31.941  1.00 53.96  ? 1369 HOH A O   1 
HETATM 10451 O  O   . HOH T 7 .   ? 43.152  86.580  25.400  1.00 60.20  ? 1370 HOH A O   1 
HETATM 10452 O  O   . HOH T 7 .   ? 23.627  31.676  7.290   1.00 55.39  ? 1371 HOH A O   1 
HETATM 10453 O  O   . HOH T 7 .   ? 12.156  92.594  2.926   1.00 28.79  ? 1372 HOH A O   1 
HETATM 10454 O  O   . HOH T 7 .   ? 21.804  93.739  0.374   1.00 55.55  ? 1373 HOH A O   1 
HETATM 10455 O  O   . HOH T 7 .   ? 57.899  90.847  24.133  1.00 59.15  ? 1374 HOH A O   1 
HETATM 10456 O  O   . HOH T 7 .   ? 35.367  53.524  16.781  1.00 57.35  ? 1375 HOH A O   1 
HETATM 10457 O  O   . HOH T 7 .   ? 24.470  98.331  29.900  1.00 62.48  ? 1376 HOH A O   1 
HETATM 10458 O  O   . HOH T 7 .   ? 30.305  86.074  -9.550  1.00 55.88  ? 1377 HOH A O   1 
HETATM 10459 O  O   . HOH T 7 .   ? 29.179  80.599  18.079  1.00 27.47  ? 1378 HOH A O   1 
HETATM 10460 O  O   . HOH T 7 .   ? 22.852  107.949 3.444   1.00 54.89  ? 1379 HOH A O   1 
HETATM 10461 O  O   . HOH T 7 .   ? 40.922  104.368 11.483  1.00 55.62  ? 1380 HOH A O   1 
HETATM 10462 O  O   . HOH T 7 .   ? 31.616  79.612  21.503  1.00 51.81  ? 1381 HOH A O   1 
HETATM 10463 O  O   . HOH T 7 .   ? 58.219  64.112  10.595  1.00 63.90  ? 1382 HOH A O   1 
HETATM 10464 O  O   . HOH T 7 .   ? 38.246  54.406  13.664  1.00 51.86  ? 1383 HOH A O   1 
HETATM 10465 O  O   . HOH T 7 .   ? 11.972  38.935  -0.916  1.00 52.96  ? 1384 HOH A O   1 
HETATM 10466 O  O   . HOH T 7 .   ? 20.523  116.076 6.291   1.00 31.42  ? 1385 HOH A O   1 
HETATM 10467 O  O   . HOH T 7 .   ? 33.267  91.091  -8.780  1.00 41.74  ? 1386 HOH A O   1 
HETATM 10468 O  O   . HOH T 7 .   ? 18.269  109.711 22.576  1.00 28.45  ? 1387 HOH A O   1 
HETATM 10469 O  O   . HOH T 7 .   ? 55.652  108.120 -4.248  1.00 38.45  ? 1388 HOH A O   1 
HETATM 10470 O  O   . HOH T 7 .   ? 31.743  47.671  25.576  1.00 52.90  ? 1389 HOH A O   1 
HETATM 10471 O  O   . HOH T 7 .   ? 17.400  97.274  23.023  1.00 65.05  ? 1390 HOH A O   1 
HETATM 10472 O  O   . HOH T 7 .   ? 29.350  95.126  -0.586  1.00 46.33  ? 1391 HOH A O   1 
HETATM 10473 O  O   . HOH T 7 .   ? 25.927  97.476  26.435  1.00 55.47  ? 1392 HOH A O   1 
HETATM 10474 O  O   . HOH T 7 .   ? 26.952  83.996  18.845  1.00 57.13  ? 1393 HOH A O   1 
HETATM 10475 O  O   . HOH T 7 .   ? 30.527  50.272  27.093  1.00 59.67  ? 1394 HOH A O   1 
HETATM 10476 O  O   . HOH T 7 .   ? 43.275  88.260  -11.509 1.00 41.01  ? 1395 HOH A O   1 
HETATM 10477 O  O   . HOH T 7 .   ? 5.924   47.155  -3.420  1.00 68.55  ? 1396 HOH A O   1 
HETATM 10478 O  O   . HOH T 7 .   ? 37.845  71.838  23.594  1.00 44.61  ? 1397 HOH A O   1 
HETATM 10479 O  O   . HOH T 7 .   ? 29.964  88.942  -10.011 1.00 48.81  ? 1398 HOH A O   1 
HETATM 10480 O  O   . HOH T 7 .   ? 25.690  123.288 11.101  1.00 46.87  ? 1399 HOH A O   1 
HETATM 10481 O  O   . HOH T 7 .   ? 63.075  80.629  15.100  1.00 51.05  ? 1400 HOH A O   1 
HETATM 10482 O  O   . HOH T 7 .   ? 16.880  83.656  14.401  1.00 53.77  ? 1401 HOH A O   1 
HETATM 10483 O  O   . HOH T 7 .   ? 44.761  104.871 12.031  1.00 60.57  ? 1402 HOH A O   1 
HETATM 10484 O  O   . HOH T 7 .   ? 16.130  100.766 1.844   1.00 23.46  ? 1403 HOH A O   1 
HETATM 10485 O  O   . HOH T 7 .   ? 11.298  35.631  0.189   1.00 41.02  ? 1404 HOH A O   1 
HETATM 10486 O  O   . HOH T 7 .   ? 17.346  85.991  1.255   1.00 50.27  ? 1405 HOH A O   1 
HETATM 10487 O  O   . HOH T 7 .   ? 18.411  115.086 5.646   1.00 36.86  ? 1406 HOH A O   1 
HETATM 10488 O  O   . HOH T 7 .   ? 19.351  83.189  -1.656  1.00 61.77  ? 1407 HOH A O   1 
HETATM 10489 O  O   . HOH T 7 .   ? 5.883   97.263  15.055  1.00 52.93  ? 1408 HOH A O   1 
HETATM 10490 O  O   . HOH T 7 .   ? 62.432  84.101  21.652  1.00 54.04  ? 1409 HOH A O   1 
HETATM 10491 O  O   . HOH T 7 .   ? 58.683  89.777  11.724  1.00 38.69  ? 1410 HOH A O   1 
HETATM 10492 O  O   . HOH T 7 .   ? 33.575  95.081  18.439  1.00 39.73  ? 1411 HOH A O   1 
HETATM 10493 O  O   . HOH T 7 .   ? 60.194  67.864  25.597  1.00 39.85  ? 1412 HOH A O   1 
HETATM 10494 O  O   . HOH T 7 .   ? 37.004  93.477  -7.702  1.00 28.99  ? 1413 HOH A O   1 
HETATM 10495 O  O   . HOH T 7 .   ? 24.113  98.118  1.978   1.00 46.01  ? 1414 HOH A O   1 
HETATM 10496 O  O   . HOH T 7 .   ? 26.028  90.238  22.811  1.00 50.62  ? 1415 HOH A O   1 
HETATM 10497 O  O   . HOH T 7 .   ? 15.835  84.528  11.085  1.00 30.36  ? 1416 HOH A O   1 
HETATM 10498 O  O   . HOH T 7 .   ? 11.483  92.637  5.531   1.00 23.29  ? 1417 HOH A O   1 
HETATM 10499 O  O   . HOH T 7 .   ? 30.519  123.699 19.644  1.00 57.88  ? 1418 HOH A O   1 
HETATM 10500 O  O   . HOH T 7 .   ? 13.642  105.581 3.527   1.00 46.28  ? 1419 HOH A O   1 
HETATM 10501 O  O   . HOH T 7 .   ? 49.116  60.842  23.203  1.00 65.72  ? 1420 HOH A O   1 
HETATM 10502 O  O   . HOH T 7 .   ? 13.811  97.573  -0.478  1.00 54.38  ? 1421 HOH A O   1 
HETATM 10503 O  O   . HOH T 7 .   ? 53.036  106.829 -7.261  1.00 82.32  ? 1422 HOH A O   1 
HETATM 10504 O  O   . HOH T 7 .   ? 30.212  60.724  14.062  1.00 48.59  ? 1423 HOH A O   1 
HETATM 10505 O  O   . HOH T 7 .   ? 15.377  57.116  21.391  1.00 59.15  ? 1424 HOH A O   1 
HETATM 10506 O  O   . HOH T 7 .   ? 24.366  77.153  -11.305 1.00 67.19  ? 1425 HOH A O   1 
HETATM 10507 O  O   . HOH T 7 .   ? 39.690  102.761 -8.367  1.00 45.40  ? 1426 HOH A O   1 
HETATM 10508 O  O   . HOH T 7 .   ? 61.782  59.179  14.416  1.00 57.63  ? 1427 HOH A O   1 
HETATM 10509 O  O   . HOH T 7 .   ? 29.009  56.797  17.310  1.00 34.27  ? 1428 HOH A O   1 
HETATM 10510 O  O   . HOH T 7 .   ? 34.167  101.313 -5.184  1.00 53.80  ? 1429 HOH A O   1 
HETATM 10511 O  O   . HOH T 7 .   ? 64.865  86.062  20.357  1.00 53.46  ? 1430 HOH A O   1 
HETATM 10512 O  O   . HOH T 7 .   ? 40.136  104.891 15.079  1.00 57.13  ? 1431 HOH A O   1 
HETATM 10513 O  O   . HOH T 7 .   ? 15.227  102.778 0.461   1.00 48.32  ? 1432 HOH A O   1 
HETATM 10514 O  O   . HOH T 7 .   ? 23.500  40.521  14.972  1.00 62.85  ? 1433 HOH A O   1 
HETATM 10515 O  O   . HOH T 7 .   ? 36.781  93.761  -10.258 1.00 42.31  ? 1434 HOH A O   1 
HETATM 10516 O  O   . HOH T 7 .   ? 25.444  86.394  19.756  1.00 54.80  ? 1435 HOH A O   1 
HETATM 10517 O  O   . HOH T 7 .   ? 20.774  80.289  -1.962  1.00 52.02  ? 1436 HOH A O   1 
HETATM 10518 O  O   . HOH T 7 .   ? 37.306  97.073  -9.369  1.00 42.88  ? 1437 HOH A O   1 
HETATM 10519 O  O   . HOH T 7 .   ? 57.755  109.355 -3.183  1.00 48.87  ? 1438 HOH A O   1 
HETATM 10520 O  O   . HOH T 7 .   ? 13.469  88.033  1.015   1.00 53.98  ? 1439 HOH A O   1 
HETATM 10521 O  O   . HOH T 7 .   ? 59.534  89.318  15.410  1.00 42.25  ? 1440 HOH A O   1 
HETATM 10522 O  O   . HOH T 7 .   ? 39.259  79.740  -11.833 1.00 55.27  ? 1441 HOH A O   1 
HETATM 10523 O  O   . HOH T 7 .   ? 5.466   39.742  10.385  1.00 64.48  ? 1442 HOH A O   1 
HETATM 10524 O  O   . HOH T 7 .   ? 29.820  122.814 12.803  1.00 57.51  ? 1443 HOH A O   1 
HETATM 10525 O  O   . HOH U 7 .   ? -30.467 53.221  50.105  1.00 40.25  ? 801  HOH B O   1 
HETATM 10526 O  O   . HOH U 7 .   ? 0.369   39.987  28.095  1.00 52.10  ? 802  HOH B O   1 
HETATM 10527 O  O   . HOH U 7 .   ? -14.403 107.309 19.343  1.00 50.99  ? 803  HOH B O   1 
HETATM 10528 O  O   . HOH U 7 .   ? 12.126  54.105  29.246  1.00 40.40  ? 804  HOH B O   1 
HETATM 10529 O  O   . HOH U 7 .   ? -0.110  57.409  14.534  1.00 50.39  ? 805  HOH B O   1 
HETATM 10530 O  O   . HOH U 7 .   ? 1.673   63.684  57.393  1.00 47.13  ? 806  HOH B O   1 
HETATM 10531 O  O   . HOH U 7 .   ? -11.410 54.822  55.691  1.00 68.02  ? 807  HOH B O   1 
HETATM 10532 O  O   . HOH U 7 .   ? -14.048 84.650  28.619  1.00 75.14  ? 808  HOH B O   1 
HETATM 10533 O  O   . HOH U 7 .   ? 15.487  31.018  12.230  1.00 39.38  ? 809  HOH B O   1 
HETATM 10534 O  O   . HOH U 7 .   ? 7.224   88.733  1.709   1.00 41.62  ? 810  HOH B O   1 
HETATM 10535 O  O   . HOH U 7 .   ? -22.587 70.085  50.962  1.00 60.34  ? 811  HOH B O   1 
HETATM 10536 O  O   . HOH U 7 .   ? -16.226 73.205  2.375   1.00 41.38  ? 812  HOH B O   1 
HETATM 10537 O  O   . HOH U 7 .   ? -24.530 48.992  50.564  1.00 49.78  ? 813  HOH B O   1 
HETATM 10538 O  O   . HOH U 7 .   ? -14.171 77.722  27.740  1.00 49.71  ? 814  HOH B O   1 
HETATM 10539 O  O   . HOH U 7 .   ? 2.278   75.833  24.250  1.00 41.17  ? 815  HOH B O   1 
HETATM 10540 O  O   . HOH U 7 .   ? 18.064  48.179  15.333  1.00 27.14  ? 816  HOH B O   1 
HETATM 10541 O  O   . HOH U 7 .   ? 5.467   108.058 3.137   1.00 35.02  ? 817  HOH B O   1 
HETATM 10542 O  O   . HOH U 7 .   ? 9.452   80.470  9.180   1.00 33.58  ? 818  HOH B O   1 
HETATM 10543 O  O   . HOH U 7 .   ? -0.326  50.376  39.931  1.00 51.48  ? 819  HOH B O   1 
HETATM 10544 O  O   . HOH U 7 .   ? 1.749   37.846  38.953  1.00 21.86  ? 820  HOH B O   1 
HETATM 10545 O  O   . HOH U 7 .   ? -5.529  54.890  16.684  1.00 33.72  ? 821  HOH B O   1 
HETATM 10546 O  O   . HOH U 7 .   ? 12.744  44.212  16.201  1.00 42.07  ? 822  HOH B O   1 
HETATM 10547 O  O   . HOH U 7 .   ? -6.564  71.495  13.104  1.00 83.56  ? 823  HOH B O   1 
HETATM 10548 O  O   . HOH U 7 .   ? 3.068   94.416  -3.204  1.00 63.10  ? 824  HOH B O   1 
HETATM 10549 O  O   . HOH U 7 .   ? -7.396  73.702  7.068   1.00 54.75  ? 825  HOH B O   1 
HETATM 10550 O  O   . HOH U 7 .   ? -2.889  36.315  29.636  1.00 43.98  ? 826  HOH B O   1 
HETATM 10551 O  O   . HOH U 7 .   ? -2.480  51.792  17.081  1.00 57.97  ? 827  HOH B O   1 
HETATM 10552 O  O   . HOH U 7 .   ? -23.293 70.238  48.345  1.00 38.90  ? 828  HOH B O   1 
HETATM 10553 O  O   . HOH U 7 .   ? 1.532   47.423  22.307  1.00 32.90  ? 829  HOH B O   1 
HETATM 10554 O  O   . HOH U 7 .   ? 8.278   35.942  51.721  1.00 33.04  ? 830  HOH B O   1 
HETATM 10555 O  O   . HOH U 7 .   ? -14.357 68.042  18.829  1.00 40.38  ? 831  HOH B O   1 
HETATM 10556 O  O   . HOH U 7 .   ? -20.421 78.656  13.493  1.00 59.88  ? 832  HOH B O   1 
HETATM 10557 O  O   . HOH U 7 .   ? 8.761   54.920  35.166  1.00 31.46  ? 833  HOH B O   1 
HETATM 10558 O  O   . HOH U 7 .   ? 7.666   39.512  28.842  1.00 21.96  ? 834  HOH B O   1 
HETATM 10559 O  O   . HOH U 7 .   ? -0.239  78.485  28.010  1.00 48.73  ? 835  HOH B O   1 
HETATM 10560 O  O   . HOH U 7 .   ? 5.203   96.651  37.135  1.00 54.40  ? 836  HOH B O   1 
HETATM 10561 O  O   . HOH U 7 .   ? 7.492   91.293  -0.882  1.00 62.63  ? 837  HOH B O   1 
HETATM 10562 O  O   . HOH U 7 .   ? -17.014 61.676  23.927  1.00 41.37  ? 838  HOH B O   1 
HETATM 10563 O  O   . HOH U 7 .   ? -13.057 68.228  51.193  1.00 27.82  ? 839  HOH B O   1 
HETATM 10564 O  O   . HOH U 7 .   ? 20.461  39.904  34.089  1.00 30.70  ? 840  HOH B O   1 
HETATM 10565 O  O   . HOH U 7 .   ? 1.659   55.339  42.293  1.00 39.15  ? 841  HOH B O   1 
HETATM 10566 O  O   . HOH U 7 .   ? -1.718  75.783  17.014  1.00 45.47  ? 842  HOH B O   1 
HETATM 10567 O  O   . HOH U 7 .   ? 10.990  30.400  11.786  1.00 55.44  ? 843  HOH B O   1 
HETATM 10568 O  O   . HOH U 7 .   ? -23.333 86.495  13.063  1.00 34.91  ? 844  HOH B O   1 
HETATM 10569 O  O   . HOH U 7 .   ? 1.070   29.433  31.316  1.00 33.51  ? 845  HOH B O   1 
HETATM 10570 O  O   . HOH U 7 .   ? 22.213  31.624  39.349  1.00 45.71  ? 846  HOH B O   1 
HETATM 10571 O  O   . HOH U 7 .   ? 9.289   95.480  3.112   1.00 22.23  ? 847  HOH B O   1 
HETATM 10572 O  O   . HOH U 7 .   ? -19.825 64.438  25.360  1.00 52.42  ? 848  HOH B O   1 
HETATM 10573 O  O   . HOH U 7 .   ? -9.513  74.995  24.494  1.00 27.78  ? 849  HOH B O   1 
HETATM 10574 O  O   . HOH U 7 .   ? 0.560   77.196  23.129  1.00 30.76  ? 850  HOH B O   1 
HETATM 10575 O  O   . HOH U 7 .   ? -8.974  62.510  48.386  1.00 27.19  ? 851  HOH B O   1 
HETATM 10576 O  O   . HOH U 7 .   ? -22.633 92.611  26.024  1.00 32.86  ? 852  HOH B O   1 
HETATM 10577 O  O   . HOH U 7 .   ? -0.162  34.694  36.088  1.00 25.36  ? 853  HOH B O   1 
HETATM 10578 O  O   . HOH U 7 .   ? -10.210 81.711  32.263  1.00 51.02  ? 854  HOH B O   1 
HETATM 10579 O  O   . HOH U 7 .   ? -25.991 63.004  49.794  1.00 28.25  ? 855  HOH B O   1 
HETATM 10580 O  O   . HOH U 7 .   ? 15.503  29.895  30.278  1.00 45.02  ? 856  HOH B O   1 
HETATM 10581 O  O   . HOH U 7 .   ? 15.698  28.716  46.678  1.00 41.26  ? 857  HOH B O   1 
HETATM 10582 O  O   . HOH U 7 .   ? 4.020   27.240  29.152  1.00 49.89  ? 858  HOH B O   1 
HETATM 10583 O  O   . HOH U 7 .   ? -1.448  48.515  48.386  1.00 51.14  ? 859  HOH B O   1 
HETATM 10584 O  O   . HOH U 7 .   ? 19.519  29.067  43.972  1.00 49.90  ? 860  HOH B O   1 
HETATM 10585 O  O   . HOH U 7 .   ? -10.220 103.024 25.862  1.00 34.70  ? 861  HOH B O   1 
HETATM 10586 O  O   . HOH U 7 .   ? 8.316   90.465  15.863  1.00 29.47  ? 862  HOH B O   1 
HETATM 10587 O  O   . HOH U 7 .   ? -19.711 56.270  42.194  1.00 25.09  ? 863  HOH B O   1 
HETATM 10588 O  O   . HOH U 7 .   ? -25.226 91.861  18.841  1.00 31.59  ? 864  HOH B O   1 
HETATM 10589 O  O   . HOH U 7 .   ? -13.679 81.044  24.174  1.00 33.60  ? 865  HOH B O   1 
HETATM 10590 O  O   . HOH U 7 .   ? 4.816   77.817  48.521  1.00 50.35  ? 866  HOH B O   1 
HETATM 10591 O  O   . HOH U 7 .   ? -11.473 59.345  25.932  1.00 21.24  ? 867  HOH B O   1 
HETATM 10592 O  O   . HOH U 7 .   ? 0.393   67.578  17.856  1.00 22.45  ? 868  HOH B O   1 
HETATM 10593 O  O   . HOH U 7 .   ? -16.558 86.542  25.558  1.00 38.63  ? 869  HOH B O   1 
HETATM 10594 O  O   . HOH U 7 .   ? 14.711  36.458  55.980  1.00 35.16  ? 870  HOH B O   1 
HETATM 10595 O  O   . HOH U 7 .   ? -10.595 101.649 28.934  1.00 39.25  ? 871  HOH B O   1 
HETATM 10596 O  O   . HOH U 7 .   ? -20.921 47.197  28.836  1.00 34.42  ? 872  HOH B O   1 
HETATM 10597 O  O   . HOH U 7 .   ? -1.765  52.613  39.817  1.00 38.13  ? 873  HOH B O   1 
HETATM 10598 O  O   . HOH U 7 .   ? 1.938   106.692 4.664   1.00 38.52  ? 874  HOH B O   1 
HETATM 10599 O  O   . HOH U 7 .   ? -12.899 98.916  -2.464  1.00 35.24  ? 875  HOH B O   1 
HETATM 10600 O  O   . HOH U 7 .   ? -12.622 36.708  43.226  1.00 52.83  ? 876  HOH B O   1 
HETATM 10601 O  O   . HOH U 7 .   ? 1.621   59.814  36.478  1.00 26.31  ? 877  HOH B O   1 
HETATM 10602 O  O   . HOH U 7 .   ? 17.364  44.037  31.108  1.00 27.53  ? 878  HOH B O   1 
HETATM 10603 O  O   . HOH U 7 .   ? -2.391  94.231  0.294   1.00 44.33  ? 879  HOH B O   1 
HETATM 10604 O  O   . HOH U 7 .   ? -12.755 82.973  1.108   1.00 47.42  ? 880  HOH B O   1 
HETATM 10605 O  O   . HOH U 7 .   ? 7.010   71.809  28.582  1.00 36.09  ? 881  HOH B O   1 
HETATM 10606 O  O   . HOH U 7 .   ? 10.741  47.804  40.793  1.00 41.60  ? 882  HOH B O   1 
HETATM 10607 O  O   . HOH U 7 .   ? -5.714  82.182  26.537  1.00 24.43  ? 883  HOH B O   1 
HETATM 10608 O  O   . HOH U 7 .   ? -4.277  99.455  5.064   1.00 18.98  ? 884  HOH B O   1 
HETATM 10609 O  O   . HOH U 7 .   ? 5.367   35.949  29.025  1.00 22.90  ? 885  HOH B O   1 
HETATM 10610 O  O   . HOH U 7 .   ? 0.358   44.802  41.192  1.00 31.76  ? 886  HOH B O   1 
HETATM 10611 O  O   . HOH U 7 .   ? -0.866  62.619  -3.682  1.00 44.74  ? 887  HOH B O   1 
HETATM 10612 O  O   . HOH U 7 .   ? 6.046   63.499  37.529  1.00 53.19  ? 888  HOH B O   1 
HETATM 10613 O  O   . HOH U 7 .   ? -10.855 75.328  4.422   1.00 49.22  ? 889  HOH B O   1 
HETATM 10614 O  O   . HOH U 7 .   ? -2.784  38.730  40.689  1.00 40.24  ? 890  HOH B O   1 
HETATM 10615 O  O   . HOH U 7 .   ? -4.598  34.628  32.884  1.00 42.19  ? 891  HOH B O   1 
HETATM 10616 O  O   . HOH U 7 .   ? -10.520 74.082  40.788  1.00 24.14  ? 892  HOH B O   1 
HETATM 10617 O  O   . HOH U 7 .   ? 2.163   47.182  44.394  1.00 59.45  ? 893  HOH B O   1 
HETATM 10618 O  O   . HOH U 7 .   ? 18.839  31.955  20.910  1.00 55.92  ? 894  HOH B O   1 
HETATM 10619 O  O   . HOH U 7 .   ? 9.791   91.695  1.664   1.00 27.71  ? 895  HOH B O   1 
HETATM 10620 O  O   . HOH U 7 .   ? -2.364  44.708  41.742  1.00 32.50  ? 896  HOH B O   1 
HETATM 10621 O  O   . HOH U 7 .   ? 18.268  46.101  41.382  1.00 41.13  ? 897  HOH B O   1 
HETATM 10622 O  O   . HOH U 7 .   ? -25.236 59.704  51.505  1.00 51.42  ? 898  HOH B O   1 
HETATM 10623 O  O   . HOH U 7 .   ? 5.331   48.462  15.982  1.00 45.50  ? 899  HOH B O   1 
HETATM 10624 O  O   . HOH U 7 .   ? -20.802 70.041  49.036  1.00 51.96  ? 900  HOH B O   1 
HETATM 10625 O  O   . HOH U 7 .   ? -6.083  38.324  41.699  1.00 50.05  ? 901  HOH B O   1 
HETATM 10626 O  O   . HOH U 7 .   ? -29.875 43.968  47.174  1.00 58.02  ? 902  HOH B O   1 
HETATM 10627 O  O   . HOH U 7 .   ? -7.631  61.406  46.277  1.00 20.79  ? 903  HOH B O   1 
HETATM 10628 O  O   . HOH U 7 .   ? -10.321 58.033  21.062  1.00 23.74  ? 904  HOH B O   1 
HETATM 10629 O  O   . HOH U 7 .   ? -14.425 81.261  30.533  1.00 58.74  ? 905  HOH B O   1 
HETATM 10630 O  O   . HOH U 7 .   ? -12.473 76.541  25.964  1.00 26.54  ? 906  HOH B O   1 
HETATM 10631 O  O   . HOH U 7 .   ? -11.681 74.821  22.821  1.00 30.78  ? 907  HOH B O   1 
HETATM 10632 O  O   . HOH U 7 .   ? 11.855  58.006  27.502  1.00 54.63  ? 908  HOH B O   1 
HETATM 10633 O  O   . HOH U 7 .   ? -1.530  42.813  39.341  1.00 24.86  ? 909  HOH B O   1 
HETATM 10634 O  O   . HOH U 7 .   ? -13.633 52.942  16.193  1.00 61.45  ? 910  HOH B O   1 
HETATM 10635 O  O   . HOH U 7 .   ? -12.575 85.254  2.409   1.00 25.43  ? 911  HOH B O   1 
HETATM 10636 O  O   . HOH U 7 .   ? 6.983   36.094  20.689  1.00 31.77  ? 912  HOH B O   1 
HETATM 10637 O  O   . HOH U 7 .   ? -5.184  47.577  21.744  1.00 41.35  ? 913  HOH B O   1 
HETATM 10638 O  O   . HOH U 7 .   ? 19.667  29.495  47.543  1.00 49.00  ? 914  HOH B O   1 
HETATM 10639 O  O   . HOH U 7 .   ? -9.301  72.319  34.208  1.00 28.91  ? 915  HOH B O   1 
HETATM 10640 O  O   . HOH U 7 .   ? 8.593   55.853  20.452  1.00 25.81  ? 916  HOH B O   1 
HETATM 10641 O  O   . HOH U 7 .   ? 5.640   78.954  12.827  1.00 48.27  ? 917  HOH B O   1 
HETATM 10642 O  O   . HOH U 7 .   ? -5.830  80.952  -4.153  1.00 44.89  ? 918  HOH B O   1 
HETATM 10643 O  O   . HOH U 7 .   ? -8.906  59.302  23.116  1.00 23.15  ? 919  HOH B O   1 
HETATM 10644 O  O   . HOH U 7 .   ? 0.413   52.928  41.066  1.00 37.42  ? 920  HOH B O   1 
HETATM 10645 O  O   . HOH U 7 .   ? 3.657   54.731  40.161  1.00 35.54  ? 921  HOH B O   1 
HETATM 10646 O  O   . HOH U 7 .   ? 1.916   42.381  25.327  1.00 28.43  ? 922  HOH B O   1 
HETATM 10647 O  O   . HOH U 7 .   ? 16.147  33.819  27.584  1.00 35.87  ? 923  HOH B O   1 
HETATM 10648 O  O   . HOH U 7 .   ? 13.332  27.894  45.744  1.00 52.67  ? 924  HOH B O   1 
HETATM 10649 O  O   . HOH U 7 .   ? -0.907  101.059 -6.191  1.00 51.51  ? 925  HOH B O   1 
HETATM 10650 O  O   . HOH U 7 .   ? 0.142   57.111  57.896  1.00 50.40  ? 926  HOH B O   1 
HETATM 10651 O  O   . HOH U 7 .   ? -15.134 53.088  54.503  1.00 46.50  ? 927  HOH B O   1 
HETATM 10652 O  O   . HOH U 7 .   ? -5.214  96.309  -0.461  1.00 19.22  ? 928  HOH B O   1 
HETATM 10653 O  O   . HOH U 7 .   ? 3.162   22.808  35.943  1.00 55.63  ? 929  HOH B O   1 
HETATM 10654 O  O   . HOH U 7 .   ? -0.928  70.297  57.955  1.00 38.73  ? 930  HOH B O   1 
HETATM 10655 O  O   . HOH U 7 .   ? 4.937   50.709  22.708  1.00 20.90  ? 931  HOH B O   1 
HETATM 10656 O  O   . HOH U 7 .   ? -20.743 84.452  15.270  1.00 28.07  ? 932  HOH B O   1 
HETATM 10657 O  O   . HOH U 7 .   ? -14.461 36.430  32.962  1.00 30.59  ? 933  HOH B O   1 
HETATM 10658 O  O   . HOH U 7 .   ? 21.923  45.749  22.992  1.00 36.71  ? 934  HOH B O   1 
HETATM 10659 O  O   . HOH U 7 .   ? 7.587   31.000  25.270  1.00 34.55  ? 935  HOH B O   1 
HETATM 10660 O  O   . HOH U 7 .   ? 9.820   41.336  29.032  1.00 19.31  ? 936  HOH B O   1 
HETATM 10661 O  O   . HOH U 7 .   ? -3.264  81.780  27.830  1.00 40.18  ? 937  HOH B O   1 
HETATM 10662 O  O   . HOH U 7 .   ? 19.833  42.275  48.082  1.00 37.95  ? 938  HOH B O   1 
HETATM 10663 O  O   . HOH U 7 .   ? -16.093 75.939  36.137  1.00 49.05  ? 939  HOH B O   1 
HETATM 10664 O  O   . HOH U 7 .   ? 5.758   78.623  41.112  1.00 59.47  ? 940  HOH B O   1 
HETATM 10665 O  O   . HOH U 7 .   ? -1.259  72.019  19.774  1.00 24.49  ? 941  HOH B O   1 
HETATM 10666 O  O   . HOH U 7 .   ? 1.418   35.460  45.217  1.00 36.67  ? 942  HOH B O   1 
HETATM 10667 O  O   . HOH U 7 .   ? -10.769 96.761  -5.042  1.00 61.95  ? 943  HOH B O   1 
HETATM 10668 O  O   . HOH U 7 .   ? -19.045 37.999  47.746  1.00 40.67  ? 944  HOH B O   1 
HETATM 10669 O  O   . HOH U 7 .   ? 15.661  46.889  51.852  1.00 80.58  ? 945  HOH B O   1 
HETATM 10670 O  O   . HOH U 7 .   ? 13.574  35.274  49.184  1.00 29.15  ? 946  HOH B O   1 
HETATM 10671 O  O   . HOH U 7 .   ? -12.316 66.097  60.354  1.00 57.71  ? 947  HOH B O   1 
HETATM 10672 O  O   . HOH U 7 .   ? 4.615   69.380  17.580  1.00 25.35  ? 948  HOH B O   1 
HETATM 10673 O  O   . HOH U 7 .   ? -21.734 47.582  25.092  1.00 54.50  ? 949  HOH B O   1 
HETATM 10674 O  O   . HOH U 7 .   ? 20.865  39.687  13.791  1.00 45.68  ? 950  HOH B O   1 
HETATM 10675 O  O   . HOH U 7 .   ? -4.013  98.329  34.457  1.00 52.24  ? 951  HOH B O   1 
HETATM 10676 O  O   . HOH U 7 .   ? -8.481  101.007 -3.059  1.00 32.16  ? 952  HOH B O   1 
HETATM 10677 O  O   . HOH U 7 .   ? -16.862 71.542  37.322  1.00 24.48  ? 953  HOH B O   1 
HETATM 10678 O  O   . HOH U 7 .   ? 8.861   95.121  15.939  1.00 24.02  ? 954  HOH B O   1 
HETATM 10679 O  O   . HOH U 7 .   ? 10.424  59.751  25.372  1.00 25.19  ? 955  HOH B O   1 
HETATM 10680 O  O   . HOH U 7 .   ? 11.248  49.932  18.889  1.00 20.85  ? 956  HOH B O   1 
HETATM 10681 O  O   . HOH U 7 .   ? -15.726 57.269  25.608  1.00 42.78  ? 957  HOH B O   1 
HETATM 10682 O  O   . HOH U 7 .   ? 2.931   90.471  30.121  1.00 37.05  ? 958  HOH B O   1 
HETATM 10683 O  O   . HOH U 7 .   ? -8.831  57.367  16.185  1.00 31.10  ? 959  HOH B O   1 
HETATM 10684 O  O   . HOH U 7 .   ? 11.285  36.068  52.202  1.00 35.83  ? 960  HOH B O   1 
HETATM 10685 O  O   . HOH U 7 .   ? -9.490  54.488  16.109  1.00 56.99  ? 961  HOH B O   1 
HETATM 10686 O  O   . HOH U 7 .   ? -19.159 36.850  33.389  1.00 39.17  ? 962  HOH B O   1 
HETATM 10687 O  O   . HOH U 7 .   ? 0.474   91.344  32.959  1.00 50.27  ? 963  HOH B O   1 
HETATM 10688 O  O   . HOH U 7 .   ? -25.228 52.788  31.672  1.00 47.19  ? 964  HOH B O   1 
HETATM 10689 O  O   . HOH U 7 .   ? -20.891 89.577  21.805  1.00 26.49  ? 965  HOH B O   1 
HETATM 10690 O  O   . HOH U 7 .   ? 13.569  85.605  9.908   1.00 22.55  ? 966  HOH B O   1 
HETATM 10691 O  O   . HOH U 7 .   ? -2.317  63.972  11.813  1.00 38.59  ? 967  HOH B O   1 
HETATM 10692 O  O   . HOH U 7 .   ? 17.960  51.562  27.044  1.00 43.76  ? 968  HOH B O   1 
HETATM 10693 O  O   . HOH U 7 .   ? 2.444   90.480  13.305  1.00 19.06  ? 969  HOH B O   1 
HETATM 10694 O  O   . HOH U 7 .   ? 10.037  73.369  20.080  1.00 63.38  ? 970  HOH B O   1 
HETATM 10695 O  O   . HOH U 7 .   ? -9.747  49.901  34.578  1.00 20.84  ? 971  HOH B O   1 
HETATM 10696 O  O   . HOH U 7 .   ? -12.292 56.847  55.056  1.00 30.18  ? 972  HOH B O   1 
HETATM 10697 O  O   . HOH U 7 .   ? 19.217  43.150  15.948  1.00 44.09  ? 973  HOH B O   1 
HETATM 10698 O  O   . HOH U 7 .   ? -14.194 79.146  1.625   1.00 56.52  ? 974  HOH B O   1 
HETATM 10699 O  O   . HOH U 7 .   ? -23.490 39.061  39.193  1.00 61.15  ? 975  HOH B O   1 
HETATM 10700 O  O   . HOH U 7 .   ? -22.479 87.864  9.804   1.00 39.54  ? 976  HOH B O   1 
HETATM 10701 O  O   . HOH U 7 .   ? -11.774 62.160  29.835  1.00 23.88  ? 977  HOH B O   1 
HETATM 10702 O  O   . HOH U 7 .   ? -12.384 72.472  14.394  1.00 42.16  ? 978  HOH B O   1 
HETATM 10703 O  O   . HOH U 7 .   ? 12.894  53.608  20.345  1.00 33.39  ? 979  HOH B O   1 
HETATM 10704 O  O   . HOH U 7 .   ? 2.512   41.627  18.341  1.00 35.07  ? 980  HOH B O   1 
HETATM 10705 O  O   . HOH U 7 .   ? -17.986 91.627  2.618   1.00 30.52  ? 981  HOH B O   1 
HETATM 10706 O  O   . HOH U 7 .   ? -1.156  79.738  31.479  1.00 52.75  ? 982  HOH B O   1 
HETATM 10707 O  O   . HOH U 7 .   ? -9.451  83.519  0.698   1.00 36.73  ? 983  HOH B O   1 
HETATM 10708 O  O   . HOH U 7 .   ? 20.564  43.327  12.029  1.00 30.20  ? 984  HOH B O   1 
HETATM 10709 O  O   . HOH U 7 .   ? -9.187  60.645  40.229  1.00 36.10  ? 985  HOH B O   1 
HETATM 10710 O  O   . HOH U 7 .   ? -5.513  45.973  27.260  1.00 25.56  ? 986  HOH B O   1 
HETATM 10711 O  O   . HOH U 7 .   ? -22.324 61.457  48.182  1.00 61.31  ? 987  HOH B O   1 
HETATM 10712 O  O   . HOH U 7 .   ? 0.136   69.357  26.985  1.00 22.23  ? 988  HOH B O   1 
HETATM 10713 O  O   . HOH U 7 .   ? 17.650  43.155  9.800   1.00 22.10  ? 989  HOH B O   1 
HETATM 10714 O  O   . HOH U 7 .   ? 6.934   66.161  39.238  1.00 35.51  ? 990  HOH B O   1 
HETATM 10715 O  O   . HOH U 7 .   ? -2.879  64.850  33.497  1.00 24.93  ? 991  HOH B O   1 
HETATM 10716 O  O   . HOH U 7 .   ? 12.629  84.176  13.182  1.00 31.11  ? 992  HOH B O   1 
HETATM 10717 O  O   . HOH U 7 .   ? 2.351   48.785  40.499  1.00 51.24  ? 993  HOH B O   1 
HETATM 10718 O  O   . HOH U 7 .   ? -15.263 42.071  30.278  1.00 27.78  ? 994  HOH B O   1 
HETATM 10719 O  O   . HOH U 7 .   ? 4.604   51.446  38.751  1.00 22.32  ? 995  HOH B O   1 
HETATM 10720 O  O   . HOH U 7 .   ? -6.445  66.993  12.973  1.00 63.73  ? 996  HOH B O   1 
HETATM 10721 O  O   . HOH U 7 .   ? 1.485   42.050  39.678  1.00 23.76  ? 997  HOH B O   1 
HETATM 10722 O  O   . HOH U 7 .   ? -3.749  31.071  45.892  1.00 60.70  ? 998  HOH B O   1 
HETATM 10723 O  O   . HOH U 7 .   ? 0.224   76.180  27.185  1.00 35.72  ? 999  HOH B O   1 
HETATM 10724 O  O   . HOH U 7 .   ? -12.942 40.711  30.840  1.00 26.64  ? 1000 HOH B O   1 
HETATM 10725 O  O   . HOH U 7 .   ? 5.049   85.322  23.234  1.00 27.44  ? 1001 HOH B O   1 
HETATM 10726 O  O   . HOH U 7 .   ? -16.073 82.745  3.924   1.00 45.91  ? 1002 HOH B O   1 
HETATM 10727 O  O   . HOH U 7 .   ? 6.163   31.930  27.950  1.00 33.37  ? 1003 HOH B O   1 
HETATM 10728 O  O   . HOH U 7 .   ? 10.026  30.365  53.569  1.00 34.96  ? 1004 HOH B O   1 
HETATM 10729 O  O   . HOH U 7 .   ? 7.831   45.069  31.447  1.00 19.95  ? 1005 HOH B O   1 
HETATM 10730 O  O   . HOH U 7 .   ? -28.945 50.692  37.457  1.00 41.36  ? 1006 HOH B O   1 
HETATM 10731 O  O   . HOH U 7 .   ? -4.537  63.311  34.963  1.00 24.89  ? 1007 HOH B O   1 
HETATM 10732 O  O   . HOH U 7 .   ? 10.389  52.881  34.164  1.00 40.84  ? 1008 HOH B O   1 
HETATM 10733 O  O   . HOH U 7 .   ? -8.621  69.672  13.423  1.00 54.87  ? 1009 HOH B O   1 
HETATM 10734 O  O   . HOH U 7 .   ? 4.081   58.938  52.396  1.00 45.87  ? 1010 HOH B O   1 
HETATM 10735 O  O   . HOH U 7 .   ? -16.201 48.627  33.657  1.00 22.04  ? 1011 HOH B O   1 
HETATM 10736 O  O   . HOH U 7 .   ? 2.566   78.035  52.838  1.00 50.79  ? 1012 HOH B O   1 
HETATM 10737 O  O   . HOH U 7 .   ? -18.971 74.881  46.472  1.00 49.15  ? 1013 HOH B O   1 
HETATM 10738 O  O   . HOH U 7 .   ? -14.094 69.201  25.167  1.00 30.93  ? 1014 HOH B O   1 
HETATM 10739 O  O   . HOH U 7 .   ? -4.277  102.494 -3.424  1.00 35.32  ? 1015 HOH B O   1 
HETATM 10740 O  O   . HOH U 7 .   ? -12.257 103.214 6.648   1.00 45.78  ? 1016 HOH B O   1 
HETATM 10741 O  O   . HOH U 7 .   ? -6.944  42.774  48.976  1.00 43.91  ? 1017 HOH B O   1 
HETATM 10742 O  O   . HOH U 7 .   ? -25.540 38.650  46.093  1.00 46.98  ? 1018 HOH B O   1 
HETATM 10743 O  O   . HOH U 7 .   ? 11.291  93.781  -1.073  1.00 59.86  ? 1019 HOH B O   1 
HETATM 10744 O  O   . HOH U 7 .   ? -1.777  44.230  26.693  1.00 44.71  ? 1020 HOH B O   1 
HETATM 10745 O  O   . HOH U 7 .   ? 2.604   42.207  35.844  1.00 22.33  ? 1021 HOH B O   1 
HETATM 10746 O  O   . HOH U 7 .   ? -3.752  89.764  32.503  1.00 42.58  ? 1022 HOH B O   1 
HETATM 10747 O  O   . HOH U 7 .   ? 8.838   87.872  16.579  1.00 20.53  ? 1023 HOH B O   1 
HETATM 10748 O  O   . HOH U 7 .   ? 1.173   48.072  32.508  1.00 22.71  ? 1024 HOH B O   1 
HETATM 10749 O  O   . HOH U 7 .   ? -24.965 60.211  45.311  1.00 46.81  ? 1025 HOH B O   1 
HETATM 10750 O  O   . HOH U 7 .   ? 9.845   45.765  17.496  1.00 30.57  ? 1026 HOH B O   1 
HETATM 10751 O  O   . HOH U 7 .   ? -14.986 97.741  -3.198  1.00 44.26  ? 1027 HOH B O   1 
HETATM 10752 O  O   . HOH U 7 .   ? -0.547  78.173  35.869  1.00 38.32  ? 1028 HOH B O   1 
HETATM 10753 O  O   . HOH U 7 .   ? 1.679   55.956  15.440  1.00 29.02  ? 1029 HOH B O   1 
HETATM 10754 O  O   . HOH U 7 .   ? -12.352 46.483  22.563  1.00 34.15  ? 1030 HOH B O   1 
HETATM 10755 O  O   . HOH U 7 .   ? -20.312 94.269  5.635   1.00 31.70  ? 1031 HOH B O   1 
HETATM 10756 O  O   . HOH U 7 .   ? -21.752 58.858  54.402  1.00 47.88  ? 1032 HOH B O   1 
HETATM 10757 O  O   . HOH U 7 .   ? -17.363 73.096  45.188  1.00 27.47  ? 1033 HOH B O   1 
HETATM 10758 O  O   . HOH U 7 .   ? 6.620   67.457  45.427  1.00 74.31  ? 1034 HOH B O   1 
HETATM 10759 O  O   . HOH U 7 .   ? -20.492 60.644  34.150  1.00 37.63  ? 1035 HOH B O   1 
HETATM 10760 O  O   . HOH U 7 .   ? -15.000 54.992  26.546  1.00 26.07  ? 1036 HOH B O   1 
HETATM 10761 O  O   . HOH U 7 .   ? -13.586 76.069  56.581  1.00 58.08  ? 1037 HOH B O   1 
HETATM 10762 O  O   . HOH U 7 .   ? -0.577  27.898  36.199  1.00 43.09  ? 1038 HOH B O   1 
HETATM 10763 O  O   . HOH U 7 .   ? -1.848  64.823  36.352  1.00 22.64  ? 1039 HOH B O   1 
HETATM 10764 O  O   . HOH U 7 .   ? -6.513  36.692  37.660  1.00 33.01  ? 1040 HOH B O   1 
HETATM 10765 O  O   . HOH U 7 .   ? -3.821  79.515  -5.634  1.00 64.59  ? 1041 HOH B O   1 
HETATM 10766 O  O   . HOH U 7 .   ? 10.546  71.066  31.576  1.00 50.25  ? 1042 HOH B O   1 
HETATM 10767 O  O   . HOH U 7 .   ? -19.298 77.965  7.171   1.00 51.30  ? 1043 HOH B O   1 
HETATM 10768 O  O   . HOH U 7 .   ? -13.142 45.732  50.415  1.00 36.23  ? 1044 HOH B O   1 
HETATM 10769 O  O   . HOH U 7 .   ? -17.227 70.067  56.811  1.00 56.66  ? 1045 HOH B O   1 
HETATM 10770 O  O   . HOH U 7 .   ? 16.662  55.107  29.889  1.00 55.25  ? 1046 HOH B O   1 
HETATM 10771 O  O   . HOH U 7 .   ? 1.515   45.424  33.743  1.00 23.71  ? 1047 HOH B O   1 
HETATM 10772 O  O   . HOH U 7 .   ? -6.092  83.912  29.045  1.00 31.82  ? 1048 HOH B O   1 
HETATM 10773 O  O   . HOH U 7 .   ? -1.671  91.252  -2.060  1.00 51.06  ? 1049 HOH B O   1 
HETATM 10774 O  O   . HOH U 7 .   ? -18.737 38.281  29.035  1.00 46.45  ? 1050 HOH B O   1 
HETATM 10775 O  O   . HOH U 7 .   ? -11.219 79.980  23.786  1.00 22.54  ? 1051 HOH B O   1 
HETATM 10776 O  O   . HOH U 7 .   ? 4.946   90.699  14.618  1.00 17.16  ? 1052 HOH B O   1 
HETATM 10777 O  O   . HOH U 7 .   ? -8.216  51.642  36.039  1.00 21.19  ? 1053 HOH B O   1 
HETATM 10778 O  O   . HOH U 7 .   ? -13.003 94.782  -2.761  1.00 47.28  ? 1054 HOH B O   1 
HETATM 10779 O  O   . HOH U 7 .   ? 5.088   41.610  42.979  1.00 27.77  ? 1055 HOH B O   1 
HETATM 10780 O  O   . HOH U 7 .   ? 6.123   76.559  46.664  1.00 51.29  ? 1056 HOH B O   1 
HETATM 10781 O  O   . HOH U 7 .   ? 7.049   31.218  46.901  1.00 29.30  ? 1057 HOH B O   1 
HETATM 10782 O  O   . HOH U 7 .   ? -2.652  46.897  20.130  1.00 54.02  ? 1058 HOH B O   1 
HETATM 10783 O  O   . HOH U 7 .   ? -15.184 77.501  22.881  1.00 30.47  ? 1059 HOH B O   1 
HETATM 10784 O  O   . HOH U 7 .   ? -16.458 46.719  23.339  1.00 36.21  ? 1060 HOH B O   1 
HETATM 10785 O  O   . HOH U 7 .   ? -5.230  36.728  35.194  1.00 31.36  ? 1061 HOH B O   1 
HETATM 10786 O  O   . HOH U 7 .   ? 12.026  47.434  18.169  1.00 21.38  ? 1062 HOH B O   1 
HETATM 10787 O  O   . HOH U 7 .   ? 10.920  41.891  14.696  1.00 25.39  ? 1063 HOH B O   1 
HETATM 10788 O  O   . HOH U 7 .   ? 9.668   69.907  28.169  1.00 42.81  ? 1064 HOH B O   1 
HETATM 10789 O  O   . HOH U 7 .   ? 1.369   75.008  29.202  1.00 33.08  ? 1065 HOH B O   1 
HETATM 10790 O  O   . HOH U 7 .   ? -4.671  71.574  16.192  1.00 43.93  ? 1066 HOH B O   1 
HETATM 10791 O  O   . HOH U 7 .   ? 5.724   79.556  24.621  1.00 47.23  ? 1067 HOH B O   1 
HETATM 10792 O  O   . HOH U 7 .   ? 0.563   51.049  42.734  1.00 49.88  ? 1068 HOH B O   1 
HETATM 10793 O  O   . HOH U 7 .   ? 10.017  90.407  7.398   1.00 22.87  ? 1069 HOH B O   1 
HETATM 10794 O  O   . HOH U 7 .   ? 22.221  32.455  49.347  1.00 52.61  ? 1070 HOH B O   1 
HETATM 10795 O  O   . HOH U 7 .   ? 2.209   73.204  25.899  1.00 22.79  ? 1071 HOH B O   1 
HETATM 10796 O  O   . HOH U 7 .   ? 5.594   100.704 12.513  1.00 51.20  ? 1072 HOH B O   1 
HETATM 10797 O  O   . HOH U 7 .   ? 10.125  81.657  13.229  1.00 40.56  ? 1073 HOH B O   1 
HETATM 10798 O  O   . HOH U 7 .   ? -19.742 61.572  46.701  1.00 48.43  ? 1074 HOH B O   1 
HETATM 10799 O  O   . HOH U 7 .   ? -9.475  79.356  25.791  1.00 24.85  ? 1075 HOH B O   1 
HETATM 10800 O  O   . HOH U 7 .   ? -17.566 77.292  45.757  1.00 52.85  ? 1076 HOH B O   1 
HETATM 10801 O  O   . HOH U 7 .   ? -12.809 94.591  34.014  1.00 52.05  ? 1077 HOH B O   1 
HETATM 10802 O  O   . HOH U 7 .   ? 6.963   39.610  54.326  1.00 32.86  ? 1078 HOH B O   1 
HETATM 10803 O  O   . HOH U 7 .   ? -21.849 90.957  13.217  1.00 28.78  ? 1079 HOH B O   1 
HETATM 10804 O  O   . HOH U 7 .   ? -21.100 55.677  52.571  1.00 48.17  ? 1080 HOH B O   1 
HETATM 10805 O  O   . HOH U 7 .   ? 3.732   36.202  46.088  1.00 36.40  ? 1081 HOH B O   1 
HETATM 10806 O  O   . HOH U 7 .   ? 4.178   48.713  38.279  1.00 26.54  ? 1082 HOH B O   1 
HETATM 10807 O  O   . HOH U 7 .   ? -13.041 93.421  31.364  1.00 47.38  ? 1083 HOH B O   1 
HETATM 10808 O  O   . HOH U 7 .   ? -0.132  45.462  22.888  1.00 36.09  ? 1084 HOH B O   1 
HETATM 10809 O  O   . HOH U 7 .   ? -28.710 49.566  33.783  1.00 56.53  ? 1085 HOH B O   1 
HETATM 10810 O  O   . HOH U 7 .   ? 5.348   89.913  31.505  1.00 63.80  ? 1086 HOH B O   1 
HETATM 10811 O  O   . HOH U 7 .   ? -14.482 71.751  21.516  1.00 32.98  ? 1087 HOH B O   1 
HETATM 10812 O  O   . HOH U 7 .   ? 0.325   43.696  36.752  1.00 25.54  ? 1088 HOH B O   1 
HETATM 10813 O  O   . HOH U 7 .   ? -1.361  76.236  14.224  1.00 26.42  ? 1089 HOH B O   1 
HETATM 10814 O  O   . HOH U 7 .   ? 21.512  45.034  28.776  1.00 36.96  ? 1090 HOH B O   1 
HETATM 10815 O  O   . HOH U 7 .   ? 14.424  44.543  24.037  1.00 23.06  ? 1091 HOH B O   1 
HETATM 10816 O  O   . HOH U 7 .   ? -11.674 87.848  35.867  1.00 39.92  ? 1092 HOH B O   1 
HETATM 10817 O  O   . HOH U 7 .   ? -14.821 83.597  26.745  1.00 51.71  ? 1093 HOH B O   1 
HETATM 10818 O  O   . HOH U 7 .   ? 19.802  35.453  18.882  1.00 55.49  ? 1094 HOH B O   1 
HETATM 10819 O  O   . HOH U 7 .   ? 9.836   37.669  47.846  1.00 22.90  ? 1095 HOH B O   1 
HETATM 10820 O  O   . HOH U 7 .   ? 6.035   41.859  52.528  1.00 52.53  ? 1096 HOH B O   1 
HETATM 10821 O  O   . HOH U 7 .   ? 13.499  52.493  38.865  1.00 52.91  ? 1097 HOH B O   1 
HETATM 10822 O  O   . HOH U 7 .   ? -8.658  48.461  23.077  1.00 26.42  ? 1098 HOH B O   1 
HETATM 10823 O  O   . HOH U 7 .   ? 8.753   34.100  20.373  1.00 28.07  ? 1099 HOH B O   1 
HETATM 10824 O  O   . HOH U 7 .   ? 22.412  35.070  47.031  1.00 30.34  ? 1100 HOH B O   1 
HETATM 10825 O  O   . HOH U 7 .   ? 22.467  28.807  47.582  1.00 40.98  ? 1101 HOH B O   1 
HETATM 10826 O  O   . HOH U 7 .   ? 9.228   91.907  -3.616  1.00 59.81  ? 1102 HOH B O   1 
HETATM 10827 O  O   . HOH U 7 .   ? -8.346  35.002  35.349  1.00 38.16  ? 1103 HOH B O   1 
HETATM 10828 O  O   . HOH U 7 .   ? 22.604  37.183  44.412  1.00 33.46  ? 1104 HOH B O   1 
HETATM 10829 O  O   . HOH U 7 .   ? 18.036  35.051  28.870  1.00 50.23  ? 1105 HOH B O   1 
HETATM 10830 O  O   . HOH U 7 .   ? 12.062  27.189  30.901  1.00 52.67  ? 1106 HOH B O   1 
HETATM 10831 O  O   . HOH U 7 .   ? 11.921  60.288  15.523  1.00 55.40  ? 1107 HOH B O   1 
HETATM 10832 O  O   . HOH U 7 .   ? -9.939  91.161  0.717   1.00 25.73  ? 1108 HOH B O   1 
HETATM 10833 O  O   . HOH U 7 .   ? -19.296 58.120  26.536  1.00 52.26  ? 1109 HOH B O   1 
HETATM 10834 O  O   . HOH U 7 .   ? 15.873  31.703  57.096  1.00 40.01  ? 1110 HOH B O   1 
HETATM 10835 O  O   . HOH U 7 .   ? 7.891   70.817  31.226  1.00 32.33  ? 1111 HOH B O   1 
HETATM 10836 O  O   . HOH U 7 .   ? -15.137 71.432  16.581  1.00 47.93  ? 1112 HOH B O   1 
HETATM 10837 O  O   . HOH U 7 .   ? 1.213   52.345  50.631  1.00 39.06  ? 1113 HOH B O   1 
HETATM 10838 O  O   . HOH U 7 .   ? -12.266 77.571  2.795   1.00 52.97  ? 1114 HOH B O   1 
HETATM 10839 O  O   . HOH U 7 .   ? 14.342  54.815  28.124  1.00 66.93  ? 1115 HOH B O   1 
HETATM 10840 O  O   . HOH U 7 .   ? -12.934 87.046  0.305   1.00 34.64  ? 1116 HOH B O   1 
HETATM 10841 O  O   . HOH U 7 .   ? 10.131  60.889  32.285  1.00 37.08  ? 1117 HOH B O   1 
HETATM 10842 O  O   . HOH U 7 .   ? -21.528 66.348  45.723  1.00 27.24  ? 1118 HOH B O   1 
HETATM 10843 O  O   . HOH U 7 .   ? 18.382  44.974  33.350  1.00 37.49  ? 1119 HOH B O   1 
HETATM 10844 O  O   . HOH U 7 .   ? -2.976  42.501  43.447  1.00 33.13  ? 1120 HOH B O   1 
HETATM 10845 O  O   . HOH U 7 .   ? -17.789 49.663  54.052  1.00 43.44  ? 1121 HOH B O   1 
HETATM 10846 O  O   . HOH U 7 .   ? -8.666  75.938  35.598  1.00 57.42  ? 1122 HOH B O   1 
HETATM 10847 O  O   . HOH U 7 .   ? -19.916 86.576  23.727  1.00 37.00  ? 1123 HOH B O   1 
HETATM 10848 O  O   . HOH U 7 .   ? -6.921  57.644  58.603  1.00 41.54  ? 1124 HOH B O   1 
HETATM 10849 O  O   . HOH U 7 .   ? -20.741 96.447  8.966   1.00 20.81  ? 1125 HOH B O   1 
HETATM 10850 O  O   . HOH U 7 .   ? -20.841 90.089  8.108   1.00 25.85  ? 1126 HOH B O   1 
HETATM 10851 O  O   . HOH U 7 .   ? 6.174   104.847 0.730   1.00 27.31  ? 1127 HOH B O   1 
HETATM 10852 O  O   . HOH U 7 .   ? -12.997 78.547  31.535  1.00 58.35  ? 1128 HOH B O   1 
HETATM 10853 O  O   . HOH U 7 .   ? 12.472  81.588  16.317  1.00 41.29  ? 1129 HOH B O   1 
HETATM 10854 O  O   . HOH U 7 .   ? -13.708 45.457  26.879  1.00 25.80  ? 1130 HOH B O   1 
HETATM 10855 O  O   . HOH U 7 .   ? -16.882 72.217  32.876  1.00 51.48  ? 1131 HOH B O   1 
HETATM 10856 O  O   . HOH U 7 .   ? 7.869   57.155  33.736  1.00 34.87  ? 1132 HOH B O   1 
HETATM 10857 O  O   . HOH U 7 .   ? -20.516 82.497  20.724  1.00 38.60  ? 1133 HOH B O   1 
HETATM 10858 O  O   . HOH U 7 .   ? 2.062   77.622  14.901  1.00 65.96  ? 1134 HOH B O   1 
HETATM 10859 O  O   . HOH U 7 .   ? 7.149   86.257  2.474   1.00 43.38  ? 1135 HOH B O   1 
HETATM 10860 O  O   . HOH U 7 .   ? 4.202   33.417  26.961  1.00 32.58  ? 1136 HOH B O   1 
HETATM 10861 O  O   . HOH U 7 .   ? -1.285  41.089  41.258  1.00 24.89  ? 1137 HOH B O   1 
HETATM 10862 O  O   . HOH U 7 .   ? 0.355   70.190  18.469  1.00 37.56  ? 1138 HOH B O   1 
HETATM 10863 O  O   . HOH U 7 .   ? 8.773   40.738  13.035  1.00 35.22  ? 1139 HOH B O   1 
HETATM 10864 O  O   . HOH U 7 .   ? 5.105   39.105  17.291  1.00 30.70  ? 1140 HOH B O   1 
HETATM 10865 O  O   . HOH U 7 .   ? -3.847  49.391  19.550  1.00 31.70  ? 1141 HOH B O   1 
HETATM 10866 O  O   . HOH U 7 .   ? -18.752 42.277  52.017  1.00 40.95  ? 1142 HOH B O   1 
HETATM 10867 O  O   . HOH U 7 .   ? 2.958   76.148  40.223  1.00 57.47  ? 1143 HOH B O   1 
HETATM 10868 O  O   . HOH U 7 .   ? -21.615 66.667  38.648  1.00 44.23  ? 1144 HOH B O   1 
HETATM 10869 O  O   . HOH U 7 .   ? 1.628   43.069  43.013  1.00 49.23  ? 1145 HOH B O   1 
HETATM 10870 O  O   . HOH U 7 .   ? -5.719  100.245 19.789  1.00 34.19  ? 1146 HOH B O   1 
HETATM 10871 O  O   . HOH U 7 .   ? 4.372   67.471  43.226  1.00 37.79  ? 1147 HOH B O   1 
HETATM 10872 O  O   . HOH U 7 .   ? 11.412  59.440  19.980  1.00 39.30  ? 1148 HOH B O   1 
HETATM 10873 O  O   . HOH U 7 .   ? -10.356 76.749  37.189  1.00 57.76  ? 1149 HOH B O   1 
HETATM 10874 O  O   . HOH U 7 .   ? 9.105   23.696  31.528  1.00 45.14  ? 1150 HOH B O   1 
HETATM 10875 O  O   . HOH U 7 .   ? 5.088   78.393  17.504  1.00 30.48  ? 1151 HOH B O   1 
HETATM 10876 O  O   . HOH U 7 .   ? 11.212  87.346  27.119  1.00 60.14  ? 1152 HOH B O   1 
HETATM 10877 O  O   . HOH U 7 .   ? -20.902 85.412  7.053   1.00 55.11  ? 1153 HOH B O   1 
HETATM 10878 O  O   . HOH U 7 .   ? -3.456  105.311 11.541  1.00 55.36  ? 1154 HOH B O   1 
HETATM 10879 O  O   . HOH U 7 .   ? -13.782 72.123  35.543  1.00 40.12  ? 1155 HOH B O   1 
HETATM 10880 O  O   . HOH U 7 .   ? -20.712 70.235  39.100  1.00 34.90  ? 1156 HOH B O   1 
HETATM 10881 O  O   . HOH U 7 .   ? -7.654  73.844  13.391  1.00 21.04  ? 1157 HOH B O   1 
HETATM 10882 O  O   . HOH U 7 .   ? -24.606 49.915  31.227  1.00 49.17  ? 1158 HOH B O   1 
HETATM 10883 O  O   . HOH U 7 .   ? 3.959   88.121  -0.956  1.00 58.27  ? 1159 HOH B O   1 
HETATM 10884 O  O   . HOH U 7 .   ? 7.353   52.698  41.839  1.00 44.71  ? 1160 HOH B O   1 
HETATM 10885 O  O   . HOH U 7 .   ? -16.335 76.248  9.123   1.00 37.49  ? 1161 HOH B O   1 
HETATM 10886 O  O   . HOH U 7 .   ? -13.916 54.505  30.794  1.00 22.64  ? 1162 HOH B O   1 
HETATM 10887 O  O   . HOH U 7 .   ? -7.539  90.042  -0.084  1.00 24.93  ? 1163 HOH B O   1 
HETATM 10888 O  O   . HOH U 7 .   ? -4.804  44.266  23.094  1.00 79.08  ? 1164 HOH B O   1 
HETATM 10889 O  O   . HOH U 7 .   ? -21.775 59.640  46.402  1.00 37.71  ? 1165 HOH B O   1 
HETATM 10890 O  O   . HOH U 7 .   ? -16.429 71.693  19.731  1.00 81.12  ? 1166 HOH B O   1 
HETATM 10891 O  O   . HOH U 7 .   ? -14.679 66.610  21.982  1.00 30.05  ? 1167 HOH B O   1 
HETATM 10892 O  O   . HOH U 7 .   ? -14.239 88.559  31.470  1.00 42.57  ? 1168 HOH B O   1 
HETATM 10893 O  O   . HOH U 7 .   ? -14.943 94.679  30.148  1.00 37.85  ? 1169 HOH B O   1 
HETATM 10894 O  O   . HOH U 7 .   ? 16.471  45.826  45.752  1.00 52.74  ? 1170 HOH B O   1 
HETATM 10895 O  O   . HOH U 7 .   ? -1.404  96.477  -0.793  1.00 25.00  ? 1171 HOH B O   1 
HETATM 10896 O  O   . HOH U 7 .   ? -21.739 44.625  29.243  1.00 35.46  ? 1172 HOH B O   1 
HETATM 10897 O  O   . HOH U 7 .   ? -11.419 56.735  17.852  1.00 42.23  ? 1173 HOH B O   1 
HETATM 10898 O  O   . HOH U 7 .   ? 6.664   59.832  31.843  1.00 31.52  ? 1174 HOH B O   1 
HETATM 10899 O  O   . HOH U 7 .   ? 12.677  51.785  34.835  1.00 48.32  ? 1175 HOH B O   1 
HETATM 10900 O  O   . HOH U 7 .   ? 1.293   41.726  20.711  1.00 41.57  ? 1176 HOH B O   1 
HETATM 10901 O  O   . HOH U 7 .   ? 3.421   105.194 5.559   1.00 40.57  ? 1177 HOH B O   1 
HETATM 10902 O  O   . HOH U 7 .   ? 3.296   71.358  18.779  1.00 28.04  ? 1178 HOH B O   1 
HETATM 10903 O  O   . HOH U 7 .   ? -13.019 34.884  40.024  1.00 50.45  ? 1179 HOH B O   1 
HETATM 10904 O  O   . HOH U 7 .   ? 2.740   44.992  17.131  1.00 52.34  ? 1180 HOH B O   1 
HETATM 10905 O  O   . HOH U 7 .   ? 22.927  41.682  41.478  1.00 58.66  ? 1181 HOH B O   1 
HETATM 10906 O  O   . HOH U 7 .   ? 11.876  90.062  24.249  1.00 49.14  ? 1182 HOH B O   1 
HETATM 10907 O  O   . HOH U 7 .   ? 16.089  38.636  56.683  1.00 48.54  ? 1183 HOH B O   1 
HETATM 10908 O  O   . HOH U 7 .   ? 20.251  36.815  28.029  1.00 50.86  ? 1184 HOH B O   1 
HETATM 10909 O  O   . HOH U 7 .   ? -8.833  84.764  35.304  1.00 37.21  ? 1185 HOH B O   1 
HETATM 10910 O  O   . HOH U 7 .   ? -20.404 75.875  14.489  1.00 52.97  ? 1186 HOH B O   1 
HETATM 10911 O  O   . HOH U 7 .   ? -17.470 95.807  3.508   1.00 23.13  ? 1187 HOH B O   1 
HETATM 10912 O  O   . HOH U 7 .   ? 17.790  45.701  37.583  1.00 33.76  ? 1188 HOH B O   1 
HETATM 10913 O  O   . HOH U 7 .   ? 2.340   66.662  14.724  1.00 36.39  ? 1189 HOH B O   1 
HETATM 10914 O  O   . HOH U 7 .   ? 1.271   89.707  -1.835  1.00 57.25  ? 1190 HOH B O   1 
HETATM 10915 O  O   . HOH U 7 .   ? -14.455 76.092  3.499   1.00 59.39  ? 1191 HOH B O   1 
HETATM 10916 O  O   . HOH U 7 .   ? 16.681  37.963  16.383  1.00 33.75  ? 1192 HOH B O   1 
HETATM 10917 O  O   . HOH U 7 .   ? -29.335 50.871  48.252  1.00 66.71  ? 1193 HOH B O   1 
HETATM 10918 O  O   . HOH U 7 .   ? -19.830 34.811  44.633  1.00 60.88  ? 1194 HOH B O   1 
HETATM 10919 O  O   . HOH U 7 .   ? 12.078  93.396  22.507  1.00 52.82  ? 1195 HOH B O   1 
HETATM 10920 O  O   . HOH U 7 .   ? 3.986   97.214  18.745  1.00 59.83  ? 1196 HOH B O   1 
HETATM 10921 O  O   . HOH U 7 .   ? 8.738   64.354  34.175  1.00 29.16  ? 1197 HOH B O   1 
HETATM 10922 O  O   . HOH U 7 .   ? 4.841   107.523 9.339   1.00 45.25  ? 1198 HOH B O   1 
HETATM 10923 O  O   . HOH U 7 .   ? -0.173  37.020  43.530  1.00 44.29  ? 1199 HOH B O   1 
HETATM 10924 O  O   . HOH U 7 .   ? 6.609   60.763  35.861  1.00 29.23  ? 1200 HOH B O   1 
HETATM 10925 O  O   . HOH U 7 .   ? -3.351  35.251  37.582  1.00 40.56  ? 1201 HOH B O   1 
HETATM 10926 O  O   . HOH U 7 .   ? 12.860  82.267  19.007  1.00 42.72  ? 1202 HOH B O   1 
HETATM 10927 O  O   . HOH U 7 .   ? -5.228  85.638  35.779  1.00 46.90  ? 1203 HOH B O   1 
HETATM 10928 O  O   . HOH U 7 .   ? 0.972   41.083  34.034  1.00 34.10  ? 1204 HOH B O   1 
HETATM 10929 O  O   . HOH U 7 .   ? 2.856   77.423  56.937  1.00 61.81  ? 1205 HOH B O   1 
HETATM 10930 O  O   . HOH U 7 .   ? -6.156  56.632  9.529   1.00 56.63  ? 1206 HOH B O   1 
HETATM 10931 O  O   . HOH U 7 .   ? -23.058 60.037  31.846  1.00 58.67  ? 1207 HOH B O   1 
HETATM 10932 O  O   . HOH U 7 .   ? -0.499  104.555 -6.948  1.00 64.57  ? 1208 HOH B O   1 
HETATM 10933 O  O   . HOH U 7 .   ? -8.114  42.734  25.250  1.00 51.97  ? 1209 HOH B O   1 
HETATM 10934 O  O   . HOH U 7 .   ? 21.455  41.789  45.943  1.00 41.54  ? 1210 HOH B O   1 
HETATM 10935 O  O   . HOH U 7 .   ? 3.050   58.643  48.988  1.00 46.31  ? 1211 HOH B O   1 
HETATM 10936 O  O   . HOH U 7 .   ? -20.326 63.670  42.492  1.00 54.26  ? 1212 HOH B O   1 
HETATM 10937 O  O   . HOH U 7 .   ? -18.238 67.000  31.463  1.00 45.06  ? 1213 HOH B O   1 
HETATM 10938 O  O   . HOH U 7 .   ? -6.889  36.389  32.249  1.00 38.28  ? 1214 HOH B O   1 
HETATM 10939 O  O   . HOH U 7 .   ? -17.808 68.717  28.252  1.00 53.13  ? 1215 HOH B O   1 
HETATM 10940 O  O   . HOH U 7 .   ? -9.033  36.416  45.391  1.00 50.88  ? 1216 HOH B O   1 
HETATM 10941 O  O   . HOH U 7 .   ? -13.145 91.665  -0.877  1.00 35.06  ? 1217 HOH B O   1 
HETATM 10942 O  O   . HOH U 7 .   ? 8.807   58.452  20.341  1.00 25.76  ? 1218 HOH B O   1 
HETATM 10943 O  O   . HOH U 7 .   ? -15.653 67.480  54.294  1.00 40.23  ? 1219 HOH B O   1 
HETATM 10944 O  O   . HOH U 7 .   ? 17.911  24.225  38.536  1.00 52.21  ? 1220 HOH B O   1 
HETATM 10945 O  O   . HOH U 7 .   ? -25.380 90.511  16.167  1.00 33.45  ? 1221 HOH B O   1 
HETATM 10946 O  O   . HOH U 7 .   ? -13.290 74.081  27.189  1.00 44.82  ? 1222 HOH B O   1 
HETATM 10947 O  O   . HOH U 7 .   ? 15.741  85.156  18.164  1.00 43.97  ? 1223 HOH B O   1 
HETATM 10948 O  O   . HOH U 7 .   ? 3.586   108.502 -5.183  1.00 43.00  ? 1224 HOH B O   1 
HETATM 10949 O  O   . HOH U 7 .   ? 13.864  63.461  30.088  1.00 45.91  ? 1225 HOH B O   1 
HETATM 10950 O  O   . HOH U 7 .   ? -22.062 91.078  28.195  1.00 58.25  ? 1226 HOH B O   1 
HETATM 10951 O  O   . HOH U 7 .   ? 13.806  36.934  53.404  1.00 43.44  ? 1227 HOH B O   1 
HETATM 10952 O  O   . HOH U 7 .   ? 14.009  55.552  25.102  1.00 76.03  ? 1228 HOH B O   1 
HETATM 10953 O  O   . HOH U 7 .   ? -1.787  99.063  6.401   1.00 19.64  ? 1229 HOH B O   1 
HETATM 10954 O  O   . HOH U 7 .   ? -4.735  45.270  44.179  1.00 29.07  ? 1230 HOH B O   1 
HETATM 10955 O  O   . HOH U 7 .   ? 18.955  44.042  28.720  1.00 33.20  ? 1231 HOH B O   1 
HETATM 10956 O  O   . HOH U 7 .   ? 3.623   91.617  -2.692  1.00 67.83  ? 1232 HOH B O   1 
HETATM 10957 O  O   . HOH U 7 .   ? 3.478   74.205  28.037  1.00 34.52  ? 1233 HOH B O   1 
HETATM 10958 O  O   . HOH U 7 .   ? -20.866 61.597  29.505  1.00 57.01  ? 1234 HOH B O   1 
HETATM 10959 O  O   . HOH U 7 .   ? 1.030   97.118  17.784  1.00 42.47  ? 1235 HOH B O   1 
HETATM 10960 O  O   . HOH U 7 .   ? 10.849  35.796  49.476  1.00 27.89  ? 1236 HOH B O   1 
HETATM 10961 O  O   . HOH U 7 .   ? 19.328  41.275  28.231  1.00 28.12  ? 1237 HOH B O   1 
HETATM 10962 O  O   . HOH U 7 .   ? 4.696   52.797  29.096  1.00 34.32  ? 1238 HOH B O   1 
HETATM 10963 O  O   . HOH U 7 .   ? -8.838  81.123  0.012   1.00 71.20  ? 1239 HOH B O   1 
HETATM 10964 O  O   . HOH U 7 .   ? -20.619 62.757  36.362  1.00 60.61  ? 1240 HOH B O   1 
HETATM 10965 O  O   . HOH U 7 .   ? -0.977  65.956  64.581  1.00 48.49  ? 1241 HOH B O   1 
HETATM 10966 O  O   . HOH U 7 .   ? -2.555  73.598  17.480  1.00 38.68  ? 1242 HOH B O   1 
HETATM 10967 O  O   . HOH U 7 .   ? 5.556   77.901  55.779  1.00 61.41  ? 1243 HOH B O   1 
HETATM 10968 O  O   . HOH U 7 .   ? -16.424 79.146  40.214  1.00 67.73  ? 1244 HOH B O   1 
HETATM 10969 O  O   . HOH U 7 .   ? -0.935  34.192  38.886  1.00 40.58  ? 1245 HOH B O   1 
HETATM 10970 O  O   . HOH U 7 .   ? -16.937 91.674  29.583  1.00 56.55  ? 1246 HOH B O   1 
HETATM 10971 O  O   . HOH U 7 .   ? -6.327  46.270  24.726  1.00 40.28  ? 1247 HOH B O   1 
HETATM 10972 O  O   . HOH U 7 .   ? 0.579   45.406  25.404  1.00 28.48  ? 1248 HOH B O   1 
HETATM 10973 O  O   . HOH U 7 .   ? 16.120  35.087  50.470  1.00 33.66  ? 1249 HOH B O   1 
HETATM 10974 O  O   . HOH U 7 .   ? -11.128 59.362  12.430  1.00 35.54  ? 1250 HOH B O   1 
HETATM 10975 O  O   . HOH U 7 .   ? -16.758 64.218  16.219  1.00 45.46  ? 1251 HOH B O   1 
HETATM 10976 O  O   . HOH U 7 .   ? -15.374 97.062  30.111  1.00 41.55  ? 1252 HOH B O   1 
HETATM 10977 O  O   . HOH U 7 .   ? -17.313 56.750  19.298  1.00 64.18  ? 1253 HOH B O   1 
HETATM 10978 O  O   . HOH U 7 .   ? -18.195 98.291  13.972  1.00 23.66  ? 1254 HOH B O   1 
HETATM 10979 O  O   . HOH U 7 .   ? 0.062   94.738  -2.375  1.00 40.02  ? 1255 HOH B O   1 
HETATM 10980 O  O   . HOH U 7 .   ? 27.679  28.577  42.344  1.00 57.44  ? 1256 HOH B O   1 
HETATM 10981 O  O   . HOH U 7 .   ? -0.616  43.746  33.146  1.00 23.05  ? 1257 HOH B O   1 
HETATM 10982 O  O   . HOH U 7 .   ? 14.565  66.055  30.892  1.00 49.69  ? 1258 HOH B O   1 
HETATM 10983 O  O   . HOH U 7 .   ? -19.963 55.391  27.135  1.00 30.64  ? 1259 HOH B O   1 
HETATM 10984 O  O   . HOH U 7 .   ? 15.202  29.765  54.896  1.00 46.25  ? 1260 HOH B O   1 
HETATM 10985 O  O   . HOH U 7 .   ? -14.590 34.775  43.344  1.00 45.17  ? 1261 HOH B O   1 
HETATM 10986 O  O   . HOH U 7 .   ? 10.676  43.213  17.855  1.00 46.14  ? 1262 HOH B O   1 
HETATM 10987 O  O   . HOH U 7 .   ? -1.373  28.656  32.370  1.00 40.94  ? 1263 HOH B O   1 
HETATM 10988 O  O   . HOH U 7 .   ? -6.305  107.538 13.015  1.00 61.31  ? 1264 HOH B O   1 
HETATM 10989 O  O   . HOH U 7 .   ? 4.888   67.258  14.239  1.00 48.15  ? 1265 HOH B O   1 
HETATM 10990 O  O   . HOH U 7 .   ? -19.525 53.678  53.881  1.00 64.22  ? 1266 HOH B O   1 
HETATM 10991 O  O   . HOH U 7 .   ? 11.134  52.600  17.620  1.00 24.24  ? 1267 HOH B O   1 
HETATM 10992 O  O   . HOH U 7 .   ? 0.832   53.363  15.873  1.00 31.34  ? 1268 HOH B O   1 
HETATM 10993 O  O   . HOH U 7 .   ? -18.213 75.978  21.075  1.00 54.79  ? 1269 HOH B O   1 
HETATM 10994 O  O   . HOH U 7 .   ? 5.698   75.409  35.758  1.00 55.70  ? 1270 HOH B O   1 
HETATM 10995 O  O   . HOH U 7 .   ? -22.390 53.960  28.644  1.00 50.65  ? 1271 HOH B O   1 
HETATM 10996 O  O   . HOH U 7 .   ? -15.281 54.238  24.282  1.00 34.95  ? 1272 HOH B O   1 
HETATM 10997 O  O   . HOH U 7 .   ? -0.450  46.283  38.492  1.00 21.27  ? 1273 HOH B O   1 
HETATM 10998 O  O   . HOH U 7 .   ? 0.476   36.044  40.508  1.00 31.99  ? 1274 HOH B O   1 
HETATM 10999 O  O   . HOH U 7 .   ? -19.555 88.347  6.088   1.00 53.72  ? 1275 HOH B O   1 
HETATM 11000 O  O   . HOH U 7 .   ? -1.320  43.363  29.344  1.00 36.54  ? 1276 HOH B O   1 
HETATM 11001 O  O   . HOH U 7 .   ? 1.490   78.639  30.326  1.00 53.24  ? 1277 HOH B O   1 
HETATM 11002 O  O   . HOH U 7 .   ? 3.832   53.148  54.891  1.00 60.69  ? 1278 HOH B O   1 
HETATM 11003 O  O   . HOH U 7 .   ? 6.002   32.369  13.764  1.00 59.76  ? 1279 HOH B O   1 
HETATM 11004 O  O   . HOH U 7 .   ? 9.318   33.322  22.796  1.00 33.03  ? 1280 HOH B O   1 
HETATM 11005 O  O   . HOH U 7 .   ? 6.486   47.240  38.604  1.00 25.72  ? 1281 HOH B O   1 
HETATM 11006 O  O   . HOH U 7 .   ? 14.359  63.817  18.691  1.00 33.08  ? 1282 HOH B O   1 
HETATM 11007 O  O   . HOH U 7 .   ? -13.924 70.466  14.244  1.00 51.42  ? 1283 HOH B O   1 
HETATM 11008 O  O   . HOH U 7 .   ? -0.838  26.409  41.118  1.00 60.81  ? 1284 HOH B O   1 
HETATM 11009 O  O   . HOH U 7 .   ? 4.402   56.399  55.167  1.00 53.83  ? 1285 HOH B O   1 
HETATM 11010 O  O   . HOH U 7 .   ? -15.701 34.397  40.920  1.00 56.15  ? 1286 HOH B O   1 
HETATM 11011 O  O   . HOH U 7 .   ? 0.489   30.839  29.250  1.00 51.65  ? 1287 HOH B O   1 
HETATM 11012 O  O   . HOH U 7 .   ? 2.741   71.750  58.183  1.00 37.43  ? 1288 HOH B O   1 
HETATM 11013 O  O   . HOH U 7 .   ? -15.070 62.949  45.687  1.00 34.65  ? 1289 HOH B O   1 
HETATM 11014 O  O   . HOH U 7 .   ? 10.860  54.912  31.539  1.00 52.65  ? 1290 HOH B O   1 
HETATM 11015 O  O   . HOH U 7 .   ? 6.873   74.580  13.524  1.00 67.28  ? 1291 HOH B O   1 
HETATM 11016 O  O   . HOH U 7 .   ? -26.726 43.773  34.527  1.00 68.79  ? 1292 HOH B O   1 
HETATM 11017 O  O   . HOH U 7 .   ? -5.490  69.362  15.342  1.00 32.71  ? 1293 HOH B O   1 
HETATM 11018 O  O   . HOH U 7 .   ? -16.439 73.546  35.369  1.00 59.16  ? 1294 HOH B O   1 
HETATM 11019 O  O   . HOH U 7 .   ? 7.196   51.122  39.556  1.00 28.36  ? 1295 HOH B O   1 
HETATM 11020 O  O   . HOH U 7 .   ? -2.819  42.701  48.357  1.00 62.44  ? 1296 HOH B O   1 
HETATM 11021 O  O   . HOH U 7 .   ? -4.102  83.931  44.238  1.00 46.44  ? 1297 HOH B O   1 
HETATM 11022 O  O   . HOH U 7 .   ? 13.611  24.049  39.932  1.00 53.68  ? 1298 HOH B O   1 
HETATM 11023 O  O   . HOH U 7 .   ? 11.917  82.699  22.700  1.00 59.06  ? 1299 HOH B O   1 
HETATM 11024 O  O   . HOH U 7 .   ? -11.179 56.052  13.131  1.00 53.79  ? 1300 HOH B O   1 
HETATM 11025 O  O   . HOH U 7 .   ? -24.272 41.244  35.034  1.00 61.58  ? 1301 HOH B O   1 
HETATM 11026 O  O   . HOH U 7 .   ? 9.348   27.667  52.897  1.00 49.32  ? 1302 HOH B O   1 
HETATM 11027 O  O   . HOH U 7 .   ? -13.788 104.277 27.073  1.00 65.32  ? 1303 HOH B O   1 
HETATM 11028 O  O   . HOH U 7 .   ? -17.378 55.990  53.932  1.00 36.12  ? 1304 HOH B O   1 
HETATM 11029 O  O   . HOH U 7 .   ? 13.167  60.262  22.445  1.00 41.30  ? 1305 HOH B O   1 
HETATM 11030 O  O   . HOH U 7 .   ? 1.220   96.923  14.560  1.00 49.65  ? 1306 HOH B O   1 
HETATM 11031 O  O   . HOH U 7 .   ? -0.462  82.461  -2.430  1.00 38.63  ? 1307 HOH B O   1 
HETATM 11032 O  O   . HOH U 7 .   ? 5.036   85.064  0.727   1.00 40.25  ? 1308 HOH B O   1 
HETATM 11033 O  O   . HOH U 7 .   ? -17.645 53.532  20.632  1.00 57.72  ? 1309 HOH B O   1 
HETATM 11034 O  O   . HOH U 7 .   ? 10.875  54.645  38.104  1.00 58.60  ? 1310 HOH B O   1 
HETATM 11035 O  O   . HOH U 7 .   ? -24.729 44.172  30.188  1.00 48.48  ? 1311 HOH B O   1 
HETATM 11036 O  O   . HOH U 7 .   ? 2.215   98.931  19.388  1.00 75.08  ? 1312 HOH B O   1 
HETATM 11037 O  O   . HOH U 7 .   ? 12.812  49.087  40.236  1.00 52.51  ? 1313 HOH B O   1 
HETATM 11038 O  O   . HOH U 7 .   ? -16.264 104.075 1.293   1.00 57.55  ? 1314 HOH B O   1 
HETATM 11039 O  O   . HOH U 7 .   ? -8.670  105.122 6.383   1.00 33.40  ? 1315 HOH B O   1 
HETATM 11040 O  O   . HOH U 7 .   ? -15.337 78.234  37.926  1.00 55.38  ? 1316 HOH B O   1 
HETATM 11041 O  O   . HOH U 7 .   ? -18.652 100.008 3.174   1.00 38.95  ? 1317 HOH B O   1 
HETATM 11042 O  O   . HOH U 7 .   ? 4.583   45.060  43.438  1.00 71.33  ? 1318 HOH B O   1 
HETATM 11043 O  O   . HOH U 7 .   ? 18.088  37.591  50.576  1.00 64.40  ? 1319 HOH B O   1 
HETATM 11044 O  O   . HOH U 7 .   ? -7.748  87.703  -1.520  1.00 38.25  ? 1320 HOH B O   1 
HETATM 11045 O  O   . HOH U 7 .   ? 3.317   96.307  15.915  1.00 47.97  ? 1321 HOH B O   1 
HETATM 11046 O  O   . HOH U 7 .   ? -3.641  45.314  47.278  1.00 62.25  ? 1322 HOH B O   1 
HETATM 11047 O  O   . HOH U 7 .   ? -18.685 84.274  4.238   1.00 63.53  ? 1323 HOH B O   1 
HETATM 11048 O  O   . HOH U 7 .   ? -25.316 88.001  17.879  1.00 39.71  ? 1324 HOH B O   1 
HETATM 11049 O  O   . HOH U 7 .   ? -30.008 52.911  47.325  1.00 55.48  ? 1325 HOH B O   1 
HETATM 11050 O  O   . HOH U 7 .   ? -17.443 59.145  21.203  1.00 51.76  ? 1326 HOH B O   1 
HETATM 11051 O  O   . HOH U 7 .   ? -9.978  72.471  13.293  1.00 33.50  ? 1327 HOH B O   1 
HETATM 11052 O  O   . HOH U 7 .   ? -15.598 106.731 -1.673  1.00 62.56  ? 1328 HOH B O   1 
HETATM 11053 O  O   . HOH U 7 .   ? 18.383  60.998  10.902  1.00 69.90  ? 1329 HOH B O   1 
HETATM 11054 O  O   . HOH U 7 .   ? -18.199 96.602  29.185  1.00 50.51  ? 1330 HOH B O   1 
HETATM 11055 O  O   . HOH U 7 .   ? -3.574  85.429  29.920  1.00 35.35  ? 1331 HOH B O   1 
HETATM 11056 O  O   . HOH U 7 .   ? 13.936  60.461  30.401  1.00 57.61  ? 1332 HOH B O   1 
HETATM 11057 O  O   . HOH U 7 .   ? -18.741 64.066  31.621  1.00 50.09  ? 1333 HOH B O   1 
HETATM 11058 O  O   . HOH U 7 .   ? -15.399 102.166 11.935  1.00 26.81  ? 1334 HOH B O   1 
HETATM 11059 O  O   . HOH U 7 .   ? -8.820  108.750 18.620  1.00 63.81  ? 1335 HOH B O   1 
HETATM 11060 O  O   . HOH U 7 .   ? -20.679 72.662  49.193  1.00 61.61  ? 1336 HOH B O   1 
HETATM 11061 O  O   . HOH U 7 .   ? -0.668  48.652  19.421  1.00 67.11  ? 1337 HOH B O   1 
HETATM 11062 O  O   . HOH U 7 .   ? 6.824   109.679 -3.039  1.00 32.77  ? 1338 HOH B O   1 
HETATM 11063 O  O   . HOH U 7 .   ? -6.377  81.004  35.114  1.00 47.90  ? 1339 HOH B O   1 
HETATM 11064 O  O   . HOH U 7 .   ? 12.473  20.253  35.844  1.00 56.03  ? 1340 HOH B O   1 
HETATM 11065 O  O   . HOH U 7 .   ? 1.773   63.393  60.084  1.00 69.14  ? 1341 HOH B O   1 
HETATM 11066 O  O   . HOH U 7 .   ? -22.058 49.158  51.800  1.00 49.72  ? 1342 HOH B O   1 
HETATM 11067 O  O   . HOH U 7 .   ? -24.881 88.132  20.305  1.00 55.45  ? 1343 HOH B O   1 
HETATM 11068 O  O   . HOH U 7 .   ? -9.759  49.142  20.643  1.00 47.91  ? 1344 HOH B O   1 
HETATM 11069 O  O   . HOH U 7 .   ? -1.530  88.248  29.084  1.00 36.78  ? 1345 HOH B O   1 
HETATM 11070 O  O   . HOH U 7 .   ? 7.467   43.633  53.836  1.00 48.52  ? 1346 HOH B O   1 
HETATM 11071 O  O   . HOH U 7 .   ? -3.859  93.171  -1.457  1.00 48.32  ? 1347 HOH B O   1 
HETATM 11072 O  O   . HOH U 7 .   ? -8.733  81.806  34.476  1.00 48.58  ? 1348 HOH B O   1 
HETATM 11073 O  O   . HOH U 7 .   ? -5.963  33.666  35.745  1.00 42.90  ? 1349 HOH B O   1 
HETATM 11074 O  O   . HOH U 7 .   ? -30.580 57.680  43.416  1.00 46.13  ? 1350 HOH B O   1 
HETATM 11075 O  O   . HOH U 7 .   ? 14.074  84.995  22.389  1.00 61.76  ? 1351 HOH B O   1 
HETATM 11076 O  O   . HOH U 7 .   ? 6.804   80.130  7.855   1.00 56.46  ? 1352 HOH B O   1 
HETATM 11077 O  O   . HOH U 7 .   ? 24.143  31.516  37.576  1.00 39.27  ? 1353 HOH B O   1 
HETATM 11078 O  O   . HOH U 7 .   ? -26.851 56.338  51.487  1.00 55.55  ? 1354 HOH B O   1 
HETATM 11079 O  O   . HOH U 7 .   ? 4.832   45.718  14.924  1.00 47.75  ? 1355 HOH B O   1 
HETATM 11080 O  O   . HOH U 7 .   ? 19.306  30.895  33.429  1.00 52.69  ? 1356 HOH B O   1 
HETATM 11081 O  O   . HOH U 7 .   ? -14.857 85.305  39.795  1.00 73.54  ? 1357 HOH B O   1 
HETATM 11082 O  O   . HOH U 7 .   ? -4.497  81.141  33.481  1.00 48.18  ? 1358 HOH B O   1 
HETATM 11083 O  O   . HOH U 7 .   ? 1.708   92.567  11.729  1.00 29.96  ? 1359 HOH B O   1 
HETATM 11084 O  O   . HOH U 7 .   ? -6.022  82.529  37.436  1.00 51.55  ? 1360 HOH B O   1 
HETATM 11085 O  O   . HOH U 7 .   ? 6.060   103.331 -1.770  1.00 40.04  ? 1361 HOH B O   1 
HETATM 11086 O  O   . HOH U 7 .   ? -7.220  59.316  59.259  1.00 56.92  ? 1362 HOH B O   1 
HETATM 11087 O  O   . HOH U 7 .   ? -30.847 42.735  44.876  1.00 60.54  ? 1363 HOH B O   1 
HETATM 11088 O  O   . HOH U 7 .   ? 13.129  58.156  24.989  1.00 57.61  ? 1364 HOH B O   1 
HETATM 11089 O  O   . HOH U 7 .   ? -22.104 87.220  21.003  1.00 36.28  ? 1365 HOH B O   1 
HETATM 11090 O  O   . HOH U 7 .   ? -16.211 78.983  27.071  1.00 66.20  ? 1366 HOH B O   1 
HETATM 11091 O  O   . HOH U 7 .   ? -10.305 107.641 0.073   1.00 54.69  ? 1367 HOH B O   1 
HETATM 11092 O  O   . HOH U 7 .   ? -0.707  61.774  60.589  1.00 81.37  ? 1368 HOH B O   1 
HETATM 11093 O  O   . HOH U 7 .   ? -22.537 63.715  57.045  1.00 65.42  ? 1369 HOH B O   1 
HETATM 11094 O  O   . HOH U 7 .   ? -15.969 81.987  0.282   1.00 62.77  ? 1370 HOH B O   1 
HETATM 11095 O  O   . HOH U 7 .   ? -7.844  107.832 16.645  1.00 54.35  ? 1371 HOH B O   1 
HETATM 11096 O  O   . HOH U 7 .   ? -11.120 42.377  23.631  1.00 64.24  ? 1372 HOH B O   1 
HETATM 11097 O  O   . HOH U 7 .   ? 1.086   80.513  26.692  1.00 70.12  ? 1373 HOH B O   1 
HETATM 11098 O  O   . HOH U 7 .   ? -20.116 74.213  16.811  1.00 59.97  ? 1374 HOH B O   1 
HETATM 11099 O  O   . HOH U 7 .   ? -18.305 93.089  0.248   1.00 73.91  ? 1375 HOH B O   1 
HETATM 11100 O  O   . HOH U 7 .   ? -12.222 56.824  57.821  1.00 53.34  ? 1376 HOH B O   1 
HETATM 11101 O  O   . HOH U 7 .   ? 4.621   77.546  14.612  1.00 78.84  ? 1377 HOH B O   1 
HETATM 11102 O  O   . HOH U 7 .   ? -12.708 77.646  23.460  1.00 29.90  ? 1378 HOH B O   1 
HETATM 11103 O  O   . HOH U 7 .   ? -31.237 49.846  46.597  1.00 60.88  ? 1379 HOH B O   1 
HETATM 11104 O  O   . HOH U 7 .   ? 14.970  61.651  20.774  1.00 55.55  ? 1380 HOH B O   1 
HETATM 11105 O  O   . HOH U 7 .   ? 6.786   23.134  30.315  1.00 50.71  ? 1381 HOH B O   1 
HETATM 11106 O  O   . HOH U 7 .   ? 17.450  46.828  48.092  1.00 70.21  ? 1382 HOH B O   1 
HETATM 11107 O  O   . HOH U 7 .   ? -11.673 50.366  19.530  1.00 59.90  ? 1383 HOH B O   1 
HETATM 11108 O  O   . HOH U 7 .   ? -13.047 38.063  30.824  1.00 40.21  ? 1384 HOH B O   1 
HETATM 11109 O  O   . HOH U 7 .   ? -23.382 51.087  28.319  1.00 56.25  ? 1385 HOH B O   1 
HETATM 11110 O  O   . HOH U 7 .   ? -16.956 72.353  26.442  1.00 57.79  ? 1386 HOH B O   1 
HETATM 11111 O  O   . HOH U 7 .   ? -19.086 77.884  11.396  1.00 60.30  ? 1387 HOH B O   1 
HETATM 11112 O  O   . HOH U 7 .   ? 6.526   41.261  14.542  1.00 56.90  ? 1388 HOH B O   1 
HETATM 11113 O  O   . HOH U 7 .   ? 2.673   31.095  27.310  1.00 50.25  ? 1389 HOH B O   1 
HETATM 11114 O  O   . HOH U 7 .   ? 6.927   92.122  31.995  1.00 56.86  ? 1390 HOH B O   1 
HETATM 11115 O  O   . HOH U 7 .   ? 4.598   76.629  27.754  1.00 43.17  ? 1391 HOH B O   1 
HETATM 11116 O  O   . HOH U 7 .   ? -14.144 71.877  25.865  1.00 34.48  ? 1392 HOH B O   1 
HETATM 11117 O  O   . HOH U 7 .   ? -22.694 64.031  45.844  1.00 44.42  ? 1393 HOH B O   1 
HETATM 11118 O  O   . HOH U 7 .   ? -14.257 45.553  24.374  1.00 30.84  ? 1394 HOH B O   1 
HETATM 11119 O  O   . HOH U 7 .   ? -14.999 85.283  4.191   1.00 46.32  ? 1395 HOH B O   1 
HETATM 11120 O  O   . HOH U 7 .   ? -24.930 85.684  15.166  1.00 61.23  ? 1396 HOH B O   1 
HETATM 11121 O  O   . HOH U 7 .   ? 1.370   76.937  35.305  1.00 57.57  ? 1397 HOH B O   1 
HETATM 11122 O  O   . HOH U 7 .   ? -11.323 89.508  -1.098  1.00 33.39  ? 1398 HOH B O   1 
HETATM 11123 O  O   . HOH U 7 .   ? -20.570 103.076 29.412  1.00 53.90  ? 1399 HOH B O   1 
HETATM 11124 O  O   . HOH U 7 .   ? 5.497   105.992 -5.453  1.00 51.59  ? 1400 HOH B O   1 
HETATM 11125 O  O   . HOH U 7 .   ? -15.251 50.301  19.597  1.00 51.78  ? 1401 HOH B O   1 
HETATM 11126 O  O   . HOH U 7 .   ? -12.600 34.571  33.901  1.00 50.37  ? 1402 HOH B O   1 
HETATM 11127 O  O   . HOH U 7 .   ? -15.524 105.154 25.331  1.00 48.71  ? 1403 HOH B O   1 
HETATM 11128 O  O   . HOH U 7 .   ? 10.186  49.443  46.456  1.00 51.13  ? 1404 HOH B O   1 
HETATM 11129 O  O   . HOH U 7 .   ? 6.971   43.897  14.290  1.00 31.72  ? 1405 HOH B O   1 
HETATM 11130 O  O   . HOH U 7 .   ? 4.805   93.509  14.270  1.00 26.82  ? 1406 HOH B O   1 
HETATM 11131 O  O   . HOH U 7 .   ? 15.096  82.575  17.474  1.00 55.47  ? 1407 HOH B O   1 
HETATM 11132 O  O   . HOH U 7 .   ? 2.372   106.168 -7.256  1.00 68.03  ? 1408 HOH B O   1 
HETATM 11133 O  O   . HOH U 7 .   ? -19.196 60.062  24.629  1.00 74.33  ? 1409 HOH B O   1 
HETATM 11134 O  O   . HOH U 7 .   ? -19.492 95.722  1.641   1.00 51.01  ? 1410 HOH B O   1 
HETATM 11135 O  O   . HOH U 7 .   ? 8.011   61.841  33.507  1.00 34.86  ? 1411 HOH B O   1 
HETATM 11136 O  O   . HOH U 7 .   ? -22.671 84.503  17.108  1.00 54.23  ? 1412 HOH B O   1 
HETATM 11137 O  O   . HOH U 7 .   ? 1.979   51.278  15.951  1.00 49.34  ? 1413 HOH B O   1 
HETATM 11138 O  O   . HOH U 7 .   ? -1.434  104.907 17.665  1.00 82.24  ? 1414 HOH B O   1 
HETATM 11139 O  O   . HOH U 7 .   ? -19.499 73.399  11.337  1.00 54.29  ? 1415 HOH B O   1 
HETATM 11140 O  O   . HOH U 7 .   ? 8.277   24.838  42.084  1.00 62.25  ? 1416 HOH B O   1 
HETATM 11141 O  O   . HOH U 7 .   ? -5.301  43.358  26.701  1.00 39.81  ? 1417 HOH B O   1 
HETATM 11142 O  O   . HOH U 7 .   ? 5.743   72.635  41.352  1.00 52.45  ? 1418 HOH B O   1 
HETATM 11143 O  O   . HOH U 7 .   ? 8.881   63.760  36.904  1.00 59.62  ? 1419 HOH B O   1 
HETATM 11144 O  O   . HOH U 7 .   ? -23.470 89.140  12.036  1.00 57.31  ? 1420 HOH B O   1 
HETATM 11145 O  O   . HOH U 7 .   ? -0.839  63.149  64.480  1.00 44.13  ? 1421 HOH B O   1 
HETATM 11146 O  O   . HOH U 7 .   ? 15.997  56.574  26.875  1.00 54.37  ? 1422 HOH B O   1 
HETATM 11147 O  O   . HOH U 7 .   ? -21.681 46.430  52.204  1.00 52.97  ? 1423 HOH B O   1 
HETATM 11148 O  O   . HOH U 7 .   ? 2.163   36.406  20.915  1.00 64.94  ? 1424 HOH B O   1 
HETATM 11149 O  O   . HOH U 7 .   ? 21.986  40.213  27.972  1.00 50.42  ? 1425 HOH B O   1 
HETATM 11150 O  O   . HOH U 7 .   ? 10.997  24.346  29.952  1.00 67.81  ? 1426 HOH B O   1 
HETATM 11151 O  O   . HOH U 7 .   ? -16.288 75.412  24.117  1.00 42.24  ? 1427 HOH B O   1 
HETATM 11152 O  O   . HOH U 7 .   ? 9.026   59.577  36.068  1.00 53.93  ? 1428 HOH B O   1 
HETATM 11153 O  O   . HOH U 7 .   ? -3.075  87.415  31.205  1.00 49.71  ? 1429 HOH B O   1 
HETATM 11154 O  O   . HOH U 7 .   ? -17.404 43.077  26.658  1.00 46.14  ? 1430 HOH B O   1 
HETATM 11155 O  O   . HOH U 7 .   ? -23.031 48.634  29.275  1.00 41.78  ? 1431 HOH B O   1 
HETATM 11156 O  O   . HOH U 7 .   ? -4.831  52.468  16.919  1.00 59.07  ? 1432 HOH B O   1 
HETATM 11157 O  O   . HOH U 7 .   ? -17.810 71.314  12.271  1.00 58.18  ? 1433 HOH B O   1 
HETATM 11158 O  O   . HOH U 7 .   ? 9.724   44.490  15.188  1.00 34.90  ? 1434 HOH B O   1 
HETATM 11159 O  O   . HOH U 7 .   ? 4.879   36.599  18.968  1.00 33.53  ? 1435 HOH B O   1 
HETATM 11160 O  O   . HOH U 7 .   ? -17.641 73.660  22.535  1.00 58.20  ? 1436 HOH B O   1 
HETATM 11161 O  O   . HOH U 7 .   ? -3.642  97.024  -2.732  1.00 37.50  ? 1437 HOH B O   1 
HETATM 11162 O  O   . HOH U 7 .   ? 3.375   52.041  40.881  1.00 47.04  ? 1438 HOH B O   1 
HETATM 11163 O  O   . HOH U 7 .   ? 4.615   29.623  27.878  1.00 42.47  ? 1439 HOH B O   1 
HETATM 11164 O  O   . HOH U 7 .   ? 17.858  27.927  45.262  1.00 60.49  ? 1440 HOH B O   1 
HETATM 11165 O  O   . HOH U 7 .   ? -14.777 55.735  54.995  1.00 37.32  ? 1441 HOH B O   1 
HETATM 11166 O  O   . HOH U 7 .   ? 7.307   48.452  40.646  1.00 29.20  ? 1442 HOH B O   1 
HETATM 11167 O  O   . HOH U 7 .   ? -22.309 85.226  19.409  1.00 48.49  ? 1443 HOH B O   1 
HETATM 11168 O  O   . HOH U 7 .   ? -0.995  42.010  45.244  1.00 67.82  ? 1444 HOH B O   1 
HETATM 11169 O  O   . HOH U 7 .   ? 8.861   74.702  31.517  1.00 58.12  ? 1445 HOH B O   1 
HETATM 11170 O  O   . HOH U 7 .   ? 14.534  82.093  13.888  1.00 59.22  ? 1446 HOH B O   1 
HETATM 11171 O  O   . HOH U 7 .   ? -21.443 43.814  52.151  1.00 55.72  ? 1447 HOH B O   1 
HETATM 11172 O  O   . HOH U 7 .   ? -20.251 77.426  2.926   1.00 60.60  ? 1448 HOH B O   1 
HETATM 11173 O  O   . HOH U 7 .   ? -13.669 88.097  34.315  1.00 54.07  ? 1449 HOH B O   1 
HETATM 11174 O  O   . HOH U 7 .   ? 2.664   34.507  10.928  1.00 61.33  ? 1450 HOH B O   1 
HETATM 11175 O  O   . HOH U 7 .   ? 10.741  54.454  19.838  1.00 47.80  ? 1451 HOH B O   1 
HETATM 11176 O  O   . HOH U 7 .   ? -16.699 40.511  28.682  1.00 53.27  ? 1452 HOH B O   1 
HETATM 11177 O  O   . HOH U 7 .   ? -16.953 35.592  32.464  1.00 50.81  ? 1453 HOH B O   1 
HETATM 11178 O  O   . HOH U 7 .   ? 4.566   84.203  25.851  1.00 35.35  ? 1454 HOH B O   1 
HETATM 11179 O  O   . HOH U 7 .   ? -15.472 43.913  28.164  1.00 29.98  ? 1455 HOH B O   1 
HETATM 11180 O  O   . HOH U 7 .   ? 4.047   52.131  51.195  1.00 60.65  ? 1456 HOH B O   1 
HETATM 11181 O  O   . HOH U 7 .   ? -14.485 91.249  31.011  1.00 58.21  ? 1457 HOH B O   1 
HETATM 11182 O  O   . HOH U 7 .   ? 4.614   38.019  12.250  1.00 55.65  ? 1458 HOH B O   1 
HETATM 11183 O  O   . HOH U 7 .   ? 14.378  55.924  30.433  1.00 73.87  ? 1459 HOH B O   1 
HETATM 11184 O  O   . HOH U 7 .   ? 19.661  61.033  23.845  1.00 75.38  ? 1460 HOH B O   1 
HETATM 11185 O  O   . HOH U 7 .   ? -20.922 61.800  25.926  1.00 64.68  ? 1461 HOH B O   1 
HETATM 11186 O  O   . HOH U 7 .   ? 6.970   81.227  27.452  1.00 56.20  ? 1462 HOH B O   1 
HETATM 11187 O  O   . HOH U 7 .   ? 14.938  26.290  31.819  1.00 62.96  ? 1463 HOH B O   1 
HETATM 11188 O  O   . HOH U 7 .   ? -1.524  100.653 9.289   1.00 40.67  ? 1464 HOH B O   1 
HETATM 11189 O  O   . HOH U 7 .   ? 15.423  31.225  27.752  1.00 41.00  ? 1465 HOH B O   1 
HETATM 11190 O  O   . HOH U 7 .   ? -15.072 69.205  22.894  1.00 35.22  ? 1466 HOH B O   1 
HETATM 11191 O  O   . HOH U 7 .   ? 3.749   82.438  40.447  1.00 62.52  ? 1467 HOH B O   1 
HETATM 11192 O  O   . HOH U 7 .   ? -16.014 79.886  24.510  1.00 50.63  ? 1468 HOH B O   1 
HETATM 11193 O  O   . HOH U 7 .   ? 8.057   32.021  18.787  1.00 38.69  ? 1469 HOH B O   1 
HETATM 11194 O  O   . HOH U 7 .   ? 1.182   100.438 12.893  1.00 66.44  ? 1470 HOH B O   1 
HETATM 11195 O  O   . HOH U 7 .   ? -19.023 63.889  13.016  1.00 57.65  ? 1471 HOH B O   1 
HETATM 11196 O  O   . HOH U 7 .   ? -9.204  85.352  -1.335  1.00 46.69  ? 1472 HOH B O   1 
HETATM 11197 O  O   . HOH U 7 .   ? -22.932 46.995  54.430  1.00 60.80  ? 1473 HOH B O   1 
HETATM 11198 O  O   . HOH U 7 .   ? -8.092  83.778  -3.829  1.00 51.42  ? 1474 HOH B O   1 
HETATM 11199 O  O   . HOH U 7 .   ? 2.774   91.691  -5.960  1.00 67.48  ? 1475 HOH B O   1 
HETATM 11200 O  O   . HOH U 7 .   ? -11.134 36.638  29.709  1.00 58.38  ? 1476 HOH B O   1 
HETATM 11201 O  O   . HOH U 7 .   ? -19.502 83.192  23.443  1.00 56.93  ? 1477 HOH B O   1 
HETATM 11202 O  O   . HOH U 7 .   ? 19.361  31.681  24.312  1.00 60.96  ? 1478 HOH B O   1 
HETATM 11203 O  O   . HOH U 7 .   ? -9.026  34.855  31.175  1.00 52.09  ? 1479 HOH B O   1 
HETATM 11204 O  O   . HOH U 7 .   ? -14.200 49.026  17.417  1.00 59.12  ? 1480 HOH B O   1 
HETATM 11205 O  O   . HOH U 7 .   ? 4.139   49.281  12.094  1.00 59.00  ? 1481 HOH B O   1 
HETATM 11206 O  O   . HOH U 7 .   ? -18.412 80.635  23.902  1.00 58.25  ? 1482 HOH B O   1 
HETATM 11207 O  O   . HOH U 7 .   ? 4.051   34.458  17.405  1.00 57.00  ? 1483 HOH B O   1 
HETATM 11208 O  O   . HOH U 7 .   ? -14.953 37.570  28.892  1.00 47.70  ? 1484 HOH B O   1 
HETATM 11209 O  O   . HOH U 7 .   ? 2.888   35.697  15.151  1.00 57.66  ? 1485 HOH B O   1 
HETATM 11210 O  O   . HOH U 7 .   ? 21.304  28.647  33.833  1.00 53.23  ? 1486 HOH B O   1 
# 
