data_9BQB
# 
_entry.id   9BQB 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   9BQB         pdb_00009bqb 10.2210/pdb9bqb/pdb 
WWPDB D_1000283155 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-25 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BQB 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-09 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          9BQ6 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              Schellenberg.matthew@mayo.edu 
_pdbx_contact_author.name_first         Matthew 
_pdbx_contact_author.name_last          Schellenberg 
_pdbx_contact_author.name_mi            J 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7036-5943 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Cong, A.T.Q.'       1  0000-0001-9307-7741 
'Austin, C.A.'       2  0000-0002-1921-5947 
'Kubes, J.'          3  0000-0002-0513-4847 
'Karabanovich, G.'   4  0000-0001-5923-7553 
'Melnikova, I.'      5  0000-0002-5378-4764 
'Lencova, O.'        6  0000-0001-7178-8470 
'Kollarova, P.'      7  0000-0001-9673-9210 
'Piskackova, H.B.'   8  0000-0002-9817-7247 
'Kerestes, V.'       9  0000-0003-0929-7376 
'Applova, L.'        10 0000-0001-6740-9685 
'Arrouye, L.'        11 0009-0006-9646-3000 
'Alvey, J.A.'        12 0000-0001-6549-9816 
'Paluncic, J.'       13 0000-0003-3420-1532 
'Witter, T.L.'       14 0000-0003-3096-3011 
'Jirkovska, A.'      15 0000-0002-0131-6010 
'Kunes, J.'          16 0000-0001-7257-0641 
'Sterbova, P.'       17 0000-0002-1242-5706 
'Sterba, M.'         18 0000-0003-0145-7697 
'Simunek, T.'        19 0000-0001-5464-4176 
'Roh, J.'            20 0000-0003-4698-8379 
'Schellenberg, M.J.' 21 0000-0001-7036-5943 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                4928 
_citation.page_last                 4928 
_citation.title                     
'Topobexin targets the Topoisomerase II ATPase domain for beta isoform-selective inhibition and anthracycline cardioprotection.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-60167-9 
_citation.pdbx_database_id_PubMed   40425539 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kubes, J.'               1  0000-0002-0513-4847 
primary 'Karabanovich, G.'        2  ?                   
primary 'Cong, A.T.Q.'            3  0000-0001-9307-7741 
primary 'Melnikova, I.'           4  ?                   
primary 'Lencova, O.'             5  ?                   
primary 'Kollarova, P.'           6  0000-0001-9673-9210 
primary 'Bavlovic Piskackova, H.' 7  0000-0002-9817-7247 
primary 'Kerestes, V.'            8  ?                   
primary 'Applova, L.'             9  ?                   
primary 'Arrouye, L.C.M.'         10 ?                   
primary 'Alvey, J.R.'             11 0000-0001-6549-9816 
primary 'Paluncic, J.'            12 0000-0003-3420-1532 
primary 'Witter, T.L.'            13 0000-0003-3096-3011 
primary 'Jirkovska, A.'           14 ?                   
primary 'Kunes, J.'               15 ?                   
primary 'Sterbova-Kovarikova, P.' 16 ?                   
primary 'Austin, C.A.'            17 0000-0002-1921-5947 
primary 'Sterba, M.'              18 ?                   
primary 'Simunek, T.'             19 ?                   
primary 'Roh, J.'                 20 ?                   
primary 'Schellenberg, M.J.'      21 0000-0001-7036-5943 
# 
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 'DNA topoisomerase 2-alpha'                                                                                   
45484.211 2   5.6.2.2 ? 'residues 29-424' ? 
2 non-polymer syn 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER'                                                                 
506.196   2   ?       ? ?                 ? 
3 non-polymer syn 'MAGNESIUM ION'                                                                                               
24.305    2   ?       ? ?                 ? 
4 non-polymer syn '8-(3,4-dihydroquinoline-1(2H)-carbonyl)-7-[2-(4-methylpiperazin-1-yl)ethoxy]-4-propyl-2H-1-benzopyran-2-one' 
489.606   2   ?       ? ?                 ? 
5 non-polymer syn 'CHLORIDE ION'                                                                                                
35.453    2   ?       ? ?                 ? 
6 non-polymer syn GLYCEROL                                                                                                      
92.094    1   ?       ? ?                 ? 
7 water       nat water                                                                                                         
18.015    639 ?       ? ?                 ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'DNA topoisomerase II,alpha isozyme' 
# 
_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       
;SNASVERIYQKKTQLEHILLRPDTYIGSVELVTQQMWVYDEDVGINYREVTFVPGLYKIFDEILVNAADNKQRDPKMSCI
RVTIDPENNLISIWNNGKGIPVVEHKVEKMYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVETASRE
YKKMFKQTWMDNMGRAGEMELKPFNGEDYTCITFQPDLSKFKMQSLDKDIVALMVRRAYDIAGSTKDVKVFLNGNKLPVK
GFRSYVDMYLKDKLDETGNSLKVIHEQVNHRWEVCLTMSEKGFQQISFVNSIATSKGGRHVDYVADQIVTKLVDVVKKKN
KGGVAVKAHQVKNHMWIFVNALIENPTFDSQTKENMTLQPKSFGSTCQLSEKFIKAAIGCGIVESILNWVKFKAQVQLN
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SNASVERIYQKKTQLEHILLRPDTYIGSVELVTQQMWVYDEDVGINYREVTFVPGLYKIFDEILVNAADNKQRDPKMSCI
RVTIDPENNLISIWNNGKGIPVVEHKVEKMYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVETASRE
YKKMFKQTWMDNMGRAGEMELKPFNGEDYTCITFQPDLSKFKMQSLDKDIVALMVRRAYDIAGSTKDVKVFLNGNKLPVK
GFRSYVDMYLKDKLDETGNSLKVIHEQVNHRWEVCLTMSEKGFQQISFVNSIATSKGGRHVDYVADQIVTKLVDVVKKKN
KGGVAVKAHQVKNHMWIFVNALIENPTFDSQTKENMTLQPKSFGSTCQLSEKFIKAAIGCGIVESILNWVKFKAQVQLN
;
_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 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER'                                                                 ANP   
3 'MAGNESIUM ION'                                                                                               MG    
4 '8-(3,4-dihydroquinoline-1(2H)-carbonyl)-7-[2-(4-methylpiperazin-1-yl)ethoxy]-4-propyl-2H-1-benzopyran-2-one' A1ASC 
5 'CHLORIDE ION'                                                                                                CL    
6 GLYCEROL                                                                                                      GOL   
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   ASN n 
1 3   ALA n 
1 4   SER n 
1 5   VAL n 
1 6   GLU n 
1 7   ARG n 
1 8   ILE n 
1 9   TYR n 
1 10  GLN n 
1 11  LYS n 
1 12  LYS n 
1 13  THR n 
1 14  GLN n 
1 15  LEU n 
1 16  GLU n 
1 17  HIS n 
1 18  ILE n 
1 19  LEU n 
1 20  LEU n 
1 21  ARG n 
1 22  PRO n 
1 23  ASP n 
1 24  THR n 
1 25  TYR n 
1 26  ILE n 
1 27  GLY n 
1 28  SER n 
1 29  VAL n 
1 30  GLU n 
1 31  LEU n 
1 32  VAL n 
1 33  THR n 
1 34  GLN n 
1 35  GLN n 
1 36  MET n 
1 37  TRP n 
1 38  VAL n 
1 39  TYR n 
1 40  ASP n 
1 41  GLU n 
1 42  ASP n 
1 43  VAL n 
1 44  GLY n 
1 45  ILE n 
1 46  ASN n 
1 47  TYR n 
1 48  ARG n 
1 49  GLU n 
1 50  VAL n 
1 51  THR n 
1 52  PHE n 
1 53  VAL n 
1 54  PRO n 
1 55  GLY n 
1 56  LEU n 
1 57  TYR n 
1 58  LYS n 
1 59  ILE n 
1 60  PHE n 
1 61  ASP n 
1 62  GLU n 
1 63  ILE n 
1 64  LEU n 
1 65  VAL n 
1 66  ASN n 
1 67  ALA n 
1 68  ALA n 
1 69  ASP n 
1 70  ASN n 
1 71  LYS n 
1 72  GLN n 
1 73  ARG n 
1 74  ASP n 
1 75  PRO n 
1 76  LYS n 
1 77  MET n 
1 78  SER n 
1 79  CYS n 
1 80  ILE n 
1 81  ARG n 
1 82  VAL n 
1 83  THR n 
1 84  ILE n 
1 85  ASP n 
1 86  PRO n 
1 87  GLU n 
1 88  ASN n 
1 89  ASN n 
1 90  LEU n 
1 91  ILE n 
1 92  SER n 
1 93  ILE n 
1 94  TRP n 
1 95  ASN n 
1 96  ASN n 
1 97  GLY n 
1 98  LYS n 
1 99  GLY n 
1 100 ILE n 
1 101 PRO n 
1 102 VAL n 
1 103 VAL n 
1 104 GLU n 
1 105 HIS n 
1 106 LYS n 
1 107 VAL n 
1 108 GLU n 
1 109 LYS n 
1 110 MET n 
1 111 TYR n 
1 112 VAL n 
1 113 PRO n 
1 114 ALA n 
1 115 LEU n 
1 116 ILE n 
1 117 PHE n 
1 118 GLY n 
1 119 GLN n 
1 120 LEU n 
1 121 LEU n 
1 122 THR n 
1 123 SER n 
1 124 SER n 
1 125 ASN n 
1 126 TYR n 
1 127 ASP n 
1 128 ASP n 
1 129 ASP n 
1 130 GLU n 
1 131 LYS n 
1 132 LYS n 
1 133 VAL n 
1 134 THR n 
1 135 GLY n 
1 136 GLY n 
1 137 ARG n 
1 138 ASN n 
1 139 GLY n 
1 140 TYR n 
1 141 GLY n 
1 142 ALA n 
1 143 LYS n 
1 144 LEU n 
1 145 CYS n 
1 146 ASN n 
1 147 ILE n 
1 148 PHE n 
1 149 SER n 
1 150 THR n 
1 151 LYS n 
1 152 PHE n 
1 153 THR n 
1 154 VAL n 
1 155 GLU n 
1 156 THR n 
1 157 ALA n 
1 158 SER n 
1 159 ARG n 
1 160 GLU n 
1 161 TYR n 
1 162 LYS n 
1 163 LYS n 
1 164 MET n 
1 165 PHE n 
1 166 LYS n 
1 167 GLN n 
1 168 THR n 
1 169 TRP n 
1 170 MET n 
1 171 ASP n 
1 172 ASN n 
1 173 MET n 
1 174 GLY n 
1 175 ARG n 
1 176 ALA n 
1 177 GLY n 
1 178 GLU n 
1 179 MET n 
1 180 GLU n 
1 181 LEU n 
1 182 LYS n 
1 183 PRO n 
1 184 PHE n 
1 185 ASN n 
1 186 GLY n 
1 187 GLU n 
1 188 ASP n 
1 189 TYR n 
1 190 THR n 
1 191 CYS n 
1 192 ILE n 
1 193 THR n 
1 194 PHE n 
1 195 GLN n 
1 196 PRO n 
1 197 ASP n 
1 198 LEU n 
1 199 SER n 
1 200 LYS n 
1 201 PHE n 
1 202 LYS n 
1 203 MET n 
1 204 GLN n 
1 205 SER n 
1 206 LEU n 
1 207 ASP n 
1 208 LYS n 
1 209 ASP n 
1 210 ILE n 
1 211 VAL n 
1 212 ALA n 
1 213 LEU n 
1 214 MET n 
1 215 VAL n 
1 216 ARG n 
1 217 ARG n 
1 218 ALA n 
1 219 TYR n 
1 220 ASP n 
1 221 ILE n 
1 222 ALA n 
1 223 GLY n 
1 224 SER n 
1 225 THR n 
1 226 LYS n 
1 227 ASP n 
1 228 VAL n 
1 229 LYS n 
1 230 VAL n 
1 231 PHE n 
1 232 LEU n 
1 233 ASN n 
1 234 GLY n 
1 235 ASN n 
1 236 LYS n 
1 237 LEU n 
1 238 PRO n 
1 239 VAL n 
1 240 LYS n 
1 241 GLY n 
1 242 PHE n 
1 243 ARG n 
1 244 SER n 
1 245 TYR n 
1 246 VAL n 
1 247 ASP n 
1 248 MET n 
1 249 TYR n 
1 250 LEU n 
1 251 LYS n 
1 252 ASP n 
1 253 LYS n 
1 254 LEU n 
1 255 ASP n 
1 256 GLU n 
1 257 THR n 
1 258 GLY n 
1 259 ASN n 
1 260 SER n 
1 261 LEU n 
1 262 LYS n 
1 263 VAL n 
1 264 ILE n 
1 265 HIS n 
1 266 GLU n 
1 267 GLN n 
1 268 VAL n 
1 269 ASN n 
1 270 HIS n 
1 271 ARG n 
1 272 TRP n 
1 273 GLU n 
1 274 VAL n 
1 275 CYS n 
1 276 LEU n 
1 277 THR n 
1 278 MET n 
1 279 SER n 
1 280 GLU n 
1 281 LYS n 
1 282 GLY n 
1 283 PHE n 
1 284 GLN n 
1 285 GLN n 
1 286 ILE n 
1 287 SER n 
1 288 PHE n 
1 289 VAL n 
1 290 ASN n 
1 291 SER n 
1 292 ILE n 
1 293 ALA n 
1 294 THR n 
1 295 SER n 
1 296 LYS n 
1 297 GLY n 
1 298 GLY n 
1 299 ARG n 
1 300 HIS n 
1 301 VAL n 
1 302 ASP n 
1 303 TYR n 
1 304 VAL n 
1 305 ALA n 
1 306 ASP n 
1 307 GLN n 
1 308 ILE n 
1 309 VAL n 
1 310 THR n 
1 311 LYS n 
1 312 LEU n 
1 313 VAL n 
1 314 ASP n 
1 315 VAL n 
1 316 VAL n 
1 317 LYS n 
1 318 LYS n 
1 319 LYS n 
1 320 ASN n 
1 321 LYS n 
1 322 GLY n 
1 323 GLY n 
1 324 VAL n 
1 325 ALA n 
1 326 VAL n 
1 327 LYS n 
1 328 ALA n 
1 329 HIS n 
1 330 GLN n 
1 331 VAL n 
1 332 LYS n 
1 333 ASN n 
1 334 HIS n 
1 335 MET n 
1 336 TRP n 
1 337 ILE n 
1 338 PHE n 
1 339 VAL n 
1 340 ASN n 
1 341 ALA n 
1 342 LEU n 
1 343 ILE n 
1 344 GLU n 
1 345 ASN n 
1 346 PRO n 
1 347 THR n 
1 348 PHE n 
1 349 ASP n 
1 350 SER n 
1 351 GLN n 
1 352 THR n 
1 353 LYS n 
1 354 GLU n 
1 355 ASN n 
1 356 MET n 
1 357 THR n 
1 358 LEU n 
1 359 GLN n 
1 360 PRO n 
1 361 LYS n 
1 362 SER n 
1 363 PHE n 
1 364 GLY n 
1 365 SER n 
1 366 THR n 
1 367 CYS n 
1 368 GLN n 
1 369 LEU n 
1 370 SER n 
1 371 GLU n 
1 372 LYS n 
1 373 PHE n 
1 374 ILE n 
1 375 LYS n 
1 376 ALA n 
1 377 ALA n 
1 378 ILE n 
1 379 GLY n 
1 380 CYS n 
1 381 GLY n 
1 382 ILE n 
1 383 VAL n 
1 384 GLU n 
1 385 SER n 
1 386 ILE n 
1 387 LEU n 
1 388 ASN n 
1 389 TRP n 
1 390 VAL n 
1 391 LYS n 
1 392 PHE n 
1 393 LYS n 
1 394 ALA n 
1 395 GLN n 
1 396 VAL n 
1 397 GLN n 
1 398 LEU n 
1 399 ASN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   399 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'TOP2A, TOP2' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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                   ? 
# 
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 
A1ASC non-polymer         . 
'8-(3,4-dihydroquinoline-1(2H)-carbonyl)-7-[2-(4-methylpiperazin-1-yl)ethoxy]-4-propyl-2H-1-benzopyran-2-one' topobexin 
'C29 H35 N3 O4'     489.606 
ALA   'L-peptide linking' y ALANINE ?                               'C3 H7 N O2'        89.093  
ANP   non-polymer         . 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' ?                               'C10 H17 N6 O12 P3' 
506.196 
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 
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  
GOL   non-polymer         . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'          92.094  
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 
MG    non-polymer         . 'MAGNESIUM ION' ?                               'Mg 2'              24.305  
PHE   'L-peptide linking' y PHENYLALANINE ?                               'C9 H11 N O2'       165.189 
PRO   'L-peptide linking' y PROLINE ?                               'C5 H9 N O2'        115.130 
SER   'L-peptide linking' y SERINE ?                               'C3 H7 N O3'        105.093 
THR   'L-peptide linking' y THREONINE ?                               'C4 H9 N O3'        119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ?                               'C11 H12 N2 O2'     204.225 
TYR   'L-peptide linking' y TYROSINE ?                               'C9 H11 N O3'       181.189 
VAL   'L-peptide linking' y VALINE ?                               'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   26  ?   ?   ?   A . n 
A 1 2   ASN 2   27  ?   ?   ?   A . n 
A 1 3   ALA 3   28  28  ALA ALA A . n 
A 1 4   SER 4   29  29  SER SER A . n 
A 1 5   VAL 5   30  30  VAL VAL A . n 
A 1 6   GLU 6   31  31  GLU GLU A . n 
A 1 7   ARG 7   32  32  ARG ARG A . n 
A 1 8   ILE 8   33  33  ILE ILE A . n 
A 1 9   TYR 9   34  34  TYR TYR A . n 
A 1 10  GLN 10  35  35  GLN GLN A . n 
A 1 11  LYS 11  36  36  LYS LYS A . n 
A 1 12  LYS 12  37  37  LYS LYS A . n 
A 1 13  THR 13  38  38  THR THR A . n 
A 1 14  GLN 14  39  39  GLN GLN A . n 
A 1 15  LEU 15  40  40  LEU LEU A . n 
A 1 16  GLU 16  41  41  GLU GLU A . n 
A 1 17  HIS 17  42  42  HIS HIS A . n 
A 1 18  ILE 18  43  43  ILE ILE A . n 
A 1 19  LEU 19  44  44  LEU LEU A . n 
A 1 20  LEU 20  45  45  LEU LEU A . n 
A 1 21  ARG 21  46  46  ARG ARG A . n 
A 1 22  PRO 22  47  47  PRO PRO A . n 
A 1 23  ASP 23  48  48  ASP ASP A . n 
A 1 24  THR 24  49  49  THR THR A . n 
A 1 25  TYR 25  50  50  TYR TYR A . n 
A 1 26  ILE 26  51  51  ILE ILE A . n 
A 1 27  GLY 27  52  52  GLY GLY A . n 
A 1 28  SER 28  53  53  SER SER A . n 
A 1 29  VAL 29  54  54  VAL VAL A . n 
A 1 30  GLU 30  55  55  GLU GLU A . n 
A 1 31  LEU 31  56  56  LEU LEU A . n 
A 1 32  VAL 32  57  57  VAL VAL A . n 
A 1 33  THR 33  58  58  THR THR A . n 
A 1 34  GLN 34  59  59  GLN GLN A . n 
A 1 35  GLN 35  60  60  GLN GLN A . n 
A 1 36  MET 36  61  61  MET MET A . n 
A 1 37  TRP 37  62  62  TRP TRP A . n 
A 1 38  VAL 38  63  63  VAL VAL A . n 
A 1 39  TYR 39  64  64  TYR TYR A . n 
A 1 40  ASP 40  65  65  ASP ASP A . n 
A 1 41  GLU 41  66  66  GLU GLU A . n 
A 1 42  ASP 42  67  67  ASP ASP A . n 
A 1 43  VAL 43  68  68  VAL VAL A . n 
A 1 44  GLY 44  69  69  GLY GLY A . n 
A 1 45  ILE 45  70  70  ILE ILE A . n 
A 1 46  ASN 46  71  71  ASN ASN A . n 
A 1 47  TYR 47  72  72  TYR TYR A . n 
A 1 48  ARG 48  73  73  ARG ARG A . n 
A 1 49  GLU 49  74  74  GLU GLU A . n 
A 1 50  VAL 50  75  75  VAL VAL A . n 
A 1 51  THR 51  76  76  THR THR A . n 
A 1 52  PHE 52  77  77  PHE PHE A . n 
A 1 53  VAL 53  78  78  VAL VAL A . n 
A 1 54  PRO 54  79  79  PRO PRO A . n 
A 1 55  GLY 55  80  80  GLY GLY A . n 
A 1 56  LEU 56  81  81  LEU LEU A . n 
A 1 57  TYR 57  82  82  TYR TYR A . n 
A 1 58  LYS 58  83  83  LYS LYS A . n 
A 1 59  ILE 59  84  84  ILE ILE A . n 
A 1 60  PHE 60  85  85  PHE PHE A . n 
A 1 61  ASP 61  86  86  ASP ASP A . n 
A 1 62  GLU 62  87  87  GLU GLU A . n 
A 1 63  ILE 63  88  88  ILE ILE A . n 
A 1 64  LEU 64  89  89  LEU LEU A . n 
A 1 65  VAL 65  90  90  VAL VAL A . n 
A 1 66  ASN 66  91  91  ASN ASN A . n 
A 1 67  ALA 67  92  92  ALA ALA A . n 
A 1 68  ALA 68  93  93  ALA ALA A . n 
A 1 69  ASP 69  94  94  ASP ASP A . n 
A 1 70  ASN 70  95  95  ASN ASN A . n 
A 1 71  LYS 71  96  96  LYS LYS A . n 
A 1 72  GLN 72  97  97  GLN GLN A . n 
A 1 73  ARG 73  98  98  ARG ARG A . n 
A 1 74  ASP 74  99  99  ASP ASP A . n 
A 1 75  PRO 75  100 100 PRO PRO A . n 
A 1 76  LYS 76  101 101 LYS LYS A . n 
A 1 77  MET 77  102 102 MET MET A . n 
A 1 78  SER 78  103 103 SER SER A . n 
A 1 79  CYS 79  104 104 CYS CYS A . n 
A 1 80  ILE 80  105 105 ILE ILE A . n 
A 1 81  ARG 81  106 106 ARG ARG A . n 
A 1 82  VAL 82  107 107 VAL VAL A . n 
A 1 83  THR 83  108 108 THR THR A . n 
A 1 84  ILE 84  109 109 ILE ILE A . n 
A 1 85  ASP 85  110 110 ASP ASP A . n 
A 1 86  PRO 86  111 111 PRO PRO A . n 
A 1 87  GLU 87  112 112 GLU GLU A . n 
A 1 88  ASN 88  113 113 ASN ASN A . n 
A 1 89  ASN 89  114 114 ASN ASN A . n 
A 1 90  LEU 90  115 115 LEU LEU A . n 
A 1 91  ILE 91  116 116 ILE ILE A . n 
A 1 92  SER 92  117 117 SER SER A . n 
A 1 93  ILE 93  118 118 ILE ILE A . n 
A 1 94  TRP 94  119 119 TRP TRP A . n 
A 1 95  ASN 95  120 120 ASN ASN A . n 
A 1 96  ASN 96  121 121 ASN ASN A . n 
A 1 97  GLY 97  122 122 GLY GLY A . n 
A 1 98  LYS 98  123 123 LYS LYS A . n 
A 1 99  GLY 99  124 124 GLY GLY A . n 
A 1 100 ILE 100 125 125 ILE ILE A . n 
A 1 101 PRO 101 126 126 PRO PRO A . n 
A 1 102 VAL 102 127 127 VAL VAL A . n 
A 1 103 VAL 103 128 128 VAL VAL A . n 
A 1 104 GLU 104 129 129 GLU GLU A . n 
A 1 105 HIS 105 130 130 HIS HIS A . n 
A 1 106 LYS 106 131 131 LYS LYS A . n 
A 1 107 VAL 107 132 132 VAL VAL A . n 
A 1 108 GLU 108 133 133 GLU GLU A . n 
A 1 109 LYS 109 134 134 LYS LYS A . n 
A 1 110 MET 110 135 135 MET MET A . n 
A 1 111 TYR 111 136 136 TYR TYR A . n 
A 1 112 VAL 112 137 137 VAL VAL A . n 
A 1 113 PRO 113 138 138 PRO PRO A . n 
A 1 114 ALA 114 139 139 ALA ALA A . n 
A 1 115 LEU 115 140 140 LEU LEU A . n 
A 1 116 ILE 116 141 141 ILE ILE A . n 
A 1 117 PHE 117 142 142 PHE PHE A . n 
A 1 118 GLY 118 143 143 GLY GLY A . n 
A 1 119 GLN 119 144 144 GLN GLN A . n 
A 1 120 LEU 120 145 145 LEU LEU A . n 
A 1 121 LEU 121 146 146 LEU LEU A . n 
A 1 122 THR 122 147 147 THR THR A . n 
A 1 123 SER 123 148 148 SER SER A . n 
A 1 124 SER 124 149 149 SER SER A . n 
A 1 125 ASN 125 150 150 ASN ASN A . n 
A 1 126 TYR 126 151 151 TYR TYR A . n 
A 1 127 ASP 127 152 152 ASP ASP A . n 
A 1 128 ASP 128 153 153 ASP ASP A . n 
A 1 129 ASP 129 154 154 ASP ASP A . n 
A 1 130 GLU 130 155 155 GLU GLU A . n 
A 1 131 LYS 131 156 156 LYS LYS A . n 
A 1 132 LYS 132 157 157 LYS LYS A . n 
A 1 133 VAL 133 158 158 VAL VAL A . n 
A 1 134 THR 134 159 159 THR THR A . n 
A 1 135 GLY 135 160 160 GLY GLY A . n 
A 1 136 GLY 136 161 161 GLY GLY A . n 
A 1 137 ARG 137 162 162 ARG ARG A . n 
A 1 138 ASN 138 163 163 ASN ASN A . n 
A 1 139 GLY 139 164 164 GLY GLY A . n 
A 1 140 TYR 140 165 165 TYR TYR A . n 
A 1 141 GLY 141 166 166 GLY GLY A . n 
A 1 142 ALA 142 167 167 ALA ALA A . n 
A 1 143 LYS 143 168 168 LYS LYS A . n 
A 1 144 LEU 144 169 169 LEU LEU A . n 
A 1 145 CYS 145 170 170 CYS CYS A . n 
A 1 146 ASN 146 171 171 ASN ASN A . n 
A 1 147 ILE 147 172 172 ILE ILE A . n 
A 1 148 PHE 148 173 173 PHE PHE A . n 
A 1 149 SER 149 174 174 SER SER A . n 
A 1 150 THR 150 175 175 THR THR A . n 
A 1 151 LYS 151 176 176 LYS LYS A . n 
A 1 152 PHE 152 177 177 PHE PHE A . n 
A 1 153 THR 153 178 178 THR THR A . n 
A 1 154 VAL 154 179 179 VAL VAL A . n 
A 1 155 GLU 155 180 180 GLU GLU A . n 
A 1 156 THR 156 181 181 THR THR A . n 
A 1 157 ALA 157 182 182 ALA ALA A . n 
A 1 158 SER 158 183 183 SER SER A . n 
A 1 159 ARG 159 184 184 ARG ARG A . n 
A 1 160 GLU 160 185 185 GLU GLU A . n 
A 1 161 TYR 161 186 186 TYR TYR A . n 
A 1 162 LYS 162 187 187 LYS LYS A . n 
A 1 163 LYS 163 188 188 LYS LYS A . n 
A 1 164 MET 164 189 189 MET MET A . n 
A 1 165 PHE 165 190 190 PHE PHE A . n 
A 1 166 LYS 166 191 191 LYS LYS A . n 
A 1 167 GLN 167 192 192 GLN GLN A . n 
A 1 168 THR 168 193 193 THR THR A . n 
A 1 169 TRP 169 194 194 TRP TRP A . n 
A 1 170 MET 170 195 195 MET MET A . n 
A 1 171 ASP 171 196 196 ASP ASP A . n 
A 1 172 ASN 172 197 197 ASN ASN A . n 
A 1 173 MET 173 198 198 MET MET A . n 
A 1 174 GLY 174 199 199 GLY GLY A . n 
A 1 175 ARG 175 200 200 ARG ARG A . n 
A 1 176 ALA 176 201 201 ALA ALA A . n 
A 1 177 GLY 177 202 202 GLY GLY A . n 
A 1 178 GLU 178 203 203 GLU GLU A . n 
A 1 179 MET 179 204 204 MET MET A . n 
A 1 180 GLU 180 205 205 GLU GLU A . n 
A 1 181 LEU 181 206 206 LEU LEU A . n 
A 1 182 LYS 182 207 207 LYS LYS A . n 
A 1 183 PRO 183 208 208 PRO PRO A . n 
A 1 184 PHE 184 209 209 PHE PHE A . n 
A 1 185 ASN 185 210 210 ASN ASN A . n 
A 1 186 GLY 186 211 211 GLY GLY A . n 
A 1 187 GLU 187 212 212 GLU GLU A . n 
A 1 188 ASP 188 213 213 ASP ASP A . n 
A 1 189 TYR 189 214 214 TYR TYR A . n 
A 1 190 THR 190 215 215 THR THR A . n 
A 1 191 CYS 191 216 216 CYS CYS A . n 
A 1 192 ILE 192 217 217 ILE ILE A . n 
A 1 193 THR 193 218 218 THR THR A . n 
A 1 194 PHE 194 219 219 PHE PHE A . n 
A 1 195 GLN 195 220 220 GLN GLN A . n 
A 1 196 PRO 196 221 221 PRO PRO A . n 
A 1 197 ASP 197 222 222 ASP ASP A . n 
A 1 198 LEU 198 223 223 LEU LEU A . n 
A 1 199 SER 199 224 224 SER SER A . n 
A 1 200 LYS 200 225 225 LYS LYS A . n 
A 1 201 PHE 201 226 226 PHE PHE A . n 
A 1 202 LYS 202 227 227 LYS LYS A . n 
A 1 203 MET 203 228 228 MET MET A . n 
A 1 204 GLN 204 229 229 GLN GLN A . n 
A 1 205 SER 205 230 230 SER SER A . n 
A 1 206 LEU 206 231 231 LEU LEU A . n 
A 1 207 ASP 207 232 232 ASP ASP A . n 
A 1 208 LYS 208 233 233 LYS LYS A . n 
A 1 209 ASP 209 234 234 ASP ASP A . n 
A 1 210 ILE 210 235 235 ILE ILE A . n 
A 1 211 VAL 211 236 236 VAL VAL A . n 
A 1 212 ALA 212 237 237 ALA ALA A . n 
A 1 213 LEU 213 238 238 LEU LEU A . n 
A 1 214 MET 214 239 239 MET MET A . n 
A 1 215 VAL 215 240 240 VAL VAL A . n 
A 1 216 ARG 216 241 241 ARG ARG A . n 
A 1 217 ARG 217 242 242 ARG ARG A . n 
A 1 218 ALA 218 243 243 ALA ALA A . n 
A 1 219 TYR 219 244 244 TYR TYR A . n 
A 1 220 ASP 220 245 245 ASP ASP A . n 
A 1 221 ILE 221 246 246 ILE ILE A . n 
A 1 222 ALA 222 247 247 ALA ALA A . n 
A 1 223 GLY 223 248 248 GLY GLY A . n 
A 1 224 SER 224 249 249 SER SER A . n 
A 1 225 THR 225 250 250 THR THR A . n 
A 1 226 LYS 226 251 251 LYS LYS A . n 
A 1 227 ASP 227 252 252 ASP ASP A . n 
A 1 228 VAL 228 253 253 VAL VAL A . n 
A 1 229 LYS 229 254 254 LYS LYS A . n 
A 1 230 VAL 230 255 255 VAL VAL A . n 
A 1 231 PHE 231 256 256 PHE PHE A . n 
A 1 232 LEU 232 257 257 LEU LEU A . n 
A 1 233 ASN 233 258 258 ASN ASN A . n 
A 1 234 GLY 234 259 259 GLY GLY A . n 
A 1 235 ASN 235 260 260 ASN ASN A . n 
A 1 236 LYS 236 261 261 LYS LYS A . n 
A 1 237 LEU 237 262 262 LEU LEU A . n 
A 1 238 PRO 238 263 263 PRO PRO A . n 
A 1 239 VAL 239 264 264 VAL VAL A . n 
A 1 240 LYS 240 265 265 LYS LYS A . n 
A 1 241 GLY 241 266 266 GLY GLY A . n 
A 1 242 PHE 242 267 267 PHE PHE A . n 
A 1 243 ARG 243 268 268 ARG ARG A . n 
A 1 244 SER 244 269 269 SER SER A . n 
A 1 245 TYR 245 270 270 TYR TYR A . n 
A 1 246 VAL 246 271 271 VAL VAL A . n 
A 1 247 ASP 247 272 272 ASP ASP A . n 
A 1 248 MET 248 273 273 MET MET A . n 
A 1 249 TYR 249 274 274 TYR TYR A . n 
A 1 250 LEU 250 275 275 LEU LEU A . n 
A 1 251 LYS 251 276 276 LYS LYS A . n 
A 1 252 ASP 252 277 277 ASP ASP A . n 
A 1 253 LYS 253 278 278 LYS LYS A . n 
A 1 254 LEU 254 279 279 LEU LEU A . n 
A 1 255 ASP 255 280 280 ASP ASP A . n 
A 1 256 GLU 256 281 281 GLU GLU A . n 
A 1 257 THR 257 282 282 THR THR A . n 
A 1 258 GLY 258 283 283 GLY GLY A . n 
A 1 259 ASN 259 284 284 ASN ASN A . n 
A 1 260 SER 260 285 285 SER SER A . n 
A 1 261 LEU 261 286 286 LEU LEU A . n 
A 1 262 LYS 262 287 287 LYS LYS A . n 
A 1 263 VAL 263 288 288 VAL VAL A . n 
A 1 264 ILE 264 289 289 ILE ILE A . n 
A 1 265 HIS 265 290 290 HIS HIS A . n 
A 1 266 GLU 266 291 291 GLU GLU A . n 
A 1 267 GLN 267 292 292 GLN GLN A . n 
A 1 268 VAL 268 293 293 VAL VAL A . n 
A 1 269 ASN 269 294 294 ASN ASN A . n 
A 1 270 HIS 270 295 295 HIS HIS A . n 
A 1 271 ARG 271 296 296 ARG ARG A . n 
A 1 272 TRP 272 297 297 TRP TRP A . n 
A 1 273 GLU 273 298 298 GLU GLU A . n 
A 1 274 VAL 274 299 299 VAL VAL A . n 
A 1 275 CYS 275 300 300 CYS CYS A . n 
A 1 276 LEU 276 301 301 LEU LEU A . n 
A 1 277 THR 277 302 302 THR THR A . n 
A 1 278 MET 278 303 303 MET MET A . n 
A 1 279 SER 279 304 304 SER SER A . n 
A 1 280 GLU 280 305 305 GLU GLU A . n 
A 1 281 LYS 281 306 306 LYS LYS A . n 
A 1 282 GLY 282 307 307 GLY GLY A . n 
A 1 283 PHE 283 308 308 PHE PHE A . n 
A 1 284 GLN 284 309 309 GLN GLN A . n 
A 1 285 GLN 285 310 310 GLN GLN A . n 
A 1 286 ILE 286 311 311 ILE ILE A . n 
A 1 287 SER 287 312 312 SER SER A . n 
A 1 288 PHE 288 313 313 PHE PHE A . n 
A 1 289 VAL 289 314 314 VAL VAL A . n 
A 1 290 ASN 290 315 315 ASN ASN A . n 
A 1 291 SER 291 316 316 SER SER A . n 
A 1 292 ILE 292 317 317 ILE ILE A . n 
A 1 293 ALA 293 318 318 ALA ALA A . n 
A 1 294 THR 294 319 319 THR THR A . n 
A 1 295 SER 295 320 320 SER SER A . n 
A 1 296 LYS 296 321 321 LYS LYS A . n 
A 1 297 GLY 297 322 322 GLY GLY A . n 
A 1 298 GLY 298 323 323 GLY GLY A . n 
A 1 299 ARG 299 324 324 ARG ARG A . n 
A 1 300 HIS 300 325 325 HIS HIS A . n 
A 1 301 VAL 301 326 326 VAL VAL A . n 
A 1 302 ASP 302 327 327 ASP ASP A . n 
A 1 303 TYR 303 328 328 TYR TYR A . n 
A 1 304 VAL 304 329 329 VAL VAL A . n 
A 1 305 ALA 305 330 330 ALA ALA A . n 
A 1 306 ASP 306 331 331 ASP ASP A . n 
A 1 307 GLN 307 332 332 GLN GLN A . n 
A 1 308 ILE 308 333 333 ILE ILE A . n 
A 1 309 VAL 309 334 334 VAL VAL A . n 
A 1 310 THR 310 335 335 THR THR A . n 
A 1 311 LYS 311 336 336 LYS LYS A . n 
A 1 312 LEU 312 337 337 LEU LEU A . n 
A 1 313 VAL 313 338 338 VAL VAL A . n 
A 1 314 ASP 314 339 339 ASP ASP A . n 
A 1 315 VAL 315 340 340 VAL VAL A . n 
A 1 316 VAL 316 341 341 VAL VAL A . n 
A 1 317 LYS 317 342 342 LYS LYS A . n 
A 1 318 LYS 318 343 343 LYS LYS A . n 
A 1 319 LYS 319 344 344 LYS LYS A . n 
A 1 320 ASN 320 345 345 ASN ASN A . n 
A 1 321 LYS 321 346 ?   ?   ?   A . n 
A 1 322 GLY 322 347 ?   ?   ?   A . n 
A 1 323 GLY 323 348 ?   ?   ?   A . n 
A 1 324 VAL 324 349 ?   ?   ?   A . n 
A 1 325 ALA 325 350 350 ALA ALA A . n 
A 1 326 VAL 326 351 351 VAL VAL A . n 
A 1 327 LYS 327 352 352 LYS LYS A . n 
A 1 328 ALA 328 353 353 ALA ALA A . n 
A 1 329 HIS 329 354 354 HIS HIS A . n 
A 1 330 GLN 330 355 355 GLN GLN A . n 
A 1 331 VAL 331 356 356 VAL VAL A . n 
A 1 332 LYS 332 357 357 LYS LYS A . n 
A 1 333 ASN 333 358 358 ASN ASN A . n 
A 1 334 HIS 334 359 359 HIS HIS A . n 
A 1 335 MET 335 360 360 MET MET A . n 
A 1 336 TRP 336 361 361 TRP TRP A . n 
A 1 337 ILE 337 362 362 ILE ILE A . n 
A 1 338 PHE 338 363 363 PHE PHE A . n 
A 1 339 VAL 339 364 364 VAL VAL A . n 
A 1 340 ASN 340 365 365 ASN ASN A . n 
A 1 341 ALA 341 366 366 ALA ALA A . n 
A 1 342 LEU 342 367 367 LEU LEU A . n 
A 1 343 ILE 343 368 368 ILE ILE A . n 
A 1 344 GLU 344 369 369 GLU GLU A . n 
A 1 345 ASN 345 370 370 ASN ASN A . n 
A 1 346 PRO 346 371 371 PRO PRO A . n 
A 1 347 THR 347 372 372 THR THR A . n 
A 1 348 PHE 348 373 373 PHE PHE A . n 
A 1 349 ASP 349 374 374 ASP ASP A . n 
A 1 350 SER 350 375 375 SER SER A . n 
A 1 351 GLN 351 376 376 GLN GLN A . n 
A 1 352 THR 352 377 377 THR THR A . n 
A 1 353 LYS 353 378 378 LYS LYS A . n 
A 1 354 GLU 354 379 379 GLU GLU A . n 
A 1 355 ASN 355 380 380 ASN ASN A . n 
A 1 356 MET 356 381 381 MET MET A . n 
A 1 357 THR 357 382 382 THR THR A . n 
A 1 358 LEU 358 383 383 LEU LEU A . n 
A 1 359 GLN 359 384 384 GLN GLN A . n 
A 1 360 PRO 360 385 385 PRO PRO A . n 
A 1 361 LYS 361 386 386 LYS LYS A . n 
A 1 362 SER 362 387 387 SER SER A . n 
A 1 363 PHE 363 388 388 PHE PHE A . n 
A 1 364 GLY 364 389 389 GLY GLY A . n 
A 1 365 SER 365 390 390 SER SER A . n 
A 1 366 THR 366 391 391 THR THR A . n 
A 1 367 CYS 367 392 392 CYS CYS A . n 
A 1 368 GLN 368 393 393 GLN GLN A . n 
A 1 369 LEU 369 394 394 LEU LEU A . n 
A 1 370 SER 370 395 395 SER SER A . n 
A 1 371 GLU 371 396 396 GLU GLU A . n 
A 1 372 LYS 372 397 397 LYS LYS A . n 
A 1 373 PHE 373 398 398 PHE PHE A . n 
A 1 374 ILE 374 399 399 ILE ILE A . n 
A 1 375 LYS 375 400 400 LYS LYS A . n 
A 1 376 ALA 376 401 401 ALA ALA A . n 
A 1 377 ALA 377 402 402 ALA ALA A . n 
A 1 378 ILE 378 403 403 ILE ILE A . n 
A 1 379 GLY 379 404 404 GLY GLY A . n 
A 1 380 CYS 380 405 405 CYS CYS A . n 
A 1 381 GLY 381 406 406 GLY GLY A . n 
A 1 382 ILE 382 407 407 ILE ILE A . n 
A 1 383 VAL 383 408 408 VAL VAL A . n 
A 1 384 GLU 384 409 409 GLU GLU A . n 
A 1 385 SER 385 410 410 SER SER A . n 
A 1 386 ILE 386 411 411 ILE ILE A . n 
A 1 387 LEU 387 412 412 LEU LEU A . n 
A 1 388 ASN 388 413 413 ASN ASN A . n 
A 1 389 TRP 389 414 414 TRP TRP A . n 
A 1 390 VAL 390 415 415 VAL VAL A . n 
A 1 391 LYS 391 416 416 LYS LYS A . n 
A 1 392 PHE 392 417 417 PHE PHE A . n 
A 1 393 LYS 393 418 ?   ?   ?   A . n 
A 1 394 ALA 394 419 ?   ?   ?   A . n 
A 1 395 GLN 395 420 ?   ?   ?   A . n 
A 1 396 VAL 396 421 ?   ?   ?   A . n 
A 1 397 GLN 397 422 ?   ?   ?   A . n 
A 1 398 LEU 398 423 ?   ?   ?   A . n 
A 1 399 ASN 399 424 ?   ?   ?   A . n 
B 1 1   SER 1   26  ?   ?   ?   B . n 
B 1 2   ASN 2   27  ?   ?   ?   B . n 
B 1 3   ALA 3   28  28  ALA ALA B . n 
B 1 4   SER 4   29  29  SER SER B . n 
B 1 5   VAL 5   30  30  VAL VAL B . n 
B 1 6   GLU 6   31  31  GLU GLU B . n 
B 1 7   ARG 7   32  32  ARG ARG B . n 
B 1 8   ILE 8   33  33  ILE ILE B . n 
B 1 9   TYR 9   34  34  TYR TYR B . n 
B 1 10  GLN 10  35  35  GLN GLN B . n 
B 1 11  LYS 11  36  36  LYS LYS B . n 
B 1 12  LYS 12  37  37  LYS LYS B . n 
B 1 13  THR 13  38  38  THR THR B . n 
B 1 14  GLN 14  39  39  GLN GLN B . n 
B 1 15  LEU 15  40  40  LEU LEU B . n 
B 1 16  GLU 16  41  41  GLU GLU B . n 
B 1 17  HIS 17  42  42  HIS HIS B . n 
B 1 18  ILE 18  43  43  ILE ILE B . n 
B 1 19  LEU 19  44  44  LEU LEU B . n 
B 1 20  LEU 20  45  45  LEU LEU B . n 
B 1 21  ARG 21  46  46  ARG ARG B . n 
B 1 22  PRO 22  47  47  PRO PRO B . n 
B 1 23  ASP 23  48  48  ASP ASP B . n 
B 1 24  THR 24  49  49  THR THR B . n 
B 1 25  TYR 25  50  50  TYR TYR B . n 
B 1 26  ILE 26  51  51  ILE ILE B . n 
B 1 27  GLY 27  52  52  GLY GLY B . n 
B 1 28  SER 28  53  53  SER SER B . n 
B 1 29  VAL 29  54  54  VAL VAL B . n 
B 1 30  GLU 30  55  55  GLU GLU B . n 
B 1 31  LEU 31  56  56  LEU LEU B . n 
B 1 32  VAL 32  57  57  VAL VAL B . n 
B 1 33  THR 33  58  58  THR THR B . n 
B 1 34  GLN 34  59  59  GLN GLN B . n 
B 1 35  GLN 35  60  60  GLN GLN B . n 
B 1 36  MET 36  61  61  MET MET B . n 
B 1 37  TRP 37  62  62  TRP TRP B . n 
B 1 38  VAL 38  63  63  VAL VAL B . n 
B 1 39  TYR 39  64  64  TYR TYR B . n 
B 1 40  ASP 40  65  65  ASP ASP B . n 
B 1 41  GLU 41  66  66  GLU GLU B . n 
B 1 42  ASP 42  67  67  ASP ASP B . n 
B 1 43  VAL 43  68  68  VAL VAL B . n 
B 1 44  GLY 44  69  69  GLY GLY B . n 
B 1 45  ILE 45  70  70  ILE ILE B . n 
B 1 46  ASN 46  71  71  ASN ASN B . n 
B 1 47  TYR 47  72  72  TYR TYR B . n 
B 1 48  ARG 48  73  73  ARG ARG B . n 
B 1 49  GLU 49  74  74  GLU GLU B . n 
B 1 50  VAL 50  75  75  VAL VAL B . n 
B 1 51  THR 51  76  76  THR THR B . n 
B 1 52  PHE 52  77  77  PHE PHE B . n 
B 1 53  VAL 53  78  78  VAL VAL B . n 
B 1 54  PRO 54  79  79  PRO PRO B . n 
B 1 55  GLY 55  80  80  GLY GLY B . n 
B 1 56  LEU 56  81  81  LEU LEU B . n 
B 1 57  TYR 57  82  82  TYR TYR B . n 
B 1 58  LYS 58  83  83  LYS LYS B . n 
B 1 59  ILE 59  84  84  ILE ILE B . n 
B 1 60  PHE 60  85  85  PHE PHE B . n 
B 1 61  ASP 61  86  86  ASP ASP B . n 
B 1 62  GLU 62  87  87  GLU GLU B . n 
B 1 63  ILE 63  88  88  ILE ILE B . n 
B 1 64  LEU 64  89  89  LEU LEU B . n 
B 1 65  VAL 65  90  90  VAL VAL B . n 
B 1 66  ASN 66  91  91  ASN ASN B . n 
B 1 67  ALA 67  92  92  ALA ALA B . n 
B 1 68  ALA 68  93  93  ALA ALA B . n 
B 1 69  ASP 69  94  94  ASP ASP B . n 
B 1 70  ASN 70  95  95  ASN ASN B . n 
B 1 71  LYS 71  96  96  LYS LYS B . n 
B 1 72  GLN 72  97  97  GLN GLN B . n 
B 1 73  ARG 73  98  98  ARG ARG B . n 
B 1 74  ASP 74  99  99  ASP ASP B . n 
B 1 75  PRO 75  100 100 PRO PRO B . n 
B 1 76  LYS 76  101 101 LYS LYS B . n 
B 1 77  MET 77  102 102 MET MET B . n 
B 1 78  SER 78  103 103 SER SER B . n 
B 1 79  CYS 79  104 104 CYS CYS B . n 
B 1 80  ILE 80  105 105 ILE ILE B . n 
B 1 81  ARG 81  106 106 ARG ARG B . n 
B 1 82  VAL 82  107 107 VAL VAL B . n 
B 1 83  THR 83  108 108 THR THR B . n 
B 1 84  ILE 84  109 109 ILE ILE B . n 
B 1 85  ASP 85  110 110 ASP ASP B . n 
B 1 86  PRO 86  111 111 PRO PRO B . n 
B 1 87  GLU 87  112 112 GLU GLU B . n 
B 1 88  ASN 88  113 113 ASN ASN B . n 
B 1 89  ASN 89  114 114 ASN ASN B . n 
B 1 90  LEU 90  115 115 LEU LEU B . n 
B 1 91  ILE 91  116 116 ILE ILE B . n 
B 1 92  SER 92  117 117 SER SER B . n 
B 1 93  ILE 93  118 118 ILE ILE B . n 
B 1 94  TRP 94  119 119 TRP TRP B . n 
B 1 95  ASN 95  120 120 ASN ASN B . n 
B 1 96  ASN 96  121 121 ASN ASN B . n 
B 1 97  GLY 97  122 122 GLY GLY B . n 
B 1 98  LYS 98  123 123 LYS LYS B . n 
B 1 99  GLY 99  124 124 GLY GLY B . n 
B 1 100 ILE 100 125 125 ILE ILE B . n 
B 1 101 PRO 101 126 126 PRO PRO B . n 
B 1 102 VAL 102 127 127 VAL VAL B . n 
B 1 103 VAL 103 128 128 VAL VAL B . n 
B 1 104 GLU 104 129 129 GLU GLU B . n 
B 1 105 HIS 105 130 130 HIS HIS B . n 
B 1 106 LYS 106 131 131 LYS LYS B . n 
B 1 107 VAL 107 132 132 VAL VAL B . n 
B 1 108 GLU 108 133 133 GLU GLU B . n 
B 1 109 LYS 109 134 134 LYS LYS B . n 
B 1 110 MET 110 135 135 MET MET B . n 
B 1 111 TYR 111 136 136 TYR TYR B . n 
B 1 112 VAL 112 137 137 VAL VAL B . n 
B 1 113 PRO 113 138 138 PRO PRO B . n 
B 1 114 ALA 114 139 139 ALA ALA B . n 
B 1 115 LEU 115 140 140 LEU LEU B . n 
B 1 116 ILE 116 141 141 ILE ILE B . n 
B 1 117 PHE 117 142 142 PHE PHE B . n 
B 1 118 GLY 118 143 143 GLY GLY B . n 
B 1 119 GLN 119 144 144 GLN GLN B . n 
B 1 120 LEU 120 145 145 LEU LEU B . n 
B 1 121 LEU 121 146 146 LEU LEU B . n 
B 1 122 THR 122 147 147 THR THR B . n 
B 1 123 SER 123 148 148 SER SER B . n 
B 1 124 SER 124 149 149 SER SER B . n 
B 1 125 ASN 125 150 150 ASN ASN B . n 
B 1 126 TYR 126 151 151 TYR TYR B . n 
B 1 127 ASP 127 152 152 ASP ASP B . n 
B 1 128 ASP 128 153 153 ASP ASP B . n 
B 1 129 ASP 129 154 154 ASP ASP B . n 
B 1 130 GLU 130 155 155 GLU GLU B . n 
B 1 131 LYS 131 156 156 LYS LYS B . n 
B 1 132 LYS 132 157 157 LYS LYS B . n 
B 1 133 VAL 133 158 158 VAL VAL B . n 
B 1 134 THR 134 159 159 THR THR B . n 
B 1 135 GLY 135 160 160 GLY GLY B . n 
B 1 136 GLY 136 161 161 GLY GLY B . n 
B 1 137 ARG 137 162 162 ARG ARG B . n 
B 1 138 ASN 138 163 163 ASN ASN B . n 
B 1 139 GLY 139 164 164 GLY GLY B . n 
B 1 140 TYR 140 165 165 TYR TYR B . n 
B 1 141 GLY 141 166 166 GLY GLY B . n 
B 1 142 ALA 142 167 167 ALA ALA B . n 
B 1 143 LYS 143 168 168 LYS LYS B . n 
B 1 144 LEU 144 169 169 LEU LEU B . n 
B 1 145 CYS 145 170 170 CYS CYS B . n 
B 1 146 ASN 146 171 171 ASN ASN B . n 
B 1 147 ILE 147 172 172 ILE ILE B . n 
B 1 148 PHE 148 173 173 PHE PHE B . n 
B 1 149 SER 149 174 174 SER SER B . n 
B 1 150 THR 150 175 175 THR THR B . n 
B 1 151 LYS 151 176 176 LYS LYS B . n 
B 1 152 PHE 152 177 177 PHE PHE B . n 
B 1 153 THR 153 178 178 THR THR B . n 
B 1 154 VAL 154 179 179 VAL VAL B . n 
B 1 155 GLU 155 180 180 GLU GLU B . n 
B 1 156 THR 156 181 181 THR THR B . n 
B 1 157 ALA 157 182 182 ALA ALA B . n 
B 1 158 SER 158 183 183 SER SER B . n 
B 1 159 ARG 159 184 184 ARG ARG B . n 
B 1 160 GLU 160 185 185 GLU GLU B . n 
B 1 161 TYR 161 186 186 TYR TYR B . n 
B 1 162 LYS 162 187 187 LYS LYS B . n 
B 1 163 LYS 163 188 188 LYS LYS B . n 
B 1 164 MET 164 189 189 MET MET B . n 
B 1 165 PHE 165 190 190 PHE PHE B . n 
B 1 166 LYS 166 191 191 LYS LYS B . n 
B 1 167 GLN 167 192 192 GLN GLN B . n 
B 1 168 THR 168 193 193 THR THR B . n 
B 1 169 TRP 169 194 194 TRP TRP B . n 
B 1 170 MET 170 195 195 MET MET B . n 
B 1 171 ASP 171 196 196 ASP ASP B . n 
B 1 172 ASN 172 197 197 ASN ASN B . n 
B 1 173 MET 173 198 198 MET MET B . n 
B 1 174 GLY 174 199 199 GLY GLY B . n 
B 1 175 ARG 175 200 200 ARG ARG B . n 
B 1 176 ALA 176 201 201 ALA ALA B . n 
B 1 177 GLY 177 202 202 GLY GLY B . n 
B 1 178 GLU 178 203 203 GLU GLU B . n 
B 1 179 MET 179 204 204 MET MET B . n 
B 1 180 GLU 180 205 205 GLU GLU B . n 
B 1 181 LEU 181 206 206 LEU LEU B . n 
B 1 182 LYS 182 207 207 LYS LYS B . n 
B 1 183 PRO 183 208 208 PRO PRO B . n 
B 1 184 PHE 184 209 209 PHE PHE B . n 
B 1 185 ASN 185 210 210 ASN ASN B . n 
B 1 186 GLY 186 211 211 GLY GLY B . n 
B 1 187 GLU 187 212 212 GLU GLU B . n 
B 1 188 ASP 188 213 213 ASP ASP B . n 
B 1 189 TYR 189 214 214 TYR TYR B . n 
B 1 190 THR 190 215 215 THR THR B . n 
B 1 191 CYS 191 216 216 CYS CYS B . n 
B 1 192 ILE 192 217 217 ILE ILE B . n 
B 1 193 THR 193 218 218 THR THR B . n 
B 1 194 PHE 194 219 219 PHE PHE B . n 
B 1 195 GLN 195 220 220 GLN GLN B . n 
B 1 196 PRO 196 221 221 PRO PRO B . n 
B 1 197 ASP 197 222 222 ASP ASP B . n 
B 1 198 LEU 198 223 223 LEU LEU B . n 
B 1 199 SER 199 224 224 SER SER B . n 
B 1 200 LYS 200 225 225 LYS LYS B . n 
B 1 201 PHE 201 226 226 PHE PHE B . n 
B 1 202 LYS 202 227 227 LYS LYS B . n 
B 1 203 MET 203 228 228 MET MET B . n 
B 1 204 GLN 204 229 229 GLN GLN B . n 
B 1 205 SER 205 230 230 SER SER B . n 
B 1 206 LEU 206 231 231 LEU LEU B . n 
B 1 207 ASP 207 232 232 ASP ASP B . n 
B 1 208 LYS 208 233 233 LYS LYS B . n 
B 1 209 ASP 209 234 234 ASP ASP B . n 
B 1 210 ILE 210 235 235 ILE ILE B . n 
B 1 211 VAL 211 236 236 VAL VAL B . n 
B 1 212 ALA 212 237 237 ALA ALA B . n 
B 1 213 LEU 213 238 238 LEU LEU B . n 
B 1 214 MET 214 239 239 MET MET B . n 
B 1 215 VAL 215 240 240 VAL VAL B . n 
B 1 216 ARG 216 241 241 ARG ARG B . n 
B 1 217 ARG 217 242 242 ARG ARG B . n 
B 1 218 ALA 218 243 243 ALA ALA B . n 
B 1 219 TYR 219 244 244 TYR TYR B . n 
B 1 220 ASP 220 245 245 ASP ASP B . n 
B 1 221 ILE 221 246 246 ILE ILE B . n 
B 1 222 ALA 222 247 247 ALA ALA B . n 
B 1 223 GLY 223 248 248 GLY GLY B . n 
B 1 224 SER 224 249 249 SER SER B . n 
B 1 225 THR 225 250 250 THR THR B . n 
B 1 226 LYS 226 251 251 LYS LYS B . n 
B 1 227 ASP 227 252 252 ASP ASP B . n 
B 1 228 VAL 228 253 253 VAL VAL B . n 
B 1 229 LYS 229 254 254 LYS LYS B . n 
B 1 230 VAL 230 255 255 VAL VAL B . n 
B 1 231 PHE 231 256 256 PHE PHE B . n 
B 1 232 LEU 232 257 257 LEU LEU B . n 
B 1 233 ASN 233 258 258 ASN ASN B . n 
B 1 234 GLY 234 259 259 GLY GLY B . n 
B 1 235 ASN 235 260 260 ASN ASN B . n 
B 1 236 LYS 236 261 261 LYS LYS B . n 
B 1 237 LEU 237 262 262 LEU LEU B . n 
B 1 238 PRO 238 263 263 PRO PRO B . n 
B 1 239 VAL 239 264 264 VAL VAL B . n 
B 1 240 LYS 240 265 265 LYS LYS B . n 
B 1 241 GLY 241 266 266 GLY GLY B . n 
B 1 242 PHE 242 267 267 PHE PHE B . n 
B 1 243 ARG 243 268 268 ARG ARG B . n 
B 1 244 SER 244 269 269 SER SER B . n 
B 1 245 TYR 245 270 270 TYR TYR B . n 
B 1 246 VAL 246 271 271 VAL VAL B . n 
B 1 247 ASP 247 272 272 ASP ASP B . n 
B 1 248 MET 248 273 273 MET MET B . n 
B 1 249 TYR 249 274 274 TYR TYR B . n 
B 1 250 LEU 250 275 275 LEU LEU B . n 
B 1 251 LYS 251 276 276 LYS LYS B . n 
B 1 252 ASP 252 277 277 ASP ASP B . n 
B 1 253 LYS 253 278 278 LYS LYS B . n 
B 1 254 LEU 254 279 279 LEU LEU B . n 
B 1 255 ASP 255 280 280 ASP ASP B . n 
B 1 256 GLU 256 281 281 GLU GLU B . n 
B 1 257 THR 257 282 282 THR THR B . n 
B 1 258 GLY 258 283 283 GLY GLY B . n 
B 1 259 ASN 259 284 284 ASN ASN B . n 
B 1 260 SER 260 285 285 SER SER B . n 
B 1 261 LEU 261 286 286 LEU LEU B . n 
B 1 262 LYS 262 287 287 LYS LYS B . n 
B 1 263 VAL 263 288 288 VAL VAL B . n 
B 1 264 ILE 264 289 289 ILE ILE B . n 
B 1 265 HIS 265 290 290 HIS HIS B . n 
B 1 266 GLU 266 291 291 GLU GLU B . n 
B 1 267 GLN 267 292 292 GLN GLN B . n 
B 1 268 VAL 268 293 293 VAL VAL B . n 
B 1 269 ASN 269 294 294 ASN ASN B . n 
B 1 270 HIS 270 295 295 HIS HIS B . n 
B 1 271 ARG 271 296 296 ARG ARG B . n 
B 1 272 TRP 272 297 297 TRP TRP B . n 
B 1 273 GLU 273 298 298 GLU GLU B . n 
B 1 274 VAL 274 299 299 VAL VAL B . n 
B 1 275 CYS 275 300 300 CYS CYS B . n 
B 1 276 LEU 276 301 301 LEU LEU B . n 
B 1 277 THR 277 302 302 THR THR B . n 
B 1 278 MET 278 303 303 MET MET B . n 
B 1 279 SER 279 304 304 SER SER B . n 
B 1 280 GLU 280 305 305 GLU GLU B . n 
B 1 281 LYS 281 306 306 LYS LYS B . n 
B 1 282 GLY 282 307 307 GLY GLY B . n 
B 1 283 PHE 283 308 308 PHE PHE B . n 
B 1 284 GLN 284 309 309 GLN GLN B . n 
B 1 285 GLN 285 310 310 GLN GLN B . n 
B 1 286 ILE 286 311 311 ILE ILE B . n 
B 1 287 SER 287 312 312 SER SER B . n 
B 1 288 PHE 288 313 313 PHE PHE B . n 
B 1 289 VAL 289 314 314 VAL VAL B . n 
B 1 290 ASN 290 315 315 ASN ASN B . n 
B 1 291 SER 291 316 316 SER SER B . n 
B 1 292 ILE 292 317 317 ILE ILE B . n 
B 1 293 ALA 293 318 318 ALA ALA B . n 
B 1 294 THR 294 319 319 THR THR B . n 
B 1 295 SER 295 320 320 SER SER B . n 
B 1 296 LYS 296 321 321 LYS LYS B . n 
B 1 297 GLY 297 322 322 GLY GLY B . n 
B 1 298 GLY 298 323 323 GLY GLY B . n 
B 1 299 ARG 299 324 324 ARG ARG B . n 
B 1 300 HIS 300 325 325 HIS HIS B . n 
B 1 301 VAL 301 326 326 VAL VAL B . n 
B 1 302 ASP 302 327 327 ASP ASP B . n 
B 1 303 TYR 303 328 328 TYR TYR B . n 
B 1 304 VAL 304 329 329 VAL VAL B . n 
B 1 305 ALA 305 330 330 ALA ALA B . n 
B 1 306 ASP 306 331 331 ASP ASP B . n 
B 1 307 GLN 307 332 332 GLN GLN B . n 
B 1 308 ILE 308 333 333 ILE ILE B . n 
B 1 309 VAL 309 334 334 VAL VAL B . n 
B 1 310 THR 310 335 335 THR THR B . n 
B 1 311 LYS 311 336 336 LYS LYS B . n 
B 1 312 LEU 312 337 337 LEU LEU B . n 
B 1 313 VAL 313 338 338 VAL VAL B . n 
B 1 314 ASP 314 339 339 ASP ASP B . n 
B 1 315 VAL 315 340 340 VAL VAL B . n 
B 1 316 VAL 316 341 341 VAL VAL B . n 
B 1 317 LYS 317 342 342 LYS LYS B . n 
B 1 318 LYS 318 343 343 LYS LYS B . n 
B 1 319 LYS 319 344 344 LYS LYS B . n 
B 1 320 ASN 320 345 345 ASN ASN B . n 
B 1 321 LYS 321 346 ?   ?   ?   B . n 
B 1 322 GLY 322 347 ?   ?   ?   B . n 
B 1 323 GLY 323 348 ?   ?   ?   B . n 
B 1 324 VAL 324 349 ?   ?   ?   B . n 
B 1 325 ALA 325 350 350 ALA ALA B . n 
B 1 326 VAL 326 351 351 VAL VAL B . n 
B 1 327 LYS 327 352 352 LYS LYS B . n 
B 1 328 ALA 328 353 353 ALA ALA B . n 
B 1 329 HIS 329 354 354 HIS HIS B . n 
B 1 330 GLN 330 355 355 GLN GLN B . n 
B 1 331 VAL 331 356 356 VAL VAL B . n 
B 1 332 LYS 332 357 357 LYS LYS B . n 
B 1 333 ASN 333 358 358 ASN ASN B . n 
B 1 334 HIS 334 359 359 HIS HIS B . n 
B 1 335 MET 335 360 360 MET MET B . n 
B 1 336 TRP 336 361 361 TRP TRP B . n 
B 1 337 ILE 337 362 362 ILE ILE B . n 
B 1 338 PHE 338 363 363 PHE PHE B . n 
B 1 339 VAL 339 364 364 VAL VAL B . n 
B 1 340 ASN 340 365 365 ASN ASN B . n 
B 1 341 ALA 341 366 366 ALA ALA B . n 
B 1 342 LEU 342 367 367 LEU LEU B . n 
B 1 343 ILE 343 368 368 ILE ILE B . n 
B 1 344 GLU 344 369 369 GLU GLU B . n 
B 1 345 ASN 345 370 370 ASN ASN B . n 
B 1 346 PRO 346 371 371 PRO PRO B . n 
B 1 347 THR 347 372 372 THR THR B . n 
B 1 348 PHE 348 373 373 PHE PHE B . n 
B 1 349 ASP 349 374 374 ASP ASP B . n 
B 1 350 SER 350 375 375 SER SER B . n 
B 1 351 GLN 351 376 376 GLN GLN B . n 
B 1 352 THR 352 377 377 THR THR B . n 
B 1 353 LYS 353 378 378 LYS LYS B . n 
B 1 354 GLU 354 379 379 GLU GLU B . n 
B 1 355 ASN 355 380 380 ASN ASN B . n 
B 1 356 MET 356 381 381 MET MET B . n 
B 1 357 THR 357 382 382 THR THR B . n 
B 1 358 LEU 358 383 383 LEU LEU B . n 
B 1 359 GLN 359 384 384 GLN GLN B . n 
B 1 360 PRO 360 385 385 PRO PRO B . n 
B 1 361 LYS 361 386 386 LYS LYS B . n 
B 1 362 SER 362 387 387 SER SER B . n 
B 1 363 PHE 363 388 388 PHE PHE B . n 
B 1 364 GLY 364 389 389 GLY GLY B . n 
B 1 365 SER 365 390 390 SER SER B . n 
B 1 366 THR 366 391 391 THR THR B . n 
B 1 367 CYS 367 392 392 CYS CYS B . n 
B 1 368 GLN 368 393 393 GLN GLN B . n 
B 1 369 LEU 369 394 394 LEU LEU B . n 
B 1 370 SER 370 395 395 SER SER B . n 
B 1 371 GLU 371 396 396 GLU GLU B . n 
B 1 372 LYS 372 397 397 LYS LYS B . n 
B 1 373 PHE 373 398 398 PHE PHE B . n 
B 1 374 ILE 374 399 399 ILE ILE B . n 
B 1 375 LYS 375 400 400 LYS LYS B . n 
B 1 376 ALA 376 401 401 ALA ALA B . n 
B 1 377 ALA 377 402 402 ALA ALA B . n 
B 1 378 ILE 378 403 403 ILE ILE B . n 
B 1 379 GLY 379 404 404 GLY GLY B . n 
B 1 380 CYS 380 405 405 CYS CYS B . n 
B 1 381 GLY 381 406 406 GLY GLY B . n 
B 1 382 ILE 382 407 407 ILE ILE B . n 
B 1 383 VAL 383 408 408 VAL VAL B . n 
B 1 384 GLU 384 409 409 GLU GLU B . n 
B 1 385 SER 385 410 410 SER SER B . n 
B 1 386 ILE 386 411 411 ILE ILE B . n 
B 1 387 LEU 387 412 412 LEU LEU B . n 
B 1 388 ASN 388 413 413 ASN ASN B . n 
B 1 389 TRP 389 414 414 TRP TRP B . n 
B 1 390 VAL 390 415 415 VAL VAL B . n 
B 1 391 LYS 391 416 416 LYS LYS B . n 
B 1 392 PHE 392 417 417 PHE PHE B . n 
B 1 393 LYS 393 418 ?   ?   ?   B . n 
B 1 394 ALA 394 419 ?   ?   ?   B . n 
B 1 395 GLN 395 420 ?   ?   ?   B . n 
B 1 396 VAL 396 421 ?   ?   ?   B . n 
B 1 397 GLN 397 422 ?   ?   ?   B . n 
B 1 398 LEU 398 423 ?   ?   ?   B . n 
B 1 399 ASN 399 424 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1ASC 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ASC 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 ANP   1   501 418 ANP   ANP A . 
D 3 MG    1   502 419 MG    MG  A . 
E 4 A1ASC 1   503 420 A1ASC 437 A . 
F 5 CL    1   504 421 CL    CL  A . 
G 2 ANP   1   501 418 ANP   ANP B . 
H 3 MG    1   502 419 MG    MG  B . 
I 6 GOL   1   503 420 GOL   GOL B . 
J 4 A1ASC 1   504 421 A1ASC 437 B . 
K 5 CL    1   505 422 CL    CL  B . 
L 7 HOH   1   601 591 HOH   HOH A . 
L 7 HOH   2   602 670 HOH   HOH A . 
L 7 HOH   3   603 590 HOH   HOH A . 
L 7 HOH   4   604 586 HOH   HOH A . 
L 7 HOH   5   605 763 HOH   HOH A . 
L 7 HOH   6   606 738 HOH   HOH A . 
L 7 HOH   7   607 687 HOH   HOH A . 
L 7 HOH   8   608 567 HOH   HOH A . 
L 7 HOH   9   609 594 HOH   HOH A . 
L 7 HOH   10  610 675 HOH   HOH A . 
L 7 HOH   11  611 751 HOH   HOH A . 
L 7 HOH   12  612 665 HOH   HOH A . 
L 7 HOH   13  613 668 HOH   HOH A . 
L 7 HOH   14  614 711 HOH   HOH A . 
L 7 HOH   15  615 542 HOH   HOH A . 
L 7 HOH   16  616 747 HOH   HOH A . 
L 7 HOH   17  617 742 HOH   HOH A . 
L 7 HOH   18  618 696 HOH   HOH A . 
L 7 HOH   19  619 569 HOH   HOH A . 
L 7 HOH   20  620 468 HOH   HOH A . 
L 7 HOH   21  621 532 HOH   HOH A . 
L 7 HOH   22  622 437 HOH   HOH A . 
L 7 HOH   23  623 712 HOH   HOH A . 
L 7 HOH   24  624 449 HOH   HOH A . 
L 7 HOH   25  625 424 HOH   HOH A . 
L 7 HOH   26  626 681 HOH   HOH A . 
L 7 HOH   27  627 588 HOH   HOH A . 
L 7 HOH   28  628 652 HOH   HOH A . 
L 7 HOH   29  629 554 HOH   HOH A . 
L 7 HOH   30  630 558 HOH   HOH A . 
L 7 HOH   31  631 485 HOH   HOH A . 
L 7 HOH   32  632 563 HOH   HOH A . 
L 7 HOH   33  633 697 HOH   HOH A . 
L 7 HOH   34  634 717 HOH   HOH A . 
L 7 HOH   35  635 690 HOH   HOH A . 
L 7 HOH   36  636 599 HOH   HOH A . 
L 7 HOH   37  637 499 HOH   HOH A . 
L 7 HOH   38  638 626 HOH   HOH A . 
L 7 HOH   39  639 444 HOH   HOH A . 
L 7 HOH   40  640 596 HOH   HOH A . 
L 7 HOH   41  641 474 HOH   HOH A . 
L 7 HOH   42  642 730 HOH   HOH A . 
L 7 HOH   43  643 706 HOH   HOH A . 
L 7 HOH   44  644 526 HOH   HOH A . 
L 7 HOH   45  645 595 HOH   HOH A . 
L 7 HOH   46  646 440 HOH   HOH A . 
L 7 HOH   47  647 436 HOH   HOH A . 
L 7 HOH   48  648 517 HOH   HOH A . 
L 7 HOH   49  649 446 HOH   HOH A . 
L 7 HOH   50  650 700 HOH   HOH A . 
L 7 HOH   51  651 592 HOH   HOH A . 
L 7 HOH   52  652 736 HOH   HOH A . 
L 7 HOH   53  653 710 HOH   HOH A . 
L 7 HOH   54  654 537 HOH   HOH A . 
L 7 HOH   55  655 759 HOH   HOH A . 
L 7 HOH   56  656 666 HOH   HOH A . 
L 7 HOH   57  657 441 HOH   HOH A . 
L 7 HOH   58  658 611 HOH   HOH A . 
L 7 HOH   59  659 505 HOH   HOH A . 
L 7 HOH   60  660 566 HOH   HOH A . 
L 7 HOH   61  661 521 HOH   HOH A . 
L 7 HOH   62  662 511 HOH   HOH A . 
L 7 HOH   63  663 728 HOH   HOH A . 
L 7 HOH   64  664 478 HOH   HOH A . 
L 7 HOH   65  665 609 HOH   HOH A . 
L 7 HOH   66  666 467 HOH   HOH A . 
L 7 HOH   67  667 646 HOH   HOH A . 
L 7 HOH   68  668 507 HOH   HOH A . 
L 7 HOH   69  669 703 HOH   HOH A . 
L 7 HOH   70  670 733 HOH   HOH A . 
L 7 HOH   71  671 543 HOH   HOH A . 
L 7 HOH   72  672 425 HOH   HOH A . 
L 7 HOH   73  673 426 HOH   HOH A . 
L 7 HOH   74  674 603 HOH   HOH A . 
L 7 HOH   75  675 632 HOH   HOH A . 
L 7 HOH   76  676 608 HOH   HOH A . 
L 7 HOH   77  677 513 HOH   HOH A . 
L 7 HOH   78  678 515 HOH   HOH A . 
L 7 HOH   79  679 734 HOH   HOH A . 
L 7 HOH   80  680 473 HOH   HOH A . 
L 7 HOH   81  681 510 HOH   HOH A . 
L 7 HOH   82  682 582 HOH   HOH A . 
L 7 HOH   83  683 475 HOH   HOH A . 
L 7 HOH   84  684 614 HOH   HOH A . 
L 7 HOH   85  685 606 HOH   HOH A . 
L 7 HOH   86  686 714 HOH   HOH A . 
L 7 HOH   87  687 490 HOH   HOH A . 
L 7 HOH   88  688 491 HOH   HOH A . 
L 7 HOH   89  689 519 HOH   HOH A . 
L 7 HOH   90  690 541 HOH   HOH A . 
L 7 HOH   91  691 559 HOH   HOH A . 
L 7 HOH   92  692 516 HOH   HOH A . 
L 7 HOH   93  693 509 HOH   HOH A . 
L 7 HOH   94  694 422 HOH   HOH A . 
L 7 HOH   95  695 564 HOH   HOH A . 
L 7 HOH   96  696 501 HOH   HOH A . 
L 7 HOH   97  697 621 HOH   HOH A . 
L 7 HOH   98  698 552 HOH   HOH A . 
L 7 HOH   99  699 673 HOH   HOH A . 
L 7 HOH   100 700 462 HOH   HOH A . 
L 7 HOH   101 701 629 HOH   HOH A . 
L 7 HOH   102 702 580 HOH   HOH A . 
L 7 HOH   103 703 514 HOH   HOH A . 
L 7 HOH   104 704 445 HOH   HOH A . 
L 7 HOH   105 705 651 HOH   HOH A . 
L 7 HOH   106 706 721 HOH   HOH A . 
L 7 HOH   107 707 565 HOH   HOH A . 
L 7 HOH   108 708 585 HOH   HOH A . 
L 7 HOH   109 709 644 HOH   HOH A . 
L 7 HOH   110 710 654 HOH   HOH A . 
L 7 HOH   111 711 583 HOH   HOH A . 
L 7 HOH   112 712 602 HOH   HOH A . 
L 7 HOH   113 713 482 HOH   HOH A . 
L 7 HOH   114 714 560 HOH   HOH A . 
L 7 HOH   115 715 664 HOH   HOH A . 
L 7 HOH   116 716 506 HOH   HOH A . 
L 7 HOH   117 717 466 HOH   HOH A . 
L 7 HOH   118 718 561 HOH   HOH A . 
L 7 HOH   119 719 423 HOH   HOH A . 
L 7 HOH   120 720 533 HOH   HOH A . 
L 7 HOH   121 721 661 HOH   HOH A . 
L 7 HOH   122 722 578 HOH   HOH A . 
L 7 HOH   123 723 452 HOH   HOH A . 
L 7 HOH   124 724 518 HOH   HOH A . 
L 7 HOH   125 725 472 HOH   HOH A . 
L 7 HOH   126 726 488 HOH   HOH A . 
L 7 HOH   127 727 539 HOH   HOH A . 
L 7 HOH   128 728 428 HOH   HOH A . 
L 7 HOH   129 729 480 HOH   HOH A . 
L 7 HOH   130 730 427 HOH   HOH A . 
L 7 HOH   131 731 553 HOH   HOH A . 
L 7 HOH   132 732 637 HOH   HOH A . 
L 7 HOH   133 733 620 HOH   HOH A . 
L 7 HOH   134 734 433 HOH   HOH A . 
L 7 HOH   135 735 617 HOH   HOH A . 
L 7 HOH   136 736 527 HOH   HOH A . 
L 7 HOH   137 737 489 HOH   HOH A . 
L 7 HOH   138 738 684 HOH   HOH A . 
L 7 HOH   139 739 645 HOH   HOH A . 
L 7 HOH   140 740 494 HOH   HOH A . 
L 7 HOH   141 741 496 HOH   HOH A . 
L 7 HOH   142 742 536 HOH   HOH A . 
L 7 HOH   143 743 623 HOH   HOH A . 
L 7 HOH   144 744 439 HOH   HOH A . 
L 7 HOH   145 745 648 HOH   HOH A . 
L 7 HOH   146 746 525 HOH   HOH A . 
L 7 HOH   147 747 638 HOH   HOH A . 
L 7 HOH   148 748 523 HOH   HOH A . 
L 7 HOH   149 749 726 HOH   HOH A . 
L 7 HOH   150 750 429 HOH   HOH A . 
L 7 HOH   151 751 658 HOH   HOH A . 
L 7 HOH   152 752 545 HOH   HOH A . 
L 7 HOH   153 753 724 HOH   HOH A . 
L 7 HOH   154 754 508 HOH   HOH A . 
L 7 HOH   155 755 481 HOH   HOH A . 
L 7 HOH   156 756 607 HOH   HOH A . 
L 7 HOH   157 757 460 HOH   HOH A . 
L 7 HOH   158 758 653 HOH   HOH A . 
L 7 HOH   159 759 487 HOH   HOH A . 
L 7 HOH   160 760 577 HOH   HOH A . 
L 7 HOH   161 761 469 HOH   HOH A . 
L 7 HOH   162 762 497 HOH   HOH A . 
L 7 HOH   163 763 448 HOH   HOH A . 
L 7 HOH   164 764 740 HOH   HOH A . 
L 7 HOH   165 765 471 HOH   HOH A . 
L 7 HOH   166 766 522 HOH   HOH A . 
L 7 HOH   167 767 534 HOH   HOH A . 
L 7 HOH   168 768 746 HOH   HOH A . 
L 7 HOH   169 769 431 HOH   HOH A . 
L 7 HOH   170 770 667 HOH   HOH A . 
L 7 HOH   171 771 544 HOH   HOH A . 
L 7 HOH   172 772 593 HOH   HOH A . 
L 7 HOH   173 773 766 HOH   HOH A . 
L 7 HOH   174 774 479 HOH   HOH A . 
L 7 HOH   175 775 574 HOH   HOH A . 
L 7 HOH   176 776 463 HOH   HOH A . 
L 7 HOH   177 777 502 HOH   HOH A . 
L 7 HOH   178 778 461 HOH   HOH A . 
L 7 HOH   179 779 659 HOH   HOH A . 
L 7 HOH   180 780 587 HOH   HOH A . 
L 7 HOH   181 781 459 HOH   HOH A . 
L 7 HOH   182 782 432 HOH   HOH A . 
L 7 HOH   183 783 723 HOH   HOH A . 
L 7 HOH   184 784 707 HOH   HOH A . 
L 7 HOH   185 785 575 HOH   HOH A . 
L 7 HOH   186 786 622 HOH   HOH A . 
L 7 HOH   187 787 435 HOH   HOH A . 
L 7 HOH   188 788 547 HOH   HOH A . 
L 7 HOH   189 789 762 HOH   HOH A . 
L 7 HOH   190 790 635 HOH   HOH A . 
L 7 HOH   191 791 671 HOH   HOH A . 
L 7 HOH   192 792 562 HOH   HOH A . 
L 7 HOH   193 793 619 HOH   HOH A . 
L 7 HOH   194 794 443 HOH   HOH A . 
L 7 HOH   195 795 528 HOH   HOH A . 
L 7 HOH   196 796 573 HOH   HOH A . 
L 7 HOH   197 797 486 HOH   HOH A . 
L 7 HOH   198 798 628 HOH   HOH A . 
L 7 HOH   199 799 704 HOH   HOH A . 
L 7 HOH   200 800 695 HOH   HOH A . 
L 7 HOH   201 801 447 HOH   HOH A . 
L 7 HOH   202 802 442 HOH   HOH A . 
L 7 HOH   203 803 458 HOH   HOH A . 
L 7 HOH   204 804 689 HOH   HOH A . 
L 7 HOH   205 805 616 HOH   HOH A . 
L 7 HOH   206 806 657 HOH   HOH A . 
L 7 HOH   207 807 456 HOH   HOH A . 
L 7 HOH   208 808 430 HOH   HOH A . 
L 7 HOH   209 809 524 HOH   HOH A . 
L 7 HOH   210 810 709 HOH   HOH A . 
L 7 HOH   211 811 476 HOH   HOH A . 
L 7 HOH   212 812 600 HOH   HOH A . 
L 7 HOH   213 813 555 HOH   HOH A . 
L 7 HOH   214 814 493 HOH   HOH A . 
L 7 HOH   215 815 548 HOH   HOH A . 
L 7 HOH   216 816 498 HOH   HOH A . 
L 7 HOH   217 817 434 HOH   HOH A . 
L 7 HOH   218 818 685 HOH   HOH A . 
L 7 HOH   219 819 764 HOH   HOH A . 
L 7 HOH   220 820 538 HOH   HOH A . 
L 7 HOH   221 821 678 HOH   HOH A . 
L 7 HOH   222 822 484 HOH   HOH A . 
L 7 HOH   223 823 630 HOH   HOH A . 
L 7 HOH   224 824 454 HOH   HOH A . 
L 7 HOH   225 825 748 HOH   HOH A . 
L 7 HOH   226 826 556 HOH   HOH A . 
L 7 HOH   227 827 581 HOH   HOH A . 
L 7 HOH   228 828 464 HOH   HOH A . 
L 7 HOH   229 829 756 HOH   HOH A . 
L 7 HOH   230 830 450 HOH   HOH A . 
L 7 HOH   231 831 649 HOH   HOH A . 
L 7 HOH   232 832 708 HOH   HOH A . 
L 7 HOH   233 833 701 HOH   HOH A . 
L 7 HOH   234 834 500 HOH   HOH A . 
L 7 HOH   235 835 572 HOH   HOH A . 
L 7 HOH   236 836 495 HOH   HOH A . 
L 7 HOH   237 837 557 HOH   HOH A . 
L 7 HOH   238 838 694 HOH   HOH A . 
L 7 HOH   239 839 483 HOH   HOH A . 
L 7 HOH   240 840 598 HOH   HOH A . 
L 7 HOH   241 841 546 HOH   HOH A . 
L 7 HOH   242 842 613 HOH   HOH A . 
L 7 HOH   243 843 470 HOH   HOH A . 
L 7 HOH   244 844 676 HOH   HOH A . 
L 7 HOH   245 845 672 HOH   HOH A . 
L 7 HOH   246 846 752 HOH   HOH A . 
L 7 HOH   247 847 680 HOH   HOH A . 
L 7 HOH   248 848 438 HOH   HOH A . 
L 7 HOH   249 849 550 HOH   HOH A . 
L 7 HOH   250 850 576 HOH   HOH A . 
L 7 HOH   251 851 589 HOH   HOH A . 
L 7 HOH   252 852 610 HOH   HOH A . 
L 7 HOH   253 853 503 HOH   HOH A . 
L 7 HOH   254 854 660 HOH   HOH A . 
L 7 HOH   255 855 749 HOH   HOH A . 
L 7 HOH   256 856 698 HOH   HOH A . 
L 7 HOH   257 857 570 HOH   HOH A . 
L 7 HOH   258 858 677 HOH   HOH A . 
L 7 HOH   259 859 455 HOH   HOH A . 
L 7 HOH   260 860 719 HOH   HOH A . 
L 7 HOH   261 861 753 HOH   HOH A . 
L 7 HOH   262 862 691 HOH   HOH A . 
L 7 HOH   263 863 465 HOH   HOH A . 
L 7 HOH   264 864 692 HOH   HOH A . 
L 7 HOH   265 865 531 HOH   HOH A . 
L 7 HOH   266 866 667 HOH   HOH A . 
L 7 HOH   267 867 631 HOH   HOH A . 
L 7 HOH   268 868 451 HOH   HOH A . 
L 7 HOH   269 869 745 HOH   HOH A . 
L 7 HOH   270 870 615 HOH   HOH A . 
L 7 HOH   271 871 453 HOH   HOH A . 
L 7 HOH   272 872 540 HOH   HOH A . 
L 7 HOH   273 873 605 HOH   HOH A . 
L 7 HOH   274 874 735 HOH   HOH A . 
L 7 HOH   275 875 741 HOH   HOH A . 
L 7 HOH   276 876 549 HOH   HOH A . 
L 7 HOH   277 877 504 HOH   HOH A . 
L 7 HOH   278 878 729 HOH   HOH A . 
L 7 HOH   279 879 647 HOH   HOH A . 
L 7 HOH   280 880 656 HOH   HOH A . 
L 7 HOH   281 881 732 HOH   HOH A . 
L 7 HOH   282 882 702 HOH   HOH A . 
L 7 HOH   283 883 520 HOH   HOH A . 
L 7 HOH   284 884 642 HOH   HOH A . 
L 7 HOH   285 885 584 HOH   HOH A . 
L 7 HOH   286 886 731 HOH   HOH A . 
L 7 HOH   287 887 683 HOH   HOH A . 
L 7 HOH   288 888 634 HOH   HOH A . 
L 7 HOH   289 889 713 HOH   HOH A . 
L 7 HOH   290 890 640 HOH   HOH A . 
L 7 HOH   291 891 720 HOH   HOH A . 
L 7 HOH   292 892 662 HOH   HOH A . 
L 7 HOH   293 893 739 HOH   HOH A . 
L 7 HOH   294 894 760 HOH   HOH A . 
L 7 HOH   295 895 633 HOH   HOH A . 
L 7 HOH   296 896 755 HOH   HOH A . 
L 7 HOH   297 897 457 HOH   HOH A . 
L 7 HOH   298 898 535 HOH   HOH A . 
L 7 HOH   299 899 571 HOH   HOH A . 
L 7 HOH   300 900 492 HOH   HOH A . 
L 7 HOH   301 901 571 HOH   HOH A . 
L 7 HOH   302 902 699 HOH   HOH A . 
L 7 HOH   303 903 618 HOH   HOH A . 
L 7 HOH   304 904 650 HOH   HOH A . 
L 7 HOH   305 905 529 HOH   HOH A . 
L 7 HOH   306 906 716 HOH   HOH A . 
L 7 HOH   307 907 663 HOH   HOH A . 
L 7 HOH   308 908 624 HOH   HOH A . 
L 7 HOH   309 909 597 HOH   HOH A . 
L 7 HOH   310 910 737 HOH   HOH A . 
L 7 HOH   311 911 655 HOH   HOH A . 
L 7 HOH   312 912 641 HOH   HOH A . 
L 7 HOH   313 913 551 HOH   HOH A . 
L 7 HOH   314 914 715 HOH   HOH A . 
L 7 HOH   315 915 686 HOH   HOH A . 
L 7 HOH   316 916 674 HOH   HOH A . 
L 7 HOH   317 917 705 HOH   HOH A . 
L 7 HOH   318 918 512 HOH   HOH A . 
L 7 HOH   319 919 612 HOH   HOH A . 
L 7 HOH   320 920 688 HOH   HOH A . 
L 7 HOH   321 921 727 HOH   HOH A . 
L 7 HOH   322 922 664 HOH   HOH A . 
L 7 HOH   323 923 643 HOH   HOH A . 
L 7 HOH   324 924 750 HOH   HOH A . 
L 7 HOH   325 925 757 HOH   HOH A . 
L 7 HOH   326 926 579 HOH   HOH A . 
L 7 HOH   327 927 682 HOH   HOH A . 
L 7 HOH   328 928 604 HOH   HOH A . 
L 7 HOH   329 929 765 HOH   HOH A . 
L 7 HOH   330 930 679 HOH   HOH A . 
L 7 HOH   331 931 568 HOH   HOH A . 
L 7 HOH   332 932 530 HOH   HOH A . 
L 7 HOH   333 933 627 HOH   HOH A . 
L 7 HOH   334 934 718 HOH   HOH A . 
L 7 HOH   335 935 744 HOH   HOH A . 
L 7 HOH   336 936 761 HOH   HOH A . 
L 7 HOH   337 937 601 HOH   HOH A . 
L 7 HOH   338 938 693 HOH   HOH A . 
L 7 HOH   339 939 639 HOH   HOH A . 
L 7 HOH   340 940 493 HOH   HOH A . 
L 7 HOH   341 941 669 HOH   HOH A . 
L 7 HOH   342 942 477 HOH   HOH A . 
L 7 HOH   343 943 636 HOH   HOH A . 
L 7 HOH   344 944 758 HOH   HOH A . 
L 7 HOH   345 945 754 HOH   HOH A . 
L 7 HOH   346 946 725 HOH   HOH A . 
L 7 HOH   347 947 743 HOH   HOH A . 
L 7 HOH   348 948 722 HOH   HOH A . 
M 7 HOH   1   601 620 HOH   HOH B . 
M 7 HOH   2   602 564 HOH   HOH B . 
M 7 HOH   3   603 714 HOH   HOH B . 
M 7 HOH   4   604 592 HOH   HOH B . 
M 7 HOH   5   605 578 HOH   HOH B . 
M 7 HOH   6   606 695 HOH   HOH B . 
M 7 HOH   7   607 663 HOH   HOH B . 
M 7 HOH   8   608 638 HOH   HOH B . 
M 7 HOH   9   609 603 HOH   HOH B . 
M 7 HOH   10  610 697 HOH   HOH B . 
M 7 HOH   11  611 604 HOH   HOH B . 
M 7 HOH   12  612 499 HOH   HOH B . 
M 7 HOH   13  613 676 HOH   HOH B . 
M 7 HOH   14  614 699 HOH   HOH B . 
M 7 HOH   15  615 517 HOH   HOH B . 
M 7 HOH   16  616 502 HOH   HOH B . 
M 7 HOH   17  617 438 HOH   HOH B . 
M 7 HOH   18  618 648 HOH   HOH B . 
M 7 HOH   19  619 431 HOH   HOH B . 
M 7 HOH   20  620 666 HOH   HOH B . 
M 7 HOH   21  621 670 HOH   HOH B . 
M 7 HOH   22  622 650 HOH   HOH B . 
M 7 HOH   23  623 634 HOH   HOH B . 
M 7 HOH   24  624 444 HOH   HOH B . 
M 7 HOH   25  625 562 HOH   HOH B . 
M 7 HOH   26  626 450 HOH   HOH B . 
M 7 HOH   27  627 623 HOH   HOH B . 
M 7 HOH   28  628 627 HOH   HOH B . 
M 7 HOH   29  629 637 HOH   HOH B . 
M 7 HOH   30  630 710 HOH   HOH B . 
M 7 HOH   31  631 458 HOH   HOH B . 
M 7 HOH   32  632 616 HOH   HOH B . 
M 7 HOH   33  633 681 HOH   HOH B . 
M 7 HOH   34  634 439 HOH   HOH B . 
M 7 HOH   35  635 560 HOH   HOH B . 
M 7 HOH   36  636 548 HOH   HOH B . 
M 7 HOH   37  637 542 HOH   HOH B . 
M 7 HOH   38  638 490 HOH   HOH B . 
M 7 HOH   39  639 530 HOH   HOH B . 
M 7 HOH   40  640 701 HOH   HOH B . 
M 7 HOH   41  641 684 HOH   HOH B . 
M 7 HOH   42  642 473 HOH   HOH B . 
M 7 HOH   43  643 487 HOH   HOH B . 
M 7 HOH   44  644 694 HOH   HOH B . 
M 7 HOH   45  645 641 HOH   HOH B . 
M 7 HOH   46  646 522 HOH   HOH B . 
M 7 HOH   47  647 430 HOH   HOH B . 
M 7 HOH   48  648 471 HOH   HOH B . 
M 7 HOH   49  649 594 HOH   HOH B . 
M 7 HOH   50  650 574 HOH   HOH B . 
M 7 HOH   51  651 488 HOH   HOH B . 
M 7 HOH   52  652 427 HOH   HOH B . 
M 7 HOH   53  653 483 HOH   HOH B . 
M 7 HOH   54  654 463 HOH   HOH B . 
M 7 HOH   55  655 622 HOH   HOH B . 
M 7 HOH   56  656 583 HOH   HOH B . 
M 7 HOH   57  657 582 HOH   HOH B . 
M 7 HOH   58  658 454 HOH   HOH B . 
M 7 HOH   59  659 597 HOH   HOH B . 
M 7 HOH   60  660 669 HOH   HOH B . 
M 7 HOH   61  661 682 HOH   HOH B . 
M 7 HOH   62  662 550 HOH   HOH B . 
M 7 HOH   63  663 591 HOH   HOH B . 
M 7 HOH   64  664 570 HOH   HOH B . 
M 7 HOH   65  665 609 HOH   HOH B . 
M 7 HOH   66  666 511 HOH   HOH B . 
M 7 HOH   67  667 686 HOH   HOH B . 
M 7 HOH   68  668 644 HOH   HOH B . 
M 7 HOH   69  669 534 HOH   HOH B . 
M 7 HOH   70  670 629 HOH   HOH B . 
M 7 HOH   71  671 585 HOH   HOH B . 
M 7 HOH   72  672 649 HOH   HOH B . 
M 7 HOH   73  673 551 HOH   HOH B . 
M 7 HOH   74  674 508 HOH   HOH B . 
M 7 HOH   75  675 436 HOH   HOH B . 
M 7 HOH   76  676 480 HOH   HOH B . 
M 7 HOH   77  677 533 HOH   HOH B . 
M 7 HOH   78  678 586 HOH   HOH B . 
M 7 HOH   79  679 505 HOH   HOH B . 
M 7 HOH   80  680 596 HOH   HOH B . 
M 7 HOH   81  681 544 HOH   HOH B . 
M 7 HOH   82  682 581 HOH   HOH B . 
M 7 HOH   83  683 510 HOH   HOH B . 
M 7 HOH   84  684 462 HOH   HOH B . 
M 7 HOH   85  685 423 HOH   HOH B . 
M 7 HOH   86  686 484 HOH   HOH B . 
M 7 HOH   87  687 485 HOH   HOH B . 
M 7 HOH   88  688 472 HOH   HOH B . 
M 7 HOH   89  689 453 HOH   HOH B . 
M 7 HOH   90  690 506 HOH   HOH B . 
M 7 HOH   91  691 467 HOH   HOH B . 
M 7 HOH   92  692 588 HOH   HOH B . 
M 7 HOH   93  693 433 HOH   HOH B . 
M 7 HOH   94  694 497 HOH   HOH B . 
M 7 HOH   95  695 543 HOH   HOH B . 
M 7 HOH   96  696 469 HOH   HOH B . 
M 7 HOH   97  697 563 HOH   HOH B . 
M 7 HOH   98  698 477 HOH   HOH B . 
M 7 HOH   99  699 461 HOH   HOH B . 
M 7 HOH   100 700 425 HOH   HOH B . 
M 7 HOH   101 701 514 HOH   HOH B . 
M 7 HOH   102 702 631 HOH   HOH B . 
M 7 HOH   103 703 545 HOH   HOH B . 
M 7 HOH   104 704 632 HOH   HOH B . 
M 7 HOH   105 705 653 HOH   HOH B . 
M 7 HOH   106 706 539 HOH   HOH B . 
M 7 HOH   107 707 526 HOH   HOH B . 
M 7 HOH   108 708 531 HOH   HOH B . 
M 7 HOH   109 709 642 HOH   HOH B . 
M 7 HOH   110 710 465 HOH   HOH B . 
M 7 HOH   111 711 489 HOH   HOH B . 
M 7 HOH   112 712 525 HOH   HOH B . 
M 7 HOH   113 713 507 HOH   HOH B . 
M 7 HOH   114 714 528 HOH   HOH B . 
M 7 HOH   115 715 452 HOH   HOH B . 
M 7 HOH   116 716 476 HOH   HOH B . 
M 7 HOH   117 717 424 HOH   HOH B . 
M 7 HOH   118 718 624 HOH   HOH B . 
M 7 HOH   119 719 532 HOH   HOH B . 
M 7 HOH   120 720 447 HOH   HOH B . 
M 7 HOH   121 721 428 HOH   HOH B . 
M 7 HOH   122 722 625 HOH   HOH B . 
M 7 HOH   123 723 612 HOH   HOH B . 
M 7 HOH   124 724 445 HOH   HOH B . 
M 7 HOH   125 725 494 HOH   HOH B . 
M 7 HOH   126 726 675 HOH   HOH B . 
M 7 HOH   127 727 482 HOH   HOH B . 
M 7 HOH   128 728 503 HOH   HOH B . 
M 7 HOH   129 729 547 HOH   HOH B . 
M 7 HOH   130 730 576 HOH   HOH B . 
M 7 HOH   131 731 481 HOH   HOH B . 
M 7 HOH   132 732 639 HOH   HOH B . 
M 7 HOH   133 733 659 HOH   HOH B . 
M 7 HOH   134 734 601 HOH   HOH B . 
M 7 HOH   135 735 448 HOH   HOH B . 
M 7 HOH   136 736 426 HOH   HOH B . 
M 7 HOH   137 737 434 HOH   HOH B . 
M 7 HOH   138 738 541 HOH   HOH B . 
M 7 HOH   139 739 441 HOH   HOH B . 
M 7 HOH   140 740 608 HOH   HOH B . 
M 7 HOH   141 741 595 HOH   HOH B . 
M 7 HOH   142 742 688 HOH   HOH B . 
M 7 HOH   143 743 486 HOH   HOH B . 
M 7 HOH   144 744 692 HOH   HOH B . 
M 7 HOH   145 745 479 HOH   HOH B . 
M 7 HOH   146 746 579 HOH   HOH B . 
M 7 HOH   147 747 607 HOH   HOH B . 
M 7 HOH   148 748 555 HOH   HOH B . 
M 7 HOH   149 749 443 HOH   HOH B . 
M 7 HOH   150 750 496 HOH   HOH B . 
M 7 HOH   151 751 656 HOH   HOH B . 
M 7 HOH   152 752 587 HOH   HOH B . 
M 7 HOH   153 753 621 HOH   HOH B . 
M 7 HOH   154 754 651 HOH   HOH B . 
M 7 HOH   155 755 614 HOH   HOH B . 
M 7 HOH   156 756 527 HOH   HOH B . 
M 7 HOH   157 757 429 HOH   HOH B . 
M 7 HOH   158 758 457 HOH   HOH B . 
M 7 HOH   159 759 538 HOH   HOH B . 
M 7 HOH   160 760 492 HOH   HOH B . 
M 7 HOH   161 761 677 HOH   HOH B . 
M 7 HOH   162 762 703 HOH   HOH B . 
M 7 HOH   163 763 599 HOH   HOH B . 
M 7 HOH   164 764 626 HOH   HOH B . 
M 7 HOH   165 765 432 HOH   HOH B . 
M 7 HOH   166 766 558 HOH   HOH B . 
M 7 HOH   167 767 440 HOH   HOH B . 
M 7 HOH   168 768 606 HOH   HOH B . 
M 7 HOH   169 769 569 HOH   HOH B . 
M 7 HOH   170 770 618 HOH   HOH B . 
M 7 HOH   171 771 529 HOH   HOH B . 
M 7 HOH   172 772 446 HOH   HOH B . 
M 7 HOH   173 773 700 HOH   HOH B . 
M 7 HOH   174 774 518 HOH   HOH B . 
M 7 HOH   175 775 679 HOH   HOH B . 
M 7 HOH   176 776 647 HOH   HOH B . 
M 7 HOH   177 777 501 HOH   HOH B . 
M 7 HOH   178 778 459 HOH   HOH B . 
M 7 HOH   179 779 674 HOH   HOH B . 
M 7 HOH   180 780 504 HOH   HOH B . 
M 7 HOH   181 781 521 HOH   HOH B . 
M 7 HOH   182 782 464 HOH   HOH B . 
M 7 HOH   183 783 628 HOH   HOH B . 
M 7 HOH   184 784 619 HOH   HOH B . 
M 7 HOH   185 785 636 HOH   HOH B . 
M 7 HOH   186 786 435 HOH   HOH B . 
M 7 HOH   187 787 693 HOH   HOH B . 
M 7 HOH   188 788 584 HOH   HOH B . 
M 7 HOH   189 789 456 HOH   HOH B . 
M 7 HOH   190 790 573 HOH   HOH B . 
M 7 HOH   191 791 559 HOH   HOH B . 
M 7 HOH   192 792 565 HOH   HOH B . 
M 7 HOH   193 793 466 HOH   HOH B . 
M 7 HOH   194 794 537 HOH   HOH B . 
M 7 HOH   195 795 567 HOH   HOH B . 
M 7 HOH   196 796 640 HOH   HOH B . 
M 7 HOH   197 797 460 HOH   HOH B . 
M 7 HOH   198 798 515 HOH   HOH B . 
M 7 HOH   199 799 577 HOH   HOH B . 
M 7 HOH   200 800 709 HOH   HOH B . 
M 7 HOH   201 801 513 HOH   HOH B . 
M 7 HOH   202 802 520 HOH   HOH B . 
M 7 HOH   203 803 553 HOH   HOH B . 
M 7 HOH   204 804 672 HOH   HOH B . 
M 7 HOH   205 805 498 HOH   HOH B . 
M 7 HOH   206 806 572 HOH   HOH B . 
M 7 HOH   207 807 451 HOH   HOH B . 
M 7 HOH   208 808 715 HOH   HOH B . 
M 7 HOH   209 809 478 HOH   HOH B . 
M 7 HOH   210 810 691 HOH   HOH B . 
M 7 HOH   211 811 633 HOH   HOH B . 
M 7 HOH   212 812 540 HOH   HOH B . 
M 7 HOH   213 813 536 HOH   HOH B . 
M 7 HOH   214 814 557 HOH   HOH B . 
M 7 HOH   215 815 437 HOH   HOH B . 
M 7 HOH   216 816 519 HOH   HOH B . 
M 7 HOH   217 817 610 HOH   HOH B . 
M 7 HOH   218 818 500 HOH   HOH B . 
M 7 HOH   219 819 475 HOH   HOH B . 
M 7 HOH   220 820 549 HOH   HOH B . 
M 7 HOH   221 821 690 HOH   HOH B . 
M 7 HOH   222 822 491 HOH   HOH B . 
M 7 HOH   223 823 580 HOH   HOH B . 
M 7 HOH   224 824 589 HOH   HOH B . 
M 7 HOH   225 825 552 HOH   HOH B . 
M 7 HOH   226 826 449 HOH   HOH B . 
M 7 HOH   227 827 455 HOH   HOH B . 
M 7 HOH   228 828 575 HOH   HOH B . 
M 7 HOH   229 829 680 HOH   HOH B . 
M 7 HOH   230 830 655 HOH   HOH B . 
M 7 HOH   231 831 509 HOH   HOH B . 
M 7 HOH   232 832 556 HOH   HOH B . 
M 7 HOH   233 833 546 HOH   HOH B . 
M 7 HOH   234 834 685 HOH   HOH B . 
M 7 HOH   235 835 671 HOH   HOH B . 
M 7 HOH   236 836 470 HOH   HOH B . 
M 7 HOH   237 837 593 HOH   HOH B . 
M 7 HOH   238 838 698 HOH   HOH B . 
M 7 HOH   239 839 635 HOH   HOH B . 
M 7 HOH   240 840 468 HOH   HOH B . 
M 7 HOH   241 841 615 HOH   HOH B . 
M 7 HOH   242 842 713 HOH   HOH B . 
M 7 HOH   243 843 442 HOH   HOH B . 
M 7 HOH   244 844 630 HOH   HOH B . 
M 7 HOH   245 845 602 HOH   HOH B . 
M 7 HOH   246 846 512 HOH   HOH B . 
M 7 HOH   247 847 661 HOH   HOH B . 
M 7 HOH   248 848 495 HOH   HOH B . 
M 7 HOH   249 849 598 HOH   HOH B . 
M 7 HOH   250 850 474 HOH   HOH B . 
M 7 HOH   251 851 605 HOH   HOH B . 
M 7 HOH   252 852 662 HOH   HOH B . 
M 7 HOH   253 853 652 HOH   HOH B . 
M 7 HOH   254 854 643 HOH   HOH B . 
M 7 HOH   255 855 702 HOH   HOH B . 
M 7 HOH   256 856 657 HOH   HOH B . 
M 7 HOH   257 857 524 HOH   HOH B . 
M 7 HOH   258 858 646 HOH   HOH B . 
M 7 HOH   259 859 712 HOH   HOH B . 
M 7 HOH   260 860 566 HOH   HOH B . 
M 7 HOH   261 861 561 HOH   HOH B . 
M 7 HOH   262 862 554 HOH   HOH B . 
M 7 HOH   263 863 668 HOH   HOH B . 
M 7 HOH   264 864 696 HOH   HOH B . 
M 7 HOH   265 865 590 HOH   HOH B . 
M 7 HOH   266 866 617 HOH   HOH B . 
M 7 HOH   267 867 658 HOH   HOH B . 
M 7 HOH   268 868 678 HOH   HOH B . 
M 7 HOH   269 869 689 HOH   HOH B . 
M 7 HOH   270 870 568 HOH   HOH B . 
M 7 HOH   271 871 611 HOH   HOH B . 
M 7 HOH   272 872 683 HOH   HOH B . 
M 7 HOH   273 873 625 HOH   HOH B . 
M 7 HOH   274 874 687 HOH   HOH B . 
M 7 HOH   275 875 516 HOH   HOH B . 
M 7 HOH   276 876 660 HOH   HOH B . 
M 7 HOH   277 877 705 HOH   HOH B . 
M 7 HOH   278 878 523 HOH   HOH B . 
M 7 HOH   279 879 708 HOH   HOH B . 
M 7 HOH   280 880 535 HOH   HOH B . 
M 7 HOH   281 881 654 HOH   HOH B . 
M 7 HOH   282 882 665 HOH   HOH B . 
M 7 HOH   283 883 704 HOH   HOH B . 
M 7 HOH   284 884 600 HOH   HOH B . 
M 7 HOH   285 885 711 HOH   HOH B . 
M 7 HOH   286 886 613 HOH   HOH B . 
M 7 HOH   287 887 673 HOH   HOH B . 
M 7 HOH   288 888 707 HOH   HOH B . 
M 7 HOH   289 889 716 HOH   HOH B . 
M 7 HOH   290 890 706 HOH   HOH B . 
M 7 HOH   291 891 645 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 1 A LYS 416 ? CG  ? A LYS 391 CG  
2  1 Y 1 A LYS 416 ? CD  ? A LYS 391 CD  
3  1 Y 1 A LYS 416 ? CE  ? A LYS 391 CE  
4  1 Y 1 A LYS 416 ? NZ  ? A LYS 391 NZ  
5  1 Y 1 A PHE 417 ? CG  ? A PHE 392 CG  
6  1 Y 1 A PHE 417 ? CD1 ? A PHE 392 CD1 
7  1 Y 1 A PHE 417 ? CD2 ? A PHE 392 CD2 
8  1 Y 1 A PHE 417 ? CE1 ? A PHE 392 CE1 
9  1 Y 1 A PHE 417 ? CE2 ? A PHE 392 CE2 
10 1 Y 1 A PHE 417 ? CZ  ? A PHE 392 CZ  
11 1 Y 1 B LYS 416 ? CG  ? B LYS 391 CG  
12 1 Y 1 B LYS 416 ? CD  ? B LYS 391 CD  
13 1 Y 1 B LYS 416 ? CE  ? B LYS 391 CE  
14 1 Y 1 B LYS 416 ? NZ  ? B LYS 391 NZ  
15 1 Y 1 B PHE 417 ? CG  ? B PHE 392 CG  
16 1 Y 1 B PHE 417 ? CD1 ? B PHE 392 CD1 
17 1 Y 1 B PHE 417 ? CD2 ? B PHE 392 CD2 
18 1 Y 1 B PHE 417 ? CE1 ? B PHE 392 CE1 
19 1 Y 1 B PHE 417 ? CE2 ? B PHE 392 CE2 
20 1 Y 1 B PHE 417 ? CZ  ? B PHE 392 CZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX    ? ? ? 1.17.1_3660 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALEPACK ? ? ? .           2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? DENZO     ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX    ? ? ? .           4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BQB 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     69.798 
_cell.length_a_esd                 ? 
_cell.length_b                     92.536 
_cell.length_b_esd                 ? 
_cell.length_c                     125.585 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9BQB 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9BQB 
_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             2.23 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.82 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '20% PEG3350 (w/v), 0.2M NH4Cl, 0.1M Tris pH 8.0' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-10-30 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 24-ID-E' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   24-ID-E 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9BQB 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.50 
_reflns.d_resolution_low                               50.00 
_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                                     130369 
_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                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.003 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.075 
_reflns.pdbx_Rpim_I_all                                0.020 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       1718606 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   0.999 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.072 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
1.50 1.55  ? ? ? ? ? ? 12903 ? ? ? ? ? ? ? ? ? ? ? 12.9 0.989 ? ? 1.600 0.441 ? 1  1 0.606 0.869 ? 100.0 ? 1.536 ? ? ? ? ? ? ? ? ? 
1.55 1.62  ? ? ? ? ? ? 12873 ? ? ? ? ? ? ? ? ? ? ? 13.4 0.975 ? ? 1.208 0.327 ? 2  1 0.777 0.935 ? 100.0 ? 1.163 ? ? ? ? ? ? ? ? ? 
1.62 1.69  ? ? ? ? ? ? 12941 ? ? ? ? ? ? ? ? ? ? ? 13.1 0.984 ? ? 0.806 0.221 ? 3  1 0.889 0.970 ? 100.0 ? 0.775 ? ? ? ? ? ? ? ? ? 
1.69 1.78  ? ? ? ? ? ? 12892 ? ? ? ? ? ? ? ? ? ? ? 12.0 1.010 ? ? 0.516 0.147 ? 4  1 0.941 0.985 ? 99.6  ? 0.494 ? ? ? ? ? ? ? ? ? 
1.78 1.89  ? ? ? ? ? ? 12954 ? ? ? ? ? ? ? ? ? ? ? 13.9 1.016 ? ? 0.327 0.087 ? 5  1 0.981 0.995 ? 100.0 ? 0.315 ? ? ? ? ? ? ? ? ? 
1.89 2.04  ? ? ? ? ? ? 12973 ? ? ? ? ? ? ? ? ? ? ? 13.8 1.019 ? ? 0.187 0.050 ? 6  1 0.993 0.998 ? 100.0 ? 0.180 ? ? ? ? ? ? ? ? ? 
2.04 2.24  ? ? ? ? ? ? 13005 ? ? ? ? ? ? ? ? ? ? ? 13.4 0.978 ? ? 0.117 0.032 ? 7  1 0.997 0.999 ? 100.0 ? 0.113 ? ? ? ? ? ? ? ? ? 
2.24 2.56  ? ? ? ? ? ? 13075 ? ? ? ? ? ? ? ? ? ? ? 12.4 1.005 ? ? 0.082 0.023 ? 8  1 0.998 0.999 ? 100.0 ? 0.078 ? ? ? ? ? ? ? ? ? 
2.56 3.23  ? ? ? ? ? ? 13166 ? ? ? ? ? ? ? ? ? ? ? 14.0 1.033 ? ? 0.057 0.015 ? 9  1 0.999 1.000 ? 100.0 ? 0.055 ? ? ? ? ? ? ? ? ? 
3.23 50.00 ? ? ? ? ? ? 13587 ? ? ? ? ? ? ? ? ? ? ? 12.8 1.013 ? ? 0.041 0.011 ? 10 1 0.999 1.000 ? 99.9  ? 0.039 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9BQB 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.50 
_refine.ls_d_res_low                             46.68 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     130275 
_refine.ls_number_reflns_R_free                  2000 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.87 
_refine.ls_percent_reflns_R_free                 1.54 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1403 
_refine.ls_R_factor_R_free                       0.1759 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1397 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 17.24 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.14 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        6176 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         144 
_refine_hist.number_atoms_solvent             639 
_refine_hist.number_atoms_total               6959 
_refine_hist.d_res_high                       1.50 
_refine_hist.d_res_low                        46.68 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.007  ? 6560 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.011  ? 8881 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 17.274 ? 2486 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.058  ? 981  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006  ? 1107 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.50 1.54  . . 139 8975 99.00  . . . . 0.2351 . . . . . . . . . . . 0.2997 
'X-RAY DIFFRACTION' 1.54 1.58  . . 142 9082 100.00 . . . . 0.2042 . . . . . . . . . . . 0.2543 
'X-RAY DIFFRACTION' 1.58 1.63  . . 142 9100 100.00 . . . . 0.1862 . . . . . . . . . . . 0.2373 
'X-RAY DIFFRACTION' 1.63 1.68  . . 142 9060 100.00 . . . . 0.1606 . . . . . . . . . . . 0.2072 
'X-RAY DIFFRACTION' 1.68 1.74  . . 141 9071 100.00 . . . . 0.1469 . . . . . . . . . . . 0.1697 
'X-RAY DIFFRACTION' 1.74 1.81  . . 142 9088 100.00 . . . . 0.1382 . . . . . . . . . . . 0.2302 
'X-RAY DIFFRACTION' 1.81 1.89  . . 142 9125 100.00 . . . . 0.1309 . . . . . . . . . . . 0.1908 
'X-RAY DIFFRACTION' 1.89 1.99  . . 142 9120 100.00 . . . . 0.1243 . . . . . . . . . . . 0.1693 
'X-RAY DIFFRACTION' 1.99 2.11  . . 143 9169 100.00 . . . . 0.1163 . . . . . . . . . . . 0.1595 
'X-RAY DIFFRACTION' 2.11 2.28  . . 142 9138 100.00 . . . . 0.1170 . . . . . . . . . . . 0.1658 
'X-RAY DIFFRACTION' 2.28 2.51  . . 144 9193 100.00 . . . . 0.1226 . . . . . . . . . . . 0.1495 
'X-RAY DIFFRACTION' 2.51 2.87  . . 144 9224 100.00 . . . . 0.1305 . . . . . . . . . . . 0.1666 
'X-RAY DIFFRACTION' 2.87 3.62  . . 146 9321 100.00 . . . . 0.1395 . . . . . . . . . . . 0.1642 
'X-RAY DIFFRACTION' 3.62 46.68 . . 149 9609 100.00 . . . . 0.1489 . . . . . . . . . . . 0.1765 
# 
_struct.entry_id                     9BQB 
_struct.title                        
'Human Topoisomerase 2 Alpha ATPase domain bound to topobexin and non-hydrolyzable ATP analog AMPPNP' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9BQB 
_struct_keywords.text            'Topoisomerase, ATPase, HYDROLASE, ISOMERASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   ISOMERASE/INHIBITOR 
# 
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 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 2 ? 
H N N 3 ? 
I N N 6 ? 
J N N 4 ? 
K N N 5 ? 
L N N 7 ? 
M N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    TOP2A_HUMAN 
_struct_ref.pdbx_db_accession          P11388 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SVERIYQKKTQLEHILLRPDTYIGSVELVTQQMWVYDEDVGINYREVTFVPGLYKIFDEILVNAADNKQRDPKMSCIRVT
IDPENNLISIWNNGKGIPVVEHKVEKMYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVETASREYKK
MFKQTWMDNMGRAGEMELKPFNGEDYTCITFQPDLSKFKMQSLDKDIVALMVRRAYDIAGSTKDVKVFLNGNKLPVKGFR
SYVDMYLKDKLDETGNSLKVIHEQVNHRWEVCLTMSEKGFQQISFVNSIATSKGGRHVDYVADQIVTKLVDVVKKKNKGG
VAVKAHQVKNHMWIFVNALIENPTFDSQTKENMTLQPKSFGSTCQLSEKFIKAAIGCGIVESILNWVKFKAQVQLN
;
_struct_ref.pdbx_align_begin           29 
# 
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 9BQB A 4 ? 399 ? P11388 29 ? 424 ? 29 424 
2 1 9BQB B 4 ? 399 ? P11388 29 ? 424 ? 29 424 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9BQB SER A 1 ? UNP P11388 ? ? 'expression tag' 26 1 
1 9BQB ASN A 2 ? UNP P11388 ? ? 'expression tag' 27 2 
1 9BQB ALA A 3 ? UNP P11388 ? ? 'expression tag' 28 3 
2 9BQB SER B 1 ? UNP P11388 ? ? 'expression tag' 26 4 
2 9BQB ASN B 2 ? UNP P11388 ? ? 'expression tag' 27 5 
2 9BQB ALA B 3 ? UNP P11388 ? ? 'expression tag' 28 6 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 9470  ? 
1 MORE         -60   ? 
1 'SSA (A^2)'  31720 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M 
# 
_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 SER A 4   ? TYR A 9   ? SER A 29  TYR A 34  1 ? 6  
HELX_P HELX_P2  AA2 THR A 13  ? ARG A 21  ? THR A 38  ARG A 46  1 ? 9  
HELX_P HELX_P3  AA3 PRO A 22  ? GLY A 27  ? PRO A 47  GLY A 52  1 ? 6  
HELX_P HELX_P4  AA4 VAL A 53  ? ASP A 74  ? VAL A 78  ASP A 99  1 ? 22 
HELX_P HELX_P5  AA5 VAL A 112 ? GLN A 119 ? VAL A 137 GLN A 144 1 ? 8  
HELX_P HELX_P6  AA6 TYR A 140 ? PHE A 148 ? TYR A 165 PHE A 173 1 ? 9  
HELX_P HELX_P7  AA7 LEU A 198 ? LYS A 202 ? LEU A 223 LYS A 227 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 207 ? THR A 225 ? ASP A 232 THR A 250 1 ? 19 
HELX_P HELX_P9  AA9 GLY A 241 ? LYS A 251 ? GLY A 266 LYS A 276 1 ? 11 
HELX_P HELX_P10 AB1 ARG A 299 ? LYS A 319 ? ARG A 324 LYS A 344 1 ? 21 
HELX_P HELX_P11 AB2 LYS A 327 ? ASN A 333 ? LYS A 352 ASN A 358 1 ? 7  
HELX_P HELX_P12 AB3 GLN A 359 ? PHE A 363 ? GLN A 384 PHE A 388 5 ? 5  
HELX_P HELX_P13 AB4 SER A 370 ? GLY A 379 ? SER A 395 GLY A 404 1 ? 10 
HELX_P HELX_P14 AB5 GLY A 381 ? PHE A 392 ? GLY A 406 PHE A 417 1 ? 12 
HELX_P HELX_P15 AB6 SER B 4   ? TYR B 9   ? SER B 29  TYR B 34  1 ? 6  
HELX_P HELX_P16 AB7 THR B 13  ? ARG B 21  ? THR B 38  ARG B 46  1 ? 9  
HELX_P HELX_P17 AB8 PRO B 22  ? GLY B 27  ? PRO B 47  GLY B 52  1 ? 6  
HELX_P HELX_P18 AB9 VAL B 53  ? ASP B 74  ? VAL B 78  ASP B 99  1 ? 22 
HELX_P HELX_P19 AC1 TYR B 111 ? GLN B 119 ? TYR B 136 GLN B 144 1 ? 9  
HELX_P HELX_P20 AC2 TYR B 140 ? PHE B 148 ? TYR B 165 PHE B 173 1 ? 9  
HELX_P HELX_P21 AC3 LEU B 198 ? LYS B 202 ? LEU B 223 LYS B 227 5 ? 5  
HELX_P HELX_P22 AC4 ASP B 207 ? THR B 225 ? ASP B 232 THR B 250 1 ? 19 
HELX_P HELX_P23 AC5 GLY B 241 ? LYS B 251 ? GLY B 266 LYS B 276 1 ? 11 
HELX_P HELX_P24 AC6 ARG B 299 ? LYS B 319 ? ARG B 324 LYS B 344 1 ? 21 
HELX_P HELX_P25 AC7 LYS B 327 ? ASN B 333 ? LYS B 352 ASN B 358 1 ? 7  
HELX_P HELX_P26 AC8 GLN B 359 ? PHE B 363 ? GLN B 384 PHE B 388 5 ? 5  
HELX_P HELX_P27 AC9 SER B 370 ? GLY B 379 ? SER B 395 GLY B 404 1 ? 10 
HELX_P HELX_P28 AD1 GLY B 381 ? PHE B 392 ? GLY B 406 PHE B 417 1 ? 12 
# 
_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 66 OD1 ? ? ? 1_555 D MG  . MG ? ? A ASN 91  A MG  502 1_555 ? ? ? ? ? ? ? 2.100 ? ? 
metalc2  metalc ? ? C ANP .  O1G ? ? ? 1_555 D MG  . MG ? ? A ANP 501 A MG  502 1_555 ? ? ? ? ? ? ? 2.096 ? ? 
metalc3  metalc ? ? C ANP .  O1B ? ? ? 1_555 D MG  . MG ? ? A ANP 501 A MG  502 1_555 ? ? ? ? ? ? ? 2.072 ? ? 
metalc4  metalc ? ? C ANP .  O1A ? ? ? 1_555 D MG  . MG ? ? A ANP 501 A MG  502 1_555 ? ? ? ? ? ? ? 2.127 ? ? 
metalc5  metalc ? ? D MG  .  MG  ? ? ? 1_555 L HOH . O  ? ? A MG  502 A HOH 625 1_555 ? ? ? ? ? ? ? 2.075 ? ? 
metalc6  metalc ? ? D MG  .  MG  ? ? ? 1_555 L HOH . O  ? ? A MG  502 A HOH 750 1_555 ? ? ? ? ? ? ? 2.144 ? ? 
metalc7  metalc ? ? B ASN 66 OD1 ? ? ? 1_555 H MG  . MG ? ? B ASN 91  B MG  502 1_555 ? ? ? ? ? ? ? 2.119 ? ? 
metalc8  metalc ? ? G ANP .  O1G ? ? ? 1_555 H MG  . MG ? ? B ANP 501 B MG  502 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
metalc9  metalc ? ? G ANP .  O1B ? ? ? 1_555 H MG  . MG ? ? B ANP 501 B MG  502 1_555 ? ? ? ? ? ? ? 2.127 ? ? 
metalc10 metalc ? ? G ANP .  O1A ? ? ? 1_555 H MG  . MG ? ? B ANP 501 B MG  502 1_555 ? ? ? ? ? ? ? 2.082 ? ? 
metalc11 metalc ? ? H MG  .  MG  ? ? ? 1_555 M HOH . O  ? ? B MG  502 B HOH 619 1_555 ? ? ? ? ? ? ? 2.061 ? ? 
metalc12 metalc ? ? H MG  .  MG  ? ? ? 1_555 M HOH . O  ? ? B MG  502 B HOH 717 1_555 ? ? ? ? ? ? ? 2.154 ? ? 
# 
_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 66 ? A ASN 91  ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O1G ? C ANP . ? A ANP 501 ? 1_555 170.7 ? 
2  OD1 ? A ASN 66 ? A ASN 91  ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O1B ? C ANP . ? A ANP 501 ? 1_555 95.7  ? 
3  O1G ? C ANP .  ? A ANP 501 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O1B ? C ANP . ? A ANP 501 ? 1_555 90.2  ? 
4  OD1 ? A ASN 66 ? A ASN 91  ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O1A ? C ANP . ? A ANP 501 ? 1_555 91.1  ? 
5  O1G ? C ANP .  ? A ANP 501 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O1A ? C ANP . ? A ANP 501 ? 1_555 96.6  ? 
6  O1B ? C ANP .  ? A ANP 501 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O1A ? C ANP . ? A ANP 501 ? 1_555 84.4  ? 
7  OD1 ? A ASN 66 ? A ASN 91  ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O   ? L HOH . ? A HOH 625 ? 1_555 86.6  ? 
8  O1G ? C ANP .  ? A ANP 501 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O   ? L HOH . ? A HOH 625 ? 1_555 88.0  ? 
9  O1B ? C ANP .  ? A ANP 501 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O   ? L HOH . ? A HOH 625 ? 1_555 174.5 ? 
10 O1A ? C ANP .  ? A ANP 501 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O   ? L HOH . ? A HOH 625 ? 1_555 90.7  ? 
11 OD1 ? A ASN 66 ? A ASN 91  ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O   ? L HOH . ? A HOH 750 ? 1_555 83.4  ? 
12 O1G ? C ANP .  ? A ANP 501 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O   ? L HOH . ? A HOH 750 ? 1_555 89.2  ? 
13 O1B ? C ANP .  ? A ANP 501 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O   ? L HOH . ? A HOH 750 ? 1_555 93.4  ? 
14 O1A ? C ANP .  ? A ANP 501 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O   ? L HOH . ? A HOH 750 ? 1_555 173.9 ? 
15 O   ? L HOH .  ? A HOH 625 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O   ? L HOH . ? A HOH 750 ? 1_555 91.7  ? 
16 OD1 ? B ASN 66 ? B ASN 91  ? 1_555 MG ? H MG . ? B MG 502 ? 1_555 O1G ? G ANP . ? B ANP 501 ? 1_555 170.3 ? 
17 OD1 ? B ASN 66 ? B ASN 91  ? 1_555 MG ? H MG . ? B MG 502 ? 1_555 O1B ? G ANP . ? B ANP 501 ? 1_555 94.9  ? 
18 O1G ? G ANP .  ? B ANP 501 ? 1_555 MG ? H MG . ? B MG 502 ? 1_555 O1B ? G ANP . ? B ANP 501 ? 1_555 91.7  ? 
19 OD1 ? B ASN 66 ? B ASN 91  ? 1_555 MG ? H MG . ? B MG 502 ? 1_555 O1A ? G ANP . ? B ANP 501 ? 1_555 91.7  ? 
20 O1G ? G ANP .  ? B ANP 501 ? 1_555 MG ? H MG . ? B MG 502 ? 1_555 O1A ? G ANP . ? B ANP 501 ? 1_555 96.1  ? 
21 O1B ? G ANP .  ? B ANP 501 ? 1_555 MG ? H MG . ? B MG 502 ? 1_555 O1A ? G ANP . ? B ANP 501 ? 1_555 83.2  ? 
22 OD1 ? B ASN 66 ? B ASN 91  ? 1_555 MG ? H MG . ? B MG 502 ? 1_555 O   ? M HOH . ? B HOH 619 ? 1_555 85.4  ? 
23 O1G ? G ANP .  ? B ANP 501 ? 1_555 MG ? H MG . ? B MG 502 ? 1_555 O   ? M HOH . ? B HOH 619 ? 1_555 88.7  ? 
24 O1B ? G ANP .  ? B ANP 501 ? 1_555 MG ? H MG . ? B MG 502 ? 1_555 O   ? M HOH . ? B HOH 619 ? 1_555 175.2 ? 
25 O1A ? G ANP .  ? B ANP 501 ? 1_555 MG ? H MG . ? B MG 502 ? 1_555 O   ? M HOH . ? B HOH 619 ? 1_555 92.0  ? 
26 OD1 ? B ASN 66 ? B ASN 91  ? 1_555 MG ? H MG . ? B MG 502 ? 1_555 O   ? M HOH . ? B HOH 717 ? 1_555 81.8  ? 
27 O1G ? G ANP .  ? B ANP 501 ? 1_555 MG ? H MG . ? B MG 502 ? 1_555 O   ? M HOH . ? B HOH 717 ? 1_555 90.8  ? 
28 O1B ? G ANP .  ? B ANP 501 ? 1_555 MG ? H MG . ? B MG 502 ? 1_555 O   ? M HOH . ? B HOH 717 ? 1_555 93.0  ? 
29 O1A ? G ANP .  ? B ANP 501 ? 1_555 MG ? H MG . ? B MG 502 ? 1_555 O   ? M HOH . ? B HOH 717 ? 1_555 172.2 ? 
30 O   ? M HOH .  ? B HOH 619 ? 1_555 MG ? H MG . ? B MG 502 ? 1_555 O   ? M HOH . ? B HOH 717 ? 1_555 91.8  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
AA3 ? 3 ? 
AA4 ? 8 ? 
AA5 ? 2 ? 
AA6 ? 2 ? 
AA7 ? 5 ? 
AA8 ? 2 ? 
AA9 ? 2 ? 
AB1 ? 3 ? 
AB2 ? 8 ? 
AB3 ? 5 ? 
AB4 ? 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 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? parallel      
AA4 7 8 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? parallel      
AA7 4 5 ? anti-parallel 
AA8 1 2 ? parallel      
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-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 ? parallel      
AB2 7 8 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? parallel      
AB3 4 5 ? anti-parallel 
AB4 1 2 ? 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 GLN A 10  ? LYS A 11  ? GLN A 35  LYS A 36  
AA1 2 THR B 122 ? SER B 123 ? THR B 147 SER B 148 
AA2 1 VAL A 32  ? ASP A 40  ? VAL A 57  ASP A 65  
AA2 2 GLY A 44  ? PHE A 52  ? GLY A 69  PHE A 77  
AA3 1 ARG A 175 ? ALA A 176 ? ARG A 200 ALA A 201 
AA3 2 LYS A 163 ? MET A 170 ? LYS A 188 MET A 195 
AA3 3 GLU A 180 ? PRO A 183 ? GLU A 205 PRO A 208 
AA4 1 ARG A 175 ? ALA A 176 ? ARG A 200 ALA A 201 
AA4 2 LYS A 163 ? MET A 170 ? LYS A 188 MET A 195 
AA4 3 SER A 149 ? SER A 158 ? SER A 174 SER A 183 
AA4 4 TYR A 189 ? PRO A 196 ? TYR A 214 PRO A 221 
AA4 5 LEU A 90  ? ASN A 96  ? LEU A 115 ASN A 121 
AA4 6 CYS A 79  ? ASP A 85  ? CYS A 104 ASP A 110 
AA4 7 LYS A 229 ? LEU A 232 ? LYS A 254 LEU A 257 
AA4 8 ASN A 235 ? LYS A 236 ? ASN A 260 LYS A 261 
AA5 1 GLU A 104 ? HIS A 105 ? GLU A 129 HIS A 130 
AA5 2 MET A 110 ? TYR A 111 ? MET A 135 TYR A 136 
AA6 1 THR A 122 ? SER A 123 ? THR A 147 SER A 148 
AA6 2 GLN B 10  ? LYS B 11  ? GLN B 35  LYS B 36  
AA7 1 ILE A 264 ? ASN A 269 ? ILE A 289 ASN A 294 
AA7 2 TRP A 272 ? MET A 278 ? TRP A 297 MET A 303 
AA7 3 MET A 335 ? ALA A 341 ? MET A 360 ALA A 366 
AA7 4 GLN A 284 ? VAL A 289 ? GLN A 309 VAL A 314 
AA7 5 ILE A 292 ? ALA A 293 ? ILE A 317 ALA A 318 
AA8 1 GLY A 297 ? GLY A 298 ? GLY A 322 GLY A 323 
AA8 2 ASN A 355 ? MET A 356 ? ASN A 380 MET A 381 
AA9 1 VAL B 32  ? ASP B 40  ? VAL B 57  ASP B 65  
AA9 2 GLY B 44  ? PHE B 52  ? GLY B 69  PHE B 77  
AB1 1 ARG B 175 ? ALA B 176 ? ARG B 200 ALA B 201 
AB1 2 LYS B 163 ? MET B 170 ? LYS B 188 MET B 195 
AB1 3 GLU B 180 ? PRO B 183 ? GLU B 205 PRO B 208 
AB2 1 ARG B 175 ? ALA B 176 ? ARG B 200 ALA B 201 
AB2 2 LYS B 163 ? MET B 170 ? LYS B 188 MET B 195 
AB2 3 SER B 149 ? SER B 158 ? SER B 174 SER B 183 
AB2 4 TYR B 189 ? PRO B 196 ? TYR B 214 PRO B 221 
AB2 5 LEU B 90  ? ASN B 96  ? LEU B 115 ASN B 121 
AB2 6 CYS B 79  ? ASP B 85  ? CYS B 104 ASP B 110 
AB2 7 LYS B 229 ? LEU B 232 ? LYS B 254 LEU B 257 
AB2 8 ASN B 235 ? LYS B 236 ? ASN B 260 LYS B 261 
AB3 1 ILE B 264 ? ASN B 269 ? ILE B 289 ASN B 294 
AB3 2 TRP B 272 ? MET B 278 ? TRP B 297 MET B 303 
AB3 3 MET B 335 ? ALA B 341 ? MET B 360 ALA B 366 
AB3 4 GLN B 284 ? VAL B 289 ? GLN B 309 VAL B 314 
AB3 5 ILE B 292 ? ALA B 293 ? ILE B 317 ALA B 318 
AB4 1 GLY B 297 ? GLY B 298 ? GLY B 322 GLY B 323 
AB4 2 ASN B 355 ? MET B 356 ? ASN B 380 MET B 381 
# 
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 GLN A 10  ? N GLN A 35  O SER B 123 ? O SER B 148 
AA2 1 2 N ASP A 40  ? N ASP A 65  O GLY A 44  ? O GLY A 69  
AA3 1 2 O ARG A 175 ? O ARG A 200 N MET A 170 ? N MET A 195 
AA3 2 3 N LYS A 166 ? N LYS A 191 O GLU A 180 ? O GLU A 205 
AA4 1 2 O ARG A 175 ? O ARG A 200 N MET A 170 ? N MET A 195 
AA4 2 3 O TRP A 169 ? O TRP A 194 N PHE A 152 ? N PHE A 177 
AA4 3 4 N THR A 153 ? N THR A 178 O THR A 193 ? O THR A 218 
AA4 4 5 O PHE A 194 ? O PHE A 219 N ILE A 91  ? N ILE A 116 
AA4 5 6 O SER A 92  ? O SER A 117 N THR A 83  ? N THR A 108 
AA4 6 7 N VAL A 82  ? N VAL A 107 O PHE A 231 ? O PHE A 256 
AA4 7 8 N LEU A 232 ? N LEU A 257 O ASN A 235 ? O ASN A 260 
AA5 1 2 N HIS A 105 ? N HIS A 130 O MET A 110 ? O MET A 135 
AA6 1 2 N SER A 123 ? N SER A 148 O GLN B 10  ? O GLN B 35  
AA7 1 2 N ILE A 264 ? N ILE A 289 O LEU A 276 ? O LEU A 301 
AA7 2 3 N CYS A 275 ? N CYS A 300 O PHE A 338 ? O PHE A 363 
AA7 3 4 O ALA A 341 ? O ALA A 366 N PHE A 288 ? N PHE A 313 
AA7 4 5 N VAL A 289 ? N VAL A 314 O ILE A 292 ? O ILE A 317 
AA8 1 2 N GLY A 297 ? N GLY A 322 O MET A 356 ? O MET A 381 
AA9 1 2 N MET B 36  ? N MET B 61  O ARG B 48  ? O ARG B 73  
AB1 1 2 O ARG B 175 ? O ARG B 200 N MET B 170 ? N MET B 195 
AB1 2 3 N LYS B 166 ? N LYS B 191 O GLU B 180 ? O GLU B 205 
AB2 1 2 O ARG B 175 ? O ARG B 200 N MET B 170 ? N MET B 195 
AB2 2 3 O TRP B 169 ? O TRP B 194 N PHE B 152 ? N PHE B 177 
AB2 3 4 N GLU B 155 ? N GLU B 180 O CYS B 191 ? O CYS B 216 
AB2 4 5 O PHE B 194 ? O PHE B 219 N ILE B 91  ? N ILE B 116 
AB2 5 6 O LEU B 90  ? O LEU B 115 N ASP B 85  ? N ASP B 110 
AB2 6 7 N VAL B 82  ? N VAL B 107 O PHE B 231 ? O PHE B 256 
AB2 7 8 N LEU B 232 ? N LEU B 257 O ASN B 235 ? O ASN B 260 
AB3 1 2 N ILE B 264 ? N ILE B 289 O LEU B 276 ? O LEU B 301 
AB3 2 3 N CYS B 275 ? N CYS B 300 O PHE B 338 ? O PHE B 363 
AB3 3 4 O ALA B 341 ? O ALA B 366 N PHE B 288 ? N PHE B 313 
AB3 4 5 N VAL B 289 ? N VAL B 314 O ILE B 292 ? O ILE B 317 
AB4 1 2 N GLY B 297 ? N GLY B 322 O MET B 356 ? O MET B 381 
# 
_pdbx_entry_details.entry_id                   9BQB 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 H    A GLY 164 ? ? HNB1 A ANP 501 ? ? 1.34 
2 1 H    B GLY 164 ? ? HNB1 B ANP 501 ? ? 1.35 
3 1 HE22 A GLN 384 ? B O    B LEU 56  ? ? 1.50 
4 1 HH   B TYR 186 ? ? O    B HOH 603 ? ? 1.54 
5 1 HZ2  B LYS 176 ? ? O    B HOH 601 ? ? 1.57 
6 1 NE2  A GLN 384 ? B O    B LEU 56  ? ? 2.16 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 VAL A 68  ? ? -131.01 -43.81  
2  1 ASN A 121 ? ? -108.94 -160.47 
3  1 ARG A 162 ? ? -137.70 -39.26  
4  1 ASN A 210 ? ? -146.50 39.33   
5  1 LYS A 265 ? ? -100.91 -92.07  
6  1 ASN B 121 ? ? -102.39 -162.75 
7  1 ARG B 162 ? ? -139.66 -36.43  
8  1 ASN B 210 ? ? -143.71 21.62   
9  1 LYS B 265 ? ? -100.75 -66.91  
10 1 LYS B 276 ? ? -36.05  -35.49  
11 1 ASN B 294 ? ? -161.34 -169.48 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A SER 26  ? A SER 1   
2  1 Y 1 A ASN 27  ? A ASN 2   
3  1 Y 1 A LYS 346 ? A LYS 321 
4  1 Y 1 A GLY 347 ? A GLY 322 
5  1 Y 1 A GLY 348 ? A GLY 323 
6  1 Y 1 A VAL 349 ? A VAL 324 
7  1 Y 1 A LYS 418 ? A LYS 393 
8  1 Y 1 A ALA 419 ? A ALA 394 
9  1 Y 1 A GLN 420 ? A GLN 395 
10 1 Y 1 A VAL 421 ? A VAL 396 
11 1 Y 1 A GLN 422 ? A GLN 397 
12 1 Y 1 A LEU 423 ? A LEU 398 
13 1 Y 1 A ASN 424 ? A ASN 399 
14 1 Y 1 B SER 26  ? B SER 1   
15 1 Y 1 B ASN 27  ? B ASN 2   
16 1 Y 1 B LYS 346 ? B LYS 321 
17 1 Y 1 B GLY 347 ? B GLY 322 
18 1 Y 1 B GLY 348 ? B GLY 323 
19 1 Y 1 B VAL 349 ? B VAL 324 
20 1 Y 1 B LYS 418 ? B LYS 393 
21 1 Y 1 B ALA 419 ? B ALA 394 
22 1 Y 1 B GLN 420 ? B GLN 395 
23 1 Y 1 B VAL 421 ? B VAL 396 
24 1 Y 1 B GLN 422 ? B GLN 397 
25 1 Y 1 B LEU 423 ? B LEU 398 
26 1 Y 1 B ASN 424 ? B ASN 399 
# 
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 
A1ASC C1     C  N N 1   
A1ASC C2     C  N N 2   
A1ASC C3     C  N N 3   
A1ASC C5     C  Y N 4   
A1ASC C8     C  Y N 5   
A1ASC C11    C  Y N 6   
A1ASC C12    C  Y N 7   
A1ASC C13    C  Y N 8   
A1ASC C14    C  Y N 9   
A1ASC C15    C  Y N 10  
A1ASC C16    C  N N 11  
A1ASC C17    C  Y N 12  
A1ASC C20    C  N N 13  
A1ASC N      N  N N 14  
A1ASC C      C  N N 15  
A1ASC O      O  N N 16  
A1ASC C10    C  N N 17  
A1ASC C18    C  Y N 18  
A1ASC C19    C  N N 19  
A1ASC C1A    C  N N 20  
A1ASC C1B    C  N N 21  
A1ASC C1C    C  N N 22  
A1ASC C1E    C  N N 23  
A1ASC C1F    C  Y N 24  
A1ASC C1G    C  N N 25  
A1ASC C1H    C  N N 26  
A1ASC C1I    C  N N 27  
A1ASC C1J    C  N N 28  
A1ASC C1K    C  Y N 29  
A1ASC C7     C  Y N 30  
A1ASC C9     C  N N 31  
A1ASC N4     N  N N 32  
A1ASC N6     N  N N 33  
A1ASC O1     O  N N 34  
A1ASC O2     O  N N 35  
A1ASC O3     O  N N 36  
A1ASC H1C    H  N N 37  
A1ASC H1A    H  N N 38  
A1ASC H1B    H  N N 39  
A1ASC H2B    H  N N 40  
A1ASC H2A    H  N N 41  
A1ASC H3A    H  N N 42  
A1ASC H3B    H  N N 43  
A1ASC H11    H  N N 44  
A1ASC H17    H  N N 45  
A1ASC H20B   H  N N 46  
A1ASC H20A   H  N N 47  
A1ASC H10    H  N N 48  
A1ASC H18    H  N N 49  
A1ASC H19A   H  N N 50  
A1ASC H19B   H  N N 51  
A1ASC H1AA   H  N N 52  
A1ASC H1AB   H  N N 53  
A1ASC H1BB   H  N N 54  
A1ASC H1BA   H  N N 55  
A1ASC H1CA   H  N N 56  
A1ASC H1CB   H  N N 57  
A1ASC H1EB   H  N N 58  
A1ASC H1EA   H  N N 59  
A1ASC H1F    H  N N 60  
A1ASC H1GA   H  N N 61  
A1ASC H1GB   H  N N 62  
A1ASC H1HA   H  N N 63  
A1ASC H1HC   H  N N 64  
A1ASC H1HB   H  N N 65  
A1ASC H1IB   H  N N 66  
A1ASC H1IA   H  N N 67  
A1ASC H1JB   H  N N 68  
A1ASC H1JA   H  N N 69  
A1ASC H1K    H  N N 70  
A1ASC H7     H  N N 71  
ALA   N      N  N N 72  
ALA   CA     C  N S 73  
ALA   C      C  N N 74  
ALA   O      O  N N 75  
ALA   CB     C  N N 76  
ALA   OXT    O  N N 77  
ALA   H      H  N N 78  
ALA   H2     H  N N 79  
ALA   HA     H  N N 80  
ALA   HB1    H  N N 81  
ALA   HB2    H  N N 82  
ALA   HB3    H  N N 83  
ALA   HXT    H  N N 84  
ANP   PG     P  N N 85  
ANP   O1G    O  N N 86  
ANP   O2G    O  N N 87  
ANP   O3G    O  N N 88  
ANP   PB     P  N N 89  
ANP   O1B    O  N N 90  
ANP   O2B    O  N N 91  
ANP   N3B    N  N N 92  
ANP   PA     P  N N 93  
ANP   O1A    O  N N 94  
ANP   O2A    O  N N 95  
ANP   O3A    O  N N 96  
ANP   "O5'"  O  N N 97  
ANP   "C5'"  C  N N 98  
ANP   "C4'"  C  N R 99  
ANP   "O4'"  O  N N 100 
ANP   "C3'"  C  N S 101 
ANP   "O3'"  O  N N 102 
ANP   "C2'"  C  N R 103 
ANP   "O2'"  O  N N 104 
ANP   "C1'"  C  N R 105 
ANP   N9     N  Y N 106 
ANP   C8     C  Y N 107 
ANP   N7     N  Y N 108 
ANP   C5     C  Y N 109 
ANP   C6     C  Y N 110 
ANP   N6     N  N N 111 
ANP   N1     N  Y N 112 
ANP   C2     C  Y N 113 
ANP   N3     N  Y N 114 
ANP   C4     C  Y N 115 
ANP   HOG2   H  N N 116 
ANP   HOG3   H  N N 117 
ANP   HOB2   H  N N 118 
ANP   HNB1   H  N N 119 
ANP   HOA2   H  N N 120 
ANP   "H5'1" H  N N 121 
ANP   "H5'2" H  N N 122 
ANP   "H4'"  H  N N 123 
ANP   "H3'"  H  N N 124 
ANP   "HO3'" H  N N 125 
ANP   "H2'"  H  N N 126 
ANP   "HO2'" H  N N 127 
ANP   "H1'"  H  N N 128 
ANP   H8     H  N N 129 
ANP   HN61   H  N N 130 
ANP   HN62   H  N N 131 
ANP   H2     H  N N 132 
ARG   N      N  N N 133 
ARG   CA     C  N S 134 
ARG   C      C  N N 135 
ARG   O      O  N N 136 
ARG   CB     C  N N 137 
ARG   CG     C  N N 138 
ARG   CD     C  N N 139 
ARG   NE     N  N N 140 
ARG   CZ     C  N N 141 
ARG   NH1    N  N N 142 
ARG   NH2    N  N N 143 
ARG   OXT    O  N N 144 
ARG   H      H  N N 145 
ARG   H2     H  N N 146 
ARG   HA     H  N N 147 
ARG   HB2    H  N N 148 
ARG   HB3    H  N N 149 
ARG   HG2    H  N N 150 
ARG   HG3    H  N N 151 
ARG   HD2    H  N N 152 
ARG   HD3    H  N N 153 
ARG   HE     H  N N 154 
ARG   HH11   H  N N 155 
ARG   HH12   H  N N 156 
ARG   HH21   H  N N 157 
ARG   HH22   H  N N 158 
ARG   HXT    H  N N 159 
ASN   N      N  N N 160 
ASN   CA     C  N S 161 
ASN   C      C  N N 162 
ASN   O      O  N N 163 
ASN   CB     C  N N 164 
ASN   CG     C  N N 165 
ASN   OD1    O  N N 166 
ASN   ND2    N  N N 167 
ASN   OXT    O  N N 168 
ASN   H      H  N N 169 
ASN   H2     H  N N 170 
ASN   HA     H  N N 171 
ASN   HB2    H  N N 172 
ASN   HB3    H  N N 173 
ASN   HD21   H  N N 174 
ASN   HD22   H  N N 175 
ASN   HXT    H  N N 176 
ASP   N      N  N N 177 
ASP   CA     C  N S 178 
ASP   C      C  N N 179 
ASP   O      O  N N 180 
ASP   CB     C  N N 181 
ASP   CG     C  N N 182 
ASP   OD1    O  N N 183 
ASP   OD2    O  N N 184 
ASP   OXT    O  N N 185 
ASP   H      H  N N 186 
ASP   H2     H  N N 187 
ASP   HA     H  N N 188 
ASP   HB2    H  N N 189 
ASP   HB3    H  N N 190 
ASP   HD2    H  N N 191 
ASP   HXT    H  N N 192 
CL    CL     CL N N 193 
CYS   N      N  N N 194 
CYS   CA     C  N R 195 
CYS   C      C  N N 196 
CYS   O      O  N N 197 
CYS   CB     C  N N 198 
CYS   SG     S  N N 199 
CYS   OXT    O  N N 200 
CYS   H      H  N N 201 
CYS   H2     H  N N 202 
CYS   HA     H  N N 203 
CYS   HB2    H  N N 204 
CYS   HB3    H  N N 205 
CYS   HG     H  N N 206 
CYS   HXT    H  N N 207 
GLN   N      N  N N 208 
GLN   CA     C  N S 209 
GLN   C      C  N N 210 
GLN   O      O  N N 211 
GLN   CB     C  N N 212 
GLN   CG     C  N N 213 
GLN   CD     C  N N 214 
GLN   OE1    O  N N 215 
GLN   NE2    N  N N 216 
GLN   OXT    O  N N 217 
GLN   H      H  N N 218 
GLN   H2     H  N N 219 
GLN   HA     H  N N 220 
GLN   HB2    H  N N 221 
GLN   HB3    H  N N 222 
GLN   HG2    H  N N 223 
GLN   HG3    H  N N 224 
GLN   HE21   H  N N 225 
GLN   HE22   H  N N 226 
GLN   HXT    H  N N 227 
GLU   N      N  N N 228 
GLU   CA     C  N S 229 
GLU   C      C  N N 230 
GLU   O      O  N N 231 
GLU   CB     C  N N 232 
GLU   CG     C  N N 233 
GLU   CD     C  N N 234 
GLU   OE1    O  N N 235 
GLU   OE2    O  N N 236 
GLU   OXT    O  N N 237 
GLU   H      H  N N 238 
GLU   H2     H  N N 239 
GLU   HA     H  N N 240 
GLU   HB2    H  N N 241 
GLU   HB3    H  N N 242 
GLU   HG2    H  N N 243 
GLU   HG3    H  N N 244 
GLU   HE2    H  N N 245 
GLU   HXT    H  N N 246 
GLY   N      N  N N 247 
GLY   CA     C  N N 248 
GLY   C      C  N N 249 
GLY   O      O  N N 250 
GLY   OXT    O  N N 251 
GLY   H      H  N N 252 
GLY   H2     H  N N 253 
GLY   HA2    H  N N 254 
GLY   HA3    H  N N 255 
GLY   HXT    H  N N 256 
GOL   C1     C  N N 257 
GOL   O1     O  N N 258 
GOL   C2     C  N N 259 
GOL   O2     O  N N 260 
GOL   C3     C  N N 261 
GOL   O3     O  N N 262 
GOL   H11    H  N N 263 
GOL   H12    H  N N 264 
GOL   HO1    H  N N 265 
GOL   H2     H  N N 266 
GOL   HO2    H  N N 267 
GOL   H31    H  N N 268 
GOL   H32    H  N N 269 
GOL   HO3    H  N N 270 
HIS   N      N  N N 271 
HIS   CA     C  N S 272 
HIS   C      C  N N 273 
HIS   O      O  N N 274 
HIS   CB     C  N N 275 
HIS   CG     C  Y N 276 
HIS   ND1    N  Y N 277 
HIS   CD2    C  Y N 278 
HIS   CE1    C  Y N 279 
HIS   NE2    N  Y N 280 
HIS   OXT    O  N N 281 
HIS   H      H  N N 282 
HIS   H2     H  N N 283 
HIS   HA     H  N N 284 
HIS   HB2    H  N N 285 
HIS   HB3    H  N N 286 
HIS   HD1    H  N N 287 
HIS   HD2    H  N N 288 
HIS   HE1    H  N N 289 
HIS   HE2    H  N N 290 
HIS   HXT    H  N N 291 
HOH   O      O  N N 292 
HOH   H1     H  N N 293 
HOH   H2     H  N N 294 
ILE   N      N  N N 295 
ILE   CA     C  N S 296 
ILE   C      C  N N 297 
ILE   O      O  N N 298 
ILE   CB     C  N S 299 
ILE   CG1    C  N N 300 
ILE   CG2    C  N N 301 
ILE   CD1    C  N N 302 
ILE   OXT    O  N N 303 
ILE   H      H  N N 304 
ILE   H2     H  N N 305 
ILE   HA     H  N N 306 
ILE   HB     H  N N 307 
ILE   HG12   H  N N 308 
ILE   HG13   H  N N 309 
ILE   HG21   H  N N 310 
ILE   HG22   H  N N 311 
ILE   HG23   H  N N 312 
ILE   HD11   H  N N 313 
ILE   HD12   H  N N 314 
ILE   HD13   H  N N 315 
ILE   HXT    H  N N 316 
LEU   N      N  N N 317 
LEU   CA     C  N S 318 
LEU   C      C  N N 319 
LEU   O      O  N N 320 
LEU   CB     C  N N 321 
LEU   CG     C  N N 322 
LEU   CD1    C  N N 323 
LEU   CD2    C  N N 324 
LEU   OXT    O  N N 325 
LEU   H      H  N N 326 
LEU   H2     H  N N 327 
LEU   HA     H  N N 328 
LEU   HB2    H  N N 329 
LEU   HB3    H  N N 330 
LEU   HG     H  N N 331 
LEU   HD11   H  N N 332 
LEU   HD12   H  N N 333 
LEU   HD13   H  N N 334 
LEU   HD21   H  N N 335 
LEU   HD22   H  N N 336 
LEU   HD23   H  N N 337 
LEU   HXT    H  N N 338 
LYS   N      N  N N 339 
LYS   CA     C  N S 340 
LYS   C      C  N N 341 
LYS   O      O  N N 342 
LYS   CB     C  N N 343 
LYS   CG     C  N N 344 
LYS   CD     C  N N 345 
LYS   CE     C  N N 346 
LYS   NZ     N  N N 347 
LYS   OXT    O  N N 348 
LYS   H      H  N N 349 
LYS   H2     H  N N 350 
LYS   HA     H  N N 351 
LYS   HB2    H  N N 352 
LYS   HB3    H  N N 353 
LYS   HG2    H  N N 354 
LYS   HG3    H  N N 355 
LYS   HD2    H  N N 356 
LYS   HD3    H  N N 357 
LYS   HE2    H  N N 358 
LYS   HE3    H  N N 359 
LYS   HZ1    H  N N 360 
LYS   HZ2    H  N N 361 
LYS   HZ3    H  N N 362 
LYS   HXT    H  N N 363 
MET   N      N  N N 364 
MET   CA     C  N S 365 
MET   C      C  N N 366 
MET   O      O  N N 367 
MET   CB     C  N N 368 
MET   CG     C  N N 369 
MET   SD     S  N N 370 
MET   CE     C  N N 371 
MET   OXT    O  N N 372 
MET   H      H  N N 373 
MET   H2     H  N N 374 
MET   HA     H  N N 375 
MET   HB2    H  N N 376 
MET   HB3    H  N N 377 
MET   HG2    H  N N 378 
MET   HG3    H  N N 379 
MET   HE1    H  N N 380 
MET   HE2    H  N N 381 
MET   HE3    H  N N 382 
MET   HXT    H  N N 383 
MG    MG     MG N N 384 
PHE   N      N  N N 385 
PHE   CA     C  N S 386 
PHE   C      C  N N 387 
PHE   O      O  N N 388 
PHE   CB     C  N N 389 
PHE   CG     C  Y N 390 
PHE   CD1    C  Y N 391 
PHE   CD2    C  Y N 392 
PHE   CE1    C  Y N 393 
PHE   CE2    C  Y N 394 
PHE   CZ     C  Y N 395 
PHE   OXT    O  N N 396 
PHE   H      H  N N 397 
PHE   H2     H  N N 398 
PHE   HA     H  N N 399 
PHE   HB2    H  N N 400 
PHE   HB3    H  N N 401 
PHE   HD1    H  N N 402 
PHE   HD2    H  N N 403 
PHE   HE1    H  N N 404 
PHE   HE2    H  N N 405 
PHE   HZ     H  N N 406 
PHE   HXT    H  N N 407 
PRO   N      N  N N 408 
PRO   CA     C  N S 409 
PRO   C      C  N N 410 
PRO   O      O  N N 411 
PRO   CB     C  N N 412 
PRO   CG     C  N N 413 
PRO   CD     C  N N 414 
PRO   OXT    O  N N 415 
PRO   H      H  N N 416 
PRO   HA     H  N N 417 
PRO   HB2    H  N N 418 
PRO   HB3    H  N N 419 
PRO   HG2    H  N N 420 
PRO   HG3    H  N N 421 
PRO   HD2    H  N N 422 
PRO   HD3    H  N N 423 
PRO   HXT    H  N N 424 
SER   N      N  N N 425 
SER   CA     C  N S 426 
SER   C      C  N N 427 
SER   O      O  N N 428 
SER   CB     C  N N 429 
SER   OG     O  N N 430 
SER   OXT    O  N N 431 
SER   H      H  N N 432 
SER   H2     H  N N 433 
SER   HA     H  N N 434 
SER   HB2    H  N N 435 
SER   HB3    H  N N 436 
SER   HG     H  N N 437 
SER   HXT    H  N N 438 
THR   N      N  N N 439 
THR   CA     C  N S 440 
THR   C      C  N N 441 
THR   O      O  N N 442 
THR   CB     C  N R 443 
THR   OG1    O  N N 444 
THR   CG2    C  N N 445 
THR   OXT    O  N N 446 
THR   H      H  N N 447 
THR   H2     H  N N 448 
THR   HA     H  N N 449 
THR   HB     H  N N 450 
THR   HG1    H  N N 451 
THR   HG21   H  N N 452 
THR   HG22   H  N N 453 
THR   HG23   H  N N 454 
THR   HXT    H  N N 455 
TRP   N      N  N N 456 
TRP   CA     C  N S 457 
TRP   C      C  N N 458 
TRP   O      O  N N 459 
TRP   CB     C  N N 460 
TRP   CG     C  Y N 461 
TRP   CD1    C  Y N 462 
TRP   CD2    C  Y N 463 
TRP   NE1    N  Y N 464 
TRP   CE2    C  Y N 465 
TRP   CE3    C  Y N 466 
TRP   CZ2    C  Y N 467 
TRP   CZ3    C  Y N 468 
TRP   CH2    C  Y N 469 
TRP   OXT    O  N N 470 
TRP   H      H  N N 471 
TRP   H2     H  N N 472 
TRP   HA     H  N N 473 
TRP   HB2    H  N N 474 
TRP   HB3    H  N N 475 
TRP   HD1    H  N N 476 
TRP   HE1    H  N N 477 
TRP   HE3    H  N N 478 
TRP   HZ2    H  N N 479 
TRP   HZ3    H  N N 480 
TRP   HH2    H  N N 481 
TRP   HXT    H  N N 482 
TYR   N      N  N N 483 
TYR   CA     C  N S 484 
TYR   C      C  N N 485 
TYR   O      O  N N 486 
TYR   CB     C  N N 487 
TYR   CG     C  Y N 488 
TYR   CD1    C  Y N 489 
TYR   CD2    C  Y N 490 
TYR   CE1    C  Y N 491 
TYR   CE2    C  Y N 492 
TYR   CZ     C  Y N 493 
TYR   OH     O  N N 494 
TYR   OXT    O  N N 495 
TYR   H      H  N N 496 
TYR   H2     H  N N 497 
TYR   HA     H  N N 498 
TYR   HB2    H  N N 499 
TYR   HB3    H  N N 500 
TYR   HD1    H  N N 501 
TYR   HD2    H  N N 502 
TYR   HE1    H  N N 503 
TYR   HE2    H  N N 504 
TYR   HH     H  N N 505 
TYR   HXT    H  N N 506 
VAL   N      N  N N 507 
VAL   CA     C  N S 508 
VAL   C      C  N N 509 
VAL   O      O  N N 510 
VAL   CB     C  N N 511 
VAL   CG1    C  N N 512 
VAL   CG2    C  N N 513 
VAL   OXT    O  N N 514 
VAL   H      H  N N 515 
VAL   H2     H  N N 516 
VAL   HA     H  N N 517 
VAL   HB     H  N N 518 
VAL   HG11   H  N N 519 
VAL   HG12   H  N N 520 
VAL   HG13   H  N N 521 
VAL   HG21   H  N N 522 
VAL   HG22   H  N N 523 
VAL   HG23   H  N N 524 
VAL   HXT    H  N N 525 
# 
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 
A1ASC C1H   C1E    sing N N 1   
A1ASC C1E   C19    sing N N 2   
A1ASC C19   C9     sing N N 3   
A1ASC C10   C9     doub N N 4   
A1ASC C10   C16    sing N N 5   
A1ASC O3    C16    doub N N 6   
A1ASC C9    C14    sing N N 7   
A1ASC C16   O1     sing N N 8   
A1ASC C14   C12    doub Y N 9   
A1ASC C14   C11    sing Y N 10  
A1ASC O1    C12    sing N N 11  
A1ASC C12   C5     sing Y N 12  
A1ASC C11   C7     doub Y N 13  
A1ASC C1G   C15    sing N N 14  
A1ASC C1G   C1I    sing N N 15  
A1ASC C18   C15    doub Y N 16  
A1ASC C18   C1F    sing Y N 17  
A1ASC C15   C8     sing Y N 18  
A1ASC C1F   C1K    doub Y N 19  
A1ASC C5    C      sing N N 20  
A1ASC C5    C13    doub Y N 21  
A1ASC C7    C13    sing Y N 22  
A1ASC C1I   C1B    sing N N 23  
A1ASC C8    N4     sing N N 24  
A1ASC C8    C17    doub Y N 25  
A1ASC C1K   C17    sing Y N 26  
A1ASC N4    C      sing N N 27  
A1ASC N4    C1B    sing N N 28  
A1ASC C     O2     doub N N 29  
A1ASC C13   O      sing N N 30  
A1ASC O     C20    sing N N 31  
A1ASC C20   C3     sing N N 32  
A1ASC C3    N      sing N N 33  
A1ASC C2    N      sing N N 34  
A1ASC C2    C1J    sing N N 35  
A1ASC N     C1C    sing N N 36  
A1ASC C1J   N6     sing N N 37  
A1ASC C1C   C1A    sing N N 38  
A1ASC N6    C1A    sing N N 39  
A1ASC N6    C1     sing N N 40  
A1ASC C1    H1C    sing N N 41  
A1ASC C1    H1A    sing N N 42  
A1ASC C1    H1B    sing N N 43  
A1ASC C2    H2B    sing N N 44  
A1ASC C2    H2A    sing N N 45  
A1ASC C3    H3A    sing N N 46  
A1ASC C3    H3B    sing N N 47  
A1ASC C11   H11    sing N N 48  
A1ASC C17   H17    sing N N 49  
A1ASC C20   H20B   sing N N 50  
A1ASC C20   H20A   sing N N 51  
A1ASC C10   H10    sing N N 52  
A1ASC C18   H18    sing N N 53  
A1ASC C19   H19A   sing N N 54  
A1ASC C19   H19B   sing N N 55  
A1ASC C1A   H1AA   sing N N 56  
A1ASC C1A   H1AB   sing N N 57  
A1ASC C1B   H1BB   sing N N 58  
A1ASC C1B   H1BA   sing N N 59  
A1ASC C1C   H1CA   sing N N 60  
A1ASC C1C   H1CB   sing N N 61  
A1ASC C1E   H1EB   sing N N 62  
A1ASC C1E   H1EA   sing N N 63  
A1ASC C1F   H1F    sing N N 64  
A1ASC C1G   H1GA   sing N N 65  
A1ASC C1G   H1GB   sing N N 66  
A1ASC C1H   H1HA   sing N N 67  
A1ASC C1H   H1HC   sing N N 68  
A1ASC C1H   H1HB   sing N N 69  
A1ASC C1I   H1IB   sing N N 70  
A1ASC C1I   H1IA   sing N N 71  
A1ASC C1J   H1JB   sing N N 72  
A1ASC C1J   H1JA   sing N N 73  
A1ASC C1K   H1K    sing N N 74  
A1ASC C7    H7     sing N N 75  
ALA   N     CA     sing N N 76  
ALA   N     H      sing N N 77  
ALA   N     H2     sing N N 78  
ALA   CA    C      sing N N 79  
ALA   CA    CB     sing N N 80  
ALA   CA    HA     sing N N 81  
ALA   C     O      doub N N 82  
ALA   C     OXT    sing N N 83  
ALA   CB    HB1    sing N N 84  
ALA   CB    HB2    sing N N 85  
ALA   CB    HB3    sing N N 86  
ALA   OXT   HXT    sing N N 87  
ANP   PG    O1G    doub N N 88  
ANP   PG    O2G    sing N N 89  
ANP   PG    O3G    sing N N 90  
ANP   PG    N3B    sing N N 91  
ANP   O2G   HOG2   sing N N 92  
ANP   O3G   HOG3   sing N N 93  
ANP   PB    O1B    doub N N 94  
ANP   PB    O2B    sing N N 95  
ANP   PB    N3B    sing N N 96  
ANP   PB    O3A    sing N N 97  
ANP   O2B   HOB2   sing N N 98  
ANP   N3B   HNB1   sing N N 99  
ANP   PA    O1A    doub N N 100 
ANP   PA    O2A    sing N N 101 
ANP   PA    O3A    sing N N 102 
ANP   PA    "O5'"  sing N N 103 
ANP   O2A   HOA2   sing N N 104 
ANP   "O5'" "C5'"  sing N N 105 
ANP   "C5'" "C4'"  sing N N 106 
ANP   "C5'" "H5'1" sing N N 107 
ANP   "C5'" "H5'2" sing N N 108 
ANP   "C4'" "O4'"  sing N N 109 
ANP   "C4'" "C3'"  sing N N 110 
ANP   "C4'" "H4'"  sing N N 111 
ANP   "O4'" "C1'"  sing N N 112 
ANP   "C3'" "O3'"  sing N N 113 
ANP   "C3'" "C2'"  sing N N 114 
ANP   "C3'" "H3'"  sing N N 115 
ANP   "O3'" "HO3'" sing N N 116 
ANP   "C2'" "O2'"  sing N N 117 
ANP   "C2'" "C1'"  sing N N 118 
ANP   "C2'" "H2'"  sing N N 119 
ANP   "O2'" "HO2'" sing N N 120 
ANP   "C1'" N9     sing N N 121 
ANP   "C1'" "H1'"  sing N N 122 
ANP   N9    C8     sing Y N 123 
ANP   N9    C4     sing Y N 124 
ANP   C8    N7     doub Y N 125 
ANP   C8    H8     sing N N 126 
ANP   N7    C5     sing Y N 127 
ANP   C5    C6     sing Y N 128 
ANP   C5    C4     doub Y N 129 
ANP   C6    N6     sing N N 130 
ANP   C6    N1     doub Y N 131 
ANP   N6    HN61   sing N N 132 
ANP   N6    HN62   sing N N 133 
ANP   N1    C2     sing Y N 134 
ANP   C2    N3     doub Y N 135 
ANP   C2    H2     sing N N 136 
ANP   N3    C4     sing Y N 137 
ARG   N     CA     sing N N 138 
ARG   N     H      sing N N 139 
ARG   N     H2     sing N N 140 
ARG   CA    C      sing N N 141 
ARG   CA    CB     sing N N 142 
ARG   CA    HA     sing N N 143 
ARG   C     O      doub N N 144 
ARG   C     OXT    sing N N 145 
ARG   CB    CG     sing N N 146 
ARG   CB    HB2    sing N N 147 
ARG   CB    HB3    sing N N 148 
ARG   CG    CD     sing N N 149 
ARG   CG    HG2    sing N N 150 
ARG   CG    HG3    sing N N 151 
ARG   CD    NE     sing N N 152 
ARG   CD    HD2    sing N N 153 
ARG   CD    HD3    sing N N 154 
ARG   NE    CZ     sing N N 155 
ARG   NE    HE     sing N N 156 
ARG   CZ    NH1    sing N N 157 
ARG   CZ    NH2    doub N N 158 
ARG   NH1   HH11   sing N N 159 
ARG   NH1   HH12   sing N N 160 
ARG   NH2   HH21   sing N N 161 
ARG   NH2   HH22   sing N N 162 
ARG   OXT   HXT    sing N N 163 
ASN   N     CA     sing N N 164 
ASN   N     H      sing N N 165 
ASN   N     H2     sing N N 166 
ASN   CA    C      sing N N 167 
ASN   CA    CB     sing N N 168 
ASN   CA    HA     sing N N 169 
ASN   C     O      doub N N 170 
ASN   C     OXT    sing N N 171 
ASN   CB    CG     sing N N 172 
ASN   CB    HB2    sing N N 173 
ASN   CB    HB3    sing N N 174 
ASN   CG    OD1    doub N N 175 
ASN   CG    ND2    sing N N 176 
ASN   ND2   HD21   sing N N 177 
ASN   ND2   HD22   sing N N 178 
ASN   OXT   HXT    sing N N 179 
ASP   N     CA     sing N N 180 
ASP   N     H      sing N N 181 
ASP   N     H2     sing N N 182 
ASP   CA    C      sing N N 183 
ASP   CA    CB     sing N N 184 
ASP   CA    HA     sing N N 185 
ASP   C     O      doub N N 186 
ASP   C     OXT    sing N N 187 
ASP   CB    CG     sing N N 188 
ASP   CB    HB2    sing N N 189 
ASP   CB    HB3    sing N N 190 
ASP   CG    OD1    doub N N 191 
ASP   CG    OD2    sing N N 192 
ASP   OD2   HD2    sing N N 193 
ASP   OXT   HXT    sing N N 194 
CYS   N     CA     sing N N 195 
CYS   N     H      sing N N 196 
CYS   N     H2     sing N N 197 
CYS   CA    C      sing N N 198 
CYS   CA    CB     sing N N 199 
CYS   CA    HA     sing N N 200 
CYS   C     O      doub N N 201 
CYS   C     OXT    sing N N 202 
CYS   CB    SG     sing N N 203 
CYS   CB    HB2    sing N N 204 
CYS   CB    HB3    sing N N 205 
CYS   SG    HG     sing N N 206 
CYS   OXT   HXT    sing N N 207 
GLN   N     CA     sing N N 208 
GLN   N     H      sing N N 209 
GLN   N     H2     sing N N 210 
GLN   CA    C      sing N N 211 
GLN   CA    CB     sing N N 212 
GLN   CA    HA     sing N N 213 
GLN   C     O      doub N N 214 
GLN   C     OXT    sing N N 215 
GLN   CB    CG     sing N N 216 
GLN   CB    HB2    sing N N 217 
GLN   CB    HB3    sing N N 218 
GLN   CG    CD     sing N N 219 
GLN   CG    HG2    sing N N 220 
GLN   CG    HG3    sing N N 221 
GLN   CD    OE1    doub N N 222 
GLN   CD    NE2    sing N N 223 
GLN   NE2   HE21   sing N N 224 
GLN   NE2   HE22   sing N N 225 
GLN   OXT   HXT    sing N N 226 
GLU   N     CA     sing N N 227 
GLU   N     H      sing N N 228 
GLU   N     H2     sing N N 229 
GLU   CA    C      sing N N 230 
GLU   CA    CB     sing N N 231 
GLU   CA    HA     sing N N 232 
GLU   C     O      doub N N 233 
GLU   C     OXT    sing N N 234 
GLU   CB    CG     sing N N 235 
GLU   CB    HB2    sing N N 236 
GLU   CB    HB3    sing N N 237 
GLU   CG    CD     sing N N 238 
GLU   CG    HG2    sing N N 239 
GLU   CG    HG3    sing N N 240 
GLU   CD    OE1    doub N N 241 
GLU   CD    OE2    sing N N 242 
GLU   OE2   HE2    sing N N 243 
GLU   OXT   HXT    sing N N 244 
GLY   N     CA     sing N N 245 
GLY   N     H      sing N N 246 
GLY   N     H2     sing N N 247 
GLY   CA    C      sing N N 248 
GLY   CA    HA2    sing N N 249 
GLY   CA    HA3    sing N N 250 
GLY   C     O      doub N N 251 
GLY   C     OXT    sing N N 252 
GLY   OXT   HXT    sing N N 253 
GOL   C1    O1     sing N N 254 
GOL   C1    C2     sing N N 255 
GOL   C1    H11    sing N N 256 
GOL   C1    H12    sing N N 257 
GOL   O1    HO1    sing N N 258 
GOL   C2    O2     sing N N 259 
GOL   C2    C3     sing N N 260 
GOL   C2    H2     sing N N 261 
GOL   O2    HO2    sing N N 262 
GOL   C3    O3     sing N N 263 
GOL   C3    H31    sing N N 264 
GOL   C3    H32    sing N N 265 
GOL   O3    HO3    sing N N 266 
HIS   N     CA     sing N N 267 
HIS   N     H      sing N N 268 
HIS   N     H2     sing N N 269 
HIS   CA    C      sing N N 270 
HIS   CA    CB     sing N N 271 
HIS   CA    HA     sing N N 272 
HIS   C     O      doub N N 273 
HIS   C     OXT    sing N N 274 
HIS   CB    CG     sing N N 275 
HIS   CB    HB2    sing N N 276 
HIS   CB    HB3    sing N N 277 
HIS   CG    ND1    sing Y N 278 
HIS   CG    CD2    doub Y N 279 
HIS   ND1   CE1    doub Y N 280 
HIS   ND1   HD1    sing N N 281 
HIS   CD2   NE2    sing Y N 282 
HIS   CD2   HD2    sing N N 283 
HIS   CE1   NE2    sing Y N 284 
HIS   CE1   HE1    sing N N 285 
HIS   NE2   HE2    sing N N 286 
HIS   OXT   HXT    sing N N 287 
HOH   O     H1     sing N N 288 
HOH   O     H2     sing N N 289 
ILE   N     CA     sing N N 290 
ILE   N     H      sing N N 291 
ILE   N     H2     sing N N 292 
ILE   CA    C      sing N N 293 
ILE   CA    CB     sing N N 294 
ILE   CA    HA     sing N N 295 
ILE   C     O      doub N N 296 
ILE   C     OXT    sing N N 297 
ILE   CB    CG1    sing N N 298 
ILE   CB    CG2    sing N N 299 
ILE   CB    HB     sing N N 300 
ILE   CG1   CD1    sing N N 301 
ILE   CG1   HG12   sing N N 302 
ILE   CG1   HG13   sing N N 303 
ILE   CG2   HG21   sing N N 304 
ILE   CG2   HG22   sing N N 305 
ILE   CG2   HG23   sing N N 306 
ILE   CD1   HD11   sing N N 307 
ILE   CD1   HD12   sing N N 308 
ILE   CD1   HD13   sing N N 309 
ILE   OXT   HXT    sing N N 310 
LEU   N     CA     sing N N 311 
LEU   N     H      sing N N 312 
LEU   N     H2     sing N N 313 
LEU   CA    C      sing N N 314 
LEU   CA    CB     sing N N 315 
LEU   CA    HA     sing N N 316 
LEU   C     O      doub N N 317 
LEU   C     OXT    sing N N 318 
LEU   CB    CG     sing N N 319 
LEU   CB    HB2    sing N N 320 
LEU   CB    HB3    sing N N 321 
LEU   CG    CD1    sing N N 322 
LEU   CG    CD2    sing N N 323 
LEU   CG    HG     sing N N 324 
LEU   CD1   HD11   sing N N 325 
LEU   CD1   HD12   sing N N 326 
LEU   CD1   HD13   sing N N 327 
LEU   CD2   HD21   sing N N 328 
LEU   CD2   HD22   sing N N 329 
LEU   CD2   HD23   sing N N 330 
LEU   OXT   HXT    sing N N 331 
LYS   N     CA     sing N N 332 
LYS   N     H      sing N N 333 
LYS   N     H2     sing N N 334 
LYS   CA    C      sing N N 335 
LYS   CA    CB     sing N N 336 
LYS   CA    HA     sing N N 337 
LYS   C     O      doub N N 338 
LYS   C     OXT    sing N N 339 
LYS   CB    CG     sing N N 340 
LYS   CB    HB2    sing N N 341 
LYS   CB    HB3    sing N N 342 
LYS   CG    CD     sing N N 343 
LYS   CG    HG2    sing N N 344 
LYS   CG    HG3    sing N N 345 
LYS   CD    CE     sing N N 346 
LYS   CD    HD2    sing N N 347 
LYS   CD    HD3    sing N N 348 
LYS   CE    NZ     sing N N 349 
LYS   CE    HE2    sing N N 350 
LYS   CE    HE3    sing N N 351 
LYS   NZ    HZ1    sing N N 352 
LYS   NZ    HZ2    sing N N 353 
LYS   NZ    HZ3    sing N N 354 
LYS   OXT   HXT    sing N N 355 
MET   N     CA     sing N N 356 
MET   N     H      sing N N 357 
MET   N     H2     sing N N 358 
MET   CA    C      sing N N 359 
MET   CA    CB     sing N N 360 
MET   CA    HA     sing N N 361 
MET   C     O      doub N N 362 
MET   C     OXT    sing N N 363 
MET   CB    CG     sing N N 364 
MET   CB    HB2    sing N N 365 
MET   CB    HB3    sing N N 366 
MET   CG    SD     sing N N 367 
MET   CG    HG2    sing N N 368 
MET   CG    HG3    sing N N 369 
MET   SD    CE     sing N N 370 
MET   CE    HE1    sing N N 371 
MET   CE    HE2    sing N N 372 
MET   CE    HE3    sing N N 373 
MET   OXT   HXT    sing N N 374 
PHE   N     CA     sing N N 375 
PHE   N     H      sing N N 376 
PHE   N     H2     sing N N 377 
PHE   CA    C      sing N N 378 
PHE   CA    CB     sing N N 379 
PHE   CA    HA     sing N N 380 
PHE   C     O      doub N N 381 
PHE   C     OXT    sing N N 382 
PHE   CB    CG     sing N N 383 
PHE   CB    HB2    sing N N 384 
PHE   CB    HB3    sing N N 385 
PHE   CG    CD1    doub Y N 386 
PHE   CG    CD2    sing Y N 387 
PHE   CD1   CE1    sing Y N 388 
PHE   CD1   HD1    sing N N 389 
PHE   CD2   CE2    doub Y N 390 
PHE   CD2   HD2    sing N N 391 
PHE   CE1   CZ     doub Y N 392 
PHE   CE1   HE1    sing N N 393 
PHE   CE2   CZ     sing Y N 394 
PHE   CE2   HE2    sing N N 395 
PHE   CZ    HZ     sing N N 396 
PHE   OXT   HXT    sing N N 397 
PRO   N     CA     sing N N 398 
PRO   N     CD     sing N N 399 
PRO   N     H      sing N N 400 
PRO   CA    C      sing N N 401 
PRO   CA    CB     sing N N 402 
PRO   CA    HA     sing N N 403 
PRO   C     O      doub N N 404 
PRO   C     OXT    sing N N 405 
PRO   CB    CG     sing N N 406 
PRO   CB    HB2    sing N N 407 
PRO   CB    HB3    sing N N 408 
PRO   CG    CD     sing N N 409 
PRO   CG    HG2    sing N N 410 
PRO   CG    HG3    sing N N 411 
PRO   CD    HD2    sing N N 412 
PRO   CD    HD3    sing N N 413 
PRO   OXT   HXT    sing N N 414 
SER   N     CA     sing N N 415 
SER   N     H      sing N N 416 
SER   N     H2     sing N N 417 
SER   CA    C      sing N N 418 
SER   CA    CB     sing N N 419 
SER   CA    HA     sing N N 420 
SER   C     O      doub N N 421 
SER   C     OXT    sing N N 422 
SER   CB    OG     sing N N 423 
SER   CB    HB2    sing N N 424 
SER   CB    HB3    sing N N 425 
SER   OG    HG     sing N N 426 
SER   OXT   HXT    sing N N 427 
THR   N     CA     sing N N 428 
THR   N     H      sing N N 429 
THR   N     H2     sing N N 430 
THR   CA    C      sing N N 431 
THR   CA    CB     sing N N 432 
THR   CA    HA     sing N N 433 
THR   C     O      doub N N 434 
THR   C     OXT    sing N N 435 
THR   CB    OG1    sing N N 436 
THR   CB    CG2    sing N N 437 
THR   CB    HB     sing N N 438 
THR   OG1   HG1    sing N N 439 
THR   CG2   HG21   sing N N 440 
THR   CG2   HG22   sing N N 441 
THR   CG2   HG23   sing N N 442 
THR   OXT   HXT    sing N N 443 
TRP   N     CA     sing N N 444 
TRP   N     H      sing N N 445 
TRP   N     H2     sing N N 446 
TRP   CA    C      sing N N 447 
TRP   CA    CB     sing N N 448 
TRP   CA    HA     sing N N 449 
TRP   C     O      doub N N 450 
TRP   C     OXT    sing N N 451 
TRP   CB    CG     sing N N 452 
TRP   CB    HB2    sing N N 453 
TRP   CB    HB3    sing N N 454 
TRP   CG    CD1    doub Y N 455 
TRP   CG    CD2    sing Y N 456 
TRP   CD1   NE1    sing Y N 457 
TRP   CD1   HD1    sing N N 458 
TRP   CD2   CE2    doub Y N 459 
TRP   CD2   CE3    sing Y N 460 
TRP   NE1   CE2    sing Y N 461 
TRP   NE1   HE1    sing N N 462 
TRP   CE2   CZ2    sing Y N 463 
TRP   CE3   CZ3    doub Y N 464 
TRP   CE3   HE3    sing N N 465 
TRP   CZ2   CH2    doub Y N 466 
TRP   CZ2   HZ2    sing N N 467 
TRP   CZ3   CH2    sing Y N 468 
TRP   CZ3   HZ3    sing N N 469 
TRP   CH2   HH2    sing N N 470 
TRP   OXT   HXT    sing N N 471 
TYR   N     CA     sing N N 472 
TYR   N     H      sing N N 473 
TYR   N     H2     sing N N 474 
TYR   CA    C      sing N N 475 
TYR   CA    CB     sing N N 476 
TYR   CA    HA     sing N N 477 
TYR   C     O      doub N N 478 
TYR   C     OXT    sing N N 479 
TYR   CB    CG     sing N N 480 
TYR   CB    HB2    sing N N 481 
TYR   CB    HB3    sing N N 482 
TYR   CG    CD1    doub Y N 483 
TYR   CG    CD2    sing Y N 484 
TYR   CD1   CE1    sing Y N 485 
TYR   CD1   HD1    sing N N 486 
TYR   CD2   CE2    doub Y N 487 
TYR   CD2   HD2    sing N N 488 
TYR   CE1   CZ     doub Y N 489 
TYR   CE1   HE1    sing N N 490 
TYR   CE2   CZ     sing Y N 491 
TYR   CE2   HE2    sing N N 492 
TYR   CZ    OH     sing N N 493 
TYR   OH    HH     sing N N 494 
TYR   OXT   HXT    sing N N 495 
VAL   N     CA     sing N N 496 
VAL   N     H      sing N N 497 
VAL   N     H2     sing N N 498 
VAL   CA    C      sing N N 499 
VAL   CA    CB     sing N N 500 
VAL   CA    HA     sing N N 501 
VAL   C     O      doub N N 502 
VAL   C     OXT    sing N N 503 
VAL   CB    CG1    sing N N 504 
VAL   CB    CG2    sing N N 505 
VAL   CB    HB     sing N N 506 
VAL   CG1   HG11   sing N N 507 
VAL   CG1   HG12   sing N N 508 
VAL   CG1   HG13   sing N N 509 
VAL   CG2   HG21   sing N N 510 
VAL   CG2   HG22   sing N N 511 
VAL   CG2   HG23   sing N N 512 
VAL   OXT   HXT    sing N N 513 
# 
_pdbx_audit_support.funding_organization   'Other private' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_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   1zxm 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9BQB 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.014327 
_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]   0.010807 
_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]   0.007963 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
H  
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N      . ALA   A 1 3   ? 23.911  -42.440 11.635 1.00 58.87  ?  28  ALA   A N      1 
ATOM   2     C  CA     . ALA   A 1 3   ? 25.011  -41.547 11.994 1.00 57.55  ?  28  ALA   A CA     1 
ATOM   3     C  C      . ALA   A 1 3   ? 25.456  -40.699 10.800 1.00 54.59  ?  28  ALA   A C      1 
ATOM   4     O  O      . ALA   A 1 3   ? 26.614  -40.283 10.704 1.00 54.30  ?  28  ALA   A O      1 
ATOM   5     C  CB     . ALA   A 1 3   ? 26.186  -42.357 12.537 1.00 58.47  ?  28  ALA   A CB     1 
ATOM   6     H  HA     . ALA   A 1 3   ? 24.709  -40.941 12.689 1.00 69.05  ?  28  ALA   A HA     1 
ATOM   7     H  HB1    . ALA   A 1 3   ? 26.905  -41.751 12.772 1.00 70.15  ?  28  ALA   A HB1    1 
ATOM   8     H  HB2    . ALA   A 1 3   ? 25.895  -42.847 13.323 1.00 70.15  ?  28  ALA   A HB2    1 
ATOM   9     H  HB3    . ALA   A 1 3   ? 26.485  -42.976 11.853 1.00 70.15  ?  28  ALA   A HB3    1 
ATOM   10    N  N      . SER   A 1 4   ? 24.525  -40.439 9.891  1.00 51.31  ?  29  SER   A N      1 
ATOM   11    C  CA     . SER   A 1 4   ? 24.838  -39.616 8.739  1.00 48.50  ?  29  SER   A CA     1 
ATOM   12    C  C      . SER   A 1 4   ? 24.944  -38.152 9.147  1.00 46.95  ?  29  SER   A C      1 
ATOM   13    O  O      . SER   A 1 4   ? 24.507  -37.742 10.224 1.00 47.06  ?  29  SER   A O      1 
ATOM   14    C  CB     . SER   A 1 4   ? 23.770  -39.765 7.661  1.00 49.27  ?  29  SER   A CB     1 
ATOM   15    O  OG     . SER   A 1 4   ? 22.545  -39.210 8.104  1.00 50.03  ?  29  SER   A OG     1 
ATOM   16    H  H      . SER   A 1 4   ? 23.714  -40.726 9.920  1.00 61.56  ?  29  SER   A H      1 
ATOM   17    H  HA     . SER   A 1 4   ? 25.687  -39.901 8.367  1.00 58.19  ?  29  SER   A HA     1 
ATOM   18    H  HB2    . SER   A 1 4   ? 24.059  -39.300 6.861  1.00 59.12  ?  29  SER   A HB2    1 
ATOM   19    H  HB3    . SER   A 1 4   ? 23.641  -40.707 7.469  1.00 59.12  ?  29  SER   A HB3    1 
ATOM   20    H  HG     . SER   A 1 4   ? 21.965  -39.275 7.500  1.00 60.03  ?  29  SER   A HG     1 
ATOM   21    N  N      . VAL   A 1 5   ? 25.533  -37.366 8.251  1.00 45.53  ?  30  VAL   A N      1 
ATOM   22    C  CA     . VAL   A 1 5   ? 25.637  -35.926 8.454  1.00 45.82  ?  30  VAL   A CA     1 
ATOM   23    C  C      . VAL   A 1 5   ? 24.257  -35.288 8.499  1.00 44.50  ?  30  VAL   A C      1 
ATOM   24    O  O      . VAL   A 1 5   ? 24.020  -34.334 9.253  1.00 42.32  ?  30  VAL   A O      1 
ATOM   25    C  CB     . VAL   A 1 5   ? 26.510  -35.325 7.337  1.00 48.18  ?  30  VAL   A CB     1 
ATOM   26    C  CG1    . VAL   A 1 5   ? 26.162  -33.876 7.107  1.00 47.61  ?  30  VAL   A CG1    1 
ATOM   27    C  CG2    . VAL   A 1 5   ? 27.985  -35.500 7.678  1.00 49.56  ?  30  VAL   A CG2    1 
ATOM   28    H  H      . VAL   A 1 5   ? 25.882  -37.641 7.514  1.00 54.63  ?  30  VAL   A H      1 
ATOM   29    H  HA     . VAL   A 1 5   ? 26.060  -35.751 9.309  1.00 54.98  ?  30  VAL   A HA     1 
ATOM   30    H  HB     . VAL   A 1 5   ? 26.337  -35.796 6.507  1.00 57.81  ?  30  VAL   A HB     1 
ATOM   31    H  HG11   . VAL   A 1 5   ? 26.871  -33.458 6.594  1.00 57.12  ?  30  VAL   A HG11   1 
ATOM   32    H  HG12   . VAL   A 1 5   ? 25.326  -33.825 6.617  1.00 57.12  ?  30  VAL   A HG12   1 
ATOM   33    H  HG13   . VAL   A 1 5   ? 26.069  -33.433 7.965  1.00 57.12  ?  30  VAL   A HG13   1 
ATOM   34    H  HG21   . VAL   A 1 5   ? 28.521  -35.131 6.958  1.00 59.47  ?  30  VAL   A HG21   1 
ATOM   35    H  HG22   . VAL   A 1 5   ? 28.176  -35.033 8.506  1.00 59.47  ?  30  VAL   A HG22   1 
ATOM   36    H  HG23   . VAL   A 1 5   ? 28.176  -36.446 7.780  1.00 59.47  ?  30  VAL   A HG23   1 
ATOM   37    N  N      . GLU   A 1 6   ? 23.329  -35.794 7.682  1.00 44.46  ?  31  GLU   A N      1 
ATOM   38    C  CA     . GLU   A 1 6   ? 21.987  -35.228 7.616  1.00 44.80  ?  31  GLU   A CA     1 
ATOM   39    C  C      . GLU   A 1 6   ? 21.179  -35.573 8.857  1.00 44.27  ?  31  GLU   A C      1 
ATOM   40    O  O      . GLU   A 1 6   ? 20.280  -34.816 9.243  1.00 45.43  ?  31  GLU   A O      1 
ATOM   41    C  CB     . GLU   A 1 6   ? 21.280  -35.730 6.356  1.00 46.47  ?  31  GLU   A CB     1 
ATOM   42    C  CG     . GLU   A 1 6   ? 21.895  -35.245 5.045  1.00 48.25  ?  31  GLU   A CG     1 
ATOM   43    C  CD     . GLU   A 1 6   ? 23.257  -35.858 4.749  1.00 48.73  ?  31  GLU   A CD     1 
ATOM   44    O  OE1    . GLU   A 1 6   ? 23.459  -37.060 5.031  1.00 49.23  ?  31  GLU   A OE1    1 
ATOM   45    O  OE2    . GLU   A 1 6   ? 24.130  -35.128 4.239  1.00 48.44  ?  31  GLU   A OE2    1 
ATOM   46    H  H      . GLU   A 1 6   ? 23.454  -36.464 7.158  1.00 53.34  ?  31  GLU   A H      1 
ATOM   47    H  HA     . GLU   A 1 6   ? 22.049  -34.262 7.561  1.00 53.75  ?  31  GLU   A HA     1 
ATOM   48    H  HB2    . GLU   A 1 6   ? 21.309  -36.699 6.352  1.00 55.75  ?  31  GLU   A HB2    1 
ATOM   49    H  HB3    . GLU   A 1 6   ? 20.359  -35.425 6.377  1.00 55.75  ?  31  GLU   A HB3    1 
ATOM   50    H  HG2    . GLU   A 1 6   ? 21.300  -35.478 4.315  1.00 57.90  ?  31  GLU   A HG2    1 
ATOM   51    H  HG3    . GLU   A 1 6   ? 22.007  -34.283 5.089  1.00 57.90  ?  31  GLU   A HG3    1 
ATOM   52    N  N      . ARG   A 1 7   ? 21.487  -36.698 9.501  1.00 42.51  ?  32  ARG   A N      1 
ATOM   53    C  CA     . ARG   A 1 7   ? 20.844  -37.012 10.769 1.00 42.89  ?  32  ARG   A CA     1 
ATOM   54    C  C      . ARG   A 1 7   ? 21.422  -36.169 11.899 1.00 40.24  ?  32  ARG   A C      1 
ATOM   55    O  O      . ARG   A 1 7   ? 20.673  -35.668 12.746 1.00 39.75  ?  32  ARG   A O      1 
ATOM   56    C  CB     . ARG   A 1 7   ? 21.001  -38.499 11.082 1.00 45.47  ?  32  ARG   A CB     1 
ATOM   57    C  CG     . ARG   A 1 7   ? 20.288  -38.926 12.348 1.00 49.53  ?  32  ARG   A CG     1 
ATOM   58    C  CD     . ARG   A 1 7   ? 20.688  -40.329 12.788 1.00 53.86  ?  32  ARG   A CD     1 
ATOM   59    N  NE     . ARG   A 1 7   ? 22.045  -40.391 13.333 1.00 57.64  ?  32  ARG   A NE     1 
ATOM   60    C  CZ     . ARG   A 1 7   ? 22.412  -39.879 14.507 1.00 60.47  ?  32  ARG   A CZ     1 
ATOM   61    N  NH1    . ARG   A 1 7   ? 21.533  -39.240 15.268 1.00 61.46  ?  32  ARG   A NH1    1 
ATOM   62    N  NH2    . ARG   A 1 7   ? 23.670  -39.997 14.915 1.00 60.94  ?  32  ARG   A NH2    1 
ATOM   63    H  H      . ARG   A 1 7   ? 22.055  -37.283 9.229  1.00 51.01  ?  32  ARG   A H      1 
ATOM   64    H  HA     . ARG   A 1 7   ? 19.896  -36.822 10.699 1.00 51.46  ?  32  ARG   A HA     1 
ATOM   65    H  HB2    . ARG   A 1 7   ? 20.634  -39.014 10.346 1.00 54.56  ?  32  ARG   A HB2    1 
ATOM   66    H  HB3    . ARG   A 1 7   ? 21.944  -38.699 11.190 1.00 54.56  ?  32  ARG   A HB3    1 
ATOM   67    H  HG2    . ARG   A 1 7   ? 20.512  -38.310 13.063 1.00 59.43  ?  32  ARG   A HG2    1 
ATOM   68    H  HG3    . ARG   A 1 7   ? 19.331  -38.919 12.193 1.00 59.43  ?  32  ARG   A HG3    1 
ATOM   69    H  HD2    . ARG   A 1 7   ? 20.075  -40.630 13.477 1.00 64.63  ?  32  ARG   A HD2    1 
ATOM   70    H  HD3    . ARG   A 1 7   ? 20.645  -40.923 12.023 1.00 64.63  ?  32  ARG   A HD3    1 
ATOM   71    H  HE     . ARG   A 1 7   ? 22.647  -40.785 12.863 1.00 69.16  ?  32  ARG   A HE     1 
ATOM   72    H  HH11   . ARG   A 1 7   ? 20.719  -39.153 15.005 1.00 73.75  ?  32  ARG   A HH11   1 
ATOM   73    H  HH12   . ARG   A 1 7   ? 21.777  -38.912 16.025 1.00 73.75  ?  32  ARG   A HH12   1 
ATOM   74    H  HH21   . ARG   A 1 7   ? 24.246  -40.404 14.422 1.00 73.12  ?  32  ARG   A HH21   1 
ATOM   75    H  HH22   . ARG   A 1 7   ? 23.909  -39.668 15.673 1.00 73.12  ?  32  ARG   A HH22   1 
ATOM   76    N  N      . ILE   A 1 8   ? 22.748  -35.997 11.916 1.00 37.58  ?  33  ILE   A N      1 
ATOM   77    C  CA     . ILE   A 1 8   ? 23.391  -35.296 13.022 1.00 35.79  ?  33  ILE   A CA     1 
ATOM   78    C  C      . ILE   A 1 8   ? 23.056  -33.809 12.991 1.00 33.66  ?  33  ILE   A C      1 
ATOM   79    O  O      . ILE   A 1 8   ? 22.606  -33.241 13.990 1.00 33.39  ?  33  ILE   A O      1 
ATOM   80    C  CB     . ILE   A 1 8   ? 24.916  -35.518 13.001 1.00 36.48  ?  33  ILE   A CB     1 
ATOM   81    C  CG1    . ILE   A 1 8   ? 25.250  -36.987 13.270 1.00 40.26  ?  33  ILE   A CG1    1 
ATOM   82    C  CG2    . ILE   A 1 8   ? 25.598  -34.592 14.028 1.00 35.97  ?  33  ILE   A CG2    1 
ATOM   83    C  CD1    . ILE   A 1 8   ? 26.715  -37.322 13.074 1.00 42.34  ?  33  ILE   A CD1    1 
ATOM   84    H  H      . ILE   A 1 8   ? 23.288  -36.273 11.306 1.00 45.09  ?  33  ILE   A H      1 
ATOM   85    H  HA     . ILE   A 1 8   ? 23.042  -35.668 13.848 1.00 42.94  ?  33  ILE   A HA     1 
ATOM   86    H  HB     . ILE   A 1 8   ? 25.253  -35.296 12.118 1.00 43.76  ?  33  ILE   A HB     1 
ATOM   87    H  HG12   . ILE   A 1 8   ? 25.018  -37.197 14.188 1.00 48.31  ?  33  ILE   A HG12   1 
ATOM   88    H  HG13   . ILE   A 1 8   ? 24.736  -37.541 12.662 1.00 48.31  ?  33  ILE   A HG13   1 
ATOM   89    H  HG21   . ILE   A 1 8   ? 26.512  -34.887 14.162 1.00 43.15  ?  33  ILE   A HG21   1 
ATOM   90    H  HG22   . ILE   A 1 8   ? 25.589  -33.684 13.689 1.00 43.15  ?  33  ILE   A HG22   1 
ATOM   91    H  HG23   . ILE   A 1 8   ? 25.110  -34.637 14.866 1.00 43.15  ?  33  ILE   A HG23   1 
ATOM   92    H  HD11   . ILE   A 1 8   ? 26.815  -38.285 13.023 1.00 50.80  ?  33  ILE   A HD11   1 
ATOM   93    H  HD12   . ILE   A 1 8   ? 27.025  -36.913 12.251 1.00 50.80  ?  33  ILE   A HD12   1 
ATOM   94    H  HD13   . ILE   A 1 8   ? 27.221  -36.976 13.826 1.00 50.80  ?  33  ILE   A HD13   1 
ATOM   95    N  N      . TYR   A 1 9   ? 23.298  -33.148 11.864 1.00 32.15  ?  34  TYR   A N      1 
ATOM   96    C  CA     . TYR   A 1 9   ? 23.132  -31.701 11.765 1.00 32.01  ?  34  TYR   A CA     1 
ATOM   97    C  C      . TYR   A 1 9   ? 21.804  -31.378 11.086 1.00 31.28  ?  34  TYR   A C      1 
ATOM   98    O  O      . TYR   A 1 9   ? 21.585  -31.753 9.929  1.00 33.58  ?  34  TYR   A O      1 
ATOM   99    C  CB     . TYR   A 1 9   ? 24.300  -31.071 11.000 1.00 31.73  ?  34  TYR   A CB     1 
ATOM   100   C  CG     . TYR   A 1 9   ? 25.658  -31.361 11.618 1.00 33.21  ?  34  TYR   A CG     1 
ATOM   101   C  CD1    . TYR   A 1 9   ? 26.140  -30.604 12.682 1.00 32.32  ?  34  TYR   A CD1    1 
ATOM   102   C  CD2    . TYR   A 1 9   ? 26.452  -32.403 11.146 1.00 34.83  ?  34  TYR   A CD2    1 
ATOM   103   C  CE1    . TYR   A 1 9   ? 27.375  -30.874 13.255 1.00 32.54  ?  34  TYR   A CE1    1 
ATOM   104   C  CE2    . TYR   A 1 9   ? 27.689  -32.678 11.712 1.00 35.12  ?  34  TYR   A CE2    1 
ATOM   105   C  CZ     . TYR   A 1 9   ? 28.144  -31.908 12.767 1.00 35.45  ?  34  TYR   A CZ     1 
ATOM   106   O  OH     . TYR   A 1 9   ? 29.370  -32.170 13.342 1.00 36.26  ?  34  TYR   A OH     1 
ATOM   107   H  H      . TYR   A 1 9   ? 23.563  -33.519 11.135 1.00 38.58  ?  34  TYR   A H      1 
ATOM   108   H  HA     . TYR   A 1 9   ? 23.108  -31.324 12.658 1.00 38.40  ?  34  TYR   A HA     1 
ATOM   109   H  HB2    . TYR   A 1 9   ? 24.305  -31.420 10.095 1.00 38.07  ?  34  TYR   A HB2    1 
ATOM   110   H  HB3    . TYR   A 1 9   ? 24.180  -30.109 10.984 1.00 38.07  ?  34  TYR   A HB3    1 
ATOM   111   H  HD1    . TYR   A 1 9   ? 25.625  -29.904 13.014 1.00 38.78  ?  34  TYR   A HD1    1 
ATOM   112   H  HD2    . TYR   A 1 9   ? 26.147  -32.925 10.439 1.00 41.79  ?  34  TYR   A HD2    1 
ATOM   113   H  HE1    . TYR   A 1 9   ? 27.682  -30.359 13.966 1.00 39.04  ?  34  TYR   A HE1    1 
ATOM   114   H  HE2    . TYR   A 1 9   ? 28.209  -33.375 11.384 1.00 42.14  ?  34  TYR   A HE2    1 
ATOM   115   H  HH     . TYR   A 1 9   ? 29.737  -32.818 12.953 1.00 43.51  ?  34  TYR   A HH     1 
ATOM   116   N  N      . GLN   A 1 10  ? 20.932  -30.664 11.789 1.00 29.85  ?  35  GLN   A N      1 
ATOM   117   C  CA     . GLN   A 1 10  ? 19.607  -30.370 11.272 1.00 29.87  ?  35  GLN   A CA     1 
ATOM   118   C  C      . GLN   A 1 10  ? 19.299  -28.881 11.339 1.00 29.02  ?  35  GLN   A C      1 
ATOM   119   O  O      . GLN   A 1 10  ? 19.785  -28.157 12.217 1.00 28.51  ?  35  GLN   A O      1 
ATOM   120   C  CB     . GLN   A 1 10  ? 18.519  -31.142 12.042 1.00 31.60  ?  35  GLN   A CB     1 
ATOM   121   C  CG     . GLN   A 1 10  ? 18.640  -32.647 11.935 1.00 33.61  ?  35  GLN   A CG     1 
ATOM   122   C  CD     . GLN   A 1 10  ? 17.596  -33.386 12.756 1.00 37.38  ?  35  GLN   A CD     1 
ATOM   123   O  OE1    . GLN   A 1 10  ? 16.487  -32.895 12.971 1.00 39.39  ?  35  GLN   A OE1    1 
ATOM   124   N  NE2    . GLN   A 1 10  ? 17.952  -34.573 13.226 1.00 37.70  ?  35  GLN   A NE2    1 
ATOM   125   H  H      . GLN   A 1 10  ? 21.088  -30.340 12.571 1.00 35.82  ?  35  GLN   A H      1 
ATOM   126   H  HA     . GLN   A 1 10  ? 19.588  -30.628 10.337 1.00 35.84  ?  35  GLN   A HA     1 
ATOM   127   H  HB2    . GLN   A 1 10  ? 18.576  -30.908 12.981 1.00 37.92  ?  35  GLN   A HB2    1 
ATOM   128   H  HB3    . GLN   A 1 10  ? 17.651  -30.890 11.690 1.00 37.92  ?  35  GLN   A HB3    1 
ATOM   129   H  HG2    . GLN   A 1 10  ? 18.529  -32.907 11.007 1.00 40.32  ?  35  GLN   A HG2    1 
ATOM   130   H  HG3    . GLN   A 1 10  ? 19.516  -32.916 12.253 1.00 40.32  ?  35  GLN   A HG3    1 
ATOM   131   H  HE21   . GLN   A 1 10  ? 18.736  -34.883 13.059 1.00 45.24  ?  35  GLN   A HE21   1 
ATOM   132   H  HE22   . GLN   A 1 10  ? 17.398  -35.033 13.696 1.00 45.24  ?  35  GLN   A HE22   1 
ATOM   133   N  N      . LYS   A 1 11  ? 18.464  -28.443 10.395 1.00 29.50  ?  36  LYS   A N      1 
ATOM   134   C  CA     . LYS   A 1 11  ? 17.934  -27.087 10.332 1.00 30.67  ?  36  LYS   A CA     1 
ATOM   135   C  C      . LYS   A 1 11  ? 16.425  -27.144 10.555 1.00 31.41  ?  36  LYS   A C      1 
ATOM   136   O  O      . LYS   A 1 11  ? 15.745  -28.042 10.041 1.00 33.34  ?  36  LYS   A O      1 
ATOM   137   C  CB     . LYS   A 1 11  ? 18.252  -26.421 8.993  1.00 32.95  ?  36  LYS   A CB     1 
ATOM   138   C  CG     . LYS   A 1 11  ? 17.718  -24.972 8.862  1.00 35.87  ?  36  LYS   A CG     1 
ATOM   139   C  CD     . LYS   A 1 11  ? 18.277  -24.235 7.655  1.00 39.79  ?  36  LYS   A CD     1 
ATOM   140   C  CE     . LYS   A 1 11  ? 17.690  -22.824 7.572  1.00 42.49  ?  36  LYS   A CE     1 
ATOM   141   N  NZ     . LYS   A 1 11  ? 18.185  -22.032 6.404  1.00 44.06  ?  36  LYS   A NZ     1 
ATOM   142   H  H      . LYS   A 1 11  ? 18.180  -28.938 9.752  1.00 35.39  ?  36  LYS   A H      1 
ATOM   143   H  HA     . LYS   A 1 11  ? 18.334  -26.538 11.025 1.00 36.80  ?  36  LYS   A HA     1 
ATOM   144   H  HB2    . LYS   A 1 11  ? 19.215  -26.391 8.882  1.00 39.54  ?  36  LYS   A HB2    1 
ATOM   145   H  HB3    . LYS   A 1 11  ? 17.853  -26.947 8.282  1.00 39.54  ?  36  LYS   A HB3    1 
ATOM   146   H  HG2    . LYS   A 1 11  ? 16.753  -24.999 8.773  1.00 43.04  ?  36  LYS   A HG2    1 
ATOM   147   H  HG3    . LYS   A 1 11  ? 17.965  -24.473 9.656  1.00 43.04  ?  36  LYS   A HG3    1 
ATOM   148   H  HD2    . LYS   A 1 11  ? 19.241  -24.164 7.735  1.00 47.74  ?  36  LYS   A HD2    1 
ATOM   149   H  HD3    . LYS   A 1 11  ? 18.046  -24.715 6.845  1.00 47.74  ?  36  LYS   A HD3    1 
ATOM   150   H  HE2    . LYS   A 1 11  ? 16.725  -22.892 7.495  1.00 50.99  ?  36  LYS   A HE2    1 
ATOM   151   H  HE3    . LYS   A 1 11  ? 17.926  -22.340 8.379  1.00 50.99  ?  36  LYS   A HE3    1 
ATOM   152   H  HZ1    . LYS   A 1 11  ? 17.809  -21.225 6.403  1.00 52.87  ?  36  LYS   A HZ1    1 
ATOM   153   H  HZ2    . LYS   A 1 11  ? 19.068  -21.939 6.452  1.00 52.87  ?  36  LYS   A HZ2    1 
ATOM   154   H  HZ3    . LYS   A 1 11  ? 17.978  -22.448 5.645  1.00 52.87  ?  36  LYS   A HZ3    1 
ATOM   155   N  N      . LYS   A 1 12  ? 15.906  -26.183 11.319 1.00 29.87  ?  37  LYS   A N      1 
ATOM   156   C  CA     . LYS   A 1 12  ? 14.483  -26.094 11.616 1.00 30.62  ?  37  LYS   A CA     1 
ATOM   157   C  C      . LYS   A 1 12  ? 13.899  -24.793 11.085 1.00 31.45  ?  37  LYS   A C      1 
ATOM   158   O  O      . LYS   A 1 12  ? 14.578  -23.758 11.083 1.00 32.52  ?  37  LYS   A O      1 
ATOM   159   C  CB     . LYS   A 1 12  ? 14.229  -26.174 13.128 1.00 30.58  ?  37  LYS   A CB     1 
ATOM   160   C  CG     . LYS   A 1 12  ? 14.673  -27.465 13.767 1.00 31.02  ?  37  LYS   A CG     1 
ATOM   161   C  CD     . LYS   A 1 12  ? 13.819  -28.625 13.273 1.00 33.21  ?  37  LYS   A CD     1 
ATOM   162   C  CE     . LYS   A 1 12  ? 14.367  -29.959 13.753 1.00 35.48  ?  37  LYS   A CE     1 
ATOM   163   N  NZ     . LYS   A 1 12  ? 13.611  -31.109 13.187 1.00 36.77  ?  37  LYS   A NZ     1 
ATOM   164   H  H      . LYS   A 1 12  ? 16.371  -25.559 11.684 1.00 35.84  ?  37  LYS   A H      1 
ATOM   165   H  HA     . LYS   A 1 12  ? 14.031  -26.830 11.174 1.00 36.73  ?  37  LYS   A HA     1 
ATOM   166   H  HB2    . LYS   A 1 12  ? 14.710  -25.451 13.560 1.00 36.69  ?  37  LYS   A HB2    1 
ATOM   167   H  HB3    . LYS   A 1 12  ? 13.276  -26.080 13.286 1.00 36.69  ?  37  LYS   A HB3    1 
ATOM   168   H  HG2    . LYS   A 1 12  ? 15.598  -27.641 13.536 1.00 37.22  ?  37  LYS   A HG2    1 
ATOM   169   H  HG3    . LYS   A 1 12  ? 14.578  -27.400 14.730 1.00 37.22  ?  37  LYS   A HG3    1 
ATOM   170   H  HD2    . LYS   A 1 12  ? 12.915  -28.527 13.611 1.00 39.85  ?  37  LYS   A HD2    1 
ATOM   171   H  HD3    . LYS   A 1 12  ? 13.812  -28.629 12.303 1.00 39.85  ?  37  LYS   A HD3    1 
ATOM   172   H  HE2    . LYS   A 1 12  ? 15.294  -30.041 13.478 1.00 42.57  ?  37  LYS   A HE2    1 
ATOM   173   H  HE3    . LYS   A 1 12  ? 14.304  -30.001 14.720 1.00 42.57  ?  37  LYS   A HE3    1 
ATOM   174   H  HZ1    . LYS   A 1 12  ? 13.947  -31.875 13.493 1.00 44.12  ?  37  LYS   A HZ1    1 
ATOM   175   H  HZ2    . LYS   A 1 12  ? 12.754  -31.055 13.422 1.00 44.12  ?  37  LYS   A HZ2    1 
ATOM   176   H  HZ3    . LYS   A 1 12  ? 13.668  -31.104 12.299 1.00 44.12  ?  37  LYS   A HZ3    1 
ATOM   177   N  N      . THR   A 1 13  ? 12.644  -24.851 10.639 1.00 31.04  ?  38  THR   A N      1 
ATOM   178   C  CA     . THR   A 1 13  ? 11.891  -23.630 10.406 1.00 31.62  ?  38  THR   A CA     1 
ATOM   179   C  C      . THR   A 1 13  ? 11.546  -22.965 11.740 1.00 30.34  ?  38  THR   A C      1 
ATOM   180   O  O      . THR   A 1 13  ? 11.606  -23.583 12.805 1.00 28.85  ?  38  THR   A O      1 
ATOM   181   C  CB     . THR   A 1 13  ? 10.593  -23.897 9.637  1.00 33.38  ?  38  THR   A CB     1 
ATOM   182   O  OG1    . THR   A 1 13  ? 9.675   -24.630 10.461 1.00 33.87  ?  38  THR   A OG1    1 
ATOM   183   C  CG2    . THR   A 1 13  ? 10.870  -24.661 8.350  1.00 36.63  ?  38  THR   A CG2    1 
ATOM   184   H  H      . THR   A 1 13  ? 12.215  -25.576 10.468 1.00 37.24  ?  38  THR   A H      1 
ATOM   185   H  HA     . THR   A 1 13  ? 12.435  -23.032 9.870  1.00 37.93  ?  38  THR   A HA     1 
ATOM   186   H  HB     . THR   A 1 13  ? 10.187  -23.050 9.394  1.00 40.05  ?  38  THR   A HB     1 
ATOM   187   H  HG1    . THR   A 1 13  ? 8.980   -24.811 10.026 1.00 40.63  ?  38  THR   A HG1    1 
ATOM   188   H  HG21   . THR   A 1 13  ? 10.049  -24.765 7.843  1.00 43.96  ?  38  THR   A HG21   1 
ATOM   189   H  HG22   . THR   A 1 13  ? 11.515  -24.179 7.809  1.00 43.96  ?  38  THR   A HG22   1 
ATOM   190   H  HG23   . THR   A 1 13  ? 11.226  -25.540 8.556  1.00 43.96  ?  38  THR   A HG23   1 
ATOM   191   N  N      . GLN   A 1 14  ? 11.158  -21.694 11.676 1.00 32.14  ?  39  GLN   A N      1 
ATOM   192   C  CA     . GLN   A 1 14  ? 10.785  -20.996 12.901 1.00 32.06  ?  39  GLN   A CA     1 
ATOM   193   C  C      . GLN   A 1 14  ? 9.664   -21.731 13.626 1.00 29.88  ?  39  GLN   A C      1 
ATOM   194   O  O      . GLN   A 1 14  ? 9.708   -21.910 14.849 1.00 28.71  ?  39  GLN   A O      1 
ATOM   195   C  CB     . GLN   A 1 14  ? 10.340  -19.572 12.587 1.00 35.29  ?  39  GLN   A CB     1 
ATOM   196   C  CG     . GLN   A 1 14  ? 11.387  -18.716 11.963 1.00 39.42  ?  39  GLN   A CG     1 
ATOM   197   C  CD     . GLN   A 1 14  ? 10.798  -17.440 11.400 1.00 43.51  ?  39  GLN   A CD     1 
ATOM   198   O  OE1    . GLN   A 1 14  ? 10.768  -16.411 12.065 1.00 46.93  ?  39  GLN   A OE1    1 
ATOM   199   N  NE2    . GLN   A 1 14  ? 10.299  -17.515 10.177 1.00 43.65  ?  39  GLN   A NE2    1 
ATOM   200   H  H      . GLN   A 1 14  ? 11.104  -21.226 10.956 1.00 38.57  ?  39  GLN   A H      1 
ATOM   201   H  HA     . GLN   A 1 14  ? 11.564  -20.956 13.478 1.00 38.47  ?  39  GLN   A HA     1 
ATOM   202   H  HB2    . GLN   A 1 14  ? 9.591   -19.611 11.973 1.00 42.34  ?  39  GLN   A HB2    1 
ATOM   203   H  HB3    . GLN   A 1 14  ? 10.068  -19.144 13.414 1.00 42.34  ?  39  GLN   A HB3    1 
ATOM   204   H  HG2    . GLN   A 1 14  ? 12.048  -18.478 12.632 1.00 47.30  ?  39  GLN   A HG2    1 
ATOM   205   H  HG3    . GLN   A 1 14  ? 11.810  -19.203 11.238 1.00 47.30  ?  39  GLN   A HG3    1 
ATOM   206   H  HE21   . GLN   A 1 14  ? 10.321  -18.260 9.748  1.00 52.37  ?  39  GLN   A HE21   1 
ATOM   207   H  HE22   . GLN   A 1 14  ? 9.952   -16.818 9.810  1.00 52.37  ?  39  GLN   A HE22   1 
ATOM   208   N  N      . LEU   A 1 15  ? 8.627   -22.130 12.881 1.00 28.73  ?  40  LEU   A N      1 
ATOM   209   C  CA     . LEU   A 1 15  ? 7.482   -22.819 13.470 1.00 28.90  ?  40  LEU   A CA     1 
ATOM   210   C  C      . LEU   A 1 15  ? 7.897   -24.167 14.045 1.00 27.89  ?  40  LEU   A C      1 
ATOM   211   O  O      . LEU   A 1 15  ? 7.503   -24.521 15.163 1.00 26.66  ?  40  LEU   A O      1 
ATOM   212   C  CB     . LEU   A 1 15  ? 6.382   -22.977 12.417 1.00 32.74  ?  40  LEU   A CB     1 
ATOM   213   C  CG     . LEU   A 1 15  ? 5.154   -23.814 12.769 1.00 35.74  ?  40  LEU   A CG     1 
ATOM   214   C  CD1    . LEU   A 1 15  ? 4.409   -23.249 13.963 1.00 36.38  ?  40  LEU   A CD1    1 
ATOM   215   C  CD2    . LEU   A 1 15  ? 4.216   -23.916 11.566 1.00 38.66  ?  40  LEU   A CD2    1 
ATOM   216   H  H      . LEU   A 1 15  ? 8.564   -22.013 12.031 1.00 34.47  ?  40  LEU   A H      1 
ATOM   217   H  HA     . LEU   A 1 15  ? 7.121   -22.289 14.198 1.00 34.68  ?  40  LEU   A HA     1 
ATOM   218   H  HB2    . LEU   A 1 15  ? 6.058   -22.090 12.195 1.00 39.29  ?  40  LEU   A HB2    1 
ATOM   219   H  HB3    . LEU   A 1 15  ? 6.782   -23.389 11.635 1.00 39.29  ?  40  LEU   A HB3    1 
ATOM   220   H  HG     . LEU   A 1 15  ? 5.456   -24.703 13.011 1.00 42.88  ?  40  LEU   A HG     1 
ATOM   221   H  HD11   . LEU   A 1 15  ? 3.630   -23.799 14.138 1.00 43.65  ?  40  LEU   A HD11   1 
ATOM   222   H  HD12   . LEU   A 1 15  ? 4.998   -23.255 14.734 1.00 43.65  ?  40  LEU   A HD12   1 
ATOM   223   H  HD13   . LEU   A 1 15  ? 4.135   -22.340 13.763 1.00 43.65  ?  40  LEU   A HD13   1 
ATOM   224   H  HD21   . LEU   A 1 15  ? 3.448   -24.455 11.809 1.00 46.39  ?  40  LEU   A HD21   1 
ATOM   225   H  HD22   . LEU   A 1 15  ? 3.929   -23.025 11.313 1.00 46.39  ?  40  LEU   A HD22   1 
ATOM   226   H  HD23   . LEU   A 1 15  ? 4.692   -24.331 10.830 1.00 46.39  ?  40  LEU   A HD23   1 
ATOM   227   N  N      . GLU   A 1 16  ? 8.712   -24.926 13.310 1.00 27.30  ?  41  GLU   A N      1 
ATOM   228   C  CA     . GLU   A 1 16  ? 9.203   -26.193 13.845 1.00 26.31  ?  41  GLU   A CA     1 
ATOM   229   C  C      . GLU   A 1 16  ? 9.967   -25.982 15.143 1.00 24.48  ?  41  GLU   A C      1 
ATOM   230   O  O      . GLU   A 1 16  ? 9.827   -26.761 16.094 1.00 23.79  ?  41  GLU   A O      1 
ATOM   231   C  CB     . GLU   A 1 16  ? 10.108  -26.884 12.828 1.00 29.21  ?  41  GLU   A CB     1 
ATOM   232   C  CG     . GLU   A 1 16  ? 9.371   -27.519 11.675 1.00 32.94  ?  41  GLU   A CG     1 
ATOM   233   C  CD     . GLU   A 1 16  ? 10.292  -27.972 10.556 1.00 35.98  ?  41  GLU   A CD     1 
ATOM   234   O  OE1    . GLU   A 1 16  ? 11.489  -27.613 10.554 1.00 35.29  ?  41  GLU   A OE1    1 
ATOM   235   O  OE2    . GLU   A 1 16  ? 9.804   -28.696 9.666  1.00 39.98  ?  41  GLU   A OE2    1 
ATOM   236   H  H      . GLU   A 1 16  ? 8.988   -24.734 12.519 1.00 32.75  ?  41  GLU   A H      1 
ATOM   237   H  HA     . GLU   A 1 16  ? 8.440   -26.766 14.018 1.00 31.56  ?  41  GLU   A HA     1 
ATOM   238   H  HB2    . GLU   A 1 16  ? 10.719  -26.226 12.461 1.00 35.04  ?  41  GLU   A HB2    1 
ATOM   239   H  HB3    . GLU   A 1 16  ? 10.605  -27.583 13.280 1.00 35.04  ?  41  GLU   A HB3    1 
ATOM   240   H  HG2    . GLU   A 1 16  ? 8.890   -28.296 11.998 1.00 39.52  ?  41  GLU   A HG2    1 
ATOM   241   H  HG3    . GLU   A 1 16  ? 8.749   -26.873 11.305 1.00 39.52  ?  41  GLU   A HG3    1 
ATOM   242   N  N      . HIS   A 1 17  ? 10.796  -24.941 15.191 1.00 24.82  ?  42  HIS   A N      1 
ATOM   243   C  CA     . HIS   A 1 17  ? 11.622  -24.689 16.365 1.00 22.61  ?  42  HIS   A CA     1 
ATOM   244   C  C      . HIS   A 1 17  ? 10.785  -24.377 17.597 1.00 21.65  ?  42  HIS   A C      1 
ATOM   245   O  O      . HIS   A 1 17  ? 11.125  -24.803 18.705 1.00 20.78  ?  42  HIS   A O      1 
ATOM   246   C  CB     . HIS   A 1 17  ? 12.565  -23.535 16.052 1.00 22.10  ?  42  HIS   A CB     1 
ATOM   247   C  CG     . HIS   A 1 17  ? 13.622  -23.309 17.081 1.00 23.07  ?  42  HIS   A CG     1 
ATOM   248   N  ND1    . HIS   A 1 17  ? 13.508  -22.358 18.072 1.00 22.87  ?  42  HIS   A ND1    1 
ATOM   249   C  CD2    . HIS   A 1 17  ? 14.833  -23.888 17.248 1.00 23.64  ?  42  HIS   A CD2    1 
ATOM   250   C  CE1    . HIS   A 1 17  ? 14.590  -22.389 18.830 1.00 23.75  ?  42  HIS   A CE1    1 
ATOM   251   N  NE2    . HIS   A 1 17  ? 15.421  -23.291 18.336 1.00 23.68  ?  42  HIS   A NE2    1 
ATOM   252   H  H      . HIS   A 1 17  ? 10.897  -24.367 14.559 1.00 29.78  ?  42  HIS   A H      1 
ATOM   253   H  HA     . HIS   A 1 17  ? 12.141  -25.483 16.569 1.00 27.13  ?  42  HIS   A HA     1 
ATOM   254   H  HB2    . HIS   A 1 17  ? 13.009  -23.718 15.209 1.00 26.52  ?  42  HIS   A HB2    1 
ATOM   255   H  HB3    . HIS   A 1 17  ? 12.044  -22.720 15.981 1.00 26.52  ?  42  HIS   A HB3    1 
ATOM   256   H  HD2    . HIS   A 1 17  ? 15.199  -24.564 16.725 1.00 28.37  ?  42  HIS   A HD2    1 
ATOM   257   H  HE1    . HIS   A 1 17  ? 14.742  -21.865 19.583 1.00 28.49  ?  42  HIS   A HE1    1 
ATOM   258   H  HE2    . HIS   A 1 17  ? 16.202  -23.474 18.646 1.00 28.41  ?  42  HIS   A HE2    1 
ATOM   259   N  N      . ILE   A 1 18  ? 9.718   -23.591 17.430 1.00 21.66  ?  43  ILE   A N      1 
ATOM   260   C  CA     . ILE   A 1 18  ? 8.829   -23.264 18.545 1.00 21.13  ?  43  ILE   A CA     1 
ATOM   261   C  C      . ILE   A 1 18  ? 8.219   -24.524 19.144 1.00 20.70  ?  43  ILE   A C      1 
ATOM   262   O  O      . ILE   A 1 18  ? 8.143   -24.673 20.368 1.00 20.53  ?  43  ILE   A O      1 
ATOM   263   C  CB     . ILE   A 1 18  ? 7.736   -22.284 18.073 1.00 22.13  ?  43  ILE   A CB     1 
ATOM   264   C  CG1    . ILE   A 1 18  ? 8.354   -20.908 17.807 1.00 22.45  ?  43  ILE   A CG1    1 
ATOM   265   C  CG2    . ILE   A 1 18  ? 6.610   -22.186 19.092 1.00 23.26  ?  43  ILE   A CG2    1 
ATOM   266   C  CD1    . ILE   A 1 18  ? 7.494   -19.994 16.957 1.00 23.21  ?  43  ILE   A CD1    1 
ATOM   267   H  H      . ILE   A 1 18  ? 9.486   -23.236 16.682 1.00 25.98  ?  43  ILE   A H      1 
ATOM   268   H  HA     . ILE   A 1 18  ? 9.354   -22.834 19.239 1.00 25.35  ?  43  ILE   A HA     1 
ATOM   269   H  HB     . ILE   A 1 18  ? 7.357   -22.621 17.246 1.00 26.55  ?  43  ILE   A HB     1 
ATOM   270   H  HG12   . ILE   A 1 18  ? 8.502   -20.465 18.657 1.00 26.93  ?  43  ILE   A HG12   1 
ATOM   271   H  HG13   . ILE   A 1 18  ? 9.198   -21.031 17.346 1.00 26.93  ?  43  ILE   A HG13   1 
ATOM   272   H  HG21   . ILE   A 1 18  ? 6.097   -21.382 18.919 1.00 27.90  ?  43  ILE   A HG21   1 
ATOM   273   H  HG22   . ILE   A 1 18  ? 6.040   -22.967 19.007 1.00 27.90  ?  43  ILE   A HG22   1 
ATOM   274   H  HG23   . ILE   A 1 18  ? 6.992   -22.150 19.982 1.00 27.90  ?  43  ILE   A HG23   1 
ATOM   275   H  HD11   . ILE   A 1 18  ? 7.989   -19.182 16.766 1.00 27.85  ?  43  ILE   A HD11   1 
ATOM   276   H  HD12   . ILE   A 1 18  ? 7.274   -20.449 16.129 1.00 27.85  ?  43  ILE   A HD12   1 
ATOM   277   H  HD13   . ILE   A 1 18  ? 6.683   -19.781 17.443 1.00 27.85  ?  43  ILE   A HD13   1 
ATOM   278   N  N      . LEU   A 1 19  ? 7.766   -25.447 18.297 1.00 21.65  ?  44  LEU   A N      1 
ATOM   279   C  CA     . LEU   A 1 19  ? 7.157   -26.668 18.820 1.00 21.13  ?  44  LEU   A CA     1 
ATOM   280   C  C      . LEU   A 1 19  ? 8.202   -27.612 19.412 1.00 20.83  ?  44  LEU   A C      1 
ATOM   281   O  O      . LEU   A 1 19  ? 7.914   -28.324 20.386 1.00 22.60  ?  44  LEU   A O      1 
ATOM   282   C  CB     . LEU   A 1 19  ? 6.352   -27.358 17.720 1.00 24.43  ?  44  LEU   A CB     1 
ATOM   283   C  CG     . LEU   A 1 19  ? 5.073   -26.610 17.330 1.00 26.30  ?  44  LEU   A CG     1 
ATOM   284   C  CD1    . LEU   A 1 19  ? 4.525   -27.139 16.028 1.00 31.63  ?  44  LEU   A CD1    1 
ATOM   285   C  CD2    . LEU   A 1 19  ? 4.038   -26.709 18.427 1.00 27.06  ?  44  LEU   A CD2    1 
ATOM   286   H  H      . LEU   A 1 19  ? 7.798   -25.393 17.439 1.00 25.97  ?  44  LEU   A H      1 
ATOM   287   H  HA     . LEU   A 1 19  ? 6.542   -26.436 19.534 1.00 25.36  ?  44  LEU   A HA     1 
ATOM   288   H  HB2    . LEU   A 1 19  ? 6.907   -27.430 16.928 1.00 29.31  ?  44  LEU   A HB2    1 
ATOM   289   H  HB3    . LEU   A 1 19  ? 6.098   -28.241 18.028 1.00 29.31  ?  44  LEU   A HB3    1 
ATOM   290   H  HG     . LEU   A 1 19  ? 5.283   -25.671 17.207 1.00 31.55  ?  44  LEU   A HG     1 
ATOM   291   H  HD11   . LEU   A 1 19  ? 3.723   -26.644 15.798 1.00 37.95  ?  44  LEU   A HD11   1 
ATOM   292   H  HD12   . LEU   A 1 19  ? 5.194   -27.025 15.334 1.00 37.95  ?  44  LEU   A HD12   1 
ATOM   293   H  HD13   . LEU   A 1 19  ? 4.314   -28.080 16.133 1.00 37.95  ?  44  LEU   A HD13   1 
ATOM   294   H  HD21   . LEU   A 1 19  ? 3.204   -26.329 18.110 1.00 32.46  ?  44  LEU   A HD21   1 
ATOM   295   H  HD22   . LEU   A 1 19  ? 3.910   -27.643 18.657 1.00 32.46  ?  44  LEU   A HD22   1 
ATOM   296   H  HD23   . LEU   A 1 19  ? 4.352   -26.217 19.202 1.00 32.46  ?  44  LEU   A HD23   1 
ATOM   297   N  N      . LEU   A 1 20  ? 9.421   -27.607 18.864 1.00 20.14  ?  45  LEU   A N      1 
ATOM   298   C  CA     . LEU   A 1 20  ? 10.479  -28.489 19.344 1.00 21.33  ?  45  LEU   A CA     1 
ATOM   299   C  C      . LEU   A 1 20  ? 11.118  -27.983 20.630 1.00 20.51  ?  45  LEU   A C      1 
ATOM   300   O  O      . LEU   A 1 20  ? 11.516  -28.780 21.492 1.00 22.67  ?  45  LEU   A O      1 
ATOM   301   C  CB     . LEU   A 1 20  ? 11.556  -28.628 18.277 1.00 23.03  ?  45  LEU   A CB     1 
ATOM   302   C  CG     . LEU   A 1 20  ? 12.674  -29.636 18.527 1.00 26.30  ?  45  LEU   A CG     1 
ATOM   303   C  CD1    . LEU   A 1 20  ? 12.121  -31.048 18.404 1.00 28.18  ?  45  LEU   A CD1    1 
ATOM   304   C  CD2    . LEU   A 1 20  ? 13.814  -29.392 17.556 1.00 28.16  ?  45  LEU   A CD2    1 
ATOM   305   H  H      . LEU   A 1 20  ? 9.659   -27.100 18.212 1.00 24.16  ?  45  LEU   A H      1 
ATOM   306   H  HA     . LEU   A 1 20  ? 10.085  -29.357 19.522 1.00 25.59  ?  45  LEU   A HA     1 
ATOM   307   H  HB2    . LEU   A 1 20  ? 11.122  -28.891 17.450 1.00 27.63  ?  45  LEU   A HB2    1 
ATOM   308   H  HB3    . LEU   A 1 20  ? 11.979  -27.762 18.168 1.00 27.63  ?  45  LEU   A HB3    1 
ATOM   309   H  HG     . LEU   A 1 20  ? 13.030  -29.535 19.424 1.00 31.55  ?  45  LEU   A HG     1 
ATOM   310   H  HD11   . LEU   A 1 20  ? 12.847  -31.682 18.514 1.00 33.81  ?  45  LEU   A HD11   1 
ATOM   311   H  HD12   . LEU   A 1 20  ? 11.453  -31.187 19.093 1.00 33.81  ?  45  LEU   A HD12   1 
ATOM   312   H  HD13   . LEU   A 1 20  ? 11.719  -31.154 17.528 1.00 33.81  ?  45  LEU   A HD13   1 
ATOM   313   H  HD21   . LEU   A 1 20  ? 14.428  -30.142 17.595 1.00 33.79  ?  45  LEU   A HD21   1 
ATOM   314   H  HD22   . LEU   A 1 20  ? 13.452  -29.307 16.660 1.00 33.79  ?  45  LEU   A HD22   1 
ATOM   315   H  HD23   . LEU   A 1 20  ? 14.273  -28.575 17.806 1.00 33.79  ?  45  LEU   A HD23   1 
ATOM   316   N  N      . ARG   A 1 21  ? 11.237  -26.659 20.752 1.00 19.33  ?  46  ARG   A N      1 
ATOM   317   C  CA     . ARG   A 1 21  ? 11.922  -25.990 21.856 1.00 20.14  ?  46  ARG   A CA     1 
ATOM   318   C  C      . ARG   A 1 21  ? 10.999  -24.926 22.433 1.00 19.21  ?  46  ARG   A C      1 
ATOM   319   O  O      . ARG   A 1 21  ? 11.260  -23.729 22.290 1.00 21.43  ?  46  ARG   A O      1 
ATOM   320   C  CB     . ARG   A 1 21  ? 13.229  -25.354 21.373 1.00 20.38  ?  46  ARG   A CB     1 
ATOM   321   C  CG     . ARG   A 1 21  ? 14.260  -26.335 20.836 1.00 21.80  ?  46  ARG   A CG     1 
ATOM   322   C  CD     . ARG   A 1 21  ? 15.039  -26.932 21.998 1.00 23.00  ?  46  ARG   A CD     1 
ATOM   323   N  NE     . ARG   A 1 21  ? 15.987  -27.969 21.613 1.00 24.01  ?  46  ARG   A NE     1 
ATOM   324   C  CZ     . ARG   A 1 21  ? 15.696  -29.264 21.586 1.00 22.95  ?  46  ARG   A CZ     1 
ATOM   325   N  NH1    . ARG   A 1 21  ? 14.482  -29.670 21.902 1.00 24.47  ?  46  ARG   A NH1    1 
ATOM   326   N  NH2    . ARG   A 1 21  ? 16.611  -30.156 21.244 1.00 24.45  ?  46  ARG   A NH2    1 
ATOM   327   H  H      . ARG   A 1 21  ? 10.914  -26.104 20.180 1.00 23.18  ?  46  ARG   A H      1 
ATOM   328   H  HA     . ARG   A 1 21  ? 12.123  -26.639 22.549 1.00 24.16  ?  46  ARG   A HA     1 
ATOM   329   H  HB2    . ARG   A 1 21  ? 13.021  -24.730 20.660 1.00 24.45  ?  46  ARG   A HB2    1 
ATOM   330   H  HB3    . ARG   A 1 21  ? 13.635  -24.883 22.118 1.00 24.45  ?  46  ARG   A HB3    1 
ATOM   331   H  HG2    . ARG   A 1 21  ? 13.815  -27.051 20.356 1.00 26.16  ?  46  ARG   A HG2    1 
ATOM   332   H  HG3    . ARG   A 1 21  ? 14.878  -25.875 20.247 1.00 26.16  ?  46  ARG   A HG3    1 
ATOM   333   H  HD2    . ARG   A 1 21  ? 15.539  -26.224 22.433 1.00 27.60  ?  46  ARG   A HD2    1 
ATOM   334   H  HD3    . ARG   A 1 21  ? 14.411  -27.327 22.623 1.00 27.60  ?  46  ARG   A HD3    1 
ATOM   335   H  HE     . ARG   A 1 21  ? 16.782  -27.728 21.391 1.00 28.81  ?  46  ARG   A HE     1 
ATOM   336   H  HH11   . ARG   A 1 21  ? 13.882  -29.097 22.125 1.00 29.36  ?  46  ARG   A HH11   1 
ATOM   337   H  HH12   . ARG   A 1 21  ? 14.291  -30.509 21.885 1.00 29.36  ?  46  ARG   A HH12   1 
ATOM   338   H  HH21   . ARG   A 1 21  ? 17.405  -29.899 21.037 1.00 29.34  ?  46  ARG   A HH21   1 
ATOM   339   H  HH22   . ARG   A 1 21  ? 16.412  -30.992 21.230 1.00 29.34  ?  46  ARG   A HH22   1 
ATOM   340   N  N      . PRO   A 1 22  ? 9.897   -25.326 23.082 1.00 18.30  ?  47  PRO   A N      1 
ATOM   341   C  CA     . PRO   A 1 22  ? 8.915   -24.325 23.531 1.00 17.93  ?  47  PRO   A CA     1 
ATOM   342   C  C      . PRO   A 1 22  ? 9.400   -23.461 24.672 1.00 17.57  ?  47  PRO   A C      1 
ATOM   343   O  O      . PRO   A 1 22  ? 8.883   -22.353 24.842 1.00 16.97  ?  47  PRO   A O      1 
ATOM   344   C  CB     . PRO   A 1 22  ? 7.705   -25.173 23.963 1.00 19.46  ?  47  PRO   A CB     1 
ATOM   345   C  CG     . PRO   A 1 22  ? 8.240   -26.558 24.160 1.00 22.94  ?  47  PRO   A CG     1 
ATOM   346   C  CD     . PRO   A 1 22  ? 9.406   -26.707 23.246 1.00 19.67  ?  47  PRO   A CD     1 
ATOM   347   H  HA     . PRO   A 1 22  ? 8.664   -23.761 22.783 1.00 21.51  ?  47  PRO   A HA     1 
ATOM   348   H  HB2    . PRO   A 1 22  ? 7.337   -24.823 24.790 1.00 23.35  ?  47  PRO   A HB2    1 
ATOM   349   H  HB3    . PRO   A 1 22  ? 7.029   -25.159 23.267 1.00 23.35  ?  47  PRO   A HB3    1 
ATOM   350   H  HG2    . PRO   A 1 22  ? 8.515   -26.670 25.083 1.00 27.52  ?  47  PRO   A HG2    1 
ATOM   351   H  HG3    . PRO   A 1 22  ? 7.551   -27.205 23.939 1.00 27.52  ?  47  PRO   A HG3    1 
ATOM   352   H  HD2    . PRO   A 1 22  ? 10.088  -27.269 23.648 1.00 23.60  ?  47  PRO   A HD2    1 
ATOM   353   H  HD3    . PRO   A 1 22  ? 9.130   -27.078 22.394 1.00 23.60  ?  47  PRO   A HD3    1 
ATOM   354   N  N      . ASP   A 1 23  ? 10.418  -23.897 25.414 1.00 19.17  ?  48  ASP   A N      1 
ATOM   355   C  CA     . ASP   A 1 23  ? 10.702  -23.314 26.724 1.00 17.50  ?  48  ASP   A CA     1 
ATOM   356   C  C      . ASP   A 1 23  ? 11.051  -21.831 26.679 1.00 17.12  ?  48  ASP   A C      1 
ATOM   357   O  O      . ASP   A 1 23  ? 10.593  -21.077 27.545 1.00 16.96  ?  48  ASP   A O      1 
ATOM   358   C  CB     . ASP   A 1 23  ? 11.826  -24.106 27.391 1.00 18.61  ?  48  ASP   A CB     1 
ATOM   359   C  CG     . ASP   A 1 23  ? 11.412  -25.512 27.678 1.00 21.10  ?  48  ASP   A CG     1 
ATOM   360   O  OD1    . ASP   A 1 23  ? 11.340  -26.313 26.721 1.00 23.49  ?  48  ASP   A OD1    1 
ATOM   361   O  OD2    . ASP   A 1 23  ? 11.103  -25.796 28.854 1.00 20.49  ?  48  ASP   A OD2    1 
ATOM   362   H  H      . ASP   A 1 23  ? 10.956  -24.527 25.184 1.00 23.00  ?  48  ASP   A H      1 
ATOM   363   H  HA     . ASP   A 1 23  ? 9.892   -23.380 27.254 1.00 21.00  ?  48  ASP   A HA     1 
ATOM   364   H  HB2    . ASP   A 1 23  ? 12.596  -24.129 26.802 1.00 22.33  ?  48  ASP   A HB2    1 
ATOM   365   H  HB3    . ASP   A 1 23  ? 12.064  -23.680 28.230 1.00 22.33  ?  48  ASP   A HB3    1 
ATOM   366   N  N      . THR   A 1 24  ? 11.886  -21.386 25.734 1.00 17.63  ?  49  THR   A N      1 
ATOM   367   C  CA     . THR   A 1 24  ? 12.211  -19.959 25.751 1.00 17.66  ?  49  THR   A CA     1 
ATOM   368   C  C      . THR   A 1 24  ? 11.081  -19.100 25.182 1.00 18.37  ?  49  THR   A C      1 
ATOM   369   O  O      . THR   A 1 24  ? 11.140  -17.871 25.294 1.00 20.89  ?  49  THR   A O      1 
ATOM   370   C  CB     . THR   A 1 24  ? 13.501  -19.630 24.983 1.00 20.28  ?  49  THR   A CB     1 
ATOM   371   O  OG1    . THR   A 1 24  ? 13.328  -19.869 23.579 1.00 23.21  ?  49  THR   A OG1    1 
ATOM   372   C  CG2    . THR   A 1 24  ? 14.665  -20.437 25.522 1.00 22.37  ?  49  THR   A CG2    1 
ATOM   373   H  H      . THR   A 1 24  ? 12.252  -21.858 25.116 1.00 21.15  ?  49  THR   A H      1 
ATOM   374   H  HA     . THR   A 1 24  ? 12.374  -19.722 26.678 1.00 21.19  ?  49  THR   A HA     1 
ATOM   375   H  HB     . THR   A 1 24  ? 13.712  -18.690 25.102 1.00 24.32  ?  49  THR   A HB     1 
ATOM   376   H  HG1    . THR   A 1 24  ? 13.127  -20.674 23.447 1.00 27.85  ?  49  THR   A HG1    1 
ATOM   377   H  HG21   . THR   A 1 24  ? 15.477  -20.208 25.044 1.00 26.84  ?  49  THR   A HG21   1 
ATOM   378   H  HG22   . THR   A 1 24  ? 14.790  -20.249 26.465 1.00 26.84  ?  49  THR   A HG22   1 
ATOM   379   H  HG23   . THR   A 1 24  ? 14.491  -21.385 25.411 1.00 26.84  ?  49  THR   A HG23   1 
ATOM   380   N  N      . TYR   A 1 25  ? 10.053  -19.718 24.599 1.00 17.57  ?  50  TYR   A N      1 
ATOM   381   C  CA     . TYR   A 1 25  ? 8.950   -18.955 24.035 1.00 17.43  ?  50  TYR   A CA     1 
ATOM   382   C  C      . TYR   A 1 25  ? 7.783   -18.808 25.009 1.00 16.95  ?  50  TYR   A C      1 
ATOM   383   O  O      . TYR   A 1 25  ? 7.208   -17.720 25.129 1.00 17.17  ?  50  TYR   A O      1 
ATOM   384   C  CB     . TYR   A 1 25  ? 8.452   -19.622 22.754 1.00 17.68  ?  50  TYR   A CB     1 
ATOM   385   C  CG     . TYR   A 1 25  ? 9.452   -19.715 21.631 1.00 18.04  ?  50  TYR   A CG     1 
ATOM   386   C  CD1    . TYR   A 1 25  ? 9.634   -18.657 20.738 1.00 18.79  ?  50  TYR   A CD1    1 
ATOM   387   C  CD2    . TYR   A 1 25  ? 10.196  -20.871 21.442 1.00 18.51  ?  50  TYR   A CD2    1 
ATOM   388   C  CE1    . TYR   A 1 25  ? 10.536  -18.757 19.688 1.00 19.48  ?  50  TYR   A CE1    1 
ATOM   389   C  CE2    . TYR   A 1 25  ? 11.103  -20.973 20.406 1.00 19.29  ?  50  TYR   A CE2    1 
ATOM   390   C  CZ     . TYR   A 1 25  ? 11.269  -19.917 19.527 1.00 21.32  ?  50  TYR   A CZ     1 
ATOM   391   O  OH     . TYR   A 1 25  ? 12.152  -20.028 18.476 1.00 23.72  ?  50  TYR   A OH     1 
ATOM   392   H  H      . TYR   A 1 25  ? 9.976   -20.570 24.520 1.00 21.08  ?  50  TYR   A H      1 
ATOM   393   H  HA     . TYR   A 1 25  ? 9.281   -18.069 23.821 1.00 20.90  ?  50  TYR   A HA     1 
ATOM   394   H  HB2    . TYR   A 1 25  ? 8.176   -20.527 22.969 1.00 21.21  ?  50  TYR   A HB2    1 
ATOM   395   H  HB3    . TYR   A 1 25  ? 7.694   -19.115 22.422 1.00 21.21  ?  50  TYR   A HB3    1 
ATOM   396   H  HD1    . TYR   A 1 25  ? 9.143   -17.875 20.849 1.00 22.54  ?  50  TYR   A HD1    1 
ATOM   397   H  HD2    . TYR   A 1 25  ? 10.081  -21.589 22.022 1.00 22.21  ?  50  TYR   A HD2    1 
ATOM   398   H  HE1    . TYR   A 1 25  ? 10.646  -18.048 19.096 1.00 23.37  ?  50  TYR   A HE1    1 
ATOM   399   H  HE2    . TYR   A 1 25  ? 11.602  -21.750 20.300 1.00 23.14  ?  50  TYR   A HE2    1 
ATOM   400   H  HH     . TYR   A 1 25  ? 12.919  -20.213 18.763 1.00 28.46  ?  50  TYR   A HH     1 
ATOM   401   N  N      . ILE   A 1 26  ? 7.392   -19.899 25.674 1.00 16.18  ?  51  ILE   A N      1 
ATOM   402   C  CA     . ILE   A 1 26  ? 6.211   -19.900 26.530 1.00 15.28  ?  51  ILE   A CA     1 
ATOM   403   C  C      . ILE   A 1 26  ? 6.478   -20.438 27.926 1.00 15.51  ?  51  ILE   A C      1 
ATOM   404   O  O      . ILE   A 1 26  ? 5.562   -20.454 28.751 1.00 16.32  ?  51  ILE   A O      1 
ATOM   405   C  CB     . ILE   A 1 26  ? 5.043   -20.684 25.889 1.00 15.69  ?  51  ILE   A CB     1 
ATOM   406   C  CG1    . ILE   A 1 26  ? 5.386   -22.169 25.695 1.00 16.60  ?  51  ILE   A CG1    1 
ATOM   407   C  CG2    . ILE   A 1 26  ? 4.621   -20.046 24.551 1.00 17.98  ?  51  ILE   A CG2    1 
ATOM   408   C  CD1    . ILE   A 1 26  ? 4.139   -23.021 25.286 1.00 17.20  ?  51  ILE   A CD1    1 
ATOM   409   H  H      . ILE   A 1 26  ? 7.801   -20.655 25.642 1.00 19.41  ?  51  ILE   A H      1 
ATOM   410   H  HA     . ILE   A 1 26  ? 5.931   -18.977 26.635 1.00 18.33  ?  51  ILE   A HA     1 
ATOM   411   H  HB     . ILE   A 1 26  ? 4.297   -20.636 26.507 1.00 18.83  ?  51  ILE   A HB     1 
ATOM   412   H  HG12   . ILE   A 1 26  ? 6.052   -22.252 24.994 1.00 19.92  ?  51  ILE   A HG12   1 
ATOM   413   H  HG13   . ILE   A 1 26  ? 5.735   -22.525 26.527 1.00 19.92  ?  51  ILE   A HG13   1 
ATOM   414   H  HG21   . ILE   A 1 26  ? 3.809   -20.474 24.239 1.00 21.57  ?  51  ILE   A HG21   1 
ATOM   415   H  HG22   . ILE   A 1 26  ? 4.464   -19.099 24.689 1.00 21.57  ?  51  ILE   A HG22   1 
ATOM   416   H  HG23   . ILE   A 1 26  ? 5.332   -20.172 23.903 1.00 21.57  ?  51  ILE   A HG23   1 
ATOM   417   H  HD11   . ILE   A 1 26  ? 4.390   -23.957 25.261 1.00 20.64  ?  51  ILE   A HD11   1 
ATOM   418   H  HD12   . ILE   A 1 26  ? 3.435   -22.884 25.939 1.00 20.64  ?  51  ILE   A HD12   1 
ATOM   419   H  HD13   . ILE   A 1 26  ? 3.836   -22.736 24.409 1.00 20.64  ?  51  ILE   A HD13   1 
ATOM   420   N  N      . GLY   A 1 27  ? 7.702   -20.873 28.228 1.00 16.11  ?  52  GLY   A N      1 
ATOM   421   C  CA     . GLY   A 1 27  ? 7.986   -21.522 29.490 1.00 15.93  ?  52  GLY   A CA     1 
ATOM   422   C  C      . GLY   A 1 27  ? 7.844   -23.024 29.398 1.00 15.93  ?  52  GLY   A C      1 
ATOM   423   O  O      . GLY   A 1 27  ? 7.607   -23.610 28.339 1.00 18.04  ?  52  GLY   A O      1 
ATOM   424   H  H      . GLY   A 1 27  ? 8.384   -20.799 27.711 1.00 19.32  ?  52  GLY   A H      1 
ATOM   425   H  HA2    . GLY   A 1 27  ? 8.894   -21.314 29.761 1.00 19.11  ?  52  GLY   A HA2    1 
ATOM   426   H  HA3    . GLY   A 1 27  ? 7.372   -21.195 30.166 1.00 19.11  ?  52  GLY   A HA3    1 
ATOM   427   N  N      . SER   A 1 28  ? 8.010   -23.672 30.542 1.00 17.07  ?  53  SER   A N      1 
ATOM   428   C  CA     . SER   A 1 28  ? 8.033   -25.125 30.571 1.00 16.47  ?  53  SER   A CA     1 
ATOM   429   C  C      . SER   A 1 28  ? 6.718   -25.728 30.091 1.00 16.68  ?  53  SER   A C      1 
ATOM   430   O  O      . SER   A 1 28  ? 5.630   -25.241 30.411 1.00 17.58  ?  53  SER   A O      1 
ATOM   431   C  CB     . SER   A 1 28  ? 8.311   -25.606 31.990 1.00 19.83  ?  53  SER   A CB     1 
ATOM   432   O  OG     . SER   A 1 28  ? 8.359   -27.012 32.018 1.00 22.36  ?  53  SER   A OG     1 
ATOM   433   H  H      . SER   A 1 28  ? 8.110   -23.297 31.310 1.00 20.48  ?  53  SER   A H      1 
ATOM   434   H  HA     . SER   A 1 28  ? 8.735   -25.431 29.975 1.00 19.75  ?  53  SER   A HA     1 
ATOM   435   H  HB2    . SER   A 1 28  ? 9.164   -25.251 32.286 1.00 23.79  ?  53  SER   A HB2    1 
ATOM   436   H  HB3    . SER   A 1 28  ? 7.602   -25.298 32.576 1.00 23.79  ?  53  SER   A HB3    1 
ATOM   437   H  HG     . SER   A 1 28  ? 8.959   -27.290 31.499 1.00 26.83  ?  53  SER   A HG     1 
ATOM   438   N  N      . VAL   A 1 29  ? 6.819   -26.817 29.335 1.00 18.09  ?  54  VAL   A N      1 
ATOM   439   C  CA     . VAL   A 1 29  ? 5.632   -27.565 28.938 1.00 18.15  ?  54  VAL   A CA     1 
ATOM   440   C  C      . VAL   A 1 29  ? 5.483   -28.834 29.759 1.00 20.06  ?  54  VAL   A C      1 
ATOM   441   O  O      . VAL   A 1 29  ? 4.668   -29.700 29.427 1.00 22.75  ?  54  VAL   A O      1 
ATOM   442   C  CB     . VAL   A 1 29  ? 5.629   -27.866 27.433 1.00 19.28  ?  54  VAL   A CB     1 
ATOM   443   C  CG1    . VAL   A 1 29  ? 5.468   -26.559 26.658 1.00 19.75  ?  54  VAL   A CG1    1 
ATOM   444   C  CG2    . VAL   A 1 29  ? 6.888   -28.609 27.006 1.00 19.61  ?  54  VAL   A CG2    1 
ATOM   445   H  H      . VAL   A 1 29  ? 7.560   -27.140 29.041 1.00 21.70  ?  54  VAL   A H      1 
ATOM   446   H  HA     . VAL   A 1 29  ? 4.854   -27.014 29.114 1.00 21.78  ?  54  VAL   A HA     1 
ATOM   447   H  HB     . VAL   A 1 29  ? 4.882   -28.449 27.226 1.00 23.12  ?  54  VAL   A HB     1 
ATOM   448   H  HG11   . VAL   A 1 29  ? 5.458   -26.754 25.708 1.00 23.69  ?  54  VAL   A HG11   1 
ATOM   449   H  HG12   . VAL   A 1 29  ? 4.635   -26.138 26.918 1.00 23.69  ?  54  VAL   A HG12   1 
ATOM   450   H  HG13   . VAL   A 1 29  ? 6.214   -25.974 26.867 1.00 23.69  ?  54  VAL   A HG13   1 
ATOM   451   H  HG21   . VAL   A 1 29  ? 6.807   -28.858 26.072 1.00 23.52  ?  54  VAL   A HG21   1 
ATOM   452   H  HG22   . VAL   A 1 29  ? 7.655   -28.027 27.128 1.00 23.52  ?  54  VAL   A HG22   1 
ATOM   453   H  HG23   . VAL   A 1 29  ? 6.986   -29.405 27.552 1.00 23.52  ?  54  VAL   A HG23   1 
ATOM   454   N  N      . GLU   A 1 30  ? 6.234   -28.947 30.845 1.00 21.37  ?  55  GLU   A N      1 
ATOM   455   C  CA     . GLU   A 1 30  ? 6.117   -30.037 31.793 1.00 22.89  ?  55  GLU   A CA     1 
ATOM   456   C  C      . GLU   A 1 30  ? 5.436   -29.542 33.060 1.00 22.03  ?  55  GLU   A C      1 
ATOM   457   O  O      . GLU   A 1 30  ? 5.330   -28.339 33.315 1.00 21.99  ?  55  GLU   A O      1 
ATOM   458   C  CB     . GLU   A 1 30  ? 7.495   -30.621 32.119 1.00 27.44  ?  55  GLU   A CB     1 
ATOM   459   C  CG     . GLU   A 1 30  ? 8.255   -31.189 30.914 1.00 33.16  ?  55  GLU   A CG     1 
ATOM   460   C  CD     . GLU   A 1 30  ? 7.549   -32.336 30.189 1.00 38.61  ?  55  GLU   A CD     1 
ATOM   461   O  OE1    . GLU   A 1 30  ? 6.992   -33.233 30.854 1.00 39.50  ?  55  GLU   A OE1    1 
ATOM   462   O  OE2    . GLU   A 1 30  ? 7.572   -32.344 28.938 1.00 42.57  ?  55  GLU   A OE2    1 
ATOM   463   H  H      . GLU   A 1 30  ? 6.844   -28.380 31.060 1.00 25.64  ?  55  GLU   A H      1 
ATOM   464   H  HA     . GLU   A 1 30  ? 5.575   -30.747 31.416 1.00 27.47  ?  55  GLU   A HA     1 
ATOM   465   H  HB2    . GLU   A 1 30  ? 8.043   -29.919 32.504 1.00 32.93  ?  55  GLU   A HB2    1 
ATOM   466   H  HB3    . GLU   A 1 30  ? 7.381   -31.341 32.757 1.00 32.93  ?  55  GLU   A HB3    1 
ATOM   467   H  HG2    . GLU   A 1 30  ? 8.388   -30.476 30.269 1.00 39.79  ?  55  GLU   A HG2    1 
ATOM   468   H  HG3    . GLU   A 1 30  ? 9.113   -31.523 31.220 1.00 39.79  ?  55  GLU   A HG3    1 
ATOM   469   N  N      . LEU   A 1 31  ? 4.940   -30.493 33.843 1.00 24.17  ?  56  LEU   A N      1 
ATOM   470   C  CA     . LEU   A 1 31  ? 4.216   -30.139 35.053 1.00 26.33  ?  56  LEU   A CA     1 
ATOM   471   C  C      . LEU   A 1 31  ? 5.182   -29.566 36.083 1.00 25.65  ?  56  LEU   A C      1 
ATOM   472   O  O      . LEU   A 1 31  ? 6.345   -29.973 36.186 1.00 29.65  ?  56  LEU   A O      1 
ATOM   473   C  CB     . LEU   A 1 31  ? 3.468   -31.352 35.615 1.00 30.24  ?  56  LEU   A CB     1 
ATOM   474   C  CG     . LEU   A 1 31  ? 2.226   -31.783 34.828 1.00 32.81  ?  56  LEU   A CG     1 
ATOM   475   C  CD1    . LEU   A 1 31  ? 1.803   -33.196 35.216 1.00 36.29  ?  56  LEU   A CD1    1 
ATOM   476   C  CD2    . LEU   A 1 31  ? 1.069   -30.840 35.054 1.00 34.81  ?  56  LEU   A CD2    1 
ATOM   477   H  H      . LEU   A 1 31  ? 5.010   -31.338 33.697 1.00 29.00  ?  56  LEU   A H      1 
ATOM   478   H  HA     . LEU   A 1 31  ? 3.548   -29.465 34.853 1.00 31.59  ?  56  LEU   A HA     1 
ATOM   479   H  HB2    . LEU   A 1 31  ? 4.078   -32.107 35.628 1.00 36.28  ?  56  LEU   A HB2    1 
ATOM   480   H  HB3    . LEU   A 1 31  ? 3.180   -31.142 36.517 1.00 36.28  ?  56  LEU   A HB3    1 
ATOM   481   H  HG     . LEU   A 1 31  ? 2.456   -31.765 33.886 1.00 39.36  ?  56  LEU   A HG     1 
ATOM   482   H  HD11   . LEU   A 1 31  ? 1.013   -33.440 34.709 1.00 43.54  ?  56  LEU   A HD11   1 
ATOM   483   H  HD12   . LEU   A 1 31  ? 2.527   -33.809 35.015 1.00 43.54  ?  56  LEU   A HD12   1 
ATOM   484   H  HD13   . LEU   A 1 31  ? 1.606   -33.217 36.166 1.00 43.54  ?  56  LEU   A HD13   1 
ATOM   485   H  HD21   . LEU   A 1 31  ? 0.303   -31.152 34.546 1.00 41.77  ?  56  LEU   A HD21   1 
ATOM   486   H  HD22   . LEU   A 1 31  ? 0.854   -30.823 35.999 1.00 41.77  ?  56  LEU   A HD22   1 
ATOM   487   H  HD23   . LEU   A 1 31  ? 1.323   -29.952 34.757 1.00 41.77  ?  56  LEU   A HD23   1 
ATOM   488   N  N      . VAL   A 1 32  ? 4.698   -28.576 36.808 1.00 20.88  ?  57  VAL   A N      1 
ATOM   489   C  CA     A VAL   A 1 32  ? 5.398   -27.984 37.935 0.49 21.69  ?  57  VAL   A CA     1 
ATOM   490   C  CA     B VAL   A 1 32  ? 5.402   -27.996 37.939 0.51 21.05  ?  57  VAL   A CA     1 
ATOM   491   C  C      . VAL   A 1 32  ? 4.445   -28.036 39.118 1.00 20.56  ?  57  VAL   A C      1 
ATOM   492   O  O      . VAL   A 1 32  ? 3.242   -27.809 38.957 1.00 21.35  ?  57  VAL   A O      1 
ATOM   493   C  CB     A VAL   A 1 32  ? 5.826   -26.536 37.633 0.49 23.36  ?  57  VAL   A CB     1 
ATOM   494   C  CB     B VAL   A 1 32  ? 5.890   -26.562 37.665 0.51 21.66  ?  57  VAL   A CB     1 
ATOM   495   C  CG1    A VAL   A 1 32  ? 6.216   -25.818 38.906 0.49 23.71  ?  57  VAL   A CG1    1 
ATOM   496   C  CG1    B VAL   A 1 32  ? 6.612   -26.485 36.319 0.51 21.58  ?  57  VAL   A CG1    1 
ATOM   497   C  CG2    A VAL   A 1 32  ? 6.975   -26.508 36.621 0.49 24.49  ?  57  VAL   A CG2    1 
ATOM   498   C  CG2    B VAL   A 1 32  ? 4.745   -25.597 37.718 0.51 21.67  ?  57  VAL   A CG2    1 
ATOM   499   H  H      . VAL   A 1 32  ? 3.934   -28.211 36.658 1.00 25.05  ?  57  VAL   A H      1 
ATOM   500   H  HA     . VAL   A 1 32  ? 6.199   -28.489 38.146 1.00 25.26  ?  57  VAL   A HA     1 
ATOM   501   H  HB     A VAL   A 1 32  ? 5.073   -26.066 37.242 0.49 28.03  ?  57  VAL   A HB     1 
ATOM   502   H  HB     B VAL   A 1 32  ? 6.524   -26.310 38.354 0.51 25.99  ?  57  VAL   A HB     1 
ATOM   503   H  HG11   A VAL   A 1 32  ? 6.749   -25.040 38.680 0.49 28.45  ?  57  VAL   A HG11   1 
ATOM   504   H  HG11   B VAL   A 1 32  ? 6.998   -25.601 36.217 0.51 25.90  ?  57  VAL   A HG11   1 
ATOM   505   H  HG12   A VAL   A 1 32  ? 5.412   -25.543 39.373 0.49 28.45  ?  57  VAL   A HG12   1 
ATOM   506   H  HG12   B VAL   A 1 32  ? 7.312   -27.156 36.297 0.51 25.90  ?  57  VAL   A HG12   1 
ATOM   507   H  HG13   A VAL   A 1 32  ? 6.732   -26.422 39.463 0.49 28.45  ?  57  VAL   A HG13   1 
ATOM   508   H  HG13   B VAL   A 1 32  ? 5.973   -26.651 35.608 0.51 25.90  ?  57  VAL   A HG13   1 
ATOM   509   H  HG21   A VAL   A 1 32  ? 7.217   -25.586 36.442 0.49 29.38  ?  57  VAL   A HG21   1 
ATOM   510   H  HG21   B VAL   A 1 32  ? 4.995   -24.784 37.252 0.51 26.00  ?  57  VAL   A HG21   1 
ATOM   511   H  HG22   A VAL   A 1 32  ? 7.735   -26.983 36.993 0.49 29.38  ?  57  VAL   A HG22   1 
ATOM   512   H  HG22   B VAL   A 1 32  ? 3.973   -25.999 37.291 0.51 26.00  ?  57  VAL   A HG22   1 
ATOM   513   H  HG23   A VAL   A 1 32  ? 6.685   -26.938 35.802 0.49 29.38  ?  57  VAL   A HG23   1 
ATOM   514   H  HG23   B VAL   A 1 32  ? 4.543   -25.398 38.646 0.51 26.00  ?  57  VAL   A HG23   1 
ATOM   515   N  N      . THR   A 1 33  ? 4.974   -28.345 40.295 1.00 21.43  ?  58  THR   A N      1 
ATOM   516   C  CA     . THR   A 1 33  ? 4.208   -28.324 41.529 1.00 23.40  ?  58  THR   A CA     1 
ATOM   517   C  C      . THR   A 1 33  ? 4.882   -27.341 42.463 1.00 23.81  ?  58  THR   A C      1 
ATOM   518   O  O      . THR   A 1 33  ? 6.025   -27.563 42.875 1.00 23.79  ?  58  THR   A O      1 
ATOM   519   C  CB     . THR   A 1 33  ? 4.141   -29.711 42.176 1.00 24.44  ?  58  THR   A CB     1 
ATOM   520   O  OG1    . THR   A 1 33  ? 3.485   -30.612 41.275 1.00 24.45  ?  58  THR   A OG1    1 
ATOM   521   C  CG2    . THR   A 1 33  ? 3.401   -29.662 43.505 1.00 26.92  ?  58  THR   A CG2    1 
ATOM   522   H  H      . THR   A 1 33  ? 5.796   -28.575 40.405 1.00 25.71  ?  58  THR   A H      1 
ATOM   523   H  HA     . THR   A 1 33  ? 3.299   -28.038 41.349 1.00 28.07  ?  58  THR   A HA     1 
ATOM   524   H  HB     . THR   A 1 33  ? 5.038   -30.031 42.360 1.00 29.32  ?  58  THR   A HB     1 
ATOM   525   H  HG1    . THR   A 1 33  ? 2.709   -30.338 41.109 1.00 29.33  ?  58  THR   A HG1    1 
ATOM   526   H  HG21   . THR   A 1 33  ? 3.197   -30.562 43.804 1.00 32.30  ?  58  THR   A HG21   1 
ATOM   527   H  HG22   . THR   A 1 33  ? 3.950   -29.224 44.174 1.00 32.30  ?  58  THR   A HG22   1 
ATOM   528   H  HG23   . THR   A 1 33  ? 2.572   -29.168 43.405 1.00 32.30  ?  58  THR   A HG23   1 
ATOM   529   N  N      . GLN   A 1 34  ? 4.186   -26.259 42.786 1.00 22.42  ?  59  GLN   A N      1 
ATOM   530   C  CA     . GLN   A 1 34  ? 4.765   -25.244 43.651 1.00 23.79  ?  59  GLN   A CA     1 
ATOM   531   C  C      . GLN   A 1 34  ? 3.644   -24.433 44.274 1.00 23.74  ?  59  GLN   A C      1 
ATOM   532   O  O      . GLN   A 1 34  ? 2.500   -24.457 43.820 1.00 23.68  ?  59  GLN   A O      1 
ATOM   533   C  CB     . GLN   A 1 34  ? 5.714   -24.326 42.880 1.00 23.82  ?  59  GLN   A CB     1 
ATOM   534   C  CG     . GLN   A 1 34  ? 5.016   -23.529 41.794 1.00 22.93  ?  59  GLN   A CG     1 
ATOM   535   C  CD     . GLN   A 1 34  ? 5.988   -22.854 40.858 1.00 24.02  ?  59  GLN   A CD     1 
ATOM   536   O  OE1    . GLN   A 1 34  ? 7.103   -23.317 40.676 1.00 27.42  ?  59  GLN   A OE1    1 
ATOM   537   N  NE2    . GLN   A 1 34  ? 5.561   -21.764 40.246 1.00 22.35  ?  59  GLN   A NE2    1 
ATOM   538   H  H      . GLN   A 1 34  ? 3.386   -26.093 42.520 1.00 26.90  ?  59  GLN   A H      1 
ATOM   539   H  HA     . GLN   A 1 34  ? 5.259   -25.685 44.359 1.00 28.55  ?  59  GLN   A HA     1 
ATOM   540   H  HB2    . GLN   A 1 34  ? 6.117   -23.698 43.500 1.00 28.58  ?  59  GLN   A HB2    1 
ATOM   541   H  HB3    . GLN   A 1 34  ? 6.402   -24.865 42.461 1.00 28.58  ?  59  GLN   A HB3    1 
ATOM   542   H  HG2    . GLN   A 1 34  ? 4.459   -24.126 41.271 1.00 27.51  ?  59  GLN   A HG2    1 
ATOM   543   H  HG3    . GLN   A 1 34  ? 4.469   -22.842 42.206 1.00 27.51  ?  59  GLN   A HG3    1 
ATOM   544   H  HE21   . GLN   A 1 34  ? 4.765   -21.474 40.391 1.00 26.81  ?  59  GLN   A HE21   1 
ATOM   545   H  HE22   . GLN   A 1 34  ? 6.079   -21.345 39.703 1.00 26.81  ?  59  GLN   A HE22   1 
ATOM   546   N  N      . GLN   A 1 35  ? 3.999   -23.682 45.299 1.00 25.48  ?  60  GLN   A N      1 
ATOM   547   C  CA     . GLN   A 1 35  ? 3.043   -22.789 45.919 1.00 27.08  ?  60  GLN   A CA     1 
ATOM   548   C  C      . GLN   A 1 35  ? 2.858   -21.534 45.081 1.00 24.45  ?  60  GLN   A C      1 
ATOM   549   O  O      . GLN   A 1 35  ? 3.822   -20.935 44.596 1.00 25.56  ?  60  GLN   A O      1 
ATOM   550   C  CB     . GLN   A 1 35  ? 3.504   -22.449 47.326 1.00 31.87  ?  60  GLN   A CB     1 
ATOM   551   C  CG     . GLN   A 1 35  ? 3.599   -23.696 48.166 1.00 37.46  ?  60  GLN   A CG     1 
ATOM   552   C  CD     . GLN   A 1 35  ? 3.371   -23.409 49.603 1.00 44.48  ?  60  GLN   A CD     1 
ATOM   553   O  OE1    . GLN   A 1 35  ? 2.231   -23.298 50.053 1.00 48.37  ?  60  GLN   A OE1    1 
ATOM   554   N  NE2    . GLN   A 1 35  ? 4.455   -23.266 50.349 1.00 46.33  ?  60  GLN   A NE2    1 
ATOM   555   H  H      . GLN   A 1 35  ? 4.783   -23.671 45.653 1.00 30.57  ?  60  GLN   A H      1 
ATOM   556   H  HA     . GLN   A 1 35  ? 2.175   -23.216 45.983 1.00 32.49  ?  60  GLN   A HA     1 
ATOM   557   H  HB2    . GLN   A 1 35  ? 4.380   -22.033 47.289 1.00 38.23  ?  60  GLN   A HB2    1 
ATOM   558   H  HB3    . GLN   A 1 35  ? 2.868   -21.845 47.739 1.00 38.23  ?  60  GLN   A HB3    1 
ATOM   559   H  HG2    . GLN   A 1 35  ? 2.927   -24.331 47.872 1.00 44.94  ?  60  GLN   A HG2    1 
ATOM   560   H  HG3    . GLN   A 1 35  ? 4.484   -24.081 48.068 1.00 44.94  ?  60  GLN   A HG3    1 
ATOM   561   H  HE21   . GLN   A 1 35  ? 5.235   -23.341 49.994 1.00 55.59  ?  60  GLN   A HE21   1 
ATOM   562   H  HE22   . GLN   A 1 35  ? 4.380   -23.099 51.189 1.00 55.59  ?  60  GLN   A HE22   1 
ATOM   563   N  N      . MET   A 1 36  ? 1.589   -21.151 44.915 1.00 23.25  ?  61  MET   A N      1 
ATOM   564   C  CA     . MET   A 1 36  ? 1.162   -20.065 44.046 1.00 23.40  ?  61  MET   A CA     1 
ATOM   565   C  C      . MET   A 1 36  ? -0.006  -19.366 44.725 1.00 21.99  ?  61  MET   A C      1 
ATOM   566   O  O      . MET   A 1 36  ? -0.708  -19.966 45.544 1.00 22.30  ?  61  MET   A O      1 
ATOM   567   C  CB     . MET   A 1 36  ? 0.662   -20.550 42.666 1.00 22.49  ?  61  MET   A CB     1 
ATOM   568   C  CG     . MET   A 1 36  ? 1.612   -21.284 41.744 1.00 21.98  ?  61  MET   A CG     1 
ATOM   569   S  SD     . MET   A 1 36  ? 2.852   -20.186 41.138 1.00 26.31  ?  61  MET   A SD     1 
ATOM   570   C  CE     . MET   A 1 36  ? 1.882   -19.385 39.861 1.00 22.30  ?  61  MET   A CE     1 
ATOM   571   H  H      . MET   A 1 36  ? 0.928   -21.526 45.318 1.00 27.89  ?  61  MET   A H      1 
ATOM   572   H  HA     . MET   A 1 36  ? 1.919   -19.475 43.908 1.00 28.07  ?  61  MET   A HA     1 
ATOM   573   H  HB2    . MET   A 1 36  ? -0.082  -21.152 42.823 1.00 26.98  ?  61  MET   A HB2    1 
ATOM   574   H  HB3    . MET   A 1 36  ? 0.360   -19.769 42.177 1.00 26.98  ?  61  MET   A HB3    1 
ATOM   575   H  HG2    . MET   A 1 36  ? 2.045   -22.003 42.229 1.00 26.37  ?  61  MET   A HG2    1 
ATOM   576   H  HG3    . MET   A 1 36  ? 1.120   -21.642 40.988 1.00 26.37  ?  61  MET   A HG3    1 
ATOM   577   H  HE1    . MET   A 1 36  ? 2.471   -19.116 39.138 1.00 26.75  ?  61  MET   A HE1    1 
ATOM   578   H  HE2    . MET   A 1 36  ? 1.218   -20.010 39.530 1.00 26.75  ?  61  MET   A HE2    1 
ATOM   579   H  HE3    . MET   A 1 36  ? 1.445   -18.606 40.238 1.00 26.75  ?  61  MET   A HE3    1 
ATOM   580   N  N      . TRP   A 1 37  ? -0.254  -18.120 44.343 1.00 19.46  ?  62  TRP   A N      1 
ATOM   581   C  CA     . TRP   A 1 37  ? -1.527  -17.471 44.620 1.00 19.34  ?  62  TRP   A CA     1 
ATOM   582   C  C      . TRP   A 1 37  ? -2.539  -17.828 43.535 1.00 19.20  ?  62  TRP   A C      1 
ATOM   583   O  O      . TRP   A 1 37  ? -2.233  -17.741 42.343 1.00 18.96  ?  62  TRP   A O      1 
ATOM   584   C  CB     . TRP   A 1 37  ? -1.340  -15.960 44.690 1.00 19.13  ?  62  TRP   A CB     1 
ATOM   585   C  CG     . TRP   A 1 37  ? -0.482  -15.512 45.825 1.00 19.98  ?  62  TRP   A CG     1 
ATOM   586   C  CD1    . TRP   A 1 37  ? 0.856   -15.205 45.793 1.00 19.20  ?  62  TRP   A CD1    1 
ATOM   587   C  CD2    . TRP   A 1 37  ? -0.910  -15.309 47.169 1.00 20.93  ?  62  TRP   A CD2    1 
ATOM   588   N  NE1    . TRP   A 1 37  ? 1.275   -14.813 47.044 1.00 21.78  ?  62  TRP   A NE1    1 
ATOM   589   C  CE2    . TRP   A 1 37  ? 0.208   -14.868 47.906 1.00 21.44  ?  62  TRP   A CE2    1 
ATOM   590   C  CE3    . TRP   A 1 37  ? -2.139  -15.445 47.820 1.00 22.89  ?  62  TRP   A CE3    1 
ATOM   591   C  CZ2    . TRP   A 1 37  ? 0.131   -14.567 49.263 1.00 22.61  ?  62  TRP   A CZ2    1 
ATOM   592   C  CZ3    . TRP   A 1 37  ? -2.214  -15.145 49.166 1.00 24.35  ?  62  TRP   A CZ3    1 
ATOM   593   C  CH2    . TRP   A 1 37  ? -1.087  -14.711 49.872 1.00 24.31  ?  62  TRP   A CH2    1 
ATOM   594   H  H      . TRP   A 1 37  ? 0.305   -17.625 43.917 1.00 23.35  ?  62  TRP   A H      1 
ATOM   595   H  HA     . TRP   A 1 37  ? -1.875  -17.780 45.471 1.00 23.20  ?  62  TRP   A HA     1 
ATOM   596   H  HB2    . TRP   A 1 37  ? -0.923  -15.659 43.867 1.00 22.95  ?  62  TRP   A HB2    1 
ATOM   597   H  HB3    . TRP   A 1 37  ? -2.209  -15.542 44.793 1.00 22.95  ?  62  TRP   A HB3    1 
ATOM   598   H  HD1    . TRP   A 1 37  ? 1.398   -15.254 45.039 1.00 23.03  ?  62  TRP   A HD1    1 
ATOM   599   H  HE1    . TRP   A 1 37  ? 2.074   -14.574 47.252 1.00 26.13  ?  62  TRP   A HE1    1 
ATOM   600   H  HE3    . TRP   A 1 37  ? -2.892  -15.732 47.356 1.00 27.46  ?  62  TRP   A HE3    1 
ATOM   601   H  HZ2    . TRP   A 1 37  ? 0.877   -14.279 49.737 1.00 27.13  ?  62  TRP   A HZ2    1 
ATOM   602   H  HZ3    . TRP   A 1 37  ? -3.026  -15.234 49.610 1.00 29.21  ?  62  TRP   A HZ3    1 
ATOM   603   H  HH2    . TRP   A 1 37  ? -1.167  -14.514 50.778 1.00 29.17  ?  62  TRP   A HH2    1 
ATOM   604   N  N      . VAL   A 1 38  ? -3.735  -18.246 43.954 1.00 21.27  ?  63  VAL   A N      1 
ATOM   605   C  CA     . VAL   A 1 38  ? -4.827  -18.588 43.055 1.00 23.03  ?  63  VAL   A CA     1 
ATOM   606   C  C      . VAL   A 1 38  ? -6.106  -17.963 43.600 1.00 24.52  ?  63  VAL   A C      1 
ATOM   607   O  O      . VAL   A 1 38  ? -6.148  -17.467 44.724 1.00 25.80  ?  63  VAL   A O      1 
ATOM   608   C  CB     . VAL   A 1 38  ? -5.007  -20.113 42.896 1.00 24.74  ?  63  VAL   A CB     1 
ATOM   609   C  CG1    . VAL   A 1 38  ? -3.714  -20.778 42.459 1.00 25.29  ?  63  VAL   A CG1    1 
ATOM   610   C  CG2    . VAL   A 1 38  ? -5.479  -20.725 44.201 1.00 27.29  ?  63  VAL   A CG2    1 
ATOM   611   H  H      . VAL   A 1 38  ? -3.940  -18.340 44.784 1.00 25.52  ?  63  VAL   A H      1 
ATOM   612   H  HA     . VAL   A 1 38  ? -4.644  -18.213 42.179 1.00 27.63  ?  63  VAL   A HA     1 
ATOM   613   H  HB     . VAL   A 1 38  ? -5.675  -20.267 42.210 1.00 29.69  ?  63  VAL   A HB     1 
ATOM   614   H  HG11   . VAL   A 1 38  ? -3.925  -21.593 41.976 1.00 30.34  ?  63  VAL   A HG11   1 
ATOM   615   H  HG12   . VAL   A 1 38  ? -3.225  -20.170 41.882 1.00 30.34  ?  63  VAL   A HG12   1 
ATOM   616   H  HG13   . VAL   A 1 38  ? -3.185  -20.986 43.244 1.00 30.34  ?  63  VAL   A HG13   1 
ATOM   617   H  HG21   . VAL   A 1 38  ? -5.340  -21.685 44.168 1.00 32.74  ?  63  VAL   A HG21   1 
ATOM   618   H  HG22   . VAL   A 1 38  ? -4.969  -20.342 44.932 1.00 32.74  ?  63  VAL   A HG22   1 
ATOM   619   H  HG23   . VAL   A 1 38  ? -6.422  -20.531 44.319 1.00 32.74  ?  63  VAL   A HG23   1 
ATOM   620   N  N      . TYR   A 1 39  ? -7.158  -17.992 42.781 1.00 24.22  ?  64  TYR   A N      1 
ATOM   621   C  CA     . TYR   A 1 39  ? -8.503  -17.628 43.217 1.00 26.80  ?  64  TYR   A CA     1 
ATOM   622   C  C      . TYR   A 1 39  ? -9.357  -18.886 43.146 1.00 29.04  ?  64  TYR   A C      1 
ATOM   623   O  O      . TYR   A 1 39  ? -9.700  -19.354 42.052 1.00 29.19  ?  64  TYR   A O      1 
ATOM   624   C  CB     . TYR   A 1 39  ? -9.105  -16.520 42.362 1.00 28.30  ?  64  TYR   A CB     1 
ATOM   625   C  CG     . TYR   A 1 39  ? -10.390 -15.981 42.940 1.00 30.36  ?  64  TYR   A CG     1 
ATOM   626   C  CD1    . TYR   A 1 39  ? -11.568 -16.705 42.860 1.00 31.73  ?  64  TYR   A CD1    1 
ATOM   627   C  CD2    . TYR   A 1 39  ? -10.425 -14.748 43.577 1.00 32.15  ?  64  TYR   A CD2    1 
ATOM   628   C  CE1    . TYR   A 1 39  ? -12.749 -16.208 43.396 1.00 34.16  ?  64  TYR   A CE1    1 
ATOM   629   C  CE2    . TYR   A 1 39  ? -11.600 -14.245 44.110 1.00 34.17  ?  64  TYR   A CE2    1 
ATOM   630   C  CZ     . TYR   A 1 39  ? -12.757 -14.977 44.016 1.00 35.33  ?  64  TYR   A CZ     1 
ATOM   631   O  OH     . TYR   A 1 39  ? -13.921 -14.478 44.552 1.00 39.62  ?  64  TYR   A OH     1 
ATOM   632   H  H      . TYR   A 1 39  ? -7.115  -18.224 41.954 1.00 29.06  ?  64  TYR   A H      1 
ATOM   633   H  HA     . TYR   A 1 39  ? -8.465  -17.305 44.130 1.00 32.16  ?  64  TYR   A HA     1 
ATOM   634   H  HB2    . TYR   A 1 39  ? -8.472  -15.788 42.301 1.00 33.95  ?  64  TYR   A HB2    1 
ATOM   635   H  HB3    . TYR   A 1 39  ? -9.295  -16.870 41.478 1.00 33.95  ?  64  TYR   A HB3    1 
ATOM   636   H  HD1    . TYR   A 1 39  ? -11.569 -17.535 42.440 1.00 38.06  ?  64  TYR   A HD1    1 
ATOM   637   H  HD2    . TYR   A 1 39  ? -9.643  -14.249 43.648 1.00 38.58  ?  64  TYR   A HD2    1 
ATOM   638   H  HE1    . TYR   A 1 39  ? -13.533 -16.706 43.338 1.00 40.98  ?  64  TYR   A HE1    1 
ATOM   639   H  HE2    . TYR   A 1 39  ? -11.605 -13.416 44.531 1.00 41.00  ?  64  TYR   A HE2    1 
ATOM   640   H  HH     . TYR   A 1 39  ? -13.784 -13.718 44.881 1.00 47.54  ?  64  TYR   A HH     1 
ATOM   641   N  N      . ASP   A 1 40  ? -9.692  -19.432 44.307 1.00 31.21  ?  65  ASP   A N      1 
ATOM   642   C  CA     . ASP   A 1 40  ? -10.483 -20.645 44.378 1.00 34.04  ?  65  ASP   A CA     1 
ATOM   643   C  C      . ASP   A 1 40  ? -11.952 -20.314 44.540 1.00 39.14  ?  65  ASP   A C      1 
ATOM   644   O  O      . ASP   A 1 40  ? -12.318 -19.363 45.238 1.00 38.91  ?  65  ASP   A O      1 
ATOM   645   C  CB     . ASP   A 1 40  ? -10.030 -21.514 45.541 1.00 33.66  ?  65  ASP   A CB     1 
ATOM   646   C  CG     . ASP   A 1 40  ? -8.826  -22.325 45.198 1.00 33.12  ?  65  ASP   A CG     1 
ATOM   647   O  OD1    . ASP   A 1 40  ? -8.849  -22.970 44.127 1.00 33.07  ?  65  ASP   A OD1    1 
ATOM   648   O  OD2    . ASP   A 1 40  ? -7.860  -22.305 45.983 1.00 34.05  ?  65  ASP   A OD2    1 
ATOM   649   H  H      . ASP   A 1 40  ? -9.469  -19.113 45.074 1.00 37.44  ?  65  ASP   A H      1 
ATOM   650   H  HA     . ASP   A 1 40  ? -10.368 -21.144 43.554 1.00 40.84  ?  65  ASP   A HA     1 
ATOM   651   H  HB2    . ASP   A 1 40  ? -9.807  -20.946 46.296 1.00 40.38  ?  65  ASP   A HB2    1 
ATOM   652   H  HB3    . ASP   A 1 40  ? -10.746 -22.121 45.783 1.00 40.38  ?  65  ASP   A HB3    1 
ATOM   653   N  N      . GLU   A 1 41  ? -12.789 -21.117 43.896 1.00 44.13  ?  66  GLU   A N      1 
ATOM   654   C  CA     . GLU   A 1 41  ? -14.227 -20.929 43.996 1.00 49.95  ?  66  GLU   A CA     1 
ATOM   655   C  C      . GLU   A 1 41  ? -14.660 -21.054 45.450 1.00 51.35  ?  66  GLU   A C      1 
ATOM   656   O  O      . GLU   A 1 41  ? -14.274 -21.995 46.149 1.00 51.66  ?  66  GLU   A O      1 
ATOM   657   C  CB     . GLU   A 1 41  ? -14.949 -21.947 43.116 1.00 54.94  ?  66  GLU   A CB     1 
ATOM   658   C  CG     . GLU   A 1 41  ? -14.688 -21.731 41.627 1.00 58.46  ?  66  GLU   A CG     1 
ATOM   659   C  CD     . GLU   A 1 41  ? -15.496 -22.647 40.719 1.00 61.94  ?  66  GLU   A CD     1 
ATOM   660   O  OE1    . GLU   A 1 41  ? -15.125 -22.765 39.530 1.00 63.63  ?  66  GLU   A OE1    1 
ATOM   661   O  OE2    . GLU   A 1 41  ? -16.495 -23.240 41.182 1.00 62.83  ?  66  GLU   A OE2    1 
ATOM   662   H  H      . GLU   A 1 41  ? -12.550 -21.775 43.397 1.00 52.95  ?  66  GLU   A H      1 
ATOM   663   H  HA     . GLU   A 1 41  ? -14.473 -20.046 43.681 1.00 59.93  ?  66  GLU   A HA     1 
ATOM   664   H  HB2    . GLU   A 1 41  ? -14.644 -22.838 43.348 1.00 65.92  ?  66  GLU   A HB2    1 
ATOM   665   H  HB3    . GLU   A 1 41  ? -15.905 -21.873 43.267 1.00 65.92  ?  66  GLU   A HB3    1 
ATOM   666   H  HG2    . GLU   A 1 41  ? -14.916 -20.816 41.400 1.00 70.15  ?  66  GLU   A HG2    1 
ATOM   667   H  HG3    . GLU   A 1 41  ? -13.749 -21.893 41.449 1.00 70.15  ?  66  GLU   A HG3    1 
ATOM   668   N  N      . ASP   A 1 42  ? -15.437 -20.075 45.910 1.00 52.74  ?  67  ASP   A N      1 
ATOM   669   C  CA     . ASP   A 1 42  ? -16.013 -20.016 47.249 1.00 55.02  ?  67  ASP   A CA     1 
ATOM   670   C  C      . ASP   A 1 42  ? -14.970 -19.744 48.330 1.00 52.95  ?  67  ASP   A C      1 
ATOM   671   O  O      . ASP   A 1 42  ? -15.274 -19.888 49.522 1.00 53.64  ?  67  ASP   A O      1 
ATOM   672   C  CB     . ASP   A 1 42  ? -16.767 -21.306 47.609 1.00 59.10  ?  67  ASP   A CB     1 
ATOM   673   C  CG     . ASP   A 1 42  ? -17.826 -21.696 46.576 1.00 62.58  ?  67  ASP   A CG     1 
ATOM   674   O  OD1    . ASP   A 1 42  ? -18.460 -20.801 45.975 1.00 64.17  ?  67  ASP   A OD1    1 
ATOM   675   O  OD2    . ASP   A 1 42  ? -18.028 -22.913 46.371 1.00 63.41  ?  67  ASP   A OD2    1 
ATOM   676   H  H      . ASP   A 1 42  ? -15.656 -19.393 45.433 1.00 63.28  ?  67  ASP   A H      1 
ATOM   677   H  HA     . ASP   A 1 42  ? -16.646 -19.281 47.255 1.00 66.02  ?  67  ASP   A HA     1 
ATOM   678   H  HB2    . ASP   A 1 42  ? -16.130 -22.035 47.672 1.00 70.91  ?  67  ASP   A HB2    1 
ATOM   679   H  HB3    . ASP   A 1 42  ? -17.214 -21.182 48.461 1.00 70.91  ?  67  ASP   A HB3    1 
ATOM   680   N  N      . VAL   A 1 43  ? -13.754 -19.347 47.953 1.00 48.84  ?  68  VAL   A N      1 
ATOM   681   C  CA     . VAL   A 1 43  ? -12.666 -19.140 48.902 1.00 46.43  ?  68  VAL   A CA     1 
ATOM   682   C  C      . VAL   A 1 43  ? -12.011 -17.788 48.651 1.00 43.17  ?  68  VAL   A C      1 
ATOM   683   O  O      . VAL   A 1 43  ? -11.706 -17.042 49.588 1.00 43.64  ?  68  VAL   A O      1 
ATOM   684   C  CB     . VAL   A 1 43  ? -11.624 -20.272 48.794 1.00 47.48  ?  68  VAL   A CB     1 
ATOM   685   C  CG1    . VAL   A 1 43  ? -10.427 -19.976 49.680 1.00 46.58  ?  68  VAL   A CG1    1 
ATOM   686   C  CG2    . VAL   A 1 43  ? -12.257 -21.611 49.138 1.00 49.44  ?  68  VAL   A CG2    1 
ATOM   687   H  H      . VAL   A 1 43  ? -13.532 -19.189 47.137 1.00 58.60  ?  68  VAL   A H      1 
ATOM   688   H  HA     . VAL   A 1 43  ? -13.034 -19.132 49.799 1.00 55.71  ?  68  VAL   A HA     1 
ATOM   689   H  HB     . VAL   A 1 43  ? -11.305 -20.327 47.880 1.00 56.97  ?  68  VAL   A HB     1 
ATOM   690   H  HG11   . VAL   A 1 43  ? -9.923  -20.794 49.812 1.00 55.89  ?  68  VAL   A HG11   1 
ATOM   691   H  HG12   . VAL   A 1 43  ? -9.871  -19.310 49.247 1.00 55.89  ?  68  VAL   A HG12   1 
ATOM   692   H  HG13   . VAL   A 1 43  ? -10.742 -19.641 50.534 1.00 55.89  ?  68  VAL   A HG13   1 
ATOM   693   H  HG21   . VAL   A 1 43  ? -11.577 -22.301 49.094 1.00 59.32  ?  68  VAL   A HG21   1 
ATOM   694   H  HG22   . VAL   A 1 43  ? -12.625 -21.565 50.034 1.00 59.32  ?  68  VAL   A HG22   1 
ATOM   695   H  HG23   . VAL   A 1 43  ? -12.962 -21.800 48.499 1.00 59.32  ?  68  VAL   A HG23   1 
ATOM   696   N  N      . GLY   A 1 44  ? -11.780 -17.473 47.391 1.00 40.41  ?  69  GLY   A N      1 
ATOM   697   C  CA     . GLY   A 1 44  ? -11.117 -16.240 47.047 1.00 37.43  ?  69  GLY   A CA     1 
ATOM   698   C  C      . GLY   A 1 44  ? -9.625  -16.440 46.873 1.00 34.46  ?  69  GLY   A C      1 
ATOM   699   O  O      . GLY   A 1 44  ? -9.125  -17.541 46.623 1.00 33.85  ?  69  GLY   A O      1 
ATOM   700   H  H      . GLY   A 1 44  ? -11.998 -17.960 46.717 1.00 48.48  ?  69  GLY   A H      1 
ATOM   701   H  HA2    . GLY   A 1 44  ? -11.482 -15.896 46.216 1.00 44.91  ?  69  GLY   A HA2    1 
ATOM   702   H  HA3    . GLY   A 1 44  ? -11.262 -15.586 47.749 1.00 44.91  ?  69  GLY   A HA3    1 
ATOM   703   N  N      . ILE   A 1 45  ? -8.897  -15.338 47.016 1.00 33.63  ?  70  ILE   A N      1 
ATOM   704   C  CA     . ILE   A 1 45  ? -7.455  -15.383 46.810 1.00 31.93  ?  70  ILE   A CA     1 
ATOM   705   C  C      . ILE   A 1 45  ? -6.809  -16.114 47.981 1.00 31.53  ?  70  ILE   A C      1 
ATOM   706   O  O      . ILE   A 1 45  ? -7.125  -15.855 49.150 1.00 33.77  ?  70  ILE   A O      1 
ATOM   707   C  CB     . ILE   A 1 45  ? -6.896  -13.964 46.618 1.00 34.99  ?  70  ILE   A CB     1 
ATOM   708   C  CG1    . ILE   A 1 45  ? -7.268  -13.477 45.207 1.00 39.62  ?  70  ILE   A CG1    1 
ATOM   709   C  CG2    . ILE   A 1 45  ? -5.384  -13.952 46.813 1.00 33.73  ?  70  ILE   A CG2    1 
ATOM   710   C  CD1    . ILE   A 1 45  ? -6.689  -12.152 44.798 1.00 43.02  ?  70  ILE   A CD1    1 
ATOM   711   H  H      . ILE   A 1 45  ? -9.209  -14.565 47.228 1.00 40.36  ?  70  ILE   A H      1 
ATOM   712   H  HA     . ILE   A 1 45  ? -7.253  -15.883 46.004 1.00 38.30  ?  70  ILE   A HA     1 
ATOM   713   H  HB     . ILE   A 1 45  ? -7.283  -13.369 47.279 1.00 41.99  ?  70  ILE   A HB     1 
ATOM   714   H  HG12   . ILE   A 1 45  ? -6.958  -14.136 44.566 1.00 47.54  ?  70  ILE   A HG12   1 
ATOM   715   H  HG13   . ILE   A 1 45  ? -8.233  -13.395 45.158 1.00 47.54  ?  70  ILE   A HG13   1 
ATOM   716   H  HG21   . ILE   A 1 45  ? -5.037  -13.087 46.543 1.00 40.47  ?  70  ILE   A HG21   1 
ATOM   717   H  HG22   . ILE   A 1 45  ? -5.185  -14.111 47.749 1.00 40.47  ?  70  ILE   A HG22   1 
ATOM   718   H  HG23   . ILE   A 1 45  ? -4.990  -14.651 46.268 1.00 40.47  ?  70  ILE   A HG23   1 
ATOM   719   H  HD11   . ILE   A 1 45  ? -7.166  -11.826 44.019 1.00 51.62  ?  70  ILE   A HD11   1 
ATOM   720   H  HD12   . ILE   A 1 45  ? -6.785  -11.526 45.532 1.00 51.62  ?  70  ILE   A HD12   1 
ATOM   721   H  HD13   . ILE   A 1 45  ? -5.750  -12.271 44.585 1.00 51.62  ?  70  ILE   A HD13   1 
ATOM   722   N  N      . ASN   A 1 46  ? -5.920  -17.060 47.670 1.00 28.35  ?  71  ASN   A N      1 
ATOM   723   C  CA     . ASN   A 1 46  ? -5.209  -17.797 48.709 1.00 27.86  ?  71  ASN   A CA     1 
ATOM   724   C  C      . ASN   A 1 46  ? -3.944  -18.423 48.128 1.00 25.65  ?  71  ASN   A C      1 
ATOM   725   O  O      . ASN   A 1 46  ? -3.795  -18.579 46.911 1.00 24.97  ?  71  ASN   A O      1 
ATOM   726   C  CB     . ASN   A 1 46  ? -6.110  -18.861 49.370 1.00 30.64  ?  71  ASN   A CB     1 
ATOM   727   C  CG     . ASN   A 1 46  ? -6.397  -20.051 48.467 1.00 31.87  ?  71  ASN   A CG     1 
ATOM   728   O  OD1    . ASN   A 1 46  ? -5.906  -21.155 48.702 1.00 33.68  ?  71  ASN   A OD1    1 
ATOM   729   N  ND2    . ASN   A 1 46  ? -7.221  -19.840 47.451 1.00 31.03  ?  71  ASN   A ND2    1 
ATOM   730   H  H      . ASN   A 1 46  ? -5.715  -17.291 46.868 1.00 34.01  ?  71  ASN   A H      1 
ATOM   731   H  HA     . ASN   A 1 46  ? -4.926  -17.172 49.395 1.00 33.43  ?  71  ASN   A HA     1 
ATOM   732   H  HB2    . ASN   A 1 46  ? -5.670  -19.193 50.169 1.00 36.76  ?  71  ASN   A HB2    1 
ATOM   733   H  HB3    . ASN   A 1 46  ? -6.958  -18.453 49.604 1.00 36.76  ?  71  ASN   A HB3    1 
ATOM   734   H  HD21   . ASN   A 1 46  ? -7.413  -20.483 46.913 1.00 37.22  ?  71  ASN   A HD21   1 
ATOM   735   H  HD22   . ASN   A 1 46  ? -7.563  -19.060 47.329 1.00 37.22  ?  71  ASN   A HD22   1 
ATOM   736   N  N      . TYR   A 1 47  ? -3.019  -18.739 49.036 1.00 25.57  ?  72  TYR   A N      1 
ATOM   737   C  CA     . TYR   A 1 47  ? -1.696  -19.268 48.715 1.00 25.41  ?  72  TYR   A CA     1 
ATOM   738   C  C      . TYR   A 1 47  ? -1.685  -20.759 49.020 1.00 25.29  ?  72  TYR   A C      1 
ATOM   739   O  O      . TYR   A 1 47  ? -1.897  -21.154 50.171 1.00 26.67  ?  72  TYR   A O      1 
ATOM   740   C  CB     . TYR   A 1 47  ? -0.628  -18.537 49.531 1.00 25.91  ?  72  TYR   A CB     1 
ATOM   741   C  CG     . TYR   A 1 47  ? 0.798   -18.764 49.089 1.00 26.18  ?  72  TYR   A CG     1 
ATOM   742   C  CD1    . TYR   A 1 47  ? 1.263   -18.208 47.908 1.00 26.65  ?  72  TYR   A CD1    1 
ATOM   743   C  CD2    . TYR   A 1 47  ? 1.684   -19.516 49.851 1.00 28.88  ?  72  TYR   A CD2    1 
ATOM   744   C  CE1    . TYR   A 1 47  ? 2.552   -18.395 47.482 1.00 27.62  ?  72  TYR   A CE1    1 
ATOM   745   C  CE2    . TYR   A 1 47  ? 3.002   -19.701 49.426 1.00 29.18  ?  72  TYR   A CE2    1 
ATOM   746   C  CZ     . TYR   A 1 47  ? 3.422   -19.135 48.233 1.00 29.03  ?  72  TYR   A CZ     1 
ATOM   747   O  OH     . TYR   A 1 47  ? 4.711   -19.300 47.762 1.00 29.88  ?  72  TYR   A OH     1 
ATOM   748   H  H      . TYR   A 1 47  ? -3.141  -18.652 49.883 1.00 30.68  ?  72  TYR   A H      1 
ATOM   749   H  HA     . TYR   A 1 47  ? -1.502  -19.147 47.772 1.00 30.49  ?  72  TYR   A HA     1 
ATOM   750   H  HB2    . TYR   A 1 47  ? -0.800  -17.584 49.473 1.00 31.08  ?  72  TYR   A HB2    1 
ATOM   751   H  HB3    . TYR   A 1 47  ? -0.695  -18.831 50.453 1.00 31.08  ?  72  TYR   A HB3    1 
ATOM   752   H  HD1    . TYR   A 1 47  ? 0.685   -17.695 47.390 1.00 31.97  ?  72  TYR   A HD1    1 
ATOM   753   H  HD2    . TYR   A 1 47  ? 1.398   -19.898 50.649 1.00 34.65  ?  72  TYR   A HD2    1 
ATOM   754   H  HE1    . TYR   A 1 47  ? 2.835   -18.018 46.681 1.00 33.14  ?  72  TYR   A HE1    1 
ATOM   755   H  HE2    . TYR   A 1 47  ? 3.593   -20.202 49.940 1.00 35.01  ?  72  TYR   A HE2    1 
ATOM   756   H  HH     . TYR   A 1 47  ? 5.161   -19.752 48.308 1.00 35.84  ?  72  TYR   A HH     1 
ATOM   757   N  N      . ARG   A 1 48  ? -1.442  -21.581 47.999 1.00 25.11  ?  73  ARG   A N      1 
ATOM   758   C  CA     . ARG   A 1 48  ? -1.435  -23.024 48.195 1.00 26.13  ?  73  ARG   A CA     1 
ATOM   759   C  C      . ARG   A 1 48  ? -0.612  -23.702 47.109 1.00 25.37  ?  73  ARG   A C      1 
ATOM   760   O  O      . ARG   A 1 48  ? -0.249  -23.104 46.094 1.00 25.87  ?  73  ARG   A O      1 
ATOM   761   C  CB     . ARG   A 1 48  ? -2.859  -23.609 48.202 1.00 28.07  ?  73  ARG   A CB     1 
ATOM   762   C  CG     . ARG   A 1 48  ? -3.605  -23.518 46.873 1.00 29.09  ?  73  ARG   A CG     1 
ATOM   763   C  CD     . ARG   A 1 48  ? -4.955  -24.200 46.965 1.00 29.99  ?  73  ARG   A CD     1 
ATOM   764   N  NE     . ARG   A 1 48  ? -5.785  -24.096 45.764 1.00 30.48  ?  73  ARG   A NE     1 
ATOM   765   C  CZ     . ARG   A 1 48  ? -5.654  -24.860 44.682 1.00 31.06  ?  73  ARG   A CZ     1 
ATOM   766   N  NH1    . ARG   A 1 48  ? -4.688  -25.767 44.613 1.00 32.91  ?  73  ARG   A NH1    1 
ATOM   767   N  NH2    . ARG   A 1 48  ? -6.476  -24.705 43.654 1.00 30.54  ?  73  ARG   A NH2    1 
ATOM   768   H  H      . ARG   A 1 48  ? -1.280  -21.326 47.193 1.00 30.13  ?  73  ARG   A H      1 
ATOM   769   H  HA     . ARG   A 1 48  ? -1.008  -23.192 49.050 1.00 31.35  ?  73  ARG   A HA     1 
ATOM   770   H  HB2    . ARG   A 1 48  ? -2.802  -24.548 48.439 1.00 33.68  ?  73  ARG   A HB2    1 
ATOM   771   H  HB3    . ARG   A 1 48  ? -3.383  -23.131 48.863 1.00 33.68  ?  73  ARG   A HB3    1 
ATOM   772   H  HG2    . ARG   A 1 48  ? -3.746  -22.586 46.645 1.00 34.90  ?  73  ARG   A HG2    1 
ATOM   773   H  HG3    . ARG   A 1 48  ? -3.086  -23.955 46.180 1.00 34.90  ?  73  ARG   A HG3    1 
ATOM   774   H  HD2    . ARG   A 1 48  ? -4.812  -25.143 47.138 1.00 35.98  ?  73  ARG   A HD2    1 
ATOM   775   H  HD3    . ARG   A 1 48  ? -5.452  -23.800 47.696 1.00 35.98  ?  73  ARG   A HD3    1 
ATOM   776   H  HE     . ARG   A 1 48  ? -6.402  -23.498 45.757 1.00 36.57  ?  73  ARG   A HE     1 
ATOM   777   H  HH11   . ARG   A 1 48  ? -4.141  -25.863 45.269 1.00 39.49  ?  73  ARG   A HH11   1 
ATOM   778   H  HH12   . ARG   A 1 48  ? -4.609  -26.258 43.911 1.00 39.49  ?  73  ARG   A HH12   1 
ATOM   779   H  HH21   . ARG   A 1 48  ? -7.096  -24.110 43.686 1.00 36.64  ?  73  ARG   A HH21   1 
ATOM   780   H  HH22   . ARG   A 1 48  ? -6.390  -25.200 42.956 1.00 36.64  ?  73  ARG   A HH22   1 
ATOM   781   N  N      . GLU   A 1 49  ? -0.336  -24.975 47.335 1.00 24.78  ?  74  GLU   A N      1 
ATOM   782   C  CA     . GLU   A 1 49  ? 0.337   -25.769 46.325 1.00 24.66  ?  74  GLU   A CA     1 
ATOM   783   C  C      . GLU   A 1 49  ? -0.595  -25.990 45.142 1.00 24.70  ?  74  GLU   A C      1 
ATOM   784   O  O      . GLU   A 1 49  ? -1.772  -26.322 45.318 1.00 25.61  ?  74  GLU   A O      1 
ATOM   785   C  CB     . GLU   A 1 49  ? 0.774   -27.098 46.921 1.00 27.55  ?  74  GLU   A CB     1 
ATOM   786   C  CG     . GLU   A 1 49  ? 1.550   -27.940 45.961 1.00 31.57  ?  74  GLU   A CG     1 
ATOM   787   C  CD     . GLU   A 1 49  ? 1.902   -29.281 46.548 1.00 36.44  ?  74  GLU   A CD     1 
ATOM   788   O  OE1    . GLU   A 1 49  ? 1.201   -30.277 46.249 1.00 38.73  ?  74  GLU   A OE1    1 
ATOM   789   O  OE2    . GLU   A 1 49  ? 2.870   -29.332 47.330 1.00 39.09  ?  74  GLU   A OE2    1 
ATOM   790   H  H      . GLU   A 1 49  ? -0.525  -25.399 48.059 1.00 29.73  ?  74  GLU   A H      1 
ATOM   791   H  HA     . GLU   A 1 49  ? 1.129   -25.306 46.007 1.00 29.59  ?  74  GLU   A HA     1 
ATOM   792   H  HB2    . GLU   A 1 49  ? 1.336   -26.928 47.693 1.00 33.06  ?  74  GLU   A HB2    1 
ATOM   793   H  HB3    . GLU   A 1 49  ? -0.014  -27.597 47.188 1.00 33.06  ?  74  GLU   A HB3    1 
ATOM   794   H  HG2    . GLU   A 1 49  ? 1.019   -28.088 45.163 1.00 37.88  ?  74  GLU   A HG2    1 
ATOM   795   H  HG3    . GLU   A 1 49  ? 2.375   -27.484 45.731 1.00 37.88  ?  74  GLU   A HG3    1 
ATOM   796   N  N      . VAL   A 1 50  ? -0.070  -25.790 43.935 1.00 24.23  ?  75  VAL   A N      1 
ATOM   797   C  CA     . VAL   A 1 50  ? -0.791  -26.088 42.706 1.00 26.16  ?  75  VAL   A CA     1 
ATOM   798   C  C      . VAL   A 1 50  ? 0.125   -26.882 41.783 1.00 24.56  ?  75  VAL   A C      1 
ATOM   799   O  O      . VAL   A 1 50  ? 1.355   -26.766 41.841 1.00 25.15  ?  75  VAL   A O      1 
ATOM   800   C  CB     . VAL   A 1 50  ? -1.282  -24.819 41.984 1.00 28.75  ?  75  VAL   A CB     1 
ATOM   801   C  CG1    . VAL   A 1 50  ? -2.401  -24.123 42.753 1.00 31.18  ?  75  VAL   A CG1    1 
ATOM   802   C  CG2    . VAL   A 1 50  ? -0.132  -23.912 41.826 1.00 29.67  ?  75  VAL   A CG2    1 
ATOM   803   H  H      . VAL   A 1 50  ? 0.719   -25.475 43.803 1.00 29.07  ?  75  VAL   A H      1 
ATOM   804   H  HA     . VAL   A 1 50  ? -1.564  -26.630 42.930 1.00 31.39  ?  75  VAL   A HA     1 
ATOM   805   H  HB     . VAL   A 1 50  ? -1.649  -25.060 41.119 1.00 34.50  ?  75  VAL   A HB     1 
ATOM   806   H  HG11   . VAL   A 1 50  ? -2.594  -23.273 42.329 1.00 37.40  ?  75  VAL   A HG11   1 
ATOM   807   H  HG12   . VAL   A 1 50  ? -3.190  -24.687 42.741 1.00 37.40  ?  75  VAL   A HG12   1 
ATOM   808   H  HG13   . VAL   A 1 50  ? -2.112  -23.978 43.668 1.00 37.40  ?  75  VAL   A HG13   1 
ATOM   809   H  HG21   . VAL   A 1 50  ? -0.413  -23.128 41.328 1.00 35.60  ?  75  VAL   A HG21   1 
ATOM   810   H  HG22   . VAL   A 1 50  ? 0.186   -23.649 42.704 1.00 35.60  ?  75  VAL   A HG22   1 
ATOM   811   H  HG23   . VAL   A 1 50  ? 0.572   -24.374 41.344 1.00 35.60  ?  75  VAL   A HG23   1 
ATOM   812   N  N      . THR   A 1 51  ? -0.489  -27.676 40.910 1.00 22.51  ?  76  THR   A N      1 
ATOM   813   C  CA     . THR   A 1 51  ? 0.210   -28.432 39.875 1.00 21.67  ?  76  THR   A CA     1 
ATOM   814   C  C      . THR   A 1 51  ? -0.330  -27.967 38.532 1.00 20.71  ?  76  THR   A C      1 
ATOM   815   O  O      . THR   A 1 51  ? -1.542  -28.024 38.297 1.00 21.12  ?  76  THR   A O      1 
ATOM   816   C  CB     . THR   A 1 51  ? 0.025   -29.932 40.085 1.00 24.35  ?  76  THR   A CB     1 
ATOM   817   O  OG1    . THR   A 1 51  ? 0.695   -30.302 41.297 1.00 26.59  ?  76  THR   A OG1    1 
ATOM   818   C  CG2    . THR   A 1 51  ? 0.622   -30.695 38.932 1.00 26.17  ?  76  THR   A CG2    1 
ATOM   819   H  H      . THR   A 1 51  ? -1.340  -27.798 40.897 1.00 27.01  ?  76  THR   A H      1 
ATOM   820   H  HA     . THR   A 1 51  ? 1.164   -28.258 39.895 1.00 26.00  ?  76  THR   A HA     1 
ATOM   821   H  HB     . THR   A 1 51  ? -0.918  -30.155 40.141 1.00 29.21  ?  76  THR   A HB     1 
ATOM   822   H  HG1    . THR   A 1 51  ? 0.620   -31.129 41.426 1.00 31.90  ?  76  THR   A HG1    1 
ATOM   823   H  HG21   . THR   A 1 51  ? 0.729   -31.629 39.172 1.00 31.40  ?  76  THR   A HG21   1 
ATOM   824   H  HG22   . THR   A 1 51  ? 0.042   -30.633 38.157 1.00 31.40  ?  76  THR   A HG22   1 
ATOM   825   H  HG23   . THR   A 1 51  ? 1.491   -30.327 38.705 1.00 31.40  ?  76  THR   A HG23   1 
ATOM   826   N  N      . PHE   A 1 52  ? 0.556   -27.439 37.685 1.00 19.19  ?  77  PHE   A N      1 
ATOM   827   C  CA     . PHE   A 1 52  ? 0.133   -26.808 36.442 1.00 19.19  ?  77  PHE   A CA     1 
ATOM   828   C  C      . PHE   A 1 52  ? 1.288   -26.810 35.451 1.00 18.34  ?  77  PHE   A C      1 
ATOM   829   O  O      . PHE   A 1 52  ? 2.446   -27.047 35.804 1.00 18.71  ?  77  PHE   A O      1 
ATOM   830   C  CB     . PHE   A 1 52  ? -0.360  -25.368 36.680 1.00 18.79  ?  77  PHE   A CB     1 
ATOM   831   C  CG     . PHE   A 1 52  ? 0.745   -24.391 36.997 1.00 18.43  ?  77  PHE   A CG     1 
ATOM   832   C  CD1    . PHE   A 1 52  ? 1.340   -24.388 38.248 1.00 20.39  ?  77  PHE   A CD1    1 
ATOM   833   C  CD2    . PHE   A 1 52  ? 1.183   -23.475 36.046 1.00 18.71  ?  77  PHE   A CD2    1 
ATOM   834   C  CE1    . PHE   A 1 52  ? 2.357   -23.497 38.549 1.00 21.46  ?  77  PHE   A CE1    1 
ATOM   835   C  CE2    . PHE   A 1 52  ? 2.209   -22.580 36.337 1.00 20.40  ?  77  PHE   A CE2    1 
ATOM   836   C  CZ     . PHE   A 1 52  ? 2.796   -22.592 37.587 1.00 20.81  ?  77  PHE   A CZ     1 
ATOM   837   H  H      . PHE   A 1 52  ? 1.407   -27.436 37.811 1.00 23.02  ?  77  PHE   A H      1 
ATOM   838   H  HA     . PHE   A 1 52  ? -0.590  -27.335 36.067 1.00 23.03  ?  77  PHE   A HA     1 
ATOM   839   H  HB2    . PHE   A 1 52  ? -0.810  -25.057 35.879 1.00 22.54  ?  77  PHE   A HB2    1 
ATOM   840   H  HB3    . PHE   A 1 52  ? -0.978  -25.370 37.428 1.00 22.54  ?  77  PHE   A HB3    1 
ATOM   841   H  HD1    . PHE   A 1 52  ? 1.053   -24.992 38.895 1.00 24.46  ?  77  PHE   A HD1    1 
ATOM   842   H  HD2    . PHE   A 1 52  ? 0.786   -23.461 35.205 1.00 22.45  ?  77  PHE   A HD2    1 
ATOM   843   H  HE1    . PHE   A 1 52  ? 2.747   -23.504 39.393 1.00 25.74  ?  77  PHE   A HE1    1 
ATOM   844   H  HE2    . PHE   A 1 52  ? 2.498   -21.976 35.692 1.00 24.47  ?  77  PHE   A HE2    1 
ATOM   845   H  HZ     . PHE   A 1 52  ? 3.483   -21.996 37.785 1.00 24.97  ?  77  PHE   A HZ     1 
ATOM   846   N  N      . VAL   A 1 53  ? 0.964   -26.485 34.207 1.00 18.20  ?  78  VAL   A N      1 
ATOM   847   C  CA     . VAL   A 1 53  ? 1.955   -26.390 33.140 1.00 17.19  ?  78  VAL   A CA     1 
ATOM   848   C  C      . VAL   A 1 53  ? 2.159   -24.917 32.804 1.00 16.75  ?  78  VAL   A C      1 
ATOM   849   O  O      . VAL   A 1 53  ? 1.225   -24.265 32.315 1.00 17.45  ?  78  VAL   A O      1 
ATOM   850   C  CB     . VAL   A 1 53  ? 1.533   -27.184 31.896 1.00 18.86  ?  78  VAL   A CB     1 
ATOM   851   C  CG1    . VAL   A 1 53  ? 2.615   -27.082 30.841 1.00 19.69  ?  78  VAL   A CG1    1 
ATOM   852   C  CG2    . VAL   A 1 53  ? 1.284   -28.635 32.268 1.00 18.88  ?  78  VAL   A CG2    1 
ATOM   853   H  H      . VAL   A 1 53  ? 0.162   -26.310 33.951 1.00 21.83  ?  78  VAL   A H      1 
ATOM   854   H  HA     . VAL   A 1 53  ? 2.797   -26.749 33.461 1.00 20.62  ?  78  VAL   A HA     1 
ATOM   855   H  HB     . VAL   A 1 53  ? 0.711   -26.819 31.534 1.00 22.62  ?  78  VAL   A HB     1 
ATOM   856   H  HG11   . VAL   A 1 53  ? 2.429   -27.722 30.136 1.00 23.62  ?  78  VAL   A HG11   1 
ATOM   857   H  HG12   . VAL   A 1 53  ? 2.619   -26.183 30.478 1.00 23.62  ?  78  VAL   A HG12   1 
ATOM   858   H  HG13   . VAL   A 1 53  ? 3.473   -27.278 31.248 1.00 23.62  ?  78  VAL   A HG13   1 
ATOM   859   H  HG21   . VAL   A 1 53  ? 1.068   -29.134 31.466 1.00 22.65  ?  78  VAL   A HG21   1 
ATOM   860   H  HG22   . VAL   A 1 53  ? 2.085   -28.997 32.678 1.00 22.65  ?  78  VAL   A HG22   1 
ATOM   861   H  HG23   . VAL   A 1 53  ? 0.544   -28.678 32.894 1.00 22.65  ?  78  VAL   A HG23   1 
ATOM   862   N  N      . PRO   A 1 54  ? 3.358   -24.361 33.021 1.00 16.64  ?  79  PRO   A N      1 
ATOM   863   C  CA     . PRO   A 1 54  ? 3.559   -22.923 32.747 1.00 15.15  ?  79  PRO   A CA     1 
ATOM   864   C  C      . PRO   A 1 54  ? 3.192   -22.498 31.334 1.00 15.71  ?  79  PRO   A C      1 
ATOM   865   O  O      . PRO   A 1 54  ? 2.585   -21.430 31.158 1.00 16.16  ?  79  PRO   A O      1 
ATOM   866   C  CB     . PRO   A 1 54  ? 5.059   -22.726 33.048 1.00 15.91  ?  79  PRO   A CB     1 
ATOM   867   C  CG     . PRO   A 1 54  ? 5.334   -23.741 34.142 1.00 16.55  ?  79  PRO   A CG     1 
ATOM   868   C  CD     . PRO   A 1 54  ? 4.518   -24.965 33.718 1.00 16.56  ?  79  PRO   A CD     1 
ATOM   869   H  HA     . PRO   A 1 54  ? 3.030   -22.398 33.368 1.00 18.17  ?  79  PRO   A HA     1 
ATOM   870   H  HB2    . PRO   A 1 54  ? 5.589   -22.909 32.256 1.00 19.08  ?  79  PRO   A HB2    1 
ATOM   871   H  HB3    . PRO   A 1 54  ? 5.225   -21.821 33.355 1.00 19.08  ?  79  PRO   A HB3    1 
ATOM   872   H  HG2    . PRO   A 1 54  ? 6.281   -23.946 34.179 1.00 19.85  ?  79  PRO   A HG2    1 
ATOM   873   H  HG3    . PRO   A 1 54  ? 5.034   -23.399 34.999 1.00 19.85  ?  79  PRO   A HG3    1 
ATOM   874   H  HD2    . PRO   A 1 54  ? 5.028   -25.531 33.117 1.00 19.87  ?  79  PRO   A HD2    1 
ATOM   875   H  HD3    . PRO   A 1 54  ? 4.231   -25.476 34.491 1.00 19.87  ?  79  PRO   A HD3    1 
ATOM   876   N  N      . GLY   A 1 55  ? 3.514   -23.301 30.322 1.00 16.48  ?  80  GLY   A N      1 
ATOM   877   C  CA     . GLY   A 1 55  ? 3.248   -22.874 28.960 1.00 16.39  ?  80  GLY   A CA     1 
ATOM   878   C  C      . GLY   A 1 55  ? 1.777   -22.675 28.663 1.00 17.14  ?  80  GLY   A C      1 
ATOM   879   O  O      . GLY   A 1 55  ? 1.421   -21.805 27.858 1.00 17.48  ?  80  GLY   A O      1 
ATOM   880   H  H      . GLY   A 1 55  ? 3.878   -24.076 30.399 1.00 19.77  ?  80  GLY   A H      1 
ATOM   881   H  HA2    . GLY   A 1 55  ? 3.704   -22.033 28.798 1.00 19.67  ?  80  GLY   A HA2    1 
ATOM   882   H  HA3    . GLY   A 1 55  ? 3.591   -23.542 28.347 1.00 19.67  ?  80  GLY   A HA3    1 
ATOM   883   N  N      . LEU   A 1 56  ? 0.912   -23.486 29.279 1.00 16.72  ?  81  LEU   A N      1 
ATOM   884   C  CA     . LEU   A 1 56  ? -0.532  -23.325 29.107 1.00 17.02  ?  81  LEU   A CA     1 
ATOM   885   C  C      . LEU   A 1 56  ? -1.018  -22.025 29.741 1.00 17.42  ?  81  LEU   A C      1 
ATOM   886   O  O      . LEU   A 1 56  ? -1.792  -21.268 29.140 1.00 18.32  ?  81  LEU   A O      1 
ATOM   887   C  CB     . LEU   A 1 56  ? -1.261  -24.526 29.717 1.00 19.74  ?  81  LEU   A CB     1 
ATOM   888   C  CG     . LEU   A 1 56  ? -2.788  -24.418 29.710 1.00 21.60  ?  81  LEU   A CG     1 
ATOM   889   C  CD1    . LEU   A 1 56  ? -3.362  -24.244 28.308 1.00 24.76  ?  81  LEU   A CD1    1 
ATOM   890   C  CD2    . LEU   A 1 56  ? -3.393  -25.654 30.401 1.00 24.73  ?  81  LEU   A CD2    1 
ATOM   891   H  H      . LEU   A 1 56  ? 1.134   -24.134 29.799 1.00 20.06  ?  81  LEU   A H      1 
ATOM   892   H  HA     . LEU   A 1 56  ? -0.736  -23.291 28.159 1.00 20.42  ?  81  LEU   A HA     1 
ATOM   893   H  HB2    . LEU   A 1 56  ? -1.022  -25.320 29.213 1.00 23.68  ?  81  LEU   A HB2    1 
ATOM   894   H  HB3    . LEU   A 1 56  ? -0.979  -24.621 30.640 1.00 23.68  ?  81  LEU   A HB3    1 
ATOM   895   H  HG     . LEU   A 1 56  ? -3.038  -23.619 30.200 1.00 25.91  ?  81  LEU   A HG     1 
ATOM   896   H  HD11   . LEU   A 1 56  ? -4.330  -24.269 28.358 1.00 29.71  ?  81  LEU   A HD11   1 
ATOM   897   H  HD12   . LEU   A 1 56  ? -3.070  -23.391 27.951 1.00 29.71  ?  81  LEU   A HD12   1 
ATOM   898   H  HD13   . LEU   A 1 56  ? -3.041  -24.966 27.744 1.00 29.71  ?  81  LEU   A HD13   1 
ATOM   899   H  HD21   . LEU   A 1 56  ? -4.341  -25.505 30.542 1.00 29.67  ?  81  LEU   A HD21   1 
ATOM   900   H  HD22   . LEU   A 1 56  ? -3.261  -26.429 29.834 1.00 29.67  ?  81  LEU   A HD22   1 
ATOM   901   H  HD23   . LEU   A 1 56  ? -2.949  -25.788 31.253 1.00 29.67  ?  81  LEU   A HD23   1 
ATOM   902   N  N      . TYR   A 1 57  ? -0.567  -21.746 30.959 1.00 17.18  ?  82  TYR   A N      1 
ATOM   903   C  CA     . TYR   A 1 57  ? -0.888  -20.481 31.611 1.00 16.63  ?  82  TYR   A CA     1 
ATOM   904   C  C      . TYR   A 1 57  ? -0.426  -19.300 30.775 1.00 16.51  ?  82  TYR   A C      1 
ATOM   905   O  O      . TYR   A 1 57  ? -1.128  -18.283 30.673 1.00 17.08  ?  82  TYR   A O      1 
ATOM   906   C  CB     . TYR   A 1 57  ? -0.217  -20.459 32.974 1.00 17.16  ?  82  TYR   A CB     1 
ATOM   907   C  CG     . TYR   A 1 57  ? -0.687  -19.461 33.997 1.00 17.63  ?  82  TYR   A CG     1 
ATOM   908   C  CD1    . TYR   A 1 57  ? -1.956  -18.897 33.967 1.00 17.61  ?  82  TYR   A CD1    1 
ATOM   909   C  CD2    . TYR   A 1 57  ? 0.152   -19.104 35.034 1.00 17.27  ?  82  TYR   A CD2    1 
ATOM   910   C  CE1    . TYR   A 1 57  ? -2.359  -18.003 34.953 1.00 19.15  ?  82  TYR   A CE1    1 
ATOM   911   C  CE2    . TYR   A 1 57  ? -0.245  -18.228 36.011 1.00 18.97  ?  82  TYR   A CE2    1 
ATOM   912   C  CZ     . TYR   A 1 57  ? -1.496  -17.691 35.975 1.00 20.09  ?  82  TYR   A CZ     1 
ATOM   913   O  OH     . TYR   A 1 57  ? -1.854  -16.832 36.979 1.00 22.49  ?  82  TYR   A OH     1 
ATOM   914   H  H      . TYR   A 1 57  ? -0.074  -22.271 31.430 1.00 20.61  ?  82  TYR   A H      1 
ATOM   915   H  HA     . TYR   A 1 57  ? -1.848  -20.403 31.724 1.00 19.95  ?  82  TYR   A HA     1 
ATOM   916   H  HB2    . TYR   A 1 57  ? -0.334  -21.336 33.371 1.00 20.59  ?  82  TYR   A HB2    1 
ATOM   917   H  HB3    . TYR   A 1 57  ? 0.726   -20.283 32.832 1.00 20.59  ?  82  TYR   A HB3    1 
ATOM   918   H  HD1    . TYR   A 1 57  ? -2.542  -19.118 33.280 1.00 21.12  ?  82  TYR   A HD1    1 
ATOM   919   H  HD2    . TYR   A 1 57  ? 1.007   -19.466 35.070 1.00 20.72  ?  82  TYR   A HD2    1 
ATOM   920   H  HE1    . TYR   A 1 57  ? -3.206  -17.620 34.920 1.00 22.97  ?  82  TYR   A HE1    1 
ATOM   921   H  HE2    . TYR   A 1 57  ? 0.340   -18.000 36.698 1.00 22.76  ?  82  TYR   A HE2    1 
ATOM   922   H  HH     . TYR   A 1 57  ? -2.641  -16.564 36.860 1.00 26.99  ?  82  TYR   A HH     1 
ATOM   923   N  N      . LYS   A 1 58  ? 0.744   -19.430 30.149 1.00 16.43  ?  83  LYS   A N      1 
ATOM   924   C  CA     . LYS   A 1 58  ? 1.335   -18.331 29.400 1.00 16.79  ?  83  LYS   A CA     1 
ATOM   925   C  C      . LYS   A 1 58  ? 0.570   -18.020 28.122 1.00 16.12  ?  83  LYS   A C      1 
ATOM   926   O  O      . LYS   A 1 58  ? 0.430   -16.845 27.771 1.00 17.05  ?  83  LYS   A O      1 
ATOM   927   C  CB     . LYS   A 1 58  ? 2.796   -18.650 29.084 1.00 17.31  ?  83  LYS   A CB     1 
ATOM   928   C  CG     . LYS   A 1 58  ? 3.525   -17.599 28.259 1.00 18.13  ?  83  LYS   A CG     1 
ATOM   929   C  CD     . LYS   A 1 58  ? 3.491   -16.177 28.846 1.00 19.52  ?  83  LYS   A CD     1 
ATOM   930   C  CE     . LYS   A 1 58  ? 3.917   -16.116 30.292 1.00 21.18  ?  83  LYS   A CE     1 
ATOM   931   N  NZ     . LYS   A 1 58  ? 3.976   -14.693 30.785 1.00 22.65  ?  83  LYS   A NZ     1 
ATOM   932   H  H      . LYS   A 1 58  ? 1.216   -20.149 30.143 1.00 19.71  ?  83  LYS   A H      1 
ATOM   933   H  HA     . LYS   A 1 58  ? 1.301   -17.535 29.953 1.00 20.14  ?  83  LYS   A HA     1 
ATOM   934   H  HB2    . LYS   A 1 58  ? 3.276   -18.746 29.921 1.00 20.76  ?  83  LYS   A HB2    1 
ATOM   935   H  HB3    . LYS   A 1 58  ? 2.827   -19.482 28.587 1.00 20.76  ?  83  LYS   A HB3    1 
ATOM   936   H  HG2    . LYS   A 1 58  ? 4.456   -17.860 28.182 1.00 21.75  ?  83  LYS   A HG2    1 
ATOM   937   H  HG3    . LYS   A 1 58  ? 3.117   -17.560 27.380 1.00 21.75  ?  83  LYS   A HG3    1 
ATOM   938   H  HD2    . LYS   A 1 58  ? 4.093   -15.612 28.335 1.00 23.41  ?  83  LYS   A HD2    1 
ATOM   939   H  HD3    . LYS   A 1 58  ? 2.586   -15.835 28.788 1.00 23.41  ?  83  LYS   A HD3    1 
ATOM   940   H  HE2    . LYS   A 1 58  ? 3.278   -16.602 30.836 1.00 25.41  ?  83  LYS   A HE2    1 
ATOM   941   H  HE3    . LYS   A 1 58  ? 4.799   -16.509 30.385 1.00 25.41  ?  83  LYS   A HE3    1 
ATOM   942   H  HZ1    . LYS   A 1 58  ? 4.556   -14.226 30.297 1.00 27.18  ?  83  LYS   A HZ1    1 
ATOM   943   H  HZ2    . LYS   A 1 58  ? 3.173   -14.315 30.720 1.00 27.18  ?  83  LYS   A HZ2    1 
ATOM   944   H  HZ3    . LYS   A 1 58  ? 4.235   -14.676 31.636 1.00 27.18  ?  83  LYS   A HZ3    1 
ATOM   945   N  N      . ILE   A 1 59  ? 0.076   -19.029 27.391 1.00 17.42  ?  84  ILE   A N      1 
ATOM   946   C  CA     . ILE   A 1 59  ? -0.606  -18.669 26.143 1.00 18.02  ?  84  ILE   A CA     1 
ATOM   947   C  C      . ILE   A 1 59  ? -1.898  -17.914 26.461 1.00 18.87  ?  84  ILE   A C      1 
ATOM   948   O  O      . ILE   A 1 59  ? -2.302  -17.007 25.719 1.00 19.83  ?  84  ILE   A O      1 
ATOM   949   C  CB     . ILE   A 1 59  ? -0.865  -19.871 25.203 1.00 18.50  ?  84  ILE   A CB     1 
ATOM   950   C  CG1    . ILE   A 1 59  ? -1.699  -20.983 25.827 1.00 18.65  ?  84  ILE   A CG1    1 
ATOM   951   C  CG2    . ILE   A 1 59  ? 0.499   -20.394 24.690 1.00 19.63  ?  84  ILE   A CG2    1 
ATOM   952   C  CD1    . ILE   A 1 59  ? -2.207  -21.994 24.803 1.00 20.05  ?  84  ILE   A CD1    1 
ATOM   953   H  H      . ILE   A 1 59  ? 0.119   -19.867 27.581 1.00 20.90  ?  84  ILE   A H      1 
ATOM   954   H  HA     . ILE   A 1 59  ? 0.000   -18.092 25.652 1.00 21.62  ?  84  ILE   A HA     1 
ATOM   955   H  HB     . ILE   A 1 59  ? -1.407  -19.554 24.464 1.00 22.20  ?  84  ILE   A HB     1 
ATOM   956   H  HG12   . ILE   A 1 59  ? -1.156  -21.459 26.474 1.00 22.37  ?  84  ILE   A HG12   1 
ATOM   957   H  HG13   . ILE   A 1 59  ? -2.469  -20.589 26.267 1.00 22.37  ?  84  ILE   A HG13   1 
ATOM   958   H  HG21   . ILE   A 1 59  ? 0.344   -21.089 24.031 1.00 23.55  ?  84  ILE   A HG21   1 
ATOM   959   H  HG22   . ILE   A 1 59  ? 0.988   -19.660 24.287 1.00 23.55  ?  84  ILE   A HG22   1 
ATOM   960   H  HG23   . ILE   A 1 59  ? 1.001   -20.755 25.438 1.00 23.55  ?  84  ILE   A HG23   1 
ATOM   961   H  HD11   . ILE   A 1 59  ? -2.802  -22.620 25.245 1.00 24.05  ?  84  ILE   A HD11   1 
ATOM   962   H  HD12   . ILE   A 1 59  ? -2.685  -21.522 24.103 1.00 24.05  ?  84  ILE   A HD12   1 
ATOM   963   H  HD13   . ILE   A 1 59  ? -1.450  -22.468 24.425 1.00 24.05  ?  84  ILE   A HD13   1 
ATOM   964   N  N      . PHE   A 1 60  ? -2.553  -18.247 27.574 1.00 18.22  ?  85  PHE   A N      1 
ATOM   965   C  CA     . PHE   A 1 60  ? -3.673  -17.446 28.068 1.00 17.24  ?  85  PHE   A CA     1 
ATOM   966   C  C      . PHE   A 1 60  ? -3.228  -16.030 28.416 1.00 17.64  ?  85  PHE   A C      1 
ATOM   967   O  O      . PHE   A 1 60  ? -3.870  -15.046 28.024 1.00 18.31  ?  85  PHE   A O      1 
ATOM   968   C  CB     . PHE   A 1 60  ? -4.264  -18.168 29.278 1.00 17.93  ?  85  PHE   A CB     1 
ATOM   969   C  CG     . PHE   A 1 60  ? -5.238  -17.366 30.087 1.00 20.44  ?  85  PHE   A CG     1 
ATOM   970   C  CD1    . PHE   A 1 60  ? -6.574  -17.325 29.730 1.00 22.55  ?  85  PHE   A CD1    1 
ATOM   971   C  CD2    . PHE   A 1 60  ? -4.843  -16.705 31.243 1.00 21.86  ?  85  PHE   A CD2    1 
ATOM   972   C  CE1    . PHE   A 1 60  ? -7.489  -16.624 30.485 1.00 23.19  ?  85  PHE   A CE1    1 
ATOM   973   C  CE2    . PHE   A 1 60  ? -5.769  -15.998 32.001 1.00 21.62  ?  85  PHE   A CE2    1 
ATOM   974   C  CZ     . PHE   A 1 60  ? -7.093  -15.967 31.618 1.00 22.38  ?  85  PHE   A CZ     1 
ATOM   975   H  H      . PHE   A 1 60  ? -2.369  -18.931 28.061 1.00 21.86  ?  85  PHE   A H      1 
ATOM   976   H  HA     . PHE   A 1 60  ? -4.359  -17.360 27.388 1.00 20.68  ?  85  PHE   A HA     1 
ATOM   977   H  HB2    . PHE   A 1 60  ? -4.729  -18.959 28.965 1.00 21.51  ?  85  PHE   A HB2    1 
ATOM   978   H  HB3    . PHE   A 1 60  ? -3.537  -18.422 29.868 1.00 21.51  ?  85  PHE   A HB3    1 
ATOM   979   H  HD1    . PHE   A 1 60  ? -6.859  -17.777 28.970 1.00 27.05  ?  85  PHE   A HD1    1 
ATOM   980   H  HD2    . PHE   A 1 60  ? -3.954  -16.737 31.512 1.00 26.23  ?  85  PHE   A HD2    1 
ATOM   981   H  HE1    . PHE   A 1 60  ? -8.380  -16.596 30.222 1.00 27.82  ?  85  PHE   A HE1    1 
ATOM   982   H  HE2    . PHE   A 1 60  ? -5.495  -15.545 32.766 1.00 25.93  ?  85  PHE   A HE2    1 
ATOM   983   H  HZ     . PHE   A 1 60  ? -7.716  -15.502 32.129 1.00 26.85  ?  85  PHE   A HZ     1 
ATOM   984   N  N      . ASP   A 1 61  ? -2.122  -15.913 29.149 1.00 16.97  ?  86  ASP   A N      1 
ATOM   985   C  CA     . ASP   A 1 61  ? -1.587  -14.609 29.523 1.00 16.09  ?  86  ASP   A CA     1 
ATOM   986   C  C      . ASP   A 1 61  ? -1.315  -13.736 28.306 1.00 16.26  ?  86  ASP   A C      1 
ATOM   987   O  O      . ASP   A 1 61  ? -1.570  -12.523 28.333 1.00 16.74  ?  86  ASP   A O      1 
ATOM   988   C  CB     . ASP   A 1 61  ? -0.300  -14.815 30.331 1.00 16.72  ?  86  ASP   A CB     1 
ATOM   989   C  CG     . ASP   A 1 61  ? 0.265   -13.528 30.889 1.00 18.69  ?  86  ASP   A CG     1 
ATOM   990   O  OD1    . ASP   A 1 61  ? -0.490  -12.794 31.549 1.00 19.06  ?  86  ASP   A OD1    1 
ATOM   991   O  OD2    . ASP   A 1 61  ? 1.472   -13.261 30.704 1.00 18.62  ?  86  ASP   A OD2    1 
ATOM   992   H  H      . ASP   A 1 61  ? -1.661  -16.577 29.443 1.00 20.36  ?  86  ASP   A H      1 
ATOM   993   H  HA     . ASP   A 1 61  ? -2.238  -14.144 30.072 1.00 19.30  ?  86  ASP   A HA     1 
ATOM   994   H  HB2    . ASP   A 1 61  ? -0.487  -15.406 31.076 1.00 20.05  ?  86  ASP   A HB2    1 
ATOM   995   H  HB3    . ASP   A 1 61  ? 0.373   -15.210 29.755 1.00 20.05  ?  86  ASP   A HB3    1 
ATOM   996   N  N      . GLU   A 1 62  ? -0.781  -14.322 27.232 1.00 16.37  ?  87  GLU   A N      1 
ATOM   997   C  CA     . GLU   A 1 62  ? -0.440  -13.505 26.072 1.00 17.41  ?  87  GLU   A CA     1 
ATOM   998   C  C      . GLU   A 1 62  ? -1.676  -12.800 25.522 1.00 17.69  ?  87  GLU   A C      1 
ATOM   999   O  O      . GLU   A 1 62  ? -1.613  -11.619 25.166 1.00 19.42  ?  87  GLU   A O      1 
ATOM   1000  C  CB     . GLU   A 1 62  ? 0.222   -14.347 24.977 1.00 18.04  ?  87  GLU   A CB     1 
ATOM   1001  C  CG     . GLU   A 1 62  ? 1.631   -14.877 25.286 1.00 18.44  ?  87  GLU   A CG     1 
ATOM   1002  C  CD     . GLU   A 1 62  ? 2.740   -13.815 25.347 1.00 19.82  ?  87  GLU   A CD     1 
ATOM   1003  O  OE1    . GLU   A 1 62  ? 3.911   -14.196 25.586 1.00 22.55  ?  87  GLU   A OE1    1 
ATOM   1004  O  OE2    . GLU   A 1 62  ? 2.469   -12.605 25.162 1.00 21.58  ?  87  GLU   A OE2    1 
ATOM   1005  H  H      . GLU   A 1 62  ? -0.612  -15.162 27.153 1.00 19.63  ?  87  GLU   A H      1 
ATOM   1006  H  HA     . GLU   A 1 62  ? 0.204   -12.836 26.352 1.00 20.88  ?  87  GLU   A HA     1 
ATOM   1007  H  HB2    . GLU   A 1 62  ? -0.342  -15.118 24.807 1.00 21.64  ?  87  GLU   A HB2    1 
ATOM   1008  H  HB3    . GLU   A 1 62  ? 0.290   -13.803 24.177 1.00 21.64  ?  87  GLU   A HB3    1 
ATOM   1009  H  HG2    . GLU   A 1 62  ? 1.609   -15.320 26.149 1.00 22.12  ?  87  GLU   A HG2    1 
ATOM   1010  H  HG3    . GLU   A 1 62  ? 1.878   -15.511 24.594 1.00 22.12  ?  87  GLU   A HG3    1 
ATOM   1011  N  N      . ILE   A 1 63  ? -2.806  -13.507 25.435 1.00 19.15  ?  88  ILE   A N      1 
ATOM   1012  C  CA     . ILE   A 1 63  ? -4.019  -12.903 24.880 1.00 19.55  ?  88  ILE   A CA     1 
ATOM   1013  C  C      . ILE   A 1 63  ? -4.633  -11.911 25.868 1.00 19.72  ?  88  ILE   A C      1 
ATOM   1014  O  O      . ILE   A 1 63  ? -5.170  -10.867 25.468 1.00 21.31  ?  88  ILE   A O      1 
ATOM   1015  C  CB     . ILE   A 1 63  ? -5.029  -14.000 24.482 1.00 21.19  ?  88  ILE   A CB     1 
ATOM   1016  C  CG1    . ILE   A 1 63  ? -4.386  -14.996 23.504 1.00 22.21  ?  88  ILE   A CG1    1 
ATOM   1017  C  CG2    . ILE   A 1 63  ? -6.315  -13.386 23.876 1.00 21.73  ?  88  ILE   A CG2    1 
ATOM   1018  C  CD1    . ILE   A 1 63  ? -3.782  -14.362 22.247 1.00 23.08  ?  88  ILE   A CD1    1 
ATOM   1019  H  H      . ILE   A 1 63  ? -2.896  -14.324 25.686 1.00 22.97  ?  88  ILE   A H      1 
ATOM   1020  H  HA     . ILE   A 1 63  ? -3.773  -12.413 24.080 1.00 23.45  ?  88  ILE   A HA     1 
ATOM   1021  H  HB     . ILE   A 1 63  ? -5.281  -14.478 25.287 1.00 25.43  ?  88  ILE   A HB     1 
ATOM   1022  H  HG12   . ILE   A 1 63  ? -3.672  -15.464 23.966 1.00 26.64  ?  88  ILE   A HG12   1 
ATOM   1023  H  HG13   . ILE   A 1 63  ? -5.064  -15.627 23.216 1.00 26.64  ?  88  ILE   A HG13   1 
ATOM   1024  H  HG21   . ILE   A 1 63  ? -6.864  -14.099 23.513 1.00 26.07  ?  88  ILE   A HG21   1 
ATOM   1025  H  HG22   . ILE   A 1 63  ? -6.800  -12.918 24.573 1.00 26.07  ?  88  ILE   A HG22   1 
ATOM   1026  H  HG23   . ILE   A 1 63  ? -6.068  -12.767 23.171 1.00 26.07  ?  88  ILE   A HG23   1 
ATOM   1027  H  HD11   . ILE   A 1 63  ? -3.544  -15.065 21.622 1.00 27.69  ?  88  ILE   A HD11   1 
ATOM   1028  H  HD12   . ILE   A 1 63  ? -4.437  -13.770 21.846 1.00 27.69  ?  88  ILE   A HD12   1 
ATOM   1029  H  HD13   . ILE   A 1 63  ? -2.990  -13.859 22.495 1.00 27.69  ?  88  ILE   A HD13   1 
ATOM   1030  N  N      . LEU   A 1 64  ? -4.568  -12.211 27.170 1.00 19.11  ?  89  LEU   A N      1 
ATOM   1031  C  CA     . LEU   A 1 64  ? -5.131  -11.304 28.170 1.00 18.70  ?  89  LEU   A CA     1 
ATOM   1032  C  C      . LEU   A 1 64  ? -4.358  -9.991  28.230 1.00 18.76  ?  89  LEU   A C      1 
ATOM   1033  O  O      . LEU   A 1 64  ? -4.958  -8.913  28.294 1.00 19.96  ?  89  LEU   A O      1 
ATOM   1034  C  CB     . LEU   A 1 64  ? -5.152  -11.990 29.532 1.00 19.18  ?  89  LEU   A CB     1 
ATOM   1035  C  CG     . LEU   A 1 64  ? -5.834  -11.281 30.696 1.00 20.89  ?  89  LEU   A CG     1 
ATOM   1036  C  CD1    . LEU   A 1 64  ? -7.279  -10.984 30.388 1.00 23.71  ?  89  LEU   A CD1    1 
ATOM   1037  C  CD2    . LEU   A 1 64  ? -5.719  -12.162 31.931 1.00 22.70  ?  89  LEU   A CD2    1 
ATOM   1038  H  H      . LEU   A 1 64  ? -4.208  -12.922 27.494 1.00 22.93  ?  89  LEU   A H      1 
ATOM   1039  H  HA     . LEU   A 1 64  ? -6.046  -11.093 27.927 1.00 22.44  ?  89  LEU   A HA     1 
ATOM   1040  H  HB2    . LEU   A 1 64  ? -5.604  -12.841 29.424 1.00 23.01  ?  89  LEU   A HB2    1 
ATOM   1041  H  HB3    . LEU   A 1 64  ? -4.231  -12.136 29.799 1.00 23.01  ?  89  LEU   A HB3    1 
ATOM   1042  H  HG     . LEU   A 1 64  ? -5.402  -10.428 30.860 1.00 25.07  ?  89  LEU   A HG     1 
ATOM   1043  H  HD11   . LEU   A 1 64  ? -7.707  -10.636 31.186 1.00 28.44  ?  89  LEU   A HD11   1 
ATOM   1044  H  HD12   . LEU   A 1 64  ? -7.321  -10.325 29.677 1.00 28.44  ?  89  LEU   A HD12   1 
ATOM   1045  H  HD13   . LEU   A 1 64  ? -7.717  -11.802 30.108 1.00 28.44  ?  89  LEU   A HD13   1 
ATOM   1046  H  HD21   . LEU   A 1 64  ? -6.169  -11.727 32.673 1.00 27.24  ?  89  LEU   A HD21   1 
ATOM   1047  H  HD22   . LEU   A 1 64  ? -6.136  -13.019 31.748 1.00 27.24  ?  89  LEU   A HD22   1 
ATOM   1048  H  HD23   . LEU   A 1 64  ? -4.781  -12.290 32.142 1.00 27.24  ?  89  LEU   A HD23   1 
ATOM   1049  N  N      . VAL   A 1 65  ? -3.028  -10.054 28.193 1.00 17.95  ?  90  VAL   A N      1 
ATOM   1050  C  CA     . VAL   A 1 65  ? -2.239  -8.823  28.173 1.00 17.97  ?  90  VAL   A CA     1 
ATOM   1051  C  C      . VAL   A 1 65  ? -2.477  -8.042  26.883 1.00 18.14  ?  90  VAL   A C      1 
ATOM   1052  O  O      . VAL   A 1 65  ? -2.511  -6.810  26.900 1.00 19.16  ?  90  VAL   A O      1 
ATOM   1053  C  CB     . VAL   A 1 65  ? -0.748  -9.141  28.377 1.00 17.67  ?  90  VAL   A CB     1 
ATOM   1054  C  CG1    . VAL   A 1 65  ? 0.149   -7.893  28.188 1.00 19.19  ?  90  VAL   A CG1    1 
ATOM   1055  C  CG2    . VAL   A 1 65  ? -0.526  -9.695  29.781 1.00 17.44  ?  90  VAL   A CG2    1 
ATOM   1056  H  H      . VAL   A 1 65  ? -2.567  -10.780 28.178 1.00 21.54  ?  90  VAL   A H      1 
ATOM   1057  H  HA     . VAL   A 1 65  ? -2.531  -8.266  28.911 1.00 21.55  ?  90  VAL   A HA     1 
ATOM   1058  H  HB     . VAL   A 1 65  ? -0.495  -9.796  27.707 1.00 21.20  ?  90  VAL   A HB     1 
ATOM   1059  H  HG11   . VAL   A 1 65  ? 1.041   -8.093  28.514 1.00 23.02  ?  90  VAL   A HG11   1 
ATOM   1060  H  HG12   . VAL   A 1 65  ? 0.184   -7.668  27.245 1.00 23.02  ?  90  VAL   A HG12   1 
ATOM   1061  H  HG13   . VAL   A 1 65  ? -0.228  -7.154  28.691 1.00 23.02  ?  90  VAL   A HG13   1 
ATOM   1062  H  HG21   . VAL   A 1 65  ? 0.417   -9.887  29.900 1.00 20.92  ?  90  VAL   A HG21   1 
ATOM   1063  H  HG22   . VAL   A 1 65  ? -0.814  -9.035  30.430 1.00 20.92  ?  90  VAL   A HG22   1 
ATOM   1064  H  HG23   . VAL   A 1 65  ? -1.045  -10.509 29.885 1.00 20.92  ?  90  VAL   A HG23   1 
ATOM   1065  N  N      . ASN   A 1 66  ? -2.639  -8.733  25.747 1.00 19.39  ?  91  ASN   A N      1 
ATOM   1066  C  CA     . ASN   A 1 66  ? -2.963  -8.026  24.507 1.00 21.04  ?  91  ASN   A CA     1 
ATOM   1067  C  C      . ASN   A 1 66  ? -4.242  -7.207  24.646 1.00 22.00  ?  91  ASN   A C      1 
ATOM   1068  O  O      . ASN   A 1 66  ? -4.358  -6.116  24.070 1.00 22.90  ?  91  ASN   A O      1 
ATOM   1069  C  CB     . ASN   A 1 66  ? -3.129  -9.000  23.339 1.00 21.83  ?  91  ASN   A CB     1 
ATOM   1070  C  CG     . ASN   A 1 66  ? -1.808  -9.448  22.736 1.00 21.13  ?  91  ASN   A CG     1 
ATOM   1071  O  OD1    . ASN   A 1 66  ? -0.752  -8.867  22.997 1.00 19.48  ?  91  ASN   A OD1    1 
ATOM   1072  N  ND2    . ASN   A 1 66  ? -1.874  -10.465 21.885 1.00 21.36  ?  91  ASN   A ND2    1 
ATOM   1073  H  H      . ASN   A 1 66  ? -2.569  -9.587  25.672 1.00 23.27  ?  91  ASN   A H      1 
ATOM   1074  H  HA     . ASN   A 1 66  ? -2.218  -7.435  24.313 1.00 25.24  ?  91  ASN   A HA     1 
ATOM   1075  H  HB2    . ASN   A 1 66  ? -3.596  -9.791  23.653 1.00 26.19  ?  91  ASN   A HB2    1 
ATOM   1076  H  HB3    . ASN   A 1 66  ? -3.643  -8.567  22.640 1.00 26.19  ?  91  ASN   A HB3    1 
ATOM   1077  H  HD21   . ASN   A 1 66  ? -1.158  -10.761 21.512 1.00 25.63  ?  91  ASN   A HD21   1 
ATOM   1078  H  HD22   . ASN   A 1 66  ? -2.633  -10.828 21.706 1.00 25.63  ?  91  ASN   A HD22   1 
ATOM   1079  N  N      . ALA   A 1 67  ? -5.232  -7.733  25.373 1.00 21.02  ?  92  ALA   A N      1 
ATOM   1080  C  CA     . ALA   A 1 67  ? -6.471  -6.989  25.580 1.00 22.98  ?  92  ALA   A CA     1 
ATOM   1081  C  C      . ALA   A 1 67  ? -6.232  -5.762  26.452 1.00 21.68  ?  92  ALA   A C      1 
ATOM   1082  O  O      . ALA   A 1 67  ? -6.719  -4.666  26.145 1.00 22.88  ?  92  ALA   A O      1 
ATOM   1083  C  CB     . ALA   A 1 67  ? -7.524  -7.898  26.211 1.00 23.23  ?  92  ALA   A CB     1 
ATOM   1084  H  H      . ALA   A 1 67  ? -5.210  -8.506  25.750 1.00 25.22  ?  92  ALA   A H      1 
ATOM   1085  H  HA     . ALA   A 1 67  ? -6.809  -6.690  24.721 1.00 27.57  ?  92  ALA   A HA     1 
ATOM   1086  H  HB1    . ALA   A 1 67  ? -8.341  -7.392  26.341 1.00 27.87  ?  92  ALA   A HB1    1 
ATOM   1087  H  HB2    . ALA   A 1 67  ? -7.691  -8.647  25.617 1.00 27.87  ?  92  ALA   A HB2    1 
ATOM   1088  H  HB3    . ALA   A 1 67  ? -7.194  -8.219  27.064 1.00 27.87  ?  92  ALA   A HB3    1 
ATOM   1089  N  N      . ALA   A 1 68  ? -5.476  -5.925  27.540 1.00 20.69  ?  93  ALA   A N      1 
ATOM   1090  C  CA     . ALA   A 1 68  ? -5.138  -4.786  28.385 1.00 20.61  ?  93  ALA   A CA     1 
ATOM   1091  C  C      . ALA   A 1 68  ? -4.348  -3.737  27.611 1.00 21.90  ?  93  ALA   A C      1 
ATOM   1092  O  O      . ALA   A 1 68  ? -4.514  -2.534  27.843 1.00 22.23  ?  93  ALA   A O      1 
ATOM   1093  C  CB     . ALA   A 1 68  ? -4.348  -5.261  29.609 1.00 20.05  ?  93  ALA   A CB     1 
ATOM   1094  H  H      . ALA   A 1 68  ? -5.151  -6.676  27.806 1.00 24.83  ?  93  ALA   A H      1 
ATOM   1095  H  HA     . ALA   A 1 68  ? -5.958  -4.372  28.696 1.00 24.73  ?  93  ALA   A HA     1 
ATOM   1096  H  HB1    . ALA   A 1 68  ? -4.116  -4.492  30.153 1.00 24.05  ?  93  ALA   A HB1    1 
ATOM   1097  H  HB2    . ALA   A 1 68  ? -4.897  -5.875  30.121 1.00 24.05  ?  93  ALA   A HB2    1 
ATOM   1098  H  HB3    . ALA   A 1 68  ? -3.541  -5.709  29.309 1.00 24.05  ?  93  ALA   A HB3    1 
ATOM   1099  N  N      . ASP   A 1 69  ? -3.470  -4.180  26.697 1.00 22.22  ?  94  ASP   A N      1 
ATOM   1100  C  CA     . ASP   A 1 69  ? -2.702  -3.254  25.869 1.00 21.88  ?  94  ASP   A CA     1 
ATOM   1101  C  C      . ASP   A 1 69  ? -3.608  -2.339  25.053 1.00 22.72  ?  94  ASP   A C      1 
ATOM   1102  O  O      . ASP   A 1 69  ? -3.231  -1.203  24.741 1.00 22.99  ?  94  ASP   A O      1 
ATOM   1103  C  CB     . ASP   A 1 69  ? -1.786  -4.021  24.899 1.00 21.99  ?  94  ASP   A CB     1 
ATOM   1104  C  CG     . ASP   A 1 69  ? -0.582  -4.651  25.572 1.00 23.09  ?  94  ASP   A CG     1 
ATOM   1105  O  OD1    . ASP   A 1 69  ? -0.294  -4.295  26.734 1.00 23.78  ?  94  ASP   A OD1    1 
ATOM   1106  O  OD2    . ASP   A 1 69  ? 0.081   -5.507  24.926 1.00 24.04  ?  94  ASP   A OD2    1 
ATOM   1107  H  H      . ASP   A 1 69  ? -3.304  -5.009  26.541 1.00 26.65  ?  94  ASP   A H      1 
ATOM   1108  H  HA     . ASP   A 1 69  ? -2.155  -2.717  26.463 1.00 26.25  ?  94  ASP   A HA     1 
ATOM   1109  H  HB2    . ASP   A 1 69  ? -2.298  -4.732  24.482 1.00 26.38  ?  94  ASP   A HB2    1 
ATOM   1110  H  HB3    . ASP   A 1 69  ? -1.460  -3.406  24.224 1.00 26.38  ?  94  ASP   A HB3    1 
ATOM   1111  N  N      . ASN   A 1 70  ? -4.785  -2.817  24.657 1.00 22.74  ?  95  ASN   A N      1 
ATOM   1112  C  CA     . ASN   A 1 70  ? -5.616  -1.966  23.819 1.00 25.08  ?  95  ASN   A CA     1 
ATOM   1113  C  C      . ASN   A 1 70  ? -6.139  -0.747  24.569 1.00 24.93  ?  95  ASN   A C      1 
ATOM   1114  O  O      . ASN   A 1 70  ? -6.577  0.218   23.929 1.00 25.60  ?  95  ASN   A O      1 
ATOM   1115  C  CB     . ASN   A 1 70  ? -6.805  -2.727  23.238 1.00 26.46  ?  95  ASN   A CB     1 
ATOM   1116  C  CG     . ASN   A 1 70  ? -7.316  -2.090  21.951 1.00 28.23  ?  95  ASN   A CG     1 
ATOM   1117  O  OD1    . ASN   A 1 70  ? -6.543  -1.861  21.014 1.00 28.65  ?  95  ASN   A OD1    1 
ATOM   1118  N  ND2    . ASN   A 1 70  ? -8.609  -1.781  21.902 1.00 28.51  ?  95  ASN   A ND2    1 
ATOM   1119  H  H      . ASN   A 1 70  ? -5.107  -3.591  24.852 1.00 27.28  ?  95  ASN   A H      1 
ATOM   1120  H  HA     . ASN   A 1 70  ? -5.064  -1.674  23.077 1.00 30.08  ?  95  ASN   A HA     1 
ATOM   1121  H  HB2    . ASN   A 1 70  ? -6.534  -3.637  23.039 1.00 31.74  ?  95  ASN   A HB2    1 
ATOM   1122  H  HB3    . ASN   A 1 70  ? -7.529  -2.730  23.883 1.00 31.74  ?  95  ASN   A HB3    1 
ATOM   1123  H  HD21   . ASN   A 1 70  ? -8.938  -1.419  21.195 1.00 34.20  ?  95  ASN   A HD21   1 
ATOM   1124  H  HD22   . ASN   A 1 70  ? -9.116  -1.942  22.578 1.00 34.20  ?  95  ASN   A HD22   1 
ATOM   1125  N  N      . LYS   A 1 71  ? -6.142  -0.773  25.904 1.00 24.76  ?  96  LYS   A N      1 
ATOM   1126  C  CA     . LYS   A 1 71  ? -6.572  0.403   26.656 1.00 24.82  ?  96  LYS   A CA     1 
ATOM   1127  C  C      . LYS   A 1 71  ? -5.566  1.539   26.517 1.00 24.63  ?  96  LYS   A C      1 
ATOM   1128  O  O      . LYS   A 1 71  ? -5.951  2.712   26.556 1.00 26.35  ?  96  LYS   A O      1 
ATOM   1129  C  CB     . LYS   A 1 71  ? -6.783  0.038   28.130 1.00 24.74  ?  96  LYS   A CB     1 
ATOM   1130  C  CG     . LYS   A 1 71  ? -7.120  1.226   29.038 1.00 24.09  ?  96  LYS   A CG     1 
ATOM   1131  C  CD     . LYS   A 1 71  ? -8.517  1.809   28.785 1.00 25.21  ?  96  LYS   A CD     1 
ATOM   1132  C  CE     . LYS   A 1 71  ? -8.778  2.937   29.772 1.00 26.38  ?  96  LYS   A CE     1 
ATOM   1133  N  NZ     . LYS   A 1 71  ? -10.178 3.425   29.754 1.00 28.19  ?  96  LYS   A NZ     1 
ATOM   1134  H  H      . LYS   A 1 71  ? -5.904  -1.444  26.387 1.00 29.71  ?  96  LYS   A H      1 
ATOM   1135  H  HA     . LYS   A 1 71  ? -7.424  0.711   26.308 1.00 29.77  ?  96  LYS   A HA     1 
ATOM   1136  H  HB2    . LYS   A 1 71  ? -7.516  -0.594  28.190 1.00 29.68  ?  96  LYS   A HB2    1 
ATOM   1137  H  HB3    . LYS   A 1 71  ? -5.968  -0.366  28.467 1.00 29.68  ?  96  LYS   A HB3    1 
ATOM   1138  H  HG2    . LYS   A 1 71  ? -7.084  0.935   29.963 1.00 28.90  ?  96  LYS   A HG2    1 
ATOM   1139  H  HG3    . LYS   A 1 71  ? -6.472  1.931   28.887 1.00 28.90  ?  96  LYS   A HG3    1 
ATOM   1140  H  HD2    . LYS   A 1 71  ? -8.568  2.163   27.883 1.00 30.25  ?  96  LYS   A HD2    1 
ATOM   1141  H  HD3    . LYS   A 1 71  ? -9.189  1.121   28.909 1.00 30.25  ?  96  LYS   A HD3    1 
ATOM   1142  H  HE2    . LYS   A 1 71  ? -8.585  2.619   30.668 1.00 31.65  ?  96  LYS   A HE2    1 
ATOM   1143  H  HE3    . LYS   A 1 71  ? -8.199  3.684   29.554 1.00 31.65  ?  96  LYS   A HE3    1 
ATOM   1144  H  HZ1    . LYS   A 1 71  ? -10.277 4.089   30.338 1.00 33.82  ?  96  LYS   A HZ1    1 
ATOM   1145  H  HZ2    . LYS   A 1 71  ? -10.386 3.722   28.941 1.00 33.82  ?  96  LYS   A HZ2    1 
ATOM   1146  H  HZ3    . LYS   A 1 71  ? -10.734 2.765   29.971 1.00 33.82  ?  96  LYS   A HZ3    1 
ATOM   1147  N  N      . GLN   A 1 72  ? -4.278  1.220   26.358 1.00 24.43  ?  97  GLN   A N      1 
ATOM   1148  C  CA     . GLN   A 1 72  ? -3.303  2.264   26.066 1.00 25.19  ?  97  GLN   A CA     1 
ATOM   1149  C  C      . GLN   A 1 72  ? -3.483  2.776   24.640 1.00 27.37  ?  97  GLN   A C      1 
ATOM   1150  O  O      . GLN   A 1 72  ? -3.412  3.985   24.387 1.00 30.18  ?  97  GLN   A O      1 
ATOM   1151  C  CB     . GLN   A 1 72  ? -1.885  1.735   26.277 1.00 25.22  ?  97  GLN   A CB     1 
ATOM   1152  C  CG     . GLN   A 1 72  ? -1.632  1.117   27.640 1.00 25.23  ?  97  GLN   A CG     1 
ATOM   1153  C  CD     . GLN   A 1 72  ? -1.828  2.097   28.777 1.00 26.93  ?  97  GLN   A CD     1 
ATOM   1154  O  OE1    . GLN   A 1 72  ? -1.525  3.281   28.653 1.00 27.59  ?  97  GLN   A OE1    1 
ATOM   1155  N  NE2    . GLN   A 1 72  ? -2.334  1.605   29.897 1.00 29.66  ?  97  GLN   A NE2    1 
ATOM   1156  H  H      . GLN   A 1 72  ? -3.954  0.425   26.414 1.00 29.31  ?  97  GLN   A H      1 
ATOM   1157  H  HA     . GLN   A 1 72  ? -3.432  3.005   26.678 1.00 30.22  ?  97  GLN   A HA     1 
ATOM   1158  H  HB2    . GLN   A 1 72  ? -1.708  1.053   25.610 1.00 30.26  ?  97  GLN   A HB2    1 
ATOM   1159  H  HB3    . GLN   A 1 72  ? -1.262  2.472   26.171 1.00 30.26  ?  97  GLN   A HB3    1 
ATOM   1160  H  HG2    . GLN   A 1 72  ? -2.249  0.380   27.771 1.00 30.27  ?  97  GLN   A HG2    1 
ATOM   1161  H  HG3    . GLN   A 1 72  ? -0.718  0.795   27.677 1.00 30.27  ?  97  GLN   A HG3    1 
ATOM   1162  H  HE21   . GLN   A 1 72  ? -2.532  0.770   29.949 1.00 35.58  ?  97  GLN   A HE21   1 
ATOM   1163  H  HE22   . GLN   A 1 72  ? -2.464  2.121   30.572 1.00 35.58  ?  97  GLN   A HE22   1 
ATOM   1164  N  N      . ARG   A 1 73  ? -3.736  1.871   23.697 1.00 27.47  ?  98  ARG   A N      1 
ATOM   1165  C  CA     . ARG   A 1 73  ? -3.964  2.279   22.315 1.00 29.01  ?  98  ARG   A CA     1 
ATOM   1166  C  C      . ARG   A 1 73  ? -5.206  3.150   22.190 1.00 30.97  ?  98  ARG   A C      1 
ATOM   1167  O  O      . ARG   A 1 73  ? -5.196  4.156   21.463 1.00 32.21  ?  98  ARG   A O      1 
ATOM   1168  C  CB     . ARG   A 1 73  ? -4.079  1.037   21.435 1.00 29.80  ?  98  ARG   A CB     1 
ATOM   1169  C  CG     . ARG   A 1 73  ? -4.529  1.306   20.016 1.00 32.08  ?  98  ARG   A CG     1 
ATOM   1170  C  CD     . ARG   A 1 73  ? -4.315  0.076   19.147 1.00 32.49  ?  98  ARG   A CD     1 
ATOM   1171  N  NE     . ARG   A 1 73  ? -4.853  0.230   17.800 1.00 33.60  ?  98  ARG   A NE     1 
ATOM   1172  C  CZ     . ARG   A 1 73  ? -6.015  -0.278  17.393 1.00 34.25  ?  98  ARG   A CZ     1 
ATOM   1173  N  NH1    . ARG   A 1 73  ? -6.781  -0.968  18.229 1.00 33.79  ?  98  ARG   A NH1    1 
ATOM   1174  N  NH2    . ARG   A 1 73  ? -6.405  -0.097  16.140 1.00 35.93  ?  98  ARG   A NH2    1 
ATOM   1175  H  H      . ARG   A 1 73  ? -3.780  1.022   23.830 1.00 32.96  ?  98  ARG   A H      1 
ATOM   1176  H  HA     . ARG   A 1 73  ? -3.209  2.805   22.008 1.00 34.81  ?  98  ARG   A HA     1 
ATOM   1177  H  HB2    . ARG   A 1 73  ? -3.209  0.610   21.389 1.00 35.76  ?  98  ARG   A HB2    1 
ATOM   1178  H  HB3    . ARG   A 1 73  ? -4.724  0.434   21.836 1.00 35.76  ?  98  ARG   A HB3    1 
ATOM   1179  H  HG2    . ARG   A 1 73  ? -5.474  1.528   20.011 1.00 38.49  ?  98  ARG   A HG2    1 
ATOM   1180  H  HG3    . ARG   A 1 73  ? -4.014  2.040   19.645 1.00 38.49  ?  98  ARG   A HG3    1 
ATOM   1181  H  HD2    . ARG   A 1 73  ? -3.364  -0.095  19.072 1.00 38.98  ?  98  ARG   A HD2    1 
ATOM   1182  H  HD3    . ARG   A 1 73  ? -4.757  -0.682  19.561 1.00 38.98  ?  98  ARG   A HD3    1 
ATOM   1183  H  HE     . ARG   A 1 73  ? -4.389  0.677   17.231 1.00 40.31  ?  98  ARG   A HE     1 
ATOM   1184  H  HH11   . ARG   A 1 73  ? -6.529  -1.091  19.042 1.00 40.54  ?  98  ARG   A HH11   1 
ATOM   1185  H  HH12   . ARG   A 1 73  ? -7.530  -1.292  17.958 1.00 40.54  ?  98  ARG   A HH12   1 
ATOM   1186  H  HH21   . ARG   A 1 73  ? -5.908  0.345   15.595 1.00 43.11  ?  98  ARG   A HH21   1 
ATOM   1187  H  HH22   . ARG   A 1 73  ? -7.154  -0.423  15.871 1.00 43.11  ?  98  ARG   A HH22   1 
ATOM   1188  N  N      . ASP   A 1 74  ? -6.280  2.785   22.888 1.00 30.31  ?  99  ASP   A N      1 
ATOM   1189  C  CA     . ASP   A 1 74  ? -7.545  3.513   22.818 1.00 30.84  ?  99  ASP   A CA     1 
ATOM   1190  C  C      . ASP   A 1 74  ? -8.142  3.701   24.204 1.00 30.34  ?  99  ASP   A C      1 
ATOM   1191  O  O      . ASP   A 1 74  ? -8.810  2.795   24.730 1.00 28.67  ?  99  ASP   A O      1 
ATOM   1192  C  CB     . ASP   A 1 74  ? -8.548  2.791   21.921 1.00 32.05  ?  99  ASP   A CB     1 
ATOM   1193  C  CG     . ASP   A 1 74  ? -9.830  3.579   21.739 1.00 34.48  ?  99  ASP   A CG     1 
ATOM   1194  O  OD1    . ASP   A 1 74  ? -9.891  4.743   22.202 1.00 35.37  ?  99  ASP   A OD1    1 
ATOM   1195  O  OD2    . ASP   A 1 74  ? -10.769 3.042   21.120 1.00 36.37  ?  99  ASP   A OD2    1 
ATOM   1196  H  H      . ASP   A 1 74  ? -6.301  2.108   23.418 1.00 36.37  ?  99  ASP   A H      1 
ATOM   1197  H  HA     . ASP   A 1 74  ? -7.351  4.393   22.460 1.00 37.01  ?  99  ASP   A HA     1 
ATOM   1198  H  HB2    . ASP   A 1 74  ? -8.151  2.655   21.046 1.00 38.45  ?  99  ASP   A HB2    1 
ATOM   1199  H  HB3    . ASP   A 1 74  ? -8.773  1.936   22.319 1.00 38.45  ?  99  ASP   A HB3    1 
ATOM   1200  N  N      . PRO   A 1 75  ? -7.958  4.880   24.811 1.00 31.21  ?  100 PRO   A N      1 
ATOM   1201  C  CA     . PRO   A 1 75  ? -8.511  5.118   26.158 1.00 32.55  ?  100 PRO   A CA     1 
ATOM   1202  C  C      . PRO   A 1 75  ? -10.031 5.034   26.229 1.00 32.28  ?  100 PRO   A C      1 
ATOM   1203  O  O      . PRO   A 1 75  ? -10.569 4.901   27.336 1.00 32.56  ?  100 PRO   A O      1 
ATOM   1204  C  CB     . PRO   A 1 75  ? -8.008  6.533   26.501 1.00 34.15  ?  100 PRO   A CB     1 
ATOM   1205  C  CG     . PRO   A 1 75  ? -6.737  6.661   25.703 1.00 35.42  ?  100 PRO   A CG     1 
ATOM   1206  C  CD     . PRO   A 1 75  ? -7.026  5.949   24.400 1.00 34.28  ?  100 PRO   A CD     1 
ATOM   1207  H  HA     . PRO   A 1 75  ? -8.133  4.484   26.788 1.00 39.06  ?  100 PRO   A HA     1 
ATOM   1208  H  HB2    . PRO   A 1 75  ? -8.662  7.196   26.231 1.00 40.98  ?  100 PRO   A HB2    1 
ATOM   1209  H  HB3    . PRO   A 1 75  ? -7.835  6.607   27.453 1.00 40.98  ?  100 PRO   A HB3    1 
ATOM   1210  H  HG2    . PRO   A 1 75  ? -6.535  7.597   25.550 1.00 42.50  ?  100 PRO   A HG2    1 
ATOM   1211  H  HG3    . PRO   A 1 75  ? -6.005  6.236   26.176 1.00 42.50  ?  100 PRO   A HG3    1 
ATOM   1212  H  HD2    . PRO   A 1 75  ? -7.445  6.548   23.762 1.00 41.13  ?  100 PRO   A HD2    1 
ATOM   1213  H  HD3    . PRO   A 1 75  ? -6.215  5.576   24.021 1.00 41.13  ?  100 PRO   A HD3    1 
ATOM   1214  N  N      . LYS   A 1 76  ? -10.737 5.073   25.099 1.00 32.91  ?  101 LYS   A N      1 
ATOM   1215  C  CA     . LYS   A 1 76  ? -12.182 4.873   25.132 1.00 34.56  ?  101 LYS   A CA     1 
ATOM   1216  C  C      . LYS   A 1 76  ? -12.562 3.457   25.555 1.00 34.19  ?  101 LYS   A C      1 
ATOM   1217  O  O      . LYS   A 1 76  ? -13.702 3.241   25.978 1.00 36.18  ?  101 LYS   A O      1 
ATOM   1218  C  CB     . LYS   A 1 76  ? -12.790 5.200   23.762 1.00 37.18  ?  101 LYS   A CB     1 
ATOM   1219  C  CG     . LYS   A 1 76  ? -12.675 6.680   23.365 1.00 39.32  ?  101 LYS   A CG     1 
ATOM   1220  C  CD     . LYS   A 1 76  ? -13.236 6.989   21.963 1.00 42.12  ?  101 LYS   A CD     1 
ATOM   1221  C  CE     . LYS   A 1 76  ? -13.112 8.496   21.665 1.00 44.84  ?  101 LYS   A CE     1 
ATOM   1222  N  NZ     . LYS   A 1 76  ? -13.817 8.949   20.418 1.00 46.05  ?  101 LYS   A NZ     1 
ATOM   1223  H  H      . LYS   A 1 76  ? -10.408 5.210   24.317 1.00 39.48  ?  101 LYS   A H      1 
ATOM   1224  H  HA     . LYS   A 1 76  ? -12.566 5.485   25.778 1.00 41.47  ?  101 LYS   A HA     1 
ATOM   1225  H  HB2    . LYS   A 1 76  ? -12.332 4.677   23.086 1.00 44.61  ?  101 LYS   A HB2    1 
ATOM   1226  H  HB3    . LYS   A 1 76  ? -13.732 4.971   23.777 1.00 44.61  ?  101 LYS   A HB3    1 
ATOM   1227  H  HG2    . LYS   A 1 76  ? -13.169 7.215   24.005 1.00 47.17  ?  101 LYS   A HG2    1 
ATOM   1228  H  HG3    . LYS   A 1 76  ? -11.739 6.934   23.372 1.00 47.17  ?  101 LYS   A HG3    1 
ATOM   1229  H  HD2    . LYS   A 1 76  ? -12.733 6.498   21.294 1.00 50.54  ?  101 LYS   A HD2    1 
ATOM   1230  H  HD3    . LYS   A 1 76  ? -14.172 6.740   21.923 1.00 50.54  ?  101 LYS   A HD3    1 
ATOM   1231  H  HE2    . LYS   A 1 76  ? -13.491 8.990   22.409 1.00 53.80  ?  101 LYS   A HE2    1 
ATOM   1232  H  HE3    . LYS   A 1 76  ? -12.173 8.715   21.565 1.00 53.80  ?  101 LYS   A HE3    1 
ATOM   1233  H  HZ1    . LYS   A 1 76  ? -13.700 9.823   20.303 1.00 55.26  ?  101 LYS   A HZ1    1 
ATOM   1234  H  HZ2    . LYS   A 1 76  ? -13.491 8.518   19.711 1.00 55.26  ?  101 LYS   A HZ2    1 
ATOM   1235  H  HZ3    . LYS   A 1 76  ? -14.688 8.780   20.482 1.00 55.26  ?  101 LYS   A HZ3    1 
ATOM   1236  N  N      . MET   A 1 77  ? -11.642 2.497   25.465 1.00 31.55  ?  102 MET   A N      1 
ATOM   1237  C  CA     . MET   A 1 77  ? -11.940 1.132   25.885 1.00 30.33  ?  102 MET   A CA     1 
ATOM   1238  C  C      . MET   A 1 77  ? -12.423 1.119   27.329 1.00 30.99  ?  102 MET   A C      1 
ATOM   1239  O  O      . MET   A 1 77  ? -11.902 1.854   28.172 1.00 29.66  ?  102 MET   A O      1 
ATOM   1240  C  CB     . MET   A 1 77  ? -10.694 0.260   25.750 1.00 27.62  ?  102 MET   A CB     1 
ATOM   1241  C  CG     . MET   A 1 77  ? -10.872 -1.159  26.251 1.00 27.55  ?  102 MET   A CG     1 
ATOM   1242  S  SD     . MET   A 1 77  ? -9.360  -2.101  26.022 1.00 28.78  ?  102 MET   A SD     1 
ATOM   1243  C  CE     . MET   A 1 77  ? -9.556  -3.312  27.332 1.00 29.40  ?  102 MET   A CE     1 
ATOM   1244  H  H      . MET   A 1 77  ? -10.843 2.610   25.167 1.00 37.86  ?  102 MET   A H      1 
ATOM   1245  H  HA     . MET   A 1 77  ? -12.631 0.766   25.311 1.00 36.39  ?  102 MET   A HA     1 
ATOM   1246  H  HB2    . MET   A 1 77  ? -10.449 0.212   24.812 1.00 33.14  ?  102 MET   A HB2    1 
ATOM   1247  H  HB3    . MET   A 1 77  ? -9.976  0.664   26.260 1.00 33.14  ?  102 MET   A HB3    1 
ATOM   1248  H  HG2    . MET   A 1 77  ? -11.087 -1.145  27.197 1.00 33.06  ?  102 MET   A HG2    1 
ATOM   1249  H  HG3    . MET   A 1 77  ? -11.584 -1.592  25.756 1.00 33.06  ?  102 MET   A HG3    1 
ATOM   1250  H  HE1    . MET   A 1 77  ? -8.789  -3.907  27.330 1.00 35.27  ?  102 MET   A HE1    1 
ATOM   1251  H  HE2    . MET   A 1 77  ? -9.613  -2.851  28.184 1.00 35.27  ?  102 MET   A HE2    1 
ATOM   1252  H  HE3    . MET   A 1 77  ? -10.368 -3.819  27.175 1.00 35.27  ?  102 MET   A HE3    1 
ATOM   1253  N  N      . SER   A 1 78  ? -13.397 0.243   27.626 1.00 31.53  ?  103 SER   A N      1 
ATOM   1254  C  CA     . SER   A 1 78  ? -13.979 0.194   28.961 1.00 32.40  ?  103 SER   A CA     1 
ATOM   1255  C  C      . SER   A 1 78  ? -14.104 -1.190  29.596 1.00 31.93  ?  103 SER   A C      1 
ATOM   1256  O  O      . SER   A 1 78  ? -14.342 -1.253  30.810 1.00 31.75  ?  103 SER   A O      1 
ATOM   1257  C  CB     . SER   A 1 78  ? -15.378 0.847   28.954 1.00 33.23  ?  103 SER   A CB     1 
ATOM   1258  O  OG     . SER   A 1 78  ? -16.295 0.150   28.125 1.00 35.13  ?  103 SER   A OG     1 
ATOM   1259  H  H      . SER   A 1 78  ? -13.728 -0.325  27.072 1.00 37.84  ?  103 SER   A H      1 
ATOM   1260  H  HA     . SER   A 1 78  ? -13.392 0.704   29.540 1.00 38.87  ?  103 SER   A HA     1 
ATOM   1261  H  HB2    . SER   A 1 78  ? -15.722 0.852   29.861 1.00 39.87  ?  103 SER   A HB2    1 
ATOM   1262  H  HB3    . SER   A 1 78  ? -15.293 1.756   28.627 1.00 39.87  ?  103 SER   A HB3    1 
ATOM   1263  H  HG     . SER   A 1 78  ? -16.416 -0.627  28.421 1.00 42.15  ?  103 SER   A HG     1 
ATOM   1264  N  N      . CYS   A 1 79  ? -13.936 -2.286  28.847 1.00 31.62  ?  104 CYS   A N      1 
ATOM   1265  C  CA     . CYS   A 1 79  ? -14.256 -3.611  29.368 1.00 31.38  ?  104 CYS   A CA     1 
ATOM   1266  C  C      . CYS   A 1 79  ? -13.400 -4.703  28.737 1.00 29.25  ?  104 CYS   A C      1 
ATOM   1267  O  O      . CYS   A 1 79  ? -13.084 -4.645  27.544 1.00 28.81  ?  104 CYS   A O      1 
ATOM   1268  C  CB     . CYS   A 1 79  ? -15.741 -3.971  29.132 1.00 35.00  ?  104 CYS   A CB     1 
ATOM   1269  S  SG     . CYS   A 1 79  ? -16.985 -2.939  29.936 1.00 40.46  ?  104 CYS   A SG     1 
ATOM   1270  H  H      . CYS   A 1 79  ? -13.640 -2.284  28.040 1.00 37.93  ?  104 CYS   A H      1 
ATOM   1271  H  HA     . CYS   A 1 79  ? -14.052 -3.589  30.317 1.00 37.65  ?  104 CYS   A HA     1 
ATOM   1272  H  HB2    . CYS   A 1 79  ? -15.910 -3.923  28.178 1.00 41.99  ?  104 CYS   A HB2    1 
ATOM   1273  H  HB3    . CYS   A 1 79  ? -15.881 -4.877  29.449 1.00 41.99  ?  104 CYS   A HB3    1 
ATOM   1274  H  HG     . CYS   A 1 79  ? -16.850 -3.020  31.126 1.00 48.55  ?  104 CYS   A HG     1 
ATOM   1275  N  N      . ILE   A 1 80  ? -13.047 -5.694  29.558 1.00 26.48  ?  105 ILE   A N      1 
ATOM   1276  C  CA     . ILE   A 1 80  ? -12.485 -6.971  29.134 1.00 25.58  ?  105 ILE   A CA     1 
ATOM   1277  C  C      . ILE   A 1 80  ? -13.408 -8.059  29.659 1.00 26.38  ?  105 ILE   A C      1 
ATOM   1278  O  O      . ILE   A 1 80  ? -13.771 -8.045  30.843 1.00 27.37  ?  105 ILE   A O      1 
ATOM   1279  C  CB     . ILE   A 1 80  ? -11.054 -7.176  29.663 1.00 23.84  ?  105 ILE   A CB     1 
ATOM   1280  C  CG1    . ILE   A 1 80  ? -10.126 -6.140  29.033 1.00 24.50  ?  105 ILE   A CG1    1 
ATOM   1281  C  CG2    . ILE   A 1 80  ? -10.568 -8.603  29.383 1.00 24.23  ?  105 ILE   A CG2    1 
ATOM   1282  C  CD1    . ILE   A 1 80  ? -8.742  -6.117  29.636 1.00 24.35  ?  105 ILE   A CD1    1 
ATOM   1283  H  H      . ILE   A 1 80  ? -13.129 -5.644  30.413 1.00 31.77  ?  105 ILE   A H      1 
ATOM   1284  H  HA     . ILE   A 1 80  ? -12.454 -7.011  28.165 1.00 30.69  ?  105 ILE   A HA     1 
ATOM   1285  H  HB     . ILE   A 1 80  ? -11.052 -7.052  30.625 1.00 28.61  ?  105 ILE   A HB     1 
ATOM   1286  H  HG12   . ILE   A 1 80  ? -10.034 -6.338  28.088 1.00 29.39  ?  105 ILE   A HG12   1 
ATOM   1287  H  HG13   . ILE   A 1 80  ? -10.516 -5.260  29.151 1.00 29.39  ?  105 ILE   A HG13   1 
ATOM   1288  H  HG21   . ILE   A 1 80  ? -9.613  -8.650  29.549 1.00 29.08  ?  105 ILE   A HG21   1 
ATOM   1289  H  HG22   . ILE   A 1 80  ? -11.036 -9.217  29.971 1.00 29.08  ?  105 ILE   A HG22   1 
ATOM   1290  H  HG23   . ILE   A 1 80  ? -10.754 -8.825  28.458 1.00 29.08  ?  105 ILE   A HG23   1 
ATOM   1291  H  HD11   . ILE   A 1 80  ? -8.289  -5.307  29.354 1.00 29.21  ?  105 ILE   A HD11   1 
ATOM   1292  H  HD12   . ILE   A 1 80  ? -8.819  -6.133  30.603 1.00 29.21  ?  105 ILE   A HD12   1 
ATOM   1293  H  HD13   . ILE   A 1 80  ? -8.251  -6.895  29.329 1.00 29.21  ?  105 ILE   A HD13   1 
ATOM   1294  N  N      . ARG   A 1 81  ? -13.785 -8.997  28.791 1.00 27.11  ?  106 ARG   A N      1 
ATOM   1295  C  CA     . ARG   A 1 81  ? -14.651 -10.114 29.157 1.00 26.98  ?  106 ARG   A CA     1 
ATOM   1296  C  C      . ARG   A 1 81  ? -13.908 -11.416 28.897 1.00 27.76  ?  106 ARG   A C      1 
ATOM   1297  O  O      . ARG   A 1 81  ? -13.490 -11.685 27.764 1.00 28.34  ?  106 ARG   A O      1 
ATOM   1298  C  CB     . ARG   A 1 81  ? -15.968 -10.072 28.378 1.00 28.44  ?  106 ARG   A CB     1 
ATOM   1299  C  CG     . ARG   A 1 81  ? -16.847 -8.881  28.766 1.00 30.23  ?  106 ARG   A CG     1 
ATOM   1300  C  CD     . ARG   A 1 81  ? -18.203 -8.864  28.046 1.00 33.08  ?  106 ARG   A CD     1 
ATOM   1301  N  NE     . ARG   A 1 81  ? -19.122 -7.912  28.666 1.00 35.53  ?  106 ARG   A NE     1 
ATOM   1302  C  CZ     . ARG   A 1 81  ? -19.963 -8.210  29.654 1.00 36.35  ?  106 ARG   A CZ     1 
ATOM   1303  N  NH1    . ARG   A 1 81  ? -20.023 -9.444  30.134 1.00 37.52  ?  106 ARG   A NH1    1 
ATOM   1304  N  NH2    . ARG   A 1 81  ? -20.755 -7.271  30.159 1.00 37.48  ?  106 ARG   A NH2    1 
ATOM   1305  H  H      . ARG   A 1 81  ? -13.546 -9.007  27.965 1.00 32.52  ?  106 ARG   A H      1 
ATOM   1306  H  HA     . ARG   A 1 81  ? -14.857 -10.065 30.104 1.00 32.37  ?  106 ARG   A HA     1 
ATOM   1307  H  HB2    . ARG   A 1 81  ? -15.773 -10.005 27.430 1.00 34.12  ?  106 ARG   A HB2    1 
ATOM   1308  H  HB3    . ARG   A 1 81  ? -16.467 -10.884 28.557 1.00 34.12  ?  106 ARG   A HB3    1 
ATOM   1309  H  HG2    . ARG   A 1 81  ? -17.019 -8.915  29.721 1.00 36.26  ?  106 ARG   A HG2    1 
ATOM   1310  H  HG3    . ARG   A 1 81  ? -16.381 -8.060  28.542 1.00 36.26  ?  106 ARG   A HG3    1 
ATOM   1311  H  HD2    . ARG   A 1 81  ? -18.072 -8.604  27.120 1.00 39.69  ?  106 ARG   A HD2    1 
ATOM   1312  H  HD3    . ARG   A 1 81  ? -18.602 -9.747  28.089 1.00 39.69  ?  106 ARG   A HD3    1 
ATOM   1313  H  HE     . ARG   A 1 81  ? -19.119 -7.104  28.373 1.00 42.63  ?  106 ARG   A HE     1 
ATOM   1314  H  HH11   . ARG   A 1 81  ? -19.517 -10.058 29.808 1.00 45.02  ?  106 ARG   A HH11   1 
ATOM   1315  H  HH12   . ARG   A 1 81  ? -20.569 -9.631  30.773 1.00 45.02  ?  106 ARG   A HH12   1 
ATOM   1316  H  HH21   . ARG   A 1 81  ? -20.724 -6.470  29.848 1.00 44.96  ?  106 ARG   A HH21   1 
ATOM   1317  H  HH22   . ARG   A 1 81  ? -21.298 -7.464  30.797 1.00 44.96  ?  106 ARG   A HH22   1 
ATOM   1318  N  N      . VAL   A 1 82  ? -13.755 -12.225 29.943 1.00 27.50  ?  107 VAL   A N      1 
ATOM   1319  C  CA     . VAL   A 1 82  ? -13.021 -13.482 29.874 1.00 28.13  ?  107 VAL   A CA     1 
ATOM   1320  C  C      . VAL   A 1 82  ? -13.997 -14.625 30.104 1.00 29.31  ?  107 VAL   A C      1 
ATOM   1321  O  O      . VAL   A 1 82  ? -14.740 -14.620 31.091 1.00 30.13  ?  107 VAL   A O      1 
ATOM   1322  C  CB     . VAL   A 1 82  ? -11.885 -13.540 30.913 1.00 27.86  ?  107 VAL   A CB     1 
ATOM   1323  C  CG1    . VAL   A 1 82  ? -11.147 -14.894 30.834 1.00 28.32  ?  107 VAL   A CG1    1 
ATOM   1324  C  CG2    . VAL   A 1 82  ? -10.925 -12.380 30.716 1.00 27.27  ?  107 VAL   A CG2    1 
ATOM   1325  H  H      . VAL   A 1 82  ? -14.077 -12.060 30.724 1.00 32.99  ?  107 VAL   A H      1 
ATOM   1326  H  HA     . VAL   A 1 82  ? -12.639 -13.568 28.987 1.00 33.75  ?  107 VAL   A HA     1 
ATOM   1327  H  HB     . VAL   A 1 82  ? -12.266 -13.462 31.802 1.00 33.43  ?  107 VAL   A HB     1 
ATOM   1328  H  HG11   . VAL   A 1 82  ? -10.319 -14.832 31.336 1.00 33.97  ?  107 VAL   A HG11   1 
ATOM   1329  H  HG12   . VAL   A 1 82  ? -11.713 -15.584 31.214 1.00 33.97  ?  107 VAL   A HG12   1 
ATOM   1330  H  HG13   . VAL   A 1 82  ? -10.956 -15.096 29.905 1.00 33.97  ?  107 VAL   A HG13   1 
ATOM   1331  H  HG21   . VAL   A 1 82  ? -10.192 -12.467 31.344 1.00 32.72  ?  107 VAL   A HG21   1 
ATOM   1332  H  HG22   . VAL   A 1 82  ? -10.587 -12.401 29.807 1.00 32.72  ?  107 VAL   A HG22   1 
ATOM   1333  H  HG23   . VAL   A 1 82  ? -11.399 -11.548 30.873 1.00 32.72  ?  107 VAL   A HG23   1 
ATOM   1334  N  N      . THR   A 1 83  ? -13.952 -15.630 29.237 1.00 30.08  ?  108 THR   A N      1 
ATOM   1335  C  CA     . THR   A 1 83  ? -14.768 -16.828 29.388 1.00 30.66  ?  108 THR   A CA     1 
ATOM   1336  C  C      . THR   A 1 83  ? -13.862 -18.051 29.392 1.00 30.29  ?  108 THR   A C      1 
ATOM   1337  O  O      . THR   A 1 83  ? -12.987 -18.184 28.531 1.00 30.80  ?  108 THR   A O      1 
ATOM   1338  C  CB     . THR   A 1 83  ? -15.816 -16.934 28.275 1.00 31.78  ?  108 THR   A CB     1 
ATOM   1339  O  OG1    . THR   A 1 83  ? -16.743 -15.846 28.386 1.00 33.54  ?  108 THR   A OG1    1 
ATOM   1340  C  CG2    . THR   A 1 83  ? -16.579 -18.267 28.383 1.00 33.55  ?  108 THR   A CG2    1 
ATOM   1341  H  H      . THR   A 1 83  ? -13.448 -15.641 28.541 1.00 36.08  ?  108 THR   A H      1 
ATOM   1342  H  HA     . THR   A 1 83  ? -15.238 -16.795 30.236 1.00 36.78  ?  108 THR   A HA     1 
ATOM   1343  H  HB     . THR   A 1 83  ? -15.379 -16.899 27.410 1.00 38.13  ?  108 THR   A HB     1 
ATOM   1344  H  HG1    . THR   A 1 83  ? -17.312 -15.889 27.769 1.00 40.24  ?  108 THR   A HG1    1 
ATOM   1345  H  HG21   . THR   A 1 83  ? -17.392 -18.228 27.857 1.00 40.25  ?  108 THR   A HG21   1 
ATOM   1346  H  HG22   . THR   A 1 83  ? -16.026 -18.993 28.054 1.00 40.25  ?  108 THR   A HG22   1 
ATOM   1347  H  HG23   . THR   A 1 83  ? -16.811 -18.443 29.309 1.00 40.25  ?  108 THR   A HG23   1 
ATOM   1348  N  N      . ILE   A 1 84  ? -14.061 -18.924 30.378 1.00 29.30  ?  109 ILE   A N      1 
ATOM   1349  C  CA     . ILE   A 1 84  ? -13.333 -20.183 30.502 1.00 29.31  ?  109 ILE   A CA     1 
ATOM   1350  C  C      . ILE   A 1 84  ? -14.371 -21.298 30.548 1.00 29.90  ?  109 ILE   A C      1 
ATOM   1351  O  O      . ILE   A 1 84  ? -15.267 -21.284 31.404 1.00 32.19  ?  109 ILE   A O      1 
ATOM   1352  C  CB     . ILE   A 1 84  ? -12.442 -20.209 31.751 1.00 30.35  ?  109 ILE   A CB     1 
ATOM   1353  C  CG1    . ILE   A 1 84  ? -11.472 -19.025 31.739 1.00 31.39  ?  109 ILE   A CG1    1 
ATOM   1354  C  CG2    . ILE   A 1 84  ? -11.660 -21.516 31.820 1.00 31.07  ?  109 ILE   A CG2    1 
ATOM   1355  C  CD1    . ILE   A 1 84  ? -10.777 -18.810 33.063 1.00 32.91  ?  109 ILE   A CD1    1 
ATOM   1356  H  H      . ILE   A 1 84  ? -14.634 -18.804 31.008 1.00 35.15  ?  109 ILE   A H      1 
ATOM   1357  H  HA     . ILE   A 1 84  ? -12.765 -20.313 29.726 1.00 35.17  ?  109 ILE   A HA     1 
ATOM   1358  H  HB     . ILE   A 1 84  ? -13.014 -20.141 32.532 1.00 36.41  ?  109 ILE   A HB     1 
ATOM   1359  H  HG12   . ILE   A 1 84  ? -10.791 -19.184 31.067 1.00 37.67  ?  109 ILE   A HG12   1 
ATOM   1360  H  HG13   . ILE   A 1 84  ? -11.966 -18.218 31.527 1.00 37.67  ?  109 ILE   A HG13   1 
ATOM   1361  H  HG21   . ILE   A 1 84  ? -11.059 -21.485 32.582 1.00 37.28  ?  109 ILE   A HG21   1 
ATOM   1362  H  HG22   . ILE   A 1 84  ? -12.283 -22.252 31.921 1.00 37.28  ?  109 ILE   A HG22   1 
ATOM   1363  H  HG23   . ILE   A 1 84  ? -11.150 -21.623 31.002 1.00 37.28  ?  109 ILE   A HG23   1 
ATOM   1364  H  HD11   . ILE   A 1 84  ? -10.298 -17.967 33.034 1.00 39.49  ?  109 ILE   A HD11   1 
ATOM   1365  H  HD12   . ILE   A 1 84  ? -11.442 -18.789 33.769 1.00 39.49  ?  109 ILE   A HD12   1 
ATOM   1366  H  HD13   . ILE   A 1 84  ? -10.156 -19.539 33.215 1.00 39.49  ?  109 ILE   A HD13   1 
ATOM   1367  N  N      . ASP   A 1 85  ? -14.258 -22.248 29.620 1.00 31.63  ?  110 ASP   A N      1 
ATOM   1368  C  CA     . ASP   A 1 85  ? -15.198 -23.358 29.477 1.00 33.11  ?  110 ASP   A CA     1 
ATOM   1369  C  C      . ASP   A 1 85  ? -14.418 -24.664 29.432 1.00 33.73  ?  110 ASP   A C      1 
ATOM   1370  O  O      . ASP   A 1 85  ? -14.050 -25.150 28.354 1.00 33.51  ?  110 ASP   A O      1 
ATOM   1371  C  CB     . ASP   A 1 85  ? -16.039 -23.179 28.217 1.00 35.66  ?  110 ASP   A CB     1 
ATOM   1372  C  CG     . ASP   A 1 85  ? -17.000 -24.326 27.970 1.00 37.95  ?  110 ASP   A CG     1 
ATOM   1373  O  OD1    . ASP   A 1 85  ? -17.058 -25.287 28.774 1.00 38.92  ?  110 ASP   A OD1    1 
ATOM   1374  O  OD2    . ASP   A 1 85  ? -17.708 -24.249 26.945 1.00 40.56  ?  110 ASP   A OD2    1 
ATOM   1375  H  H      . ASP   A 1 85  ? -13.623 -22.271 29.041 1.00 37.95  ?  110 ASP   A H      1 
ATOM   1376  H  HA     . ASP   A 1 85  ? -15.782 -23.390 30.250 1.00 39.72  ?  110 ASP   A HA     1 
ATOM   1377  H  HB2    . ASP   A 1 85  ? -16.561 -22.366 28.301 1.00 42.78  ?  110 ASP   A HB2    1 
ATOM   1378  H  HB3    . ASP   A 1 85  ? -15.447 -23.116 27.451 1.00 42.78  ?  110 ASP   A HB3    1 
ATOM   1379  N  N      . PRO   A 1 86  ? -14.141 -25.262 30.589 1.00 32.00  ?  111 PRO   A N      1 
ATOM   1380  C  CA     . PRO   A 1 86  ? -13.360 -26.506 30.579 1.00 32.69  ?  111 PRO   A CA     1 
ATOM   1381  C  C      . PRO   A 1 86  ? -14.038 -27.632 29.839 1.00 34.94  ?  111 PRO   A C      1 
ATOM   1382  O  O      . PRO   A 1 86  ? -13.354 -28.438 29.191 1.00 36.59  ?  111 PRO   A O      1 
ATOM   1383  C  CB     . PRO   A 1 86  ? -13.200 -26.830 32.072 1.00 32.35  ?  111 PRO   A CB     1 
ATOM   1384  C  CG     . PRO   A 1 86  ? -13.271 -25.503 32.741 1.00 31.74  ?  111 PRO   A CG     1 
ATOM   1385  C  CD     . PRO   A 1 86  ? -14.307 -24.729 31.956 1.00 31.82  ?  111 PRO   A CD     1 
ATOM   1386  H  HA     . PRO   A 1 86  ? -12.487 -26.344 30.188 1.00 39.23  ?  111 PRO   A HA     1 
ATOM   1387  H  HB2    . PRO   A 1 86  ? -13.919 -27.410 32.366 1.00 38.81  ?  111 PRO   A HB2    1 
ATOM   1388  H  HB3    . PRO   A 1 86  ? -12.344 -27.256 32.231 1.00 38.81  ?  111 PRO   A HB3    1 
ATOM   1389  H  HG2    . PRO   A 1 86  ? -13.546 -25.612 33.665 1.00 38.08  ?  111 PRO   A HG2    1 
ATOM   1390  H  HG3    . PRO   A 1 86  ? -12.407 -25.065 32.702 1.00 38.08  ?  111 PRO   A HG3    1 
ATOM   1391  H  HD2    . PRO   A 1 86  ? -15.200 -24.904 32.292 1.00 38.18  ?  111 PRO   A HD2    1 
ATOM   1392  H  HD3    . PRO   A 1 86  ? -14.123 -23.777 31.983 1.00 38.18  ?  111 PRO   A HD3    1 
ATOM   1393  N  N      . GLU   A 1 87  ? -15.367 -27.715 29.895 1.00 37.77  ?  112 GLU   A N      1 
ATOM   1394  C  CA     . GLU   A 1 87  ? -16.030 -28.883 29.332 1.00 41.40  ?  112 GLU   A CA     1 
ATOM   1395  C  C      . GLU   A 1 87  ? -15.829 -28.954 27.824 1.00 41.58  ?  112 GLU   A C      1 
ATOM   1396  O  O      . GLU   A 1 87  ? -15.670 -30.045 27.267 1.00 42.74  ?  112 GLU   A O      1 
ATOM   1397  C  CB     . GLU   A 1 87  ? -17.515 -28.872 29.682 1.00 46.53  ?  112 GLU   A CB     1 
ATOM   1398  C  CG     . GLU   A 1 87  ? -17.793 -28.978 31.174 1.00 50.13  ?  112 GLU   A CG     1 
ATOM   1399  C  CD     . GLU   A 1 87  ? -19.264 -29.176 31.472 1.00 55.74  ?  112 GLU   A CD     1 
ATOM   1400  O  OE1    . GLU   A 1 87  ? -20.042 -29.340 30.511 1.00 57.80  ?  112 GLU   A OE1    1 
ATOM   1401  O  OE2    . GLU   A 1 87  ? -19.646 -29.171 32.663 1.00 57.71  ?  112 GLU   A OE2    1 
ATOM   1402  H  H      . GLU   A 1 87  ? -15.889 -27.127 30.243 1.00 45.32  ?  112 GLU   A H      1 
ATOM   1403  H  HA     . GLU   A 1 87  ? -15.643 -29.681 29.725 1.00 49.67  ?  112 GLU   A HA     1 
ATOM   1404  H  HB2    . GLU   A 1 87  ? -17.904 -28.041 29.367 1.00 55.83  ?  112 GLU   A HB2    1 
ATOM   1405  H  HB3    . GLU   A 1 87  ? -17.944 -29.625 29.247 1.00 55.83  ?  112 GLU   A HB3    1 
ATOM   1406  H  HG2    . GLU   A 1 87  ? -17.307 -29.736 31.534 1.00 60.15  ?  112 GLU   A HG2    1 
ATOM   1407  H  HG3    . GLU   A 1 87  ? -17.504 -28.161 31.610 1.00 60.15  ?  112 GLU   A HG3    1 
ATOM   1408  N  N      . ASN   A 1 88  ? -15.839 -27.808 27.142 1.00 39.68  ?  113 ASN   A N      1 
ATOM   1409  C  CA     . ASN   A 1 88  ? -15.612 -27.774 25.706 1.00 38.45  ?  113 ASN   A CA     1 
ATOM   1410  C  C      . ASN   A 1 88  ? -14.209 -27.311 25.335 1.00 35.95  ?  113 ASN   A C      1 
ATOM   1411  O  O      . ASN   A 1 88  ? -13.945 -27.071 24.153 1.00 36.20  ?  113 ASN   A O      1 
ATOM   1412  C  CB     . ASN   A 1 88  ? -16.635 -26.866 25.026 1.00 40.22  ?  113 ASN   A CB     1 
ATOM   1413  C  CG     . ASN   A 1 88  ? -18.048 -27.306 25.285 1.00 44.56  ?  113 ASN   A CG     1 
ATOM   1414  O  OD1    . ASN   A 1 88  ? -18.468 -28.374 24.845 1.00 46.70  ?  113 ASN   A OD1    1 
ATOM   1415  N  ND2    . ASN   A 1 88  ? -18.796 -26.483 26.005 1.00 45.42  ?  113 ASN   A ND2    1 
ATOM   1416  H  H      . ASN   A 1 88  ? -15.977 -27.036 27.496 1.00 47.61  ?  113 ASN   A H      1 
ATOM   1417  H  HA     . ASN   A 1 88  ? -15.730 -28.676 25.368 1.00 46.14  ?  113 ASN   A HA     1 
ATOM   1418  H  HB2    . ASN   A 1 88  ? -16.533 -25.963 25.365 1.00 48.26  ?  113 ASN   A HB2    1 
ATOM   1419  H  HB3    . ASN   A 1 88  ? -16.485 -26.880 24.068 1.00 48.26  ?  113 ASN   A HB3    1 
ATOM   1420  H  HD21   . ASN   A 1 88  ? -19.612 -26.688 26.182 1.00 54.50  ?  113 ASN   A HD21   1 
ATOM   1421  H  HD22   . ASN   A 1 88  ? -18.465 -25.745 26.296 1.00 54.50  ?  113 ASN   A HD22   1 
ATOM   1422  N  N      . ASN   A 1 89  ? -13.321 -27.170 26.320 1.00 34.20  ?  114 ASN   A N      1 
ATOM   1423  C  CA     . ASN   A 1 89  ? -11.931 -26.741 26.140 1.00 33.35  ?  114 ASN   A CA     1 
ATOM   1424  C  C      . ASN   A 1 89  ? -11.836 -25.454 25.317 1.00 32.32  ?  114 ASN   A C      1 
ATOM   1425  O  O      . ASN   A 1 89  ? -11.172 -25.383 24.277 1.00 31.43  ?  114 ASN   A O      1 
ATOM   1426  C  CB     . ASN   A 1 89  ? -11.083 -27.846 25.508 1.00 33.50  ?  114 ASN   A CB     1 
ATOM   1427  C  CG     . ASN   A 1 89  ? -9.590  -27.540 25.572 1.00 34.82  ?  114 ASN   A CG     1 
ATOM   1428  O  OD1    . ASN   A 1 89  ? -9.086  -27.084 26.596 1.00 36.87  ?  114 ASN   A OD1    1 
ATOM   1429  N  ND2    . ASN   A 1 89  ? -8.887  -27.767 24.471 1.00 34.33  ?  114 ASN   A ND2    1 
ATOM   1430  H  H      . ASN   A 1 89  ? -13.509 -27.325 27.145 1.00 41.03  ?  114 ASN   A H      1 
ATOM   1431  H  HA     . ASN   A 1 89  ? -11.576 -26.550 27.023 1.00 40.01  ?  114 ASN   A HA     1 
ATOM   1432  H  HB2    . ASN   A 1 89  ? -11.241 -28.678 25.981 1.00 40.19  ?  114 ASN   A HB2    1 
ATOM   1433  H  HB3    . ASN   A 1 89  ? -11.331 -27.943 24.575 1.00 40.19  ?  114 ASN   A HB3    1 
ATOM   1434  H  HD21   . ASN   A 1 89  ? -8.042  -27.609 24.460 1.00 41.19  ?  114 ASN   A HD21   1 
ATOM   1435  H  HD22   . ASN   A 1 89  ? -9.277  -28.073 23.768 1.00 41.19  ?  114 ASN   A HD22   1 
ATOM   1436  N  N      . LEU   A 1 90  ? -12.489 -24.416 25.833 1.00 30.81  ?  115 LEU   A N      1 
ATOM   1437  C  CA     . LEU   A 1 90  ? -12.653 -23.153 25.131 1.00 32.50  ?  115 LEU   A CA     1 
ATOM   1438  C  C      . LEU   A 1 90  ? -12.306 -22.007 26.059 1.00 30.13  ?  115 LEU   A C      1 
ATOM   1439  O  O      . LEU   A 1 90  ? -12.823 -21.939 27.179 1.00 31.29  ?  115 LEU   A O      1 
ATOM   1440  C  CB     . LEU   A 1 90  ? -14.090 -22.974 24.644 1.00 37.29  ?  115 LEU   A CB     1 
ATOM   1441  C  CG     . LEU   A 1 90  ? -14.388 -23.233 23.175 1.00 43.26  ?  115 LEU   A CG     1 
ATOM   1442  C  CD1    . LEU   A 1 90  ? -15.888 -23.117 22.948 1.00 45.23  ?  115 LEU   A CD1    1 
ATOM   1443  C  CD2    . LEU   A 1 90  ? -13.628 -22.257 22.310 1.00 45.86  ?  115 LEU   A CD2    1 
ATOM   1444  H  H      . LEU   A 1 90  ? -12.854 -24.422 26.612 1.00 36.97  ?  115 LEU   A H      1 
ATOM   1445  H  HA     . LEU   A 1 90  ? -12.050 -23.140 24.371 1.00 38.99  ?  115 LEU   A HA     1 
ATOM   1446  H  HB2    . LEU   A 1 90  ? -14.650 -23.581 25.153 1.00 44.75  ?  115 LEU   A HB2    1 
ATOM   1447  H  HB3    . LEU   A 1 90  ? -14.348 -22.056 24.823 1.00 44.75  ?  115 LEU   A HB3    1 
ATOM   1448  H  HG     . LEU   A 1 90  ? -14.104 -24.126 22.923 1.00 51.90  ?  115 LEU   A HG     1 
ATOM   1449  H  HD11   . LEU   A 1 90  ? -16.077 -23.271 22.009 1.00 54.27  ?  115 LEU   A HD11   1 
ATOM   1450  H  HD12   . LEU   A 1 90  ? -16.342 -23.781 23.490 1.00 54.27  ?  115 LEU   A HD12   1 
ATOM   1451  H  HD13   . LEU   A 1 90  ? -16.178 -22.227 23.202 1.00 54.27  ?  115 LEU   A HD13   1 
ATOM   1452  H  HD21   . LEU   A 1 90  ? -13.983 -22.291 21.408 1.00 55.03  ?  115 LEU   A HD21   1 
ATOM   1453  H  HD22   . LEU   A 1 90  ? -13.734 -21.364 22.674 1.00 55.03  ?  115 LEU   A HD22   1 
ATOM   1454  H  HD23   . LEU   A 1 90  ? -12.690 -22.503 22.306 1.00 55.03  ?  115 LEU   A HD23   1 
ATOM   1455  N  N      . ILE   A 1 91  ? -11.443 -21.113 25.593 1.00 27.28  ?  116 ILE   A N      1 
ATOM   1456  C  CA     . ILE   A 1 91  ? -11.165 -19.854 26.269 1.00 25.59  ?  116 ILE   A CA     1 
ATOM   1457  C  C      . ILE   A 1 91  ? -11.472 -18.732 25.295 1.00 26.24  ?  116 ILE   A C      1 
ATOM   1458  O  O      . ILE   A 1 91  ? -11.114 -18.808 24.115 1.00 26.60  ?  116 ILE   A O      1 
ATOM   1459  C  CB     . ILE   A 1 91  ? -9.711  -19.762 26.774 1.00 25.32  ?  116 ILE   A CB     1 
ATOM   1460  C  CG1    . ILE   A 1 91  ? -9.479  -20.902 27.757 1.00 26.41  ?  116 ILE   A CG1    1 
ATOM   1461  C  CG2    . ILE   A 1 91  ? -9.484  -18.389 27.403 1.00 25.78  ?  116 ILE   A CG2    1 
ATOM   1462  C  CD1    . ILE   A 1 91  ? -8.038  -21.157 28.095 1.00 27.30  ?  116 ILE   A CD1    1 
ATOM   1463  H  H      . ILE   A 1 91  ? -10.994 -21.217 24.866 1.00 32.73  ?  116 ILE   A H      1 
ATOM   1464  H  HA     . ILE   A 1 91  ? -11.742 -19.773 27.044 1.00 30.71  ?  116 ILE   A HA     1 
ATOM   1465  H  HB     . ILE   A 1 91  ? -9.076  -19.854 26.046 1.00 30.37  ?  116 ILE   A HB     1 
ATOM   1466  H  HG12   . ILE   A 1 91  ? -9.940  -20.693 28.585 1.00 31.68  ?  116 ILE   A HG12   1 
ATOM   1467  H  HG13   . ILE   A 1 91  ? -9.838  -21.717 27.374 1.00 31.68  ?  116 ILE   A HG13   1 
ATOM   1468  H  HG21   . ILE   A 1 91  ? -8.659  -18.408 27.913 1.00 30.93  ?  116 ILE   A HG21   1 
ATOM   1469  H  HG22   . ILE   A 1 91  ? -9.422  -17.725 26.699 1.00 30.93  ?  116 ILE   A HG22   1 
ATOM   1470  H  HG23   . ILE   A 1 91  ? -10.230 -18.183 27.988 1.00 30.93  ?  116 ILE   A HG23   1 
ATOM   1471  H  HD11   . ILE   A 1 91  ? -7.981  -21.942 28.663 1.00 32.75  ?  116 ILE   A HD11   1 
ATOM   1472  H  HD12   . ILE   A 1 91  ? -7.543  -21.307 27.274 1.00 32.75  ?  116 ILE   A HD12   1 
ATOM   1473  H  HD13   . ILE   A 1 91  ? -7.681  -20.385 28.561 1.00 32.75  ?  116 ILE   A HD13   1 
ATOM   1474  N  N      . SER   A 1 92  ? -12.136 -17.695 25.784 1.00 27.46  ?  117 SER   A N      1 
ATOM   1475  C  CA     . SER   A 1 92  ? -12.471 -16.554 24.955 1.00 27.77  ?  117 SER   A CA     1 
ATOM   1476  C  C      . SER   A 1 92  ? -12.163 -15.263 25.697 1.00 27.59  ?  117 SER   A C      1 
ATOM   1477  O  O      . SER   A 1 92  ? -12.534 -15.112 26.864 1.00 29.74  ?  117 SER   A O      1 
ATOM   1478  C  CB     . SER   A 1 92  ? -13.946 -16.624 24.552 1.00 30.64  ?  117 SER   A CB     1 
ATOM   1479  O  OG     . SER   A 1 92  ? -14.217 -15.649 23.576 1.00 33.58  ?  117 SER   A OG     1 
ATOM   1480  H  H      . SER   A 1 92  ? -12.404 -17.631 26.598 1.00 32.95  ?  117 SER   A H      1 
ATOM   1481  H  HA     . SER   A 1 92  ? -11.925 -16.547 24.153 1.00 33.32  ?  117 SER   A HA     1 
ATOM   1482  H  HB2    . SER   A 1 92  ? -14.137 -17.502 24.188 1.00 36.76  ?  117 SER   A HB2    1 
ATOM   1483  H  HB3    . SER   A 1 92  ? -14.499 -16.459 25.331 1.00 36.76  ?  117 SER   A HB3    1 
ATOM   1484  H  HG     . SER   A 1 92  ? -15.034 -15.655 23.383 1.00 40.29  ?  117 SER   A HG     1 
ATOM   1485  N  N      . ILE   A 1 93  ? -11.502 -14.328 25.015 1.00 26.18  ?  118 ILE   A N      1 
ATOM   1486  C  CA     . ILE   A 1 93  ? -11.156 -13.031 25.601 1.00 26.42  ?  118 ILE   A CA     1 
ATOM   1487  C  C      . ILE   A 1 93  ? -11.604 -11.921 24.653 1.00 27.91  ?  118 ILE   A C      1 
ATOM   1488  O  O      . ILE   A 1 93  ? -11.163 -11.858 23.500 1.00 28.17  ?  118 ILE   A O      1 
ATOM   1489  C  CB     . ILE   A 1 93  ? -9.653  -12.930 25.918 1.00 27.02  ?  118 ILE   A CB     1 
ATOM   1490  C  CG1    . ILE   A 1 93  ? -9.306  -13.984 26.967 1.00 25.57  ?  118 ILE   A CG1    1 
ATOM   1491  C  CG2    . ILE   A 1 93  ? -9.317  -11.556 26.446 1.00 27.91  ?  118 ILE   A CG2    1 
ATOM   1492  C  CD1    . ILE   A 1 93  ? -7.816  -14.252 27.135 1.00 26.34  ?  118 ILE   A CD1    1 
ATOM   1493  H  H      . ILE   A 1 93  ? -11.240 -14.422 24.201 1.00 31.41  ?  118 ILE   A H      1 
ATOM   1494  H  HA     . ILE   A 1 93  ? -11.650 -12.913 26.427 1.00 31.70  ?  118 ILE   A HA     1 
ATOM   1495  H  HB     . ILE   A 1 93  ? -9.142  -13.082 25.108 1.00 32.42  ?  118 ILE   A HB     1 
ATOM   1496  H  HG12   . ILE   A 1 93  ? -9.647  -13.688 27.826 1.00 30.68  ?  118 ILE   A HG12   1 
ATOM   1497  H  HG13   . ILE   A 1 93  ? -9.726  -14.821 26.714 1.00 30.68  ?  118 ILE   A HG13   1 
ATOM   1498  H  HG21   . ILE   A 1 93  ? -8.421  -11.570 26.818 1.00 33.48  ?  118 ILE   A HG21   1 
ATOM   1499  H  HG22   . ILE   A 1 93  ? -9.363  -10.917 25.717 1.00 33.48  ?  118 ILE   A HG22   1 
ATOM   1500  H  HG23   . ILE   A 1 93  ? -9.956  -11.317 27.136 1.00 33.48  ?  118 ILE   A HG23   1 
ATOM   1501  H  HD11   . ILE   A 1 93  ? -7.696  -14.992 27.751 1.00 31.60  ?  118 ILE   A HD11   1 
ATOM   1502  H  HD12   . ILE   A 1 93  ? -7.436  -14.475 26.271 1.00 31.60  ?  118 ILE   A HD12   1 
ATOM   1503  H  HD13   . ILE   A 1 93  ? -7.390  -13.455 27.488 1.00 31.60  ?  118 ILE   A HD13   1 
ATOM   1504  N  N      . TRP   A 1 94  ? -12.473 -11.045 25.150 1.00 27.65  ?  119 TRP   A N      1 
ATOM   1505  C  CA     . TRP   A 1 94  ? -13.137 -9.995  24.383 1.00 28.13  ?  119 TRP   A CA     1 
ATOM   1506  C  C      . TRP   A 1 94  ? -12.758 -8.647  24.976 1.00 27.98  ?  119 TRP   A C      1 
ATOM   1507  O  O      . TRP   A 1 94  ? -12.626 -8.519  26.195 1.00 29.57  ?  119 TRP   A O      1 
ATOM   1508  C  CB     . TRP   A 1 94  ? -14.661 -10.224 24.435 1.00 29.66  ?  119 TRP   A CB     1 
ATOM   1509  C  CG     . TRP   A 1 94  ? -15.568 -9.199  23.779 1.00 31.69  ?  119 TRP   A CG     1 
ATOM   1510  C  CD1    . TRP   A 1 94  ? -16.171 -9.288  22.546 1.00 34.92  ?  119 TRP   A CD1    1 
ATOM   1511  C  CD2    . TRP   A 1 94  ? -16.017 -7.960  24.348 1.00 34.19  ?  119 TRP   A CD2    1 
ATOM   1512  N  NE1    . TRP   A 1 94  ? -16.949 -8.176  22.316 1.00 37.11  ?  119 TRP   A NE1    1 
ATOM   1513  C  CE2    . TRP   A 1 94  ? -16.867 -7.344  23.401 1.00 35.86  ?  119 TRP   A CE2    1 
ATOM   1514  C  CE3    . TRP   A 1 94  ? -15.777 -7.309  25.562 1.00 34.48  ?  119 TRP   A CE3    1 
ATOM   1515  C  CZ2    . TRP   A 1 94  ? -17.467 -6.107  23.632 1.00 37.64  ?  119 TRP   A CZ2    1 
ATOM   1516  C  CZ3    . TRP   A 1 94  ? -16.371 -6.080  25.787 1.00 35.71  ?  119 TRP   A CZ3    1 
ATOM   1517  C  CH2    . TRP   A 1 94  ? -17.217 -5.499  24.832 1.00 36.61  ?  119 TRP   A CH2    1 
ATOM   1518  H  H      . TRP   A 1 94  ? -12.708 -11.038 25.977 1.00 33.17  ?  119 TRP   A H      1 
ATOM   1519  H  HA     . TRP   A 1 94  ? -12.859 -9.989  23.454 1.00 33.75  ?  119 TRP   A HA     1 
ATOM   1520  H  HB2    . TRP   A 1 94  ? -14.846 -11.072 24.003 1.00 35.58  ?  119 TRP   A HB2    1 
ATOM   1521  H  HB3    . TRP   A 1 94  ? -14.921 -10.264 25.369 1.00 35.58  ?  119 TRP   A HB3    1 
ATOM   1522  H  HD1    . TRP   A 1 94  ? -16.069 -9.998  21.954 1.00 41.90  ?  119 TRP   A HD1    1 
ATOM   1523  H  HE1    . TRP   A 1 94  ? -17.411 -8.028  21.606 1.00 44.52  ?  119 TRP   A HE1    1 
ATOM   1524  H  HE3    . TRP   A 1 94  ? -15.228 -7.694  26.206 1.00 41.37  ?  119 TRP   A HE3    1 
ATOM   1525  H  HZ2    . TRP   A 1 94  ? -18.016 -5.711  22.995 1.00 45.16  ?  119 TRP   A HZ2    1 
ATOM   1526  H  HZ3    . TRP   A 1 94  ? -16.207 -5.633  26.585 1.00 42.84  ?  119 TRP   A HZ3    1 
ATOM   1527  H  HH2    . TRP   A 1 94  ? -17.617 -4.680  25.019 1.00 43.93  ?  119 TRP   A HH2    1 
ATOM   1528  N  N      . ASN   A 1 95  ? -12.552 -7.644  24.125 1.00 27.57  ?  120 ASN   A N      1 
ATOM   1529  C  CA     . ASN   A 1 95  ? -12.339 -6.287  24.611 1.00 27.64  ?  120 ASN   A CA     1 
ATOM   1530  C  C      . ASN   A 1 95  ? -13.026 -5.313  23.665 1.00 30.94  ?  120 ASN   A C      1 
ATOM   1531  O  O      . ASN   A 1 95  ? -13.265 -5.625  22.495 1.00 33.32  ?  120 ASN   A O      1 
ATOM   1532  C  CB     . ASN   A 1 95  ? -10.849 -5.931  24.719 1.00 28.62  ?  120 ASN   A CB     1 
ATOM   1533  C  CG     . ASN   A 1 95  ? -10.175 -5.849  23.375 1.00 28.76  ?  120 ASN   A CG     1 
ATOM   1534  O  OD1    . ASN   A 1 95  ? -9.601  -6.825  22.894 1.00 28.63  ?  120 ASN   A OD1    1 
ATOM   1535  N  ND2    . ASN   A 1 95  ? -10.260 -4.687  22.743 1.00 29.20  ?  120 ASN   A ND2    1 
ATOM   1536  H  H      . ASN   A 1 95  ? -12.532 -7.725  23.269 1.00 33.07  ?  120 ASN   A H      1 
ATOM   1537  H  HA     . ASN   A 1 95  ? -12.732 -6.206  25.494 1.00 33.16  ?  120 ASN   A HA     1 
ATOM   1538  H  HB2    . ASN   A 1 95  ? -10.760 -5.068  25.154 1.00 34.34  ?  120 ASN   A HB2    1 
ATOM   1539  H  HB3    . ASN   A 1 95  ? -10.397 -6.613  25.241 1.00 34.34  ?  120 ASN   A HB3    1 
ATOM   1540  H  HD21   . ASN   A 1 95  ? -9.892  -4.589  21.972 1.00 35.03  ?  120 ASN   A HD21   1 
ATOM   1541  H  HD22   . ASN   A 1 95  ? -10.683 -4.031  23.104 1.00 35.03  ?  120 ASN   A HD22   1 
ATOM   1542  N  N      . ASN   A 1 96  ? -13.346 -4.120  24.171 1.00 31.86  ?  121 ASN   A N      1 
ATOM   1543  C  CA     . ASN   A 1 96  ? -13.895 -3.081  23.311 1.00 31.89  ?  121 ASN   A CA     1 
ATOM   1544  C  C      . ASN   A 1 96  ? -12.835 -1.984  23.126 1.00 32.24  ?  121 ASN   A C      1 
ATOM   1545  O  O      . ASN   A 1 96  ? -11.636 -2.228  23.306 1.00 33.15  ?  121 ASN   A O      1 
ATOM   1546  C  CB     . ASN   A 1 96  ? -15.245 -2.571  23.843 1.00 33.89  ?  121 ASN   A CB     1 
ATOM   1547  C  CG     . ASN   A 1 96  ? -15.181 -2.004  25.235 1.00 35.13  ?  121 ASN   A CG     1 
ATOM   1548  O  OD1    . ASN   A 1 96  ? -14.112 -1.819  25.804 1.00 34.25  ?  121 ASN   A OD1    1 
ATOM   1549  N  ND2    . ASN   A 1 96  ? -16.351 -1.683  25.784 1.00 36.95  ?  121 ASN   A ND2    1 
ATOM   1550  H  H      . ASN   A 1 96  ? -13.254 -3.897  24.997 1.00 38.23  ?  121 ASN   A H      1 
ATOM   1551  H  HA     . ASN   A 1 96  ? -14.093 -3.474  22.447 1.00 38.26  ?  121 ASN   A HA     1 
ATOM   1552  H  HB2    . ASN   A 1 96  ? -15.566 -1.870  23.255 1.00 40.66  ?  121 ASN   A HB2    1 
ATOM   1553  H  HB3    . ASN   A 1 96  ? -15.874 -3.309  23.855 1.00 40.66  ?  121 ASN   A HB3    1 
ATOM   1554  H  HD21   . ASN   A 1 96  ? -16.379 -1.354  26.578 1.00 44.33  ?  121 ASN   A HD21   1 
ATOM   1555  H  HD22   . ASN   A 1 96  ? -17.080 -1.804  25.343 1.00 44.33  ?  121 ASN   A HD22   1 
ATOM   1556  N  N      . GLY   A 1 97  ? -13.256 -0.799  22.724 1.00 32.69  ?  122 GLY   A N      1 
ATOM   1557  C  CA     . GLY   A 1 97  ? -12.312 0.141   22.146 1.00 34.43  ?  122 GLY   A CA     1 
ATOM   1558  C  C      . GLY   A 1 97  ? -11.964 -0.274  20.723 1.00 35.82  ?  122 GLY   A C      1 
ATOM   1559  O  O      . GLY   A 1 97  ? -12.480 -1.245  20.172 1.00 36.37  ?  122 GLY   A O      1 
ATOM   1560  H  H      . GLY   A 1 97  ? -14.067 -0.518  22.775 1.00 39.22  ?  122 GLY   A H      1 
ATOM   1561  H  HA2    . GLY   A 1 97  ? -12.699 1.030   22.129 1.00 41.31  ?  122 GLY   A HA2    1 
ATOM   1562  H  HA3    . GLY   A 1 97  ? -11.499 0.160   22.676 1.00 41.31  ?  122 GLY   A HA3    1 
ATOM   1563  N  N      . LYS   A 1 98  ? -11.029 0.470   20.137 1.00 36.71  ?  123 LYS   A N      1 
ATOM   1564  C  CA     . LYS   A 1 98  ? -10.732 0.377   18.710 1.00 37.99  ?  123 LYS   A CA     1 
ATOM   1565  C  C      . LYS   A 1 98  ? -10.352 -1.029  18.264 1.00 37.90  ?  123 LYS   A C      1 
ATOM   1566  O  O      . LYS   A 1 98  ? -9.477  -1.673  18.848 1.00 36.86  ?  123 LYS   A O      1 
ATOM   1567  C  CB     . LYS   A 1 98  ? -9.593  1.351   18.395 1.00 42.24  ?  123 LYS   A CB     1 
ATOM   1568  C  CG     . LYS   A 1 98  ? -9.349  1.660   16.946 1.00 46.08  ?  123 LYS   A CG     1 
ATOM   1569  C  CD     . LYS   A 1 98  ? -8.584  2.980   16.825 1.00 49.37  ?  123 LYS   A CD     1 
ATOM   1570  C  CE     . LYS   A 1 98  ? -8.191  3.263   15.383 1.00 52.62  ?  123 LYS   A CE     1 
ATOM   1571  N  NZ     . LYS   A 1 98  ? -9.338  3.081   14.453 1.00 54.94  ?  123 LYS   A NZ     1 
ATOM   1572  H  H      . LYS   A 1 98  ? -10.544 1.048   20.550 1.00 44.04  ?  123 LYS   A H      1 
ATOM   1573  H  HA     . LYS   A 1 98  ? -11.532 0.608   18.212 1.00 45.58  ?  123 LYS   A HA     1 
ATOM   1574  H  HB2    . LYS   A 1 98  ? -9.787  2.193   18.836 1.00 50.68  ?  123 LYS   A HB2    1 
ATOM   1575  H  HB3    . LYS   A 1 98  ? -8.770  0.974   18.746 1.00 50.68  ?  123 LYS   A HB3    1 
ATOM   1576  H  HG2    . LYS   A 1 98  ? -8.820  0.954   16.544 1.00 55.29  ?  123 LYS   A HG2    1 
ATOM   1577  H  HG3    . LYS   A 1 98  ? -10.196 1.746   16.482 1.00 55.29  ?  123 LYS   A HG3    1 
ATOM   1578  H  HD2    . LYS   A 1 98  ? -9.145  3.708   17.137 1.00 59.24  ?  123 LYS   A HD2    1 
ATOM   1579  H  HD3    . LYS   A 1 98  ? -7.775  2.934   17.358 1.00 59.24  ?  123 LYS   A HD3    1 
ATOM   1580  H  HE2    . LYS   A 1 98  ? -7.882  4.179   15.309 1.00 63.14  ?  123 LYS   A HE2    1 
ATOM   1581  H  HE3    . LYS   A 1 98  ? -7.486  2.652   15.118 1.00 63.14  ?  123 LYS   A HE3    1 
ATOM   1582  H  HZ1    . LYS   A 1 98  ? -10.036 3.557   14.734 1.00 65.92  ?  123 LYS   A HZ1    1 
ATOM   1583  H  HZ2    . LYS   A 1 98  ? -9.113  3.353   13.636 1.00 65.92  ?  123 LYS   A HZ2    1 
ATOM   1584  H  HZ3    . LYS   A 1 98  ? -9.569  2.223   14.418 1.00 65.92  ?  123 LYS   A HZ3    1 
ATOM   1585  N  N      . GLY   A 1 99  ? -11.010 -1.487  17.191 1.00 38.21  ?  124 GLY   A N      1 
ATOM   1586  C  CA     . GLY   A 1 99  ? -10.654 -2.748  16.585 1.00 37.89  ?  124 GLY   A CA     1 
ATOM   1587  C  C      . GLY   A 1 99  ? -9.419  -2.631  15.724 1.00 38.74  ?  124 GLY   A C      1 
ATOM   1588  O  O      . GLY   A 1 99  ? -8.852  -1.563  15.516 1.00 40.49  ?  124 GLY   A O      1 
ATOM   1589  H  H      . GLY   A 1 99  ? -11.662 -1.080  16.806 1.00 45.85  ?  124 GLY   A H      1 
ATOM   1590  H  HA2    . GLY   A 1 99  ? -10.484 -3.403  17.279 1.00 45.46  ?  124 GLY   A HA2    1 
ATOM   1591  H  HA3    . GLY   A 1 99  ? -11.387 -3.058  16.031 1.00 45.46  ?  124 GLY   A HA3    1 
ATOM   1592  N  N      . ILE   A 1 100 ? -8.966  -3.767  15.213 1.00 37.53  ?  125 ILE   A N      1 
ATOM   1593  C  CA     . ILE   A 1 100 ? -7.799  -3.791  14.334 1.00 37.48  ?  125 ILE   A CA     1 
ATOM   1594  C  C      . ILE   A 1 100 ? -8.265  -3.360  12.952 1.00 38.67  ?  125 ILE   A C      1 
ATOM   1595  O  O      . ILE   A 1 100 ? -9.355  -3.768  12.534 1.00 39.57  ?  125 ILE   A O      1 
ATOM   1596  C  CB     . ILE   A 1 100 ? -7.165  -5.184  14.309 1.00 37.36  ?  125 ILE   A CB     1 
ATOM   1597  C  CG1    . ILE   A 1 100 ? -6.676  -5.525  15.713 1.00 37.59  ?  125 ILE   A CG1    1 
ATOM   1598  C  CG2    . ILE   A 1 100 ? -6.021  -5.244  13.330 1.00 37.11  ?  125 ILE   A CG2    1 
ATOM   1599  C  CD1    . ILE   A 1 100 ? -6.611  -6.975  15.952 1.00 37.19  ?  125 ILE   A CD1    1 
ATOM   1600  H  H      . ILE   A 1 100 ? -9.315  -4.539  15.359 1.00 45.03  ?  125 ILE   A H      1 
ATOM   1601  H  HA     . ILE   A 1 100 ? -7.124  -3.168  14.646 1.00 44.97  ?  125 ILE   A HA     1 
ATOM   1602  H  HB     . ILE   A 1 100 ? -7.832  -5.827  14.024 1.00 44.83  ?  125 ILE   A HB     1 
ATOM   1603  H  HG12   . ILE   A 1 100 ? -5.785  -5.160  15.835 1.00 45.10  ?  125 ILE   A HG12   1 
ATOM   1604  H  HG13   . ILE   A 1 100 ? -7.284  -5.140  16.363 1.00 45.10  ?  125 ILE   A HG13   1 
ATOM   1605  H  HG21   . ILE   A 1 100 ? -5.600  -6.115  13.390 1.00 44.53  ?  125 ILE   A HG21   1 
ATOM   1606  H  HG22   . ILE   A 1 100 ? -6.365  -5.103  12.434 1.00 44.53  ?  125 ILE   A HG22   1 
ATOM   1607  H  HG23   . ILE   A 1 100 ? -5.380  -4.550  13.551 1.00 44.53  ?  125 ILE   A HG23   1 
ATOM   1608  H  HD11   . ILE   A 1 100 ? -6.230  -7.133  16.829 1.00 44.62  ?  125 ILE   A HD11   1 
ATOM   1609  H  HD12   . ILE   A 1 100 ? -7.508  -7.342  15.909 1.00 44.62  ?  125 ILE   A HD12   1 
ATOM   1610  H  HD13   . ILE   A 1 100 ? -6.054  -7.382  15.270 1.00 44.62  ?  125 ILE   A HD13   1 
ATOM   1611  N  N      . PRO   A 1 101 ? -7.500  -2.553  12.214 1.00 39.17  ?  126 PRO   A N      1 
ATOM   1612  C  CA     . PRO   A 1 101 ? -7.976  -2.114  10.890 1.00 40.29  ?  126 PRO   A CA     1 
ATOM   1613  C  C      . PRO   A 1 101 ? -8.259  -3.308  9.989  1.00 40.97  ?  126 PRO   A C      1 
ATOM   1614  O  O      . PRO   A 1 101 ? -7.410  -4.184  9.815  1.00 41.76  ?  126 PRO   A O      1 
ATOM   1615  C  CB     . PRO   A 1 101 ? -6.822  -1.268  10.340 1.00 41.65  ?  126 PRO   A CB     1 
ATOM   1616  C  CG     . PRO   A 1 101 ? -5.878  -1.023  11.482 1.00 42.00  ?  126 PRO   A CG     1 
ATOM   1617  C  CD     . PRO   A 1 101 ? -6.316  -1.806  12.682 1.00 41.05  ?  126 PRO   A CD     1 
ATOM   1618  H  HA     . PRO   A 1 101 ? -8.770  -1.564  10.983 1.00 48.34  ?  126 PRO   A HA     1 
ATOM   1619  H  HB2    . PRO   A 1 101 ? -6.377  -1.753  9.629  1.00 49.97  ?  126 PRO   A HB2    1 
ATOM   1620  H  HB3    . PRO   A 1 101 ? -7.171  -0.428  10.002 1.00 49.97  ?  126 PRO   A HB3    1 
ATOM   1621  H  HG2    . PRO   A 1 101 ? -4.989  -1.303  11.214 1.00 50.40  ?  126 PRO   A HG2    1 
ATOM   1622  H  HG3    . PRO   A 1 101 ? -5.880  -0.076  11.689 1.00 50.40  ?  126 PRO   A HG3    1 
ATOM   1623  H  HD2    . PRO   A 1 101 ? -5.618  -2.416  12.966 1.00 49.25  ?  126 PRO   A HD2    1 
ATOM   1624  H  HD3    . PRO   A 1 101 ? -6.554  -1.211  13.410 1.00 49.25  ?  126 PRO   A HD3    1 
ATOM   1625  N  N      . VAL   A 1 102 ? -9.449  -3.334  9.393  1.00 39.78  ?  127 VAL   A N      1 
ATOM   1626  C  CA     . VAL   A 1 102 ? -9.858  -4.437  8.516  1.00 40.56  ?  127 VAL   A CA     1 
ATOM   1627  C  C      . VAL   A 1 102 ? -9.608  -3.965  7.087  1.00 41.19  ?  127 VAL   A C      1 
ATOM   1628  O  O      . VAL   A 1 102 ? -10.484 -3.417  6.411  1.00 42.08  ?  127 VAL   A O      1 
ATOM   1629  C  CB     . VAL   A 1 102 ? -11.305 -4.869  8.766  1.00 40.18  ?  127 VAL   A CB     1 
ATOM   1630  C  CG1    . VAL   A 1 102 ? -11.689 -6.011  7.822  1.00 40.23  ?  127 VAL   A CG1    1 
ATOM   1631  C  CG2    . VAL   A 1 102 ? -11.474 -5.281  10.247 1.00 40.90  ?  127 VAL   A CG2    1 
ATOM   1632  H  H      . VAL   A 1 102 ? -10.045 -2.720  9.481  1.00 47.73  ?  127 VAL   A H      1 
ATOM   1633  H  HA     . VAL   A 1 102 ? -9.290  -5.206  8.679  1.00 48.67  ?  127 VAL   A HA     1 
ATOM   1634  H  HB     . VAL   A 1 102 ? -11.905 -4.129  8.587  1.00 48.21  ?  127 VAL   A HB     1 
ATOM   1635  H  HG11   . VAL   A 1 102 ? -12.554 -6.362  8.086  1.00 48.27  ?  127 VAL   A HG11   1 
ATOM   1636  H  HG12   . VAL   A 1 102 ? -11.733 -5.670  6.915  1.00 48.27  ?  127 VAL   A HG12   1 
ATOM   1637  H  HG13   . VAL   A 1 102 ? -11.018 -6.709  7.881  1.00 48.27  ?  127 VAL   A HG13   1 
ATOM   1638  H  HG21   . VAL   A 1 102 ? -12.378 -5.606  10.382 1.00 49.08  ?  127 VAL   A HG21   1 
ATOM   1639  H  HG22   . VAL   A 1 102 ? -10.836 -5.981  10.455 1.00 49.08  ?  127 VAL   A HG22   1 
ATOM   1640  H  HG23   . VAL   A 1 102 ? -11.312 -4.508  10.810 1.00 49.08  ?  127 VAL   A HG23   1 
ATOM   1641  N  N      . VAL   A 1 103 ? -8.378  -4.190  6.624  1.00 41.90  ?  128 VAL   A N      1 
ATOM   1642  C  CA     . VAL   A 1 103 ? -7.901  -3.633  5.365  1.00 42.43  ?  128 VAL   A CA     1 
ATOM   1643  C  C      . VAL   A 1 103 ? -6.652  -4.397  4.959  1.00 42.84  ?  128 VAL   A C      1 
ATOM   1644  O  O      . VAL   A 1 103 ? -5.957  -4.980  5.798  1.00 40.30  ?  128 VAL   A O      1 
ATOM   1645  C  CB     . VAL   A 1 103 ? -7.614  -2.115  5.495  1.00 41.98  ?  128 VAL   A CB     1 
ATOM   1646  C  CG1    . VAL   A 1 103 ? -6.428  -1.881  6.435  1.00 42.62  ?  128 VAL   A CG1    1 
ATOM   1647  C  CG2    . VAL   A 1 103 ? -7.361  -1.493  4.130  1.00 42.81  ?  128 VAL   A CG2    1 
ATOM   1648  H  H      . VAL   A 1 103 ? -7.792  -4.671  7.031  1.00 50.27  ?  128 VAL   A H      1 
ATOM   1649  H  HA     . VAL   A 1 103 ? -8.579  -3.762  4.683  1.00 50.91  ?  128 VAL   A HA     1 
ATOM   1650  H  HB     . VAL   A 1 103 ? -8.391  -1.677  5.874  1.00 50.37  ?  128 VAL   A HB     1 
ATOM   1651  H  HG11   . VAL   A 1 103 ? -6.395  -0.942  6.675  1.00 51.14  ?  128 VAL   A HG11   1 
ATOM   1652  H  HG12   . VAL   A 1 103 ? -6.545  -2.422  7.231  1.00 51.14  ?  128 VAL   A HG12   1 
ATOM   1653  H  HG13   . VAL   A 1 103 ? -5.610  -2.135  5.980  1.00 51.14  ?  128 VAL   A HG13   1 
ATOM   1654  H  HG21   . VAL   A 1 103 ? -7.338  -0.528  4.222  1.00 51.37  ?  128 VAL   A HG21   1 
ATOM   1655  H  HG22   . VAL   A 1 103 ? -6.510  -1.813  3.790  1.00 51.37  ?  128 VAL   A HG22   1 
ATOM   1656  H  HG23   . VAL   A 1 103 ? -8.076  -1.751  3.528  1.00 51.37  ?  128 VAL   A HG23   1 
ATOM   1657  N  N      . GLU   A 1 104 ? -6.359  -4.390  3.662  1.00 43.83  ?  129 GLU   A N      1 
ATOM   1658  C  CA     . GLU   A 1 104 ? -5.182  -5.067  3.149  1.00 43.86  ?  129 GLU   A CA     1 
ATOM   1659  C  C      . GLU   A 1 104 ? -3.925  -4.248  3.420  1.00 43.63  ?  129 GLU   A C      1 
ATOM   1660  O  O      . GLU   A 1 104 ? -3.849  -3.063  3.082  1.00 43.19  ?  129 GLU   A O      1 
ATOM   1661  C  CB     . GLU   A 1 104 ? -5.341  -5.329  1.654  1.00 47.38  ?  129 GLU   A CB     1 
ATOM   1662  C  CG     . GLU   A 1 104 ? -4.164  -6.056  1.057  1.00 50.76  ?  129 GLU   A CG     1 
ATOM   1663  C  CD     . GLU   A 1 104 ? -4.392  -6.417  -0.384 1.00 55.00  ?  129 GLU   A CD     1 
ATOM   1664  O  OE1    . GLU   A 1 104 ? -4.483  -7.625  -0.694 1.00 57.43  ?  129 GLU   A OE1    1 
ATOM   1665  O  OE2    . GLU   A 1 104 ? -4.492  -5.485  -1.204 1.00 56.28  ?  129 GLU   A OE2    1 
ATOM   1666  H  H      . GLU   A 1 104 ? -6.830  -3.996  3.060  1.00 52.59  ?  129 GLU   A H      1 
ATOM   1667  H  HA     . GLU   A 1 104 ? -5.080  -5.919  3.601  1.00 52.62  ?  129 GLU   A HA     1 
ATOM   1668  H  HB2    . GLU   A 1 104 ? -6.132  -5.873  1.512  1.00 56.85  ?  129 GLU   A HB2    1 
ATOM   1669  H  HB3    . GLU   A 1 104 ? -5.434  -4.481  1.194  1.00 56.85  ?  129 GLU   A HB3    1 
ATOM   1670  H  HG2    . GLU   A 1 104 ? -3.380  -5.486  1.106  1.00 60.90  ?  129 GLU   A HG2    1 
ATOM   1671  H  HG3    . GLU   A 1 104 ? -4.010  -6.875  1.554  1.00 60.90  ?  129 GLU   A HG3    1 
ATOM   1672  N  N      . HIS   A 1 105 ? -2.957  -4.882  4.066  1.00 41.87  ?  130 HIS   A N      1 
ATOM   1673  C  CA     . HIS   A 1 105 ? -1.618  -4.329  4.237  1.00 42.44  ?  130 HIS   A CA     1 
ATOM   1674  C  C      . HIS   A 1 105 ? -0.910  -4.294  2.889  1.00 44.31  ?  130 HIS   A C      1 
ATOM   1675  O  O      . HIS   A 1 105 ? -0.709  -5.340  2.264  1.00 45.99  ?  130 HIS   A O      1 
ATOM   1676  C  CB     . HIS   A 1 105 ? -0.887  -5.213  5.237  1.00 40.45  ?  130 HIS   A CB     1 
ATOM   1677  C  CG     . HIS   A 1 105 ? 0.337   -4.610  5.839  1.00 40.39  ?  130 HIS   A CG     1 
ATOM   1678  N  ND1    . HIS   A 1 105 ? 1.519   -4.463  5.147  1.00 40.69  ?  130 HIS   A ND1    1 
ATOM   1679  C  CD2    . HIS   A 1 105 ? 0.582   -4.181  7.100  1.00 38.35  ?  130 HIS   A CD2    1 
ATOM   1680  C  CE1    . HIS   A 1 105 ? 2.435   -3.950  5.950  1.00 40.59  ?  130 HIS   A CE1    1 
ATOM   1681  N  NE2    . HIS   A 1 105 ? 1.891   -3.767  7.140  1.00 39.19  ?  130 HIS   A NE2    1 
ATOM   1682  H  H      . HIS   A 1 105 ? -3.050  -5.658  4.426  1.00 50.24  ?  130 HIS   A H      1 
ATOM   1683  H  HA     . HIS   A 1 105 ? -1.641  -3.419  4.571  1.00 50.92  ?  130 HIS   A HA     1 
ATOM   1684  H  HB2    . HIS   A 1 105 ? -1.495  -5.422  5.963  1.00 48.53  ?  130 HIS   A HB2    1 
ATOM   1685  H  HB3    . HIS   A 1 105 ? -0.617  -6.028  4.785  1.00 48.53  ?  130 HIS   A HB3    1 
ATOM   1686  H  HD2    . HIS   A 1 105 ? -0.023  -4.168  7.806  1.00 46.01  ?  130 HIS   A HD2    1 
ATOM   1687  H  HE1    . HIS   A 1 105 ? 3.313   -3.751  5.717  1.00 48.70  ?  130 HIS   A HE1    1 
ATOM   1688  H  HE2    . HIS   A 1 105 ? 2.291   -3.441  7.828  1.00 47.02  ?  130 HIS   A HE2    1 
ATOM   1689  N  N      . LYS   A 1 106 ? -0.512  -3.096  2.446  1.00 44.23  ?  131 LYS   A N      1 
ATOM   1690  C  CA     A LYS   A 1 106 ? -0.024  -2.939  1.080  0.55 45.04  ?  131 LYS   A CA     1 
ATOM   1691  C  CA     B LYS   A 1 106 ? -0.026  -2.943  1.078  0.45 43.76  ?  131 LYS   A CA     1 
ATOM   1692  C  C      . LYS   A 1 106 ? 1.379   -3.504  0.881  1.00 45.45  ?  131 LYS   A C      1 
ATOM   1693  O  O      . LYS   A 1 106 ? 1.772   -3.761  -0.263 1.00 47.33  ?  131 LYS   A O      1 
ATOM   1694  C  CB     A LYS   A 1 106 ? -0.023  -1.461  0.678  0.55 45.24  ?  131 LYS   A CB     1 
ATOM   1695  C  CB     B LYS   A 1 106 ? -0.040  -1.470  0.658  0.45 41.43  ?  131 LYS   A CB     1 
ATOM   1696  C  CG     A LYS   A 1 106 ? -1.389  -0.798  0.632  0.55 45.27  ?  131 LYS   A CG     1 
ATOM   1697  C  CG     B LYS   A 1 106 ? -1.348  -0.736  0.921  0.45 39.12  ?  131 LYS   A CG     1 
ATOM   1698  C  CD     A LYS   A 1 106 ? -1.252  0.704   0.382  0.55 44.64  ?  131 LYS   A CD     1 
ATOM   1699  C  CD     B LYS   A 1 106 ? -2.555  -1.471  0.354  0.45 36.66  ?  131 LYS   A CD     1 
ATOM   1700  C  CE     A LYS   A 1 106 ? -2.587  1.341   0.039  0.55 44.41  ?  131 LYS   A CE     1 
ATOM   1701  C  CE     B LYS   A 1 106 ? -3.838  -0.767  0.758  0.45 35.26  ?  131 LYS   A CE     1 
ATOM   1702  N  NZ     A LYS   A 1 106 ? -3.607  1.164   1.106  0.55 44.34  ?  131 LYS   A NZ     1 
ATOM   1703  N  NZ     B LYS   A 1 106 ? -4.960  -1.704  1.007  0.45 34.19  ?  131 LYS   A NZ     1 
ATOM   1704  H  H      . LYS   A 1 106 ? -0.515  -2.372  2.910  1.00 53.07  ?  131 LYS   A H      1 
ATOM   1705  H  HA     . LYS   A 1 106 ? -0.631  -3.419  0.496  1.00 52.50  ?  131 LYS   A HA     1 
ATOM   1706  H  HB2    A LYS   A 1 106 ? 0.516   -0.971  1.319  0.55 54.28  ?  131 LYS   A HB2    1 
ATOM   1707  H  HB2    B LYS   A 1 106 ? 0.658   -1.006  1.146  0.45 49.71  ?  131 LYS   A HB2    1 
ATOM   1708  H  HB3    A LYS   A 1 106 ? 0.365   -1.386  -0.208 0.55 54.28  ?  131 LYS   A HB3    1 
ATOM   1709  H  HB3    B LYS   A 1 106 ? 0.134   -1.422  -0.295 0.45 49.71  ?  131 LYS   A HB3    1 
ATOM   1710  H  HG2    A LYS   A 1 106 ? -1.914  -1.183  -0.087 0.55 54.31  ?  131 LYS   A HG2    1 
ATOM   1711  H  HG2    B LYS   A 1 106 ? -1.474  -0.645  1.878  0.45 46.94  ?  131 LYS   A HG2    1 
ATOM   1712  H  HG3    A LYS   A 1 106 ? -1.842  -0.929  1.480  0.55 54.31  ?  131 LYS   A HG3    1 
ATOM   1713  H  HG3    B LYS   A 1 106 ? -1.308  0.141   0.507  0.45 46.94  ?  131 LYS   A HG3    1 
ATOM   1714  H  HD2    A LYS   A 1 106 ? -0.907  1.132   1.182  0.55 53.56  ?  131 LYS   A HD2    1 
ATOM   1715  H  HD2    B LYS   A 1 106 ? -2.502  -1.487  -0.614 0.45 43.99  ?  131 LYS   A HD2    1 
ATOM   1716  H  HD3    A LYS   A 1 106 ? -0.645  0.851   -0.360 0.55 53.56  ?  131 LYS   A HD3    1 
ATOM   1717  H  HD3    B LYS   A 1 106 ? -2.577  -2.377  0.700  0.45 43.99  ?  131 LYS   A HD3    1 
ATOM   1718  H  HE2    A LYS   A 1 106 ? -2.457  2.293   -0.095 0.55 53.28  ?  131 LYS   A HE2    1 
ATOM   1719  H  HE2    B LYS   A 1 106 ? -3.680  -0.267  1.574  0.45 42.30  ?  131 LYS   A HE2    1 
ATOM   1720  H  HE3    A LYS   A 1 106 ? -2.931  0.935   -0.772 0.55 53.28  ?  131 LYS   A HE3    1 
ATOM   1721  H  HE3    B LYS   A 1 106 ? -4.105  -0.164  0.047  0.45 42.30  ?  131 LYS   A HE3    1 
ATOM   1722  H  HZ1    A LYS   A 1 106 ? -4.369  1.559   0.867  0.55 53.21  ?  131 LYS   A HZ1    1 
ATOM   1723  H  HZ1    B LYS   A 1 106 ? -4.742  -2.274  1.654  0.45 41.02  ?  131 LYS   A HZ1    1 
ATOM   1724  H  HZ2    A LYS   A 1 106 ? -3.761  0.298   1.240  0.55 53.21  ?  131 LYS   A HZ2    1 
ATOM   1725  H  HZ2    B LYS   A 1 106 ? -5.686  -1.251  1.253  0.45 41.02  ?  131 LYS   A HZ2    1 
ATOM   1726  H  HZ3    A LYS   A 1 106 ? -3.319  1.528   1.865  0.55 53.21  ?  131 LYS   A HZ3    1 
ATOM   1727  H  HZ3    B LYS   A 1 106 ? -5.143  -2.163  0.267  0.45 41.02  ?  131 LYS   A HZ3    1 
ATOM   1728  N  N      . VAL   A 1 107 ? 2.147   -3.683  1.951  1.00 45.53  ?  132 VAL   A N      1 
ATOM   1729  C  CA     . VAL   A 1 107 ? 3.507   -4.205  1.831  1.00 45.49  ?  132 VAL   A CA     1 
ATOM   1730  C  C      . VAL   A 1 107 ? 3.524   -5.724  1.932  1.00 45.44  ?  132 VAL   A C      1 
ATOM   1731  O  O      . VAL   A 1 107 ? 4.149   -6.408  1.118  1.00 45.81  ?  132 VAL   A O      1 
ATOM   1732  C  CB     . VAL   A 1 107 ? 4.415   -3.553  2.899  1.00 45.58  ?  132 VAL   A CB     1 
ATOM   1733  C  CG1    . VAL   A 1 107 ? 5.793   -4.208  2.917  1.00 44.40  ?  132 VAL   A CG1    1 
ATOM   1734  C  CG2    . VAL   A 1 107 ? 4.535   -2.045  2.642  1.00 45.92  ?  132 VAL   A CG2    1 
ATOM   1735  H  H      . VAL   A 1 107 ? 1.906   -3.509  2.758  1.00 54.63  ?  132 VAL   A H      1 
ATOM   1736  H  HA     . VAL   A 1 107 ? 3.856   -3.966  0.958  1.00 54.59  ?  132 VAL   A HA     1 
ATOM   1737  H  HB     . VAL   A 1 107 ? 4.014   -3.686  3.772  1.00 54.69  ?  132 VAL   A HB     1 
ATOM   1738  H  HG11   . VAL   A 1 107 ? 6.407   -3.636  3.404  1.00 53.27  ?  132 VAL   A HG11   1 
ATOM   1739  H  HG12   . VAL   A 1 107 ? 5.726   -5.071  3.355  1.00 53.27  ?  132 VAL   A HG12   1 
ATOM   1740  H  HG13   . VAL   A 1 107 ? 6.100   -4.322  2.004  1.00 53.27  ?  132 VAL   A HG13   1 
ATOM   1741  H  HG21   . VAL   A 1 107 ? 5.088   -1.650  3.333  1.00 55.10  ?  132 VAL   A HG21   1 
ATOM   1742  H  HG22   . VAL   A 1 107 ? 4.941   -1.904  1.772  1.00 55.10  ?  132 VAL   A HG22   1 
ATOM   1743  H  HG23   . VAL   A 1 107 ? 3.649   -1.650  2.661  1.00 55.10  ?  132 VAL   A HG23   1 
ATOM   1744  N  N      . GLU   A 1 108 ? 2.814   -6.276  2.916  1.00 43.92  ?  133 GLU   A N      1 
ATOM   1745  C  CA     . GLU   A 1 108 ? 2.752   -7.718  3.114  1.00 44.16  ?  133 GLU   A CA     1 
ATOM   1746  C  C      . GLU   A 1 108 ? 1.652   -8.378  2.294  1.00 46.35  ?  133 GLU   A C      1 
ATOM   1747  O  O      . GLU   A 1 108 ? 1.596   -9.612  2.239  1.00 45.98  ?  133 GLU   A O      1 
ATOM   1748  C  CB     . GLU   A 1 108 ? 2.539   -8.039  4.597  1.00 42.95  ?  133 GLU   A CB     1 
ATOM   1749  C  CG     . GLU   A 1 108 ? 3.644   -7.537  5.512  1.00 43.85  ?  133 GLU   A CG     1 
ATOM   1750  C  CD     . GLU   A 1 108 ? 5.011   -8.076  5.144  1.00 46.49  ?  133 GLU   A CD     1 
ATOM   1751  O  OE1    . GLU   A 1 108 ? 5.096   -9.250  4.732  1.00 47.88  ?  133 GLU   A OE1    1 
ATOM   1752  O  OE2    . GLU   A 1 108 ? 5.996   -7.318  5.258  1.00 48.12  ?  133 GLU   A OE2    1 
ATOM   1753  H  H      . GLU   A 1 108 ? 2.354   -5.828  3.488  1.00 52.70  ?  133 GLU   A H      1 
ATOM   1754  H  HA     . GLU   A 1 108 ? 3.600   -8.105  2.846  1.00 52.99  ?  133 GLU   A HA     1 
ATOM   1755  H  HB2    . GLU   A 1 108 ? 1.709   -7.630  4.886  1.00 51.54  ?  133 GLU   A HB2    1 
ATOM   1756  H  HB3    . GLU   A 1 108 ? 2.488   -9.003  4.700  1.00 51.54  ?  133 GLU   A HB3    1 
ATOM   1757  H  HG2    . GLU   A 1 108 ? 3.680   -6.569  5.460  1.00 52.61  ?  133 GLU   A HG2    1 
ATOM   1758  H  HG3    . GLU   A 1 108 ? 3.449   -7.813  6.421  1.00 52.61  ?  133 GLU   A HG3    1 
ATOM   1759  N  N      . LYS   A 1 109 ? 0.782   -7.586  1.663  1.00 49.17  ?  134 LYS   A N      1 
ATOM   1760  C  CA     . LYS   A 1 109 ? -0.223  -8.089  0.724  1.00 50.55  ?  134 LYS   A CA     1 
ATOM   1761  C  C      . LYS   A 1 109 ? -1.140  -9.125  1.380  1.00 50.74  ?  134 LYS   A C      1 
ATOM   1762  O  O      . LYS   A 1 109 ? -1.382  -10.211 0.846  1.00 51.18  ?  134 LYS   A O      1 
ATOM   1763  C  CB     . LYS   A 1 109 ? 0.449   -8.657  -0.534 1.00 52.42  ?  134 LYS   A CB     1 
ATOM   1764  C  CG     . LYS   A 1 109 ? 1.191   -7.621  -1.397 1.00 55.19  ?  134 LYS   A CG     1 
ATOM   1765  C  CD     . LYS   A 1 109 ? 0.263   -6.513  -1.897 1.00 57.09  ?  134 LYS   A CD     1 
ATOM   1766  C  CE     . LYS   A 1 109 ? 0.974   -5.558  -2.854 1.00 59.61  ?  134 LYS   A CE     1 
ATOM   1767  N  NZ     . LYS   A 1 109 ? 0.440   -4.161  -2.768 1.00 60.69  ?  134 LYS   A NZ     1 
ATOM   1768  H  H      . LYS   A 1 109 ? 0.753   -6.733  1.765  1.00 59.00  ?  134 LYS   A H      1 
ATOM   1769  H  HA     . LYS   A 1 109 ? -0.787  -7.347  0.456  1.00 60.65  ?  134 LYS   A HA     1 
ATOM   1770  H  HB2    . LYS   A 1 109 ? 1.096   -9.326  -0.261 1.00 62.90  ?  134 LYS   A HB2    1 
ATOM   1771  H  HB3    . LYS   A 1 109 ? -0.234  -9.064  -1.090 1.00 62.90  ?  134 LYS   A HB3    1 
ATOM   1772  H  HG2    . LYS   A 1 109 ? 1.893   -7.211  -0.868 1.00 66.23  ?  134 LYS   A HG2    1 
ATOM   1773  H  HG3    . LYS   A 1 109 ? 1.573   -8.065  -2.169 1.00 66.23  ?  134 LYS   A HG3    1 
ATOM   1774  H  HD2    . LYS   A 1 109 ? -0.485  -6.912  -2.367 1.00 68.50  ?  134 LYS   A HD2    1 
ATOM   1775  H  HD3    . LYS   A 1 109 ? -0.057  -5.999  -1.139 1.00 68.50  ?  134 LYS   A HD3    1 
ATOM   1776  H  HE2    . LYS   A 1 109 ? 1.919   -5.534  -2.636 1.00 71.53  ?  134 LYS   A HE2    1 
ATOM   1777  H  HE3    . LYS   A 1 109 ? 0.852   -5.871  -3.764 1.00 71.53  ?  134 LYS   A HE3    1 
ATOM   1778  H  HZ1    . LYS   A 1 109 ? 0.551   -3.843  -1.944 1.00 72.82  ?  134 LYS   A HZ1    1 
ATOM   1779  H  HZ2    . LYS   A 1 109 ? 0.871   -3.634  -3.342 1.00 72.82  ?  134 LYS   A HZ2    1 
ATOM   1780  H  HZ3    . LYS   A 1 109 ? -0.428  -4.153  -2.965 1.00 72.82  ?  134 LYS   A HZ3    1 
ATOM   1781  N  N      . MET   A 1 110 ? -1.660  -8.773  2.554  1.00 48.97  ?  135 MET   A N      1 
ATOM   1782  C  CA     . MET   A 1 110 ? -2.703  -9.554  3.209  1.00 48.35  ?  135 MET   A CA     1 
ATOM   1783  C  C      . MET   A 1 110 ? -3.381  -8.660  4.241  1.00 44.54  ?  135 MET   A C      1 
ATOM   1784  O  O      . MET   A 1 110 ? -2.849  -7.617  4.634  1.00 44.19  ?  135 MET   A O      1 
ATOM   1785  C  CB     . MET   A 1 110 ? -2.144  -10.831 3.859  1.00 51.27  ?  135 MET   A CB     1 
ATOM   1786  C  CG     . MET   A 1 110 ? -1.237  -10.617 5.055  1.00 52.88  ?  135 MET   A CG     1 
ATOM   1787  S  SD     . MET   A 1 110 ? -0.622  -12.142 5.831  1.00 54.00  ?  135 MET   A SD     1 
ATOM   1788  C  CE     . MET   A 1 110 ? -2.108  -13.136 5.830  1.00 55.84  ?  135 MET   A CE     1 
ATOM   1789  H  H      . MET   A 1 110 ? -1.422  -8.075  2.997  1.00 58.76  ?  135 MET   A H      1 
ATOM   1790  H  HA     . MET   A 1 110 ? -3.358  -9.835  2.551  1.00 58.01  ?  135 MET   A HA     1 
ATOM   1791  H  HB2    . MET   A 1 110 ? -2.891  -11.373 4.157  1.00 61.51  ?  135 MET   A HB2    1 
ATOM   1792  H  HB3    . MET   A 1 110 ? -1.631  -11.313 3.191  1.00 61.51  ?  135 MET   A HB3    1 
ATOM   1793  H  HG2    . MET   A 1 110 ? -0.464  -10.105 4.769  1.00 63.45  ?  135 MET   A HG2    1 
ATOM   1794  H  HG3    . MET   A 1 110 ? -1.729  -10.125 5.731  1.00 63.45  ?  135 MET   A HG3    1 
ATOM   1795  H  HE1    . MET   A 1 110 ? -1.954  -13.936 6.357  1.00 67.00  ?  135 MET   A HE1    1 
ATOM   1796  H  HE2    . MET   A 1 110 ? -2.833  -12.620 6.215  1.00 67.00  ?  135 MET   A HE2    1 
ATOM   1797  H  HE3    . MET   A 1 110 ? -2.324  -13.380 4.916  1.00 67.00  ?  135 MET   A HE3    1 
ATOM   1798  N  N      . TYR   A 1 111 ? -4.576  -9.073  4.658  1.00 42.35  ?  136 TYR   A N      1 
ATOM   1799  C  CA     . TYR   A 1 111 ? -5.358  -8.279  5.596  1.00 40.30  ?  136 TYR   A CA     1 
ATOM   1800  C  C      . TYR   A 1 111 ? -4.669  -8.206  6.948  1.00 39.41  ?  136 TYR   A C      1 
ATOM   1801  O  O      . TYR   A 1 111 ? -4.055  -9.173  7.406  1.00 39.71  ?  136 TYR   A O      1 
ATOM   1802  C  CB     . TYR   A 1 111 ? -6.759  -8.861  5.739  1.00 40.38  ?  136 TYR   A CB     1 
ATOM   1803  C  CG     . TYR   A 1 111 ? -7.684  -8.233  4.734  1.00 43.55  ?  136 TYR   A CG     1 
ATOM   1804  C  CD1    . TYR   A 1 111 ? -7.483  -8.426  3.377  1.00 46.09  ?  136 TYR   A CD1    1 
ATOM   1805  C  CD2    . TYR   A 1 111 ? -8.731  -7.414  5.135  1.00 43.74  ?  136 TYR   A CD2    1 
ATOM   1806  C  CE1    . TYR   A 1 111 ? -8.304  -7.838  2.452  1.00 47.31  ?  136 TYR   A CE1    1 
ATOM   1807  C  CE2    . TYR   A 1 111 ? -9.562  -6.825  4.216  1.00 45.52  ?  136 TYR   A CE2    1 
ATOM   1808  C  CZ     . TYR   A 1 111 ? -9.342  -7.039  2.878  1.00 47.95  ?  136 TYR   A CZ     1 
ATOM   1809  O  OH     . TYR   A 1 111 ? -10.166 -6.455  1.957  1.00 51.21  ?  136 TYR   A OH     1 
ATOM   1810  H  H      . TYR   A 1 111 ? -4.953  -9.807  4.414  1.00 50.81  ?  136 TYR   A H      1 
ATOM   1811  H  HA     . TYR   A 1 111 ? -5.444  -7.374  5.260  1.00 48.36  ?  136 TYR   A HA     1 
ATOM   1812  H  HB2    . TYR   A 1 111 ? -6.732  -9.818  5.583  1.00 48.45  ?  136 TYR   A HB2    1 
ATOM   1813  H  HB3    . TYR   A 1 111 ? -7.098  -8.680  6.630  1.00 48.45  ?  136 TYR   A HB3    1 
ATOM   1814  H  HD1    . TYR   A 1 111 ? -6.779  -8.962  3.090  1.00 55.30  ?  136 TYR   A HD1    1 
ATOM   1815  H  HD2    . TYR   A 1 111 ? -8.871  -7.261  6.042  1.00 52.48  ?  136 TYR   A HD2    1 
ATOM   1816  H  HE1    . TYR   A 1 111 ? -8.162  -7.977  1.544  1.00 56.76  ?  136 TYR   A HE1    1 
ATOM   1817  H  HE2    . TYR   A 1 111 ? -10.266 -6.287  4.497  1.00 54.62  ?  136 TYR   A HE2    1 
ATOM   1818  H  HH     . TYR   A 1 111 ? -10.725 -5.961  2.343  1.00 61.45  ?  136 TYR   A HH     1 
ATOM   1819  N  N      . VAL   A 1 112 ? -4.772  -7.043  7.588  1.00 37.37  ?  137 VAL   A N      1 
ATOM   1820  C  CA     . VAL   A 1 112 ? -3.961  -6.790  8.778  1.00 35.61  ?  137 VAL   A CA     1 
ATOM   1821  C  C      . VAL   A 1 112 ? -4.212  -7.826  9.865  1.00 35.40  ?  137 VAL   A C      1 
ATOM   1822  O  O      . VAL   A 1 112 ? -3.233  -8.334  10.439 1.00 35.89  ?  137 VAL   A O      1 
ATOM   1823  C  CB     . VAL   A 1 112 ? -4.196  -5.354  9.283  1.00 37.84  ?  137 VAL   A CB     1 
ATOM   1824  C  CG1    . VAL   A 1 112 ? -3.456  -5.141  10.609 1.00 37.25  ?  137 VAL   A CG1    1 
ATOM   1825  C  CG2    . VAL   A 1 112 ? -3.720  -4.347  8.258  1.00 39.29  ?  137 VAL   A CG2    1 
ATOM   1826  H  H      . VAL   A 1 112 ? -5.291  -6.397  7.359  1.00 44.84  ?  137 VAL   A H      1 
ATOM   1827  H  HA     . VAL   A 1 112 ? -3.032  -6.860  8.508  1.00 42.73  ?  137 VAL   A HA     1 
ATOM   1828  H  HB     . VAL   A 1 112 ? -5.146  -5.219  9.426  1.00 45.40  ?  137 VAL   A HB     1 
ATOM   1829  H  HG11   . VAL   A 1 112 ? -3.394  -4.189  10.787 1.00 44.70  ?  137 VAL   A HG11   1 
ATOM   1830  H  HG12   . VAL   A 1 112 ? -3.951  -5.578  11.320 1.00 44.70  ?  137 VAL   A HG12   1 
ATOM   1831  H  HG13   . VAL   A 1 112 ? -2.568  -5.524  10.540 1.00 44.70  ?  137 VAL   A HG13   1 
ATOM   1832  H  HG21   . VAL   A 1 112 ? -3.898  -3.453  8.588  1.00 47.14  ?  137 VAL   A HG21   1 
ATOM   1833  H  HG22   . VAL   A 1 112 ? -2.768  -4.465  8.118  1.00 47.14  ?  137 VAL   A HG22   1 
ATOM   1834  H  HG23   . VAL   A 1 112 ? -4.198  -4.494  7.426  1.00 47.14  ?  137 VAL   A HG23   1 
ATOM   1835  N  N      . PRO   A 1 113 ? -5.454  -8.159  10.225 1.00 34.99  ?  138 PRO   A N      1 
ATOM   1836  C  CA     . PRO   A 1 113 ? -5.637  -9.159  11.294 1.00 36.46  ?  138 PRO   A CA     1 
ATOM   1837  C  C      . PRO   A 1 113 ? -4.993  -10.490 10.960 1.00 36.26  ?  138 PRO   A C      1 
ATOM   1838  O  O      . PRO   A 1 113 ? -4.407  -11.132 11.840 1.00 35.94  ?  138 PRO   A O      1 
ATOM   1839  C  CB     . PRO   A 1 113 ? -7.162  -9.277  11.423 1.00 36.41  ?  138 PRO   A CB     1 
ATOM   1840  C  CG     . PRO   A 1 113 ? -7.690  -7.941  10.878 1.00 36.84  ?  138 PRO   A CG     1 
ATOM   1841  C  CD     . PRO   A 1 113 ? -6.732  -7.575  9.766  1.00 35.76  ?  138 PRO   A CD     1 
ATOM   1842  H  HA     . PRO   A 1 113 ? -5.279  -8.820  12.129 1.00 43.75  ?  138 PRO   A HA     1 
ATOM   1843  H  HB2    . PRO   A 1 113 ? -7.484  -10.023 10.893 1.00 43.69  ?  138 PRO   A HB2    1 
ATOM   1844  H  HB3    . PRO   A 1 113 ? -7.409  -9.398  12.352 1.00 43.69  ?  138 PRO   A HB3    1 
ATOM   1845  H  HG2    . PRO   A 1 113 ? -8.591  -8.054  10.537 1.00 44.20  ?  138 PRO   A HG2    1 
ATOM   1846  H  HG3    . PRO   A 1 113 ? -7.682  -7.270  11.578 1.00 44.20  ?  138 PRO   A HG3    1 
ATOM   1847  H  HD2    . PRO   A 1 113 ? -7.011  -7.969  8.924  1.00 42.90  ?  138 PRO   A HD2    1 
ATOM   1848  H  HD3    . PRO   A 1 113 ? -6.660  -6.612  9.673  1.00 42.90  ?  138 PRO   A HD3    1 
ATOM   1849  N  N      . ALA   A 1 114 ? -5.076  -10.920 9.698  1.00 36.28  ?  139 ALA   A N      1 
ATOM   1850  C  CA     . ALA   A 1 114 ? -4.470  -12.191 9.315  1.00 36.51  ?  139 ALA   A CA     1 
ATOM   1851  C  C      . ALA   A 1 114 ? -2.949  -12.113 9.422  1.00 36.43  ?  139 ALA   A C      1 
ATOM   1852  O  O      . ALA   A 1 114 ? -2.290  -13.089 9.805  1.00 37.05  ?  139 ALA   A O      1 
ATOM   1853  C  CB     . ALA   A 1 114 ? -4.901  -12.576 7.901  1.00 37.73  ?  139 ALA   A CB     1 
ATOM   1854  H  H      . ALA   A 1 114 ? -5.470  -10.502 9.058  1.00 43.53  ?  139 ALA   A H      1 
ATOM   1855  H  HA     . ALA   A 1 114 ? -4.781  -12.888 9.914  1.00 43.80  ?  139 ALA   A HA     1 
ATOM   1856  H  HB1    . ALA   A 1 114 ? -4.459  -13.402 7.650  1.00 45.27  ?  139 ALA   A HB1    1 
ATOM   1857  H  HB2    . ALA   A 1 114 ? -5.863  -12.699 7.887  1.00 45.27  ?  139 ALA   A HB2    1 
ATOM   1858  H  HB3    . ALA   A 1 114 ? -4.649  -11.867 7.290  1.00 45.27  ?  139 ALA   A HB3    1 
ATOM   1859  N  N      . LEU   A 1 115 ? -2.374  -10.948 9.095  1.00 34.90  ?  140 LEU   A N      1 
ATOM   1860  C  CA     . LEU   A 1 115 ? -0.932  -10.749 9.210  1.00 34.89  ?  140 LEU   A CA     1 
ATOM   1861  C  C      . LEU   A 1 115 ? -0.455  -10.874 10.648 1.00 33.18  ?  140 LEU   A C      1 
ATOM   1862  O  O      . LEU   A 1 115 ? 0.514   -11.585 10.938 1.00 34.47  ?  140 LEU   A O      1 
ATOM   1863  C  CB     . LEU   A 1 115 ? -0.561  -9.360  8.684  1.00 36.54  ?  140 LEU   A CB     1 
ATOM   1864  C  CG     . LEU   A 1 115 ? 0.883   -8.891  8.882  1.00 37.08  ?  140 LEU   A CG     1 
ATOM   1865  C  CD1    . LEU   A 1 115 ? 1.866   -9.748  8.085  1.00 37.51  ?  140 LEU   A CD1    1 
ATOM   1866  C  CD2    . LEU   A 1 115 ? 1.013   -7.426  8.488  1.00 38.29  ?  140 LEU   A CD2    1 
ATOM   1867  H  H      . LEU   A 1 115 ? -2.800  -10.259 8.804  1.00 41.87  ?  140 LEU   A H      1 
ATOM   1868  H  HA     . LEU   A 1 115 ? -0.493  -11.432 8.679  1.00 41.86  ?  140 LEU   A HA     1 
ATOM   1869  H  HB2    . LEU   A 1 115 ? -0.731  -9.350  7.729  1.00 43.84  ?  140 LEU   A HB2    1 
ATOM   1870  H  HB3    . LEU   A 1 115 ? -1.130  -8.713  9.130  1.00 43.84  ?  140 LEU   A HB3    1 
ATOM   1871  H  HG     . LEU   A 1 115 ? 1.113   -8.986  9.820  1.00 44.49  ?  140 LEU   A HG     1 
ATOM   1872  H  HD11   . LEU   A 1 115 ? 2.766   -9.420  8.237  1.00 45.00  ?  140 LEU   A HD11   1 
ATOM   1873  H  HD12   . LEU   A 1 115 ? 1.795   -10.669 8.381  1.00 45.00  ?  140 LEU   A HD12   1 
ATOM   1874  H  HD13   . LEU   A 1 115 ? 1.647   -9.686  7.142  1.00 45.00  ?  140 LEU   A HD13   1 
ATOM   1875  H  HD21   . LEU   A 1 115 ? 1.933   -7.147  8.612  1.00 45.95  ?  140 LEU   A HD21   1 
ATOM   1876  H  HD22   . LEU   A 1 115 ? 0.759   -7.326  7.558  1.00 45.95  ?  140 LEU   A HD22   1 
ATOM   1877  H  HD23   . LEU   A 1 115 ? 0.427   -6.895  9.050  1.00 45.95  ?  140 LEU   A HD23   1 
ATOM   1878  N  N      . ILE   A 1 116 ? -1.078  -10.130 11.558 1.00 30.74  ?  141 ILE   A N      1 
ATOM   1879  C  CA     . ILE   A 1 116 ? -0.512  -10.008 12.901 1.00 29.39  ?  141 ILE   A CA     1 
ATOM   1880  C  C      . ILE   A 1 116 ? -0.956  -11.109 13.852 1.00 29.06  ?  141 ILE   A C      1 
ATOM   1881  O  O      . ILE   A 1 116 ? -0.417  -11.193 14.968 1.00 27.79  ?  141 ILE   A O      1 
ATOM   1882  C  CB     . ILE   A 1 116 ? -0.819  -8.606  13.473 1.00 30.16  ?  141 ILE   A CB     1 
ATOM   1883  C  CG1    . ILE   A 1 116 ? -2.311  -8.409  13.753 1.00 30.51  ?  141 ILE   A CG1    1 
ATOM   1884  C  CG2    . ILE   A 1 116 ? -0.335  -7.529  12.488 1.00 31.25  ?  141 ILE   A CG2    1 
ATOM   1885  C  CD1    . ILE   A 1 116 ? -2.677  -6.987  14.236 1.00 30.95  ?  141 ILE   A CD1    1 
ATOM   1886  H  H      . ILE   A 1 116 ? -1.810  -9.697  11.427 1.00 36.88  ?  141 ILE   A H      1 
ATOM   1887  H  HA     . ILE   A 1 116 ? 0.452   -10.101 12.842 1.00 35.26  ?  141 ILE   A HA     1 
ATOM   1888  H  HB     . ILE   A 1 116 ? -0.348  -8.530  14.318 1.00 36.19  ?  141 ILE   A HB     1 
ATOM   1889  H  HG12   . ILE   A 1 116 ? -2.805  -8.580  12.936 1.00 36.61  ?  141 ILE   A HG12   1 
ATOM   1890  H  HG13   . ILE   A 1 116 ? -2.583  -9.034  14.443 1.00 36.61  ?  141 ILE   A HG13   1 
ATOM   1891  H  HG21   . ILE   A 1 116 ? -0.312  -6.673  12.943 1.00 37.50  ?  141 ILE   A HG21   1 
ATOM   1892  H  HG22   . ILE   A 1 116 ? 0.553   -7.762  12.176 1.00 37.50  ?  141 ILE   A HG22   1 
ATOM   1893  H  HG23   . ILE   A 1 116 ? -0.949  -7.488  11.738 1.00 37.50  ?  141 ILE   A HG23   1 
ATOM   1894  H  HD11   . ILE   A 1 116 ? -3.589  -6.991  14.565 1.00 37.13  ?  141 ILE   A HD11   1 
ATOM   1895  H  HD12   . ILE   A 1 116 ? -2.070  -6.729  14.946 1.00 37.13  ?  141 ILE   A HD12   1 
ATOM   1896  H  HD13   . ILE   A 1 116 ? -2.596  -6.371  13.491 1.00 37.13  ?  141 ILE   A HD13   1 
ATOM   1897  N  N      . PHE   A 1 117 ? -1.892  -11.977 13.450 1.00 29.41  ?  142 PHE   A N      1 
ATOM   1898  C  CA     . PHE   A 1 117 ? -2.207  -13.165 14.237 1.00 29.86  ?  142 PHE   A CA     1 
ATOM   1899  C  C      . PHE   A 1 117 ? -1.723  -14.467 13.604 1.00 29.62  ?  142 PHE   A C      1 
ATOM   1900  O  O      . PHE   A 1 117 ? -1.702  -15.496 14.290 1.00 29.08  ?  142 PHE   A O      1 
ATOM   1901  C  CB     . PHE   A 1 117 ? -3.723  -13.262 14.488 1.00 30.46  ?  142 PHE   A CB     1 
ATOM   1902  C  CG     . PHE   A 1 117 ? -4.231  -12.277 15.512 1.00 30.90  ?  142 PHE   A CG     1 
ATOM   1903  C  CD1    . PHE   A 1 117 ? -4.183  -12.589 16.862 1.00 31.43  ?  142 PHE   A CD1    1 
ATOM   1904  C  CD2    . PHE   A 1 117 ? -4.730  -11.035 15.134 1.00 31.52  ?  142 PHE   A CD2    1 
ATOM   1905  C  CE1    . PHE   A 1 117 ? -4.625  -11.699 17.820 1.00 30.84  ?  142 PHE   A CE1    1 
ATOM   1906  C  CE2    . PHE   A 1 117 ? -5.177  -10.126 16.096 1.00 31.16  ?  142 PHE   A CE2    1 
ATOM   1907  C  CZ     . PHE   A 1 117 ? -5.124  -10.461 17.440 1.00 29.89  ?  142 PHE   A CZ     1 
ATOM   1908  H  H      . PHE   A 1 117 ? -2.353  -11.895 12.729 1.00 35.29  ?  142 PHE   A H      1 
ATOM   1909  H  HA     . PHE   A 1 117 ? -1.770  -13.078 15.099 1.00 35.83  ?  142 PHE   A HA     1 
ATOM   1910  H  HB2    . PHE   A 1 117 ? -4.189  -13.089 13.655 1.00 36.55  ?  142 PHE   A HB2    1 
ATOM   1911  H  HB3    . PHE   A 1 117 ? -3.931  -14.154 14.806 1.00 36.55  ?  142 PHE   A HB3    1 
ATOM   1912  H  HD1    . PHE   A 1 117 ? -3.846  -13.415 17.127 1.00 37.71  ?  142 PHE   A HD1    1 
ATOM   1913  H  HD2    . PHE   A 1 117 ? -4.765  -10.808 14.233 1.00 37.82  ?  142 PHE   A HD2    1 
ATOM   1914  H  HE1    . PHE   A 1 117 ? -4.589  -11.928 18.720 1.00 37.00  ?  142 PHE   A HE1    1 
ATOM   1915  H  HE2    . PHE   A 1 117 ? -5.510  -9.297  15.835 1.00 37.38  ?  142 PHE   A HE2    1 
ATOM   1916  H  HZ     . PHE   A 1 117 ? -5.421  -9.859  18.083 1.00 35.86  ?  142 PHE   A HZ     1 
ATOM   1917  N  N      . GLY   A 1 118 ? -1.320  -14.450 12.330 1.00 30.29  ?  143 GLY   A N      1 
ATOM   1918  C  CA     . GLY   A 1 118 ? -0.963  -15.677 11.645 1.00 31.68  ?  143 GLY   A CA     1 
ATOM   1919  C  C      . GLY   A 1 118 ? 0.439   -15.754 11.072 1.00 31.97  ?  143 GLY   A C      1 
ATOM   1920  O  O      . GLY   A 1 118 ? 0.809   -16.785 10.497 1.00 32.80  ?  143 GLY   A O      1 
ATOM   1921  H  H      . GLY   A 1 118 ? -1.247  -13.740 11.850 1.00 36.34  ?  143 GLY   A H      1 
ATOM   1922  H  HA2    . GLY   A 1 118 ? -1.058  -16.413 12.271 1.00 38.01  ?  143 GLY   A HA2    1 
ATOM   1923  H  HA3    . GLY   A 1 118 ? -1.582  -15.806 10.910 1.00 38.01  ?  143 GLY   A HA3    1 
ATOM   1924  N  N      . GLN   A 1 119 ? 1.218   -14.677 11.206 1.00 31.20  ?  144 GLN   A N      1 
ATOM   1925  C  CA     . GLN   A 1 119 ? 2.600   -14.627 10.743 1.00 31.01  ?  144 GLN   A CA     1 
ATOM   1926  C  C      . GLN   A 1 119 ? 3.504   -14.242 11.904 1.00 28.87  ?  144 GLN   A C      1 
ATOM   1927  O  O      . GLN   A 1 119 ? 3.206   -13.284 12.623 1.00 28.90  ?  144 GLN   A O      1 
ATOM   1928  C  CB     . GLN   A 1 119 ? 2.775   -13.612 9.613  1.00 33.07  ?  144 GLN   A CB     1 
ATOM   1929  C  CG     . GLN   A 1 119 ? 1.877   -13.841 8.421  1.00 36.74  ?  144 GLN   A CG     1 
ATOM   1930  C  CD     . GLN   A 1 119 ? 2.247   -15.084 7.670  1.00 39.51  ?  144 GLN   A CD     1 
ATOM   1931  O  OE1    . GLN   A 1 119 ? 3.427   -15.365 7.457  1.00 41.38  ?  144 GLN   A OE1    1 
ATOM   1932  N  NE2    . GLN   A 1 119 ? 1.244   -15.857 7.276  1.00 39.64  ?  144 GLN   A NE2    1 
ATOM   1933  H  H      . GLN   A 1 119 ? 0.957   -13.944 11.573 1.00 37.43  ?  144 GLN   A H      1 
ATOM   1934  H  HA     . GLN   A 1 119 ? 2.854   -15.505 10.418 1.00 37.21  ?  144 GLN   A HA     1 
ATOM   1935  H  HB2    . GLN   A 1 119 ? 2.581   -12.727 9.960  1.00 39.68  ?  144 GLN   A HB2    1 
ATOM   1936  H  HB3    . GLN   A 1 119 ? 3.692   -13.653 9.301  1.00 39.68  ?  144 GLN   A HB3    1 
ATOM   1937  H  HG2    . GLN   A 1 119 ? 0.961   -13.932 8.725  1.00 44.09  ?  144 GLN   A HG2    1 
ATOM   1938  H  HG3    . GLN   A 1 119 ? 1.953   -13.087 7.815  1.00 44.09  ?  144 GLN   A HG3    1 
ATOM   1939  H  HE21   . GLN   A 1 119 ? 0.433   -15.633 7.455  1.00 47.56  ?  144 GLN   A HE21   1 
ATOM   1940  H  HE22   . GLN   A 1 119 ? 1.404   -16.581 6.842  1.00 47.56  ?  144 GLN   A HE22   1 
ATOM   1941  N  N      . LEU   A 1 120 ? 4.594   -14.981 12.096 1.00 28.37  ?  145 LEU   A N      1 
ATOM   1942  C  CA     . LEU   A 1 120 ? 5.516   -14.673 13.183 1.00 28.20  ?  145 LEU   A CA     1 
ATOM   1943  C  C      . LEU   A 1 120 ? 6.220   -13.338 12.961 1.00 26.72  ?  145 LEU   A C      1 
ATOM   1944  O  O      . LEU   A 1 120 ? 6.401   -12.883 11.827 1.00 28.93  ?  145 LEU   A O      1 
ATOM   1945  C  CB     . LEU   A 1 120 ? 6.569   -15.773 13.319 1.00 28.86  ?  145 LEU   A CB     1 
ATOM   1946  C  CG     . LEU   A 1 120 ? 6.022   -17.128 13.768 1.00 29.63  ?  145 LEU   A CG     1 
ATOM   1947  C  CD1    . LEU   A 1 120 ? 7.022   -18.243 13.504 1.00 30.86  ?  145 LEU   A CD1    1 
ATOM   1948  C  CD2    . LEU   A 1 120 ? 5.669   -17.067 15.244 1.00 30.35  ?  145 LEU   A CD2    1 
ATOM   1949  H  H      . LEU   A 1 120 ? 4.818   -15.658 11.617 1.00 34.03  ?  145 LEU   A H      1 
ATOM   1950  H  HA     . LEU   A 1 120 ? 5.008   -14.616 14.007 1.00 33.83  ?  145 LEU   A HA     1 
ATOM   1951  H  HB2    . LEU   A 1 120 ? 6.995   -15.899 12.457 1.00 34.62  ?  145 LEU   A HB2    1 
ATOM   1952  H  HB3    . LEU   A 1 120 ? 7.225   -15.490 13.975 1.00 34.62  ?  145 LEU   A HB3    1 
ATOM   1953  H  HG     . LEU   A 1 120 ? 5.223   -17.334 13.258 1.00 35.55  ?  145 LEU   A HG     1 
ATOM   1954  H  HD11   . LEU   A 1 120 ? 6.644   -19.083 13.806 1.00 37.02  ?  145 LEU   A HD11   1 
ATOM   1955  H  HD12   . LEU   A 1 120 ? 7.204   -18.285 12.552 1.00 37.02  ?  145 LEU   A HD12   1 
ATOM   1956  H  HD13   . LEU   A 1 120 ? 7.841   -18.054 13.989 1.00 37.02  ?  145 LEU   A HD13   1 
ATOM   1957  H  HD21   . LEU   A 1 120 ? 5.386   -17.947 15.538 1.00 36.41  ?  145 LEU   A HD21   1 
ATOM   1958  H  HD22   . LEU   A 1 120 ? 6.451   -16.786 15.745 1.00 36.41  ?  145 LEU   A HD22   1 
ATOM   1959  H  HD23   . LEU   A 1 120 ? 4.949   -16.429 15.370 1.00 36.41  ?  145 LEU   A HD23   1 
ATOM   1960  N  N      . LEU   A 1 121 ? 6.627   -12.717 14.079 1.00 26.70  ?  146 LEU   A N      1 
ATOM   1961  C  CA     . LEU   A 1 121 ? 7.418   -11.482 14.097 1.00 27.05  ?  146 LEU   A CA     1 
ATOM   1962  C  C      . LEU   A 1 121 ? 6.654   -10.328 13.449 1.00 27.24  ?  146 LEU   A C      1 
ATOM   1963  O  O      . LEU   A 1 121 ? 7.162   -9.625  12.571 1.00 28.80  ?  146 LEU   A O      1 
ATOM   1964  C  CB     . LEU   A 1 121 ? 8.787   -11.685 13.439 1.00 28.62  ?  146 LEU   A CB     1 
ATOM   1965  C  CG     . LEU   A 1 121 ? 9.548   -12.921 13.921 1.00 30.07  ?  146 LEU   A CG     1 
ATOM   1966  C  CD1    . LEU   A 1 121 ? 10.945  -12.989 13.315 1.00 30.92  ?  146 LEU   A CD1    1 
ATOM   1967  C  CD2    . LEU   A 1 121 ? 9.626   -12.984 15.441 1.00 32.34  ?  146 LEU   A CD2    1 
ATOM   1968  H  H      . LEU   A 1 121 ? 6.449   -13.006 14.870 1.00 32.04  ?  146 LEU   A H      1 
ATOM   1969  H  HA     . LEU   A 1 121 ? 7.575   -11.237 15.023 1.00 32.45  ?  146 LEU   A HA     1 
ATOM   1970  H  HB2    . LEU   A 1 121 ? 8.657   -11.775 12.482 1.00 34.34  ?  146 LEU   A HB2    1 
ATOM   1971  H  HB3    . LEU   A 1 121 ? 9.337   -10.909 13.628 1.00 34.34  ?  146 LEU   A HB3    1 
ATOM   1972  H  HG     . LEU   A 1 121 ? 9.054   -13.699 13.621 1.00 36.08  ?  146 LEU   A HG     1 
ATOM   1973  H  HD11   . LEU   A 1 121 ? 11.390  -13.789 13.636 1.00 37.09  ?  146 LEU   A HD11   1 
ATOM   1974  H  HD12   . LEU   A 1 121 ? 10.869  -13.018 12.348 1.00 37.09  ?  146 LEU   A HD12   1 
ATOM   1975  H  HD13   . LEU   A 1 121 ? 11.445  -12.203 13.583 1.00 37.09  ?  146 LEU   A HD13   1 
ATOM   1976  H  HD21   . LEU   A 1 121 ? 10.247  -13.683 15.697 1.00 38.81  ?  146 LEU   A HD21   1 
ATOM   1977  H  HD22   . LEU   A 1 121 ? 9.935   -12.128 15.778 1.00 38.81  ?  146 LEU   A HD22   1 
ATOM   1978  H  HD23   . LEU   A 1 121 ? 8.744   -13.179 15.795 1.00 38.81  ?  146 LEU   A HD23   1 
ATOM   1979  N  N      . THR   A 1 122 ? 5.417   -10.130 13.910 1.00 26.82  ?  147 THR   A N      1 
ATOM   1980  C  CA     . THR   A 1 122 ? 4.544   -9.058  13.441 1.00 27.04  ?  147 THR   A CA     1 
ATOM   1981  C  C      . THR   A 1 122 ? 4.025   -8.273  14.638 1.00 26.84  ?  147 THR   A C      1 
ATOM   1982  O  O      . THR   A 1 122 ? 3.536   -8.866  15.608 1.00 26.88  ?  147 THR   A O      1 
ATOM   1983  C  CB     . THR   A 1 122 ? 3.370   -9.614  12.610 1.00 28.31  ?  147 THR   A CB     1 
ATOM   1984  O  OG1    . THR   A 1 122 ? 2.688   -10.643 13.345 1.00 29.23  ?  147 THR   A OG1    1 
ATOM   1985  C  CG2    . THR   A 1 122 ? 3.860   -10.184 11.256 1.00 29.29  ?  147 THR   A CG2    1 
ATOM   1986  H  H      . THR   A 1 122 ? 5.052   -10.620 14.515 1.00 32.17  ?  147 THR   A H      1 
ATOM   1987  H  HA     . THR   A 1 122 ? 5.051   -8.451  12.879 1.00 32.44  ?  147 THR   A HA     1 
ATOM   1988  H  HB     . THR   A 1 122 ? 2.751   -8.891  12.424 1.00 33.96  ?  147 THR   A HB     1 
ATOM   1989  H  HG1    . THR   A 1 122 ? 3.211   -11.281 13.499 1.00 35.07  ?  147 THR   A HG1    1 
ATOM   1990  H  HG21   . THR   A 1 122 ? 3.107   -10.522 10.747 1.00 35.14  ?  147 THR   A HG21   1 
ATOM   1991  H  HG22   . THR   A 1 122 ? 4.300   -9.489  10.743 1.00 35.14  ?  147 THR   A HG22   1 
ATOM   1992  H  HG23   . THR   A 1 122 ? 4.487   -10.908 11.409 1.00 35.14  ?  147 THR   A HG23   1 
ATOM   1993  N  N      . SER   A 1 123 ? 4.111   -6.946  14.565 1.00 26.65  ?  148 SER   A N      1 
ATOM   1994  C  CA     . SER   A 1 123 ? 3.838   -6.148  15.755 1.00 25.67  ?  148 SER   A CA     1 
ATOM   1995  C  C      . SER   A 1 123 ? 3.646   -4.686  15.392 1.00 26.47  ?  148 SER   A C      1 
ATOM   1996  O  O      . SER   A 1 123 ? 4.184   -4.203  14.390 1.00 27.02  ?  148 SER   A O      1 
ATOM   1997  C  CB     . SER   A 1 123 ? 4.987   -6.257  16.767 1.00 25.83  ?  148 SER   A CB     1 
ATOM   1998  O  OG     . SER   A 1 123 ? 4.723   -5.553  17.970 1.00 23.55  ?  148 SER   A OG     1 
ATOM   1999  H  H      . SER   A 1 123 ? 4.319   -6.500  13.860 1.00 31.97  ?  148 SER   A H      1 
ATOM   2000  H  HA     . SER   A 1 123 ? 3.008   -6.470  16.140 1.00 30.79  ?  148 SER   A HA     1 
ATOM   2001  H  HB2    . SER   A 1 123 ? 5.122   -7.194  16.981 1.00 30.99  ?  148 SER   A HB2    1 
ATOM   2002  H  HB3    . SER   A 1 123 ? 5.789   -5.890  16.364 1.00 30.99  ?  148 SER   A HB3    1 
ATOM   2003  H  HG     . SER   A 1 123 ? 4.017   -5.840  18.322 1.00 28.25  ?  148 SER   A HG     1 
ATOM   2004  N  N      . SER   A 1 124 ? 2.920   -3.979  16.256 1.00 26.73  ?  149 SER   A N      1 
ATOM   2005  C  CA     . SER   A 1 124 ? 2.881   -2.520  16.247 1.00 27.81  ?  149 SER   A CA     1 
ATOM   2006  C  C      . SER   A 1 124 ? 3.874   -1.890  17.225 1.00 27.40  ?  149 SER   A C      1 
ATOM   2007  O  O      . SER   A 1 124 ? 3.911   -0.650  17.349 1.00 27.62  ?  149 SER   A O      1 
ATOM   2008  C  CB     . SER   A 1 124 ? 1.455   -2.029  16.567 1.00 28.15  ?  149 SER   A CB     1 
ATOM   2009  O  OG     . SER   A 1 124 ? 0.992   -2.458  17.835 1.00 28.97  ?  149 SER   A OG     1 
ATOM   2010  H  H      . SER   A 1 124 ? 2.431   -4.331  16.870 1.00 32.07  ?  149 SER   A H      1 
ATOM   2011  H  HA     . SER   A 1 124 ? 3.111   -2.210  15.357 1.00 33.36  ?  149 SER   A HA     1 
ATOM   2012  H  HB2    . SER   A 1 124 ? 1.454   -1.060  16.551 1.00 33.77  ?  149 SER   A HB2    1 
ATOM   2013  H  HB3    . SER   A 1 124 ? 0.853   -2.373  15.888 1.00 33.77  ?  149 SER   A HB3    1 
ATOM   2014  H  HG     . SER   A 1 124 ? 1.008   -3.296  17.879 1.00 34.76  ?  149 SER   A HG     1 
ATOM   2015  N  N      . ASN   A 1 125 ? 4.707   -2.704  17.874 1.00 27.07  ?  150 ASN   A N      1 
ATOM   2016  C  CA     . ASN   A 1 125 ? 5.606   -2.259  18.928 1.00 26.49  ?  150 ASN   A CA     1 
ATOM   2017  C  C      . ASN   A 1 125 ? 7.071   -2.289  18.523 1.00 26.80  ?  150 ASN   A C      1 
ATOM   2018  O  O      . ASN   A 1 125 ? 7.946   -2.300  19.397 1.00 28.12  ?  150 ASN   A O      1 
ATOM   2019  C  CB     . ASN   A 1 125 ? 5.374   -3.121  20.159 1.00 26.70  ?  150 ASN   A CB     1 
ATOM   2020  C  CG     . ASN   A 1 125 ? 4.049   -2.836  20.787 1.00 27.33  ?  150 ASN   A CG     1 
ATOM   2021  O  OD1    . ASN   A 1 125 ? 3.814   -1.713  21.227 1.00 27.19  ?  150 ASN   A OD1    1 
ATOM   2022  N  ND2    . ASN   A 1 125 ? 3.145   -3.821  20.782 1.00 26.71  ?  150 ASN   A ND2    1 
ATOM   2023  H  H      . ASN   A 1 125 ? 4.767   -3.547  17.714 1.00 32.48  ?  150 ASN   A H      1 
ATOM   2024  H  HA     . ASN   A 1 125 ? 5.407   -1.333  19.140 1.00 31.78  ?  150 ASN   A HA     1 
ATOM   2025  H  HB2    . ASN   A 1 125 ? 5.396   -4.057  19.905 1.00 32.04  ?  150 ASN   A HB2    1 
ATOM   2026  H  HB3    . ASN   A 1 125 ? 6.067   -2.939  20.814 1.00 32.04  ?  150 ASN   A HB3    1 
ATOM   2027  H  HD21   . ASN   A 1 125 ? 2.371   -3.695  21.133 1.00 32.04  ?  150 ASN   A HD21   1 
ATOM   2028  H  HD22   . ASN   A 1 125 ? 3.339   -4.580  20.427 1.00 32.04  ?  150 ASN   A HD22   1 
ATOM   2029  N  N      . TYR   A 1 126 ? 7.357   -2.250  17.217 1.00 26.61  ?  151 TYR   A N      1 
ATOM   2030  C  CA     . TYR   A 1 126 ? 8.727   -2.362  16.736 1.00 28.64  ?  151 TYR   A CA     1 
ATOM   2031  C  C      . TYR   A 1 126 ? 9.429   -1.013  16.561 1.00 29.92  ?  151 TYR   A C      1 
ATOM   2032  O  O      . TYR   A 1 126 ? 10.630  -1.000  16.269 1.00 31.01  ?  151 TYR   A O      1 
ATOM   2033  C  CB     . TYR   A 1 126 ? 8.749   -3.137  15.403 1.00 27.86  ?  151 TYR   A CB     1 
ATOM   2034  C  CG     . TYR   A 1 126 ? 8.597   -4.660  15.516 1.00 28.13  ?  151 TYR   A CG     1 
ATOM   2035  C  CD1    . TYR   A 1 126 ? 9.046   -5.369  16.636 1.00 27.01  ?  151 TYR   A CD1    1 
ATOM   2036  C  CD2    . TYR   A 1 126 ? 8.018   -5.391  14.480 1.00 28.97  ?  151 TYR   A CD2    1 
ATOM   2037  C  CE1    . TYR   A 1 126 ? 8.913   -6.769  16.706 1.00 26.12  ?  151 TYR   A CE1    1 
ATOM   2038  C  CE2    . TYR   A 1 126 ? 7.874   -6.767  14.551 1.00 28.12  ?  151 TYR   A CE2    1 
ATOM   2039  C  CZ     . TYR   A 1 126 ? 8.317   -7.459  15.654 1.00 26.80  ?  151 TYR   A CZ     1 
ATOM   2040  O  OH     . TYR   A 1 126 ? 8.156   -8.834  15.679 1.00 27.58  ?  151 TYR   A OH     1 
ATOM   2041  H  H      . TYR   A 1 126 ? 6.771   -2.159  16.594 1.00 31.93  ?  151 TYR   A H      1 
ATOM   2042  H  HA     . TYR   A 1 126 ? 9.243   -2.865  17.386 1.00 34.36  ?  151 TYR   A HA     1 
ATOM   2043  H  HB2    . TYR   A 1 126 ? 8.018   -2.816  14.852 1.00 33.43  ?  151 TYR   A HB2    1 
ATOM   2044  H  HB3    . TYR   A 1 126 ? 9.596   -2.965  14.964 1.00 33.43  ?  151 TYR   A HB3    1 
ATOM   2045  H  HD1    . TYR   A 1 126 ? 9.438   -4.909  17.343 1.00 32.41  ?  151 TYR   A HD1    1 
ATOM   2046  H  HD2    . TYR   A 1 126 ? 7.721   -4.944  13.721 1.00 34.76  ?  151 TYR   A HD2    1 
ATOM   2047  H  HE1    . TYR   A 1 126 ? 9.222   -7.231  17.452 1.00 31.34  ?  151 TYR   A HE1    1 
ATOM   2048  H  HE2    . TYR   A 1 126 ? 7.474   -7.225  13.847 1.00 33.73  ?  151 TYR   A HE2    1 
ATOM   2049  H  HH     . TYR   A 1 126 ? 8.438   -9.143  16.408 1.00 33.09  ?  151 TYR   A HH     1 
ATOM   2050  N  N      . ASP   A 1 127 ? 8.741   0.116   16.755 1.00 29.74  ?  152 ASP   A N      1 
ATOM   2051  C  CA     . ASP   A 1 127 ? 9.345   1.443   16.604 1.00 30.90  ?  152 ASP   A CA     1 
ATOM   2052  C  C      . ASP   A 1 127 ? 9.518   2.071   17.986 1.00 31.10  ?  152 ASP   A C      1 
ATOM   2053  O  O      . ASP   A 1 127 ? 8.588   2.677   18.525 1.00 31.08  ?  152 ASP   A O      1 
ATOM   2054  C  CB     . ASP   A 1 127 ? 8.492   2.332   15.699 1.00 34.41  ?  152 ASP   A CB     1 
ATOM   2055  C  CG     . ASP   A 1 127 ? 9.067   3.730   15.539 1.00 37.14  ?  152 ASP   A CG     1 
ATOM   2056  O  OD1    . ASP   A 1 127 ? 10.159  4.003   16.077 1.00 38.27  ?  152 ASP   A OD1    1 
ATOM   2057  O  OD2    . ASP   A 1 127 ? 8.427   4.563   14.869 1.00 38.82  ?  152 ASP   A OD2    1 
ATOM   2058  H  H      . ASP   A 1 127 ? 7.910   0.138   16.977 1.00 35.69  ?  152 ASP   A H      1 
ATOM   2059  H  HA     . ASP   A 1 127 ? 10.224  1.338   16.209 1.00 37.08  ?  152 ASP   A HA     1 
ATOM   2060  H  HB2    . ASP   A 1 127 ? 8.437   1.927   14.819 1.00 41.28  ?  152 ASP   A HB2    1 
ATOM   2061  H  HB3    . ASP   A 1 127 ? 7.604   2.414   16.082 1.00 41.28  ?  152 ASP   A HB3    1 
ATOM   2062  N  N      . ASP   A 1 128 ? 10.720  1.951   18.547 1.00 31.71  ?  153 ASP   A N      1 
ATOM   2063  C  CA     . ASP   A 1 128 ? 10.938  2.423   19.912 1.00 32.56  ?  153 ASP   A CA     1 
ATOM   2064  C  C      . ASP   A 1 128 ? 11.255  3.917   19.995 1.00 33.13  ?  153 ASP   A C      1 
ATOM   2065  O  O      . ASP   A 1 128 ? 11.510  4.413   21.103 1.00 33.00  ?  153 ASP   A O      1 
ATOM   2066  C  CB     . ASP   A 1 128 ? 12.032  1.581   20.577 1.00 32.86  ?  153 ASP   A CB     1 
ATOM   2067  C  CG     . ASP   A 1 128 ? 11.495  0.252   21.104 1.00 33.32  ?  153 ASP   A CG     1 
ATOM   2068  O  OD1    . ASP   A 1 128 ? 10.290  -0.033  20.907 1.00 32.76  ?  153 ASP   A OD1    1 
ATOM   2069  O  OD2    . ASP   A 1 128 ? 12.266  -0.505  21.731 1.00 34.34  ?  153 ASP   A OD2    1 
ATOM   2070  H  H      . ASP   A 1 128 ? 11.409  1.606   18.166 1.00 38.04  ?  153 ASP   A H      1 
ATOM   2071  H  HA     . ASP   A 1 128 ? 10.125  2.294   20.424 1.00 39.07  ?  153 ASP   A HA     1 
ATOM   2072  H  HB2    . ASP   A 1 128 ? 12.727  1.390   19.928 1.00 39.42  ?  153 ASP   A HB2    1 
ATOM   2073  H  HB3    . ASP   A 1 128 ? 12.404  2.075   21.325 1.00 39.42  ?  153 ASP   A HB3    1 
ATOM   2074  N  N      . ASP   A 1 129 ? 11.196  4.662   18.888 1.00 33.83  ?  154 ASP   A N      1 
ATOM   2075  C  CA     . ASP   A 1 129 ? 11.048  6.111   19.012 1.00 34.97  ?  154 ASP   A CA     1 
ATOM   2076  C  C      . ASP   A 1 129 ? 9.697   6.466   19.623 1.00 34.51  ?  154 ASP   A C      1 
ATOM   2077  O  O      . ASP   A 1 129 ? 9.544   7.552   20.194 1.00 34.73  ?  154 ASP   A O      1 
ATOM   2078  C  CB     . ASP   A 1 129 ? 11.206  6.801   17.656 1.00 37.62  ?  154 ASP   A CB     1 
ATOM   2079  C  CG     . ASP   A 1 129 ? 12.633  6.745   17.132 1.00 42.96  ?  154 ASP   A CG     1 
ATOM   2080  O  OD1    . ASP   A 1 129 ? 13.563  6.544   17.941 1.00 45.58  ?  154 ASP   A OD1    1 
ATOM   2081  O  OD2    . ASP   A 1 129 ? 12.826  6.922   15.911 1.00 45.15  ?  154 ASP   A OD2    1 
ATOM   2082  H  H      . ASP   A 1 129 ? 11.238  4.363   18.083 1.00 40.59  ?  154 ASP   A H      1 
ATOM   2083  H  HA     . ASP   A 1 129 ? 11.757  6.452   19.580 1.00 41.96  ?  154 ASP   A HA     1 
ATOM   2084  H  HB2    . ASP   A 1 129 ? 10.632  6.363   17.009 1.00 45.13  ?  154 ASP   A HB2    1 
ATOM   2085  H  HB3    . ASP   A 1 129 ? 10.956  7.734   17.744 1.00 45.13  ?  154 ASP   A HB3    1 
ATOM   2086  N  N      . GLU   A 1 130 ? 8.717   5.570   19.502 1.00 33.24  ?  155 GLU   A N      1 
ATOM   2087  C  CA     . GLU   A 1 130 ? 7.455   5.686   20.220 1.00 32.03  ?  155 GLU   A CA     1 
ATOM   2088  C  C      . GLU   A 1 130 ? 7.670   5.123   21.620 1.00 28.92  ?  155 GLU   A C      1 
ATOM   2089  O  O      . GLU   A 1 130 ? 8.024   3.949   21.775 1.00 29.18  ?  155 GLU   A O      1 
ATOM   2090  C  CB     . GLU   A 1 130 ? 6.350   4.927   19.487 1.00 34.54  ?  155 GLU   A CB     1 
ATOM   2091  C  CG     . GLU   A 1 130 ? 6.241   5.306   18.009 1.00 37.26  ?  155 GLU   A CG     1 
ATOM   2092  C  CD     . GLU   A 1 130 ? 5.246   4.473   17.199 1.00 39.64  ?  155 GLU   A CD     1 
ATOM   2093  O  OE1    . GLU   A 1 130 ? 5.213   3.227   17.334 1.00 38.34  ?  155 GLU   A OE1    1 
ATOM   2094  O  OE2    . GLU   A 1 130 ? 4.515   5.081   16.387 1.00 42.51  ?  155 GLU   A OE2    1 
ATOM   2095  H  H      . GLU   A 1 130 ? 8.762   4.873   19.000 1.00 39.88  ?  155 GLU   A H      1 
ATOM   2096  H  HA     . GLU   A 1 130 ? 7.177   6.614   20.279 1.00 38.42  ?  155 GLU   A HA     1 
ATOM   2097  H  HB2    . GLU   A 1 130 ? 6.535   3.976   19.539 1.00 41.44  ?  155 GLU   A HB2    1 
ATOM   2098  H  HB3    . GLU   A 1 130 ? 5.500   5.124   19.910 1.00 41.44  ?  155 GLU   A HB3    1 
ATOM   2099  H  HG2    . GLU   A 1 130 ? 5.960   6.232   17.949 1.00 44.71  ?  155 GLU   A HG2    1 
ATOM   2100  H  HG3    . GLU   A 1 130 ? 7.113   5.197   17.598 1.00 44.71  ?  155 GLU   A HG3    1 
ATOM   2101  N  N      . LYS   A 1 131 ? 7.475   5.950   22.638 1.00 28.25  ?  156 LYS   A N      1 
ATOM   2102  C  CA     . LYS   A 1 131 ? 7.715   5.519   24.016 1.00 25.99  ?  156 LYS   A CA     1 
ATOM   2103  C  C      . LYS   A 1 131 ? 6.398   5.011   24.599 1.00 25.26  ?  156 LYS   A C      1 
ATOM   2104  O  O      . LYS   A 1 131 ? 5.643   5.752   25.229 1.00 28.90  ?  156 LYS   A O      1 
ATOM   2105  C  CB     . LYS   A 1 131 ? 8.310   6.660   24.833 1.00 28.03  ?  156 LYS   A CB     1 
ATOM   2106  C  CG     . LYS   A 1 131 ? 9.569   7.294   24.220 1.00 31.63  ?  156 LYS   A CG     1 
ATOM   2107  C  CD     . LYS   A 1 131 ? 10.707  6.298   23.987 1.00 34.44  ?  156 LYS   A CD     1 
ATOM   2108  C  CE     . LYS   A 1 131 ? 11.938  6.993   23.389 1.00 37.94  ?  156 LYS   A CE     1 
ATOM   2109  N  NZ     . LYS   A 1 131 ? 12.933  6.051   22.803 1.00 39.59  ?  156 LYS   A NZ     1 
ATOM   2110  H  H      . LYS   A 1 131 ? 7.206   6.763   22.561 1.00 33.90  ?  156 LYS   A H      1 
ATOM   2111  H  HA     . LYS   A 1 131 ? 8.343   4.780   24.021 1.00 31.19  ?  156 LYS   A HA     1 
ATOM   2112  H  HB2    . LYS   A 1 131 ? 7.643   7.358   24.921 1.00 33.64  ?  156 LYS   A HB2    1 
ATOM   2113  H  HB3    . LYS   A 1 131 ? 8.551   6.319   25.709 1.00 33.64  ?  156 LYS   A HB3    1 
ATOM   2114  H  HG2    . LYS   A 1 131 ? 9.337   7.684   23.363 1.00 37.94  ?  156 LYS   A HG2    1 
ATOM   2115  H  HG3    . LYS   A 1 131 ? 9.897   7.982   24.820 1.00 37.94  ?  156 LYS   A HG3    1 
ATOM   2116  H  HD2    . LYS   A 1 131 ? 10.962  5.896   24.832 1.00 41.32  ?  156 LYS   A HD2    1 
ATOM   2117  H  HD3    . LYS   A 1 131 ? 10.413  5.611   23.368 1.00 41.32  ?  156 LYS   A HD3    1 
ATOM   2118  H  HE2    . LYS   A 1 131 ? 11.647  7.592   22.684 1.00 45.53  ?  156 LYS   A HE2    1 
ATOM   2119  H  HE3    . LYS   A 1 131 ? 12.383  7.495   24.089 1.00 45.53  ?  156 LYS   A HE3    1 
ATOM   2120  H  HZ1    . LYS   A 1 131 ? 12.557  5.577   22.150 1.00 47.50  ?  156 LYS   A HZ1    1 
ATOM   2121  H  HZ2    . LYS   A 1 131 ? 13.622  6.505   22.469 1.00 47.50  ?  156 LYS   A HZ2    1 
ATOM   2122  H  HZ3    . LYS   A 1 131 ? 13.231  5.493   23.429 1.00 47.50  ?  156 LYS   A HZ3    1 
ATOM   2123  N  N      . LYS   A 1 132 ? 6.139   3.718   24.421 1.00 23.03  ?  157 LYS   A N      1 
ATOM   2124  C  CA     . LYS   A 1 132 ? 4.860   3.122   24.770 1.00 21.79  ?  157 LYS   A CA     1 
ATOM   2125  C  C      . LYS   A 1 132 ? 4.924   2.379   26.098 1.00 20.52  ?  157 LYS   A C      1 
ATOM   2126  O  O      . LYS   A 1 132 ? 5.953   1.811   26.460 1.00 20.82  ?  157 LYS   A O      1 
ATOM   2127  C  CB     . LYS   A 1 132 ? 4.416   2.133   23.687 1.00 25.01  ?  157 LYS   A CB     1 
ATOM   2128  C  CG     . LYS   A 1 132 ? 4.203   2.778   22.332 1.00 28.41  ?  157 LYS   A CG     1 
ATOM   2129  C  CD     . LYS   A 1 132 ? 3.640   1.766   21.329 1.00 33.52  ?  157 LYS   A CD     1 
ATOM   2130  C  CE     . LYS   A 1 132 ? 3.447   2.402   19.964 1.00 39.07  ?  157 LYS   A CE     1 
ATOM   2131  N  NZ     . LYS   A 1 132 ? 2.213   1.954   19.262 1.00 43.48  ?  157 LYS   A NZ     1 
ATOM   2132  H  H      . LYS   A 1 132 ? 6.702   3.158   24.092 1.00 27.63  ?  157 LYS   A H      1 
ATOM   2133  H  HA     . LYS   A 1 132 ? 4.209   3.836   24.854 1.00 26.15  ?  157 LYS   A HA     1 
ATOM   2134  H  HB2    . LYS   A 1 132 ? 5.098   1.450   23.588 1.00 30.01  ?  157 LYS   A HB2    1 
ATOM   2135  H  HB3    . LYS   A 1 132 ? 3.578   1.727   23.959 1.00 30.01  ?  157 LYS   A HB3    1 
ATOM   2136  H  HG2    . LYS   A 1 132 ? 3.573   3.510   22.418 1.00 34.09  ?  157 LYS   A HG2    1 
ATOM   2137  H  HG3    . LYS   A 1 132 ? 5.051   3.107   21.994 1.00 34.09  ?  157 LYS   A HG3    1 
ATOM   2138  H  HD2    . LYS   A 1 132 ? 4.257   1.024   21.238 1.00 40.22  ?  157 LYS   A HD2    1 
ATOM   2139  H  HD3    . LYS   A 1 132 ? 2.779   1.446   21.643 1.00 40.22  ?  157 LYS   A HD3    1 
ATOM   2140  H  HE2    . LYS   A 1 132 ? 3.393   3.364   20.072 1.00 46.87  ?  157 LYS   A HE2    1 
ATOM   2141  H  HE3    . LYS   A 1 132 ? 4.205   2.173   19.403 1.00 46.87  ?  157 LYS   A HE3    1 
ATOM   2142  H  HZ1    . LYS   A 1 132 ? 1.495   2.170   19.741 1.00 52.17  ?  157 LYS   A HZ1    1 
ATOM   2143  H  HZ2    . LYS   A 1 132 ? 2.157   2.345   18.465 1.00 52.17  ?  157 LYS   A HZ2    1 
ATOM   2144  H  HZ3    . LYS   A 1 132 ? 2.230   1.071   19.150 1.00 52.17  ?  157 LYS   A HZ3    1 
ATOM   2145  N  N      . VAL   A 1 133 ? 3.784   2.334   26.792 1.00 18.70  ?  158 VAL   A N      1 
ATOM   2146  C  CA     . VAL   A 1 133 ? 3.680   1.564   28.029 1.00 17.61  ?  158 VAL   A CA     1 
ATOM   2147  C  C      . VAL   A 1 133 ? 2.720   0.387   27.848 1.00 17.71  ?  158 VAL   A C      1 
ATOM   2148  O  O      . VAL   A 1 133 ? 2.077   -0.068  28.805 1.00 18.71  ?  158 VAL   A O      1 
ATOM   2149  C  CB     . VAL   A 1 133 ? 3.258   2.445   29.226 1.00 19.24  ?  158 VAL   A CB     1 
ATOM   2150  C  CG1    . VAL   A 1 133 ? 4.345   3.495   29.538 1.00 19.05  ?  158 VAL   A CG1    1 
ATOM   2151  C  CG2    . VAL   A 1 133 ? 1.906   3.131   28.988 1.00 20.70  ?  158 VAL   A CG2    1 
ATOM   2152  H  H      . VAL   A 1 133 ? 3.061   2.741   26.567 1.00 22.43  ?  158 VAL   A H      1 
ATOM   2153  H  HA     . VAL   A 1 133 ? 4.558   1.199   28.219 1.00 21.13  ?  158 VAL   A HA     1 
ATOM   2154  H  HB     . VAL   A 1 133 ? 3.155   1.865   29.996 1.00 23.08  ?  158 VAL   A HB     1 
ATOM   2155  H  HG11   . VAL   A 1 133 ? 4.056   4.035   30.290 1.00 22.85  ?  158 VAL   A HG11   1 
ATOM   2156  H  HG12   . VAL   A 1 133 ? 5.172   3.037   29.758 1.00 22.85  ?  158 VAL   A HG12   1 
ATOM   2157  H  HG13   . VAL   A 1 133 ? 4.476   4.056   28.758 1.00 22.85  ?  158 VAL   A HG13   1 
ATOM   2158  H  HG21   . VAL   A 1 133 ? 1.693   3.684   29.756 1.00 24.84  ?  158 VAL   A HG21   1 
ATOM   2159  H  HG22   . VAL   A 1 133 ? 1.965   3.680   28.191 1.00 24.84  ?  158 VAL   A HG22   1 
ATOM   2160  H  HG23   . VAL   A 1 133 ? 1.223   2.451   28.871 1.00 24.84  ?  158 VAL   A HG23   1 
ATOM   2161  N  N      . THR   A 1 134 ? 2.654   -0.136  26.624 1.00 19.01  ?  159 THR   A N      1 
ATOM   2162  C  CA     . THR   A 1 134 ? 2.074   -1.444  26.363 1.00 19.41  ?  159 THR   A CA     1 
ATOM   2163  C  C      . THR   A 1 134 ? 2.993   -2.564  26.849 1.00 18.04  ?  159 THR   A C      1 
ATOM   2164  O  O      . THR   A 1 134 ? 4.212   -2.402  26.959 1.00 19.94  ?  159 THR   A O      1 
ATOM   2165  C  CB     . THR   A 1 134 ? 1.836   -1.635  24.869 1.00 23.58  ?  159 THR   A CB     1 
ATOM   2166  O  OG1    . THR   A 1 134 ? 3.040   -1.323  24.151 1.00 26.65  ?  159 THR   A OG1    1 
ATOM   2167  C  CG2    . THR   A 1 134 ? 0.738   -0.734  24.399 1.00 24.98  ?  159 THR   A CG2    1 
ATOM   2168  H  H      . THR   A 1 134 ? 2.945   0.257   25.917 1.00 22.80  ?  159 THR   A H      1 
ATOM   2169  H  HA     . THR   A 1 134 ? 1.229   -1.502  26.836 1.00 23.29  ?  159 THR   A HA     1 
ATOM   2170  H  HB     . THR   A 1 134 ? 1.580   -2.554  24.693 1.00 28.29  ?  159 THR   A HB     1 
ATOM   2171  H  HG1    . THR   A 1 134 ? 2.925   -1.449  23.328 1.00 31.97  ?  159 THR   A HG1    1 
ATOM   2172  H  HG21   . THR   A 1 134 ? 0.588   -0.861  23.449 1.00 29.96  ?  159 THR   A HG21   1 
ATOM   2173  H  HG22   . THR   A 1 134 ? -0.082  -0.933  24.877 1.00 29.96  ?  159 THR   A HG22   1 
ATOM   2174  H  HG23   . THR   A 1 134 ? 0.978   0.193   24.558 1.00 29.96  ?  159 THR   A HG23   1 
ATOM   2175  N  N      . GLY   A 1 135 ? 2.390   -3.720  27.136 1.00 18.98  ?  160 GLY   A N      1 
ATOM   2176  C  CA     . GLY   A 1 135 ? 3.181   -4.898  27.448 1.00 18.87  ?  160 GLY   A CA     1 
ATOM   2177  C  C      . GLY   A 1 135 ? 3.786   -5.569  26.235 1.00 19.68  ?  160 GLY   A C      1 
ATOM   2178  O  O      . GLY   A 1 135 ? 4.798   -6.271  26.363 1.00 19.84  ?  160 GLY   A O      1 
ATOM   2179  H  H      . GLY   A 1 135 ? 1.539   -3.841  27.156 1.00 22.77  ?  160 GLY   A H      1 
ATOM   2180  H  HA2    . GLY   A 1 135 ? 3.905   -4.643  28.041 1.00 22.64  ?  160 GLY   A HA2    1 
ATOM   2181  H  HA3    . GLY   A 1 135 ? 2.616   -5.545  27.898 1.00 22.64  ?  160 GLY   A HA3    1 
ATOM   2182  N  N      . GLY   A 1 136 ? 3.199   -5.356  25.060 1.00 21.02  ?  161 GLY   A N      1 
ATOM   2183  C  CA     . GLY   A 1 136 ? 3.718   -5.973  23.851 1.00 20.87  ?  161 GLY   A CA     1 
ATOM   2184  C  C      . GLY   A 1 136 ? 5.039   -5.373  23.405 1.00 20.88  ?  161 GLY   A C      1 
ATOM   2185  O  O      . GLY   A 1 136 ? 5.223   -4.151  23.379 1.00 20.34  ?  161 GLY   A O      1 
ATOM   2186  H  H      . GLY   A 1 136 ? 2.506   -4.862  24.939 1.00 25.22  ?  161 GLY   A H      1 
ATOM   2187  H  HA2    . GLY   A 1 136 ? 3.853   -6.921  24.009 1.00 25.04  ?  161 GLY   A HA2    1 
ATOM   2188  H  HA3    . GLY   A 1 136 ? 3.075   -5.860  23.134 1.00 25.04  ?  161 GLY   A HA3    1 
ATOM   2189  N  N      . ARG   A 1 137 ? 5.967   -6.259  23.038 1.00 20.50  ?  162 ARG   A N      1 
ATOM   2190  C  CA     . ARG   A 1 137 ? 7.295   -5.834  22.625 1.00 21.09  ?  162 ARG   A CA     1 
ATOM   2191  C  C      . ARG   A 1 137 ? 7.816   -6.589  21.405 1.00 21.74  ?  162 ARG   A C      1 
ATOM   2192  O  O      . ARG   A 1 137 ? 8.450   -5.976  20.542 1.00 23.58  ?  162 ARG   A O      1 
ATOM   2193  C  CB     . ARG   A 1 137 ? 8.286   -6.011  23.788 1.00 20.77  ?  162 ARG   A CB     1 
ATOM   2194  C  CG     . ARG   A 1 137 ? 7.930   -5.213  25.049 1.00 21.70  ?  162 ARG   A CG     1 
ATOM   2195  C  CD     . ARG   A 1 137 ? 8.061   -3.666  24.871 1.00 22.18  ?  162 ARG   A CD     1 
ATOM   2196  N  NE     . ARG   A 1 137 ? 9.450   -3.327  24.552 1.00 23.86  ?  162 ARG   A NE     1 
ATOM   2197  C  CZ     . ARG   A 1 137 ? 9.861   -2.562  23.543 1.00 24.46  ?  162 ARG   A CZ     1 
ATOM   2198  N  NH1    . ARG   A 1 137 ? 8.999   -1.963  22.738 1.00 26.31  ?  162 ARG   A NH1    1 
ATOM   2199  N  NH2    . ARG   A 1 137 ? 11.161  -2.388  23.349 1.00 26.86  ?  162 ARG   A NH2    1 
ATOM   2200  H  H      . ARG   A 1 137 ? 5.848   -7.110  23.021 1.00 24.59  ?  162 ARG   A H      1 
ATOM   2201  H  HA     . ARG   A 1 137 ? 7.233   -4.899  22.374 1.00 25.30  ?  162 ARG   A HA     1 
ATOM   2202  H  HB2    . ARG   A 1 137 ? 8.311   -6.950  24.033 1.00 24.92  ?  162 ARG   A HB2    1 
ATOM   2203  H  HB3    . ARG   A 1 137 ? 9.163   -5.721  23.495 1.00 24.92  ?  162 ARG   A HB3    1 
ATOM   2204  H  HG2    . ARG   A 1 137 ? 7.011   -5.406  25.292 1.00 26.03  ?  162 ARG   A HG2    1 
ATOM   2205  H  HG3    . ARG   A 1 137 ? 8.526   -5.480  25.766 1.00 26.03  ?  162 ARG   A HG3    1 
ATOM   2206  H  HD2    . ARG   A 1 137 ? 7.491   -3.369  24.144 1.00 26.61  ?  162 ARG   A HD2    1 
ATOM   2207  H  HD3    . ARG   A 1 137 ? 7.810   -3.218  25.694 1.00 26.61  ?  162 ARG   A HD3    1 
ATOM   2208  H  HE     . ARG   A 1 137 ? 10.057  -3.653  25.065 1.00 28.63  ?  162 ARG   A HE     1 
ATOM   2209  H  HH11   . ARG   A 1 137 ? 8.154   -2.064  22.861 1.00 31.56  ?  162 ARG   A HH11   1 
ATOM   2210  H  HH12   . ARG   A 1 137 ? 9.283   -1.472  22.092 1.00 31.56  ?  162 ARG   A HH12   1 
ATOM   2211  H  HH21   . ARG   A 1 137 ? 11.728  -2.767  23.872 1.00 32.23  ?  162 ARG   A HH21   1 
ATOM   2212  H  HH22   . ARG   A 1 137 ? 11.437  -1.895  22.700 1.00 32.23  ?  162 ARG   A HH22   1 
ATOM   2213  N  N      . ASN   A 1 138 ? 7.568   -7.902  21.305 1.00 21.20  ?  163 ASN   A N      1 
ATOM   2214  C  CA     . ASN   A 1 138 ? 8.366   -8.739  20.418 1.00 21.78  ?  163 ASN   A CA     1 
ATOM   2215  C  C      . ASN   A 1 138 ? 7.677   -9.255  19.160 1.00 22.89  ?  163 ASN   A C      1 
ATOM   2216  O  O      . ASN   A 1 138 ? 8.379   -9.736  18.264 1.00 23.19  ?  163 ASN   A O      1 
ATOM   2217  C  CB     . ASN   A 1 138 ? 8.892   -9.957  21.190 1.00 23.87  ?  163 ASN   A CB     1 
ATOM   2218  C  CG     . ASN   A 1 138 ? 9.655   -9.568  22.428 1.00 25.78  ?  163 ASN   A CG     1 
ATOM   2219  O  OD1    . ASN   A 1 138 ? 10.533  -8.694  22.373 1.00 26.19  ?  163 ASN   A OD1    1 
ATOM   2220  N  ND2    . ASN   A 1 138 ? 9.302   -10.171 23.565 1.00 27.77  ?  163 ASN   A ND2    1 
ATOM   2221  H  H      . ASN   A 1 138 ? 6.951   -8.319  21.735 1.00 25.43  ?  163 ASN   A H      1 
ATOM   2222  H  HA     . ASN   A 1 138 ? 9.106   -8.190  20.113 1.00 26.13  ?  163 ASN   A HA     1 
ATOM   2223  H  HB2    . ASN   A 1 138 ? 8.141   -10.509 21.460 1.00 28.63  ?  163 ASN   A HB2    1 
ATOM   2224  H  HB3    . ASN   A 1 138 ? 9.487   -10.464 20.616 1.00 28.63  ?  163 ASN   A HB3    1 
ATOM   2225  H  HD21   . ASN   A 1 138 ? 9.710   -9.980  24.298 1.00 33.32  ?  163 ASN   A HD21   1 
ATOM   2226  H  HD22   . ASN   A 1 138 ? 8.666   -10.750 23.566 1.00 33.32  ?  163 ASN   A HD22   1 
ATOM   2227  N  N      . GLY   A 1 139 ? 6.347   -9.190  19.069 1.00 22.51  ?  164 GLY   A N      1 
ATOM   2228  C  CA     . GLY   A 1 139 ? 5.632   -9.684  17.903 1.00 23.05  ?  164 GLY   A CA     1 
ATOM   2229  C  C      . GLY   A 1 139 ? 5.419   -11.177 17.848 1.00 21.96  ?  164 GLY   A C      1 
ATOM   2230  O  O      . GLY   A 1 139 ? 5.264   -11.722 16.748 1.00 23.25  ?  164 GLY   A O      1 
ATOM   2231  H  H      . GLY   A 1 139 ? 5.835   -8.860  19.676 1.00 27.01  ?  164 GLY   A H      1 
ATOM   2232  H  HA2    . GLY   A 1 139 ? 4.758   -9.264  17.878 1.00 27.65  ?  164 GLY   A HA2    1 
ATOM   2233  H  HA3    . GLY   A 1 139 ? 6.127   -9.430  17.109 1.00 27.65  ?  164 GLY   A HA3    1 
ATOM   2234  N  N      . TYR   A 1 140 ? 5.418   -11.855 19.001 1.00 20.90  ?  165 TYR   A N      1 
ATOM   2235  C  CA     . TYR   A 1 140 ? 5.257   -13.297 19.110 1.00 20.46  ?  165 TYR   A CA     1 
ATOM   2236  C  C      . TYR   A 1 140 ? 3.960   -13.736 19.780 1.00 20.25  ?  165 TYR   A C      1 
ATOM   2237  O  O      . TYR   A 1 140 ? 3.361   -14.723 19.351 1.00 21.26  ?  165 TYR   A O      1 
ATOM   2238  C  CB     . TYR   A 1 140 ? 6.408   -13.885 19.942 1.00 20.17  ?  165 TYR   A CB     1 
ATOM   2239  C  CG     . TYR   A 1 140 ? 7.605   -14.415 19.198 1.00 22.74  ?  165 TYR   A CG     1 
ATOM   2240  C  CD1    . TYR   A 1 140 ? 7.480   -15.478 18.329 1.00 25.36  ?  165 TYR   A CD1    1 
ATOM   2241  C  CD2    . TYR   A 1 140 ? 8.876   -13.893 19.414 1.00 25.50  ?  165 TYR   A CD2    1 
ATOM   2242  C  CE1    . TYR   A 1 140 ? 8.568   -15.990 17.676 1.00 27.94  ?  165 TYR   A CE1    1 
ATOM   2243  C  CE2    . TYR   A 1 140 ? 9.981   -14.407 18.759 1.00 28.02  ?  165 TYR   A CE2    1 
ATOM   2244  C  CZ     . TYR   A 1 140 ? 9.813   -15.455 17.890 1.00 28.89  ?  165 TYR   A CZ     1 
ATOM   2245  O  OH     . TYR   A 1 140 ? 10.878  -16.005 17.218 1.00 30.29  ?  165 TYR   A OH     1 
ATOM   2246  H  H      . TYR   A 1 140 ? 5.513   -11.477 19.768 1.00 25.07  ?  165 TYR   A H      1 
ATOM   2247  H  HA     . TYR   A 1 140 ? 5.275   -13.660 18.211 1.00 24.55  ?  165 TYR   A HA     1 
ATOM   2248  H  HB2    . TYR   A 1 140 ? 6.733   -13.189 20.534 1.00 24.20  ?  165 TYR   A HB2    1 
ATOM   2249  H  HB3    . TYR   A 1 140 ? 6.052   -14.623 20.461 1.00 24.20  ?  165 TYR   A HB3    1 
ATOM   2250  H  HD1    . TYR   A 1 140 ? 6.642   -15.853 18.183 1.00 30.42  ?  165 TYR   A HD1    1 
ATOM   2251  H  HD2    . TYR   A 1 140 ? 8.984   -13.186 20.009 1.00 30.60  ?  165 TYR   A HD2    1 
ATOM   2252  H  HE1    . TYR   A 1 140 ? 8.464   -16.702 17.087 1.00 33.52  ?  165 TYR   A HE1    1 
ATOM   2253  H  HE2    . TYR   A 1 140 ? 10.826  -14.047 18.906 1.00 33.62  ?  165 TYR   A HE2    1 
ATOM   2254  H  HH     . TYR   A 1 140 ? 11.583  -15.590 17.410 1.00 36.34  ?  165 TYR   A HH     1 
ATOM   2255  N  N      . GLY   A 1 141 ? 3.533   -13.030 20.834 1.00 19.43  ?  166 GLY   A N      1 
ATOM   2256  C  CA     . GLY   A 1 141 ? 2.607   -13.605 21.804 1.00 20.59  ?  166 GLY   A CA     1 
ATOM   2257  C  C      . GLY   A 1 141 ? 1.365   -14.249 21.217 1.00 21.11  ?  166 GLY   A C      1 
ATOM   2258  O  O      . GLY   A 1 141 ? 0.991   -15.366 21.595 1.00 20.72  ?  166 GLY   A O      1 
ATOM   2259  H  H      . GLY   A 1 141 ? 3.764   -12.219 21.006 1.00 23.31  ?  166 GLY   A H      1 
ATOM   2260  H  HA2    . GLY   A 1 141 ? 3.076   -14.285 22.313 1.00 24.70  ?  166 GLY   A HA2    1 
ATOM   2261  H  HA3    . GLY   A 1 141 ? 2.316   -12.903 22.408 1.00 24.70  ?  166 GLY   A HA3    1 
ATOM   2262  N  N      . ALA   A 1 142 ? 0.662   -13.525 20.342 1.00 21.90  ?  167 ALA   A N      1 
ATOM   2263  C  CA     . ALA   A 1 142 ? -0.595  -14.034 19.800 1.00 22.03  ?  167 ALA   A CA     1 
ATOM   2264  C  C      . ALA   A 1 142 ? -0.358  -15.233 18.895 1.00 22.70  ?  167 ALA   A C      1 
ATOM   2265  O  O      . ALA   A 1 142 ? -1.150  -16.189 18.889 1.00 22.75  ?  167 ALA   A O      1 
ATOM   2266  C  CB     . ALA   A 1 142 ? -1.320  -12.918 19.042 1.00 24.37  ?  167 ALA   A CB     1 
ATOM   2267  H  H      . ALA   A 1 142 ? 0.888   -12.748 20.052 1.00 26.27  ?  167 ALA   A H      1 
ATOM   2268  H  HA     . ALA   A 1 142 ? -1.164  -14.322 20.531 1.00 26.43  ?  167 ALA   A HA     1 
ATOM   2269  H  HB1    . ALA   A 1 142 ? -2.155  -13.266 18.690 1.00 29.24  ?  167 ALA   A HB1    1 
ATOM   2270  H  HB2    . ALA   A 1 142 ? -1.498  -12.186 19.653 1.00 29.24  ?  167 ALA   A HB2    1 
ATOM   2271  H  HB3    . ALA   A 1 142 ? -0.756  -12.613 18.315 1.00 29.24  ?  167 ALA   A HB3    1 
ATOM   2272  N  N      . LYS   A 1 143 ? 0.724   -15.196 18.116 1.00 21.73  ?  168 LYS   A N      1 
ATOM   2273  C  CA     . LYS   A 1 143 ? 1.073   -16.350 17.299 1.00 22.58  ?  168 LYS   A CA     1 
ATOM   2274  C  C      . LYS   A 1 143 ? 1.462   -17.551 18.153 1.00 21.72  ?  168 LYS   A C      1 
ATOM   2275  O  O      . LYS   A 1 143 ? 1.208   -18.694 17.758 1.00 23.25  ?  168 LYS   A O      1 
ATOM   2276  C  CB     . LYS   A 1 143 ? 2.212   -16.010 16.336 1.00 22.87  ?  168 LYS   A CB     1 
ATOM   2277  C  CG     . LYS   A 1 143 ? 1.783   -15.252 15.071 1.00 24.20  ?  168 LYS   A CG     1 
ATOM   2278  C  CD     . LYS   A 1 143 ? 1.368   -13.798 15.338 1.00 25.50  ?  168 LYS   A CD     1 
ATOM   2279  C  CE     . LYS   A 1 143 ? 2.534   -12.923 15.810 1.00 25.66  ?  168 LYS   A CE     1 
ATOM   2280  N  NZ     . LYS   A 1 143 ? 2.150   -11.476 16.007 1.00 24.70  ?  168 LYS   A NZ     1 
ATOM   2281  H  H      . LYS   A 1 143 ? 1.260   -14.527 18.045 1.00 26.06  ?  168 LYS   A H      1 
ATOM   2282  H  HA     . LYS   A 1 143 ? 0.295   -16.587 16.770 1.00 27.09  ?  168 LYS   A HA     1 
ATOM   2283  H  HB2    . LYS   A 1 143 ? 2.854   -15.455 16.805 1.00 27.44  ?  168 LYS   A HB2    1 
ATOM   2284  H  HB3    . LYS   A 1 143 ? 2.632   -16.837 16.053 1.00 27.44  ?  168 LYS   A HB3    1 
ATOM   2285  H  HG2    . LYS   A 1 143 ? 2.526   -15.239 14.448 1.00 29.03  ?  168 LYS   A HG2    1 
ATOM   2286  H  HG3    . LYS   A 1 143 ? 1.025   -15.709 14.674 1.00 29.03  ?  168 LYS   A HG3    1 
ATOM   2287  H  HD2    . LYS   A 1 143 ? 1.018   -13.414 14.519 1.00 30.59  ?  168 LYS   A HD2    1 
ATOM   2288  H  HD3    . LYS   A 1 143 ? 0.686   -13.786 16.028 1.00 30.59  ?  168 LYS   A HD3    1 
ATOM   2289  H  HE2    . LYS   A 1 143 ? 2.859   -13.263 16.659 1.00 30.79  ?  168 LYS   A HE2    1 
ATOM   2290  H  HE3    . LYS   A 1 143 ? 3.241   -12.956 15.147 1.00 30.79  ?  168 LYS   A HE3    1 
ATOM   2291  H  HZ1    . LYS   A 1 143 ? 1.512   -11.412 16.625 1.00 29.64  ?  168 LYS   A HZ1    1 
ATOM   2292  H  HZ2    . LYS   A 1 143 ? 1.848   -11.135 15.243 1.00 29.64  ?  168 LYS   A HZ2    1 
ATOM   2293  H  HZ3    . LYS   A 1 143 ? 2.858   -11.007 16.273 1.00 29.64  ?  168 LYS   A HZ3    1 
ATOM   2294  N  N      . LEU   A 1 144 ? 2.101   -17.333 19.307 1.00 20.35  ?  169 LEU   A N      1 
ATOM   2295  C  CA     . LEU   A 1 144 ? 2.414   -18.466 20.176 1.00 20.15  ?  169 LEU   A CA     1 
ATOM   2296  C  C      . LEU   A 1 144 ? 1.135   -19.121 20.689 1.00 18.76  ?  169 LEU   A C      1 
ATOM   2297  O  O      . LEU   A 1 144 ? 1.034   -20.352 20.734 1.00 18.75  ?  169 LEU   A O      1 
ATOM   2298  C  CB     . LEU   A 1 144 ? 3.312   -18.031 21.333 1.00 19.05  ?  169 LEU   A CB     1 
ATOM   2299  C  CG     . LEU   A 1 144 ? 4.716   -17.560 20.932 1.00 19.09  ?  169 LEU   A CG     1 
ATOM   2300  C  CD1    . LEU   A 1 144 ? 5.478   -16.963 22.100 1.00 19.59  ?  169 LEU   A CD1    1 
ATOM   2301  C  CD2    . LEU   A 1 144 ? 5.515   -18.712 20.283 1.00 21.75  ?  169 LEU   A CD2    1 
ATOM   2302  H  H      . LEU   A 1 144 ? 2.354   -16.564 19.598 1.00 24.42  ?  169 LEU   A H      1 
ATOM   2303  H  HA     . LEU   A 1 144 ? 2.911   -19.125 19.666 1.00 24.18  ?  169 LEU   A HA     1 
ATOM   2304  H  HB2    . LEU   A 1 144 ? 2.880   -17.295 21.794 1.00 22.86  ?  169 LEU   A HB2    1 
ATOM   2305  H  HB3    . LEU   A 1 144 ? 3.419   -18.783 21.936 1.00 22.86  ?  169 LEU   A HB3    1 
ATOM   2306  H  HG     . LEU   A 1 144 ? 4.614   -16.853 20.276 1.00 22.91  ?  169 LEU   A HG     1 
ATOM   2307  H  HD11   . LEU   A 1 144 ? 6.359   -16.695 21.798 1.00 23.50  ?  169 LEU   A HD11   1 
ATOM   2308  H  HD12   . LEU   A 1 144 ? 4.993   -16.192 22.432 1.00 23.50  ?  169 LEU   A HD12   1 
ATOM   2309  H  HD13   . LEU   A 1 144 ? 5.557   -17.630 22.800 1.00 23.50  ?  169 LEU   A HD13   1 
ATOM   2310  H  HD21   . LEU   A 1 144 ? 6.431   -18.423 20.147 1.00 26.09  ?  169 LEU   A HD21   1 
ATOM   2311  H  HD22   . LEU   A 1 144 ? 5.495   -19.481 20.873 1.00 26.09  ?  169 LEU   A HD22   1 
ATOM   2312  H  HD23   . LEU   A 1 144 ? 5.109   -18.937 19.432 1.00 26.09  ?  169 LEU   A HD23   1 
ATOM   2313  N  N      . CYS   A 1 145 ? 0.129   -18.321 21.054 1.00 20.00  ?  170 CYS   A N      1 
ATOM   2314  C  CA     . CYS   A 1 145 ? -1.137  -18.921 21.465 1.00 20.69  ?  170 CYS   A CA     1 
ATOM   2315  C  C      . CYS   A 1 145 ? -1.753  -19.728 20.318 1.00 21.12  ?  170 CYS   A C      1 
ATOM   2316  O  O      . CYS   A 1 145 ? -2.194  -20.865 20.515 1.00 22.23  ?  170 CYS   A O      1 
ATOM   2317  C  CB     . CYS   A 1 145 ? -2.103  -17.842 21.949 1.00 21.58  ?  170 CYS   A CB     1 
ATOM   2318  S  SG     . CYS   A 1 145 ? -3.627  -18.564 22.633 1.00 23.60  ?  170 CYS   A SG     1 
ATOM   2319  H  H      . CYS   A 1 145 ? 0.156   -17.462 21.072 1.00 23.99  ?  170 CYS   A H      1 
ATOM   2320  H  HA     . CYS   A 1 145 ? -0.976  -19.523 22.208 1.00 24.82  ?  170 CYS   A HA     1 
ATOM   2321  H  HB2    . CYS   A 1 145 ? -1.675  -17.318 22.644 1.00 25.89  ?  170 CYS   A HB2    1 
ATOM   2322  H  HB3    . CYS   A 1 145 ? -2.344  -17.270 21.204 1.00 25.89  ?  170 CYS   A HB3    1 
ATOM   2323  H  HG     . CYS   A 1 145 ? -4.351  -17.678 22.995 1.00 28.31  ?  170 CYS   A HG     1 
ATOM   2324  N  N      . ASN   A 1 146 ? -1.750  -19.165 19.106 1.00 21.84  ?  171 ASN   A N      1 
ATOM   2325  C  CA     . ASN   A 1 146 ? -2.226  -19.865 17.909 1.00 22.90  ?  171 ASN   A CA     1 
ATOM   2326  C  C      . ASN   A 1 146 ? -1.498  -21.198 17.717 1.00 23.78  ?  171 ASN   A C      1 
ATOM   2327  O  O      . ASN   A 1 146 ? -2.135  -22.251 17.556 1.00 23.96  ?  171 ASN   A O      1 
ATOM   2328  C  CB     . ASN   A 1 146 ? -2.021  -18.910 16.715 1.00 23.50  ?  171 ASN   A CB     1 
ATOM   2329  C  CG     . ASN   A 1 146 ? -2.848  -19.261 15.493 1.00 26.13  ?  171 ASN   A CG     1 
ATOM   2330  O  OD1    . ASN   A 1 146 ? -3.293  -20.395 15.316 1.00 27.55  ?  171 ASN   A OD1    1 
ATOM   2331  N  ND2    . ASN   A 1 146 ? -3.028  -18.272 14.612 1.00 27.21  ?  171 ASN   A ND2    1 
ATOM   2332  H  H      . ASN   A 1 146 ? -1.474  -18.367 18.946 1.00 26.20  ?  171 ASN   A H      1 
ATOM   2333  H  HA     . ASN   A 1 146 ? -3.167  -20.086 17.982 1.00 27.48  ?  171 ASN   A HA     1 
ATOM   2334  H  HB2    . ASN   A 1 146 ? -2.267  -18.013 16.989 1.00 28.19  ?  171 ASN   A HB2    1 
ATOM   2335  H  HB3    . ASN   A 1 146 ? -1.087  -18.933 16.455 1.00 28.19  ?  171 ASN   A HB3    1 
ATOM   2336  H  HD21   . ASN   A 1 146 ? -3.489  -18.410 13.899 1.00 32.65  ?  171 ASN   A HD21   1 
ATOM   2337  H  HD22   . ASN   A 1 146 ? -2.684  -17.498 14.759 1.00 32.65  ?  171 ASN   A HD22   1 
ATOM   2338  N  N      . ILE   A 1 147 ? -0.162  -21.171 17.769 1.00 22.20  ?  172 ILE   A N      1 
ATOM   2339  C  CA     . ILE   A 1 147 ? 0.650   -22.369 17.537 1.00 21.89  ?  172 ILE   A CA     1 
ATOM   2340  C  C      . ILE   A 1 147 ? 0.341   -23.457 18.557 1.00 20.66  ?  172 ILE   A C      1 
ATOM   2341  O  O      . ILE   A 1 147 ? 0.384   -24.651 18.233 1.00 21.24  ?  172 ILE   A O      1 
ATOM   2342  C  CB     . ILE   A 1 147 ? 2.146   -21.985 17.550 1.00 22.51  ?  172 ILE   A CB     1 
ATOM   2343  C  CG1    . ILE   A 1 147 ? 2.508   -21.204 16.277 1.00 23.36  ?  172 ILE   A CG1    1 
ATOM   2344  C  CG2    . ILE   A 1 147 ? 3.036   -23.215 17.665 1.00 24.06  ?  172 ILE   A CG2    1 
ATOM   2345  C  CD1    . ILE   A 1 147 ? 3.792   -20.418 16.364 1.00 24.27  ?  172 ILE   A CD1    1 
ATOM   2346  H  H      . ILE   A 1 147 ? 0.303   -20.467 17.937 1.00 26.63  ?  172 ILE   A H      1 
ATOM   2347  H  HA     . ILE   A 1 147 ? 0.428   -22.728 16.664 1.00 26.26  ?  172 ILE   A HA     1 
ATOM   2348  H  HB     . ILE   A 1 147 ? 2.294   -21.424 18.327 1.00 27.01  ?  172 ILE   A HB     1 
ATOM   2349  H  HG12   . ILE   A 1 147 ? 2.600   -21.834 15.545 1.00 28.02  ?  172 ILE   A HG12   1 
ATOM   2350  H  HG13   . ILE   A 1 147 ? 1.794   -20.576 16.087 1.00 28.02  ?  172 ILE   A HG13   1 
ATOM   2351  H  HG21   . ILE   A 1 147 ? 3.940   -22.976 17.406 1.00 28.86  ?  172 ILE   A HG21   1 
ATOM   2352  H  HG22   . ILE   A 1 147 ? 3.027   -23.527 18.583 1.00 28.86  ?  172 ILE   A HG22   1 
ATOM   2353  H  HG23   . ILE   A 1 147 ? 2.696   -23.907 17.077 1.00 28.86  ?  172 ILE   A HG23   1 
ATOM   2354  H  HD11   . ILE   A 1 147 ? 3.887   -19.879 15.563 1.00 29.12  ?  172 ILE   A HD11   1 
ATOM   2355  H  HD12   . ILE   A 1 147 ? 3.760   -19.846 17.146 1.00 29.12  ?  172 ILE   A HD12   1 
ATOM   2356  H  HD13   . ILE   A 1 147 ? 4.536   -21.036 16.437 1.00 29.12  ?  172 ILE   A HD13   1 
ATOM   2357  N  N      . PHE   A 1 148 ? 0.028   -23.082 19.797 1.00 20.70  ?  173 PHE   A N      1 
ATOM   2358  C  CA     . PHE   A 1 148 ? -0.278  -24.065 20.832 1.00 20.17  ?  173 PHE   A CA     1 
ATOM   2359  C  C      . PHE   A 1 148 ? -1.779  -24.260 21.025 1.00 21.64  ?  173 PHE   A C      1 
ATOM   2360  O  O      . PHE   A 1 148 ? -2.216  -24.715 22.088 1.00 21.49  ?  173 PHE   A O      1 
ATOM   2361  C  CB     . PHE   A 1 148 ? 0.440   -23.687 22.132 1.00 18.66  ?  173 PHE   A CB     1 
ATOM   2362  C  CG     . PHE   A 1 148 ? 1.936   -23.919 22.049 1.00 18.27  ?  173 PHE   A CG     1 
ATOM   2363  C  CD1    . PHE   A 1 148 ? 2.464   -25.184 22.256 1.00 20.37  ?  173 PHE   A CD1    1 
ATOM   2364  C  CD2    . PHE   A 1 148 ? 2.799   -22.898 21.693 1.00 20.26  ?  173 PHE   A CD2    1 
ATOM   2365  C  CE1    . PHE   A 1 148 ? 3.818   -25.415 22.135 1.00 20.87  ?  173 PHE   A CE1    1 
ATOM   2366  C  CE2    . PHE   A 1 148 ? 4.149   -23.119 21.583 1.00 21.31  ?  173 PHE   A CE2    1 
ATOM   2367  C  CZ     . PHE   A 1 148 ? 4.662   -24.381 21.796 1.00 21.87  ?  173 PHE   A CZ     1 
ATOM   2368  H  H      . PHE   A 1 148 ? -0.013  -22.265 20.060 1.00 24.83  ?  173 PHE   A H      1 
ATOM   2369  H  HA     . PHE   A 1 148 ? 0.064   -24.932 20.567 1.00 24.19  ?  173 PHE   A HA     1 
ATOM   2370  H  HB2    . PHE   A 1 148 ? 0.290   -22.747 22.316 1.00 22.39  ?  173 PHE   A HB2    1 
ATOM   2371  H  HB3    . PHE   A 1 148 ? 0.090   -24.227 22.857 1.00 22.39  ?  173 PHE   A HB3    1 
ATOM   2372  H  HD1    . PHE   A 1 148 ? 1.897   -25.887 22.479 1.00 24.44  ?  173 PHE   A HD1    1 
ATOM   2373  H  HD2    . PHE   A 1 148 ? 2.459   -22.049 21.526 1.00 24.31  ?  173 PHE   A HD2    1 
ATOM   2374  H  HE1    . PHE   A 1 148 ? 4.160   -26.267 22.283 1.00 25.03  ?  173 PHE   A HE1    1 
ATOM   2375  H  HE2    . PHE   A 1 148 ? 4.718   -22.417 21.364 1.00 25.56  ?  173 PHE   A HE2    1 
ATOM   2376  H  HZ     . PHE   A 1 148 ? 5.576   -24.534 21.712 1.00 26.23  ?  173 PHE   A HZ     1 
ATOM   2377  N  N      . SER   A 1 149 ? -2.564  -23.995 19.972 1.00 22.53  ?  174 SER   A N      1 
ATOM   2378  C  CA     . SER   A 1 149 ? -3.999  -24.246 19.937 1.00 23.53  ?  174 SER   A CA     1 
ATOM   2379  C  C      . SER   A 1 149 ? -4.364  -25.185 18.792 1.00 25.51  ?  174 SER   A C      1 
ATOM   2380  O  O      . SER   A 1 149 ? -3.740  -25.172 17.725 1.00 26.13  ?  174 SER   A O      1 
ATOM   2381  C  CB     . SER   A 1 149 ? -4.792  -22.930 19.778 1.00 24.25  ?  174 SER   A CB     1 
ATOM   2382  O  OG     . SER   A 1 149 ? -4.670  -22.113 20.933 1.00 24.62  ?  174 SER   A OG     1 
ATOM   2383  H  H      . SER   A 1 149 ? -2.270  -23.655 19.238 1.00 27.03  ?  174 SER   A H      1 
ATOM   2384  H  HA     . SER   A 1 149 ? -4.256  -24.674 20.768 1.00 28.23  ?  174 SER   A HA     1 
ATOM   2385  H  HB2    . SER   A 1 149 ? -4.447  -22.446 19.012 1.00 29.09  ?  174 SER   A HB2    1 
ATOM   2386  H  HB3    . SER   A 1 149 ? -5.729  -23.143 19.641 1.00 29.09  ?  174 SER   A HB3    1 
ATOM   2387  H  HG     . SER   A 1 149 ? -3.865  -21.906 21.055 1.00 29.54  ?  174 SER   A HG     1 
ATOM   2388  N  N      . THR   A 1 150 ? -5.395  -26.001 19.020 1.00 25.80  ?  175 THR   A N      1 
ATOM   2389  C  CA     . THR   A 1 150 ? -5.969  -26.790 17.936 1.00 26.54  ?  175 THR   A CA     1 
ATOM   2390  C  C      . THR   A 1 150 ? -6.947  -25.974 17.095 1.00 27.24  ?  175 THR   A C      1 
ATOM   2391  O  O      . THR   A 1 150 ? -7.184  -26.311 15.932 1.00 29.34  ?  175 THR   A O      1 
ATOM   2392  C  CB     . THR   A 1 150 ? -6.686  -28.020 18.491 1.00 29.43  ?  175 THR   A CB     1 
ATOM   2393  O  OG1    . THR   A 1 150 ? -7.781  -27.601 19.315 1.00 32.99  ?  175 THR   A OG1    1 
ATOM   2394  C  CG2    . THR   A 1 150 ? -5.730  -28.880 19.307 1.00 29.38  ?  175 THR   A CG2    1 
ATOM   2395  H  H      . THR   A 1 150 ? -5.774  -26.112 19.784 1.00 30.96  ?  175 THR   A H      1 
ATOM   2396  H  HA     . THR   A 1 150 ? -5.252  -27.103 17.363 1.00 31.85  ?  175 THR   A HA     1 
ATOM   2397  H  HB     . THR   A 1 150 ? -7.021  -28.560 17.758 1.00 35.31  ?  175 THR   A HB     1 
ATOM   2398  H  HG1    . THR   A 1 150 ? -8.177  -28.272 19.630 1.00 39.59  ?  175 THR   A HG1    1 
ATOM   2399  H  HG21   . THR   A 1 150 ? -6.197  -29.657 19.654 1.00 35.25  ?  175 THR   A HG21   1 
ATOM   2400  H  HG22   . THR   A 1 150 ? -4.994  -29.177 18.750 1.00 35.25  ?  175 THR   A HG22   1 
ATOM   2401  H  HG23   . THR   A 1 150 ? -5.376  -28.368 20.051 1.00 35.25  ?  175 THR   A HG23   1 
ATOM   2402  N  N      . LYS   A 1 151 ? -7.502  -24.904 17.663 1.00 28.22  ?  176 LYS   A N      1 
ATOM   2403  C  CA     . LYS   A 1 151 ? -8.439  -24.013 16.991 1.00 29.23  ?  176 LYS   A CA     1 
ATOM   2404  C  C      . LYS   A 1 151 ? -8.207  -22.625 17.574 1.00 28.38  ?  176 LYS   A C      1 
ATOM   2405  O  O      . LYS   A 1 151 ? -8.158  -22.477 18.798 1.00 27.34  ?  176 LYS   A O      1 
ATOM   2406  C  CB     . LYS   A 1 151 ? -9.879  -24.467 17.212 1.00 32.72  ?  176 LYS   A CB     1 
ATOM   2407  C  CG     . LYS   A 1 151 ? -10.903 -23.753 16.362 1.00 37.23  ?  176 LYS   A CG     1 
ATOM   2408  C  CD     . LYS   A 1 151 ? -12.279 -24.403 16.490 1.00 40.54  ?  176 LYS   A CD     1 
ATOM   2409  C  CE     . LYS   A 1 151 ? -13.340 -23.582 15.771 1.00 44.49  ?  176 LYS   A CE     1 
ATOM   2410  N  NZ     . LYS   A 1 151 ? -14.714 -24.142 15.933 1.00 47.23  ?  176 LYS   A NZ     1 
ATOM   2411  H  H      . LYS   A 1 151 ? -7.345  -24.665 18.474 1.00 33.86  ?  176 LYS   A H      1 
ATOM   2412  H  HA     . LYS   A 1 151 ? -8.286  -23.993 16.034 1.00 35.07  ?  176 LYS   A HA     1 
ATOM   2413  H  HB2    . LYS   A 1 151 ? -9.938  -25.414 17.009 1.00 39.25  ?  176 LYS   A HB2    1 
ATOM   2414  H  HB3    . LYS   A 1 151 ? -10.112 -24.312 18.141 1.00 39.25  ?  176 LYS   A HB3    1 
ATOM   2415  H  HG2    . LYS   A 1 151 ? -10.973 -22.829 16.649 1.00 44.67  ?  176 LYS   A HG2    1 
ATOM   2416  H  HG3    . LYS   A 1 151 ? -10.632 -23.792 15.431 1.00 44.67  ?  176 LYS   A HG3    1 
ATOM   2417  H  HD2    . LYS   A 1 151 ? -12.256 -25.289 16.094 1.00 48.65  ?  176 LYS   A HD2    1 
ATOM   2418  H  HD3    . LYS   A 1 151 ? -12.521 -24.465 17.427 1.00 48.65  ?  176 LYS   A HD3    1 
ATOM   2419  H  HE2    . LYS   A 1 151 ? -13.340 -22.681 16.131 1.00 53.39  ?  176 LYS   A HE2    1 
ATOM   2420  H  HE3    . LYS   A 1 151 ? -13.135 -23.561 14.824 1.00 53.39  ?  176 LYS   A HE3    1 
ATOM   2421  H  HZ1    . LYS   A 1 151 ? -15.303 -23.633 15.501 1.00 56.67  ?  176 LYS   A HZ1    1 
ATOM   2422  H  HZ2    . LYS   A 1 151 ? -14.748 -24.967 15.602 1.00 56.67  ?  176 LYS   A HZ2    1 
ATOM   2423  H  HZ3    . LYS   A 1 151 ? -14.933 -24.168 16.795 1.00 56.67  ?  176 LYS   A HZ3    1 
ATOM   2424  N  N      . PHE   A 1 152 ? -8.060  -21.619 16.713 1.00 28.57  ?  177 PHE   A N      1 
ATOM   2425  C  CA     . PHE   A 1 152 ? -7.739  -20.259 17.152 1.00 27.56  ?  177 PHE   A CA     1 
ATOM   2426  C  C      . PHE   A 1 152 ? -8.491  -19.286 16.256 1.00 29.05  ?  177 PHE   A C      1 
ATOM   2427  O  O      . PHE   A 1 152 ? -8.184  -19.183 15.064 1.00 30.57  ?  177 PHE   A O      1 
ATOM   2428  C  CB     . PHE   A 1 152 ? -6.225  -20.023 17.089 1.00 27.13  ?  177 PHE   A CB     1 
ATOM   2429  C  CG     . PHE   A 1 152 ? -5.777  -18.678 17.596 1.00 26.23  ?  177 PHE   A CG     1 
ATOM   2430  C  CD1    . PHE   A 1 152 ? -5.660  -17.607 16.721 1.00 27.32  ?  177 PHE   A CD1    1 
ATOM   2431  C  CD2    . PHE   A 1 152 ? -5.433  -18.486 18.934 1.00 25.32  ?  177 PHE   A CD2    1 
ATOM   2432  C  CE1    . PHE   A 1 152 ? -5.232  -16.361 17.165 1.00 27.09  ?  177 PHE   A CE1    1 
ATOM   2433  C  CE2    . PHE   A 1 152 ? -5.007  -17.239 19.391 1.00 24.19  ?  177 PHE   A CE2    1 
ATOM   2434  C  CZ     . PHE   A 1 152 ? -4.904  -16.174 18.500 1.00 24.29  ?  177 PHE   A CZ     1 
ATOM   2435  H  H      . PHE   A 1 152 ? -8.141  -21.699 15.861 1.00 34.28  ?  177 PHE   A H      1 
ATOM   2436  H  HA     . PHE   A 1 152 ? -8.039  -20.119 18.064 1.00 33.07  ?  177 PHE   A HA     1 
ATOM   2437  H  HB2    . PHE   A 1 152 ? -5.785  -20.699 17.628 1.00 32.55  ?  177 PHE   A HB2    1 
ATOM   2438  H  HB3    . PHE   A 1 152 ? -5.940  -20.097 16.165 1.00 32.55  ?  177 PHE   A HB3    1 
ATOM   2439  H  HD1    . PHE   A 1 152 ? -5.872  -17.725 15.823 1.00 32.78  ?  177 PHE   A HD1    1 
ATOM   2440  H  HD2    . PHE   A 1 152 ? -5.489  -19.199 19.529 1.00 30.37  ?  177 PHE   A HD2    1 
ATOM   2441  H  HE1    . PHE   A 1 152 ? -5.166  -15.652 16.567 1.00 32.50  ?  177 PHE   A HE1    1 
ATOM   2442  H  HE2    . PHE   A 1 152 ? -4.793  -17.119 20.288 1.00 29.02  ?  177 PHE   A HE2    1 
ATOM   2443  H  HZ     . PHE   A 1 152 ? -4.616  -15.341 18.798 1.00 29.14  ?  177 PHE   A HZ     1 
ATOM   2444  N  N      . THR   A 1 153 ? -9.468  -18.572 16.818 1.00 29.37  ?  178 THR   A N      1 
ATOM   2445  C  CA     . THR   A 1 153 ? -10.331 -17.682 16.050 1.00 30.82  ?  178 THR   A CA     1 
ATOM   2446  C  C      . THR   A 1 153 ? -10.101 -16.224 16.427 1.00 30.64  ?  178 THR   A C      1 
ATOM   2447  O  O      . THR   A 1 153 ? -10.067 -15.875 17.614 1.00 30.95  ?  178 THR   A O      1 
ATOM   2448  C  CB     . THR   A 1 153 ? -11.803 -18.046 16.267 1.00 32.74  ?  178 THR   A CB     1 
ATOM   2449  O  OG1    . THR   A 1 153 ? -12.039 -19.387 15.824 1.00 33.48  ?  178 THR   A OG1    1 
ATOM   2450  C  CG2    . THR   A 1 153 ? -12.718 -17.109 15.484 1.00 34.09  ?  178 THR   A CG2    1 
ATOM   2451  H  H      . THR   A 1 153 ? -9.650  -18.589 17.658 1.00 35.23  ?  178 THR   A H      1 
ATOM   2452  H  HA     . THR   A 1 153 ? -10.107 -17.775 15.111 1.00 36.97  ?  178 THR   A HA     1 
ATOM   2453  H  HB     . THR   A 1 153 ? -12.010 -17.965 17.212 1.00 39.28  ?  178 THR   A HB     1 
ATOM   2454  H  HG1    . THR   A 1 153 ? -11.553 -19.921 16.253 1.00 40.17  ?  178 THR   A HG1    1 
ATOM   2455  H  HG21   . THR   A 1 153 ? -13.612 -17.482 15.435 1.00 40.91  ?  178 THR   A HG21   1 
ATOM   2456  H  HG22   . THR   A 1 153 ? -12.762 -16.245 15.923 1.00 40.91  ?  178 THR   A HG22   1 
ATOM   2457  H  HG23   . THR   A 1 153 ? -12.378 -16.988 14.584 1.00 40.91  ?  178 THR   A HG23   1 
ATOM   2458  N  N      . VAL   A 1 154 ? -9.958  -15.379 15.403 1.00 31.84  ?  179 VAL   A N      1 
ATOM   2459  C  CA     . VAL   A 1 154 ? -9.824  -13.932 15.549 1.00 31.87  ?  179 VAL   A CA     1 
ATOM   2460  C  C      . VAL   A 1 154 ? -11.056 -13.273 14.944 1.00 33.66  ?  179 VAL   A C      1 
ATOM   2461  O  O      . VAL   A 1 154 ? -11.343 -13.471 13.759 1.00 34.48  ?  179 VAL   A O      1 
ATOM   2462  C  CB     . VAL   A 1 154 ? -8.565  -13.399 14.847 1.00 32.75  ?  179 VAL   A CB     1 
ATOM   2463  C  CG1    . VAL   A 1 154 ? -8.512  -11.867 14.932 1.00 34.90  ?  179 VAL   A CG1    1 
ATOM   2464  C  CG2    . VAL   A 1 154 ? -7.317  -14.022 15.422 1.00 32.46  ?  179 VAL   A CG2    1 
ATOM   2465  H  H      . VAL   A 1 154 ? -9.936  -15.633 14.582 1.00 38.20  ?  179 VAL   A H      1 
ATOM   2466  H  HA     . VAL   A 1 154 ? -9.780  -13.725 16.496 1.00 38.23  ?  179 VAL   A HA     1 
ATOM   2467  H  HB     . VAL   A 1 154 ? -8.605  -13.646 13.910 1.00 39.29  ?  179 VAL   A HB     1 
ATOM   2468  H  HG11   . VAL   A 1 154 ? -7.613  -11.570 14.719 1.00 41.88  ?  179 VAL   A HG11   1 
ATOM   2469  H  HG12   . VAL   A 1 154 ? -9.143  -11.493 14.298 1.00 41.88  ?  179 VAL   A HG12   1 
ATOM   2470  H  HG13   . VAL   A 1 154 ? -8.746  -11.593 15.833 1.00 41.88  ?  179 VAL   A HG13   1 
ATOM   2471  H  HG21   . VAL   A 1 154 ? -6.549  -13.714 14.915 1.00 38.94  ?  179 VAL   A HG21   1 
ATOM   2472  H  HG22   . VAL   A 1 154 ? -7.229  -13.755 16.350 1.00 38.94  ?  179 VAL   A HG22   1 
ATOM   2473  H  HG23   . VAL   A 1 154 ? -7.388  -14.987 15.360 1.00 38.94  ?  179 VAL   A HG23   1 
ATOM   2474  N  N      . GLU   A 1 155 ? -11.762 -12.472 15.742 1.00 32.90  ?  180 GLU   A N      1 
ATOM   2475  C  CA     . GLU   A 1 155 ? -12.879 -11.653 15.276 1.00 34.54  ?  180 GLU   A CA     1 
ATOM   2476  C  C      . GLU   A 1 155 ? -12.603 -10.217 15.709 1.00 35.90  ?  180 GLU   A C      1 
ATOM   2477  O  O      . GLU   A 1 155 ? -12.306 -9.973  16.880 1.00 35.56  ?  180 GLU   A O      1 
ATOM   2478  C  CB     . GLU   A 1 155 ? -14.220 -12.144 15.843 1.00 36.49  ?  180 GLU   A CB     1 
ATOM   2479  C  CG     . GLU   A 1 155 ? -15.439 -11.363 15.289 1.00 39.40  ?  180 GLU   A CG     1 
ATOM   2480  C  CD     . GLU   A 1 155 ? -16.797 -11.922 15.707 1.00 41.27  ?  180 GLU   A CD     1 
ATOM   2481  O  OE1    . GLU   A 1 155 ? -16.914 -13.146 15.939 1.00 42.09  ?  180 GLU   A OE1    1 
ATOM   2482  O  OE2    . GLU   A 1 155 ? -17.761 -11.132 15.773 1.00 41.85  ?  180 GLU   A OE2    1 
ATOM   2483  H  H      . GLU   A 1 155 ? -11.608 -12.383 16.583 1.00 39.47  ?  180 GLU   A H      1 
ATOM   2484  H  HA     . GLU   A 1 155 ? -12.948 -11.690 14.309 1.00 41.44  ?  180 GLU   A HA     1 
ATOM   2485  H  HB2    . GLU   A 1 155 ? -14.335 -13.080 15.612 1.00 43.79  ?  180 GLU   A HB2    1 
ATOM   2486  H  HB3    . GLU   A 1 155 ? -14.211 -12.040 16.807 1.00 43.79  ?  180 GLU   A HB3    1 
ATOM   2487  H  HG2    . GLU   A 1 155 ? -15.390 -10.448 15.608 1.00 47.27  ?  180 GLU   A HG2    1 
ATOM   2488  H  HG3    . GLU   A 1 155 ? -15.402 -11.379 14.320 1.00 47.27  ?  180 GLU   A HG3    1 
ATOM   2489  N  N      . THR   A 1 156 ? -12.665 -9.271  14.778 1.00 36.69  ?  181 THR   A N      1 
ATOM   2490  C  CA     . THR   A 1 156 ? -12.378 -7.882  15.119 1.00 36.82  ?  181 THR   A CA     1 
ATOM   2491  C  C      . THR   A 1 156 ? -13.148 -6.994  14.156 1.00 38.37  ?  181 THR   A C      1 
ATOM   2492  O  O      . THR   A 1 156 ? -13.285 -7.323  12.977 1.00 38.31  ?  181 THR   A O      1 
ATOM   2493  C  CB     . THR   A 1 156 ? -10.874 -7.578  15.072 1.00 38.65  ?  181 THR   A CB     1 
ATOM   2494  O  OG1    . THR   A 1 156 ? -10.615 -6.275  15.616 1.00 38.23  ?  181 THR   A OG1    1 
ATOM   2495  C  CG2    . THR   A 1 156 ? -10.347 -7.634  13.650 1.00 40.88  ?  181 THR   A CG2    1 
ATOM   2496  H  H      . THR   A 1 156 ? -12.868 -9.407  13.954 1.00 44.02  ?  181 THR   A H      1 
ATOM   2497  H  HA     . THR   A 1 156 ? -12.677 -7.689  16.021 1.00 44.18  ?  181 THR   A HA     1 
ATOM   2498  H  HB     . THR   A 1 156 ? -10.408 -8.248  15.597 1.00 46.38  ?  181 THR   A HB     1 
ATOM   2499  H  HG1    . THR   A 1 156 ? -10.890 -6.235  16.409 1.00 45.87  ?  181 THR   A HG1    1 
ATOM   2500  H  HG21   . THR   A 1 156 ? -9.377  -7.657  13.657 1.00 49.05  ?  181 THR   A HG21   1 
ATOM   2501  H  HG22   . THR   A 1 156 ? -10.678 -8.429  13.204 1.00 49.05  ?  181 THR   A HG22   1 
ATOM   2502  H  HG23   . THR   A 1 156 ? -10.640 -6.852  13.157 1.00 49.05  ?  181 THR   A HG23   1 
ATOM   2503  N  N      . ALA   A 1 157 ? -13.656 -5.881  14.670 1.00 37.98  ?  182 ALA   A N      1 
ATOM   2504  C  CA     . ALA   A 1 157 ? -14.550 -5.003  13.929 1.00 38.14  ?  182 ALA   A CA     1 
ATOM   2505  C  C      . ALA   A 1 157 ? -14.009 -3.584  13.963 1.00 38.52  ?  182 ALA   A C      1 
ATOM   2506  O  O      . ALA   A 1 157 ? -13.624 -3.092  15.028 1.00 38.08  ?  182 ALA   A O      1 
ATOM   2507  C  CB     . ALA   A 1 157 ? -15.958 -5.053  14.527 1.00 38.40  ?  182 ALA   A CB     1 
ATOM   2508  H  H      . ALA   A 1 157 ? -13.492 -5.606  15.468 1.00 45.58  ?  182 ALA   A H      1 
ATOM   2509  H  HA     . ALA   A 1 157 ? -14.593 -5.280  13.001 1.00 45.76  ?  182 ALA   A HA     1 
ATOM   2510  H  HB1    . ALA   A 1 157 ? -16.562 -4.554  13.956 1.00 46.07  ?  182 ALA   A HB1    1 
ATOM   2511  H  HB2    . ALA   A 1 157 ? -16.245 -5.979  14.583 1.00 46.07  ?  182 ALA   A HB2    1 
ATOM   2512  H  HB3    . ALA   A 1 157 ? -15.940 -4.659  15.413 1.00 46.07  ?  182 ALA   A HB3    1 
ATOM   2513  N  N      . SER   A 1 158 ? -14.005 -2.923  12.805 1.00 38.14  ?  183 SER   A N      1 
ATOM   2514  C  CA     . SER   A 1 158 ? -13.390 -1.603  12.643 1.00 38.56  ?  183 SER   A CA     1 
ATOM   2515  C  C      . SER   A 1 158 ? -14.394 -0.671  11.982 1.00 39.44  ?  183 SER   A C      1 
ATOM   2516  O  O      . SER   A 1 158 ? -14.605 -0.760  10.772 1.00 40.71  ?  183 SER   A O      1 
ATOM   2517  C  CB     . SER   A 1 158 ? -12.133 -1.682  11.795 1.00 40.66  ?  183 SER   A CB     1 
ATOM   2518  O  OG     . SER   A 1 158 ? -11.595 -0.401  11.511 1.00 42.86  ?  183 SER   A OG     1 
ATOM   2519  H  H      . SER   A 1 158 ? -14.359 -3.225  12.082 1.00 45.76  ?  183 SER   A H      1 
ATOM   2520  H  HA     . SER   A 1 158 ? -13.172 -1.261  13.524 1.00 46.27  ?  183 SER   A HA     1 
ATOM   2521  H  HB2    . SER   A 1 158 ? -11.467 -2.198  12.275 1.00 48.78  ?  183 SER   A HB2    1 
ATOM   2522  H  HB3    . SER   A 1 158 ? -12.351 -2.119  10.957 1.00 48.78  ?  183 SER   A HB3    1 
ATOM   2523  H  HG     . SER   A 1 158 ? -11.419 0.002   12.226 1.00 51.42  ?  183 SER   A HG     1 
ATOM   2524  N  N      . ARG   A 1 159 ? -14.988 0.231   12.754 1.00 38.11  ?  184 ARG   A N      1 
ATOM   2525  C  CA     . ARG   A 1 159 ? -15.893 1.197   12.145 1.00 39.32  ?  184 ARG   A CA     1 
ATOM   2526  C  C      . ARG   A 1 159 ? -15.151 2.095   11.159 1.00 39.67  ?  184 ARG   A C      1 
ATOM   2527  O  O      . ARG   A 1 159 ? -15.698 2.476   10.119 1.00 39.72  ?  184 ARG   A O      1 
ATOM   2528  C  CB     . ARG   A 1 159 ? -16.591 2.019   13.222 1.00 42.31  ?  184 ARG   A CB     1 
ATOM   2529  C  CG     . ARG   A 1 159 ? -17.697 2.899   12.659 1.00 45.47  ?  184 ARG   A CG     1 
ATOM   2530  C  CD     . ARG   A 1 159 ? -18.466 3.641   13.735 1.00 47.80  ?  184 ARG   A CD     1 
ATOM   2531  N  NE     . ARG   A 1 159 ? -19.407 4.544   13.082 1.00 51.48  ?  184 ARG   A NE     1 
ATOM   2532  C  CZ     . ARG   A 1 159 ? -19.389 5.871   13.188 1.00 53.98  ?  184 ARG   A CZ     1 
ATOM   2533  N  NH1    . ARG   A 1 159 ? -18.506 6.478   13.967 1.00 55.29  ?  184 ARG   A NH1    1 
ATOM   2534  N  NH2    . ARG   A 1 159 ? -20.287 6.586   12.531 1.00 54.70  ?  184 ARG   A NH2    1 
ATOM   2535  H  H      . ARG   A 1 159 ? -14.889 0.303   13.605 1.00 45.73  ?  184 ARG   A H      1 
ATOM   2536  H  HA     . ARG   A 1 159 ? -16.580 0.720   11.654 1.00 47.18  ?  184 ARG   A HA     1 
ATOM   2537  H  HB2    . ARG   A 1 159 ? -16.986 1.418   13.873 1.00 50.77  ?  184 ARG   A HB2    1 
ATOM   2538  H  HB3    . ARG   A 1 159 ? -15.939 2.593   13.654 1.00 50.77  ?  184 ARG   A HB3    1 
ATOM   2539  H  HG2    . ARG   A 1 159 ? -17.304 3.557   12.064 1.00 54.55  ?  184 ARG   A HG2    1 
ATOM   2540  H  HG3    . ARG   A 1 159 ? -18.325 2.343   12.171 1.00 54.55  ?  184 ARG   A HG3    1 
ATOM   2541  H  HD2    . ARG   A 1 159 ? -18.959 3.013   14.286 1.00 57.35  ?  184 ARG   A HD2    1 
ATOM   2542  H  HD3    . ARG   A 1 159 ? -17.857 4.159   14.284 1.00 57.35  ?  184 ARG   A HD3    1 
ATOM   2543  H  HE     . ARG   A 1 159 ? -20.019 4.193   12.590 1.00 61.77  ?  184 ARG   A HE     1 
ATOM   2544  H  HH11   . ARG   A 1 159 ? -17.934 6.014   14.411 1.00 66.34  ?  184 ARG   A HH11   1 
ATOM   2545  H  HH12   . ARG   A 1 159 ? -18.504 7.336   14.028 1.00 66.34  ?  184 ARG   A HH12   1 
ATOM   2546  H  HH21   . ARG   A 1 159 ? -20.875 6.193   12.041 1.00 65.64  ?  184 ARG   A HH21   1 
ATOM   2547  H  HH22   . ARG   A 1 159 ? -20.284 7.444   12.595 1.00 65.64  ?  184 ARG   A HH22   1 
ATOM   2548  N  N      . GLU   A 1 160 ? -13.893 2.439   11.459 1.00 39.92  ?  185 GLU   A N      1 
ATOM   2549  C  CA     . GLU   A 1 160 ? -13.146 3.297   10.540 1.00 42.77  ?  185 GLU   A CA     1 
ATOM   2550  C  C      . GLU   A 1 160 ? -13.161 2.727   9.124  1.00 43.86  ?  185 GLU   A C      1 
ATOM   2551  O  O      . GLU   A 1 160 ? -13.343 3.464   8.150  1.00 44.52  ?  185 GLU   A O      1 
ATOM   2552  C  CB     . GLU   A 1 160 ? -11.707 3.488   11.020 1.00 45.88  ?  185 GLU   A CB     1 
ATOM   2553  C  CG     . GLU   A 1 160 ? -10.843 4.227   10.016 1.00 48.52  ?  185 GLU   A CG     1 
ATOM   2554  C  CD     . GLU   A 1 160 ? -9.482  4.584   10.566 1.00 52.43  ?  185 GLU   A CD     1 
ATOM   2555  O  OE1    . GLU   A 1 160 ? -9.198  4.222   11.724 1.00 53.65  ?  185 GLU   A OE1    1 
ATOM   2556  O  OE2    . GLU   A 1 160 ? -8.697  5.226   9.840  1.00 54.40  ?  185 GLU   A OE2    1 
ATOM   2557  H  H      . GLU   A 1 160 ? -13.465 2.195   12.164 1.00 47.90  ?  185 GLU   A H      1 
ATOM   2558  H  HA     . GLU   A 1 160 ? -13.567 4.171   10.527 1.00 51.32  ?  185 GLU   A HA     1 
ATOM   2559  H  HB2    . GLU   A 1 160 ? -11.715 4.002   11.843 1.00 55.05  ?  185 GLU   A HB2    1 
ATOM   2560  H  HB3    . GLU   A 1 160 ? -11.308 2.618   11.176 1.00 55.05  ?  185 GLU   A HB3    1 
ATOM   2561  H  HG2    . GLU   A 1 160 ? -10.713 3.665   9.236  1.00 58.21  ?  185 GLU   A HG2    1 
ATOM   2562  H  HG3    . GLU   A 1 160 ? -11.288 5.050   9.761  1.00 58.21  ?  185 GLU   A HG3    1 
ATOM   2563  N  N      . TYR   A 1 161 ? -12.990 1.414   8.992  1.00 43.99  ?  186 TYR   A N      1 
ATOM   2564  C  CA     . TYR   A 1 161 ? -12.995 0.748   7.694  1.00 44.73  ?  186 TYR   A CA     1 
ATOM   2565  C  C      . TYR   A 1 161 ? -14.346 0.135   7.349  1.00 44.99  ?  186 TYR   A C      1 
ATOM   2566  O  O      . TYR   A 1 161 ? -14.487 -0.468  6.280  1.00 46.27  ?  186 TYR   A O      1 
ATOM   2567  C  CB     . TYR   A 1 161 ? -11.887 -0.311  7.672  1.00 44.57  ?  186 TYR   A CB     1 
ATOM   2568  C  CG     . TYR   A 1 161 ? -10.513 0.324   7.597  1.00 45.78  ?  186 TYR   A CG     1 
ATOM   2569  C  CD1    . TYR   A 1 161 ? -9.825  0.690   8.750  1.00 45.13  ?  186 TYR   A CD1    1 
ATOM   2570  C  CD2    . TYR   A 1 161 ? -9.921  0.593   6.369  1.00 47.22  ?  186 TYR   A CD2    1 
ATOM   2571  C  CE1    . TYR   A 1 161 ? -8.579  1.295   8.676  1.00 47.54  ?  186 TYR   A CE1    1 
ATOM   2572  C  CE2    . TYR   A 1 161 ? -8.674  1.188   6.284  1.00 49.45  ?  186 TYR   A CE2    1 
ATOM   2573  C  CZ     . TYR   A 1 161 ? -8.005  1.536   7.438  1.00 50.50  ?  186 TYR   A CZ     1 
ATOM   2574  O  OH     . TYR   A 1 161 ? -6.763  2.130   7.349  1.00 53.29  ?  186 TYR   A OH     1 
ATOM   2575  H  H      . TYR   A 1 161 ? -12.867 0.877   9.653  1.00 52.78  ?  186 TYR   A H      1 
ATOM   2576  H  HA     . TYR   A 1 161 ? -12.801 1.390   6.994  1.00 53.66  ?  186 TYR   A HA     1 
ATOM   2577  H  HB2    . TYR   A 1 161 ? -11.935 -0.842  8.482  1.00 53.48  ?  186 TYR   A HB2    1 
ATOM   2578  H  HB3    . TYR   A 1 161 ? -12.003 -0.880  6.895  1.00 53.48  ?  186 TYR   A HB3    1 
ATOM   2579  H  HD1    . TYR   A 1 161 ? -10.207 0.528   9.583  1.00 54.15  ?  186 TYR   A HD1    1 
ATOM   2580  H  HD2    . TYR   A 1 161 ? -10.373 0.368   5.587  1.00 56.65  ?  186 TYR   A HD2    1 
ATOM   2581  H  HE1    . TYR   A 1 161 ? -8.130  1.537   9.453  1.00 57.04  ?  186 TYR   A HE1    1 
ATOM   2582  H  HE2    . TYR   A 1 161 ? -8.289  1.353   5.453  1.00 59.33  ?  186 TYR   A HE2    1 
ATOM   2583  H  HH     . TYR   A 1 161 ? -6.542  2.214   6.543  1.00 63.94  ?  186 TYR   A HH     1 
ATOM   2584  N  N      . LYS   A 1 162 ? -15.337 0.288   8.222  1.00 44.77  ?  187 LYS   A N      1 
ATOM   2585  C  CA     . LYS   A 1 162 ? -16.697 -0.185  7.976  1.00 44.07  ?  187 LYS   A CA     1 
ATOM   2586  C  C      . LYS   A 1 162 ? -16.749 -1.675  7.664  1.00 44.19  ?  187 LYS   A C      1 
ATOM   2587  O  O      . LYS   A 1 162 ? -17.536 -2.119  6.829  1.00 44.74  ?  187 LYS   A O      1 
ATOM   2588  C  CB     . LYS   A 1 162 ? -17.344 0.622   6.843  1.00 46.14  ?  187 LYS   A CB     1 
ATOM   2589  C  CG     . LYS   A 1 162 ? -17.478 2.097   7.160  1.00 48.61  ?  187 LYS   A CG     1 
ATOM   2590  C  CD     . LYS   A 1 162 ? -18.890 2.422   7.650  1.00 52.84  ?  187 LYS   A CD     1 
ATOM   2591  C  CE     . LYS   A 1 162 ? -19.390 3.777   7.130  1.00 55.52  ?  187 LYS   A CE     1 
ATOM   2592  N  NZ     . LYS   A 1 162 ? -18.923 4.895   7.994  1.00 57.82  ?  187 LYS   A NZ     1 
ATOM   2593  H  H      . LYS   A 1 162 ? -15.245 0.673   8.986  1.00 53.72  ?  187 LYS   A H      1 
ATOM   2594  H  HA     . LYS   A 1 162 ? -17.208 -0.056  8.790  1.00 52.88  ?  187 LYS   A HA     1 
ATOM   2595  H  HB2    . LYS   A 1 162 ? -16.798 0.536   6.046  1.00 55.36  ?  187 LYS   A HB2    1 
ATOM   2596  H  HB3    . LYS   A 1 162 ? -18.232 0.270   6.676  1.00 55.36  ?  187 LYS   A HB3    1 
ATOM   2597  H  HG2    . LYS   A 1 162 ? -16.848 2.337   7.858  1.00 58.33  ?  187 LYS   A HG2    1 
ATOM   2598  H  HG3    . LYS   A 1 162 ? -17.302 2.618   6.361  1.00 58.33  ?  187 LYS   A HG3    1 
ATOM   2599  H  HD2    . LYS   A 1 162 ? -19.501 1.736   7.339  1.00 63.41  ?  187 LYS   A HD2    1 
ATOM   2600  H  HD3    . LYS   A 1 162 ? -18.892 2.453   8.620  1.00 63.41  ?  187 LYS   A HD3    1 
ATOM   2601  H  HE2    . LYS   A 1 162 ? -19.052 3.922   6.232  1.00 66.62  ?  187 LYS   A HE2    1 
ATOM   2602  H  HE3    . LYS   A 1 162 ? -20.360 3.780   7.122  1.00 66.62  ?  187 LYS   A HE3    1 
ATOM   2603  H  HZ1    . LYS   A 1 162 ? -19.215 5.672   7.671  1.00 69.37  ?  187 LYS   A HZ1    1 
ATOM   2604  H  HZ2    . LYS   A 1 162 ? -19.235 4.791   8.821  1.00 69.37  ?  187 LYS   A HZ2    1 
ATOM   2605  H  HZ3    . LYS   A 1 162 ? -18.034 4.909   8.020  1.00 69.37  ?  187 LYS   A HZ3    1 
ATOM   2606  N  N      . LYS   A 1 163 ? -15.936 -2.464  8.357  1.00 42.40  ?  188 LYS   A N      1 
ATOM   2607  C  CA     . LYS   A 1 163 ? -15.900 -3.894  8.092  1.00 43.81  ?  188 LYS   A CA     1 
ATOM   2608  C  C      . LYS   A 1 163 ? -15.570 -4.648  9.369  1.00 43.94  ?  188 LYS   A C      1 
ATOM   2609  O  O      . LYS   A 1 163 ? -14.922 -4.114  10.271 1.00 43.22  ?  188 LYS   A O      1 
ATOM   2610  C  CB     . LYS   A 1 163 ? -14.859 -4.249  7.026  1.00 47.66  ?  188 LYS   A CB     1 
ATOM   2611  C  CG     . LYS   A 1 163 ? -15.281 -4.016  5.590  1.00 53.47  ?  188 LYS   A CG     1 
ATOM   2612  C  CD     . LYS   A 1 163 ? -14.056 -4.085  4.689  1.00 57.16  ?  188 LYS   A CD     1 
ATOM   2613  C  CE     . LYS   A 1 163 ? -14.423 -3.919  3.230  1.00 59.37  ?  188 LYS   A CE     1 
ATOM   2614  N  NZ     . LYS   A 1 163 ? -13.207 -3.921  2.369  1.00 61.34  ?  188 LYS   A NZ     1 
ATOM   2615  H  H      . LYS   A 1 163 ? -15.404 -2.198  8.978  1.00 50.88  ?  188 LYS   A H      1 
ATOM   2616  H  HA     . LYS   A 1 163 ? -16.778 -4.168  7.787  1.00 52.57  ?  188 LYS   A HA     1 
ATOM   2617  H  HB2    . LYS   A 1 163 ? -14.067 -3.711  7.184  1.00 57.18  ?  188 LYS   A HB2    1 
ATOM   2618  H  HB3    . LYS   A 1 163 ? -14.644 -5.190  7.113  1.00 57.18  ?  188 LYS   A HB3    1 
ATOM   2619  H  HG2    . LYS   A 1 163 ? -15.911 -4.700  5.316  1.00 64.15  ?  188 LYS   A HG2    1 
ATOM   2620  H  HG3    . LYS   A 1 163 ? -15.685 -3.138  5.503  1.00 64.15  ?  188 LYS   A HG3    1 
ATOM   2621  H  HD2    . LYS   A 1 163 ? -13.441 -3.375  4.930  1.00 68.59  ?  188 LYS   A HD2    1 
ATOM   2622  H  HD3    . LYS   A 1 163 ? -13.627 -4.948  4.798  1.00 68.59  ?  188 LYS   A HD3    1 
ATOM   2623  H  HE2    . LYS   A 1 163 ? -14.995 -4.653  2.955  1.00 71.24  ?  188 LYS   A HE2    1 
ATOM   2624  H  HE3    . LYS   A 1 163 ? -14.885 -3.075  3.107  1.00 71.24  ?  188 LYS   A HE3    1 
ATOM   2625  H  HZ1    . LYS   A 1 163 ? -13.438 -3.825  1.515  1.00 73.60  ?  188 LYS   A HZ1    1 
ATOM   2626  H  HZ2    . LYS   A 1 163 ? -12.669 -3.251  2.600  1.00 73.60  ?  188 LYS   A HZ2    1 
ATOM   2627  H  HZ3    . LYS   A 1 163 ? -12.767 -4.690  2.464  1.00 73.60  ?  188 LYS   A HZ3    1 
ATOM   2628  N  N      . MET   A 1 164 ? -16.029 -5.892  9.435  1.00 43.88  ?  189 MET   A N      1 
ATOM   2629  C  CA     . MET   A 1 164 ? -15.634 -6.833  10.473 1.00 43.93  ?  189 MET   A CA     1 
ATOM   2630  C  C      . MET   A 1 164 ? -14.923 -8.013  9.820  1.00 42.49  ?  189 MET   A C      1 
ATOM   2631  O  O      . MET   A 1 164 ? -15.312 -8.460  8.735  1.00 41.10  ?  189 MET   A O      1 
ATOM   2632  C  CB     . MET   A 1 164 ? -16.841 -7.311  11.287 1.00 47.74  ?  189 MET   A CB     1 
ATOM   2633  C  CG     . MET   A 1 164 ? -16.483 -8.279  12.410 1.00 53.60  ?  189 MET   A CG     1 
ATOM   2634  S  SD     . MET   A 1 164 ? -16.606 -10.015 11.931 1.00 58.35  ?  189 MET   A SD     1 
ATOM   2635  C  CE     . MET   A 1 164 ? -18.379 -10.253 12.028 1.00 59.85  ?  189 MET   A CE     1 
ATOM   2636  H  H      . MET   A 1 164 ? -16.588 -6.224  8.871  1.00 52.65  ?  189 MET   A H      1 
ATOM   2637  H  HA     . MET   A 1 164 ? -15.028 -6.403  11.096 1.00 52.71  ?  189 MET   A HA     1 
ATOM   2638  H  HB2    . MET   A 1 164 ? -17.272 -6.539  11.687 1.00 57.28  ?  189 MET   A HB2    1 
ATOM   2639  H  HB3    . MET   A 1 164 ? -17.459 -7.764  10.691 1.00 57.28  ?  189 MET   A HB3    1 
ATOM   2640  H  HG2    . MET   A 1 164 ? -15.569 -8.111  12.688 1.00 64.31  ?  189 MET   A HG2    1 
ATOM   2641  H  HG3    . MET   A 1 164 ? -17.088 -8.133  13.154 1.00 64.31  ?  189 MET   A HG3    1 
ATOM   2642  H  HE1    . MET   A 1 164 ? -18.588 -11.168 11.784 1.00 71.81  ?  189 MET   A HE1    1 
ATOM   2643  H  HE2    . MET   A 1 164 ? -18.672 -10.077 12.935 1.00 71.81  ?  189 MET   A HE2    1 
ATOM   2644  H  HE3    . MET   A 1 164 ? -18.814 -9.640  11.415 1.00 71.81  ?  189 MET   A HE3    1 
ATOM   2645  N  N      . PHE   A 1 165 ? -13.884 -8.507  10.499 1.00 39.25  ?  190 PHE   A N      1 
ATOM   2646  C  CA     . PHE   A 1 165 ? -13.017 -9.590  10.046 1.00 38.19  ?  190 PHE   A CA     1 
ATOM   2647  C  C      . PHE   A 1 165 ? -13.208 -10.795 10.958 1.00 37.69  ?  190 PHE   A C      1 
ATOM   2648  O  O      . PHE   A 1 165 ? -13.270 -10.645 12.182 1.00 37.50  ?  190 PHE   A O      1 
ATOM   2649  C  CB     . PHE   A 1 165 ? -11.537 -9.142  10.086 1.00 37.94  ?  190 PHE   A CB     1 
ATOM   2650  C  CG     . PHE   A 1 165 ? -10.522 -10.264 9.910  1.00 37.72  ?  190 PHE   A CG     1 
ATOM   2651  C  CD1    . PHE   A 1 165 ? -10.232 -11.148 10.948 1.00 36.51  ?  190 PHE   A CD1    1 
ATOM   2652  C  CD2    . PHE   A 1 165 ? -9.824  -10.394 8.721  1.00 37.66  ?  190 PHE   A CD2    1 
ATOM   2653  C  CE1    . PHE   A 1 165 ? -9.300  -12.160 10.789 1.00 36.83  ?  190 PHE   A CE1    1 
ATOM   2654  C  CE2    . PHE   A 1 165 ? -8.894  -11.402 8.555  1.00 37.94  ?  190 PHE   A CE2    1 
ATOM   2655  C  CZ     . PHE   A 1 165 ? -8.628  -12.287 9.595  1.00 37.67  ?  190 PHE   A CZ     1 
ATOM   2656  H  H      . PHE   A 1 165 ? -13.650 -8.210  11.272 1.00 47.09  ?  190 PHE   A H      1 
ATOM   2657  H  HA     . PHE   A 1 165 ? -13.243 -9.845  9.138  1.00 45.83  ?  190 PHE   A HA     1 
ATOM   2658  H  HB2    . PHE   A 1 165 ? -11.390 -8.502  9.371  1.00 45.52  ?  190 PHE   A HB2    1 
ATOM   2659  H  HB3    . PHE   A 1 165 ? -11.364 -8.726  10.945 1.00 45.52  ?  190 PHE   A HB3    1 
ATOM   2660  H  HD1    . PHE   A 1 165 ? -10.672 -11.057 11.762 1.00 43.81  ?  190 PHE   A HD1    1 
ATOM   2661  H  HD2    . PHE   A 1 165 ? -9.983  -9.796  8.027  1.00 45.18  ?  190 PHE   A HD2    1 
ATOM   2662  H  HE1    . PHE   A 1 165 ? -9.129  -12.751 11.487 1.00 44.20  ?  190 PHE   A HE1    1 
ATOM   2663  H  HE2    . PHE   A 1 165 ? -8.444  -11.489 7.746  1.00 45.52  ?  190 PHE   A HE2    1 
ATOM   2664  H  HZ     . PHE   A 1 165 ? -7.998  -12.962 9.483  1.00 45.19  ?  190 PHE   A HZ     1 
ATOM   2665  N  N      . LYS   A 1 166 ? -13.273 -11.993 10.372 1.00 37.41  ?  191 LYS   A N      1 
ATOM   2666  C  CA     . LYS   A 1 166 ? -13.260 -13.204 11.183 1.00 38.18  ?  191 LYS   A CA     1 
ATOM   2667  C  C      . LYS   A 1 166 ? -12.551 -14.342 10.464 1.00 38.07  ?  191 LYS   A C      1 
ATOM   2668  O  O      . LYS   A 1 166 ? -12.832 -14.620 9.295  1.00 38.29  ?  191 LYS   A O      1 
ATOM   2669  C  CB     . LYS   A 1 166 ? -14.690 -13.630 11.551 1.00 38.20  ?  191 LYS   A CB     1 
ATOM   2670  C  CG     . LYS   A 1 166 ? -14.739 -14.905 12.366 1.00 41.57  ?  191 LYS   A CG     1 
ATOM   2671  C  CD     . LYS   A 1 166 ? -16.138 -15.210 12.860 1.00 44.76  ?  191 LYS   A CD     1 
ATOM   2672  C  CE     . LYS   A 1 166 ? -16.159 -16.540 13.600 1.00 46.78  ?  191 LYS   A CE     1 
ATOM   2673  N  NZ     . LYS   A 1 166 ? -17.529 -16.940 14.024 1.00 47.85  ?  191 LYS   A NZ     1 
ATOM   2674  H  H      . LYS   A 1 166 ? -13.324 -12.124 9.524  1.00 44.89  ?  191 LYS   A H      1 
ATOM   2675  H  HA     . LYS   A 1 166 ? -12.753 -13.021 11.990 1.00 45.81  ?  191 LYS   A HA     1 
ATOM   2676  H  HB2    . LYS   A 1 166 ? -15.103 -12.925 12.073 1.00 45.83  ?  191 LYS   A HB2    1 
ATOM   2677  H  HB3    . LYS   A 1 166 ? -15.193 -13.777 10.735 1.00 45.83  ?  191 LYS   A HB3    1 
ATOM   2678  H  HG2    . LYS   A 1 166 ? -14.444 -15.647 11.815 1.00 49.88  ?  191 LYS   A HG2    1 
ATOM   2679  H  HG3    . LYS   A 1 166 ? -14.159 -14.813 13.138 1.00 49.88  ?  191 LYS   A HG3    1 
ATOM   2680  H  HD2    . LYS   A 1 166 ? -16.428 -14.512 13.468 1.00 53.71  ?  191 LYS   A HD2    1 
ATOM   2681  H  HD3    . LYS   A 1 166 ? -16.745 -15.266 12.105 1.00 53.71  ?  191 LYS   A HD3    1 
ATOM   2682  H  HE2    . LYS   A 1 166 ? -15.812 -17.233 13.016 1.00 56.13  ?  191 LYS   A HE2    1 
ATOM   2683  H  HE3    . LYS   A 1 166 ? -15.607 -16.469 14.394 1.00 56.13  ?  191 LYS   A HE3    1 
ATOM   2684  H  HZ1    . LYS   A 1 166 ? -17.501 -17.724 14.445 1.00 57.42  ?  191 LYS   A HZ1    1 
ATOM   2685  H  HZ2    . LYS   A 1 166 ? -17.867 -16.328 14.575 1.00 57.42  ?  191 LYS   A HZ2    1 
ATOM   2686  H  HZ3    . LYS   A 1 166 ? -18.059 -17.012 13.313 1.00 57.42  ?  191 LYS   A HZ3    1 
ATOM   2687  N  N      . GLN   A 1 167 ? -11.648 -15.012 11.174 1.00 36.60  ?  192 GLN   A N      1 
ATOM   2688  C  CA     . GLN   A 1 167 ? -10.952 -16.147 10.590 1.00 37.46  ?  192 GLN   A CA     1 
ATOM   2689  C  C      . GLN   A 1 167 ? -10.465 -17.071 11.693 1.00 37.08  ?  192 GLN   A C      1 
ATOM   2690  O  O      . GLN   A 1 167 ? -10.110 -16.626 12.788 1.00 37.34  ?  192 GLN   A O      1 
ATOM   2691  C  CB     . GLN   A 1 167 ? -9.768  -15.705 9.725  1.00 39.97  ?  192 GLN   A CB     1 
ATOM   2692  C  CG     . GLN   A 1 167 ? -9.182  -16.839 8.901  1.00 41.82  ?  192 GLN   A CG     1 
ATOM   2693  C  CD     . GLN   A 1 167 ? -8.244  -16.357 7.817  1.00 44.17  ?  192 GLN   A CD     1 
ATOM   2694  O  OE1    . GLN   A 1 167 ? -7.586  -15.325 7.966  1.00 45.81  ?  192 GLN   A OE1    1 
ATOM   2695  N  NE2    . GLN   A 1 167 ? -8.193  -17.089 6.706  1.00 44.41  ?  192 GLN   A NE2    1 
ATOM   2696  H  H      . GLN   A 1 167 ? -11.426 -14.830 11.985 1.00 43.91  ?  192 GLN   A H      1 
ATOM   2697  H  HA     . GLN   A 1 167 ? -11.577 -16.639 10.036 1.00 44.95  ?  192 GLN   A HA     1 
ATOM   2698  H  HB2    . GLN   A 1 167 ? -10.065 -15.012 9.115  1.00 47.96  ?  192 GLN   A HB2    1 
ATOM   2699  H  HB3    . GLN   A 1 167 ? -9.068  -15.360 10.302 1.00 47.96  ?  192 GLN   A HB3    1 
ATOM   2700  H  HG2    . GLN   A 1 167 ? -8.684  -17.430 9.486  1.00 50.17  ?  192 GLN   A HG2    1 
ATOM   2701  H  HG3    . GLN   A 1 167 ? -9.905  -17.326 8.476  1.00 50.17  ?  192 GLN   A HG3    1 
ATOM   2702  H  HE21   . GLN   A 1 167 ? -8.678  -17.796 6.633  1.00 53.28  ?  192 GLN   A HE21   1 
ATOM   2703  H  HE22   . GLN   A 1 167 ? -7.675  -16.856 6.060  1.00 53.28  ?  192 GLN   A HE22   1 
ATOM   2704  N  N      . THR   A 1 168 ? -10.458 -18.363 11.378 1.00 36.53  ?  193 THR   A N      1 
ATOM   2705  C  CA     . THR   A 1 168 ? -10.046 -19.413 12.300 1.00 37.08  ?  193 THR   A CA     1 
ATOM   2706  C  C      . THR   A 1 168 ? -8.817  -20.116 11.744 1.00 35.44  ?  193 THR   A C      1 
ATOM   2707  O  O      . THR   A 1 168 ? -8.782  -20.455 10.555 1.00 38.43  ?  193 THR   A O      1 
ATOM   2708  C  CB     . THR   A 1 168 ? -11.177 -20.426 12.511 1.00 37.84  ?  193 THR   A CB     1 
ATOM   2709  O  OG1    . THR   A 1 168 ? -12.298 -19.774 13.122 1.00 39.15  ?  193 THR   A OG1    1 
ATOM   2710  C  CG2    . THR   A 1 168 ? -10.723 -21.572 13.403 1.00 37.90  ?  193 THR   A CG2    1 
ATOM   2711  H  H      . THR   A 1 168 ? -10.697 -18.665 10.610 1.00 43.83  ?  193 THR   A H      1 
ATOM   2712  H  HA     . THR   A 1 168 ? -9.814  -19.022 13.156 1.00 44.49  ?  193 THR   A HA     1 
ATOM   2713  H  HB     . THR   A 1 168 ? -11.438 -20.794 11.652 1.00 45.40  ?  193 THR   A HB     1 
ATOM   2714  H  HG1    . THR   A 1 168 ? -12.070 -19.441 13.859 1.00 46.97  ?  193 THR   A HG1    1 
ATOM   2715  H  HG21   . THR   A 1 168 ? -11.492 -22.082 13.704 1.00 45.48  ?  193 THR   A HG21   1 
ATOM   2716  H  HG22   . THR   A 1 168 ? -10.129 -22.160 12.911 1.00 45.48  ?  193 THR   A HG22   1 
ATOM   2717  H  HG23   . THR   A 1 168 ? -10.253 -21.225 14.177 1.00 45.48  ?  193 THR   A HG23   1 
ATOM   2718  N  N      . TRP   A 1 169 ? -7.813  -20.309 12.605 1.00 32.64  ?  194 TRP   A N      1 
ATOM   2719  C  CA     . TRP   A 1 169 ? -6.646  -21.144 12.351 1.00 31.93  ?  194 TRP   A CA     1 
ATOM   2720  C  C      . TRP   A 1 169 ? -6.820  -22.481 13.070 1.00 31.99  ?  194 TRP   A C      1 
ATOM   2721  O  O      . TRP   A 1 169 ? -7.510  -22.569 14.090 1.00 32.27  ?  194 TRP   A O      1 
ATOM   2722  C  CB     . TRP   A 1 169 ? -5.367  -20.445 12.831 1.00 31.97  ?  194 TRP   A CB     1 
ATOM   2723  C  CG     . TRP   A 1 169 ? -4.930  -19.286 11.971 1.00 33.64  ?  194 TRP   A CG     1 
ATOM   2724  C  CD1    . TRP   A 1 169 ? -3.933  -19.286 11.030 1.00 34.16  ?  194 TRP   A CD1    1 
ATOM   2725  C  CD2    . TRP   A 1 169 ? -5.480  -17.962 11.970 1.00 32.91  ?  194 TRP   A CD2    1 
ATOM   2726  N  NE1    . TRP   A 1 169 ? -3.828  -18.038 10.455 1.00 34.36  ?  194 TRP   A NE1    1 
ATOM   2727  C  CE2    . TRP   A 1 169 ? -4.770  -17.212 11.009 1.00 33.56  ?  194 TRP   A CE2    1 
ATOM   2728  C  CE3    . TRP   A 1 169 ? -6.505  -17.337 12.687 1.00 33.60  ?  194 TRP   A CE3    1 
ATOM   2729  C  CZ2    . TRP   A 1 169 ? -5.054  -15.868 10.748 1.00 34.54  ?  194 TRP   A CZ2    1 
ATOM   2730  C  CZ3    . TRP   A 1 169 ? -6.783  -16.004 12.426 1.00 34.49  ?  194 TRP   A CZ3    1 
ATOM   2731  C  CH2    . TRP   A 1 169 ? -6.058  -15.286 11.470 1.00 34.71  ?  194 TRP   A CH2    1 
ATOM   2732  H  H      . TRP   A 1 169 ? -7.788  -19.946 13.384 1.00 39.16  ?  194 TRP   A H      1 
ATOM   2733  H  HA     . TRP   A 1 169 ? -6.551  -21.311 11.401 1.00 38.31  ?  194 TRP   A HA     1 
ATOM   2734  H  HB2    . TRP   A 1 169 ? -5.517  -20.106 13.727 1.00 38.35  ?  194 TRP   A HB2    1 
ATOM   2735  H  HB3    . TRP   A 1 169 ? -4.645  -21.093 12.838 1.00 38.35  ?  194 TRP   A HB3    1 
ATOM   2736  H  HD1    . TRP   A 1 169 ? -3.405  -20.020 10.812 1.00 40.98  ?  194 TRP   A HD1    1 
ATOM   2737  H  HE1    . TRP   A 1 169 ? -3.263  -17.814 9.847  1.00 41.22  ?  194 TRP   A HE1    1 
ATOM   2738  H  HE3    . TRP   A 1 169 ? -6.991  -17.807 13.326 1.00 40.32  ?  194 TRP   A HE3    1 
ATOM   2739  H  HZ2    . TRP   A 1 169 ? -4.578  -15.388 10.109 1.00 41.44  ?  194 TRP   A HZ2    1 
ATOM   2740  H  HZ3    . TRP   A 1 169 ? -7.464  -15.580 12.895 1.00 41.38  ?  194 TRP   A HZ3    1 
ATOM   2741  H  HH2    . TRP   A 1 169 ? -6.264  -14.392 11.322 1.00 41.65  ?  194 TRP   A HH2    1 
ATOM   2742  N  N      . MET   A 1 170 ? -6.218  -23.532 12.514 1.00 32.19  ?  195 MET   A N      1 
ATOM   2743  C  CA     . MET   A 1 170 ? -6.326  -24.855 13.115 1.00 32.63  ?  195 MET   A CA     1 
ATOM   2744  C  C      . MET   A 1 170 ? -4.970  -25.545 13.130 1.00 32.13  ?  195 MET   A C      1 
ATOM   2745  O  O      . MET   A 1 170 ? -4.055  -25.192 12.383 1.00 32.49  ?  195 MET   A O      1 
ATOM   2746  C  CB     . MET   A 1 170 ? -7.323  -25.763 12.371 1.00 35.90  ?  195 MET   A CB     1 
ATOM   2747  C  CG     . MET   A 1 170 ? -8.694  -25.168 12.203 1.00 40.05  ?  195 MET   A CG     1 
ATOM   2748  S  SD     . MET   A 1 170 ? -8.780  -23.979 10.839 1.00 45.10  ?  195 MET   A SD     1 
ATOM   2749  C  CE     . MET   A 1 170 ? -10.531 -24.046 10.453 1.00 46.30  ?  195 MET   A CE     1 
ATOM   2750  H  H      . MET   A 1 170 ? -5.747  -23.502 11.796 1.00 38.62  ?  195 MET   A H      1 
ATOM   2751  H  HA     . MET   A 1 170 ? -6.636  -24.725 14.025 1.00 39.15  ?  195 MET   A HA     1 
ATOM   2752  H  HB2    . MET   A 1 170 ? -6.972  -25.948 11.486 1.00 43.07  ?  195 MET   A HB2    1 
ATOM   2753  H  HB3    . MET   A 1 170 ? -7.420  -26.590 12.869 1.00 43.07  ?  195 MET   A HB3    1 
ATOM   2754  H  HG2    . MET   A 1 170 ? -9.327  -25.879 12.020 1.00 48.06  ?  195 MET   A HG2    1 
ATOM   2755  H  HG3    . MET   A 1 170 ? -8.941  -24.705 13.019 1.00 48.06  ?  195 MET   A HG3    1 
ATOM   2756  H  HE1    . MET   A 1 170 ? -10.717 -23.435 9.724  1.00 55.55  ?  195 MET   A HE1    1 
ATOM   2757  H  HE2    . MET   A 1 170 ? -10.763 -24.952 10.194 1.00 55.55  ?  195 MET   A HE2    1 
ATOM   2758  H  HE3    . MET   A 1 170 ? -11.038 -23.788 11.239 1.00 55.55  ?  195 MET   A HE3    1 
ATOM   2759  N  N      . ASP   A 1 171 ? -4.854  -26.548 13.997 1.00 30.62  ?  196 ASP   A N      1 
ATOM   2760  C  CA     . ASP   A 1 171 ? -3.766  -27.517 13.932 1.00 32.27  ?  196 ASP   A CA     1 
ATOM   2761  C  C      . ASP   A 1 171 ? -2.404  -26.842 14.113 1.00 30.68  ?  196 ASP   A C      1 
ATOM   2762  O  O      . ASP   A 1 171 ? -1.498  -26.972 13.283 1.00 31.36  ?  196 ASP   A O      1 
ATOM   2763  C  CB     . ASP   A 1 171 ? -3.813  -28.285 12.606 1.00 34.57  ?  196 ASP   A CB     1 
ATOM   2764  C  CG     . ASP   A 1 171 ? -5.129  -29.002 12.382 1.00 38.47  ?  196 ASP   A CG     1 
ATOM   2765  O  OD1    . ASP   A 1 171 ? -5.800  -29.366 13.372 1.00 39.98  ?  196 ASP   A OD1    1 
ATOM   2766  O  OD2    . ASP   A 1 171 ? -5.481  -29.212 11.202 1.00 40.48  ?  196 ASP   A OD2    1 
ATOM   2767  H  H      . ASP   A 1 171 ? -5.404  -26.690 14.643 1.00 36.74  ?  196 ASP   A H      1 
ATOM   2768  H  HA     . ASP   A 1 171 ? -3.879  -28.143 14.665 1.00 38.72  ?  196 ASP   A HA     1 
ATOM   2769  H  HB2    . ASP   A 1 171 ? -3.685  -27.660 11.875 1.00 41.48  ?  196 ASP   A HB2    1 
ATOM   2770  H  HB3    . ASP   A 1 171 ? -3.107  -28.949 12.602 1.00 41.48  ?  196 ASP   A HB3    1 
ATOM   2771  N  N      . ASN   A 1 172 ? -2.268  -26.123 15.228 1.00 27.95  ?  197 ASN   A N      1 
ATOM   2772  C  CA     . ASN   A 1 172 ? -0.999  -25.492 15.601 1.00 26.41  ?  197 ASN   A CA     1 
ATOM   2773  C  C      . ASN   A 1 172 ? -0.552  -24.488 14.537 1.00 27.32  ?  197 ASN   A C      1 
ATOM   2774  O  O      . ASN   A 1 172 ? 0.605   -24.460 14.106 1.00 27.82  ?  197 ASN   A O      1 
ATOM   2775  C  CB     . ASN   A 1 172 ? 0.062   -26.564 15.856 1.00 26.59  ?  197 ASN   A CB     1 
ATOM   2776  C  CG     . ASN   A 1 172 ? -0.434  -27.655 16.793 1.00 26.61  ?  197 ASN   A CG     1 
ATOM   2777  O  OD1    . ASN   A 1 172 ? -0.586  -28.809 16.394 1.00 29.26  ?  197 ASN   A OD1    1 
ATOM   2778  N  ND2    . ASN   A 1 172 ? -0.708  -27.287 18.042 1.00 25.24  ?  197 ASN   A ND2    1 
ATOM   2779  H  H      . ASN   A 1 172 ? -2.903  -25.984 15.792 1.00 33.53  ?  197 ASN   A H      1 
ATOM   2780  H  HA     . ASN   A 1 172 ? -1.119  -24.987 16.421 1.00 31.69  ?  197 ASN   A HA     1 
ATOM   2781  H  HB2    . ASN   A 1 172 ? 0.306   -26.977 15.013 1.00 31.91  ?  197 ASN   A HB2    1 
ATOM   2782  H  HB3    . ASN   A 1 172 ? 0.841   -26.150 16.259 1.00 31.91  ?  197 ASN   A HB3    1 
ATOM   2783  H  HD21   . ASN   A 1 172 ? -0.992  -27.868 18.609 1.00 30.29  ?  197 ASN   A HD21   1 
ATOM   2784  H  HD22   . ASN   A 1 172 ? -0.602  -26.468 18.282 1.00 30.29  ?  197 ASN   A HD22   1 
ATOM   2785  N  N      . MET   A 1 173 ? -1.498  -23.635 14.133 1.00 26.54  ?  198 MET   A N      1 
ATOM   2786  C  CA     . MET   A 1 173 ? -1.299  -22.609 13.104 1.00 29.06  ?  198 MET   A CA     1 
ATOM   2787  C  C      . MET   A 1 173 ? -0.824  -23.221 11.786 1.00 31.57  ?  198 MET   A C      1 
ATOM   2788  O  O      . MET   A 1 173 ? -0.167  -22.559 10.981 1.00 33.97  ?  198 MET   A O      1 
ATOM   2789  C  CB     . MET   A 1 173 ? -0.339  -21.508 13.585 1.00 29.28  ?  198 MET   A CB     1 
ATOM   2790  C  CG     . MET   A 1 173 ? -0.598  -20.132 12.933 1.00 30.32  ?  198 MET   A CG     1 
ATOM   2791  S  SD     . MET   A 1 173 ? 0.328   -18.769 13.675 1.00 30.62  ?  198 MET   A SD     1 
ATOM   2792  C  CE     . MET   A 1 173 ? 1.957   -19.088 13.032 1.00 31.05  ?  198 MET   A CE     1 
ATOM   2793  H  H      . MET   A 1 173 ? -2.297  -23.631 14.453 1.00 31.84  ?  198 MET   A H      1 
ATOM   2794  H  HA     . MET   A 1 173 ? -2.153  -22.181 12.935 1.00 34.86  ?  198 MET   A HA     1 
ATOM   2795  H  HB2    . MET   A 1 173 ? -0.438  -21.405 14.544 1.00 35.12  ?  198 MET   A HB2    1 
ATOM   2796  H  HB3    . MET   A 1 173 ? 0.570   -21.771 13.372 1.00 35.12  ?  198 MET   A HB3    1 
ATOM   2797  H  HG2    . MET   A 1 173 ? -0.348  -20.181 11.997 1.00 36.38  ?  198 MET   A HG2    1 
ATOM   2798  H  HG3    . MET   A 1 173 ? -1.542  -19.924 13.014 1.00 36.38  ?  198 MET   A HG3    1 
ATOM   2799  H  HE1    . MET   A 1 173 ? 2.566   -18.411 13.364 1.00 37.25  ?  198 MET   A HE1    1 
ATOM   2800  H  HE2    . MET   A 1 173 ? 2.246   -19.966 13.326 1.00 37.25  ?  198 MET   A HE2    1 
ATOM   2801  H  HE3    . MET   A 1 173 ? 1.925   -19.058 12.063 1.00 37.25  ?  198 MET   A HE3    1 
ATOM   2802  N  N      . GLY   A 1 174 ? -1.205  -24.480 11.532 1.00 31.28  ?  199 GLY   A N      1 
ATOM   2803  C  CA     . GLY   A 1 174 ? -0.807  -25.167 10.311 1.00 33.01  ?  199 GLY   A CA     1 
ATOM   2804  C  C      . GLY   A 1 174 ? -1.705  -24.898 9.127  1.00 36.43  ?  199 GLY   A C      1 
ATOM   2805  O  O      . GLY   A 1 174 ? -1.293  -25.111 7.981  1.00 38.60  ?  199 GLY   A O      1 
ATOM   2806  H  H      . GLY   A 1 174 ? -1.696  -24.955 12.055 1.00 37.53  ?  199 GLY   A H      1 
ATOM   2807  H  HA2    . GLY   A 1 174 ? 0.091   -24.888 10.074 1.00 39.61  ?  199 GLY   A HA2    1 
ATOM   2808  H  HA3    . GLY   A 1 174 ? -0.808  -26.123 10.475 1.00 39.61  ?  199 GLY   A HA3    1 
ATOM   2809  N  N      . ARG   A 1 175 ? -2.923  -24.434 9.380  1.00 37.35  ?  200 ARG   A N      1 
ATOM   2810  C  CA     . ARG   A 1 175 ? -3.843  -24.078 8.312  1.00 38.84  ?  200 ARG   A CA     1 
ATOM   2811  C  C      . ARG   A 1 175 ? -4.831  -23.056 8.851  1.00 39.02  ?  200 ARG   A C      1 
ATOM   2812  O  O      . ARG   A 1 175 ? -4.911  -22.812 10.058 1.00 37.09  ?  200 ARG   A O      1 
ATOM   2813  C  CB     . ARG   A 1 175 ? -4.572  -25.309 7.775  1.00 40.02  ?  200 ARG   A CB     1 
ATOM   2814  C  CG     . ARG   A 1 175 ? -5.335  -26.075 8.837  1.00 41.69  ?  200 ARG   A CG     1 
ATOM   2815  C  CD     . ARG   A 1 175 ? -5.941  -27.345 8.248  1.00 44.31  ?  200 ARG   A CD     1 
ATOM   2816  N  NE     . ARG   A 1 175 ? -6.803  -28.024 9.210  1.00 47.80  ?  200 ARG   A NE     1 
ATOM   2817  C  CZ     . ARG   A 1 175 ? -8.126  -27.884 9.263  1.00 50.60  ?  200 ARG   A CZ     1 
ATOM   2818  N  NH1    . ARG   A 1 175 ? -8.753  -27.092 8.402  1.00 51.76  ?  200 ARG   A NH1    1 
ATOM   2819  N  NH2    . ARG   A 1 175 ? -8.823  -28.539 10.181 1.00 51.27  ?  200 ARG   A NH2    1 
ATOM   2820  H  H      . ARG   A 1 175 ? -3.242  -24.316 10.169 1.00 44.82  ?  200 ARG   A H      1 
ATOM   2821  H  HA     . ARG   A 1 175 ? -3.347  -23.672 7.583  1.00 46.60  ?  200 ARG   A HA     1 
ATOM   2822  H  HB2    . ARG   A 1 175 ? -5.208  -25.026 7.100  1.00 48.02  ?  200 ARG   A HB2    1 
ATOM   2823  H  HB3    . ARG   A 1 175 ? -3.920  -25.912 7.385  1.00 48.02  ?  200 ARG   A HB3    1 
ATOM   2824  H  HG2    . ARG   A 1 175 ? -4.732  -26.325 9.554  1.00 50.03  ?  200 ARG   A HG2    1 
ATOM   2825  H  HG3    . ARG   A 1 175 ? -6.052  -25.523 9.184  1.00 50.03  ?  200 ARG   A HG3    1 
ATOM   2826  H  HD2    . ARG   A 1 175 ? -6.474  -27.115 7.471  1.00 53.16  ?  200 ARG   A HD2    1 
ATOM   2827  H  HD3    . ARG   A 1 175 ? -5.229  -27.953 7.995  1.00 53.16  ?  200 ARG   A HD3    1 
ATOM   2828  H  HE     . ARG   A 1 175 ? -6.432  -28.549 9.781  1.00 57.36  ?  200 ARG   A HE     1 
ATOM   2829  H  HH11   . ARG   A 1 175 ? -8.304  -26.665 7.805  1.00 62.11  ?  200 ARG   A HH11   1 
ATOM   2830  H  HH12   . ARG   A 1 175 ? -9.608  -27.006 8.440  1.00 62.11  ?  200 ARG   A HH12   1 
ATOM   2831  H  HH21   . ARG   A 1 175 ? -8.420  -29.053 10.741 1.00 61.52  ?  200 ARG   A HH21   1 
ATOM   2832  H  HH22   . ARG   A 1 175 ? -9.677  -28.451 10.216 1.00 61.52  ?  200 ARG   A HH22   1 
ATOM   2833  N  N      . ALA   A 1 176 ? -5.580  -22.453 7.931  1.00 40.79  ?  201 ALA   A N      1 
ATOM   2834  C  CA     . ALA   A 1 176 ? -6.631  -21.510 8.269  1.00 40.74  ?  201 ALA   A CA     1 
ATOM   2835  C  C      . ALA   A 1 176 ? -7.870  -21.830 7.447  1.00 41.40  ?  201 ALA   A C      1 
ATOM   2836  O  O      . ALA   A 1 176 ? -7.779  -22.345 6.326  1.00 42.97  ?  201 ALA   A O      1 
ATOM   2837  C  CB     . ALA   A 1 176 ? -6.204  -20.052 8.011  1.00 41.15  ?  201 ALA   A CB     1 
ATOM   2838  H  H      . ALA   A 1 176 ? -5.492  -22.580 7.085  1.00 48.94  ?  201 ALA   A H      1 
ATOM   2839  H  HA     . ALA   A 1 176 ? -6.848  -21.593 9.210  1.00 48.89  ?  201 ALA   A HA     1 
ATOM   2840  H  HB1    . ALA   A 1 176 ? -6.933  -19.461 8.257  1.00 49.37  ?  201 ALA   A HB1    1 
ATOM   2841  H  HB2    . ALA   A 1 176 ? -5.422  -19.852 8.549  1.00 49.37  ?  201 ALA   A HB2    1 
ATOM   2842  H  HB3    . ALA   A 1 176 ? -5.995  -19.945 7.070  1.00 49.37  ?  201 ALA   A HB3    1 
ATOM   2843  N  N      . GLY   A 1 177 ? -9.033  -21.548 8.027  1.00 41.64  ?  202 GLY   A N      1 
ATOM   2844  C  CA     . GLY   A 1 177 ? -10.287 -21.662 7.319  1.00 42.77  ?  202 GLY   A CA     1 
ATOM   2845  C  C      . GLY   A 1 177 ? -10.567 -20.404 6.523  1.00 43.59  ?  202 GLY   A C      1 
ATOM   2846  O  O      . GLY   A 1 177 ? -9.731  -19.506 6.408  1.00 44.39  ?  202 GLY   A O      1 
ATOM   2847  H  H      . GLY   A 1 177 ? -9.115  -21.286 8.842  1.00 49.96  ?  202 GLY   A H      1 
ATOM   2848  H  HA2    . GLY   A 1 177 ? -10.252 -22.417 6.710  1.00 51.31  ?  202 GLY   A HA2    1 
ATOM   2849  H  HA3    . GLY   A 1 177 ? -11.010 -21.800 7.951  1.00 51.31  ?  202 GLY   A HA3    1 
ATOM   2850  N  N      . GLU   A 1 178 ? -11.780 -20.346 5.962  1.00 42.83  ?  203 GLU   A N      1 
ATOM   2851  C  CA     . GLU   A 1 178 ? -12.187 -19.220 5.127  1.00 44.40  ?  203 GLU   A CA     1 
ATOM   2852  C  C      . GLU   A 1 178 ? -12.243 -17.923 5.927  1.00 46.14  ?  203 GLU   A C      1 
ATOM   2853  O  O      . GLU   A 1 178 ? -12.727 -17.893 7.061  1.00 48.43  ?  203 GLU   A O      1 
ATOM   2854  C  CB     . GLU   A 1 178 ? -13.563 -19.508 4.503  1.00 45.99  ?  203 GLU   A CB     1 
ATOM   2855  C  CG     . GLU   A 1 178 ? -13.624 -20.831 3.729  1.00 48.48  ?  203 GLU   A CG     1 
ATOM   2856  C  CD     . GLU   A 1 178 ? -14.930 -21.063 2.960  1.00 51.97  ?  203 GLU   A CD     1 
ATOM   2857  O  OE1    . GLU   A 1 178 ? -15.929 -20.352 3.195  1.00 53.90  ?  203 GLU   A OE1    1 
ATOM   2858  O  OE2    . GLU   A 1 178 ? -14.957 -21.974 2.105  1.00 53.27  ?  203 GLU   A OE2    1 
ATOM   2859  H  H      . GLU   A 1 178 ? -12.386 -20.950 6.052  1.00 51.39  ?  203 GLU   A H      1 
ATOM   2860  H  HA     . GLU   A 1 178 ? -11.534 -19.101 4.419  1.00 53.27  ?  203 GLU   A HA     1 
ATOM   2861  H  HB2    . GLU   A 1 178 ? -14.225 -19.547 5.211  1.00 55.18  ?  203 GLU   A HB2    1 
ATOM   2862  H  HB3    . GLU   A 1 178 ? -13.781 -18.792 3.885  1.00 55.18  ?  203 GLU   A HB3    1 
ATOM   2863  H  HG2    . GLU   A 1 178 ? -12.900 -20.845 3.084  1.00 58.17  ?  203 GLU   A HG2    1 
ATOM   2864  H  HG3    . GLU   A 1 178 ? -13.522 -21.561 4.358  1.00 58.17  ?  203 GLU   A HG3    1 
ATOM   2865  N  N      . MET   A 1 179 ? -11.746 -16.843 5.321  1.00 45.74  ?  204 MET   A N      1 
ATOM   2866  C  CA     . MET   A 1 179 ? -11.837 -15.512 5.915  1.00 46.44  ?  204 MET   A CA     1 
ATOM   2867  C  C      . MET   A 1 179 ? -13.220 -14.937 5.630  1.00 46.90  ?  204 MET   A C      1 
ATOM   2868  O  O      . MET   A 1 179 ? -13.712 -15.027 4.503  1.00 49.44  ?  204 MET   A O      1 
ATOM   2869  C  CB     . MET   A 1 179 ? -10.760 -14.587 5.341  1.00 48.39  ?  204 MET   A CB     1 
ATOM   2870  C  CG     . MET   A 1 179 ? -10.745 -13.191 5.962  1.00 52.11  ?  204 MET   A CG     1 
ATOM   2871  S  SD     . MET   A 1 179 ? -9.756  -11.941 5.101  1.00 55.18  ?  204 MET   A SD     1 
ATOM   2872  C  CE     . MET   A 1 179 ? -8.204  -12.803 4.876  1.00 55.02  ?  204 MET   A CE     1 
ATOM   2873  H  H      . MET   A 1 179 ? -11.348 -16.856 4.559  1.00 54.89  ?  204 MET   A H      1 
ATOM   2874  H  HA     . MET   A 1 179 ? -11.691 -15.574 6.871  1.00 55.72  ?  204 MET   A HA     1 
ATOM   2875  H  HB2    . MET   A 1 179 ? -9.891  -14.988 5.497  1.00 58.06  ?  204 MET   A HB2    1 
ATOM   2876  H  HB3    . MET   A 1 179 ? -10.912 -14.485 4.389  1.00 58.06  ?  204 MET   A HB3    1 
ATOM   2877  H  HG2    . MET   A 1 179 ? -11.658 -12.862 5.990  1.00 62.53  ?  204 MET   A HG2    1 
ATOM   2878  H  HG3    . MET   A 1 179 ? -10.392 -13.263 6.862  1.00 62.53  ?  204 MET   A HG3    1 
ATOM   2879  H  HE1    . MET   A 1 179 ? -7.610  -12.250 4.346  1.00 66.02  ?  204 MET   A HE1    1 
ATOM   2880  H  HE2    . MET   A 1 179 ? -7.809  -12.974 5.746  1.00 66.02  ?  204 MET   A HE2    1 
ATOM   2881  H  HE3    . MET   A 1 179 ? -8.372  -13.642 4.419  1.00 66.02  ?  204 MET   A HE3    1 
ATOM   2882  N  N      . GLU   A 1 180 ? -13.854 -14.366 6.647  1.00 45.61  ?  205 GLU   A N      1 
ATOM   2883  C  CA     . GLU   A 1 180 ? -15.149 -13.724 6.494  1.00 46.51  ?  205 GLU   A CA     1 
ATOM   2884  C  C      . GLU   A 1 180 ? -14.988 -12.226 6.696  1.00 45.95  ?  205 GLU   A C      1 
ATOM   2885  O  O      . GLU   A 1 180 ? -14.453 -11.789 7.717  1.00 44.90  ?  205 GLU   A O      1 
ATOM   2886  C  CB     . GLU   A 1 180 ? -16.174 -14.275 7.493  1.00 48.86  ?  205 GLU   A CB     1 
ATOM   2887  C  CG     . GLU   A 1 180 ? -16.455 -15.756 7.345  1.00 52.57  ?  205 GLU   A CG     1 
ATOM   2888  C  CD     . GLU   A 1 180 ? -17.237 -16.322 8.517  1.00 56.50  ?  205 GLU   A CD     1 
ATOM   2889  O  OE1    . GLU   A 1 180 ? -17.619 -15.543 9.417  1.00 58.12  ?  205 GLU   A OE1    1 
ATOM   2890  O  OE2    . GLU   A 1 180 ? -17.466 -17.551 8.536  1.00 58.33  ?  205 GLU   A OE2    1 
ATOM   2891  H  H      . GLU   A 1 180 ? -13.546 -14.337 7.449  1.00 54.73  ?  205 GLU   A H      1 
ATOM   2892  H  HA     . GLU   A 1 180 ? -15.483 -13.891 5.598  1.00 55.80  ?  205 GLU   A HA     1 
ATOM   2893  H  HB2    . GLU   A 1 180 ? -15.840 -14.128 8.391  1.00 58.62  ?  205 GLU   A HB2    1 
ATOM   2894  H  HB3    . GLU   A 1 180 ? -17.012 -13.803 7.368  1.00 58.62  ?  205 GLU   A HB3    1 
ATOM   2895  H  HG2    . GLU   A 1 180 ? -16.975 -15.901 6.539  1.00 63.08  ?  205 GLU   A HG2    1 
ATOM   2896  H  HG3    . GLU   A 1 180 ? -15.613 -16.234 7.287  1.00 63.08  ?  205 GLU   A HG3    1 
ATOM   2897  N  N      . LEU   A 1 181 ? -15.424 -11.448 5.712  1.00 45.98  ?  206 LEU   A N      1 
ATOM   2898  C  CA     . LEU   A 1 181 ? -15.502 -9.998  5.810  1.00 46.85  ?  206 LEU   A CA     1 
ATOM   2899  C  C      . LEU   A 1 181 ? -16.970 -9.621  5.668  1.00 47.00  ?  206 LEU   A C      1 
ATOM   2900  O  O      . LEU   A 1 181 ? -17.650 -10.113 4.759  1.00 47.63  ?  206 LEU   A O      1 
ATOM   2901  C  CB     . LEU   A 1 181 ? -14.656 -9.321  4.734  1.00 47.52  ?  206 LEU   A CB     1 
ATOM   2902  C  CG     . LEU   A 1 181 ? -13.144 -9.550  4.777  1.00 49.38  ?  206 LEU   A CG     1 
ATOM   2903  C  CD1    . LEU   A 1 181 ? -12.496 -9.102  3.475  1.00 50.43  ?  206 LEU   A CD1    1 
ATOM   2904  C  CD2    . LEU   A 1 181 ? -12.513 -8.818  5.951  1.00 49.90  ?  206 LEU   A CD2    1 
ATOM   2905  H  H      . LEU   A 1 181 ? -15.690 -11.750 4.951  1.00 55.17  ?  206 LEU   A H      1 
ATOM   2906  H  HA     . LEU   A 1 181 ? -15.168 -9.688  6.666  1.00 56.21  ?  206 LEU   A HA     1 
ATOM   2907  H  HB2    . LEU   A 1 181 ? -14.963 -9.639  3.871  1.00 57.01  ?  206 LEU   A HB2    1 
ATOM   2908  H  HB3    . LEU   A 1 181 ? -14.797 -8.364  4.804  1.00 57.01  ?  206 LEU   A HB3    1 
ATOM   2909  H  HG     . LEU   A 1 181 ? -12.983 -10.499 4.891  1.00 59.25  ?  206 LEU   A HG     1 
ATOM   2910  H  HD11   . LEU   A 1 181 ? -11.540 -9.256  3.529  1.00 60.51  ?  206 LEU   A HD11   1 
ATOM   2911  H  HD12   . LEU   A 1 181 ? -12.872 -9.614  2.742  1.00 60.51  ?  206 LEU   A HD12   1 
ATOM   2912  H  HD13   . LEU   A 1 181 ? -12.672 -8.157  3.343  1.00 60.51  ?  206 LEU   A HD13   1 
ATOM   2913  H  HD21   . LEU   A 1 181 ? -11.556 -8.980  5.946  1.00 59.88  ?  206 LEU   A HD21   1 
ATOM   2914  H  HD22   . LEU   A 1 181 ? -12.688 -7.868  5.862  1.00 59.88  ?  206 LEU   A HD22   1 
ATOM   2915  H  HD23   . LEU   A 1 181 ? -12.900 -9.151  6.775  1.00 59.88  ?  206 LEU   A HD23   1 
ATOM   2916  N  N      . LYS   A 1 182 ? -17.464 -8.789  6.580  1.00 45.93  ?  207 LYS   A N      1 
ATOM   2917  C  CA     . LYS   A 1 182 ? -18.841 -8.324  6.542  1.00 47.22  ?  207 LYS   A CA     1 
ATOM   2918  C  C      . LYS   A 1 182 ? -18.888 -6.825  6.792  1.00 45.04  ?  207 LYS   A C      1 
ATOM   2919  O  O      . LYS   A 1 182 ? -18.018 -6.279  7.479  1.00 42.71  ?  207 LYS   A O      1 
ATOM   2920  C  CB     . LYS   A 1 182 ? -19.715 -9.019  7.596  1.00 51.16  ?  207 LYS   A CB     1 
ATOM   2921  C  CG     . LYS   A 1 182 ? -19.856 -10.521 7.444  1.00 54.55  ?  207 LYS   A CG     1 
ATOM   2922  C  CD     . LYS   A 1 182 ? -20.764 -11.085 8.537  1.00 57.54  ?  207 LYS   A CD     1 
ATOM   2923  C  CE     . LYS   A 1 182 ? -20.472 -12.555 8.822  1.00 60.12  ?  207 LYS   A CE     1 
ATOM   2924  N  NZ     . LYS   A 1 182 ? -20.701 -13.423 7.637  1.00 61.57  ?  207 LYS   A NZ     1 
ATOM   2925  H  H      . LYS   A 1 182 ? -17.011 -8.476  7.240  1.00 55.11  ?  207 LYS   A H      1 
ATOM   2926  H  HA     . LYS   A 1 182 ? -19.208 -8.516  5.665  1.00 56.66  ?  207 LYS   A HA     1 
ATOM   2927  H  HB2    . LYS   A 1 182 ? -19.328 -8.853  8.470  1.00 61.39  ?  207 LYS   A HB2    1 
ATOM   2928  H  HB3    . LYS   A 1 182 ? -20.606 -8.640  7.550  1.00 61.39  ?  207 LYS   A HB3    1 
ATOM   2929  H  HG2    . LYS   A 1 182 ? -20.247 -10.725 6.580  1.00 65.45  ?  207 LYS   A HG2    1 
ATOM   2930  H  HG3    . LYS   A 1 182 ? -18.984 -10.938 7.520  1.00 65.45  ?  207 LYS   A HG3    1 
ATOM   2931  H  HD2    . LYS   A 1 182 ? -20.626 -10.585 9.357  1.00 69.04  ?  207 LYS   A HD2    1 
ATOM   2932  H  HD3    . LYS   A 1 182 ? -21.689 -11.010 8.254  1.00 69.04  ?  207 LYS   A HD3    1 
ATOM   2933  H  HE2    . LYS   A 1 182 ? -19.543 -12.648 9.087  1.00 72.13  ?  207 LYS   A HE2    1 
ATOM   2934  H  HE3    . LYS   A 1 182 ? -21.053 -12.862 9.536  1.00 72.13  ?  207 LYS   A HE3    1 
ATOM   2935  H  HZ1    . LYS   A 1 182 ? -20.520 -14.271 7.841  1.00 73.88  ?  207 LYS   A HZ1    1 
ATOM   2936  H  HZ2    . LYS   A 1 182 ? -21.550 -13.364 7.376  1.00 73.88  ?  207 LYS   A HZ2    1 
ATOM   2937  H  HZ3    . LYS   A 1 182 ? -20.175 -13.169 6.966  1.00 73.88  ?  207 LYS   A HZ3    1 
ATOM   2938  N  N      . PRO   A 1 183 ? -19.896 -6.134  6.260  1.00 44.93  ?  208 PRO   A N      1 
ATOM   2939  C  CA     . PRO   A 1 183 ? -20.066 -4.716  6.602  1.00 44.33  ?  208 PRO   A CA     1 
ATOM   2940  C  C      . PRO   A 1 183 ? -20.352 -4.536  8.084  1.00 45.44  ?  208 PRO   A C      1 
ATOM   2941  O  O      . PRO   A 1 183 ? -21.029 -5.351  8.717  1.00 46.32  ?  208 PRO   A O      1 
ATOM   2942  C  CB     . PRO   A 1 183 ? -21.261 -4.276  5.743  1.00 44.63  ?  208 PRO   A CB     1 
ATOM   2943  C  CG     . PRO   A 1 183 ? -21.340 -5.281  4.659  1.00 45.70  ?  208 PRO   A CG     1 
ATOM   2944  C  CD     . PRO   A 1 183 ? -20.869 -6.578  5.244  1.00 45.64  ?  208 PRO   A CD     1 
ATOM   2945  H  HA     . PRO   A 1 183 ? -19.280 -4.206  6.353  1.00 53.19  ?  208 PRO   A HA     1 
ATOM   2946  H  HB2    . PRO   A 1 183 ? -22.070 -4.277  6.278  1.00 53.55  ?  208 PRO   A HB2    1 
ATOM   2947  H  HB3    . PRO   A 1 183 ? -21.101 -3.389  5.385  1.00 53.55  ?  208 PRO   A HB3    1 
ATOM   2948  H  HG2    . PRO   A 1 183 ? -22.258 -5.357  4.354  1.00 54.83  ?  208 PRO   A HG2    1 
ATOM   2949  H  HG3    . PRO   A 1 183 ? -20.768 -5.010  3.924  1.00 54.83  ?  208 PRO   A HG3    1 
ATOM   2950  H  HD2    . PRO   A 1 183 ? -21.602 -7.063  5.653  1.00 54.76  ?  208 PRO   A HD2    1 
ATOM   2951  H  HD3    . PRO   A 1 183 ? -20.441 -7.130  4.571  1.00 54.76  ?  208 PRO   A HD3    1 
ATOM   2952  N  N      . PHE   A 1 184 ? -19.845 -3.431  8.631  1.00 43.63  ?  209 PHE   A N      1 
ATOM   2953  C  CA     . PHE   A 1 184 ? -19.932 -3.155  10.059 1.00 44.41  ?  209 PHE   A CA     1 
ATOM   2954  C  C      . PHE   A 1 184 ? -19.966 -1.646  10.254 1.00 45.67  ?  209 PHE   A C      1 
ATOM   2955  O  O      . PHE   A 1 184 ? -19.189 -0.919  9.630  1.00 46.82  ?  209 PHE   A O      1 
ATOM   2956  C  CB     . PHE   A 1 184 ? -18.748 -3.786  10.823 1.00 44.33  ?  209 PHE   A CB     1 
ATOM   2957  C  CG     . PHE   A 1 184 ? -18.730 -3.455  12.298 1.00 45.04  ?  209 PHE   A CG     1 
ATOM   2958  C  CD1    . PHE   A 1 184 ? -19.572 -4.116  13.183 1.00 45.12  ?  209 PHE   A CD1    1 
ATOM   2959  C  CD2    . PHE   A 1 184 ? -17.881 -2.477  12.796 1.00 46.07  ?  209 PHE   A CD2    1 
ATOM   2960  C  CE1    . PHE   A 1 184 ? -19.571 -3.805  14.536 1.00 45.42  ?  209 PHE   A CE1    1 
ATOM   2961  C  CE2    . PHE   A 1 184 ? -17.880 -2.163  14.146 1.00 46.25  ?  209 PHE   A CE2    1 
ATOM   2962  C  CZ     . PHE   A 1 184 ? -18.732 -2.828  15.015 1.00 45.38  ?  209 PHE   A CZ     1 
ATOM   2963  H  H      . PHE   A 1 184 ? -19.439 -2.817  8.186  1.00 52.35  ?  209 PHE   A H      1 
ATOM   2964  H  HA     . PHE   A 1 184 ? -20.750 -3.525  10.427 1.00 53.29  ?  209 PHE   A HA     1 
ATOM   2965  H  HB2    . PHE   A 1 184 ? -18.799 -4.750  10.736 1.00 53.19  ?  209 PHE   A HB2    1 
ATOM   2966  H  HB3    . PHE   A 1 184 ? -17.919 -3.461  10.437 1.00 53.19  ?  209 PHE   A HB3    1 
ATOM   2967  H  HD1    . PHE   A 1 184 ? -20.144 -4.776  12.865 1.00 54.14  ?  209 PHE   A HD1    1 
ATOM   2968  H  HD2    . PHE   A 1 184 ? -17.307 -2.027  12.218 1.00 55.28  ?  209 PHE   A HD2    1 
ATOM   2969  H  HE1    . PHE   A 1 184 ? -20.139 -4.257  15.117 1.00 54.50  ?  209 PHE   A HE1    1 
ATOM   2970  H  HE2    . PHE   A 1 184 ? -17.307 -1.506  14.470 1.00 55.50  ?  209 PHE   A HE2    1 
ATOM   2971  H  HZ     . PHE   A 1 184 ? -18.735 -2.614  15.919 1.00 54.45  ?  209 PHE   A HZ     1 
ATOM   2972  N  N      . ASN   A 1 185 ? -20.874 -1.179  11.117 1.00 45.65  ?  210 ASN   A N      1 
ATOM   2973  C  CA     . ASN   A 1 185 ? -20.934 0.241   11.454 1.00 46.86  ?  210 ASN   A CA     1 
ATOM   2974  C  C      . ASN   A 1 185 ? -21.369 0.428   12.909 1.00 48.26  ?  210 ASN   A C      1 
ATOM   2975  O  O      . ASN   A 1 185 ? -22.121 1.352   13.235 1.00 50.34  ?  210 ASN   A O      1 
ATOM   2976  C  CB     . ASN   A 1 185 ? -21.872 0.999   10.506 1.00 47.35  ?  210 ASN   A CB     1 
ATOM   2977  C  CG     . ASN   A 1 185 ? -21.692 2.517   10.583 1.00 49.45  ?  210 ASN   A CG     1 
ATOM   2978  O  OD1    . ASN   A 1 185 ? -20.582 3.022   10.754 1.00 51.56  ?  210 ASN   A OD1    1 
ATOM   2979  N  ND2    . ASN   A 1 185 ? -22.793 3.246   10.463 1.00 48.96  ?  210 ASN   A ND2    1 
ATOM   2980  H  H      . ASN   A 1 185 ? -21.461 -1.664  11.518 1.00 54.77  ?  210 ASN   A H      1 
ATOM   2981  H  HA     . ASN   A 1 185 ? -20.045 0.617   11.363 1.00 56.22  ?  210 ASN   A HA     1 
ATOM   2982  H  HB2    . ASN   A 1 185 ? -21.691 0.722   9.594  1.00 56.81  ?  210 ASN   A HB2    1 
ATOM   2983  H  HB3    . ASN   A 1 185 ? -22.790 0.794   10.739 1.00 56.81  ?  210 ASN   A HB3    1 
ATOM   2984  H  HD21   . ASN   A 1 185 ? -22.747 4.104   10.499 1.00 58.75  ?  210 ASN   A HD21   1 
ATOM   2985  H  HD22   . ASN   A 1 185 ? -23.553 2.860   10.349 1.00 58.75  ?  210 ASN   A HD22   1 
ATOM   2986  N  N      . GLY   A 1 186 ? -20.879 -0.429  13.800 1.00 46.96  ?  211 GLY   A N      1 
ATOM   2987  C  CA     . GLY   A 1 186 ? -21.247 -0.334  15.197 1.00 45.82  ?  211 GLY   A CA     1 
ATOM   2988  C  C      . GLY   A 1 186 ? -20.055 -0.005  16.071 1.00 45.13  ?  211 GLY   A C      1 
ATOM   2989  O  O      . GLY   A 1 186 ? -19.104 0.629   15.603 1.00 45.16  ?  211 GLY   A O      1 
ATOM   2990  H  H      . GLY   A 1 186 ? -20.335 -1.069  13.616 1.00 56.35  ?  211 GLY   A H      1 
ATOM   2991  H  HA2    . GLY   A 1 186 ? -21.913 0.362   15.309 1.00 54.97  ?  211 GLY   A HA2    1 
ATOM   2992  H  HA3    . GLY   A 1 186 ? -21.621 -1.179  15.491 1.00 54.97  ?  211 GLY   A HA3    1 
ATOM   2993  N  N      . GLU   A 1 187 ? -20.081 -0.446  17.328 1.00 44.71  ?  212 GLU   A N      1 
ATOM   2994  C  CA     . GLU   A 1 187 ? -19.000 -0.184  18.269 1.00 43.24  ?  212 GLU   A CA     1 
ATOM   2995  C  C      . GLU   A 1 187 ? -17.907 -1.240  18.126 1.00 40.37  ?  212 GLU   A C      1 
ATOM   2996  O  O      . GLU   A 1 187 ? -18.184 -2.439  18.217 1.00 39.68  ?  212 GLU   A O      1 
ATOM   2997  C  CB     . GLU   A 1 187 ? -19.523 -0.178  19.707 1.00 46.04  ?  212 GLU   A CB     1 
ATOM   2998  C  CG     . GLU   A 1 187 ? -20.399 1.009   20.072 1.00 49.69  ?  212 GLU   A CG     1 
ATOM   2999  C  CD     . GLU   A 1 187 ? -19.682 2.339   19.907 1.00 54.67  ?  212 GLU   A CD     1 
ATOM   3000  O  OE1    . GLU   A 1 187 ? -18.587 2.517   20.479 1.00 57.28  ?  212 GLU   A OE1    1 
ATOM   3001  O  OE2    . GLU   A 1 187 ? -20.213 3.205   19.188 1.00 56.80  ?  212 GLU   A OE2    1 
ATOM   3002  H  H      . GLU   A 1 187 ? -20.726 -0.907  17.663 1.00 53.65  ?  212 GLU   A H      1 
ATOM   3003  H  HA     . GLU   A 1 187 ? -18.617 0.686   18.072 1.00 51.88  ?  212 GLU   A HA     1 
ATOM   3004  H  HB2    . GLU   A 1 187 ? -20.050 -0.980  19.845 1.00 55.24  ?  212 GLU   A HB2    1 
ATOM   3005  H  HB3    . GLU   A 1 187 ? -18.763 -0.173  20.310 1.00 55.24  ?  212 GLU   A HB3    1 
ATOM   3006  H  HG2    . GLU   A 1 187 ? -21.179 1.015   19.496 1.00 59.62  ?  212 GLU   A HG2    1 
ATOM   3007  H  HG3    . GLU   A 1 187 ? -20.671 0.928   20.999 1.00 59.62  ?  212 GLU   A HG3    1 
ATOM   3008  N  N      . ASP   A 1 188 ? -16.664 -0.788  17.941 1.00 39.14  ?  213 ASP   A N      1 
ATOM   3009  C  CA     . ASP   A 1 188 ? -15.536 -1.687  17.721 1.00 36.70  ?  213 ASP   A CA     1 
ATOM   3010  C  C      . ASP   A 1 188 ? -15.330 -2.670  18.877 1.00 35.84  ?  213 ASP   A C      1 
ATOM   3011  O  O      . ASP   A 1 188 ? -15.575 -2.354  20.042 1.00 35.23  ?  213 ASP   A O      1 
ATOM   3012  C  CB     . ASP   A 1 188 ? -14.234 -0.891  17.565 1.00 39.58  ?  213 ASP   A CB     1 
ATOM   3013  C  CG     . ASP   A 1 188 ? -14.096 -0.199  16.225 1.00 40.43  ?  213 ASP   A CG     1 
ATOM   3014  O  OD1    . ASP   A 1 188 ? -15.110 0.115   15.564 1.00 41.06  ?  213 ASP   A OD1    1 
ATOM   3015  O  OD2    . ASP   A 1 188 ? -12.930 0.051   15.840 1.00 40.29  ?  213 ASP   A OD2    1 
ATOM   3016  H  H      . ASP   A 1 188 ? -16.447 0.044   17.938 1.00 46.96  ?  213 ASP   A H      1 
ATOM   3017  H  HA     . ASP   A 1 188 ? -15.730 -2.189  16.914 1.00 44.03  ?  213 ASP   A HA     1 
ATOM   3018  H  HB2    . ASP   A 1 188 ? -14.201 -0.209  18.254 1.00 47.49  ?  213 ASP   A HB2    1 
ATOM   3019  H  HB3    . ASP   A 1 188 ? -13.484 -1.498  17.662 1.00 47.49  ?  213 ASP   A HB3    1 
ATOM   3020  N  N      . TYR   A 1 189 ? -14.813 -3.858  18.546 1.00 34.95  ?  214 TYR   A N      1 
ATOM   3021  C  CA     . TYR   A 1 189 ? -14.413 -4.848  19.542 1.00 35.46  ?  214 TYR   A CA     1 
ATOM   3022  C  C      . TYR   A 1 189 ? -13.430 -5.813  18.891 1.00 34.54  ?  214 TYR   A C      1 
ATOM   3023  O  O      . TYR   A 1 189 ? -13.308 -5.862  17.664 1.00 34.03  ?  214 TYR   A O      1 
ATOM   3024  C  CB     . TYR   A 1 189 ? -15.610 -5.641  20.085 1.00 35.86  ?  214 TYR   A CB     1 
ATOM   3025  C  CG     . TYR   A 1 189 ? -16.272 -6.439  18.980 1.00 37.83  ?  214 TYR   A CG     1 
ATOM   3026  C  CD1    . TYR   A 1 189 ? -17.115 -5.822  18.067 1.00 38.44  ?  214 TYR   A CD1    1 
ATOM   3027  C  CD2    . TYR   A 1 189 ? -16.015 -7.794  18.817 1.00 38.07  ?  214 TYR   A CD2    1 
ATOM   3028  C  CE1    . TYR   A 1 189 ? -17.702 -6.531  17.034 1.00 38.79  ?  214 TYR   A CE1    1 
ATOM   3029  C  CE2    . TYR   A 1 189 ? -16.600 -8.516  17.784 1.00 39.23  ?  214 TYR   A CE2    1 
ATOM   3030  C  CZ     . TYR   A 1 189 ? -17.444 -7.878  16.895 1.00 38.66  ?  214 TYR   A CZ     1 
ATOM   3031  O  OH     . TYR   A 1 189 ? -18.036 -8.576  15.862 1.00 39.87  ?  214 TYR   A OH     1 
ATOM   3032  H  H      . TYR   A 1 189 ? -14.684 -4.117  17.736 1.00 41.93  ?  214 TYR   A H      1 
ATOM   3033  H  HA     . TYR   A 1 189 ? -13.983 -4.388  20.280 1.00 42.55  ?  214 TYR   A HA     1 
ATOM   3034  H  HB2    . TYR   A 1 189 ? -15.307 -6.256  20.771 1.00 43.03  ?  214 TYR   A HB2    1 
ATOM   3035  H  HB3    . TYR   A 1 189 ? -16.263 -5.027  20.456 1.00 43.03  ?  214 TYR   A HB3    1 
ATOM   3036  H  HD1    . TYR   A 1 189 ? -17.289 -4.912  18.151 1.00 46.12  ?  214 TYR   A HD1    1 
ATOM   3037  H  HD2    . TYR   A 1 189 ? -15.442 -8.225  19.410 1.00 45.68  ?  214 TYR   A HD2    1 
ATOM   3038  H  HE1    . TYR   A 1 189 ? -18.268 -6.100  16.435 1.00 46.54  ?  214 TYR   A HE1    1 
ATOM   3039  H  HE2    . TYR   A 1 189 ? -16.423 -9.424  17.691 1.00 47.07  ?  214 TYR   A HE2    1 
ATOM   3040  H  HH     . TYR   A 1 189 ? -17.799 -9.381  15.886 1.00 47.84  ?  214 TYR   A HH     1 
ATOM   3041  N  N      . THR   A 1 190 ? -12.735 -6.583  19.727 1.00 32.91  ?  215 THR   A N      1 
ATOM   3042  C  CA     . THR   A 1 190 ? -11.933 -7.719  19.292 1.00 32.70  ?  215 THR   A CA     1 
ATOM   3043  C  C      . THR   A 1 190 ? -12.227 -8.885  20.225 1.00 32.05  ?  215 THR   A C      1 
ATOM   3044  O  O      . THR   A 1 190 ? -12.335 -8.705  21.444 1.00 32.28  ?  215 THR   A O      1 
ATOM   3045  C  CB     . THR   A 1 190 ? -10.430 -7.385  19.296 1.00 33.93  ?  215 THR   A CB     1 
ATOM   3046  O  OG1    . THR   A 1 190 ? -10.166 -6.360  18.322 1.00 35.44  ?  215 THR   A OG1    1 
ATOM   3047  C  CG2    . THR   A 1 190 ? -9.559  -8.632  18.998 1.00 33.64  ?  215 THR   A CG2    1 
ATOM   3048  H  H      . THR   A 1 190 ? -12.712 -6.461  20.578 1.00 39.49  ?  215 THR   A H      1 
ATOM   3049  H  HA     . THR   A 1 190 ? -12.165 -7.974  18.385 1.00 39.24  ?  215 THR   A HA     1 
ATOM   3050  H  HB     . THR   A 1 190 ? -10.181 -7.070  20.179 1.00 40.70  ?  215 THR   A HB     1 
ATOM   3051  H  HG1    . THR   A 1 190 ? -10.593 -5.663  18.515 1.00 42.53  ?  215 THR   A HG1    1 
ATOM   3052  H  HG21   . THR   A 1 190 ? -8.640  -8.365  18.840 1.00 40.36  ?  215 THR   A HG21   1 
ATOM   3053  H  HG22   . THR   A 1 190 ? -9.585  -9.242  19.752 1.00 40.36  ?  215 THR   A HG22   1 
ATOM   3054  H  HG23   . THR   A 1 190 ? -9.894  -9.090  18.211 1.00 40.36  ?  215 THR   A HG23   1 
ATOM   3055  N  N      . CYS   A 1 191 ? -12.360 -10.077 19.648 1.00 31.64  ?  216 CYS   A N      1 
ATOM   3056  C  CA     . CYS   A 1 191 ? -12.619 -11.283 20.425 1.00 31.90  ?  216 CYS   A CA     1 
ATOM   3057  C  C      . CYS   A 1 191 ? -11.733 -12.407 19.910 1.00 30.68  ?  216 CYS   A C      1 
ATOM   3058  O  O      . CYS   A 1 191 ? -11.808 -12.768 18.733 1.00 31.97  ?  216 CYS   A O      1 
ATOM   3059  C  CB     . CYS   A 1 191 ? -14.097 -11.681 20.344 1.00 33.81  ?  216 CYS   A CB     1 
ATOM   3060  S  SG     . CYS   A 1 191 ? -14.511 -13.046 21.462 1.00 36.49  ?  216 CYS   A SG     1 
ATOM   3061  H  H      . CYS   A 1 191 ? -12.305 -10.212 18.801 1.00 37.96  ?  216 CYS   A H      1 
ATOM   3062  H  HA     . CYS   A 1 191 ? -12.390 -11.123 21.354 1.00 38.27  ?  216 CYS   A HA     1 
ATOM   3063  H  HB2    . CYS   A 1 191 ? -14.644 -10.917 20.585 1.00 40.57  ?  216 CYS   A HB2    1 
ATOM   3064  H  HB3    . CYS   A 1 191 ? -14.300 -11.962 19.438 1.00 40.57  ?  216 CYS   A HB3    1 
ATOM   3065  H  HG     . CYS   A 1 191 ? -15.671 -13.323 21.329 1.00 43.78  ?  216 CYS   A HG     1 
ATOM   3066  N  N      . ILE   A 1 192 ? -10.899 -12.953 20.792 1.00 28.79  ?  217 ILE   A N      1 
ATOM   3067  C  CA     . ILE   A 1 192 ? -10.000 -14.064 20.484 1.00 28.14  ?  217 ILE   A CA     1 
ATOM   3068  C  C      . ILE   A 1 192 ? -10.530 -15.312 21.194 1.00 26.74  ?  217 ILE   A C      1 
ATOM   3069  O  O      . ILE   A 1 192 ? -10.636 -15.334 22.424 1.00 26.78  ?  217 ILE   A O      1 
ATOM   3070  C  CB     . ILE   A 1 192 ? -8.553  -13.744 20.912 1.00 27.71  ?  217 ILE   A CB     1 
ATOM   3071  C  CG1    . ILE   A 1 192 ? -8.099  -12.371 20.380 1.00 29.35  ?  217 ILE   A CG1    1 
ATOM   3072  C  CG2    . ILE   A 1 192 ? -7.609  -14.895 20.529 1.00 27.78  ?  217 ILE   A CG2    1 
ATOM   3073  C  CD1    . ILE   A 1 192 ? -8.126  -12.226 18.864 1.00 30.42  ?  217 ILE   A CD1    1 
ATOM   3074  H  H      . ILE   A 1 192 ? -10.833 -12.686 21.607 1.00 34.54  ?  217 ILE   A H      1 
ATOM   3075  H  HA     . ILE   A 1 192 ? -10.008 -14.237 19.529 1.00 33.76  ?  217 ILE   A HA     1 
ATOM   3076  H  HB     . ILE   A 1 192 ? -8.523  -13.671 21.879 1.00 33.24  ?  217 ILE   A HB     1 
ATOM   3077  H  HG12   . ILE   A 1 192 ? -8.685  -11.691 20.748 1.00 35.22  ?  217 ILE   A HG12   1 
ATOM   3078  H  HG13   . ILE   A 1 192 ? -7.187  -12.215 20.671 1.00 35.22  ?  217 ILE   A HG13   1 
ATOM   3079  H  HG21   . ILE   A 1 192 ? -6.693  -14.619 20.688 1.00 33.33  ?  217 ILE   A HG21   1 
ATOM   3080  H  HG22   . ILE   A 1 192 ? -7.819  -15.670 21.073 1.00 33.33  ?  217 ILE   A HG22   1 
ATOM   3081  H  HG23   . ILE   A 1 192 ? -7.733  -15.107 19.591 1.00 33.33  ?  217 ILE   A HG23   1 
ATOM   3082  H  HD11   . ILE   A 1 192 ? -7.785  -11.350 18.625 1.00 36.49  ?  217 ILE   A HD11   1 
ATOM   3083  H  HD12   . ILE   A 1 192 ? -7.569  -12.916 18.471 1.00 36.49  ?  217 ILE   A HD12   1 
ATOM   3084  H  HD13   . ILE   A 1 192 ? -9.040  -12.321 18.554 1.00 36.49  ?  217 ILE   A HD13   1 
ATOM   3085  N  N      . THR   A 1 193 ? -10.875 -16.349 20.437 1.00 27.58  ?  218 THR   A N      1 
ATOM   3086  C  CA     . THR   A 1 193 ? -11.391 -17.589 21.006 1.00 27.96  ?  218 THR   A CA     1 
ATOM   3087  C  C      . THR   A 1 193 ? -10.485 -18.745 20.606 1.00 28.40  ?  218 THR   A C      1 
ATOM   3088  O  O      . THR   A 1 193 ? -10.235 -18.952 19.415 1.00 30.29  ?  218 THR   A O      1 
ATOM   3089  C  CB     . THR   A 1 193 ? -12.827 -17.864 20.525 1.00 30.47  ?  218 THR   A CB     1 
ATOM   3090  O  OG1    . THR   A 1 193 ? -13.668 -16.744 20.838 1.00 30.89  ?  218 THR   A OG1    1 
ATOM   3091  C  CG2    . THR   A 1 193 ? -13.385 -19.121 21.179 1.00 31.13  ?  218 THR   A CG2    1 
ATOM   3092  H  H      . THR   A 1 193 ? -10.819 -16.356 19.578 1.00 33.08  ?  218 THR   A H      1 
ATOM   3093  H  HA     . THR   A 1 193 ? -11.394 -17.520 21.973 1.00 33.55  ?  218 THR   A HA     1 
ATOM   3094  H  HB     . THR   A 1 193 ? -12.821 -18.001 19.565 1.00 36.55  ?  218 THR   A HB     1 
ATOM   3095  H  HG1    . THR   A 1 193 ? -13.684 -16.619 21.668 1.00 37.07  ?  218 THR   A HG1    1 
ATOM   3096  H  HG21   . THR   A 1 193 ? -14.335 -19.196 20.997 1.00 37.35  ?  218 THR   A HG21   1 
ATOM   3097  H  HG22   . THR   A 1 193 ? -12.935 -19.906 20.828 1.00 37.35  ?  218 THR   A HG22   1 
ATOM   3098  H  HG23   . THR   A 1 193 ? -13.250 -19.084 22.139 1.00 37.35  ?  218 THR   A HG23   1 
ATOM   3099  N  N      . PHE   A 1 194 ? -9.986  -19.498 21.584 1.00 27.13  ?  219 PHE   A N      1 
ATOM   3100  C  CA     . PHE   A 1 194 ? -9.061  -20.568 21.247 1.00 26.88  ?  219 PHE   A CA     1 
ATOM   3101  C  C      . PHE   A 1 194 ? -9.301  -21.821 22.069 1.00 25.80  ?  219 PHE   A C      1 
ATOM   3102  O  O      . PHE   A 1 194 ? -9.799  -21.779 23.195 1.00 25.74  ?  219 PHE   A O      1 
ATOM   3103  C  CB     . PHE   A 1 194 ? -7.596  -20.112 21.392 1.00 27.45  ?  219 PHE   A CB     1 
ATOM   3104  C  CG     . PHE   A 1 194 ? -7.177  -19.736 22.794 1.00 27.75  ?  219 PHE   A CG     1 
ATOM   3105  C  CD1    . PHE   A 1 194 ? -7.450  -18.476 23.313 1.00 27.49  ?  219 PHE   A CD1    1 
ATOM   3106  C  CD2    . PHE   A 1 194 ? -6.440  -20.627 23.572 1.00 27.71  ?  219 PHE   A CD2    1 
ATOM   3107  C  CE1    . PHE   A 1 194 ? -7.019  -18.121 24.600 1.00 28.41  ?  219 PHE   A CE1    1 
ATOM   3108  C  CE2    . PHE   A 1 194 ? -6.009  -20.277 24.858 1.00 28.14  ?  219 PHE   A CE2    1 
ATOM   3109  C  CZ     . PHE   A 1 194 ? -6.302  -19.026 25.369 1.00 28.26  ?  219 PHE   A CZ     1 
ATOM   3110  H  H      . PHE   A 1 194 ? -10.165 -19.409 22.421 1.00 32.55  ?  219 PHE   A H      1 
ATOM   3111  H  HA     . PHE   A 1 194 ? -9.230  -20.821 20.326 1.00 32.25  ?  219 PHE   A HA     1 
ATOM   3112  H  HB2    . PHE   A 1 194 ? -7.020  -20.836 21.101 1.00 32.93  ?  219 PHE   A HB2    1 
ATOM   3113  H  HB3    . PHE   A 1 194 ? -7.460  -19.334 20.830 1.00 32.93  ?  219 PHE   A HB3    1 
ATOM   3114  H  HD1    . PHE   A 1 194 ? -7.924  -17.861 22.801 1.00 32.99  ?  219 PHE   A HD1    1 
ATOM   3115  H  HD2    . PHE   A 1 194 ? -6.232  -21.468 23.232 1.00 33.24  ?  219 PHE   A HD2    1 
ATOM   3116  H  HE1    . PHE   A 1 194 ? -7.215  -17.277 24.939 1.00 34.08  ?  219 PHE   A HE1    1 
ATOM   3117  H  HE2    . PHE   A 1 194 ? -5.525  -20.886 25.368 1.00 33.76  ?  219 PHE   A HE2    1 
ATOM   3118  H  HZ     . PHE   A 1 194 ? -6.020  -18.792 26.224 1.00 33.90  ?  219 PHE   A HZ     1 
ATOM   3119  N  N      . GLN   A 1 195 ? -8.950  -22.946 21.465 1.00 25.12  ?  220 GLN   A N      1 
ATOM   3120  C  CA     . GLN   A 1 195 ? -8.974  -24.240 22.134 1.00 25.97  ?  220 GLN   A CA     1 
ATOM   3121  C  C      . GLN   A 1 195 ? -7.522  -24.658 22.316 1.00 24.81  ?  220 GLN   A C      1 
ATOM   3122  O  O      . GLN   A 1 195 ? -6.862  -25.043 21.338 1.00 25.14  ?  220 GLN   A O      1 
ATOM   3123  C  CB     . GLN   A 1 195 ? -9.744  -25.264 21.304 1.00 28.62  ?  220 GLN   A CB     1 
ATOM   3124  C  CG     . GLN   A 1 195 ? -11.191 -24.899 21.120 1.00 33.44  ?  220 GLN   A CG     1 
ATOM   3125  C  CD     . GLN   A 1 195 ? -11.974 -26.032 20.529 1.00 39.43  ?  220 GLN   A CD     1 
ATOM   3126  O  OE1    . GLN   A 1 195 ? -12.100 -26.141 19.318 1.00 44.28  ?  220 GLN   A OE1    1 
ATOM   3127  N  NE2    . GLN   A 1 195 ? -12.467 -26.914 21.383 1.00 41.73  ?  220 GLN   A NE2    1 
ATOM   3128  H  H      . GLN   A 1 195 ? -8.688  -22.989 20.647 1.00 30.14  ?  220 GLN   A H      1 
ATOM   3129  H  HA     . GLN   A 1 195 ? -9.416  -24.184 22.995 1.00 31.16  ?  220 GLN   A HA     1 
ATOM   3130  H  HB2    . GLN   A 1 195 ? -9.337  -25.329 20.426 1.00 34.34  ?  220 GLN   A HB2    1 
ATOM   3131  H  HB3    . GLN   A 1 195 ? -9.707  -26.124 21.751 1.00 34.34  ?  220 GLN   A HB3    1 
ATOM   3132  H  HG2    . GLN   A 1 195 ? -11.578 -24.678 21.981 1.00 40.12  ?  220 GLN   A HG2    1 
ATOM   3133  H  HG3    . GLN   A 1 195 ? -11.256 -24.139 20.521 1.00 40.12  ?  220 GLN   A HG3    1 
ATOM   3134  H  HE21   . GLN   A 1 195 ? -12.330 -26.818 22.226 1.00 50.07  ?  220 GLN   A HE21   1 
ATOM   3135  H  HE22   . GLN   A 1 195 ? -12.924 -27.583 21.094 1.00 50.07  ?  220 GLN   A HE22   1 
ATOM   3136  N  N      . PRO   A 1 196 ? -6.962  -24.562 23.522 1.00 23.82  ?  221 PRO   A N      1 
ATOM   3137  C  CA     . PRO   A 1 196 ? -5.547  -24.920 23.707 1.00 23.35  ?  221 PRO   A CA     1 
ATOM   3138  C  C      . PRO   A 1 196 ? -5.297  -26.375 23.351 1.00 23.41  ?  221 PRO   A C      1 
ATOM   3139  O  O      . PRO   A 1 196 ? -6.123  -27.245 23.630 1.00 23.89  ?  221 PRO   A O      1 
ATOM   3140  C  CB     . PRO   A 1 196 ? -5.298  -24.661 25.199 1.00 24.28  ?  221 PRO   A CB     1 
ATOM   3141  C  CG     . PRO   A 1 196 ? -6.648  -24.602 25.825 1.00 27.15  ?  221 PRO   A CG     1 
ATOM   3142  C  CD     . PRO   A 1 196 ? -7.624  -24.181 24.780 1.00 25.89  ?  221 PRO   A CD     1 
ATOM   3143  H  HA     . PRO   A 1 196 ? -4.977  -24.343 23.175 1.00 28.01  ?  221 PRO   A HA     1 
ATOM   3144  H  HB2    . PRO   A 1 196 ? -4.774  -25.386 25.575 1.00 29.13  ?  221 PRO   A HB2    1 
ATOM   3145  H  HB3    . PRO   A 1 196 ? -4.828  -23.819 25.312 1.00 29.13  ?  221 PRO   A HB3    1 
ATOM   3146  H  HG2    . PRO   A 1 196 ? -6.880  -25.481 26.165 1.00 32.58  ?  221 PRO   A HG2    1 
ATOM   3147  H  HG3    . PRO   A 1 196 ? -6.635  -23.959 26.551 1.00 32.58  ?  221 PRO   A HG3    1 
ATOM   3148  H  HD2    . PRO   A 1 196 ? -8.466  -24.652 24.884 1.00 31.06  ?  221 PRO   A HD2    1 
ATOM   3149  H  HD3    . PRO   A 1 196 ? -7.774  -23.223 24.814 1.00 31.06  ?  221 PRO   A HD3    1 
ATOM   3150  N  N      . ASP   A 1 197 ? -4.133  -26.643 22.754 1.00 22.76  ?  222 ASP   A N      1 
ATOM   3151  C  CA     . ASP   A 1 197 ? -3.758  -28.007 22.365 1.00 22.30  ?  222 ASP   A CA     1 
ATOM   3152  C  C      . ASP   A 1 197 ? -3.184  -28.699 23.596 1.00 22.14  ?  222 ASP   A C      1 
ATOM   3153  O  O      . ASP   A 1 197 ? -1.975  -28.696 23.847 1.00 21.16  ?  222 ASP   A O      1 
ATOM   3154  C  CB     . ASP   A 1 197 ? -2.774  -27.990 21.202 1.00 24.38  ?  222 ASP   A CB     1 
ATOM   3155  C  CG     . ASP   A 1 197 ? -2.461  -29.376 20.683 1.00 26.98  ?  222 ASP   A CG     1 
ATOM   3156  O  OD1    . ASP   A 1 197 ? -2.863  -30.364 21.328 1.00 27.68  ?  222 ASP   A OD1    1 
ATOM   3157  O  OD2    . ASP   A 1 197 ? -1.812  -29.479 19.621 1.00 27.29  ?  222 ASP   A OD2    1 
ATOM   3158  H  H      . ASP   A 1 197 ? -3.541  -26.050 22.562 1.00 27.31  ?  222 ASP   A H      1 
ATOM   3159  H  HA     . ASP   A 1 197 ? -4.545  -28.496 22.076 1.00 26.75  ?  222 ASP   A HA     1 
ATOM   3160  H  HB2    . ASP   A 1 197 ? -3.154  -27.475 20.473 1.00 29.25  ?  222 ASP   A HB2    1 
ATOM   3161  H  HB3    . ASP   A 1 197 ? -1.943  -27.585 21.496 1.00 29.25  ?  222 ASP   A HB3    1 
ATOM   3162  N  N      . LEU   A 1 198 ? -4.082  -29.293 24.384 1.00 22.92  ?  223 LEU   A N      1 
ATOM   3163  C  CA     . LEU   A 1 198 ? -3.684  -29.844 25.673 1.00 23.04  ?  223 LEU   A CA     1 
ATOM   3164  C  C      . LEU   A 1 198 ? -2.704  -30.992 25.512 1.00 22.66  ?  223 LEU   A C      1 
ATOM   3165  O  O      . LEU   A 1 198 ? -1.929  -31.256 26.436 1.00 23.24  ?  223 LEU   A O      1 
ATOM   3166  C  CB     . LEU   A 1 198 ? -4.925  -30.265 26.453 1.00 23.60  ?  223 LEU   A CB     1 
ATOM   3167  C  CG     . LEU   A 1 198 ? -5.823  -29.081 26.841 1.00 24.93  ?  223 LEU   A CG     1 
ATOM   3168  C  CD1    . LEU   A 1 198 ? -7.038  -29.587 27.620 1.00 27.28  ?  223 LEU   A CD1    1 
ATOM   3169  C  CD2    . LEU   A 1 198 ? -5.083  -27.994 27.637 1.00 24.97  ?  223 LEU   A CD2    1 
ATOM   3170  H  H      . LEU   A 1 198 ? -4.915  -29.388 24.196 1.00 27.50  ?  223 LEU   A H      1 
ATOM   3171  H  HA     . LEU   A 1 198 ? -3.237  -29.165 26.202 1.00 27.65  ?  223 LEU   A HA     1 
ATOM   3172  H  HB2    . LEU   A 1 198 ? -5.449  -30.871 25.906 1.00 28.31  ?  223 LEU   A HB2    1 
ATOM   3173  H  HB3    . LEU   A 1 198 ? -4.648  -30.710 27.269 1.00 28.31  ?  223 LEU   A HB3    1 
ATOM   3174  H  HG     . LEU   A 1 198 ? -6.119  -28.653 26.022 1.00 29.91  ?  223 LEU   A HG     1 
ATOM   3175  H  HD11   . LEU   A 1 198 ? -7.602  -28.832 27.853 1.00 32.73  ?  223 LEU   A HD11   1 
ATOM   3176  H  HD12   . LEU   A 1 198 ? -7.532  -30.210 27.065 1.00 32.73  ?  223 LEU   A HD12   1 
ATOM   3177  H  HD13   . LEU   A 1 198 ? -6.733  -30.032 28.426 1.00 32.73  ?  223 LEU   A HD13   1 
ATOM   3178  H  HD21   . LEU   A 1 198 ? -5.734  -27.400 28.042 1.00 29.95  ?  223 LEU   A HD21   1 
ATOM   3179  H  HD22   . LEU   A 1 198 ? -4.548  -28.417 28.327 1.00 29.95  ?  223 LEU   A HD22   1 
ATOM   3180  H  HD23   . LEU   A 1 198 ? -4.510  -27.495 27.034 1.00 29.95  ?  223 LEU   A HD23   1 
ATOM   3181  N  N      . SER   A 1 199 ? -2.672  -31.645 24.344 1.00 24.12  ?  224 SER   A N      1 
ATOM   3182  C  CA     . SER   A 1 199 ? -1.685  -32.703 24.134 1.00 25.99  ?  224 SER   A CA     1 
ATOM   3183  C  C      . SER   A 1 199 ? -0.255  -32.163 24.210 1.00 24.93  ?  224 SER   A C      1 
ATOM   3184  O  O      . SER   A 1 199 ? 0.651   -32.886 24.643 1.00 25.78  ?  224 SER   A O      1 
ATOM   3185  C  CB     . SER   A 1 199 ? -1.916  -33.397 22.788 1.00 28.85  ?  224 SER   A CB     1 
ATOM   3186  O  OG     . SER   A 1 199 ? -1.464  -32.596 21.707 1.00 29.57  ?  224 SER   A OG     1 
ATOM   3187  H  H      . SER   A 1 199 ? -3.197  -31.498 23.679 1.00 28.94  ?  224 SER   A H      1 
ATOM   3188  H  HA     . SER   A 1 199 ? -1.797  -33.366 24.832 1.00 31.18  ?  224 SER   A HA     1 
ATOM   3189  H  HB2    . SER   A 1 199 ? -1.430  -34.236 22.780 1.00 34.61  ?  224 SER   A HB2    1 
ATOM   3190  H  HB3    . SER   A 1 199 ? -2.866  -33.562 22.679 1.00 34.61  ?  224 SER   A HB3    1 
ATOM   3191  H  HG     . SER   A 1 199 ? -1.875  -31.863 21.702 1.00 35.48  ?  224 SER   A HG     1 
ATOM   3192  N  N      . LYS   A 1 200 ? -0.035  -30.898 23.814 1.00 22.68  ?  225 LYS   A N      1 
ATOM   3193  C  CA     . LYS   A 1 200 ? 1.300   -30.304 23.876 1.00 22.36  ?  225 LYS   A CA     1 
ATOM   3194  C  C      . LYS   A 1 200 ? 1.765   -30.079 25.308 1.00 21.30  ?  225 LYS   A C      1 
ATOM   3195  O  O      . LYS   A 1 200 ? 2.967   -29.903 25.545 1.00 22.75  ?  225 LYS   A O      1 
ATOM   3196  C  CB     . LYS   A 1 200 ? 1.323   -28.967 23.126 1.00 23.10  ?  225 LYS   A CB     1 
ATOM   3197  C  CG     . LYS   A 1 200 ? 0.943   -29.058 21.657 1.00 26.26  ?  225 LYS   A CG     1 
ATOM   3198  C  CD     . LYS   A 1 200 ? 1.990   -29.840 20.875 1.00 28.51  ?  225 LYS   A CD     1 
ATOM   3199  C  CE     . LYS   A 1 200 ? 1.720   -29.823 19.391 1.00 30.67  ?  225 LYS   A CE     1 
ATOM   3200  N  NZ     . LYS   A 1 200 ? 0.644   -30.781 19.074 1.00 33.72  ?  225 LYS   A NZ     1 
ATOM   3201  H  H      . LYS   A 1 200 ? -0.641  -30.370 23.508 1.00 27.21  ?  225 LYS   A H      1 
ATOM   3202  H  HA     . LYS   A 1 200 ? 1.922   -30.909 23.442 1.00 26.83  ?  225 LYS   A HA     1 
ATOM   3203  H  HB2    . LYS   A 1 200 ? 0.695   -28.363 23.553 1.00 27.72  ?  225 LYS   A HB2    1 
ATOM   3204  H  HB3    . LYS   A 1 200 ? 2.220   -28.602 23.174 1.00 27.72  ?  225 LYS   A HB3    1 
ATOM   3205  H  HG2    . LYS   A 1 200 ? 0.091   -29.514 21.571 1.00 31.51  ?  225 LYS   A HG2    1 
ATOM   3206  H  HG3    . LYS   A 1 200 ? 0.882   -28.166 21.282 1.00 31.51  ?  225 LYS   A HG3    1 
ATOM   3207  H  HD2    . LYS   A 1 200 ? 2.863   -29.446 21.028 1.00 34.21  ?  225 LYS   A HD2    1 
ATOM   3208  H  HD3    . LYS   A 1 200 ? 1.986   -30.763 21.172 1.00 34.21  ?  225 LYS   A HD3    1 
ATOM   3209  H  HE2    . LYS   A 1 200 ? 1.440   -28.935 19.118 1.00 36.80  ?  225 LYS   A HE2    1 
ATOM   3210  H  HE3    . LYS   A 1 200 ? 2.521   -30.081 18.909 1.00 36.80  ?  225 LYS   A HE3    1 
ATOM   3211  H  HZ1    . LYS   A 1 200 ? 0.476   -30.773 18.200 1.00 40.46  ?  225 LYS   A HZ1    1 
ATOM   3212  H  HZ2    . LYS   A 1 200 ? 0.888   -31.603 19.314 1.00 40.46  ?  225 LYS   A HZ2    1 
ATOM   3213  H  HZ3    . LYS   A 1 200 ? -0.099  -30.561 19.513 1.00 40.46  ?  225 LYS   A HZ3    1 
ATOM   3214  N  N      . PHE   A 1 201 ? 0.828   -30.067 26.255 1.00 20.29  ?  226 PHE   A N      1 
ATOM   3215  C  CA     . PHE   A 1 201 ? 1.080   -29.818 27.664 1.00 19.88  ?  226 PHE   A CA     1 
ATOM   3216  C  C      . PHE   A 1 201 ? 0.854   -31.063 28.514 1.00 19.60  ?  226 PHE   A C      1 
ATOM   3217  O  O      . PHE   A 1 201 ? 0.893   -30.976 29.744 1.00 22.17  ?  226 PHE   A O      1 
ATOM   3218  C  CB     . PHE   A 1 201 ? 0.172   -28.682 28.126 1.00 20.45  ?  226 PHE   A CB     1 
ATOM   3219  C  CG     . PHE   A 1 201 ? 0.295   -27.428 27.292 1.00 19.63  ?  226 PHE   A CG     1 
ATOM   3220  C  CD1    . PHE   A 1 201 ? 1.501   -26.759 27.210 1.00 20.38  ?  226 PHE   A CD1    1 
ATOM   3221  C  CD2    . PHE   A 1 201 ? -0.788  -26.920 26.588 1.00 22.13  ?  226 PHE   A CD2    1 
ATOM   3222  C  CE1    . PHE   A 1 201 ? 1.628   -25.609 26.458 1.00 21.08  ?  226 PHE   A CE1    1 
ATOM   3223  C  CE2    . PHE   A 1 201 ? -0.658  -25.753 25.837 1.00 22.47  ?  226 PHE   A CE2    1 
ATOM   3224  C  CZ     . PHE   A 1 201 ? 0.554   -25.107 25.764 1.00 20.49  ?  226 PHE   A CZ     1 
ATOM   3225  H  H      . PHE   A 1 201 ? -0.005  -30.209 26.093 1.00 24.34  ?  226 PHE   A H      1 
ATOM   3226  H  HA     . PHE   A 1 201 ? 2.002   -29.547 27.794 1.00 23.85  ?  226 PHE   A HA     1 
ATOM   3227  H  HB2    . PHE   A 1 201 ? -0.750  -28.980 28.078 1.00 24.53  ?  226 PHE   A HB2    1 
ATOM   3228  H  HB3    . PHE   A 1 201 ? 0.399   -28.453 29.041 1.00 24.53  ?  226 PHE   A HB3    1 
ATOM   3229  H  HD1    . PHE   A 1 201 ? 2.240   -27.090 27.668 1.00 24.45  ?  226 PHE   A HD1    1 
ATOM   3230  H  HD2    . PHE   A 1 201 ? -1.606  -27.362 26.617 1.00 26.56  ?  226 PHE   A HD2    1 
ATOM   3231  H  HE1    . PHE   A 1 201 ? 2.447   -25.169 26.421 1.00 25.28  ?  226 PHE   A HE1    1 
ATOM   3232  H  HE2    . PHE   A 1 201 ? -1.394  -25.410 25.384 1.00 26.96  ?  226 PHE   A HE2    1 
ATOM   3233  H  HZ     . PHE   A 1 201 ? 0.645   -24.338 25.249 1.00 24.58  ?  226 PHE   A HZ     1 
ATOM   3234  N  N      . LYS   A 1 202 ? 0.618   -32.219 27.882 1.00 19.93  ?  227 LYS   A N      1 
ATOM   3235  C  CA     . LYS   A 1 202 ? 0.329   -33.474 28.582 1.00 20.60  ?  227 LYS   A CA     1 
ATOM   3236  C  C      . LYS   A 1 202 ? -0.805  -33.291 29.585 1.00 20.03  ?  227 LYS   A C      1 
ATOM   3237  O  O      . LYS   A 1 202 ? -0.760  -33.784 30.717 1.00 22.26  ?  227 LYS   A O      1 
ATOM   3238  C  CB     . LYS   A 1 202 ? 1.579   -34.038 29.250 1.00 24.02  ?  227 LYS   A CB     1 
ATOM   3239  C  CG     . LYS   A 1 202 ? 2.662   -34.372 28.248 1.00 28.38  ?  227 LYS   A CG     1 
ATOM   3240  C  CD     . LYS   A 1 202 ? 3.847   -35.024 28.923 1.00 32.60  ?  227 LYS   A CD     1 
ATOM   3241  C  CE     . LYS   A 1 202 ? 5.082   -34.913 28.067 1.00 39.09  ?  227 LYS   A CE     1 
ATOM   3242  N  NZ     . LYS   A 1 202 ? 4.763   -35.096 26.633 1.00 42.90  ?  227 LYS   A NZ     1 
ATOM   3243  H  H      . LYS   A 1 202 ? 0.619   -32.303 27.026 1.00 23.91  ?  227 LYS   A H      1 
ATOM   3244  H  HA     . LYS   A 1 202 ? 0.033   -34.127 27.928 1.00 24.71  ?  227 LYS   A HA     1 
ATOM   3245  H  HB2    . LYS   A 1 202 ? 1.933   -33.380 29.869 1.00 28.81  ?  227 LYS   A HB2    1 
ATOM   3246  H  HB3    . LYS   A 1 202 ? 1.346   -34.850 29.727 1.00 28.81  ?  227 LYS   A HB3    1 
ATOM   3247  H  HG2    . LYS   A 1 202 ? 2.310   -34.987 27.586 1.00 34.05  ?  227 LYS   A HG2    1 
ATOM   3248  H  HG3    . LYS   A 1 202 ? 2.965   -33.558 27.817 1.00 34.05  ?  227 LYS   A HG3    1 
ATOM   3249  H  HD2    . LYS   A 1 202 ? 4.020   -34.584 29.770 1.00 39.12  ?  227 LYS   A HD2    1 
ATOM   3250  H  HD3    . LYS   A 1 202 ? 3.659   -35.965 29.071 1.00 39.12  ?  227 LYS   A HD3    1 
ATOM   3251  H  HE2    . LYS   A 1 202 ? 5.475   -34.034 28.183 1.00 46.90  ?  227 LYS   A HE2    1 
ATOM   3252  H  HE3    . LYS   A 1 202 ? 5.717   -35.598 28.329 1.00 46.90  ?  227 LYS   A HE3    1 
ATOM   3253  H  HZ1    . LYS   A 1 202 ? 4.236   -35.806 26.527 1.00 51.47  ?  227 LYS   A HZ1    1 
ATOM   3254  H  HZ2    . LYS   A 1 202 ? 4.344   -34.376 26.320 1.00 51.47  ?  227 LYS   A HZ2    1 
ATOM   3255  H  HZ3    . LYS   A 1 202 ? 5.511   -35.220 26.168 1.00 51.47  ?  227 LYS   A HZ3    1 
ATOM   3256  N  N      . MET   A 1 203 ? -1.843  -32.585 29.145 1.00 19.04  ?  228 MET   A N      1 
ATOM   3257  C  CA     A MET   A 1 203 ? -3.024  -32.383 29.959 0.53 19.57  ?  228 MET   A CA     1 
ATOM   3258  C  CA     B MET   A 1 203 ? -3.034  -32.307 29.929 0.47 19.75  ?  228 MET   A CA     1 
ATOM   3259  C  C      . MET   A 1 203 ? -4.246  -32.932 29.245 1.00 19.76  ?  228 MET   A C      1 
ATOM   3260  O  O      . MET   A 1 203 ? -4.258  -33.119 28.022 1.00 21.46  ?  228 MET   A O      1 
ATOM   3261  C  CB     A MET   A 1 203 ? -3.238  -30.905 30.268 0.53 20.98  ?  228 MET   A CB     1 
ATOM   3262  C  CB     B MET   A 1 203 ? -3.280  -30.794 30.068 0.47 21.10  ?  228 MET   A CB     1 
ATOM   3263  C  CG     A MET   A 1 203 ? -2.230  -30.346 31.230 0.53 22.73  ?  228 MET   A CG     1 
ATOM   3264  C  CG     B MET   A 1 203 ? -2.215  -30.013 30.810 0.47 23.17  ?  228 MET   A CG     1 
ATOM   3265  S  SD     A MET   A 1 203 ? -2.486  -28.583 31.383 0.53 22.33  ?  228 MET   A SD     1 
ATOM   3266  S  SD     B MET   A 1 203 ? -2.368  -30.170 32.596 0.47 24.31  ?  228 MET   A SD     1 
ATOM   3267  C  CE     A MET   A 1 203 ? -4.126  -28.522 32.106 0.53 22.18  ?  228 MET   A CE     1 
ATOM   3268  C  CE     B MET   A 1 203 ? -3.956  -29.402 32.926 0.47 23.72  ?  228 MET   A CE     1 
ATOM   3269  H  H      A MET   A 1 203 ? -1.881  -32.213 28.370 0.53 22.84  ?  228 MET   A H      1 
ATOM   3270  H  H      B MET   A 1 203 ? -1.878  -32.242 28.357 0.47 22.84  ?  228 MET   A H      1 
ATOM   3271  H  HA     A MET   A 1 203 ? -2.908  -32.853 30.799 0.53 23.48  ?  228 MET   A HA     1 
ATOM   3272  H  HA     B MET   A 1 203 ? -2.917  -32.681 30.816 0.47 23.70  ?  228 MET   A HA     1 
ATOM   3273  H  HB2    A MET   A 1 203 ? -3.174  -30.400 29.442 0.53 25.17  ?  228 MET   A HB2    1 
ATOM   3274  H  HB2    B MET   A 1 203 ? -3.345  -30.414 29.177 0.47 25.32  ?  228 MET   A HB2    1 
ATOM   3275  H  HB3    A MET   A 1 203 ? -4.119  -30.791 30.659 0.53 25.17  ?  228 MET   A HB3    1 
ATOM   3276  H  HB3    B MET   A 1 203 ? -4.115  -30.665 30.544 0.47 25.32  ?  228 MET   A HB3    1 
ATOM   3277  H  HG2    A MET   A 1 203 ? -2.341  -30.758 32.101 0.53 27.27  ?  228 MET   A HG2    1 
ATOM   3278  H  HG2    B MET   A 1 203 ? -1.341  -30.345 30.552 0.47 27.80  ?  228 MET   A HG2    1 
ATOM   3279  H  HG3    A MET   A 1 203 ? -1.333  -30.507 30.899 0.53 27.27  ?  228 MET   A HG3    1 
ATOM   3280  H  HG3    B MET   A 1 203 ? -2.294  -29.074 30.582 0.47 27.80  ?  228 MET   A HG3    1 
ATOM   3281  H  HE1    A MET   A 1 203 ? -4.307  -27.616 32.402 0.53 26.61  ?  228 MET   A HE1    1 
ATOM   3282  H  HE1    B MET   A 1 203 ? -4.062  -29.294 33.884 0.47 28.46  ?  228 MET   A HE1    1 
ATOM   3283  H  HE2    A MET   A 1 203 ? -4.776  -28.787 31.437 0.53 26.61  ?  228 MET   A HE2    1 
ATOM   3284  H  HE2    B MET   A 1 203 ? -3.984  -28.535 32.490 0.47 28.46  ?  228 MET   A HE2    1 
ATOM   3285  H  HE3    A MET   A 1 203 ? -4.161  -29.129 32.862 0.53 26.61  ?  228 MET   A HE3    1 
ATOM   3286  H  HE3    B MET   A 1 203 ? -4.660  -29.970 32.577 0.47 28.46  ?  228 MET   A HE3    1 
ATOM   3287  N  N      . GLN   A 1 204 ? -5.289  -33.205 30.041 1.00 21.56  ?  229 GLN   A N      1 
ATOM   3288  C  CA     . GLN   A 1 204 ? -6.544  -33.712 29.511 1.00 23.02  ?  229 GLN   A CA     1 
ATOM   3289  C  C      . GLN   A 1 204 ? -7.683  -32.705 29.570 1.00 25.65  ?  229 GLN   A C      1 
ATOM   3290  O  O      . GLN   A 1 204 ? -8.632  -32.828 28.787 1.00 28.02  ?  229 GLN   A O      1 
ATOM   3291  C  CB     . GLN   A 1 204 ? -6.990  -34.972 30.272 1.00 24.43  ?  229 GLN   A CB     1 
ATOM   3292  C  CG     . GLN   A 1 204 ? -6.017  -36.113 30.228 1.00 25.78  ?  229 GLN   A CG     1 
ATOM   3293  C  CD     . GLN   A 1 204 ? -4.949  -35.977 31.277 1.00 26.46  ?  229 GLN   A CD     1 
ATOM   3294  O  OE1    . GLN   A 1 204 ? -5.210  -35.885 32.482 1.00 30.13  ?  229 GLN   A OE1    1 
ATOM   3295  N  NE2    . GLN   A 1 204 ? -3.730  -35.923 30.820 1.00 25.68  ?  229 GLN   A NE2    1 
ATOM   3296  H  H      . GLN   A 1 204 ? -5.286  -33.101 30.895 1.00 25.87  ?  229 GLN   A H      1 
ATOM   3297  H  HA     . GLN   A 1 204 ? -6.399  -33.958 28.584 1.00 27.61  ?  229 GLN   A HA     1 
ATOM   3298  H  HB2    . GLN   A 1 204 ? -7.122  -34.738 31.204 1.00 29.31  ?  229 GLN   A HB2    1 
ATOM   3299  H  HB3    . GLN   A 1 204 ? -7.824  -35.285 29.888 1.00 29.31  ?  229 GLN   A HB3    1 
ATOM   3300  H  HG2    . GLN   A 1 204 ? -6.492  -36.944 30.383 1.00 30.93  ?  229 GLN   A HG2    1 
ATOM   3301  H  HG3    . GLN   A 1 204 ? -5.588  -36.133 29.358 1.00 30.93  ?  229 GLN   A HG3    1 
ATOM   3302  H  HE21   . GLN   A 1 204 ? -3.585  -35.964 29.973 1.00 30.81  ?  229 GLN   A HE21   1 
ATOM   3303  H  HE22   . GLN   A 1 204 ? -3.069  -35.845 31.365 1.00 30.81  ?  229 GLN   A HE22   1 
ATOM   3304  N  N      . SER   A 1 205 ? -7.632  -31.740 30.477 1.00 24.51  ?  230 SER   A N      1 
ATOM   3305  C  CA     . SER   A 1 205 ? -8.684  -30.740 30.532 1.00 26.73  ?  230 SER   A CA     1 
ATOM   3306  C  C      . SER   A 1 205 ? -8.163  -29.531 31.288 1.00 26.48  ?  230 SER   A C      1 
ATOM   3307  O  O      . SER   A 1 205 ? -7.100  -29.571 31.910 1.00 27.07  ?  230 SER   A O      1 
ATOM   3308  C  CB     . SER   A 1 205 ? -9.940  -31.278 31.218 1.00 29.79  ?  230 SER   A CB     1 
ATOM   3309  O  OG     . SER   A 1 205 ? -9.716  -31.366 32.617 1.00 31.94  ?  230 SER   A OG     1 
ATOM   3310  H  H      . SER   A 1 205 ? -7.009  -31.645 31.062 1.00 29.41  ?  230 SER   A H      1 
ATOM   3311  H  HA     . SER   A 1 205 ? -8.909  -30.478 29.626 1.00 32.07  ?  230 SER   A HA     1 
ATOM   3312  H  HB2    . SER   A 1 205 ? -10.681 -30.675 31.049 1.00 35.74  ?  230 SER   A HB2    1 
ATOM   3313  H  HB3    . SER   A 1 205 ? -10.143 -32.160 30.870 1.00 35.74  ?  230 SER   A HB3    1 
ATOM   3314  H  HG     . SER   A 1 205 ? -9.083  -31.895 32.774 1.00 38.33  ?  230 SER   A HG     1 
ATOM   3315  N  N      . LEU   A 1 206 ? -8.932  -28.454 31.238 1.00 26.46  ?  231 LEU   A N      1 
ATOM   3316  C  CA     . LEU   A 1 206 ? -8.625  -27.268 32.035 1.00 26.23  ?  231 LEU   A CA     1 
ATOM   3317  C  C      . LEU   A 1 206 ? -9.119  -27.565 33.447 1.00 27.30  ?  231 LEU   A C      1 
ATOM   3318  O  O      . LEU   A 1 206 ? -10.287 -27.338 33.781 1.00 29.52  ?  231 LEU   A O      1 
ATOM   3319  C  CB     . LEU   A 1 206 ? -9.275  -26.025 31.444 1.00 27.30  ?  231 LEU   A CB     1 
ATOM   3320  C  CG     . LEU   A 1 206 ? -8.839  -25.646 30.025 1.00 26.77  ?  231 LEU   A CG     1 
ATOM   3321  C  CD1    . LEU   A 1 206 ? -9.773  -24.577 29.461 1.00 28.18  ?  231 LEU   A CD1    1 
ATOM   3322  C  CD2    . LEU   A 1 206 ? -7.385  -25.171 30.004 1.00 28.09  ?  231 LEU   A CD2    1 
ATOM   3323  H  H      . LEU   A 1 206 ? -9.638  -28.382 30.751 1.00 31.75  ?  231 LEU   A H      1 
ATOM   3324  H  HA     . LEU   A 1 206 ? -7.669  -27.104 32.053 1.00 31.47  ?  231 LEU   A HA     1 
ATOM   3325  H  HB2    . LEU   A 1 206 ? -10.234 -26.169 31.420 1.00 32.75  ?  231 LEU   A HB2    1 
ATOM   3326  H  HB3    . LEU   A 1 206 ? -9.067  -25.272 32.019 1.00 32.75  ?  231 LEU   A HB3    1 
ATOM   3327  H  HG     . LEU   A 1 206 ? -8.891  -26.430 29.455 1.00 32.12  ?  231 LEU   A HG     1 
ATOM   3328  H  HD11   . LEU   A 1 206 ? -9.488  -24.350 28.562 1.00 33.81  ?  231 LEU   A HD11   1 
ATOM   3329  H  HD12   . LEU   A 1 206 ? -10.678 -24.926 29.443 1.00 33.81  ?  231 LEU   A HD12   1 
ATOM   3330  H  HD13   . LEU   A 1 206 ? -9.733  -23.791 30.029 1.00 33.81  ?  231 LEU   A HD13   1 
ATOM   3331  H  HD21   . LEU   A 1 206 ? -7.151  -24.908 29.100 1.00 33.70  ?  231 LEU   A HD21   1 
ATOM   3332  H  HD22   . LEU   A 1 206 ? -7.291  -24.415 30.604 1.00 33.70  ?  231 LEU   A HD22   1 
ATOM   3333  H  HD23   . LEU   A 1 206 ? -6.811  -25.897 30.296 1.00 33.70  ?  231 LEU   A HD23   1 
ATOM   3334  N  N      . ASP   A 1 207 ? -8.217  -28.100 34.277 1.00 26.94  ?  232 ASP   A N      1 
ATOM   3335  C  CA     . ASP   A 1 207 ? -8.561  -28.618 35.596 1.00 27.45  ?  232 ASP   A CA     1 
ATOM   3336  C  C      . ASP   A 1 207 ? -8.631  -27.493 36.630 1.00 27.35  ?  232 ASP   A C      1 
ATOM   3337  O  O      . ASP   A 1 207 ? -8.451  -26.311 36.326 1.00 27.81  ?  232 ASP   A O      1 
ATOM   3338  C  CB     . ASP   A 1 207 ? -7.589  -29.742 35.997 1.00 27.31  ?  232 ASP   A CB     1 
ATOM   3339  C  CG     . ASP   A 1 207 ? -6.139  -29.280 36.243 1.00 28.53  ?  232 ASP   A CG     1 
ATOM   3340  O  OD1    . ASP   A 1 207 ? -5.836  -28.068 36.298 1.00 27.67  ?  232 ASP   A OD1    1 
ATOM   3341  O  OD2    . ASP   A 1 207 ? -5.282  -30.186 36.405 1.00 30.11  ?  232 ASP   A OD2    1 
ATOM   3342  H  H      . ASP   A 1 207 ? -7.381  -28.175 34.091 1.00 32.32  ?  232 ASP   A H      1 
ATOM   3343  H  HA     . ASP   A 1 207 ? -9.449  -29.006 35.555 1.00 32.94  ?  232 ASP   A HA     1 
ATOM   3344  H  HB2    . ASP   A 1 207 ? -7.908  -30.149 36.817 1.00 32.76  ?  232 ASP   A HB2    1 
ATOM   3345  H  HB3    . ASP   A 1 207 ? -7.568  -30.401 35.286 1.00 32.76  ?  232 ASP   A HB3    1 
ATOM   3346  N  N      . LYS   A 1 208 ? -8.962  -27.880 37.868 1.00 28.10  ?  233 LYS   A N      1 
ATOM   3347  C  CA     . LYS   A 1 208 ? -9.234  -26.906 38.918 1.00 27.26  ?  233 LYS   A CA     1 
ATOM   3348  C  C      . LYS   A 1 208 ? -8.066  -25.951 39.119 1.00 25.71  ?  233 LYS   A C      1 
ATOM   3349  O  O      . LYS   A 1 208 ? -8.273  -24.745 39.300 1.00 25.41  ?  233 LYS   A O      1 
ATOM   3350  C  CB     . LYS   A 1 208 ? -9.551  -27.623 40.233 1.00 30.31  ?  233 LYS   A CB     1 
ATOM   3351  C  CG     . LYS   A 1 208 ? -9.806  -26.702 41.424 1.00 36.20  ?  233 LYS   A CG     1 
ATOM   3352  C  CD     . LYS   A 1 208 ? -9.774  -27.470 42.739 1.00 40.91  ?  233 LYS   A CD     1 
ATOM   3353  C  CE     . LYS   A 1 208 ? -9.943  -26.549 43.937 1.00 46.00  ?  233 LYS   A CE     1 
ATOM   3354  N  NZ     . LYS   A 1 208 ? -9.546  -27.240 45.201 1.00 49.40  ?  233 LYS   A NZ     1 
ATOM   3355  H  H      . LYS   A 1 208 ? -9.034  -28.698 38.121 1.00 33.72  ?  233 LYS   A H      1 
ATOM   3356  H  HA     . LYS   A 1 208 ? -10.009 -26.385 38.654 1.00 32.71  ?  233 LYS   A HA     1 
ATOM   3357  H  HB2    . LYS   A 1 208 ? -10.348 -28.161 40.105 1.00 36.37  ?  233 LYS   A HB2    1 
ATOM   3358  H  HB3    . LYS   A 1 208 ? -8.799  -28.193 40.461 1.00 36.37  ?  233 LYS   A HB3    1 
ATOM   3359  H  HG2    . LYS   A 1 208 ? -9.119  -26.017 41.454 1.00 43.43  ?  233 LYS   A HG2    1 
ATOM   3360  H  HG3    . LYS   A 1 208 ? -10.680 -26.291 41.331 1.00 43.43  ?  233 LYS   A HG3    1 
ATOM   3361  H  HD2    . LYS   A 1 208 ? -10.497 -28.117 42.749 1.00 49.09  ?  233 LYS   A HD2    1 
ATOM   3362  H  HD3    . LYS   A 1 208 ? -8.922  -27.925 42.823 1.00 49.09  ?  233 LYS   A HD3    1 
ATOM   3363  H  HE2    . LYS   A 1 208 ? -9.381  -25.766 43.824 1.00 55.19  ?  233 LYS   A HE2    1 
ATOM   3364  H  HE3    . LYS   A 1 208 ? -10.872 -26.281 44.011 1.00 55.19  ?  233 LYS   A HE3    1 
ATOM   3365  H  HZ1    . LYS   A 1 208 ? -9.654  -26.693 45.895 1.00 59.27  ?  233 LYS   A HZ1    1 
ATOM   3366  H  HZ2    . LYS   A 1 208 ? -10.049 -27.964 45.323 1.00 59.27  ?  233 LYS   A HZ2    1 
ATOM   3367  H  HZ3    . LYS   A 1 208 ? -8.691  -27.486 45.159 1.00 59.27  ?  233 LYS   A HZ3    1 
ATOM   3368  N  N      . ASP   A 1 209 ? -6.833  -26.469 39.116 1.00 24.57  ?  234 ASP   A N      1 
ATOM   3369  C  CA     . ASP   A 1 209 ? -5.691  -25.620 39.445 1.00 23.26  ?  234 ASP   A CA     1 
ATOM   3370  C  C      . ASP   A 1 209 ? -5.418  -24.598 38.348 1.00 22.64  ?  234 ASP   A C      1 
ATOM   3371  O  O      . ASP   A 1 209 ? -5.169  -23.424 38.638 1.00 22.55  ?  234 ASP   A O      1 
ATOM   3372  C  CB     . ASP   A 1 209 ? -4.434  -26.463 39.693 1.00 23.63  ?  234 ASP   A CB     1 
ATOM   3373  C  CG     . ASP   A 1 209 ? -4.371  -27.062 41.102 1.00 25.10  ?  234 ASP   A CG     1 
ATOM   3374  O  OD1    . ASP   A 1 209 ? -5.271  -26.814 41.936 1.00 27.77  ?  234 ASP   A OD1    1 
ATOM   3375  O  OD2    . ASP   A 1 209 ? -3.393  -27.802 41.360 1.00 25.57  ?  234 ASP   A OD2    1 
ATOM   3376  H  H      . ASP   A 1 209 ? -6.639  -27.287 38.931 1.00 29.48  ?  234 ASP   A H      1 
ATOM   3377  H  HA     . ASP   A 1 209 ? -5.903  -25.148 40.265 1.00 27.90  ?  234 ASP   A HA     1 
ATOM   3378  H  HB2    . ASP   A 1 209 ? -4.416  -27.195 39.058 1.00 28.35  ?  234 ASP   A HB2    1 
ATOM   3379  H  HB3    . ASP   A 1 209 ? -3.652  -25.901 39.574 1.00 28.35  ?  234 ASP   A HB3    1 
ATOM   3380  N  N      . ILE   A 1 210 ? -5.451  -25.005 37.078 1.00 23.73  ?  235 ILE   A N      1 
ATOM   3381  C  CA     . ILE   A 1 210 ? -5.180  -24.018 36.035 1.00 22.70  ?  235 ILE   A CA     1 
ATOM   3382  C  C      . ILE   A 1 210 ? -6.315  -23.000 35.966 1.00 22.30  ?  235 ILE   A C      1 
ATOM   3383  O  O      . ILE   A 1 210 ? -6.073  -21.805 35.779 1.00 22.06  ?  235 ILE   A O      1 
ATOM   3384  C  CB     . ILE   A 1 210 ? -4.902  -24.693 34.678 1.00 22.19  ?  235 ILE   A CB     1 
ATOM   3385  C  CG1    . ILE   A 1 210 ? -4.409  -23.662 33.648 1.00 21.96  ?  235 ILE   A CG1    1 
ATOM   3386  C  CG2    . ILE   A 1 210 ? -6.114  -25.419 34.120 1.00 22.37  ?  235 ILE   A CG2    1 
ATOM   3387  C  CD1    . ILE   A 1 210 ? -3.055  -23.045 33.960 1.00 22.53  ?  235 ILE   A CD1    1 
ATOM   3388  H  H      . ILE   A 1 210 ? -5.618  -25.804 36.809 1.00 28.46  ?  235 ILE   A H      1 
ATOM   3389  H  HA     . ILE   A 1 210 ? -4.368  -23.542 36.270 1.00 27.24  ?  235 ILE   A HA     1 
ATOM   3390  H  HB     . ILE   A 1 210 ? -4.212  -25.354 34.844 1.00 26.63  ?  235 ILE   A HB     1 
ATOM   3391  H  HG12   . ILE   A 1 210 ? -4.338  -24.098 32.785 1.00 26.35  ?  235 ILE   A HG12   1 
ATOM   3392  H  HG13   . ILE   A 1 210 ? -5.054  -22.939 33.603 1.00 26.35  ?  235 ILE   A HG13   1 
ATOM   3393  H  HG21   . ILE   A 1 210 ? -5.854  -25.894 33.315 1.00 26.84  ?  235 ILE   A HG21   1 
ATOM   3394  H  HG22   . ILE   A 1 210 ? -6.440  -26.046 34.784 1.00 26.84  ?  235 ILE   A HG22   1 
ATOM   3395  H  HG23   . ILE   A 1 210 ? -6.803  -24.769 33.912 1.00 26.84  ?  235 ILE   A HG23   1 
ATOM   3396  H  HD11   . ILE   A 1 210 ? -2.765  -22.518 33.199 1.00 27.03  ?  235 ILE   A HD11   1 
ATOM   3397  H  HD12   . ILE   A 1 210 ? -3.138  -22.478 34.743 1.00 27.03  ?  235 ILE   A HD12   1 
ATOM   3398  H  HD13   . ILE   A 1 210 ? -2.417  -23.755 34.133 1.00 27.03  ?  235 ILE   A HD13   1 
ATOM   3399  N  N      . VAL   A 1 211 ? -7.565  -23.433 36.171 1.00 22.85  ?  236 VAL   A N      1 
ATOM   3400  C  CA     . VAL   A 1 211 ? -8.663  -22.465 36.194 1.00 23.41  ?  236 VAL   A CA     1 
ATOM   3401  C  C      . VAL   A 1 211 ? -8.461  -21.452 37.318 1.00 22.52  ?  236 VAL   A C      1 
ATOM   3402  O  O      . VAL   A 1 211 ? -8.683  -20.250 37.129 1.00 21.91  ?  236 VAL   A O      1 
ATOM   3403  C  CB     . VAL   A 1 211 ? -10.021 -23.183 36.310 1.00 25.12  ?  236 VAL   A CB     1 
ATOM   3404  C  CG1    . VAL   A 1 211 ? -11.161 -22.185 36.535 1.00 24.72  ?  236 VAL   A CG1    1 
ATOM   3405  C  CG2    . VAL   A 1 211 ? -10.276 -23.972 35.037 1.00 27.02  ?  236 VAL   A CG2    1 
ATOM   3406  H  H      . VAL   A 1 211 ? -7.794  -24.253 36.294 1.00 27.41  ?  236 VAL   A H      1 
ATOM   3407  H  HA     . VAL   A 1 211 ? -8.657  -21.983 35.353 1.00 28.08  ?  236 VAL   A HA     1 
ATOM   3408  H  HB     . VAL   A 1 211 ? -9.997  -23.781 37.073 1.00 30.13  ?  236 VAL   A HB     1 
ATOM   3409  H  HG11   . VAL   A 1 211 ? -12.007 -22.633 36.380 1.00 29.66  ?  236 VAL   A HG11   1 
ATOM   3410  H  HG12   . VAL   A 1 211 ? -11.120 -21.860 37.448 1.00 29.66  ?  236 VAL   A HG12   1 
ATOM   3411  H  HG13   . VAL   A 1 211 ? -11.059 -21.445 35.916 1.00 29.66  ?  236 VAL   A HG13   1 
ATOM   3412  H  HG21   . VAL   A 1 211 ? -11.124 -24.436 35.117 1.00 32.42  ?  236 VAL   A HG21   1 
ATOM   3413  H  HG22   . VAL   A 1 211 ? -10.304 -23.359 34.285 1.00 32.42  ?  236 VAL   A HG22   1 
ATOM   3414  H  HG23   . VAL   A 1 211 ? -9.559  -24.613 34.914 1.00 32.42  ?  236 VAL   A HG23   1 
ATOM   3415  N  N      . ALA   A 1 212 ? -8.025  -21.909 38.497 1.00 22.94  ?  237 ALA   A N      1 
ATOM   3416  C  CA     . ALA   A 1 212 ? -7.866  -21.002 39.634 1.00 22.90  ?  237 ALA   A CA     1 
ATOM   3417  C  C      . ALA   A 1 212 ? -6.741  -20.008 39.384 1.00 21.54  ?  237 ALA   A C      1 
ATOM   3418  O  O      . ALA   A 1 212 ? -6.807  -18.858 39.841 1.00 20.92  ?  237 ALA   A O      1 
ATOM   3419  C  CB     . ALA   A 1 212 ? -7.603  -21.807 40.907 1.00 23.81  ?  237 ALA   A CB     1 
ATOM   3420  H  H      . ALA   A 1 212 ? -7.819  -22.728 38.661 1.00 27.53  ?  237 ALA   A H      1 
ATOM   3421  H  HA     . ALA   A 1 212 ? -8.686  -20.501 39.766 1.00 27.47  ?  237 ALA   A HA     1 
ATOM   3422  H  HB1    . ALA   A 1 212 ? -7.591  -21.203 41.666 1.00 28.56  ?  237 ALA   A HB1    1 
ATOM   3423  H  HB2    . ALA   A 1 212 ? -8.308  -22.463 41.017 1.00 28.56  ?  237 ALA   A HB2    1 
ATOM   3424  H  HB3    . ALA   A 1 212 ? -6.745  -22.254 40.826 1.00 28.56  ?  237 ALA   A HB3    1 
ATOM   3425  N  N      . LEU   A 1 213 ? -5.714  -20.435 38.643 1.00 20.34  ?  238 LEU   A N      1 
ATOM   3426  C  CA     . LEU   A 1 213 ? -4.651  -19.522 38.239 1.00 18.81  ?  238 LEU   A CA     1 
ATOM   3427  C  C      . LEU   A 1 213 ? -5.145  -18.509 37.212 1.00 19.18  ?  238 LEU   A C      1 
ATOM   3428  O  O      . LEU   A 1 213 ? -4.788  -17.326 37.283 1.00 18.44  ?  238 LEU   A O      1 
ATOM   3429  C  CB     . LEU   A 1 213 ? -3.477  -20.317 37.670 1.00 18.68  ?  238 LEU   A CB     1 
ATOM   3430  C  CG     . LEU   A 1 213 ? -2.576  -21.040 38.663 1.00 19.31  ?  238 LEU   A CG     1 
ATOM   3431  C  CD1    . LEU   A 1 213 ? -1.665  -22.047 37.947 1.00 20.31  ?  238 LEU   A CD1    1 
ATOM   3432  C  CD2    . LEU   A 1 213 ? -1.736  -20.034 39.440 1.00 19.62  ?  238 LEU   A CD2    1 
ATOM   3433  H  H      . LEU   A 1 213 ? -5.612  -21.242 38.365 1.00 24.40  ?  238 LEU   A H      1 
ATOM   3434  H  HA     . LEU   A 1 213 ? -4.347  -19.035 39.020 1.00 22.56  ?  238 LEU   A HA     1 
ATOM   3435  H  HB2    . LEU   A 1 213 ? -3.835  -20.992 37.073 1.00 22.41  ?  238 LEU   A HB2    1 
ATOM   3436  H  HB3    . LEU   A 1 213 ? -2.913  -19.702 37.175 1.00 22.41  ?  238 LEU   A HB3    1 
ATOM   3437  H  HG     . LEU   A 1 213 ? -3.132  -21.531 39.288 1.00 23.17  ?  238 LEU   A HG     1 
ATOM   3438  H  HD11   . LEU   A 1 213 ? -1.100  -22.484 38.603 1.00 24.36  ?  238 LEU   A HD11   1 
ATOM   3439  H  HD12   . LEU   A 1 213 ? -2.215  -22.704 37.494 1.00 24.36  ?  238 LEU   A HD12   1 
ATOM   3440  H  HD13   . LEU   A 1 213 ? -1.117  -21.573 37.302 1.00 24.36  ?  238 LEU   A HD13   1 
ATOM   3441  H  HD21   . LEU   A 1 213 ? -1.167  -20.513 40.063 1.00 23.54  ?  238 LEU   A HD21   1 
ATOM   3442  H  HD22   . LEU   A 1 213 ? -1.192  -19.528 38.816 1.00 23.54  ?  238 LEU   A HD22   1 
ATOM   3443  H  HD23   . LEU   A 1 213 ? -2.327  -19.437 39.924 1.00 23.54  ?  238 LEU   A HD23   1 
ATOM   3444  N  N      . MET   A 1 214 ? -5.945  -18.959 36.237 1.00 19.49  ?  239 MET   A N      1 
ATOM   3445  C  CA     . MET   A 1 214 ? -6.474  -18.062 35.211 1.00 21.64  ?  239 MET   A CA     1 
ATOM   3446  C  C      . MET   A 1 214 ? -7.455  -17.057 35.801 1.00 21.64  ?  239 MET   A C      1 
ATOM   3447  O  O      . MET   A 1 214 ? -7.429  -15.870 35.444 1.00 22.12  ?  239 MET   A O      1 
ATOM   3448  C  CB     . MET   A 1 214 ? -7.142  -18.887 34.110 1.00 23.39  ?  239 MET   A CB     1 
ATOM   3449  C  CG     . MET   A 1 214 ? -6.159  -19.708 33.287 1.00 24.66  ?  239 MET   A CG     1 
ATOM   3450  S  SD     . MET   A 1 214 ? -6.995  -20.729 32.067 1.00 29.23  ?  239 MET   A SD     1 
ATOM   3451  C  CE     . MET   A 1 214 ? -5.608  -21.291 31.075 1.00 30.51  ?  239 MET   A CE     1 
ATOM   3452  H  H      . MET   A 1 214 ? -6.193  -19.777 36.149 1.00 23.38  ?  239 MET   A H      1 
ATOM   3453  H  HA     . MET   A 1 214 ? -5.737  -17.570 34.816 1.00 25.96  ?  239 MET   A HA     1 
ATOM   3454  H  HB2    . MET   A 1 214 ? -7.774  -19.500 34.518 1.00 28.06  ?  239 MET   A HB2    1 
ATOM   3455  H  HB3    . MET   A 1 214 ? -7.607  -18.286 33.507 1.00 28.06  ?  239 MET   A HB3    1 
ATOM   3456  H  HG2    . MET   A 1 214 ? -5.555  -19.110 32.820 1.00 29.58  ?  239 MET   A HG2    1 
ATOM   3457  H  HG3    . MET   A 1 214 ? -5.657  -20.291 33.878 1.00 29.58  ?  239 MET   A HG3    1 
ATOM   3458  H  HE1    . MET   A 1 214 ? -5.935  -21.892 30.388 1.00 36.61  ?  239 MET   A HE1    1 
ATOM   3459  H  HE2    . MET   A 1 214 ? -5.180  -20.522 30.666 1.00 36.61  ?  239 MET   A HE2    1 
ATOM   3460  H  HE3    . MET   A 1 214 ? -4.978  -21.755 31.648 1.00 36.61  ?  239 MET   A HE3    1 
ATOM   3461  N  N      . VAL   A 1 215 ? -8.328  -17.511 36.702 1.00 22.61  ?  240 VAL   A N      1 
ATOM   3462  C  CA     . VAL   A 1 215 ? -9.245  -16.586 37.359 1.00 22.99  ?  240 VAL   A CA     1 
ATOM   3463  C  C      . VAL   A 1 215 ? -8.463  -15.545 38.149 1.00 21.19  ?  240 VAL   A C      1 
ATOM   3464  O  O      . VAL   A 1 215 ? -8.768  -14.347 38.084 1.00 21.57  ?  240 VAL   A O      1 
ATOM   3465  C  CB     . VAL   A 1 215 ? -10.254 -17.343 38.246 1.00 24.98  ?  240 VAL   A CB     1 
ATOM   3466  C  CG1    . VAL   A 1 215 ? -11.088 -16.357 39.090 1.00 26.60  ?  240 VAL   A CG1    1 
ATOM   3467  C  CG2    . VAL   A 1 215 ? -11.163 -18.222 37.377 1.00 25.31  ?  240 VAL   A CG2    1 
ATOM   3468  H  H      . VAL   A 1 215 ? -8.407  -18.332 36.944 1.00 27.13  ?  240 VAL   A H      1 
ATOM   3469  H  HA     . VAL   A 1 215 ? -9.756  -16.127 36.674 1.00 27.58  ?  240 VAL   A HA     1 
ATOM   3470  H  HB     . VAL   A 1 215 ? -9.768  -17.917 38.858 1.00 29.97  ?  240 VAL   A HB     1 
ATOM   3471  H  HG11   . VAL   A 1 215 ? -11.840 -16.831 39.478 1.00 31.91  ?  240 VAL   A HG11   1 
ATOM   3472  H  HG12   . VAL   A 1 215 ? -10.528 -15.992 39.794 1.00 31.91  ?  240 VAL   A HG12   1 
ATOM   3473  H  HG13   . VAL   A 1 215 ? -11.407 -15.642 38.518 1.00 31.91  ?  240 VAL   A HG13   1 
ATOM   3474  H  HG21   . VAL   A 1 215 ? -11.734 -18.753 37.954 1.00 30.37  ?  240 VAL   A HG21   1 
ATOM   3475  H  HG22   . VAL   A 1 215 ? -11.705 -17.652 36.810 1.00 30.37  ?  240 VAL   A HG22   1 
ATOM   3476  H  HG23   . VAL   A 1 215 ? -10.612 -18.804 36.831 1.00 30.37  ?  240 VAL   A HG23   1 
ATOM   3477  N  N      . ARG   A 1 216 ? -7.423  -15.970 38.881 1.00 19.99  ?  241 ARG   A N      1 
ATOM   3478  C  CA     . ARG   A 1 216 ? -6.625  -14.991 39.621 1.00 19.72  ?  241 ARG   A CA     1 
ATOM   3479  C  C      . ARG   A 1 216 ? -5.977  -13.988 38.669 1.00 18.67  ?  241 ARG   A C      1 
ATOM   3480  O  O      . ARG   A 1 216 ? -5.910  -12.794 38.960 1.00 18.64  ?  241 ARG   A O      1 
ATOM   3481  C  CB     . ARG   A 1 216 ? -5.533  -15.653 40.472 1.00 19.48  ?  241 ARG   A CB     1 
ATOM   3482  C  CG     . ARG   A 1 216 ? -5.017  -14.710 41.587 1.00 19.46  ?  241 ARG   A CG     1 
ATOM   3483  C  CD     . ARG   A 1 216 ? -3.481  -14.669 41.755 1.00 17.90  ?  241 ARG   A CD     1 
ATOM   3484  N  NE     . ARG   A 1 216 ? -2.838  -14.165 40.547 1.00 16.98  ?  241 ARG   A NE     1 
ATOM   3485  C  CZ     . ARG   A 1 216 ? -2.040  -14.874 39.751 1.00 16.80  ?  241 ARG   A CZ     1 
ATOM   3486  N  NH1    . ARG   A 1 216 ? -1.737  -16.140 40.026 1.00 19.47  ?  241 ARG   A NH1    1 
ATOM   3487  N  NH2    . ARG   A 1 216 ? -1.539  -14.304 38.670 1.00 17.94  ?  241 ARG   A NH2    1 
ATOM   3488  H  H      . ARG   A 1 216 ? -7.171  -16.788 38.961 1.00 23.98  ?  241 ARG   A H      1 
ATOM   3489  H  HA     . ARG   A 1 216 ? -7.228  -14.534 40.228 1.00 23.66  ?  241 ARG   A HA     1 
ATOM   3490  H  HB2    . ARG   A 1 216 ? -5.894  -16.450 40.892 1.00 23.37  ?  241 ARG   A HB2    1 
ATOM   3491  H  HB3    . ARG   A 1 216 ? -4.784  -15.889 39.903 1.00 23.37  ?  241 ARG   A HB3    1 
ATOM   3492  H  HG2    . ARG   A 1 216 ? -5.310  -13.808 41.386 1.00 23.35  ?  241 ARG   A HG2    1 
ATOM   3493  H  HG3    . ARG   A 1 216 ? -5.393  -15.000 42.433 1.00 23.35  ?  241 ARG   A HG3    1 
ATOM   3494  H  HD2    . ARG   A 1 216 ? -3.252  -14.083 42.493 1.00 21.48  ?  241 ARG   A HD2    1 
ATOM   3495  H  HD3    . ARG   A 1 216 ? -3.151  -15.565 41.928 1.00 21.48  ?  241 ARG   A HD3    1 
ATOM   3496  H  HE     . ARG   A 1 216 ? -2.986  -13.346 40.331 1.00 20.37  ?  241 ARG   A HE     1 
ATOM   3497  H  HH11   . ARG   A 1 216 ? -2.058  -16.517 40.729 1.00 23.36  ?  241 ARG   A HH11   1 
ATOM   3498  H  HH12   . ARG   A 1 216 ? -1.219  -16.582 39.500 1.00 23.36  ?  241 ARG   A HH12   1 
ATOM   3499  H  HH21   . ARG   A 1 216 ? -1.730  -13.485 38.489 1.00 21.53  ?  241 ARG   A HH21   1 
ATOM   3500  H  HH22   . ARG   A 1 216 ? -1.022  -14.751 38.149 1.00 21.53  ?  241 ARG   A HH22   1 
ATOM   3501  N  N      . ARG   A 1 217 ? -5.499  -14.456 37.517 1.00 18.89  ?  242 ARG   A N      1 
ATOM   3502  C  CA     . ARG   A 1 217 ? -4.897  -13.544 36.546 1.00 19.55  ?  242 ARG   A CA     1 
ATOM   3503  C  C      . ARG   A 1 217 ? -5.901  -12.490 36.072 1.00 19.59  ?  242 ARG   A C      1 
ATOM   3504  O  O      . ARG   A 1 217 ? -5.531  -11.331 35.843 1.00 19.20  ?  242 ARG   A O      1 
ATOM   3505  C  CB     . ARG   A 1 217 ? -4.343  -14.351 35.372 1.00 19.79  ?  242 ARG   A CB     1 
ATOM   3506  C  CG     . ARG   A 1 217 ? -3.356  -13.590 34.527 1.00 19.14  ?  242 ARG   A CG     1 
ATOM   3507  C  CD     . ARG   A 1 217 ? -1.903  -13.429 35.168 1.00 17.10  ?  242 ARG   A CD     1 
ATOM   3508  N  NE     . ARG   A 1 217 ? -1.252  -12.567 34.204 1.00 16.55  ?  242 ARG   A NE     1 
ATOM   3509  C  CZ     . ARG   A 1 217 ? -1.214  -11.244 34.279 1.00 16.08  ?  242 ARG   A CZ     1 
ATOM   3510  N  NH1    . ARG   A 1 217 ? -1.634  -10.624 35.375 1.00 16.81  ?  242 ARG   A NH1    1 
ATOM   3511  N  NH2    . ARG   A 1 217 ? -0.718  -10.554 33.262 1.00 16.62  ?  242 ARG   A NH2    1 
ATOM   3512  H  H      . ARG   A 1 217 ? -5.511  -15.281 37.276 1.00 22.66  ?  242 ARG   A H      1 
ATOM   3513  H  HA     . ARG   A 1 217 ? -4.160  -13.070 36.961 1.00 23.46  ?  242 ARG   A HA     1 
ATOM   3514  H  HB2    . ARG   A 1 217 ? -3.892  -15.136 35.719 1.00 23.75  ?  242 ARG   A HB2    1 
ATOM   3515  H  HB3    . ARG   A 1 217 ? -5.080  -14.617 34.800 1.00 23.75  ?  242 ARG   A HB3    1 
ATOM   3516  H  HG2    . ARG   A 1 217 ? -3.251  -14.056 33.683 1.00 22.97  ?  242 ARG   A HG2    1 
ATOM   3517  H  HG3    . ARG   A 1 217 ? -3.706  -12.699 34.373 1.00 22.97  ?  242 ARG   A HG3    1 
ATOM   3518  H  HD2    . ARG   A 1 217 ? -1.942  -13.005 36.040 1.00 20.51  ?  242 ARG   A HD2    1 
ATOM   3519  H  HD3    . ARG   A 1 217 ? -1.445  -14.281 35.234 1.00 20.51  ?  242 ARG   A HD3    1 
ATOM   3520  H  HE     . ARG   A 1 217 ? -0.863  -12.940 33.534 1.00 19.86  ?  242 ARG   A HE     1 
ATOM   3521  H  HH11   . ARG   A 1 217 ? -1.932  -11.080 36.040 1.00 20.17  ?  242 ARG   A HH11   1 
ATOM   3522  H  HH12   . ARG   A 1 217 ? -1.607  -9.765  35.420 1.00 20.17  ?  242 ARG   A HH12   1 
ATOM   3523  H  HH21   . ARG   A 1 217 ? -0.427  -10.965 32.564 1.00 19.94  ?  242 ARG   A HH21   1 
ATOM   3524  H  HH22   . ARG   A 1 217 ? -0.688  -9.696  33.299 1.00 19.94  ?  242 ARG   A HH22   1 
ATOM   3525  N  N      . ALA   A 1 218 ? -7.168  -12.873 35.900 1.00 19.62  ?  243 ALA   A N      1 
ATOM   3526  C  CA     . ALA   A 1 218 ? -8.202  -11.891 35.580 1.00 20.60  ?  243 ALA   A CA     1 
ATOM   3527  C  C      . ALA   A 1 218 ? -8.353  -10.848 36.686 1.00 20.50  ?  243 ALA   A C      1 
ATOM   3528  O  O      . ALA   A 1 218 ? -8.533  -9.654  36.406 1.00 20.43  ?  243 ALA   A O      1 
ATOM   3529  C  CB     . ALA   A 1 218 ? -9.527  -12.613 35.335 1.00 20.42  ?  243 ALA   A CB     1 
ATOM   3530  H  H      . ALA   A 1 218 ? -7.450  -13.683 35.963 1.00 23.53  ?  243 ALA   A H      1 
ATOM   3531  H  HA     . ALA   A 1 218 ? -7.951  -11.421 34.769 1.00 24.71  ?  243 ALA   A HA     1 
ATOM   3532  H  HB1    . ALA   A 1 218 ? -10.208 -11.957 35.120 1.00 24.49  ?  243 ALA   A HB1    1 
ATOM   3533  H  HB2    . ALA   A 1 218 ? -9.418  -13.232 34.596 1.00 24.49  ?  243 ALA   A HB2    1 
ATOM   3534  H  HB3    . ALA   A 1 218 ? -9.776  -13.097 36.138 1.00 24.49  ?  243 ALA   A HB3    1 
ATOM   3535  N  N      . TYR   A 1 219 ? -8.291  -11.277 37.949 1.00 19.74  ?  244 TYR   A N      1 
ATOM   3536  C  CA     . TYR   A 1 219 ? -8.307  -10.315 39.048 1.00 19.91  ?  244 TYR   A CA     1 
ATOM   3537  C  C      . TYR   A 1 219 ? -7.086  -9.400  38.997 1.00 19.26  ?  244 TYR   A C      1 
ATOM   3538  O  O      . TYR   A 1 219 ? -7.199  -8.200  39.276 1.00 20.07  ?  244 TYR   A O      1 
ATOM   3539  C  CB     . TYR   A 1 219 ? -8.377  -11.039 40.401 1.00 21.48  ?  244 TYR   A CB     1 
ATOM   3540  C  CG     . TYR   A 1 219 ? -9.777  -11.392 40.856 1.00 23.34  ?  244 TYR   A CG     1 
ATOM   3541  C  CD1    . TYR   A 1 219 ? -10.382 -12.583 40.469 1.00 25.85  ?  244 TYR   A CD1    1 
ATOM   3542  C  CD2    . TYR   A 1 219 ? -10.484 -10.544 41.691 1.00 25.57  ?  244 TYR   A CD2    1 
ATOM   3543  C  CE1    . TYR   A 1 219 ? -11.664 -12.900 40.890 1.00 27.46  ?  244 TYR   A CE1    1 
ATOM   3544  C  CE2    . TYR   A 1 219 ? -11.759 -10.856 42.109 1.00 28.26  ?  244 TYR   A CE2    1 
ATOM   3545  C  CZ     . TYR   A 1 219 ? -12.346 -12.031 41.713 1.00 29.40  ?  244 TYR   A CZ     1 
ATOM   3546  O  OH     . TYR   A 1 219 ? -13.616 -12.320 42.144 1.00 32.38  ?  244 TYR   A OH     1 
ATOM   3547  H  H      . TYR   A 1 219 ? -8.239  -12.101 38.190 1.00 23.68  ?  244 TYR   A H      1 
ATOM   3548  H  HA     . TYR   A 1 219 ? -9.103  -9.768  38.965 1.00 23.88  ?  244 TYR   A HA     1 
ATOM   3549  H  HB2    . TYR   A 1 219 ? -7.874  -11.866 40.334 1.00 25.77  ?  244 TYR   A HB2    1 
ATOM   3550  H  HB3    . TYR   A 1 219 ? -7.984  -10.466 41.078 1.00 25.77  ?  244 TYR   A HB3    1 
ATOM   3551  H  HD1    . TYR   A 1 219 ? -9.920  -13.175 39.921 1.00 31.01  ?  244 TYR   A HD1    1 
ATOM   3552  H  HD2    . TYR   A 1 219 ? -10.092 -9.750  41.974 1.00 30.67  ?  244 TYR   A HD2    1 
ATOM   3553  H  HE1    . TYR   A 1 219 ? -12.061 -13.695 40.618 1.00 32.95  ?  244 TYR   A HE1    1 
ATOM   3554  H  HE2    . TYR   A 1 219 ? -12.224 -10.269 42.661 1.00 33.90  ?  244 TYR   A HE2    1 
ATOM   3555  H  HH     . TYR   A 1 219 ? -13.871 -13.051 41.817 1.00 38.85  ?  244 TYR   A HH     1 
ATOM   3556  N  N      . ASP   A 1 220 ? -5.911  -9.949  38.631 1.00 18.37  ?  245 ASP   A N      1 
ATOM   3557  C  CA     . ASP   A 1 220 ? -4.709  -9.131  38.464 1.00 16.99  ?  245 ASP   A CA     1 
ATOM   3558  C  C      . ASP   A 1 220 ? -4.974  -7.974  37.502 1.00 16.78  ?  245 ASP   A C      1 
ATOM   3559  O  O      . ASP   A 1 220 ? -4.583  -6.830  37.747 1.00 17.27  ?  245 ASP   A O      1 
ATOM   3560  C  CB     . ASP   A 1 220 ? -3.529  -9.913  37.857 1.00 16.44  ?  245 ASP   A CB     1 
ATOM   3561  C  CG     . ASP   A 1 220 ? -2.975  -11.046 38.699 1.00 16.40  ?  245 ASP   A CG     1 
ATOM   3562  O  OD1    . ASP   A 1 220 ? -3.361  -11.243 39.883 1.00 17.41  ?  245 ASP   A OD1    1 
ATOM   3563  O  OD2    . ASP   A 1 220 ? -2.094  -11.738 38.135 1.00 16.65  ?  245 ASP   A OD2    1 
ATOM   3564  H  H      . ASP   A 1 220 ? -5.790  -10.786 38.475 1.00 22.04  ?  245 ASP   A H      1 
ATOM   3565  H  HA     . ASP   A 1 220 ? -4.472  -8.832  39.356 1.00 20.38  ?  245 ASP   A HA     1 
ATOM   3566  H  HB2    . ASP   A 1 220 ? -3.822  -10.299 37.017 1.00 19.72  ?  245 ASP   A HB2    1 
ATOM   3567  H  HB3    . ASP   A 1 220 ? -2.802  -9.291  37.701 1.00 19.72  ?  245 ASP   A HB3    1 
ATOM   3568  N  N      . ILE   A 1 221 ? -5.572  -8.290  36.343 1.00 16.51  ?  246 ILE   A N      1 
ATOM   3569  C  CA     . ILE   A 1 221 ? -5.852  -7.283  35.314 1.00 18.10  ?  246 ILE   A CA     1 
ATOM   3570  C  C      . ILE   A 1 221 ? -6.814  -6.233  35.854 1.00 20.47  ?  246 ILE   A C      1 
ATOM   3571  O  O      . ILE   A 1 221 ? -6.639  -5.029  35.626 1.00 21.53  ?  246 ILE   A O      1 
ATOM   3572  C  CB     . ILE   A 1 221 ? -6.407  -7.968  34.044 1.00 20.45  ?  246 ILE   A CB     1 
ATOM   3573  C  CG1    . ILE   A 1 221 ? -5.355  -8.903  33.421 1.00 20.55  ?  246 ILE   A CG1    1 
ATOM   3574  C  CG2    . ILE   A 1 221 ? -6.947  -6.940  33.021 1.00 21.79  ?  246 ILE   A CG2    1 
ATOM   3575  C  CD1    . ILE   A 1 221 ? -4.169  -8.183  32.804 1.00 21.49  ?  246 ILE   A CD1    1 
ATOM   3576  H  H      . ILE   A 1 221 ? -5.826  -9.083  36.128 1.00 19.80  ?  246 ILE   A H      1 
ATOM   3577  H  HA     . ILE   A 1 221 ? -5.025  -6.835  35.078 1.00 21.72  ?  246 ILE   A HA     1 
ATOM   3578  H  HB     . ILE   A 1 221 ? -7.163  -8.513  34.315 1.00 24.53  ?  246 ILE   A HB     1 
ATOM   3579  H  HG12   . ILE   A 1 221 ? -5.015  -9.492  34.113 1.00 24.65  ?  246 ILE   A HG12   1 
ATOM   3580  H  HG13   . ILE   A 1 221 ? -5.779  -9.425  32.722 1.00 24.65  ?  246 ILE   A HG13   1 
ATOM   3581  H  HG21   . ILE   A 1 221 ? -7.058  -7.377  32.162 1.00 26.15  ?  246 ILE   A HG21   1 
ATOM   3582  H  HG22   . ILE   A 1 221 ? -7.801  -6.602  33.332 1.00 26.15  ?  246 ILE   A HG22   1 
ATOM   3583  H  HG23   . ILE   A 1 221 ? -6.312  -6.211  32.941 1.00 26.15  ?  246 ILE   A HG23   1 
ATOM   3584  H  HD11   . ILE   A 1 221 ? -3.562  -8.839  32.429 1.00 25.78  ?  246 ILE   A HD11   1 
ATOM   3585  H  HD12   . ILE   A 1 221 ? -4.489  -7.590  32.106 1.00 25.78  ?  246 ILE   A HD12   1 
ATOM   3586  H  HD13   . ILE   A 1 221 ? -3.718  -7.670  33.493 1.00 25.78  ?  246 ILE   A HD13   1 
ATOM   3587  N  N      . ALA   A 1 222 ? -7.845  -6.673  36.577 1.00 20.66  ?  247 ALA   A N      1 
ATOM   3588  C  CA     . ALA   A 1 222 ? -8.780  -5.731  37.181 1.00 21.77  ?  247 ALA   A CA     1 
ATOM   3589  C  C      . ALA   A 1 222 ? -8.059  -4.811  38.161 1.00 21.60  ?  247 ALA   A C      1 
ATOM   3590  O  O      . ALA   A 1 222 ? -8.409  -3.631  38.296 1.00 23.99  ?  247 ALA   A O      1 
ATOM   3591  C  CB     . ALA   A 1 222 ? -9.907  -6.484  37.883 1.00 21.68  ?  247 ALA   A CB     1 
ATOM   3592  H  H      . ALA   A 1 222 ? -8.023  -7.501  36.729 1.00 24.78  ?  247 ALA   A H      1 
ATOM   3593  H  HA     . ALA   A 1 222 ? -9.177  -5.186  36.484 1.00 26.12  ?  247 ALA   A HA     1 
ATOM   3594  H  HB1    . ALA   A 1 222 ? -10.533 -5.843  38.253 1.00 26.01  ?  247 ALA   A HB1    1 
ATOM   3595  H  HB2    . ALA   A 1 222 ? -10.357 -7.052  37.237 1.00 26.01  ?  247 ALA   A HB2    1 
ATOM   3596  H  HB3    . ALA   A 1 222 ? -9.530  -7.026  38.593 1.00 26.01  ?  247 ALA   A HB3    1 
ATOM   3597  N  N      . GLY   A 1 223 ? -7.048  -5.346  38.868 1.00 20.08  ?  248 GLY   A N      1 
ATOM   3598  C  CA     . GLY   A 1 223 ? -6.307  -4.528  39.819 1.00 21.48  ?  248 GLY   A CA     1 
ATOM   3599  C  C      . GLY   A 1 223 ? -5.234  -3.650  39.213 1.00 20.29  ?  248 GLY   A C      1 
ATOM   3600  O  O      . GLY   A 1 223 ? -4.918  -2.596  39.772 1.00 22.71  ?  248 GLY   A O      1 
ATOM   3601  H  H      . GLY   A 1 223 ? -6.783  -6.162  38.812 1.00 24.09  ?  248 GLY   A H      1 
ATOM   3602  H  HA2    . GLY   A 1 223 ? -6.932  -3.950  40.283 1.00 25.77  ?  248 GLY   A HA2    1 
ATOM   3603  H  HA3    . GLY   A 1 223 ? -5.879  -5.113  40.464 1.00 25.77  ?  248 GLY   A HA3    1 
ATOM   3604  N  N      . SER   A 1 224 ? -4.650  -4.053  38.082 1.00 18.31  ?  249 SER   A N      1 
ATOM   3605  C  CA     . SER   A 1 224 ? -3.483  -3.361  37.552 1.00 18.17  ?  249 SER   A CA     1 
ATOM   3606  C  C      . SER   A 1 224 ? -3.828  -2.340  36.478 1.00 19.03  ?  249 SER   A C      1 
ATOM   3607  O  O      . SER   A 1 224 ? -3.038  -1.418  36.254 1.00 20.03  ?  249 SER   A O      1 
ATOM   3608  C  CB     . SER   A 1 224 ? -2.469  -4.366  36.983 1.00 18.47  ?  249 SER   A CB     1 
ATOM   3609  O  OG     . SER   A 1 224 ? -2.955  -5.001  35.817 1.00 19.32  ?  249 SER   A OG     1 
ATOM   3610  H  H      . SER   A 1 224 ? -4.913  -4.722  37.608 1.00 21.96  ?  249 SER   A H      1 
ATOM   3611  H  HA     . SER   A 1 224 ? -3.047  -2.891  38.280 1.00 21.80  ?  249 SER   A HA     1 
ATOM   3612  H  HB2    . SER   A 1 224 ? -1.651  -3.894  36.763 1.00 22.15  ?  249 SER   A HB2    1 
ATOM   3613  H  HB3    . SER   A 1 224 ? -2.290  -5.043  37.655 1.00 22.15  ?  249 SER   A HB3    1 
ATOM   3614  H  HG     . SER   A 1 224 ? -3.663  -5.417  35.991 1.00 23.17  ?  249 SER   A HG     1 
ATOM   3615  N  N      . THR   A 1 225 ? -4.983  -2.468  35.824 1.00 21.04  ?  250 THR   A N      1 
ATOM   3616  C  CA     . THR   A 1 225 ? -5.424  -1.519  34.814 1.00 23.15  ?  250 THR   A CA     1 
ATOM   3617  C  C      . THR   A 1 225 ? -6.182  -0.367  35.480 1.00 24.59  ?  250 THR   A C      1 
ATOM   3618  O  O      . THR   A 1 225 ? -6.548  -0.427  36.653 1.00 27.36  ?  250 THR   A O      1 
ATOM   3619  C  CB     . THR   A 1 225 ? -6.312  -2.203  33.770 1.00 25.72  ?  250 THR   A CB     1 
ATOM   3620  O  OG1    . THR   A 1 225 ? -7.484  -2.737  34.402 1.00 24.97  ?  250 THR   A OG1    1 
ATOM   3621  C  CG2    . THR   A 1 225 ? -5.581  -3.321  33.061 1.00 25.66  ?  250 THR   A CG2    1 
ATOM   3622  H  H      . THR   A 1 225 ? -5.537  -3.113  35.952 1.00 25.24  ?  250 THR   A H      1 
ATOM   3623  H  HA     . THR   A 1 225 ? -4.648  -1.162  34.354 1.00 27.77  ?  250 THR   A HA     1 
ATOM   3624  H  HB     . THR   A 1 225 ? -6.566  -1.544  33.105 1.00 30.86  ?  250 THR   A HB     1 
ATOM   3625  H  HG1    . THR   A 1 225 ? -7.265  -3.310  34.975 1.00 29.96  ?  250 THR   A HG1    1 
ATOM   3626  H  HG21   . THR   A 1 225 ? -6.150  -3.708  32.378 1.00 30.79  ?  250 THR   A HG21   1 
ATOM   3627  H  HG22   . THR   A 1 225 ? -4.776  -2.978  32.642 1.00 30.79  ?  250 THR   A HG22   1 
ATOM   3628  H  HG23   . THR   A 1 225 ? -5.336  -4.012  33.696 1.00 30.79  ?  250 THR   A HG23   1 
ATOM   3629  N  N      . LYS   A 1 226 ? -6.395  0.705   34.720 1.00 23.83  ?  251 LYS   A N      1 
ATOM   3630  C  CA     . LYS   A 1 226 ? -7.222  1.828   35.142 1.00 25.67  ?  251 LYS   A CA     1 
ATOM   3631  C  C      . LYS   A 1 226 ? -8.403  1.953   34.190 1.00 25.21  ?  251 LYS   A C      1 
ATOM   3632  O  O      . LYS   A 1 226 ? -8.234  1.852   32.971 1.00 26.36  ?  251 LYS   A O      1 
ATOM   3633  C  CB     . LYS   A 1 226 ? -6.405  3.125   35.173 1.00 29.38  ?  251 LYS   A CB     1 
ATOM   3634  C  CG     . LYS   A 1 226 ? -5.281  3.081   36.212 1.00 33.93  ?  251 LYS   A CG     1 
ATOM   3635  C  CD     . LYS   A 1 226 ? -4.564  4.412   36.448 1.00 38.32  ?  251 LYS   A CD     1 
ATOM   3636  C  CE     . LYS   A 1 226 ? -3.476  4.203   37.518 1.00 39.78  ?  251 LYS   A CE     1 
ATOM   3637  N  NZ     . LYS   A 1 226 ? -2.738  5.411   37.917 1.00 43.05  ?  251 LYS   A NZ     1 
ATOM   3638  H  H      . LYS   A 1 226 ? -6.061  0.805   33.934 1.00 28.59  ?  251 LYS   A H      1 
ATOM   3639  H  HA     . LYS   A 1 226 ? -7.569  1.673   36.034 1.00 30.80  ?  251 LYS   A HA     1 
ATOM   3640  H  HB2    . LYS   A 1 226 ? -6.004  3.269   34.302 1.00 35.25  ?  251 LYS   A HB2    1 
ATOM   3641  H  HB3    . LYS   A 1 226 ? -6.992  3.865   35.395 1.00 35.25  ?  251 LYS   A HB3    1 
ATOM   3642  H  HG2    . LYS   A 1 226 ? -5.658  2.801   37.061 1.00 40.71  ?  251 LYS   A HG2    1 
ATOM   3643  H  HG3    . LYS   A 1 226 ? -4.615  2.441   35.918 1.00 40.71  ?  251 LYS   A HG3    1 
ATOM   3644  H  HD2    . LYS   A 1 226 ? -4.147  4.714   35.626 1.00 45.98  ?  251 LYS   A HD2    1 
ATOM   3645  H  HD3    . LYS   A 1 226 ? -5.195  5.078   36.764 1.00 45.98  ?  251 LYS   A HD3    1 
ATOM   3646  H  HE2    . LYS   A 1 226 ? -3.896  3.846   38.315 1.00 47.73  ?  251 LYS   A HE2    1 
ATOM   3647  H  HE3    . LYS   A 1 226 ? -2.826  3.570   37.173 1.00 47.73  ?  251 LYS   A HE3    1 
ATOM   3648  H  HZ1    . LYS   A 1 226 ? -2.136  5.207   38.541 1.00 51.65  ?  251 LYS   A HZ1    1 
ATOM   3649  H  HZ2    . LYS   A 1 226 ? -2.318  5.758   37.213 1.00 51.65  ?  251 LYS   A HZ2    1 
ATOM   3650  H  HZ3    . LYS   A 1 226 ? -3.301  6.017   38.245 1.00 51.65  ?  251 LYS   A HZ3    1 
ATOM   3651  N  N      . ASP   A 1 227 ? -9.600  2.139   34.753 1.00 25.49  ?  252 ASP   A N      1 
ATOM   3652  C  CA     . ASP   A 1 227 ? -10.801 2.427   33.970 1.00 28.43  ?  252 ASP   A CA     1 
ATOM   3653  C  C      . ASP   A 1 227 ? -11.137 1.305   32.991 1.00 28.97  ?  252 ASP   A C      1 
ATOM   3654  O  O      . ASP   A 1 227 ? -11.561 1.555   31.860 1.00 30.25  ?  252 ASP   A O      1 
ATOM   3655  C  CB     . ASP   A 1 227 ? -10.646 3.767   33.239 1.00 30.29  ?  252 ASP   A CB     1 
ATOM   3656  C  CG     . ASP   A 1 227 ? -10.489 4.930   34.197 1.00 34.68  ?  252 ASP   A CG     1 
ATOM   3657  O  OD1    . ASP   A 1 227 ? -11.320 5.063   35.118 1.00 36.71  ?  252 ASP   A OD1    1 
ATOM   3658  O  OD2    . ASP   A 1 227 ? -9.524  5.701   34.045 1.00 35.64  ?  252 ASP   A OD2    1 
ATOM   3659  H  H      . ASP   A 1 227 ? -9.743  2.102   35.600 1.00 30.58  ?  252 ASP   A H      1 
ATOM   3660  H  HA     . ASP   A 1 227 ? -11.554 2.487   34.578 1.00 34.11  ?  252 ASP   A HA     1 
ATOM   3661  H  HB2    . ASP   A 1 227 ? -9.858  3.732   32.675 1.00 36.34  ?  252 ASP   A HB2    1 
ATOM   3662  H  HB3    . ASP   A 1 227 ? -11.435 3.926   32.698 1.00 36.34  ?  252 ASP   A HB3    1 
ATOM   3663  N  N      . VAL   A 1 228 ? -10.977 0.061   33.437 1.00 27.90  ?  253 VAL   A N      1 
ATOM   3664  C  CA     . VAL   A 1 228 ? -11.424 -1.115  32.696 1.00 27.29  ?  253 VAL   A CA     1 
ATOM   3665  C  C      . VAL   A 1 228 ? -12.181 -2.015  33.662 1.00 27.29  ?  253 VAL   A C      1 
ATOM   3666  O  O      . VAL   A 1 228 ? -11.621 -2.434  34.683 1.00 27.51  ?  253 VAL   A O      1 
ATOM   3667  C  CB     . VAL   A 1 228 ? -10.249 -1.885  32.065 1.00 26.80  ?  253 VAL   A CB     1 
ATOM   3668  C  CG1    . VAL   A 1 228 ? -10.748 -3.146  31.322 1.00 27.51  ?  253 VAL   A CG1    1 
ATOM   3669  C  CG2    . VAL   A 1 228 ? -9.438  -0.990  31.132 1.00 27.95  ?  253 VAL   A CG2    1 
ATOM   3670  H  H      . VAL   A 1 228 ? -10.602 -0.131  34.187 1.00 33.47  ?  253 VAL   A H      1 
ATOM   3671  H  HA     . VAL   A 1 228 ? -12.027 -0.837  31.989 1.00 32.74  ?  253 VAL   A HA     1 
ATOM   3672  H  HB     . VAL   A 1 228 ? -9.660  -2.173  32.779 1.00 32.16  ?  253 VAL   A HB     1 
ATOM   3673  H  HG11   . VAL   A 1 228 ? -10.021 -3.509  30.792 1.00 33.00  ?  253 VAL   A HG11   1 
ATOM   3674  H  HG12   . VAL   A 1 228 ? -11.041 -3.802  31.974 1.00 33.00  ?  253 VAL   A HG12   1 
ATOM   3675  H  HG13   . VAL   A 1 228 ? -11.488 -2.901  30.744 1.00 33.00  ?  253 VAL   A HG13   1 
ATOM   3676  H  HG21   . VAL   A 1 228 ? -8.732  -1.515  30.725 1.00 33.53  ?  253 VAL   A HG21   1 
ATOM   3677  H  HG22   . VAL   A 1 228 ? -10.025 -0.636  30.445 1.00 33.53  ?  253 VAL   A HG22   1 
ATOM   3678  H  HG23   . VAL   A 1 228 ? -9.055  -0.262  31.647 1.00 33.53  ?  253 VAL   A HG23   1 
ATOM   3679  N  N      . LYS   A 1 229 ? -13.443 -2.310  33.343 1.00 28.36  ?  254 LYS   A N      1 
ATOM   3680  C  CA     . LYS   A 1 229 ? -14.184 -3.345  34.052 1.00 29.12  ?  254 LYS   A CA     1 
ATOM   3681  C  C      . LYS   A 1 229 ? -13.788 -4.708  33.494 1.00 28.28  ?  254 LYS   A C      1 
ATOM   3682  O  O      . LYS   A 1 229 ? -13.627 -4.866  32.279 1.00 29.27  ?  254 LYS   A O      1 
ATOM   3683  C  CB     . LYS   A 1 229 ? -15.694 -3.157  33.887 1.00 32.25  ?  254 LYS   A CB     1 
ATOM   3684  C  CG     . LYS   A 1 229 ? -16.229 -1.754  34.185 1.00 35.98  ?  254 LYS   A CG     1 
ATOM   3685  C  CD     . LYS   A 1 229 ? -17.721 -1.613  33.814 1.00 41.10  ?  254 LYS   A CD     1 
ATOM   3686  C  CE     . LYS   A 1 229 ? -18.652 -2.147  34.906 1.00 45.67  ?  254 LYS   A CE     1 
ATOM   3687  N  NZ     . LYS   A 1 229 ? -20.108 -1.804  34.709 1.00 48.07  ?  254 LYS   A NZ     1 
ATOM   3688  H  H      . LYS   A 1 229 ? -13.890 -1.922  32.719 1.00 34.03  ?  254 LYS   A H      1 
ATOM   3689  H  HA     . LYS   A 1 229 ? -13.982 -3.297  34.999 1.00 34.94  ?  254 LYS   A HA     1 
ATOM   3690  H  HB2    . LYS   A 1 229 ? -15.927 -3.364  32.968 1.00 38.69  ?  254 LYS   A HB2    1 
ATOM   3691  H  HB3    . LYS   A 1 229 ? -16.144 -3.770  34.489 1.00 38.69  ?  254 LYS   A HB3    1 
ATOM   3692  H  HG2    . LYS   A 1 229 ? -16.134 -1.571  35.133 1.00 43.17  ?  254 LYS   A HG2    1 
ATOM   3693  H  HG3    . LYS   A 1 229 ? -15.726 -1.104  33.669 1.00 43.17  ?  254 LYS   A HG3    1 
ATOM   3694  H  HD2    . LYS   A 1 229 ? -17.926 -0.675  33.677 1.00 49.32  ?  254 LYS   A HD2    1 
ATOM   3695  H  HD3    . LYS   A 1 229 ? -17.894 -2.112  33.001 1.00 49.32  ?  254 LYS   A HD3    1 
ATOM   3696  H  HE2    . LYS   A 1 229 ? -18.580 -3.114  34.929 1.00 54.79  ?  254 LYS   A HE2    1 
ATOM   3697  H  HE3    . LYS   A 1 229 ? -18.377 -1.774  35.758 1.00 54.79  ?  254 LYS   A HE3    1 
ATOM   3698  H  HZ1    . LYS   A 1 229 ? -20.594 -2.146  35.372 1.00 57.67  ?  254 LYS   A HZ1    1 
ATOM   3699  H  HZ2    . LYS   A 1 229 ? -20.214 -0.921  34.699 1.00 57.67  ?  254 LYS   A HZ2    1 
ATOM   3700  H  HZ3    . LYS   A 1 229 ? -20.397 -2.139  33.937 1.00 57.67  ?  254 LYS   A HZ3    1 
ATOM   3701  N  N      . VAL   A 1 230 ? -13.650 -5.699  34.375 1.00 27.29  ?  255 VAL   A N      1 
ATOM   3702  C  CA     . VAL   A 1 230 ? -13.279 -7.055  33.983 1.00 26.74  ?  255 VAL   A CA     1 
ATOM   3703  C  C      . VAL   A 1 230 ? -14.395 -8.008  34.390 1.00 28.29  ?  255 VAL   A C      1 
ATOM   3704  O  O      . VAL   A 1 230 ? -14.885 -7.958  35.524 1.00 28.44  ?  255 VAL   A O      1 
ATOM   3705  C  CB     . VAL   A 1 230 ? -11.942 -7.496  34.613 1.00 26.74  ?  255 VAL   A CB     1 
ATOM   3706  C  CG1    . VAL   A 1 230 ? -11.606 -8.922  34.184 1.00 27.53  ?  255 VAL   A CG1    1 
ATOM   3707  C  CG2    . VAL   A 1 230 ? -10.831 -6.536  34.229 1.00 26.35  ?  255 VAL   A CG2    1 
ATOM   3708  H  H      . VAL   A 1 230 ? -13.770 -5.606  35.222 1.00 32.75  ?  255 VAL   A H      1 
ATOM   3709  H  HA     . VAL   A 1 230 ? -13.189 -7.081  33.018 1.00 32.09  ?  255 VAL   A HA     1 
ATOM   3710  H  HB     . VAL   A 1 230 ? -12.024 -7.482  35.579 1.00 32.08  ?  255 VAL   A HB     1 
ATOM   3711  H  HG11   . VAL   A 1 230 ? -10.681 -9.109  34.409 1.00 33.03  ?  255 VAL   A HG11   1 
ATOM   3712  H  HG12   . VAL   A 1 230 ? -12.191 -9.539  34.652 1.00 33.03  ?  255 VAL   A HG12   1 
ATOM   3713  H  HG13   . VAL   A 1 230 ? -11.737 -9.004  33.227 1.00 33.03  ?  255 VAL   A HG13   1 
ATOM   3714  H  HG21   . VAL   A 1 230 ? -9.996  -6.851  34.610 1.00 31.61  ?  255 VAL   A HG21   1 
ATOM   3715  H  HG22   . VAL   A 1 230 ? -10.762 -6.503  33.262 1.00 31.61  ?  255 VAL   A HG22   1 
ATOM   3716  H  HG23   . VAL   A 1 230 ? -11.041 -5.655  34.576 1.00 31.61  ?  255 VAL   A HG23   1 
ATOM   3717  N  N      . PHE   A 1 231 ? -14.782 -8.880  33.467 1.00 28.73  ?  256 PHE   A N      1 
ATOM   3718  C  CA     . PHE   A 1 231 ? -15.787 -9.905  33.706 1.00 29.30  ?  256 PHE   A CA     1 
ATOM   3719  C  C      . PHE   A 1 231 ? -15.147 -11.274 33.547 1.00 29.79  ?  256 PHE   A C      1 
ATOM   3720  O  O      . PHE   A 1 231 ? -14.280 -11.460 32.689 1.00 30.74  ?  256 PHE   A O      1 
ATOM   3721  C  CB     . PHE   A 1 231 ? -16.952 -9.771  32.724 1.00 31.86  ?  256 PHE   A CB     1 
ATOM   3722  C  CG     . PHE   A 1 231 ? -17.735 -8.501  32.881 1.00 32.88  ?  256 PHE   A CG     1 
ATOM   3723  C  CD1    . PHE   A 1 231 ? -17.238 -7.306  32.391 1.00 33.51  ?  256 PHE   A CD1    1 
ATOM   3724  C  CD2    . PHE   A 1 231 ? -18.971 -8.500  33.517 1.00 33.05  ?  256 PHE   A CD2    1 
ATOM   3725  C  CE1    . PHE   A 1 231 ? -17.954 -6.130  32.538 1.00 33.31  ?  256 PHE   A CE1    1 
ATOM   3726  C  CE2    . PHE   A 1 231 ? -19.694 -7.325  33.664 1.00 33.49  ?  256 PHE   A CE2    1 
ATOM   3727  C  CZ     . PHE   A 1 231 ? -19.185 -6.141  33.173 1.00 34.10  ?  256 PHE   A CZ     1 
ATOM   3728  H  H      . PHE   A 1 231 ? -14.466 -8.898  32.668 1.00 34.47  ?  256 PHE   A H      1 
ATOM   3729  H  HA     . PHE   A 1 231 ? -16.135 -9.822  34.607 1.00 35.15  ?  256 PHE   A HA     1 
ATOM   3730  H  HB2    . PHE   A 1 231 ? -16.601 -9.793  31.820 1.00 38.23  ?  256 PHE   A HB2    1 
ATOM   3731  H  HB3    . PHE   A 1 231 ? -17.562 -10.513 32.861 1.00 38.23  ?  256 PHE   A HB3    1 
ATOM   3732  H  HD1    . PHE   A 1 231 ? -16.415 -7.293  31.958 1.00 40.21  ?  256 PHE   A HD1    1 
ATOM   3733  H  HD2    . PHE   A 1 231 ? -19.318 -9.297  33.847 1.00 39.66  ?  256 PHE   A HD2    1 
ATOM   3734  H  HE1    . PHE   A 1 231 ? -17.608 -5.332  32.209 1.00 39.96  ?  256 PHE   A HE1    1 
ATOM   3735  H  HE2    . PHE   A 1 231 ? -20.519 -7.335  34.093 1.00 40.18  ?  256 PHE   A HE2    1 
ATOM   3736  H  HZ     . PHE   A 1 231 ? -19.667 -5.351  33.269 1.00 40.92  ?  256 PHE   A HZ     1 
ATOM   3737  N  N      . LEU   A 1 232 ? -15.573 -12.225 34.375 1.00 28.77  ?  257 LEU   A N      1 
ATOM   3738  C  CA     . LEU   A 1 232 ? -15.136 -13.614 34.300 1.00 30.83  ?  257 LEU   A CA     1 
ATOM   3739  C  C      . LEU   A 1 232 ? -16.392 -14.461 34.199 1.00 32.21  ?  257 LEU   A C      1 
ATOM   3740  O  O      . LEU   A 1 232 ? -17.228 -14.440 35.110 1.00 32.70  ?  257 LEU   A O      1 
ATOM   3741  C  CB     . LEU   A 1 232 ? -14.303 -14.007 35.524 1.00 32.26  ?  257 LEU   A CB     1 
ATOM   3742  C  CG     . LEU   A 1 232 ? -13.486 -15.302 35.556 1.00 34.25  ?  257 LEU   A CG     1 
ATOM   3743  C  CD1    . LEU   A 1 232 ? -14.364 -16.539 35.610 1.00 35.03  ?  257 LEU   A CD1    1 
ATOM   3744  C  CD2    . LEU   A 1 232 ? -12.509 -15.409 34.372 1.00 36.44  ?  257 LEU   A CD2    1 
ATOM   3745  H  H      . LEU   A 1 232 ? -16.135 -12.084 35.010 1.00 34.52  ?  257 LEU   A H      1 
ATOM   3746  H  HA     . LEU   A 1 232 ? -14.581 -13.759 33.518 1.00 36.99  ?  257 LEU   A HA     1 
ATOM   3747  H  HB2    . LEU   A 1 232 ? -13.665 -13.291 35.670 1.00 38.71  ?  257 LEU   A HB2    1 
ATOM   3748  H  HB3    . LEU   A 1 232 ? -14.916 -14.065 36.273 1.00 38.71  ?  257 LEU   A HB3    1 
ATOM   3749  H  HG     . LEU   A 1 232 ? -12.965 -15.270 36.374 1.00 41.10  ?  257 LEU   A HG     1 
ATOM   3750  H  HD11   . LEU   A 1 232 ? -13.807 -17.315 35.774 1.00 42.03  ?  257 LEU   A HD11   1 
ATOM   3751  H  HD12   . LEU   A 1 232 ? -15.009 -16.438 36.328 1.00 42.03  ?  257 LEU   A HD12   1 
ATOM   3752  H  HD13   . LEU   A 1 232 ? -14.825 -16.636 34.762 1.00 42.03  ?  257 LEU   A HD13   1 
ATOM   3753  H  HD21   . LEU   A 1 232 ? -11.987 -16.220 34.466 1.00 43.72  ?  257 LEU   A HD21   1 
ATOM   3754  H  HD22   . LEU   A 1 232 ? -13.016 -15.436 33.546 1.00 43.72  ?  257 LEU   A HD22   1 
ATOM   3755  H  HD23   . LEU   A 1 232 ? -11.923 -14.636 34.376 1.00 43.72  ?  257 LEU   A HD23   1 
ATOM   3756  N  N      . ASN   A 1 233 ? -16.552 -15.153 33.072 1.00 31.75  ?  258 ASN   A N      1 
ATOM   3757  C  CA     . ASN   A 1 233 ? -17.741 -15.963 32.805 1.00 32.40  ?  258 ASN   A CA     1 
ATOM   3758  C  C      . ASN   A 1 233 ? -19.020 -15.174 33.069 1.00 34.71  ?  258 ASN   A C      1 
ATOM   3759  O  O      . ASN   A 1 233 ? -20.013 -15.703 33.576 1.00 34.71  ?  258 ASN   A O      1 
ATOM   3760  C  CB     . ASN   A 1 233 ? -17.721 -17.255 33.624 1.00 33.25  ?  258 ASN   A CB     1 
ATOM   3761  C  CG     . ASN   A 1 233 ? -16.786 -18.306 33.036 1.00 35.52  ?  258 ASN   A CG     1 
ATOM   3762  O  OD1    . ASN   A 1 233 ? -15.887 -17.988 32.262 1.00 36.99  ?  258 ASN   A OD1    1 
ATOM   3763  N  ND2    . ASN   A 1 233 ? -17.013 -19.562 33.388 1.00 37.98  ?  258 ASN   A ND2    1 
ATOM   3764  H  H      . ASN   A 1 233 ? -15.975 -15.170 32.434 1.00 38.10  ?  258 ASN   A H      1 
ATOM   3765  H  HA     . ASN   A 1 233 ? -17.736 -16.203 31.865 1.00 38.88  ?  258 ASN   A HA     1 
ATOM   3766  H  HB2    . ASN   A 1 233 ? -17.421 -17.055 34.524 1.00 39.89  ?  258 ASN   A HB2    1 
ATOM   3767  H  HB3    . ASN   A 1 233 ? -18.616 -17.629 33.648 1.00 39.89  ?  258 ASN   A HB3    1 
ATOM   3768  H  HD21   . ASN   A 1 233 ? -16.512 -20.191 33.083 1.00 45.57  ?  258 ASN   A HD21   1 
ATOM   3769  H  HD22   . ASN   A 1 233 ? -17.661 -19.748 33.922 1.00 45.57  ?  258 ASN   A HD22   1 
ATOM   3770  N  N      . GLY   A 1 234 ? -18.995 -13.893 32.714 1.00 33.35  ?  259 GLY   A N      1 
ATOM   3771  C  CA     . GLY   A 1 234 ? -20.173 -13.058 32.755 1.00 33.99  ?  259 GLY   A CA     1 
ATOM   3772  C  C      . GLY   A 1 234 ? -20.450 -12.381 34.077 1.00 34.74  ?  259 GLY   A C      1 
ATOM   3773  O  O      . GLY   A 1 234 ? -21.462 -11.676 34.193 1.00 35.61  ?  259 GLY   A O      1 
ATOM   3774  H  H      . GLY   A 1 234 ? -18.290 -13.483 32.441 1.00 40.01  ?  259 GLY   A H      1 
ATOM   3775  H  HA2    . GLY   A 1 234 ? -20.081 -12.363 32.085 1.00 40.79  ?  259 GLY   A HA2    1 
ATOM   3776  H  HA3    . GLY   A 1 234 ? -20.945 -13.604 32.539 1.00 40.79  ?  259 GLY   A HA3    1 
ATOM   3777  N  N      . ASN   A 1 235 ? -19.596 -12.569 35.075 1.00 33.27  ?  260 ASN   A N      1 
ATOM   3778  C  CA     . ASN   A 1 235 ? -19.758 -11.937 36.375 1.00 33.53  ?  260 ASN   A CA     1 
ATOM   3779  C  C      . ASN   A 1 235 ? -18.697 -10.866 36.547 1.00 32.92  ?  260 ASN   A C      1 
ATOM   3780  O  O      . ASN   A 1 235 ? -17.507 -11.134 36.354 1.00 32.84  ?  260 ASN   A O      1 
ATOM   3781  C  CB     . ASN   A 1 235 ? -19.662 -12.969 37.491 1.00 34.14  ?  260 ASN   A CB     1 
ATOM   3782  C  CG     . ASN   A 1 235 ? -20.763 -13.981 37.409 1.00 36.13  ?  260 ASN   A CG     1 
ATOM   3783  O  OD1    . ASN   A 1 235 ? -21.933 -13.622 37.297 1.00 37.10  ?  260 ASN   A OD1    1 
ATOM   3784  N  ND2    . ASN   A 1 235 ? -20.402 -15.254 37.439 1.00 36.85  ?  260 ASN   A ND2    1 
ATOM   3785  H  H      . ASN   A 1 235 ? -18.899 -13.071 35.021 1.00 39.92  ?  260 ASN   A H      1 
ATOM   3786  H  HA     . ASN   A 1 235 ? -20.628 -11.511 36.430 1.00 40.22  ?  260 ASN   A HA     1 
ATOM   3787  H  HB2    . ASN   A 1 235 ? -18.815 -13.436 37.422 1.00 40.96  ?  260 ASN   A HB2    1 
ATOM   3788  H  HB3    . ASN   A 1 235 ? -19.726 -12.520 38.348 1.00 40.96  ?  260 ASN   A HB3    1 
ATOM   3789  H  HD21   . ASN   A 1 235 ? -20.999 -15.872 37.395 1.00 44.21  ?  260 ASN   A HD21   1 
ATOM   3790  H  HD22   . ASN   A 1 235 ? -19.570 -15.464 37.503 1.00 44.21  ?  260 ASN   A HD22   1 
ATOM   3791  N  N      . LYS   A 1 236 ? -19.131 -9.661  36.908 1.00 31.51  ?  261 LYS   A N      1 
ATOM   3792  C  CA     . LYS   A 1 236 ? -18.204 -8.555  37.093 1.00 32.18  ?  261 LYS   A CA     1 
ATOM   3793  C  C      . LYS   A 1 236 ? -17.310 -8.804  38.304 1.00 32.55  ?  261 LYS   A C      1 
ATOM   3794  O  O      . LYS   A 1 236 ? -17.798 -9.147  39.385 1.00 33.95  ?  261 LYS   A O      1 
ATOM   3795  C  CB     . LYS   A 1 236 ? -18.973 -7.246  37.270 1.00 33.45  ?  261 LYS   A CB     1 
ATOM   3796  C  CG     . LYS   A 1 236 ? -18.073 -6.016  37.257 1.00 36.51  ?  261 LYS   A CG     1 
ATOM   3797  C  CD     . LYS   A 1 236 ? -18.862 -4.746  37.505 1.00 41.24  ?  261 LYS   A CD     1 
ATOM   3798  C  CE     . LYS   A 1 236 ? -17.928 -3.559  37.632 1.00 46.45  ?  261 LYS   A CE     1 
ATOM   3799  N  NZ     . LYS   A 1 236 ? -16.952 -3.706  38.754 1.00 50.40  ?  261 LYS   A NZ     1 
ATOM   3800  H  H      . LYS   A 1 236 ? -19.955 -9.460  37.051 1.00 37.81  ?  261 LYS   A H      1 
ATOM   3801  H  HA     . LYS   A 1 236 ? -17.639 -8.477  36.308 1.00 38.61  ?  261 LYS   A HA     1 
ATOM   3802  H  HB2    . LYS   A 1 236 ? -19.612 -7.156  36.546 1.00 40.13  ?  261 LYS   A HB2    1 
ATOM   3803  H  HB3    . LYS   A 1 236 ? -19.438 -7.267  38.121 1.00 40.13  ?  261 LYS   A HB3    1 
ATOM   3804  H  HG2    . LYS   A 1 236 ? -17.404 -6.100  37.954 1.00 43.80  ?  261 LYS   A HG2    1 
ATOM   3805  H  HG3    . LYS   A 1 236 ? -17.641 -5.942  36.391 1.00 43.80  ?  261 LYS   A HG3    1 
ATOM   3806  H  HD2    . LYS   A 1 236 ? -19.465 -4.587  36.761 1.00 49.48  ?  261 LYS   A HD2    1 
ATOM   3807  H  HD3    . LYS   A 1 236 ? -19.367 -4.832  38.328 1.00 49.48  ?  261 LYS   A HD3    1 
ATOM   3808  H  HE2    . LYS   A 1 236 ? -17.425 -3.463  36.809 1.00 55.73  ?  261 LYS   A HE2    1 
ATOM   3809  H  HE3    . LYS   A 1 236 ? -18.453 -2.760  37.795 1.00 55.73  ?  261 LYS   A HE3    1 
ATOM   3810  H  HZ1    . LYS   A 1 236 ? -16.383 -4.367  38.578 1.00 60.48  ?  261 LYS   A HZ1    1 
ATOM   3811  H  HZ2    . LYS   A 1 236 ? -16.493 -2.951  38.859 1.00 60.48  ?  261 LYS   A HZ2    1 
ATOM   3812  H  HZ3    . LYS   A 1 236 ? -17.383 -3.890  39.511 1.00 60.48  ?  261 LYS   A HZ3    1 
ATOM   3813  N  N      . LEU   A 1 237 ? -15.988 -8.632  38.124 1.00 31.18  ?  262 LEU   A N      1 
ATOM   3814  C  CA     . LEU   A 1 237 ? -15.051 -8.773  39.242 1.00 31.00  ?  262 LEU   A CA     1 
ATOM   3815  C  C      . LEU   A 1 237 ? -15.107 -7.534  40.132 1.00 31.79  ?  262 LEU   A C      1 
ATOM   3816  O  O      . LEU   A 1 237 ? -14.958 -6.412  39.634 1.00 33.78  ?  262 LEU   A O      1 
ATOM   3817  C  CB     . LEU   A 1 237 ? -13.629 -8.993  38.732 1.00 30.96  ?  262 LEU   A CB     1 
ATOM   3818  C  CG     . LEU   A 1 237 ? -13.480 -10.238 37.854 1.00 30.20  ?  262 LEU   A CG     1 
ATOM   3819  C  CD1    . LEU   A 1 237 ? -11.986 -10.522 37.635 1.00 29.59  ?  262 LEU   A CD1    1 
ATOM   3820  C  CD2    . LEU   A 1 237 ? -14.180 -11.468 38.428 1.00 31.45  ?  262 LEU   A CD2    1 
ATOM   3821  H  H      . LEU   A 1 237 ? -15.618 -8.437  37.373 1.00 37.41  ?  262 LEU   A H      1 
ATOM   3822  H  HA     . LEU   A 1 237 ? -15.299 -9.543  39.777 1.00 37.19  ?  262 LEU   A HA     1 
ATOM   3823  H  HB2    . LEU   A 1 237 ? -13.365 -8.223  38.204 1.00 37.15  ?  262 LEU   A HB2    1 
ATOM   3824  H  HB3    . LEU   A 1 237 ? -13.037 -9.093  39.494 1.00 37.15  ?  262 LEU   A HB3    1 
ATOM   3825  H  HG     . LEU   A 1 237 ? -13.915 -10.062 37.005 1.00 36.23  ?  262 LEU   A HG     1 
ATOM   3826  H  HD11   . LEU   A 1 237 ? -11.893 -11.302 37.066 1.00 35.50  ?  262 LEU   A HD11   1 
ATOM   3827  H  HD12   . LEU   A 1 237 ? -11.577 -9.752  37.210 1.00 35.50  ?  262 LEU   A HD12   1 
ATOM   3828  H  HD13   . LEU   A 1 237 ? -11.566 -10.687 38.494 1.00 35.50  ?  262 LEU   A HD13   1 
ATOM   3829  H  HD21   . LEU   A 1 237 ? -13.876 -12.256 37.951 1.00 37.74  ?  262 LEU   A HD21   1 
ATOM   3830  H  HD22   . LEU   A 1 237 ? -13.961 -11.546 39.370 1.00 37.74  ?  262 LEU   A HD22   1 
ATOM   3831  H  HD23   . LEU   A 1 237 ? -15.139 -11.365 38.320 1.00 37.74  ?  262 LEU   A HD23   1 
ATOM   3832  N  N      . PRO   A 1 238 ? -15.305 -7.696  41.450 1.00 33.44  ?  263 PRO   A N      1 
ATOM   3833  C  CA     . PRO   A 1 238 ? -15.492 -6.535  42.342 1.00 35.31  ?  263 PRO   A CA     1 
ATOM   3834  C  C      . PRO   A 1 238 ? -14.159 -5.948  42.807 1.00 36.62  ?  263 PRO   A C      1 
ATOM   3835  O  O      . PRO   A 1 238 ? -13.846 -5.913  44.002 1.00 40.43  ?  263 PRO   A O      1 
ATOM   3836  C  CB     . PRO   A 1 238 ? -16.302 -7.135  43.496 1.00 35.99  ?  263 PRO   A CB     1 
ATOM   3837  C  CG     . PRO   A 1 238 ? -15.793 -8.538  43.592 1.00 37.12  ?  263 PRO   A CG     1 
ATOM   3838  C  CD     . PRO   A 1 238 ? -15.517 -8.972  42.163 1.00 36.10  ?  263 PRO   A CD     1 
ATOM   3839  H  HA     . PRO   A 1 238 ? -16.016 -5.848  41.900 1.00 42.37  ?  263 PRO   A HA     1 
ATOM   3840  H  HB2    . PRO   A 1 238 ? -16.134 -6.643  44.315 1.00 43.18  ?  263 PRO   A HB2    1 
ATOM   3841  H  HB3    . PRO   A 1 238 ? -17.249 -7.118  43.287 1.00 43.18  ?  263 PRO   A HB3    1 
ATOM   3842  H  HG2    . PRO   A 1 238 ? -14.980 -8.556  44.120 1.00 44.54  ?  263 PRO   A HG2    1 
ATOM   3843  H  HG3    . PRO   A 1 238 ? -16.467 -9.104  43.999 1.00 44.54  ?  263 PRO   A HG3    1 
ATOM   3844  H  HD2    . PRO   A 1 238 ? -14.722 -9.527  42.119 1.00 43.31  ?  263 PRO   A HD2    1 
ATOM   3845  H  HD3    . PRO   A 1 238 ? -16.276 -9.450  41.795 1.00 43.31  ?  263 PRO   A HD3    1 
ATOM   3846  N  N      . VAL   A 1 239 ? -13.359 -5.502  41.850 1.00 34.40  ?  264 VAL   A N      1 
ATOM   3847  C  CA     . VAL   A 1 239 ? -12.080 -4.868  42.124 1.00 33.53  ?  264 VAL   A CA     1 
ATOM   3848  C  C      . VAL   A 1 239 ? -12.184 -3.428  41.660 1.00 34.76  ?  264 VAL   A C      1 
ATOM   3849  O  O      . VAL   A 1 239 ? -12.710 -3.154  40.573 1.00 36.69  ?  264 VAL   A O      1 
ATOM   3850  C  CB     . VAL   A 1 239 ? -10.919 -5.586  41.418 1.00 31.69  ?  264 VAL   A CB     1 
ATOM   3851  C  CG1    . VAL   A 1 239 ? -9.595  -4.869  41.711 1.00 29.87  ?  264 VAL   A CG1    1 
ATOM   3852  C  CG2    . VAL   A 1 239 ? -10.863 -7.032  41.848 1.00 32.83  ?  264 VAL   A CG2    1 
ATOM   3853  H  H      . VAL   A 1 239 ? -13.541 -5.557  41.011 1.00 41.27  ?  264 VAL   A H      1 
ATOM   3854  H  HA     . VAL   A 1 239 ? -11.905 -4.889  43.078 1.00 40.23  ?  264 VAL   A HA     1 
ATOM   3855  H  HB     . VAL   A 1 239 ? -11.062 -5.565  40.459 1.00 38.02  ?  264 VAL   A HB     1 
ATOM   3856  H  HG11   . VAL   A 1 239 ? -8.860  -5.430  41.418 1.00 35.83  ?  264 VAL   A HG11   1 
ATOM   3857  H  HG12   . VAL   A 1 239 ? -9.579  -4.026  41.231 1.00 35.83  ?  264 VAL   A HG12   1 
ATOM   3858  H  HG13   . VAL   A 1 239 ? -9.527  -4.707  42.665 1.00 35.83  ?  264 VAL   A HG13   1 
ATOM   3859  H  HG21   . VAL   A 1 239 ? -10.094 -7.455  41.436 1.00 39.38  ?  264 VAL   A HG21   1 
ATOM   3860  H  HG22   . VAL   A 1 239 ? -10.784 -7.071  42.814 1.00 39.38  ?  264 VAL   A HG22   1 
ATOM   3861  H  HG23   . VAL   A 1 239 ? -11.677 -7.477  41.565 1.00 39.38  ?  264 VAL   A HG23   1 
ATOM   3862  N  N      . LYS   A 1 240 ? -11.708 -2.507  42.484 1.00 34.00  ?  265 LYS   A N      1 
ATOM   3863  C  CA     . LYS   A 1 240 ? -11.681 -1.110  42.074 1.00 39.70  ?  265 LYS   A CA     1 
ATOM   3864  C  C      . LYS   A 1 240 ? -10.257 -0.785  41.640 1.00 40.46  ?  265 LYS   A C      1 
ATOM   3865  O  O      . LYS   A 1 240 ? -9.892  -1.014  40.483 1.00 44.34  ?  265 LYS   A O      1 
ATOM   3866  C  CB     . LYS   A 1 240 ? -12.180 -0.209  43.196 1.00 45.28  ?  265 LYS   A CB     1 
ATOM   3867  C  CG     . LYS   A 1 240 ? -13.701 -0.262  43.374 1.00 50.05  ?  265 LYS   A CG     1 
ATOM   3868  C  CD     . LYS   A 1 240 ? -14.122 -1.374  44.320 1.00 53.86  ?  265 LYS   A CD     1 
ATOM   3869  C  CE     . LYS   A 1 240 ? -15.638 -1.549  44.355 1.00 56.24  ?  265 LYS   A CE     1 
ATOM   3870  N  NZ     . LYS   A 1 240 ? -16.371 -0.300  44.706 1.00 57.55  ?  265 LYS   A NZ     1 
ATOM   3871  H  H      . LYS   A 1 240 ? -11.401 -2.662  43.272 1.00 40.79  ?  265 LYS   A H      1 
ATOM   3872  H  HA     . LYS   A 1 240 ? -12.279 -0.940  41.330 1.00 47.64  ?  265 LYS   A HA     1 
ATOM   3873  H  HB2    . LYS   A 1 240 ? -11.771 -0.488  44.030 1.00 54.33  ?  265 LYS   A HB2    1 
ATOM   3874  H  HB3    . LYS   A 1 240 ? -11.934 0.708   42.996 1.00 54.33  ?  265 LYS   A HB3    1 
ATOM   3875  H  HG2    . LYS   A 1 240 ? -14.010 0.581   43.741 1.00 60.06  ?  265 LYS   A HG2    1 
ATOM   3876  H  HG3    . LYS   A 1 240 ? -14.119 -0.422  42.514 1.00 60.06  ?  265 LYS   A HG3    1 
ATOM   3877  H  HD2    . LYS   A 1 240 ? -13.727 -2.210  44.027 1.00 64.62  ?  265 LYS   A HD2    1 
ATOM   3878  H  HD3    . LYS   A 1 240 ? -13.821 -1.162  45.218 1.00 64.62  ?  265 LYS   A HD3    1 
ATOM   3879  H  HE2    . LYS   A 1 240 ? -15.941 -1.835  43.479 1.00 67.48  ?  265 LYS   A HE2    1 
ATOM   3880  H  HE3    . LYS   A 1 240 ? -15.861 -2.220  45.019 1.00 67.48  ?  265 LYS   A HE3    1 
ATOM   3881  H  HZ1    . LYS   A 1 240 ? -16.209 0.329   44.098 1.00 69.05  ?  265 LYS   A HZ1    1 
ATOM   3882  H  HZ2    . LYS   A 1 240 ? -17.246 -0.458  44.733 1.00 69.05  ?  265 LYS   A HZ2    1 
ATOM   3883  H  HZ3    . LYS   A 1 240 ? -16.106 -0.005  45.503 1.00 69.05  ?  265 LYS   A HZ3    1 
ATOM   3884  N  N      . GLY   A 1 241 ? -9.428  -0.295  42.557 1.00 37.19  ?  266 GLY   A N      1 
ATOM   3885  C  CA     . GLY   A 1 241 ? -8.056  0.036   42.251 1.00 30.40  ?  266 GLY   A CA     1 
ATOM   3886  C  C      . GLY   A 1 241 ? -7.067  -1.021  42.710 1.00 26.47  ?  266 GLY   A C      1 
ATOM   3887  O  O      . GLY   A 1 241 ? -7.419  -2.110  43.167 1.00 27.81  ?  266 GLY   A O      1 
ATOM   3888  H  H      . GLY   A 1 241 ? -9.648  -0.146  43.375 1.00 44.62  ?  266 GLY   A H      1 
ATOM   3889  H  HA2    . GLY   A 1 241 ? -7.962  0.142   41.291 1.00 36.47  ?  266 GLY   A HA2    1 
ATOM   3890  H  HA3    . GLY   A 1 241 ? -7.827  0.873   42.685 1.00 36.47  ?  266 GLY   A HA3    1 
ATOM   3891  N  N      . PHE   A 1 242 ? -5.789  -0.679  42.578 1.00 23.57  ?  267 PHE   A N      1 
ATOM   3892  C  CA     . PHE   A 1 242 ? -4.742  -1.594  43.017 1.00 21.97  ?  267 PHE   A CA     1 
ATOM   3893  C  C      . PHE   A 1 242 ? -4.785  -1.813  44.522 1.00 23.68  ?  267 PHE   A C      1 
ATOM   3894  O  O      . PHE   A 1 242 ? -4.494  -2.917  44.990 1.00 22.49  ?  267 PHE   A O      1 
ATOM   3895  C  CB     . PHE   A 1 242 ? -3.386  -1.046  42.581 1.00 20.69  ?  267 PHE   A CB     1 
ATOM   3896  C  CG     . PHE   A 1 242 ? -2.228  -2.006  42.742 1.00 20.22  ?  267 PHE   A CG     1 
ATOM   3897  C  CD1    . PHE   A 1 242 ? -2.170  -3.196  42.032 1.00 20.84  ?  267 PHE   A CD1    1 
ATOM   3898  C  CD2    . PHE   A 1 242 ? -1.155  -1.674  43.570 1.00 19.73  ?  267 PHE   A CD2    1 
ATOM   3899  C  CE1    . PHE   A 1 242 ? -1.075  -4.051  42.170 1.00 19.59  ?  267 PHE   A CE1    1 
ATOM   3900  C  CE2    . PHE   A 1 242 ? -0.058  -2.525  43.711 1.00 20.51  ?  267 PHE   A CE2    1 
ATOM   3901  C  CZ     . PHE   A 1 242 ? -0.019  -3.708  43.008 1.00 19.68  ?  267 PHE   A CZ     1 
ATOM   3902  H  H      . PHE   A 1 242 ? -5.507  0.063   42.245 1.00 28.28  ?  267 PHE   A H      1 
ATOM   3903  H  HA     . PHE   A 1 242 ? -4.867  -2.460  42.598 1.00 26.35  ?  267 PHE   A HA     1 
ATOM   3904  H  HB2    . PHE   A 1 242 ? -3.438  -0.809  41.642 1.00 24.82  ?  267 PHE   A HB2    1 
ATOM   3905  H  HB3    . PHE   A 1 242 ? -3.187  -0.259  43.112 1.00 24.82  ?  267 PHE   A HB3    1 
ATOM   3906  H  HD1    . PHE   A 1 242 ? -2.866  -3.427  41.460 1.00 25.00  ?  267 PHE   A HD1    1 
ATOM   3907  H  HD2    . PHE   A 1 242 ? -1.172  -0.870  44.036 1.00 23.66  ?  267 PHE   A HD2    1 
ATOM   3908  H  HE1    . PHE   A 1 242 ? -1.052  -4.853  41.700 1.00 23.50  ?  267 PHE   A HE1    1 
ATOM   3909  H  HE2    . PHE   A 1 242 ? 0.643   -2.294  44.277 1.00 24.61  ?  267 PHE   A HE2    1 
ATOM   3910  H  HZ     . PHE   A 1 242 ? 0.712   -4.276  43.093 1.00 23.61  ?  267 PHE   A HZ     1 
ATOM   3911  N  N      . ARG   A 1 243 ? -5.142  -0.789  45.300 1.00 25.45  ?  268 ARG   A N      1 
ATOM   3912  C  CA     A ARG   A 1 243 ? -5.183  -0.959  46.748 0.43 26.53  ?  268 ARG   A CA     1 
ATOM   3913  C  CA     B ARG   A 1 243 ? -5.172  -0.968  46.748 0.57 26.02  ?  268 ARG   A CA     1 
ATOM   3914  C  C      . ARG   A 1 243 ? -6.215  -2.011  47.142 1.00 25.76  ?  268 ARG   A C      1 
ATOM   3915  O  O      . ARG   A 1 243 ? -5.959  -2.848  48.014 1.00 26.08  ?  268 ARG   A O      1 
ATOM   3916  C  CB     A ARG   A 1 243 ? -5.477  0.378   47.426 0.43 28.55  ?  268 ARG   A CB     1 
ATOM   3917  C  CB     B ARG   A 1 243 ? -5.433  0.361   47.458 0.57 27.20  ?  268 ARG   A CB     1 
ATOM   3918  C  CG     A ARG   A 1 243 ? -5.286  0.357   48.927 0.43 31.11  ?  268 ARG   A CG     1 
ATOM   3919  C  CG     B ARG   A 1 243 ? -5.444  0.267   48.987 0.57 30.03  ?  268 ARG   A CG     1 
ATOM   3920  C  CD     A ARG   A 1 243 ? -5.161  1.762   49.501 0.43 32.71  ?  268 ARG   A CD     1 
ATOM   3921  C  CD     B ARG   A 1 243 ? -4.086  -0.143  49.558 0.57 32.47  ?  268 ARG   A CD     1 
ATOM   3922  N  NE     A ARG   A 1 243 ? -4.726  1.710   50.892 0.43 34.09  ?  268 ARG   A NE     1 
ATOM   3923  N  NE     B ARG   A 1 243 ? -4.107  -0.276  51.016 0.57 35.39  ?  268 ARG   A NE     1 
ATOM   3924  C  CZ     A ARG   A 1 243 ? -4.501  2.773   51.655 0.43 35.84  ?  268 ARG   A CZ     1 
ATOM   3925  C  CZ     B ARG   A 1 243 ? -4.346  -1.411  51.670 0.57 36.24  ?  268 ARG   A CZ     1 
ATOM   3926  N  NH1    A ARG   A 1 243 ? -4.667  3.998   51.171 0.43 36.10  ?  268 ARG   A NH1    1 
ATOM   3927  N  NH1    B ARG   A 1 243 ? -4.591  -2.532  51.005 0.57 35.99  ?  268 ARG   A NH1    1 
ATOM   3928  N  NH2    A ARG   A 1 243 ? -4.104  2.602   52.907 0.43 37.02  ?  268 ARG   A NH2    1 
ATOM   3929  N  NH2    B ARG   A 1 243 ? -4.344  -1.423  52.996 0.57 36.97  ?  268 ARG   A NH2    1 
ATOM   3930  H  H      A ARG   A 1 243 ? -5.359  -0.006  45.020 0.43 30.54  ?  268 ARG   A H      1 
ATOM   3931  H  H      B ARG   A 1 243 ? -5.364  -0.006  45.022 0.57 30.54  ?  268 ARG   A H      1 
ATOM   3932  H  HA     A ARG   A 1 243 ? -4.315  -1.260  47.058 0.43 31.83  ?  268 ARG   A HA     1 
ATOM   3933  H  HA     B ARG   A 1 243 ? -4.301  -1.279  47.040 0.57 31.22  ?  268 ARG   A HA     1 
ATOM   3934  H  HB2    A ARG   A 1 243 ? -4.880  1.050   47.062 0.43 34.25  ?  268 ARG   A HB2    1 
ATOM   3935  H  HB2    B ARG   A 1 243 ? -4.736  0.988   47.207 0.57 32.63  ?  268 ARG   A HB2    1 
ATOM   3936  H  HB3    A ARG   A 1 243 ? -6.399  0.622   47.249 0.43 34.25  ?  268 ARG   A HB3    1 
ATOM   3937  H  HB3    B ARG   A 1 243 ? -6.298  0.697   47.177 0.57 32.63  ?  268 ARG   A HB3    1 
ATOM   3938  H  HG2    A ARG   A 1 243 ? -6.050  -0.073  49.341 0.43 37.32  ?  268 ARG   A HG2    1 
ATOM   3939  H  HG2    B ARG   A 1 243 ? -5.677  1.133   49.357 0.57 36.03  ?  268 ARG   A HG2    1 
ATOM   3940  H  HG3    A ARG   A 1 243 ? -4.475  -0.131  49.139 0.43 37.32  ?  268 ARG   A HG3    1 
ATOM   3941  H  HG3    B ARG   A 1 243 ? -6.098  -0.397  49.260 0.57 36.03  ?  268 ARG   A HG3    1 
ATOM   3942  H  HD2    A ARG   A 1 243 ? -4.506  2.265   48.991 0.43 39.25  ?  268 ARG   A HD2    1 
ATOM   3943  H  HD2    B ARG   A 1 243 ? -3.829  -0.999  49.181 0.57 38.96  ?  268 ARG   A HD2    1 
ATOM   3944  H  HD3    A ARG   A 1 243 ? -6.023  2.207   49.463 0.43 39.25  ?  268 ARG   A HD3    1 
ATOM   3945  H  HD3    B ARG   A 1 243 ? -3.428  0.532   49.326 0.57 38.96  ?  268 ARG   A HD3    1 
ATOM   3946  H  HE     A ARG   A 1 243 ? -4.607  0.934   51.243 0.43 40.90  ?  268 ARG   A HE     1 
ATOM   3947  H  HE     B ARG   A 1 243 ? -3.953  0.430   51.483 0.57 42.46  ?  268 ARG   A HE     1 
ATOM   3948  H  HH11   A ARG   A 1 243 ? -4.923  4.108   50.358 0.43 43.31  ?  268 ARG   A HH11   1 
ATOM   3949  H  HH11   B ARG   A 1 243 ? -4.596  -2.530  50.145 0.57 43.18  ?  268 ARG   A HH11   1 
ATOM   3950  H  HH12   A ARG   A 1 243 ? -4.520  4.681   51.672 0.43 43.31  ?  268 ARG   A HH12   1 
ATOM   3951  H  HH12   B ARG   A 1 243 ? -4.745  -3.261  51.434 0.57 43.18  ?  268 ARG   A HH12   1 
ATOM   3952  H  HH21   A ARG   A 1 243 ? -3.994  1.808   53.219 0.43 44.41  ?  268 ARG   A HH21   1 
ATOM   3953  H  HH21   B ARG   A 1 243 ? -4.188  -0.699  53.432 0.57 44.36  ?  268 ARG   A HH21   1 
ATOM   3954  H  HH22   A ARG   A 1 243 ? -3.956  3.285   53.408 0.43 44.41  ?  268 ARG   A HH22   1 
ATOM   3955  H  HH22   B ARG   A 1 243 ? -4.499  -2.156  53.419 0.57 44.36  ?  268 ARG   A HH22   1 
ATOM   3956  N  N      . SER   A 1 244 ? -7.391  -1.997  46.496 1.00 25.43  ?  269 SER   A N      1 
ATOM   3957  C  CA     . SER   A 1 244 ? -8.402  -3.007  46.810 1.00 26.76  ?  269 SER   A CA     1 
ATOM   3958  C  C      . SER   A 1 244 ? -7.949  -4.394  46.361 1.00 26.29  ?  269 SER   A C      1 
ATOM   3959  O  O      . SER   A 1 244 ? -8.321  -5.402  46.976 1.00 27.21  ?  269 SER   A O      1 
ATOM   3960  C  CB     . SER   A 1 244 ? -9.751  -2.635  46.177 1.00 28.83  ?  269 SER   A CB     1 
ATOM   3961  O  OG     . SER   A 1 244 ? -9.770  -2.804  44.771 1.00 29.91  ?  269 SER   A OG     1 
ATOM   3962  H  H      . SER   A 1 244 ? -7.618  -1.429  45.891 1.00 30.50  ?  269 SER   A H      1 
ATOM   3963  H  HA     . SER   A 1 244 ? -8.539  -3.032  47.770 1.00 32.11  ?  269 SER   A HA     1 
ATOM   3964  H  HB2    . SER   A 1 244 ? -10.437 -3.201  46.563 1.00 34.59  ?  269 SER   A HB2    1 
ATOM   3965  H  HB3    . SER   A 1 244 ? -9.936  -1.704  46.376 1.00 34.59  ?  269 SER   A HB3    1 
ATOM   3966  H  HG     . SER   A 1 244 ? -9.165  -2.342  44.418 1.00 35.88  ?  269 SER   A HG     1 
ATOM   3967  N  N      . TYR   A 1 245 ? -7.117  -4.464  45.320 1.00 23.76  ?  270 TYR   A N      1 
ATOM   3968  C  CA     . TYR   A 1 245 ? -6.561  -5.744  44.892 1.00 21.93  ?  270 TYR   A CA     1 
ATOM   3969  C  C      . TYR   A 1 245 ? -5.594  -6.273  45.943 1.00 21.59  ?  270 TYR   A C      1 
ATOM   3970  O  O      . TYR   A 1 245 ? -5.689  -7.429  46.368 1.00 21.53  ?  270 TYR   A O      1 
ATOM   3971  C  CB     . TYR   A 1 245 ? -5.878  -5.570  43.525 1.00 21.48  ?  270 TYR   A CB     1 
ATOM   3972  C  CG     . TYR   A 1 245 ? -5.014  -6.745  43.079 1.00 21.97  ?  270 TYR   A CG     1 
ATOM   3973  C  CD1    . TYR   A 1 245 ? -5.567  -7.836  42.429 1.00 23.38  ?  270 TYR   A CD1    1 
ATOM   3974  C  CD2    . TYR   A 1 245 ? -3.645  -6.751  43.312 1.00 23.01  ?  270 TYR   A CD2    1 
ATOM   3975  C  CE1    . TYR   A 1 245 ? -4.782  -8.905  42.044 1.00 20.56  ?  270 TYR   A CE1    1 
ATOM   3976  C  CE2    . TYR   A 1 245 ? -2.850  -7.809  42.921 1.00 22.31  ?  270 TYR   A CE2    1 
ATOM   3977  C  CZ     . TYR   A 1 245 ? -3.418  -8.882  42.288 1.00 21.72  ?  270 TYR   A CZ     1 
ATOM   3978  O  OH     . TYR   A 1 245 ? -2.617  -9.937  41.911 1.00 21.24  ?  270 TYR   A OH     1 
ATOM   3979  H  H      . TYR   A 1 245 ? -6.862  -3.791  44.850 1.00 28.51  ?  270 TYR   A H      1 
ATOM   3980  H  HA     . TYR   A 1 245 ? -7.268  -6.399  44.783 1.00 26.30  ?  270 TYR   A HA     1 
ATOM   3981  H  HB2    . TYR   A 1 245 ? -6.565  -5.443  42.852 1.00 25.76  ?  270 TYR   A HB2    1 
ATOM   3982  H  HB3    . TYR   A 1 245 ? -5.306  -4.788  43.565 1.00 25.76  ?  270 TYR   A HB3    1 
ATOM   3983  H  HD1    . TYR   A 1 245 ? -6.479  -7.848  42.249 1.00 28.05  ?  270 TYR   A HD1    1 
ATOM   3984  H  HD2    . TYR   A 1 245 ? -3.254  -6.024  43.742 1.00 27.61  ?  270 TYR   A HD2    1 
ATOM   3985  H  HE1    . TYR   A 1 245 ? -5.168  -9.639  41.623 1.00 24.66  ?  270 TYR   A HE1    1 
ATOM   3986  H  HE2    . TYR   A 1 245 ? -1.935  -7.793  43.086 1.00 26.76  ?  270 TYR   A HE2    1 
ATOM   3987  H  HH     . TYR   A 1 245 ? -3.072  -10.509 41.498 1.00 25.48  ?  270 TYR   A HH     1 
ATOM   3988  N  N      . VAL   A 1 246 ? -4.660  -5.426  46.381 1.00 20.74  ?  271 VAL   A N      1 
ATOM   3989  C  CA     . VAL   A 1 246 ? -3.710  -5.825  47.412 1.00 21.94  ?  271 VAL   A CA     1 
ATOM   3990  C  C      . VAL   A 1 246 ? -4.438  -6.252  48.677 1.00 24.25  ?  271 VAL   A C      1 
ATOM   3991  O  O      . VAL   A 1 246 ? -3.993  -7.174  49.376 1.00 24.62  ?  271 VAL   A O      1 
ATOM   3992  C  CB     . VAL   A 1 246 ? -2.728  -4.671  47.690 1.00 22.17  ?  271 VAL   A CB     1 
ATOM   3993  C  CG1    . VAL   A 1 246 ? -1.837  -4.982  48.890 1.00 24.98  ?  271 VAL   A CG1    1 
ATOM   3994  C  CG2    . VAL   A 1 246 ? -1.876  -4.357  46.456 1.00 21.49  ?  271 VAL   A CG2    1 
ATOM   3995  H  H      . VAL   A 1 246 ? -4.558  -4.620  46.098 1.00 24.88  ?  271 VAL   A H      1 
ATOM   3996  H  HA     . VAL   A 1 246 ? -3.202  -6.587  47.092 1.00 26.32  ?  271 VAL   A HA     1 
ATOM   3997  H  HB     . VAL   A 1 246 ? -3.250  -3.882  47.901 1.00 26.59  ?  271 VAL   A HB     1 
ATOM   3998  H  HG11   . VAL   A 1 246 ? -1.078  -4.378  48.885 1.00 29.97  ?  271 VAL   A HG11   1 
ATOM   3999  H  HG12   . VAL   A 1 246 ? -2.351  -4.862  49.704 1.00 29.97  ?  271 VAL   A HG12   1 
ATOM   4000  H  HG13   . VAL   A 1 246 ? -1.530  -5.900  48.826 1.00 29.97  ?  271 VAL   A HG13   1 
ATOM   4001  H  HG21   . VAL   A 1 246 ? -1.246  -3.653  46.678 1.00 25.78  ?  271 VAL   A HG21   1 
ATOM   4002  H  HG22   . VAL   A 1 246 ? -1.396  -5.158  46.191 1.00 25.78  ?  271 VAL   A HG22   1 
ATOM   4003  H  HG23   . VAL   A 1 246 ? -2.457  -4.066  45.736 1.00 25.78  ?  271 VAL   A HG23   1 
ATOM   4004  N  N      . ASP   A 1 247 ? -5.569  -5.597  48.989 1.00 26.38  ?  272 ASP   A N      1 
ATOM   4005  C  CA     A ASP   A 1 247 ? -6.309  -5.932  50.200 0.48 28.59  ?  272 ASP   A CA     1 
ATOM   4006  C  CA     B ASP   A 1 247 ? -6.307  -5.935  50.204 0.52 27.84  ?  272 ASP   A CA     1 
ATOM   4007  C  C      . ASP   A 1 247 ? -6.809  -7.371  50.169 1.00 28.13  ?  272 ASP   A C      1 
ATOM   4008  O  O      . ASP   A 1 247 ? -7.005  -7.981  51.223 1.00 29.66  ?  272 ASP   A O      1 
ATOM   4009  C  CB     A ASP   A 1 247 ? -7.486  -4.969  50.387 0.48 31.94  ?  272 ASP   A CB     1 
ATOM   4010  C  CB     B ASP   A 1 247 ? -7.484  -4.972  50.419 0.52 29.74  ?  272 ASP   A CB     1 
ATOM   4011  C  CG     A ASP   A 1 247 ? -7.045  -3.571  50.806 0.48 37.05  ?  272 ASP   A CG     1 
ATOM   4012  C  CG     B ASP   A 1 247 ? -8.129  -5.115  51.812 0.52 33.57  ?  272 ASP   A CG     1 
ATOM   4013  O  OD1    A ASP   A 1 247 ? -5.911  -3.425  51.307 0.48 39.46  ?  272 ASP   A OD1    1 
ATOM   4014  O  OD1    B ASP   A 1 247 ? -7.439  -4.897  52.833 0.52 34.68  ?  272 ASP   A OD1    1 
ATOM   4015  O  OD2    A ASP   A 1 247 ? -7.839  -2.618  50.639 0.48 39.29  ?  272 ASP   A OD2    1 
ATOM   4016  O  OD2    B ASP   A 1 247 ? -9.335  -5.435  51.895 0.52 35.67  ?  272 ASP   A OD2    1 
ATOM   4017  H  H      . ASP   A 1 247 ? -5.921  -4.966  48.523 1.00 31.64  ?  272 ASP   A H      1 
ATOM   4018  H  HA     . ASP   A 1 247 ? -5.717  -5.833  50.961 1.00 33.40  ?  272 ASP   A HA     1 
ATOM   4019  H  HB2    A ASP   A 1 247 ? -7.969  -4.893  49.549 0.48 38.33  ?  272 ASP   A HB2    1 
ATOM   4020  H  HB2    B ASP   A 1 247 ? -7.167  -4.060  50.328 0.52 35.68  ?  272 ASP   A HB2    1 
ATOM   4021  H  HB3    A ASP   A 1 247 ? -8.072  -5.318  51.077 0.48 38.33  ?  272 ASP   A HB3    1 
ATOM   4022  H  HB3    B ASP   A 1 247 ? -8.166  -5.153  49.753 0.52 35.68  ?  272 ASP   A HB3    1 
ATOM   4023  N  N      . MET   A 1 248 ? -7.019  -7.934  48.973 1.00 26.14  ?  273 MET   A N      1 
ATOM   4024  C  CA     . MET   A 1 248 ? -7.465  -9.323  48.891 1.00 26.96  ?  273 MET   A CA     1 
ATOM   4025  C  C      . MET   A 1 248 ? -6.397  -10.279 49.406 1.00 26.65  ?  273 MET   A C      1 
ATOM   4026  O  O      . MET   A 1 248 ? -6.722  -11.372 49.889 1.00 28.66  ?  273 MET   A O      1 
ATOM   4027  C  CB     . MET   A 1 248 ? -7.841  -9.675  47.452 1.00 28.76  ?  273 MET   A CB     1 
ATOM   4028  C  CG     . MET   A 1 248 ? -9.016  -8.862  46.932 1.00 33.04  ?  273 MET   A CG     1 
ATOM   4029  S  SD     . MET   A 1 248 ? -9.496  -9.225  45.232 1.00 36.99  ?  273 MET   A SD     1 
ATOM   4030  C  CE     . MET   A 1 248 ? -10.044 -10.915 45.409 1.00 40.41  ?  273 MET   A CE     1 
ATOM   4031  H  H      . MET   A 1 248 ? -6.913  -7.541  48.215 1.00 31.36  ?  273 MET   A H      1 
ATOM   4032  H  HA     . MET   A 1 248 ? -8.263  -9.422  49.434 1.00 32.34  ?  273 MET   A HA     1 
ATOM   4033  H  HB2    . MET   A 1 248 ? -7.080  -9.504  46.876 1.00 34.50  ?  273 MET   A HB2    1 
ATOM   4034  H  HB3    . MET   A 1 248 ? -8.084  -10.613 47.410 1.00 34.50  ?  273 MET   A HB3    1 
ATOM   4035  H  HG2    . MET   A 1 248 ? -9.785  -9.037  47.496 1.00 39.65  ?  273 MET   A HG2    1 
ATOM   4036  H  HG3    . MET   A 1 248 ? -8.782  -7.921  46.973 1.00 39.65  ?  273 MET   A HG3    1 
ATOM   4037  H  HE1    . MET   A 1 248 ? -10.362 -11.236 44.551 1.00 48.48  ?  273 MET   A HE1    1 
ATOM   4038  H  HE2    . MET   A 1 248 ? -9.300  -11.459 45.711 1.00 48.48  ?  273 MET   A HE2    1 
ATOM   4039  H  HE3    . MET   A 1 248 ? -10.762 -10.947 46.061 1.00 48.48  ?  273 MET   A HE3    1 
ATOM   4040  N  N      . TYR   A 1 249 ? -5.125  -9.885  49.314 1.00 23.63  ?  274 TYR   A N      1 
ATOM   4041  C  CA     . TYR   A 1 249 ? -4.042  -10.702 49.842 1.00 22.49  ?  274 TYR   A CA     1 
ATOM   4042  C  C      . TYR   A 1 249 ? -3.859  -10.525 51.343 1.00 25.39  ?  274 TYR   A C      1 
ATOM   4043  O  O      . TYR   A 1 249 ? -3.489  -11.474 52.044 1.00 28.59  ?  274 TYR   A O      1 
ATOM   4044  C  CB     . TYR   A 1 249 ? -2.720  -10.337 49.151 1.00 20.62  ?  274 TYR   A CB     1 
ATOM   4045  C  CG     . TYR   A 1 249 ? -2.629  -10.739 47.706 1.00 20.42  ?  274 TYR   A CG     1 
ATOM   4046  C  CD1    . TYR   A 1 249 ? -3.240  -9.989  46.711 1.00 21.07  ?  274 TYR   A CD1    1 
ATOM   4047  C  CD2    . TYR   A 1 249 ? -1.917  -11.864 47.338 1.00 21.46  ?  274 TYR   A CD2    1 
ATOM   4048  C  CE1    . TYR   A 1 249 ? -3.159  -10.366 45.390 1.00 21.30  ?  274 TYR   A CE1    1 
ATOM   4049  C  CE2    . TYR   A 1 249 ? -1.825  -12.242 46.034 1.00 22.04  ?  274 TYR   A CE2    1 
ATOM   4050  C  CZ     . TYR   A 1 249 ? -2.434  -11.490 45.057 1.00 21.90  ?  274 TYR   A CZ     1 
ATOM   4051  O  OH     . TYR   A 1 249 ? -2.316  -11.905 43.746 1.00 24.12  ?  274 TYR   A OH     1 
ATOM   4052  H  H      . TYR   A 1 249 ? -4.866  -9.150  48.950 1.00 28.35  ?  274 TYR   A H      1 
ATOM   4053  H  HA     . TYR   A 1 249 ? -4.263  -11.629 49.659 1.00 26.98  ?  274 TYR   A HA     1 
ATOM   4054  H  HB2    . TYR   A 1 249 ? -2.607  -9.375  49.193 1.00 24.74  ?  274 TYR   A HB2    1 
ATOM   4055  H  HB3    . TYR   A 1 249 ? -1.995  -10.778 49.622 1.00 24.74  ?  274 TYR   A HB3    1 
ATOM   4056  H  HD1    . TYR   A 1 249 ? -3.711  -9.220  46.941 1.00 25.28  ?  274 TYR   A HD1    1 
ATOM   4057  H  HD2    . TYR   A 1 249 ? -1.494  -12.372 47.992 1.00 25.75  ?  274 TYR   A HD2    1 
ATOM   4058  H  HE1    . TYR   A 1 249 ? -3.588  -9.869  44.731 1.00 25.56  ?  274 TYR   A HE1    1 
ATOM   4059  H  HE2    . TYR   A 1 249 ? -1.351  -13.009 45.804 1.00 26.44  ?  274 TYR   A HE2    1 
ATOM   4060  H  HH     . TYR   A 1 249 ? -2.748  -11.390 43.242 1.00 28.93  ?  274 TYR   A HH     1 
ATOM   4061  N  N      . LEU   A 1 250 ? -4.071  -9.305  51.844 1.00 26.01  ?  275 LEU   A N      1 
ATOM   4062  C  CA     . LEU   A 1 250 ? -3.636  -8.929  53.181 1.00 27.74  ?  275 LEU   A CA     1 
ATOM   4063  C  C      . LEU   A 1 250 ? -4.764  -8.806  54.195 1.00 31.92  ?  275 LEU   A C      1 
ATOM   4064  O  O      . LEU   A 1 250 ? -4.480  -8.753  55.397 1.00 32.65  ?  275 LEU   A O      1 
ATOM   4065  C  CB     . LEU   A 1 250 ? -2.875  -7.594  53.127 1.00 26.17  ?  275 LEU   A CB     1 
ATOM   4066  C  CG     . LEU   A 1 250 ? -1.673  -7.587  52.178 1.00 26.20  ?  275 LEU   A CG     1 
ATOM   4067  C  CD1    . LEU   A 1 250 ? -0.950  -6.238  52.218 1.00 27.31  ?  275 LEU   A CD1    1 
ATOM   4068  C  CD2    . LEU   A 1 250 ? -0.677  -8.728  52.447 1.00 26.83  ?  275 LEU   A CD2    1 
ATOM   4069  H  H      . LEU   A 1 250 ? -4.470  -8.673  51.420 1.00 31.20  ?  275 LEU   A H      1 
ATOM   4070  H  HA     . LEU   A 1 250 ? -3.034  -9.618  53.503 1.00 33.29  ?  275 LEU   A HA     1 
ATOM   4071  H  HB2    . LEU   A 1 250 ? -3.487  -6.902  52.832 1.00 31.40  ?  275 LEU   A HB2    1 
ATOM   4072  H  HB3    . LEU   A 1 250 ? -2.548  -7.390  54.017 1.00 31.40  ?  275 LEU   A HB3    1 
ATOM   4073  H  HG     . LEU   A 1 250 ? -2.026  -7.732  51.286 1.00 31.44  ?  275 LEU   A HG     1 
ATOM   4074  H  HD11   . LEU   A 1 250 ? -0.205  -6.260  51.597 1.00 32.76  ?  275 LEU   A HD11   1 
ATOM   4075  H  HD12   . LEU   A 1 250 ? -1.572  -5.538  51.964 1.00 32.76  ?  275 LEU   A HD12   1 
ATOM   4076  H  HD13   . LEU   A 1 250 ? -0.625  -6.081  53.119 1.00 32.76  ?  275 LEU   A HD13   1 
ATOM   4077  H  HD21   . LEU   A 1 250 ? 0.109   -8.599  51.893 1.00 32.19  ?  275 LEU   A HD21   1 
ATOM   4078  H  HD22   . LEU   A 1 250 ? -0.426  -8.714  53.384 1.00 32.19  ?  275 LEU   A HD22   1 
ATOM   4079  H  HD23   . LEU   A 1 250 ? -1.099  -9.574  52.230 1.00 32.19  ?  275 LEU   A HD23   1 
ATOM   4080  N  N      . LYS   A 1 251 ? -6.019  -8.765  53.755 1.00 36.76  ?  276 LYS   A N      1 
ATOM   4081  C  CA     . LYS   A 1 251 ? -7.145  -8.602  54.669 1.00 42.38  ?  276 LYS   A CA     1 
ATOM   4082  C  C      . LYS   A 1 251 ? -7.114  -9.653  55.767 1.00 44.88  ?  276 LYS   A C      1 
ATOM   4083  O  O      . LYS   A 1 251 ? -7.112  -10.856 55.495 1.00 45.81  ?  276 LYS   A O      1 
ATOM   4084  C  CB     . LYS   A 1 251 ? -8.456  -8.696  53.884 1.00 44.56  ?  276 LYS   A CB     1 
ATOM   4085  C  CG     . LYS   A 1 251 ? -9.721  -8.612  54.728 1.00 48.01  ?  276 LYS   A CG     1 
ATOM   4086  C  CD     . LYS   A 1 251 ? -10.940 -9.044  53.917 1.00 51.36  ?  276 LYS   A CD     1 
ATOM   4087  C  CE     . LYS   A 1 251 ? -11.027 -10.562 53.807 1.00 54.04  ?  276 LYS   A CE     1 
ATOM   4088  N  NZ     . LYS   A 1 251 ? -11.513 -11.193 55.076 1.00 56.11  ?  276 LYS   A NZ     1 
ATOM   4089  H  H      . LYS   A 1 251 ? -6.246  -8.830  52.928 1.00 44.11  ?  276 LYS   A H      1 
ATOM   4090  H  HA     . LYS   A 1 251 ? -7.093  -7.727  55.085 1.00 50.85  ?  276 LYS   A HA     1 
ATOM   4091  H  HB2    . LYS   A 1 251 ? -8.484  -7.966  53.245 1.00 53.46  ?  276 LYS   A HB2    1 
ATOM   4092  H  HB3    . LYS   A 1 251 ? -8.474  -9.546  53.418 1.00 53.46  ?  276 LYS   A HB3    1 
ATOM   4093  H  HG2    . LYS   A 1 251 ? -9.638  -9.198  55.496 1.00 57.61  ?  276 LYS   A HG2    1 
ATOM   4094  H  HG3    . LYS   A 1 251 ? -9.855  -7.697  55.021 1.00 57.61  ?  276 LYS   A HG3    1 
ATOM   4095  H  HD2    . LYS   A 1 251 ? -11.746 -8.723  54.352 1.00 61.63  ?  276 LYS   A HD2    1 
ATOM   4096  H  HD3    . LYS   A 1 251 ? -10.878 -8.676  53.022 1.00 61.63  ?  276 LYS   A HD3    1 
ATOM   4097  H  HE2    . LYS   A 1 251 ? -11.645 -10.796 53.097 1.00 64.85  ?  276 LYS   A HE2    1 
ATOM   4098  H  HE3    . LYS   A 1 251 ? -10.146 -10.918 53.610 1.00 64.85  ?  276 LYS   A HE3    1 
ATOM   4099  H  HZ1    . LYS   A 1 251 ? -11.552 -12.077 54.982 1.00 67.33  ?  276 LYS   A HZ1    1 
ATOM   4100  H  HZ2    . LYS   A 1 251 ? -10.959 -10.998 55.745 1.00 67.33  ?  276 LYS   A HZ2    1 
ATOM   4101  H  HZ3    . LYS   A 1 251 ? -12.325 -10.888 55.276 1.00 67.33  ?  276 LYS   A HZ3    1 
ATOM   4102  N  N      . ASP   A 1 252 ? -7.087  -9.191  57.012 1.00 47.09  ?  277 ASP   A N      1 
ATOM   4103  C  CA     . ASP   A 1 252 ? -7.153  -10.017 58.208 1.00 49.62  ?  277 ASP   A CA     1 
ATOM   4104  C  C      . ASP   A 1 252 ? -5.928  -10.901 58.414 1.00 48.38  ?  277 ASP   A C      1 
ATOM   4105  O  O      . ASP   A 1 252 ? -5.907  -11.672 59.375 1.00 50.50  ?  277 ASP   A O      1 
ATOM   4106  C  CB     . ASP   A 1 252 ? -8.402  -10.917 58.214 1.00 53.58  ?  277 ASP   A CB     1 
ATOM   4107  C  CG     . ASP   A 1 252 ? -9.702  -10.127 58.138 1.00 56.69  ?  277 ASP   A CG     1 
ATOM   4108  O  OD1    . ASP   A 1 252 ? -9.793  -9.066  58.795 1.00 56.87  ?  277 ASP   A OD1    1 
ATOM   4109  O  OD2    . ASP   A 1 252 ? -10.628 -10.569 57.418 1.00 58.20  ?  277 ASP   A OD2    1 
ATOM   4110  H  H      . ASP   A 1 252 ? -7.026  -8.353  57.195 1.00 56.50  ?  277 ASP   A H      1 
ATOM   4111  H  HA     . ASP   A 1 252 ? -7.197  -9.413  58.966 1.00 59.54  ?  277 ASP   A HA     1 
ATOM   4112  H  HB2    . ASP   A 1 252 ? -8.367  -11.510 57.447 1.00 64.29  ?  277 ASP   A HB2    1 
ATOM   4113  H  HB3    . ASP   A 1 252 ? -8.414  -11.436 59.033 1.00 64.29  ?  277 ASP   A HB3    1 
ATOM   4114  N  N      . LYS   A 1 253 ? -4.908  -10.823 57.566 1.00 45.43  ?  278 LYS   A N      1 
ATOM   4115  C  CA     . LYS   A 1 253 ? -3.713  -11.619 57.813 1.00 44.77  ?  278 LYS   A CA     1 
ATOM   4116  C  C      . LYS   A 1 253 ? -2.991  -11.117 59.062 1.00 43.66  ?  278 LYS   A C      1 
ATOM   4117  O  O      . LYS   A 1 253 ? -2.973  -9.919  59.359 1.00 42.04  ?  278 LYS   A O      1 
ATOM   4118  C  CB     . LYS   A 1 253 ? -2.773  -11.586 56.607 1.00 46.95  ?  278 LYS   A CB     1 
ATOM   4119  C  CG     . LYS   A 1 253 ? -3.210  -12.506 55.467 1.00 49.50  ?  278 LYS   A CG     1 
ATOM   4120  C  CD     . LYS   A 1 253 ? -2.012  -13.078 54.711 1.00 51.13  ?  278 LYS   A CD     1 
ATOM   4121  C  CE     . LYS   A 1 253 ? -2.412  -14.197 53.740 1.00 51.90  ?  278 LYS   A CE     1 
ATOM   4122  N  NZ     . LYS   A 1 253 ? -3.670  -13.933 52.975 1.00 51.96  ?  278 LYS   A NZ     1 
ATOM   4123  H  H      . LYS   A 1 253 ? -4.884  -10.331 56.861 1.00 54.51  ?  278 LYS   A H      1 
ATOM   4124  H  HA     . LYS   A 1 253 ? -3.967  -12.544 57.956 1.00 53.71  ?  278 LYS   A HA     1 
ATOM   4125  H  HB2    . LYS   A 1 253 ? -2.740  -10.681 56.262 1.00 56.33  ?  278 LYS   A HB2    1 
ATOM   4126  H  HB3    . LYS   A 1 253 ? -1.889  -11.866 56.892 1.00 56.33  ?  278 LYS   A HB3    1 
ATOM   4127  H  HG2    . LYS   A 1 253 ? -3.721  -13.247 55.830 1.00 59.39  ?  278 LYS   A HG2    1 
ATOM   4128  H  HG3    . LYS   A 1 253 ? -3.753  -12.004 54.840 1.00 59.39  ?  278 LYS   A HG3    1 
ATOM   4129  H  HD2    . LYS   A 1 253 ? -1.593  -12.369 54.198 1.00 61.35  ?  278 LYS   A HD2    1 
ATOM   4130  H  HD3    . LYS   A 1 253 ? -1.379  -13.444 55.349 1.00 61.35  ?  278 LYS   A HD3    1 
ATOM   4131  H  HE2    . LYS   A 1 253 ? -1.697  -14.318 53.095 1.00 62.27  ?  278 LYS   A HE2    1 
ATOM   4132  H  HE3    . LYS   A 1 253 ? -2.543  -15.014 54.246 1.00 62.27  ?  278 LYS   A HE3    1 
ATOM   4133  H  HZ1    . LYS   A 1 253 ? -4.358  -13.862 53.535 1.00 62.35  ?  278 LYS   A HZ1    1 
ATOM   4134  H  HZ2    . LYS   A 1 253 ? -3.594  -13.175 52.515 1.00 62.35  ?  278 LYS   A HZ2    1 
ATOM   4135  H  HZ3    . LYS   A 1 253 ? -3.828  -14.601 52.408 1.00 62.35  ?  278 LYS   A HZ3    1 
ATOM   4136  N  N      . LEU   A 1 254 ? -2.393  -12.057 59.796 1.00 43.20  ?  279 LEU   A N      1 
ATOM   4137  C  CA     . LEU   A 1 254 ? -1.642  -11.781 61.011 1.00 42.89  ?  279 LEU   A CA     1 
ATOM   4138  C  C      . LEU   A 1 254 ? -0.193  -12.228 60.848 1.00 44.31  ?  279 LEU   A C      1 
ATOM   4139  O  O      . LEU   A 1 254 ? 0.124   -13.076 60.011 1.00 45.66  ?  279 LEU   A O      1 
ATOM   4140  C  CB     . LEU   A 1 254 ? -2.262  -12.511 62.210 1.00 42.18  ?  279 LEU   A CB     1 
ATOM   4141  C  CG     . LEU   A 1 254 ? -3.779  -12.421 62.349 1.00 42.29  ?  279 LEU   A CG     1 
ATOM   4142  C  CD1    . LEU   A 1 254 ? -4.270  -13.359 63.446 1.00 42.07  ?  279 LEU   A CD1    1 
ATOM   4143  C  CD2    . LEU   A 1 254 ? -4.218  -10.992 62.633 1.00 42.95  ?  279 LEU   A CD2    1 
ATOM   4144  H  H      . LEU   A 1 254 ? -2.412  -12.894 59.598 1.00 51.84  ?  279 LEU   A H      1 
ATOM   4145  H  HA     . LEU   A 1 254 ? -1.650  -10.826 61.180 1.00 51.46  ?  279 LEU   A HA     1 
ATOM   4146  H  HB2    . LEU   A 1 254 ? -2.037  -13.452 62.139 1.00 50.61  ?  279 LEU   A HB2    1 
ATOM   4147  H  HB3    . LEU   A 1 254 ? -1.878  -12.139 63.020 1.00 50.61  ?  279 LEU   A HB3    1 
ATOM   4148  H  HG     . LEU   A 1 254 ? -4.185  -12.692 61.510 1.00 50.74  ?  279 LEU   A HG     1 
ATOM   4149  H  HD11   . LEU   A 1 254 ? -5.234  -13.285 63.517 1.00 50.48  ?  279 LEU   A HD11   1 
ATOM   4150  H  HD12   . LEU   A 1 254 ? -4.023  -14.269 63.217 1.00 50.48  ?  279 LEU   A HD12   1 
ATOM   4151  H  HD13   . LEU   A 1 254 ? -3.856  -13.106 64.286 1.00 50.48  ?  279 LEU   A HD13   1 
ATOM   4152  H  HD21   . LEU   A 1 254 ? -5.181  -10.973 62.739 1.00 51.53  ?  279 LEU   A HD21   1 
ATOM   4153  H  HD22   . LEU   A 1 254 ? -3.789  -10.686 63.447 1.00 51.53  ?  279 LEU   A HD22   1 
ATOM   4154  H  HD23   . LEU   A 1 254 ? -3.955  -10.427 61.889 1.00 51.53  ?  279 LEU   A HD23   1 
ATOM   4155  N  N      . ASP   A 1 255 ? 0.692   -11.665 61.669 1.00 44.76  ?  280 ASP   A N      1 
ATOM   4156  C  CA     . ASP   A 1 255 ? 2.051   -12.184 61.740 1.00 47.23  ?  280 ASP   A CA     1 
ATOM   4157  C  C      . ASP   A 1 255 ? 2.089   -13.371 62.708 1.00 49.93  ?  280 ASP   A C      1 
ATOM   4158  O  O      . ASP   A 1 255 ? 1.067   -13.790 63.263 1.00 49.16  ?  280 ASP   A O      1 
ATOM   4159  C  CB     . ASP   A 1 255 ? 3.036   -11.076 62.118 1.00 47.73  ?  280 ASP   A CB     1 
ATOM   4160  C  CG     . ASP   A 1 255 ? 2.788   -10.493 63.495 1.00 48.36  ?  280 ASP   A CG     1 
ATOM   4161  O  OD1    . ASP   A 1 255 ? 2.189   -11.182 64.346 1.00 48.45  ?  280 ASP   A OD1    1 
ATOM   4162  O  OD2    . ASP   A 1 255 ? 3.198   -9.332  63.724 1.00 48.49  ?  280 ASP   A OD2    1 
ATOM   4163  H  H      . ASP   A 1 255 ? 0.531   -10.994 62.183 1.00 53.71  ?  280 ASP   A H      1 
ATOM   4164  H  HA     . ASP   A 1 255 ? 2.324   -12.505 60.866 1.00 56.67  ?  280 ASP   A HA     1 
ATOM   4165  H  HB2    . ASP   A 1 255 ? 3.935   -11.439 62.107 1.00 57.28  ?  280 ASP   A HB2    1 
ATOM   4166  H  HB3    . ASP   A 1 255 ? 2.961   -10.357 61.472 1.00 57.28  ?  280 ASP   A HB3    1 
ATOM   4167  N  N      . GLU   A 1 256 ? 3.280   -13.941 62.907 1.00 53.23  ?  281 GLU   A N      1 
ATOM   4168  C  CA     . GLU   A 1 256 ? 3.381   -15.172 63.684 1.00 56.08  ?  281 GLU   A CA     1 
ATOM   4169  C  C      . GLU   A 1 256 ? 3.005   -14.977 65.146 1.00 56.73  ?  281 GLU   A C      1 
ATOM   4170  O  O      . GLU   A 1 256 ? 2.640   -15.952 65.813 1.00 57.47  ?  281 GLU   A O      1 
ATOM   4171  C  CB     . GLU   A 1 256 ? 4.795   -15.750 63.583 1.00 59.03  ?  281 GLU   A CB     1 
ATOM   4172  C  CG     . GLU   A 1 256 ? 4.902   -16.905 62.595 1.00 61.59  ?  281 GLU   A CG     1 
ATOM   4173  C  CD     . GLU   A 1 256 ? 6.209   -16.916 61.826 1.00 63.90  ?  281 GLU   A CD     1 
ATOM   4174  O  OE1    . GLU   A 1 256 ? 7.261   -16.574 62.409 1.00 65.40  ?  281 GLU   A OE1    1 
ATOM   4175  O  OE2    . GLU   A 1 256 ? 6.177   -17.263 60.628 1.00 64.12  ?  281 GLU   A OE2    1 
ATOM   4176  H  H      . GLU   A 1 256 ? 4.028   -13.639 62.608 1.00 63.87  ?  281 GLU   A H      1 
ATOM   4177  H  HA     . GLU   A 1 256 ? 2.766   -15.820 63.305 1.00 67.29  ?  281 GLU   A HA     1 
ATOM   4178  H  HB2    . GLU   A 1 256 ? 5.400   -15.051 63.291 1.00 70.83  ?  281 GLU   A HB2    1 
ATOM   4179  H  HB3    . GLU   A 1 256 ? 5.063   -16.078 64.456 1.00 70.83  ?  281 GLU   A HB3    1 
ATOM   4180  H  HG2    . GLU   A 1 256 ? 4.836   -17.742 63.082 1.00 73.91  ?  281 GLU   A HG2    1 
ATOM   4181  H  HG3    . GLU   A 1 256 ? 4.179   -16.837 61.952 1.00 73.91  ?  281 GLU   A HG3    1 
ATOM   4182  N  N      . THR   A 1 257 ? 3.082   -13.753 65.659 1.00 56.29  ?  282 THR   A N      1 
ATOM   4183  C  CA     . THR   A 1 257 ? 2.704   -13.470 67.036 1.00 55.72  ?  282 THR   A CA     1 
ATOM   4184  C  C      . THR   A 1 257 ? 1.243   -13.056 67.173 1.00 53.32  ?  282 THR   A C      1 
ATOM   4185  O  O      . THR   A 1 257 ? 0.823   -12.667 68.268 1.00 53.99  ?  282 THR   A O      1 
ATOM   4186  C  CB     . THR   A 1 257 ? 3.610   -12.381 67.614 1.00 58.11  ?  282 THR   A CB     1 
ATOM   4187  O  OG1    . THR   A 1 257 ? 3.450   -11.174 66.860 1.00 59.47  ?  282 THR   A OG1    1 
ATOM   4188  C  CG2    . THR   A 1 257 ? 5.073   -12.819 67.554 1.00 58.30  ?  282 THR   A CG2    1 
ATOM   4189  H  H      . THR   A 1 257 ? 3.354   -13.063 65.223 1.00 67.54  ?  282 THR   A H      1 
ATOM   4190  H  HA     . THR   A 1 257 ? 2.833   -14.275 67.562 1.00 66.86  ?  282 THR   A HA     1 
ATOM   4191  H  HB     . THR   A 1 257 ? 3.373   -12.220 68.541 1.00 69.73  ?  282 THR   A HB     1 
ATOM   4192  H  HG1    . THR   A 1 257 ? 2.646   -10.932 66.875 1.00 71.36  ?  282 THR   A HG1    1 
ATOM   4193  H  HG21   . THR   A 1 257 ? 5.634   -12.162 67.996 1.00 69.96  ?  282 THR   A HG21   1 
ATOM   4194  H  HG22   . THR   A 1 257 ? 5.182   -13.675 67.997 1.00 69.96  ?  282 THR   A HG22   1 
ATOM   4195  H  HG23   . THR   A 1 257 ? 5.356   -12.904 66.630 1.00 69.96  ?  282 THR   A HG23   1 
ATOM   4196  N  N      . GLY   A 1 258 ? 0.463   -13.134 66.098 1.00 50.32  ?  283 GLY   A N      1 
ATOM   4197  C  CA     . GLY   A 1 258 ? -0.956  -12.854 66.157 1.00 47.60  ?  283 GLY   A CA     1 
ATOM   4198  C  C      . GLY   A 1 258 ? -1.352  -11.410 65.956 1.00 46.71  ?  283 GLY   A C      1 
ATOM   4199  O  O      . GLY   A 1 258 ? -2.539  -11.085 66.099 1.00 47.28  ?  283 GLY   A O      1 
ATOM   4200  H  H      . GLY   A 1 258 ? 0.742   -13.350 65.313 1.00 60.37  ?  283 GLY   A H      1 
ATOM   4201  H  HA2    . GLY   A 1 258 ? -1.401  -13.377 65.471 1.00 57.11  ?  283 GLY   A HA2    1 
ATOM   4202  H  HA3    . GLY   A 1 258 ? -1.287  -13.129 67.027 1.00 57.11  ?  283 GLY   A HA3    1 
ATOM   4203  N  N      . ASN   A 1 259 ? -0.402  -10.534 65.638 1.00 45.82  ?  284 ASN   A N      1 
ATOM   4204  C  CA     . ASN   A 1 259 ? -0.684  -9.126  65.405 1.00 46.02  ?  284 ASN   A CA     1 
ATOM   4205  C  C      . ASN   A 1 259 ? -1.053  -8.906  63.944 1.00 43.08  ?  284 ASN   A C      1 
ATOM   4206  O  O      . ASN   A 1 259 ? -0.509  -9.561  63.048 1.00 42.14  ?  284 ASN   A O      1 
ATOM   4207  C  CB     . ASN   A 1 259 ? 0.524   -8.261  65.760 1.00 48.94  ?  284 ASN   A CB     1 
ATOM   4208  C  CG     . ASN   A 1 259 ? 1.124   -8.618  67.100 1.00 52.92  ?  284 ASN   A CG     1 
ATOM   4209  O  OD1    . ASN   A 1 259 ? 2.060   -9.411  67.185 1.00 55.54  ?  284 ASN   A OD1    1 
ATOM   4210  N  ND2    . ASN   A 1 259 ? 0.588   -8.031  68.158 1.00 53.53  ?  284 ASN   A ND2    1 
ATOM   4211  H  H      . ASN   A 1 259 ? 0.429   -10.738 65.550 1.00 54.98  ?  284 ASN   A H      1 
ATOM   4212  H  HA     . ASN   A 1 259 ? -1.429  -8.854  65.963 1.00 55.22  ?  284 ASN   A HA     1 
ATOM   4213  H  HB2    . ASN   A 1 259 ? 1.209   -8.381  65.084 1.00 58.73  ?  284 ASN   A HB2    1 
ATOM   4214  H  HB3    . ASN   A 1 259 ? 0.249   -7.331  65.793 1.00 58.73  ?  284 ASN   A HB3    1 
ATOM   4215  H  HD21   . ASN   A 1 259 ? -0.065  -7.481  68.059 1.00 64.23  ?  284 ASN   A HD21   1 
ATOM   4216  H  HD22   . ASN   A 1 259 ? 0.893   -8.201  68.944 1.00 64.23  ?  284 ASN   A HD22   1 
ATOM   4217  N  N      . SER   A 1 260 ? -1.981  -7.979  63.713 1.00 41.30  ?  285 SER   A N      1 
ATOM   4218  C  CA     . SER   A 1 260 ? -2.386  -7.644  62.355 1.00 40.42  ?  285 SER   A CA     1 
ATOM   4219  C  C      . SER   A 1 260 ? -1.199  -7.100  61.569 1.00 39.46  ?  285 SER   A C      1 
ATOM   4220  O  O      . SER   A 1 260 ? -0.363  -6.367  62.105 1.00 39.88  ?  285 SER   A O      1 
ATOM   4221  C  CB     . SER   A 1 260 ? -3.511  -6.608  62.379 1.00 42.58  ?  285 SER   A CB     1 
ATOM   4222  O  OG     . SER   A 1 260 ? -4.699  -7.139  62.943 1.00 44.87  ?  285 SER   A OG     1 
ATOM   4223  H  H      . SER   A 1 260 ? -2.390  -7.533  64.325 1.00 49.55  ?  285 SER   A H      1 
ATOM   4224  H  HA     . SER   A 1 260 ? -2.714  -8.441  61.911 1.00 48.49  ?  285 SER   A HA     1 
ATOM   4225  H  HB2    . SER   A 1 260 ? -3.226  -5.848  62.909 1.00 51.09  ?  285 SER   A HB2    1 
ATOM   4226  H  HB3    . SER   A 1 260 ? -3.696  -6.327  61.469 1.00 51.09  ?  285 SER   A HB3    1 
ATOM   4227  H  HG     . SER   A 1 260 ? -5.368  -6.728  62.643 1.00 53.84  ?  285 SER   A HG     1 
ATOM   4228  N  N      . LEU   A 1 261 ? -1.121  -7.469  60.291 1.00 38.23  ?  286 LEU   A N      1 
ATOM   4229  C  CA     . LEU   A 1 261 ? -0.109  -6.886  59.421 1.00 38.38  ?  286 LEU   A CA     1 
ATOM   4230  C  C      . LEU   A 1 261 ? -0.357  -5.390  59.248 1.00 38.28  ?  286 LEU   A C      1 
ATOM   4231  O  O      . LEU   A 1 261 ? -1.486  -4.958  59.006 1.00 39.29  ?  286 LEU   A O      1 
ATOM   4232  C  CB     . LEU   A 1 261 ? -0.115  -7.577  58.058 1.00 38.47  ?  286 LEU   A CB     1 
ATOM   4233  C  CG     . LEU   A 1 261 ? 0.385   -9.019  57.967 1.00 38.78  ?  286 LEU   A CG     1 
ATOM   4234  C  CD1    . LEU   A 1 261 ? 0.498   -9.443  56.503 1.00 38.43  ?  286 LEU   A CD1    1 
ATOM   4235  C  CD2    . LEU   A 1 261 ? 1.712   -9.182  58.670 1.00 38.56  ?  286 LEU   A CD2    1 
ATOM   4236  H  H      . LEU   A 1 261 ? -1.636  -8.044  59.911 1.00 45.87  ?  286 LEU   A H      1 
ATOM   4237  H  HA     . LEU   A 1 261 ? 0.766   -7.013  59.821 1.00 46.06  ?  286 LEU   A HA     1 
ATOM   4238  H  HB2    . LEU   A 1 261 ? -1.030  -7.582  57.737 1.00 46.15  ?  286 LEU   A HB2    1 
ATOM   4239  H  HB3    . LEU   A 1 261 ? 0.443   -7.054  57.462 1.00 46.15  ?  286 LEU   A HB3    1 
ATOM   4240  H  HG     . LEU   A 1 261 ? -0.252  -9.601  58.410 1.00 46.52  ?  286 LEU   A HG     1 
ATOM   4241  H  HD11   . LEU   A 1 261 ? 0.814   -10.359 56.462 1.00 46.11  ?  286 LEU   A HD11   1 
ATOM   4242  H  HD12   . LEU   A 1 261 ? -0.376  -9.375  56.086 1.00 46.11  ?  286 LEU   A HD12   1 
ATOM   4243  H  HD13   . LEU   A 1 261 ? 1.125   -8.856  56.052 1.00 46.11  ?  286 LEU   A HD13   1 
ATOM   4244  H  HD21   . LEU   A 1 261 ? 2.080   -10.053 58.452 1.00 46.27  ?  286 LEU   A HD21   1 
ATOM   4245  H  HD22   . LEU   A 1 261 ? 2.316   -8.484  58.371 1.00 46.27  ?  286 LEU   A HD22   1 
ATOM   4246  H  HD23   . LEU   A 1 261 ? 1.574   -9.112  59.627 1.00 46.27  ?  286 LEU   A HD23   1 
ATOM   4247  N  N      . LYS   A 1 262 ? 0.701   -4.598  59.394 1.00 37.33  ?  287 LYS   A N      1 
ATOM   4248  C  CA     . LYS   A 1 262 ? 0.661   -3.171  59.096 1.00 38.20  ?  287 LYS   A CA     1 
ATOM   4249  C  C      . LYS   A 1 262 ? 0.976   -2.978  57.619 1.00 35.40  ?  287 LYS   A C      1 
ATOM   4250  O  O      . LYS   A 1 262 ? 1.950   -3.542  57.113 1.00 36.02  ?  287 LYS   A O      1 
ATOM   4251  C  CB     . LYS   A 1 262 ? 1.654   -2.416  59.977 1.00 42.13  ?  287 LYS   A CB     1 
ATOM   4252  C  CG     . LYS   A 1 262 ? 1.382   -2.624  61.473 1.00 46.02  ?  287 LYS   A CG     1 
ATOM   4253  C  CD     . LYS   A 1 262 ? 2.536   -2.187  62.366 1.00 50.28  ?  287 LYS   A CD     1 
ATOM   4254  C  CE     . LYS   A 1 262 ? 2.581   -0.678  62.542 1.00 53.46  ?  287 LYS   A CE     1 
ATOM   4255  N  NZ     . LYS   A 1 262 ? 3.290   -0.293  63.806 1.00 55.11  ?  287 LYS   A NZ     1 
ATOM   4256  H  H      . LYS   A 1 262 ? 1.469   -4.870  59.669 1.00 44.78  ?  287 LYS   A H      1 
ATOM   4257  H  HA     . LYS   A 1 262 ? -0.220  -2.805  59.274 1.00 45.83  ?  287 LYS   A HA     1 
ATOM   4258  H  HB2    . LYS   A 1 262 ? 2.551   -2.732  59.787 1.00 50.54  ?  287 LYS   A HB2    1 
ATOM   4259  H  HB3    . LYS   A 1 262 ? 1.589   -1.467  59.788 1.00 50.54  ?  287 LYS   A HB3    1 
ATOM   4260  H  HG2    . LYS   A 1 262 ? 0.601   -2.106  61.725 1.00 55.22  ?  287 LYS   A HG2    1 
ATOM   4261  H  HG3    . LYS   A 1 262 ? 1.222   -3.566  61.635 1.00 55.22  ?  287 LYS   A HG3    1 
ATOM   4262  H  HD2    . LYS   A 1 262 ? 2.432   -2.591  63.242 1.00 60.32  ?  287 LYS   A HD2    1 
ATOM   4263  H  HD3    . LYS   A 1 262 ? 3.373   -2.471  61.967 1.00 60.32  ?  287 LYS   A HD3    1 
ATOM   4264  H  HE2    . LYS   A 1 262 ? 3.054   -0.282  61.793 1.00 64.14  ?  287 LYS   A HE2    1 
ATOM   4265  H  HE3    . LYS   A 1 262 ? 1.676   -0.332  62.582 1.00 64.14  ?  287 LYS   A HE3    1 
ATOM   4266  H  HZ1    . LYS   A 1 262 ? 2.872   -0.644  64.509 1.00 66.13  ?  287 LYS   A HZ1    1 
ATOM   4267  H  HZ2    . LYS   A 1 262 ? 4.128   -0.593  63.789 1.00 66.13  ?  287 LYS   A HZ2    1 
ATOM   4268  H  HZ3    . LYS   A 1 262 ? 3.303   0.593   63.891 1.00 66.13  ?  287 LYS   A HZ3    1 
ATOM   4269  N  N      . VAL   A 1 263 ? 0.143   -2.199  56.932 1.00 32.51  ?  288 VAL   A N      1 
ATOM   4270  C  CA     . VAL   A 1 263 ? 0.212   -2.048  55.482 1.00 31.28  ?  288 VAL   A CA     1 
ATOM   4271  C  C      . VAL   A 1 263 ? 0.366   -0.571  55.145 1.00 30.89  ?  288 VAL   A C      1 
ATOM   4272  O  O      . VAL   A 1 263 ? -0.482  0.250   55.522 1.00 32.30  ?  288 VAL   A O      1 
ATOM   4273  C  CB     . VAL   A 1 263 ? -1.034  -2.635  54.798 1.00 32.81  ?  288 VAL   A CB     1 
ATOM   4274  C  CG1    . VAL   A 1 263 ? -0.933  -2.475  53.311 1.00 31.86  ?  288 VAL   A CG1    1 
ATOM   4275  C  CG2    . VAL   A 1 263 ? -1.218  -4.098  55.181 1.00 35.30  ?  288 VAL   A CG2    1 
ATOM   4276  H  H      . VAL   A 1 263 ? -0.486  -1.738  57.293 1.00 39.00  ?  288 VAL   A H      1 
ATOM   4277  H  HA     . VAL   A 1 263 ? 1.001   -2.508  55.156 1.00 37.53  ?  288 VAL   A HA     1 
ATOM   4278  H  HB     . VAL   A 1 263 ? -1.818  -2.151  55.099 1.00 39.36  ?  288 VAL   A HB     1 
ATOM   4279  H  HG11   . VAL   A 1 263 ? -1.181  -3.311  52.887 1.00 38.22  ?  288 VAL   A HG11   1 
ATOM   4280  H  HG12   . VAL   A 1 263 ? -1.534  -1.769  53.028 1.00 38.22  ?  288 VAL   A HG12   1 
ATOM   4281  H  HG13   . VAL   A 1 263 ? -0.020  -2.245  53.080 1.00 38.22  ?  288 VAL   A HG13   1 
ATOM   4282  H  HG21   . VAL   A 1 263 ? -1.987  -4.453  54.709 1.00 42.36  ?  288 VAL   A HG21   1 
ATOM   4283  H  HG22   . VAL   A 1 263 ? -0.421  -4.592  54.933 1.00 42.36  ?  288 VAL   A HG22   1 
ATOM   4284  H  HG23   . VAL   A 1 263 ? -1.361  -4.158  56.138 1.00 42.36  ?  288 VAL   A HG23   1 
ATOM   4285  N  N      . ILE   A 1 264 ? 1.442   -0.248  54.428 1.00 28.58  ?  289 ILE   A N      1 
ATOM   4286  C  CA     . ILE   A 1 264 ? 1.791   1.107   54.022 1.00 30.44  ?  289 ILE   A CA     1 
ATOM   4287  C  C      . ILE   A 1 264 ? 1.516   1.224   52.529 1.00 29.21  ?  289 ILE   A C      1 
ATOM   4288  O  O      . ILE   A 1 264 ? 1.940   0.357   51.760 1.00 27.95  ?  289 ILE   A O      1 
ATOM   4289  C  CB     . ILE   A 1 264 ? 3.274   1.404   54.304 1.00 33.95  ?  289 ILE   A CB     1 
ATOM   4290  C  CG1    . ILE   A 1 264 ? 3.661   0.978   55.721 1.00 37.39  ?  289 ILE   A CG1    1 
ATOM   4291  C  CG2    . ILE   A 1 264 ? 3.591   2.880   54.089 1.00 35.26  ?  289 ILE   A CG2    1 
ATOM   4292  C  CD1    . ILE   A 1 264 ? 2.751   1.526   56.778 1.00 39.99  ?  289 ILE   A CD1    1 
ATOM   4293  H  H      . ILE   A 1 264 ? 2.012   -0.830  54.151 1.00 34.29  ?  289 ILE   A H      1 
ATOM   4294  H  HA     . ILE   A 1 264 ? 1.242   1.745   54.504 1.00 36.52  ?  289 ILE   A HA     1 
ATOM   4295  H  HB     . ILE   A 1 264 ? 3.798   0.883   53.675 1.00 40.74  ?  289 ILE   A HB     1 
ATOM   4296  H  HG12   . ILE   A 1 264 ? 3.631   0.010   55.776 1.00 44.86  ?  289 ILE   A HG12   1 
ATOM   4297  H  HG13   . ILE   A 1 264 ? 4.559   1.293   55.909 1.00 44.86  ?  289 ILE   A HG13   1 
ATOM   4298  H  HG21   . ILE   A 1 264 ? 4.552   3.004   54.114 1.00 42.31  ?  289 ILE   A HG21   1 
ATOM   4299  H  HG22   . ILE   A 1 264 ? 3.245   3.154   53.225 1.00 42.31  ?  289 ILE   A HG22   1 
ATOM   4300  H  HG23   . ILE   A 1 264 ? 3.171   3.399   54.793 1.00 42.31  ?  289 ILE   A HG23   1 
ATOM   4301  H  HD11   . ILE   A 1 264 ? 3.199   1.477   57.637 1.00 47.98  ?  289 ILE   A HD11   1 
ATOM   4302  H  HD12   . ILE   A 1 264 ? 2.542   2.450   56.566 1.00 47.98  ?  289 ILE   A HD12   1 
ATOM   4303  H  HD13   . ILE   A 1 264 ? 1.937   0.999   56.798 1.00 47.98  ?  289 ILE   A HD13   1 
ATOM   4304  N  N      . HIS   A 1 265 ? 0.857   2.309   52.115 1.00 29.71  ?  290 HIS   A N      1 
ATOM   4305  C  CA     . HIS   A 1 265 ? 0.437   2.489   50.732 1.00 29.91  ?  290 HIS   A CA     1 
ATOM   4306  C  C      . HIS   A 1 265 ? 0.765   3.882   50.221 1.00 29.25  ?  290 HIS   A C      1 
ATOM   4307  O  O      . HIS   A 1 265 ? 0.581   4.872   50.932 1.00 31.24  ?  290 HIS   A O      1 
ATOM   4308  C  CB     . HIS   A 1 265 ? -1.081  2.256   50.601 1.00 31.19  ?  290 HIS   A CB     1 
ATOM   4309  C  CG     . HIS   A 1 265 ? -1.661  2.754   49.316 1.00 32.49  ?  290 HIS   A CG     1 
ATOM   4310  N  ND1    . HIS   A 1 265 ? -2.453  3.880   49.240 1.00 35.99  ?  290 HIS   A ND1    1 
ATOM   4311  C  CD2    . HIS   A 1 265 ? -1.559  2.282   48.052 1.00 31.95  ?  290 HIS   A CD2    1 
ATOM   4312  C  CE1    . HIS   A 1 265 ? -2.805  4.085   47.983 1.00 35.67  ?  290 HIS   A CE1    1 
ATOM   4313  N  NE2    . HIS   A 1 265 ? -2.282  3.125   47.243 1.00 33.20  ?  290 HIS   A NE2    1 
ATOM   4314  H  H      . HIS   A 1 265 ? 0.640   2.964   52.629 1.00 35.65  ?  290 HIS   A H      1 
ATOM   4315  H  HA     . HIS   A 1 265 ? 0.925   1.860   50.178 1.00 35.89  ?  290 HIS   A HA     1 
ATOM   4316  H  HB2    . HIS   A 1 265 ? -1.255  1.304   50.654 1.00 37.42  ?  290 HIS   A HB2    1 
ATOM   4317  H  HB3    . HIS   A 1 265 ? -1.530  2.717   51.326 1.00 37.42  ?  290 HIS   A HB3    1 
ATOM   4318  H  HD2    . HIS   A 1 265 ? -1.087  1.528   47.782 1.00 38.33  ?  290 HIS   A HD2    1 
ATOM   4319  H  HE1    . HIS   A 1 265 ? -3.332  4.786   47.672 1.00 42.79  ?  290 HIS   A HE1    1 
ATOM   4320  H  HE2    . HIS   A 1 265 ? -2.378  3.040   46.393 1.00 39.83  ?  290 HIS   A HE2    1 
ATOM   4321  N  N      . GLU   A 1 266 ? 1.222   3.962   48.972 1.00 27.34  ?  291 GLU   A N      1 
ATOM   4322  C  CA     . GLU   A 1 266 ? 1.274   5.253   48.293 1.00 27.92  ?  291 GLU   A CA     1 
ATOM   4323  C  C      . GLU   A 1 266 ? 1.051   5.064   46.797 1.00 26.41  ?  291 GLU   A C      1 
ATOM   4324  O  O      . GLU   A 1 266 ? 1.709   4.235   46.162 1.00 24.81  ?  291 GLU   A O      1 
ATOM   4325  C  CB     . GLU   A 1 266 ? 2.612   5.986   48.537 1.00 29.80  ?  291 GLU   A CB     1 
ATOM   4326  C  CG     . GLU   A 1 266 ? 2.650   7.376   47.852 1.00 31.58  ?  291 GLU   A CG     1 
ATOM   4327  C  CD     . GLU   A 1 266 ? 3.989   8.118   47.929 1.00 33.93  ?  291 GLU   A CD     1 
ATOM   4328  O  OE1    . GLU   A 1 266 ? 4.931   7.649   48.587 1.00 35.62  ?  291 GLU   A OE1    1 
ATOM   4329  O  OE2    . GLU   A 1 266 ? 4.107   9.190   47.303 1.00 35.81  ?  291 GLU   A OE2    1 
ATOM   4330  H  H      . GLU   A 1 266 ? 1.502   3.296   48.506 1.00 32.80  ?  291 GLU   A H      1 
ATOM   4331  H  HA     . GLU   A 1 266 ? 0.555   5.804   48.641 1.00 33.50  ?  291 GLU   A HA     1 
ATOM   4332  H  HB2    . GLU   A 1 266 ? 2.735   6.115   49.491 1.00 35.75  ?  291 GLU   A HB2    1 
ATOM   4333  H  HB3    . GLU   A 1 266 ? 3.338   5.451   48.178 1.00 35.75  ?  291 GLU   A HB3    1 
ATOM   4334  H  HG2    . GLU   A 1 266 ? 2.441   7.258   46.912 1.00 37.89  ?  291 GLU   A HG2    1 
ATOM   4335  H  HG3    . GLU   A 1 266 ? 1.984   7.941   48.272 1.00 37.89  ?  291 GLU   A HG3    1 
ATOM   4336  N  N      . GLN   A 1 267 ? 0.106   5.820   46.247 1.00 26.62  ?  292 GLN   A N      1 
ATOM   4337  C  CA     . GLN   A 1 267 ? 0.015   6.004   44.800 1.00 26.37  ?  292 GLN   A CA     1 
ATOM   4338  C  C      . GLN   A 1 267 ? 0.944   7.179   44.520 1.00 27.06  ?  292 GLN   A C      1 
ATOM   4339  O  O      . GLN   A 1 267 ? 0.594   8.336   44.775 1.00 27.77  ?  292 GLN   A O      1 
ATOM   4340  C  CB     . GLN   A 1 267 ? -1.411  6.255   44.335 1.00 27.33  ?  292 GLN   A CB     1 
ATOM   4341  C  CG     . GLN   A 1 267 ? -1.511  6.271   42.813 1.00 31.06  ?  292 GLN   A CG     1 
ATOM   4342  C  CD     . GLN   A 1 267 ? -2.937  6.297   42.320 1.00 35.62  ?  292 GLN   A CD     1 
ATOM   4343  O  OE1    . GLN   A 1 267 ? -3.295  5.600   41.372 1.00 37.49  ?  292 GLN   A OE1    1 
ATOM   4344  N  NE2    . GLN   A 1 267 ? -3.762  7.110   42.959 1.00 37.83  ?  292 GLN   A NE2    1 
ATOM   4345  H  H      . GLN   A 1 267 ? -0.498  6.240   46.692 1.00 31.94  ?  292 GLN   A H      1 
ATOM   4346  H  HA     . GLN   A 1 267 ? 0.300   5.209   44.322 1.00 31.64  ?  292 GLN   A HA     1 
ATOM   4347  H  HB2    . GLN   A 1 267 ? -1.986  5.550   44.672 1.00 32.79  ?  292 GLN   A HB2    1 
ATOM   4348  H  HB3    . GLN   A 1 267 ? -1.709  7.115   44.670 1.00 32.79  ?  292 GLN   A HB3    1 
ATOM   4349  H  HG2    . GLN   A 1 267 ? -1.064  7.063   42.475 1.00 37.27  ?  292 GLN   A HG2    1 
ATOM   4350  H  HG3    . GLN   A 1 267 ? -1.087  5.474   42.460 1.00 37.27  ?  292 GLN   A HG3    1 
ATOM   4351  H  HE21   . GLN   A 1 267 ? -3.474  7.586   43.614 1.00 45.39  ?  292 GLN   A HE21   1 
ATOM   4352  H  HE22   . GLN   A 1 267 ? -4.586  7.162   42.718 1.00 45.39  ?  292 GLN   A HE22   1 
ATOM   4353  N  N      . VAL   A 1 268 ? 2.160   6.866   44.065 1.00 26.17  ?  293 VAL   A N      1 
ATOM   4354  C  CA     . VAL   A 1 268 ? 3.201   7.878   43.925 1.00 27.52  ?  293 VAL   A CA     1 
ATOM   4355  C  C      . VAL   A 1 268 ? 2.894   8.799   42.754 1.00 27.92  ?  293 VAL   A C      1 
ATOM   4356  O  O      . VAL   A 1 268 ? 3.066   10.024  42.841 1.00 29.75  ?  293 VAL   A O      1 
ATOM   4357  C  CB     . VAL   A 1 268 ? 4.573   7.192   43.765 1.00 29.02  ?  293 VAL   A CB     1 
ATOM   4358  C  CG1    . VAL   A 1 268 ? 5.674   8.227   43.597 1.00 30.52  ?  293 VAL   A CG1    1 
ATOM   4359  C  CG2    . VAL   A 1 268 ? 4.841   6.288   44.954 1.00 29.56  ?  293 VAL   A CG2    1 
ATOM   4360  H  H      . VAL   A 1 268 ? 2.406   6.076   43.832 1.00 31.40  ?  293 VAL   A H      1 
ATOM   4361  H  HA     . VAL   A 1 268 ? 3.222   8.422   44.728 1.00 33.01  ?  293 VAL   A HA     1 
ATOM   4362  H  HB     . VAL   A 1 268 ? 4.567   6.643   42.965 1.00 34.81  ?  293 VAL   A HB     1 
ATOM   4363  H  HG11   . VAL   A 1 268 ? 6.535   7.789   43.689 1.00 36.61  ?  293 VAL   A HG11   1 
ATOM   4364  H  HG12   . VAL   A 1 268 ? 5.599   8.628   42.718 1.00 36.61  ?  293 VAL   A HG12   1 
ATOM   4365  H  HG13   . VAL   A 1 268 ? 5.575   8.908   44.281 1.00 36.61  ?  293 VAL   A HG13   1 
ATOM   4366  H  HG21   . VAL   A 1 268 ? 5.722   5.894   44.859 1.00 35.47  ?  293 VAL   A HG21   1 
ATOM   4367  H  HG22   . VAL   A 1 268 ? 4.801   6.816   45.767 1.00 35.47  ?  293 VAL   A HG22   1 
ATOM   4368  H  HG23   . VAL   A 1 268 ? 4.167   5.591   44.979 1.00 35.47  ?  293 VAL   A HG23   1 
ATOM   4369  N  N      . ASN   A 1 269 ? 2.456   8.228   41.639 1.00 26.62  ?  294 ASN   A N      1 
ATOM   4370  C  CA     . ASN   A 1 269 ? 2.004   9.008   40.498 1.00 26.44  ?  294 ASN   A CA     1 
ATOM   4371  C  C      . ASN   A 1 269 ? 1.169   8.091   39.612 1.00 25.90  ?  294 ASN   A C      1 
ATOM   4372  O  O      . ASN   A 1 269 ? 0.818   6.972   40.002 1.00 26.21  ?  294 ASN   A O      1 
ATOM   4373  C  CB     . ASN   A 1 269 ? 3.191   9.642   39.761 1.00 25.21  ?  294 ASN   A CB     1 
ATOM   4374  C  CG     . ASN   A 1 269 ? 4.239   8.618   39.333 1.00 23.94  ?  294 ASN   A CG     1 
ATOM   4375  O  OD1    . ASN   A 1 269 ? 3.930   7.636   38.662 1.00 23.15  ?  294 ASN   A OD1    1 
ATOM   4376  N  ND2    . ASN   A 1 269 ? 5.486   8.852   39.717 1.00 24.80  ?  294 ASN   A ND2    1 
ATOM   4377  H  H      . ASN   A 1 269 ? 2.411   7.378   41.518 1.00 31.93  ?  294 ASN   A H      1 
ATOM   4378  H  HA     . ASN   A 1 269 ? 1.433   9.730   40.806 1.00 31.72  ?  294 ASN   A HA     1 
ATOM   4379  H  HB2    . ASN   A 1 269 ? 2.866   10.089  38.964 1.00 30.25  ?  294 ASN   A HB2    1 
ATOM   4380  H  HB3    . ASN   A 1 269 ? 3.622   10.283  40.349 1.00 30.25  ?  294 ASN   A HB3    1 
ATOM   4381  H  HD21   . ASN   A 1 269 ? 6.113   8.304   39.500 1.00 29.75  ?  294 ASN   A HD21   1 
ATOM   4382  H  HD22   . ASN   A 1 269 ? 5.668   9.551   40.183 1.00 29.75  ?  294 ASN   A HD22   1 
ATOM   4383  N  N      . HIS   A 1 270 ? 0.838   8.566   38.418 1.00 25.42  ?  295 HIS   A N      1 
ATOM   4384  C  CA     . HIS   A 1 270 ? -0.065  7.819   37.556 1.00 25.19  ?  295 HIS   A CA     1 
ATOM   4385  C  C      . HIS   A 1 270 ? 0.599   6.597   36.931 1.00 23.18  ?  295 HIS   A C      1 
ATOM   4386  O  O      . HIS   A 1 270 ? -0.093  5.806   36.277 1.00 24.94  ?  295 HIS   A O      1 
ATOM   4387  C  CB     . HIS   A 1 270 ? -0.594  8.767   36.482 1.00 27.52  ?  295 HIS   A CB     1 
ATOM   4388  C  CG     . HIS   A 1 270 ? 0.483   9.327   35.616 1.00 28.78  ?  295 HIS   A CG     1 
ATOM   4389  N  ND1    . HIS   A 1 270 ? 1.488   10.135  36.106 1.00 29.86  ?  295 HIS   A ND1    1 
ATOM   4390  C  CD2    . HIS   A 1 270 ? 0.727   9.181   34.293 1.00 28.54  ?  295 HIS   A CD2    1 
ATOM   4391  C  CE1    . HIS   A 1 270 ? 2.304   10.461  35.119 1.00 29.85  ?  295 HIS   A CE1    1 
ATOM   4392  N  NE2    . HIS   A 1 270 ? 1.869   9.892   34.010 1.00 30.47  ?  295 HIS   A NE2    1 
ATOM   4393  H  H      . HIS   A 1 270 ? 1.119   9.309   38.089 1.00 30.50  ?  295 HIS   A H      1 
ATOM   4394  H  HA     . HIS   A 1 270 ? -0.821  7.488   38.065 1.00 30.22  ?  295 HIS   A HA     1 
ATOM   4395  H  HB2    . HIS   A 1 270 ? -1.213  8.283   35.913 1.00 33.02  ?  295 HIS   A HB2    1 
ATOM   4396  H  HB3    . HIS   A 1 270 ? -1.048  9.508   36.912 1.00 33.02  ?  295 HIS   A HB3    1 
ATOM   4397  H  HD2    . HIS   A 1 270 ? 0.217   8.692   33.688 1.00 34.24  ?  295 HIS   A HD2    1 
ATOM   4398  H  HE1    . HIS   A 1 270 ? 3.058   11.000  35.194 1.00 35.82  ?  295 HIS   A HE1    1 
ATOM   4399  H  HE2    . HIS   A 1 270 ? 2.239   9.956   33.236 1.00 36.56  ?  295 HIS   A HE2    1 
ATOM   4400  N  N      . ARG   A 1 271 ? 1.907   6.406   37.138 1.00 19.97  ?  296 ARG   A N      1 
ATOM   4401  C  CA     . ARG   A 1 271 ? 2.618   5.249   36.618 1.00 19.03  ?  296 ARG   A CA     1 
ATOM   4402  C  C      . ARG   A 1 271 ? 3.182   4.338   37.696 1.00 18.71  ?  296 ARG   A C      1 
ATOM   4403  O  O      . ARG   A 1 271 ? 3.725   3.283   37.353 1.00 19.19  ?  296 ARG   A O      1 
ATOM   4404  C  CB     . ARG   A 1 271 ? 3.752   5.697   35.684 1.00 18.24  ?  296 ARG   A CB     1 
ATOM   4405  C  CG     . ARG   A 1 271 ? 3.216   6.284   34.397 1.00 18.66  ?  296 ARG   A CG     1 
ATOM   4406  C  CD     . ARG   A 1 271 ? 4.256   6.355   33.306 1.00 18.58  ?  296 ARG   A CD     1 
ATOM   4407  N  NE     . ARG   A 1 271 ? 3.672   6.725   32.022 1.00 19.73  ?  296 ARG   A NE     1 
ATOM   4408  C  CZ     . ARG   A 1 271 ? 4.380   6.942   30.916 1.00 20.49  ?  296 ARG   A CZ     1 
ATOM   4409  N  NH1    . ARG   A 1 271 ? 5.704   6.823   30.930 1.00 20.22  ?  296 ARG   A NH1    1 
ATOM   4410  N  NH2    . ARG   A 1 271 ? 3.761   7.290   29.798 1.00 21.56  ?  296 ARG   A NH2    1 
ATOM   4411  H  H      . ARG   A 1 271 ? 2.406   6.946   37.585 1.00 23.96  ?  296 ARG   A H      1 
ATOM   4412  H  HA     . ARG   A 1 271 ? 1.992   4.722   36.098 1.00 22.84  ?  296 ARG   A HA     1 
ATOM   4413  H  HB2    . ARG   A 1 271 ? 4.284   6.375   36.130 1.00 21.88  ?  296 ARG   A HB2    1 
ATOM   4414  H  HB3    . ARG   A 1 271 ? 4.306   4.932   35.464 1.00 21.88  ?  296 ARG   A HB3    1 
ATOM   4415  H  HG2    . ARG   A 1 271 ? 2.486   5.731   34.078 1.00 22.38  ?  296 ARG   A HG2    1 
ATOM   4416  H  HG3    . ARG   A 1 271 ? 2.900   7.185   34.568 1.00 22.38  ?  296 ARG   A HG3    1 
ATOM   4417  H  HD2    . ARG   A 1 271 ? 4.921   7.022   33.541 1.00 22.29  ?  296 ARG   A HD2    1 
ATOM   4418  H  HD3    . ARG   A 1 271 ? 4.678   5.487   33.209 1.00 22.29  ?  296 ARG   A HD3    1 
ATOM   4419  H  HE     . ARG   A 1 271 ? 2.817   6.808   31.977 1.00 23.66  ?  296 ARG   A HE     1 
ATOM   4420  H  HH11   . ARG   A 1 271 ? 6.108   6.605   31.657 1.00 24.25  ?  296 ARG   A HH11   1 
ATOM   4421  H  HH12   . ARG   A 1 271 ? 6.156   6.964   30.212 1.00 24.25  ?  296 ARG   A HH12   1 
ATOM   4422  H  HH21   . ARG   A 1 271 ? 2.905   7.376   29.789 1.00 25.87  ?  296 ARG   A HH21   1 
ATOM   4423  H  HH22   . ARG   A 1 271 ? 4.215   7.431   29.081 1.00 25.87  ?  296 ARG   A HH22   1 
ATOM   4424  N  N      . TRP   A 1 272 ? 3.039   4.684   38.979 1.00 19.46  ?  297 TRP   A N      1 
ATOM   4425  C  CA     . TRP   A 1 272 ? 3.597   3.881   40.061 1.00 18.33  ?  297 TRP   A CA     1 
ATOM   4426  C  C      . TRP   A 1 272 ? 2.692   3.865   41.283 1.00 18.06  ?  297 TRP   A C      1 
ATOM   4427  O  O      . TRP   A 1 272 ? 2.306   4.925   41.788 1.00 20.02  ?  297 TRP   A O      1 
ATOM   4428  C  CB     . TRP   A 1 272 ? 4.966   4.425   40.501 1.00 18.47  ?  297 TRP   A CB     1 
ATOM   4429  C  CG     . TRP   A 1 272 ? 6.027   4.334   39.478 1.00 18.16  ?  297 TRP   A CG     1 
ATOM   4430  C  CD1    . TRP   A 1 272 ? 6.262   5.212   38.454 1.00 18.76  ?  297 TRP   A CD1    1 
ATOM   4431  C  CD2    . TRP   A 1 272 ? 7.020   3.310   39.363 1.00 16.48  ?  297 TRP   A CD2    1 
ATOM   4432  N  NE1    . TRP   A 1 272 ? 7.331   4.793   37.707 1.00 18.82  ?  297 TRP   A NE1    1 
ATOM   4433  C  CE2    . TRP   A 1 272 ? 7.810   3.624   38.239 1.00 16.76  ?  297 TRP   A CE2    1 
ATOM   4434  C  CE3    . TRP   A 1 272 ? 7.314   2.151   40.091 1.00 17.61  ?  297 TRP   A CE3    1 
ATOM   4435  C  CZ2    . TRP   A 1 272 ? 8.881   2.837   37.838 1.00 16.92  ?  297 TRP   A CZ2    1 
ATOM   4436  C  CZ3    . TRP   A 1 272 ? 8.385   1.373   39.687 1.00 17.00  ?  297 TRP   A CZ3    1 
ATOM   4437  C  CH2    . TRP   A 1 272 ? 9.153   1.723   38.569 1.00 16.67  ?  297 TRP   A CH2    1 
ATOM   4438  H  H      . TRP   A 1 272 ? 2.618   5.385   39.246 1.00 23.35  ?  297 TRP   A H      1 
ATOM   4439  H  HA     . TRP   A 1 272 ? 3.670   2.972   39.730 1.00 21.99  ?  297 TRP   A HA     1 
ATOM   4440  H  HB2    . TRP   A 1 272 ? 4.865   5.361   40.733 1.00 22.16  ?  297 TRP   A HB2    1 
ATOM   4441  H  HB3    . TRP   A 1 272 ? 5.263   3.921   41.275 1.00 22.16  ?  297 TRP   A HB3    1 
ATOM   4442  H  HD1    . TRP   A 1 272 ? 5.767   5.982   38.289 1.00 22.51  ?  297 TRP   A HD1    1 
ATOM   4443  H  HE1    . TRP   A 1 272 ? 7.650   5.197   37.018 1.00 22.58  ?  297 TRP   A HE1    1 
ATOM   4444  H  HE3    . TRP   A 1 272 ? 6.801   1.909   40.829 1.00 21.13  ?  297 TRP   A HE3    1 
ATOM   4445  H  HZ2    . TRP   A 1 272 ? 9.393   3.062   37.095 1.00 20.30  ?  297 TRP   A HZ2    1 
ATOM   4446  H  HZ3    . TRP   A 1 272 ? 8.599   0.604   40.166 1.00 20.39  ?  297 TRP   A HZ3    1 
ATOM   4447  H  HH2    . TRP   A 1 272 ? 9.867   1.181   38.322 1.00 20.00  ?  297 TRP   A HH2    1 
ATOM   4448  N  N      . GLU   A 1 273 ? 2.427   2.668   41.806 1.00 17.98  ?  298 GLU   A N      1 
ATOM   4449  C  CA     . GLU   A 1 273 ? 1.676   2.488   43.047 1.00 19.04  ?  298 GLU   A CA     1 
ATOM   4450  C  C      . GLU   A 1 273 ? 2.341   1.363   43.831 1.00 18.70  ?  298 GLU   A C      1 
ATOM   4451  O  O      . GLU   A 1 273 ? 2.707   0.327   43.264 1.00 19.56  ?  298 GLU   A O      1 
ATOM   4452  C  CB     . GLU   A 1 273 ? 0.190   2.204   42.759 1.00 22.34  ?  298 GLU   A CB     1 
ATOM   4453  C  CG     . GLU   A 1 273 ? -0.720  2.270   43.982 1.00 24.11  ?  298 GLU   A CG     1 
ATOM   4454  C  CD     . GLU   A 1 273 ? -2.210  2.392   43.630 1.00 26.88  ?  298 GLU   A CD     1 
ATOM   4455  O  OE1    . GLU   A 1 273 ? -2.572  2.396   42.423 1.00 27.19  ?  298 GLU   A OE1    1 
ATOM   4456  O  OE2    . GLU   A 1 273 ? -3.014  2.498   44.588 1.00 30.23  ?  298 GLU   A OE2    1 
ATOM   4457  H  H      . GLU   A 1 273 ? 2.679   1.927   41.450 1.00 21.57  ?  298 GLU   A H      1 
ATOM   4458  H  HA     . GLU   A 1 273 ? 1.699   3.284   43.600 1.00 22.84  ?  298 GLU   A HA     1 
ATOM   4459  H  HB2    . GLU   A 1 273 ? -0.131  2.859   42.120 1.00 26.81  ?  298 GLU   A HB2    1 
ATOM   4460  H  HB3    . GLU   A 1 273 ? 0.114   1.312   42.386 1.00 26.81  ?  298 GLU   A HB3    1 
ATOM   4461  H  HG2    . GLU   A 1 273 ? -0.604  1.460   44.503 1.00 28.93  ?  298 GLU   A HG2    1 
ATOM   4462  H  HG3    . GLU   A 1 273 ? -0.476  3.044   44.513 1.00 28.93  ?  298 GLU   A HG3    1 
ATOM   4463  N  N      . VAL   A 1 274 ? 2.504   1.583   45.141 1.00 19.36  ?  299 VAL   A N      1 
ATOM   4464  C  CA     . VAL   A 1 274 ? 3.306   0.728   46.007 1.00 20.21  ?  299 VAL   A CA     1 
ATOM   4465  C  C      . VAL   A 1 274 ? 2.570   0.434   47.307 1.00 20.82  ?  299 VAL   A C      1 
ATOM   4466  O  O      . VAL   A 1 274 ? 1.963   1.326   47.911 1.00 22.25  ?  299 VAL   A O      1 
ATOM   4467  C  CB     . VAL   A 1 274 ? 4.672   1.390   46.324 1.00 20.79  ?  299 VAL   A CB     1 
ATOM   4468  C  CG1    . VAL   A 1 274 ? 5.503   0.522   47.264 1.00 21.24  ?  299 VAL   A CG1    1 
ATOM   4469  C  CG2    . VAL   A 1 274 ? 5.449   1.664   45.058 1.00 21.70  ?  299 VAL   A CG2    1 
ATOM   4470  H  H      . VAL   A 1 274 ? 2.146   2.244   45.558 1.00 23.23  ?  299 VAL   A H      1 
ATOM   4471  H  HA     . VAL   A 1 274 ? 3.438   -0.118  45.552 1.00 24.24  ?  299 VAL   A HA     1 
ATOM   4472  H  HB     . VAL   A 1 274 ? 4.494   2.234   46.767 1.00 24.94  ?  299 VAL   A HB     1 
ATOM   4473  H  HG11   . VAL   A 1 274 ? 6.417   0.849   47.269 1.00 25.48  ?  299 VAL   A HG11   1 
ATOM   4474  H  HG12   . VAL   A 1 274 ? 5.128   0.575   48.157 1.00 25.48  ?  299 VAL   A HG12   1 
ATOM   4475  H  HG13   . VAL   A 1 274 ? 5.482   -0.395  46.949 1.00 25.48  ?  299 VAL   A HG13   1 
ATOM   4476  H  HG21   . VAL   A 1 274 ? 6.313   2.038   45.293 1.00 26.04  ?  299 VAL   A HG21   1 
ATOM   4477  H  HG22   . VAL   A 1 274 ? 5.568   0.832   44.575 1.00 26.04  ?  299 VAL   A HG22   1 
ATOM   4478  H  HG23   . VAL   A 1 274 ? 4.952   2.295   44.513 1.00 26.04  ?  299 VAL   A HG23   1 
ATOM   4479  N  N      . CYS   A 1 275 ? 2.631   -0.822  47.741 1.00 18.75  ?  300 CYS   A N      1 
ATOM   4480  C  CA     A CYS   A 1 275 ? 2.218   -1.215  49.084 0.74 20.65  ?  300 CYS   A CA     1 
ATOM   4481  C  CA     B CYS   A 1 275 ? 2.227   -1.208  49.087 0.26 20.30  ?  300 CYS   A CA     1 
ATOM   4482  C  C      . CYS   A 1 275 ? 3.344   -2.016  49.727 1.00 21.10  ?  300 CYS   A C      1 
ATOM   4483  O  O      . CYS   A 1 275 ? 4.019   -2.796  49.051 1.00 22.04  ?  300 CYS   A O      1 
ATOM   4484  C  CB     A CYS   A 1 275 ? 0.946   -2.072  49.092 0.74 22.10  ?  300 CYS   A CB     1 
ATOM   4485  C  CB     B CYS   A 1 275 ? 0.940   -2.021  49.059 0.26 20.98  ?  300 CYS   A CB     1 
ATOM   4486  S  SG     A CYS   A 1 275 ? -0.571  -1.239  48.573 0.74 25.05  ?  300 CYS   A SG     1 
ATOM   4487  S  SG     B CYS   A 1 275 ? 0.535   -2.749  50.635 0.26 22.13  ?  300 CYS   A SG     1 
ATOM   4488  H  H      A CYS   A 1 275 ? 2.915   -1.479  47.264 0.74 22.50  ?  300 CYS   A H      1 
ATOM   4489  H  H      B CYS   A 1 275 ? 2.909   -1.481  47.263 0.26 22.50  ?  300 CYS   A H      1 
ATOM   4490  H  HA     A CYS   A 1 275 ? 2.039   -0.412  49.599 0.74 24.77  ?  300 CYS   A HA     1 
ATOM   4491  H  HA     B CYS   A 1 275 ? 2.073   -0.418  49.629 0.26 24.35  ?  300 CYS   A HA     1 
ATOM   4492  H  HB2    A CYS   A 1 275 ? 1.082   -2.821  48.491 0.74 26.51  ?  300 CYS   A HB2    1 
ATOM   4493  H  HB2    B CYS   A 1 275 ? 0.207   -1.440  48.801 0.26 25.16  ?  300 CYS   A HB2    1 
ATOM   4494  H  HB3    A CYS   A 1 275 ? 0.802   -2.394  49.995 0.74 26.51  ?  300 CYS   A HB3    1 
ATOM   4495  H  HB3    B CYS   A 1 275 ? 1.036   -2.739  48.414 0.26 25.16  ?  300 CYS   A HB3    1 
ATOM   4496  H  HG     A CYS   A 1 275 ? -1.485  -2.013  48.642 0.74 30.06  ?  300 CYS   A HG     1 
ATOM   4497  H  HG     B CYS   A 1 275 ? 1.392   -3.534  50.934 0.26 26.55  ?  300 CYS   A HG     1 
ATOM   4498  N  N      . LEU   A 1 276 ? 3.532   -1.840  51.037 1.00 21.70  ?  301 LEU   A N      1 
ATOM   4499  C  CA     . LEU   A 1 276 ? 4.571   -2.543  51.789 1.00 22.77  ?  301 LEU   A CA     1 
ATOM   4500  C  C      . LEU   A 1 276 ? 3.993   -3.126  53.069 1.00 22.65  ?  301 LEU   A C      1 
ATOM   4501  O  O      . LEU   A 1 276 ? 3.268   -2.437  53.794 1.00 22.11  ?  301 LEU   A O      1 
ATOM   4502  C  CB     . LEU   A 1 276 ? 5.736   -1.606  52.133 1.00 24.92  ?  301 LEU   A CB     1 
ATOM   4503  C  CG     . LEU   A 1 276 ? 6.825   -2.150  53.063 1.00 27.42  ?  301 LEU   A CG     1 
ATOM   4504  C  CD1    . LEU   A 1 276 ? 7.669   -3.189  52.343 1.00 28.76  ?  301 LEU   A CD1    1 
ATOM   4505  C  CD2    . LEU   A 1 276 ? 7.670   -1.000  53.592 1.00 29.84  ?  301 LEU   A CD2    1 
ATOM   4506  H  H      . LEU   A 1 276 ? 3.060   -1.308  51.521 1.00 26.04  ?  301 LEU   A H      1 
ATOM   4507  H  HA     . LEU   A 1 276 ? 4.901   -3.277  51.247 1.00 27.32  ?  301 LEU   A HA     1 
ATOM   4508  H  HB2    . LEU   A 1 276 ? 6.172   -1.357  51.303 1.00 29.90  ?  301 LEU   A HB2    1 
ATOM   4509  H  HB3    . LEU   A 1 276 ? 5.367   -0.818  52.562 1.00 29.90  ?  301 LEU   A HB3    1 
ATOM   4510  H  HG     . LEU   A 1 276 ? 6.421   -2.595  53.824 1.00 32.90  ?  301 LEU   A HG     1 
ATOM   4511  H  HD11   . LEU   A 1 276 ? 8.346   -3.523  52.952 1.00 34.51  ?  301 LEU   A HD11   1 
ATOM   4512  H  HD12   . LEU   A 1 276 ? 7.096   -3.917  52.055 1.00 34.51  ?  301 LEU   A HD12   1 
ATOM   4513  H  HD13   . LEU   A 1 276 ? 8.090   -2.776  51.573 1.00 34.51  ?  301 LEU   A HD13   1 
ATOM   4514  H  HD21   . LEU   A 1 276 ? 8.396   -1.360  54.124 1.00 35.81  ?  301 LEU   A HD21   1 
ATOM   4515  H  HD22   . LEU   A 1 276 ? 8.026   -0.498  52.842 1.00 35.81  ?  301 LEU   A HD22   1 
ATOM   4516  H  HD23   . LEU   A 1 276 ? 7.112   -0.425  54.140 1.00 35.81  ?  301 LEU   A HD23   1 
ATOM   4517  N  N      . THR   A 1 277 ? 4.329   -4.375  53.360 1.00 22.96  ?  302 THR   A N      1 
ATOM   4518  C  CA     . THR   A 1 277 ? 4.027   -4.953  54.657 1.00 23.87  ?  302 THR   A CA     1 
ATOM   4519  C  C      . THR   A 1 277 ? 5.166   -5.895  55.029 1.00 24.42  ?  302 THR   A C      1 
ATOM   4520  O  O      . THR   A 1 277 ? 6.203   -5.946  54.368 1.00 24.29  ?  302 THR   A O      1 
ATOM   4521  C  CB     . THR   A 1 277 ? 2.657   -5.646  54.659 1.00 26.25  ?  302 THR   A CB     1 
ATOM   4522  O  OG1    . THR   A 1 277 ? 2.315   -5.983  56.011 1.00 28.55  ?  302 THR   A OG1    1 
ATOM   4523  C  CG2    . THR   A 1 277 ? 2.671   -6.900  53.810 1.00 27.38  ?  302 THR   A CG2    1 
ATOM   4524  H  H      . THR   A 1 277 ? 4.734   -4.908  52.820 1.00 27.55  ?  302 THR   A H      1 
ATOM   4525  H  HA     . THR   A 1 277 ? 3.993   -4.237  55.310 1.00 28.64  ?  302 THR   A HA     1 
ATOM   4526  H  HB     . THR   A 1 277 ? 1.991   -5.050  54.283 1.00 31.50  ?  302 THR   A HB     1 
ATOM   4527  H  HG1    . THR   A 1 277 ? 2.273   -5.287  56.479 1.00 34.25  ?  302 THR   A HG1    1 
ATOM   4528  H  HG21   . THR   A 1 277 ? 1.764   -7.216  53.671 1.00 32.85  ?  302 THR   A HG21   1 
ATOM   4529  H  HG22   . THR   A 1 277 ? 3.075   -6.713  52.949 1.00 32.85  ?  302 THR   A HG22   1 
ATOM   4530  H  HG23   . THR   A 1 277 ? 3.182   -7.595  54.254 1.00 32.85  ?  302 THR   A HG23   1 
ATOM   4531  N  N      . MET   A 1 278 ? 4.997   -6.625  56.124 1.00 26.34  ?  303 MET   A N      1 
ATOM   4532  C  CA     . MET   A 1 278 ? 6.041   -7.524  56.586 1.00 29.57  ?  303 MET   A CA     1 
ATOM   4533  C  C      . MET   A 1 278 ? 5.859   -8.931  56.037 1.00 28.70  ?  303 MET   A C      1 
ATOM   4534  O  O      . MET   A 1 278 ? 4.737   -9.395  55.805 1.00 29.16  ?  303 MET   A O      1 
ATOM   4535  C  CB     . MET   A 1 278 ? 6.072   -7.560  58.115 1.00 35.61  ?  303 MET   A CB     1 
ATOM   4536  C  CG     . MET   A 1 278 ? 7.147   -6.668  58.685 1.00 44.95  ?  303 MET   A CG     1 
ATOM   4537  S  SD     . MET   A 1 278 ? 7.170   -6.658  60.479 1.00 53.23  ?  303 MET   A SD     1 
ATOM   4538  C  CE     . MET   A 1 278 ? 7.160   -8.416  60.850 1.00 53.73  ?  303 MET   A CE     1 
ATOM   4539  H  H      . MET   A 1 278 ? 4.290   -6.616  56.613 1.00 31.60  ?  303 MET   A H      1 
ATOM   4540  H  HA     . MET   A 1 278 ? 6.895   -7.191  56.269 1.00 35.48  ?  303 MET   A HA     1 
ATOM   4541  H  HB2    . MET   A 1 278 ? 5.216   -7.259  58.457 1.00 42.73  ?  303 MET   A HB2    1 
ATOM   4542  H  HB3    . MET   A 1 278 ? 6.246   -8.468  58.408 1.00 42.73  ?  303 MET   A HB3    1 
ATOM   4543  H  HG2    . MET   A 1 278 ? 8.012   -6.980  58.376 1.00 53.93  ?  303 MET   A HG2    1 
ATOM   4544  H  HG3    . MET   A 1 278 ? 6.995   -5.759  58.382 1.00 53.93  ?  303 MET   A HG3    1 
ATOM   4545  H  HE1    . MET   A 1 278 ? 7.360   -8.542  61.791 1.00 64.47  ?  303 MET   A HE1    1 
ATOM   4546  H  HE2    . MET   A 1 278 ? 6.283   -8.777  60.646 1.00 64.47  ?  303 MET   A HE2    1 
ATOM   4547  H  HE3    . MET   A 1 278 ? 7.833   -8.857  60.307 1.00 64.47  ?  303 MET   A HE3    1 
ATOM   4548  N  N      . SER   A 1 279 ? 6.989   -9.598  55.816 1.00 27.51  ?  304 SER   A N      1 
ATOM   4549  C  CA     . SER   A 1 279 ? 7.019   -10.992 55.414 1.00 28.44  ?  304 SER   A CA     1 
ATOM   4550  C  C      . SER   A 1 279 ? 7.654   -11.853 56.496 1.00 30.87  ?  304 SER   A C      1 
ATOM   4551  O  O      . SER   A 1 279 ? 8.599   -11.435 57.168 1.00 32.35  ?  304 SER   A O      1 
ATOM   4552  C  CB     . SER   A 1 279 ? 7.829   -11.195 54.130 1.00 27.40  ?  304 SER   A CB     1 
ATOM   4553  O  OG     . SER   A 1 279 ? 7.920   -12.578 53.816 1.00 26.47  ?  304 SER   A OG     1 
ATOM   4554  H  H      . SER   A 1 279 ? 7.771   -9.250  55.895 1.00 33.01  ?  304 SER   A H      1 
ATOM   4555  H  HA     . SER   A 1 279 ? 6.104   -11.277 55.268 1.00 34.13  ?  304 SER   A HA     1 
ATOM   4556  H  HB2    . SER   A 1 279 ? 7.389   -10.732 53.401 1.00 32.87  ?  304 SER   A HB2    1 
ATOM   4557  H  HB3    . SER   A 1 279 ? 8.722   -10.839 54.259 1.00 32.87  ?  304 SER   A HB3    1 
ATOM   4558  H  HG     . SER   A 1 279 ? 8.363   -12.684 53.110 1.00 31.76  ?  304 SER   A HG     1 
ATOM   4559  N  N      . GLU   A 1 280 ? 7.164   -13.083 56.615 1.00 33.97  ?  305 GLU   A N      1 
ATOM   4560  C  CA     . GLU   A 1 280 ? 7.772   -14.083 57.479 1.00 36.64  ?  305 GLU   A CA     1 
ATOM   4561  C  C      . GLU   A 1 280 ? 8.347   -15.250 56.692 1.00 35.29  ?  305 GLU   A C      1 
ATOM   4562  O  O      . GLU   A 1 280 ? 8.654   -16.294 57.279 1.00 36.75  ?  305 GLU   A O      1 
ATOM   4563  C  CB     . GLU   A 1 280 ? 6.751   -14.566 58.500 1.00 41.14  ?  305 GLU   A CB     1 
ATOM   4564  C  CG     . GLU   A 1 280 ? 6.280   -13.433 59.347 1.00 45.22  ?  305 GLU   A CG     1 
ATOM   4565  C  CD     . GLU   A 1 280 ? 5.348   -13.877 60.420 1.00 48.94  ?  305 GLU   A CD     1 
ATOM   4566  O  OE1    . GLU   A 1 280 ? 4.520   -14.774 60.144 1.00 52.03  ?  305 GLU   A OE1    1 
ATOM   4567  O  OE2    . GLU   A 1 280 ? 5.460   -13.331 61.535 1.00 49.16  ?  305 GLU   A OE2    1 
ATOM   4568  H  H      . GLU   A 1 280 ? 6.467   -13.365 56.198 1.00 40.76  ?  305 GLU   A H      1 
ATOM   4569  H  HA     . GLU   A 1 280 ? 8.509   -13.677 57.962 1.00 43.96  ?  305 GLU   A HA     1 
ATOM   4570  H  HB2    . GLU   A 1 280 ? 5.987   -14.947 58.039 1.00 49.36  ?  305 GLU   A HB2    1 
ATOM   4571  H  HB3    . GLU   A 1 280 ? 7.158   -15.234 59.074 1.00 49.36  ?  305 GLU   A HB3    1 
ATOM   4572  H  HG2    . GLU   A 1 280 ? 7.045   -13.012 59.768 1.00 54.26  ?  305 GLU   A HG2    1 
ATOM   4573  H  HG3    . GLU   A 1 280 ? 5.813   -12.792 58.789 1.00 54.26  ?  305 GLU   A HG3    1 
ATOM   4574  N  N      . LYS   A 1 281 ? 8.514   -15.074 55.367 1.00 33.35  ?  306 LYS   A N      1 
ATOM   4575  C  CA     . LYS   A 1 281 ? 9.013   -16.107 54.469 1.00 33.12  ?  306 LYS   A CA     1 
ATOM   4576  C  C      . LYS   A 1 281 ? 10.223  -15.634 53.668 1.00 28.14  ?  306 LYS   A C      1 
ATOM   4577  O  O      . LYS   A 1 281 ? 10.482  -16.162 52.576 1.00 28.17  ?  306 LYS   A O      1 
ATOM   4578  C  CB     . LYS   A 1 281 ? 7.953   -16.540 53.456 1.00 38.45  ?  306 LYS   A CB     1 
ATOM   4579  C  CG     . LYS   A 1 281 ? 6.545   -16.663 53.939 1.00 43.38  ?  306 LYS   A CG     1 
ATOM   4580  C  CD     . LYS   A 1 281 ? 5.655   -16.815 52.715 1.00 47.05  ?  306 LYS   A CD     1 
ATOM   4581  C  CE     . LYS   A 1 281 ? 4.394   -17.579 53.018 1.00 49.51  ?  306 LYS   A CE     1 
ATOM   4582  N  NZ     . LYS   A 1 281 ? 4.149   -18.521 51.898 1.00 51.17  ?  306 LYS   A NZ     1 
ATOM   4583  H  H      . LYS   A 1 281 ? 8.336   -14.337 54.960 1.00 40.01  ?  306 LYS   A H      1 
ATOM   4584  H  HA     . LYS   A 1 281 ? 9.256   -16.862 55.026 1.00 39.73  ?  306 LYS   A HA     1 
ATOM   4585  H  HB2    . LYS   A 1 281 ? 7.946   -15.889 52.736 1.00 46.13  ?  306 LYS   A HB2    1 
ATOM   4586  H  HB3    . LYS   A 1 281 ? 8.208   -17.411 53.112 1.00 46.13  ?  306 LYS   A HB3    1 
ATOM   4587  H  HG2    . LYS   A 1 281 ? 6.451   -17.446 54.505 1.00 52.05  ?  306 LYS   A HG2    1 
ATOM   4588  H  HG3    . LYS   A 1 281 ? 6.286   -15.867 54.429 1.00 52.05  ?  306 LYS   A HG3    1 
ATOM   4589  H  HD2    . LYS   A 1 281 ? 5.404   -15.935 52.392 1.00 56.46  ?  306 LYS   A HD2    1 
ATOM   4590  H  HD3    . LYS   A 1 281 ? 6.140   -17.295 52.026 1.00 56.46  ?  306 LYS   A HD3    1 
ATOM   4591  H  HE2    . LYS   A 1 281 ? 4.497   -18.081 53.841 1.00 59.41  ?  306 LYS   A HE2    1 
ATOM   4592  H  HE3    . LYS   A 1 281 ? 3.643   -16.969 53.092 1.00 59.41  ?  306 LYS   A HE3    1 
ATOM   4593  H  HZ1    . LYS   A 1 281 ? 3.378   -18.948 52.023 1.00 61.40  ?  306 LYS   A HZ1    1 
ATOM   4594  H  HZ2    . LYS   A 1 281 ? 4.111   -18.076 51.128 1.00 61.40  ?  306 LYS   A HZ2    1 
ATOM   4595  H  HZ3    . LYS   A 1 281 ? 4.807   -19.119 51.854 1.00 61.40  ?  306 LYS   A HZ3    1 
ATOM   4596  N  N      . GLY   A 1 282 ? 10.927  -14.619 54.145 1.00 25.12  ?  307 GLY   A N      1 
ATOM   4597  C  CA     . GLY   A 1 282 ? 11.953  -13.982 53.350 1.00 24.30  ?  307 GLY   A CA     1 
ATOM   4598  C  C      . GLY   A 1 282 ? 11.347  -12.946 52.422 1.00 23.08  ?  307 GLY   A C      1 
ATOM   4599  O  O      . GLY   A 1 282 ? 10.141  -12.703 52.406 1.00 22.92  ?  307 GLY   A O      1 
ATOM   4600  H  H      . GLY   A 1 282 ? 10.827  -14.282 54.930 1.00 30.14  ?  307 GLY   A H      1 
ATOM   4601  H  HA2    . GLY   A 1 282 ? 12.594  -13.544 53.931 1.00 29.15  ?  307 GLY   A HA2    1 
ATOM   4602  H  HA3    . GLY   A 1 282 ? 12.415  -14.648 52.816 1.00 29.15  ?  307 GLY   A HA3    1 
ATOM   4603  N  N      . PHE   A 1 283 ? 12.205  -12.321 51.622 1.00 21.95  ?  308 PHE   A N      1 
ATOM   4604  C  CA     . PHE   A 1 283 ? 11.714  -11.264 50.743 1.00 20.45  ?  308 PHE   A CA     1 
ATOM   4605  C  C      . PHE   A 1 283 ? 10.639  -11.811 49.807 1.00 19.37  ?  308 PHE   A C      1 
ATOM   4606  O  O      . PHE   A 1 283 ? 10.816  -12.865 49.194 1.00 22.44  ?  308 PHE   A O      1 
ATOM   4607  C  CB     . PHE   A 1 283 ? 12.847  -10.654 49.927 1.00 20.70  ?  308 PHE   A CB     1 
ATOM   4608  C  CG     . PHE   A 1 283 ? 12.392  -9.577  48.974 1.00 19.92  ?  308 PHE   A CG     1 
ATOM   4609  C  CD1    . PHE   A 1 283 ? 11.955  -8.353  49.451 1.00 19.93  ?  308 PHE   A CD1    1 
ATOM   4610  C  CD2    . PHE   A 1 283 ? 12.409  -9.783  47.604 1.00 20.70  ?  308 PHE   A CD2    1 
ATOM   4611  C  CE1    . PHE   A 1 283 ? 11.540  -7.353  48.580 1.00 19.81  ?  308 PHE   A CE1    1 
ATOM   4612  C  CE2    . PHE   A 1 283 ? 11.996  -8.784  46.728 1.00 20.60  ?  308 PHE   A CE2    1 
ATOM   4613  C  CZ     . PHE   A 1 283 ? 11.564  -7.570  47.219 1.00 20.17  ?  308 PHE   A CZ     1 
ATOM   4614  H  H      . PHE   A 1 283 ? 13.048  -12.484 51.571 1.00 26.34  ?  308 PHE   A H      1 
ATOM   4615  H  HA     . PHE   A 1 283 ? 11.332  -10.561 51.291 1.00 24.54  ?  308 PHE   A HA     1 
ATOM   4616  H  HB2    . PHE   A 1 283 ? 13.492  -10.259 50.535 1.00 24.83  ?  308 PHE   A HB2    1 
ATOM   4617  H  HB3    . PHE   A 1 283 ? 13.269  -11.354 49.405 1.00 24.83  ?  308 PHE   A HB3    1 
ATOM   4618  H  HD1    . PHE   A 1 283 ? 11.938  -8.197  50.367 1.00 23.91  ?  308 PHE   A HD1    1 
ATOM   4619  H  HD2    . PHE   A 1 283 ? 12.701  -10.599 47.265 1.00 24.83  ?  308 PHE   A HD2    1 
ATOM   4620  H  HE1    . PHE   A 1 283 ? 11.247  -6.537  48.915 1.00 23.77  ?  308 PHE   A HE1    1 
ATOM   4621  H  HE2    . PHE   A 1 283 ? 12.010  -8.936  45.810 1.00 24.71  ?  308 PHE   A HE2    1 
ATOM   4622  H  HZ     . PHE   A 1 283 ? 11.291  -6.900  46.634 1.00 24.20  ?  308 PHE   A HZ     1 
ATOM   4623  N  N      . GLN   A 1 284 ? 9.528   -11.080 49.686 1.00 19.39  ?  309 GLN   A N      1 
ATOM   4624  C  CA     . GLN   A 1 284 ? 8.445   -11.414 48.771 1.00 19.18  ?  309 GLN   A CA     1 
ATOM   4625  C  C      . GLN   A 1 284 ? 8.073   -10.171 47.975 1.00 17.82  ?  309 GLN   A C      1 
ATOM   4626  O  O      . GLN   A 1 284 ? 8.047   -9.070  48.528 1.00 17.94  ?  309 GLN   A O      1 
ATOM   4627  C  CB     . GLN   A 1 284 ? 7.176   -11.880 49.488 1.00 21.63  ?  309 GLN   A CB     1 
ATOM   4628  C  CG     . GLN   A 1 284 ? 7.261   -13.133 50.270 1.00 23.39  ?  309 GLN   A CG     1 
ATOM   4629  C  CD     . GLN   A 1 284 ? 5.894   -13.523 50.769 1.00 25.23  ?  309 GLN   A CD     1 
ATOM   4630  O  OE1    . GLN   A 1 284 ? 5.029   -13.935 49.996 1.00 26.11  ?  309 GLN   A OE1    1 
ATOM   4631  N  NE2    . GLN   A 1 284 ? 5.676   -13.352 52.065 1.00 25.76  ?  309 GLN   A NE2    1 
ATOM   4632  H  H      . GLN   A 1 284 ? 9.378   -10.365 50.140 1.00 23.26  ?  309 GLN   A H      1 
ATOM   4633  H  HA     . GLN   A 1 284 ? 8.756   -12.126 48.191 1.00 23.01  ?  309 GLN   A HA     1 
ATOM   4634  H  HB2    . GLN   A 1 284 ? 6.909   -11.182 50.106 1.00 25.95  ?  309 GLN   A HB2    1 
ATOM   4635  H  HB3    . GLN   A 1 284 ? 6.487   -12.013 48.819 1.00 25.95  ?  309 GLN   A HB3    1 
ATOM   4636  H  HG2    . GLN   A 1 284 ? 7.602   -13.846 49.708 1.00 28.07  ?  309 GLN   A HG2    1 
ATOM   4637  H  HG3    . GLN   A 1 284 ? 7.846   -13.003 51.033 1.00 28.07  ?  309 GLN   A HG3    1 
ATOM   4638  H  HE21   . GLN   A 1 284 ? 6.298   -13.036 52.568 1.00 30.90  ?  309 GLN   A HE21   1 
ATOM   4639  H  HE22   . GLN   A 1 284 ? 4.913   -13.559 52.403 1.00 30.90  ?  309 GLN   A HE22   1 
ATOM   4640  N  N      . GLN   A 1 285 ? 7.734   -10.348 46.700 1.00 16.52  ?  310 GLN   A N      1 
ATOM   4641  C  CA     . GLN   A 1 285 ? 7.286   -9.243  45.860 1.00 15.18  ?  310 GLN   A CA     1 
ATOM   4642  C  C      . GLN   A 1 285 ? 6.169   -9.733  44.950 1.00 16.22  ?  310 GLN   A C      1 
ATOM   4643  O  O      . GLN   A 1 285 ? 6.237   -10.840 44.414 1.00 16.40  ?  310 GLN   A O      1 
ATOM   4644  C  CB     . GLN   A 1 285 ? 8.447   -8.664  45.029 1.00 16.50  ?  310 GLN   A CB     1 
ATOM   4645  C  CG     . GLN   A 1 285 ? 9.069   -9.631  44.017 1.00 16.35  ?  310 GLN   A CG     1 
ATOM   4646  C  CD     . GLN   A 1 285 ? 8.318   -9.667  42.690 1.00 16.32  ?  310 GLN   A CD     1 
ATOM   4647  O  OE1    . GLN   A 1 285 ? 7.525   -8.778  42.380 1.00 17.68  ?  310 GLN   A OE1    1 
ATOM   4648  N  NE2    . GLN   A 1 285 ? 8.569   -10.699 41.907 1.00 16.17  ?  310 GLN   A NE2    1 
ATOM   4649  H  H      . GLN   A 1 285 ? 7.756   -11.107 46.296 1.00 19.81  ?  310 GLN   A H      1 
ATOM   4650  H  HA     . GLN   A 1 285 ? 6.932   -8.528  46.411 1.00 18.21  ?  310 GLN   A HA     1 
ATOM   4651  H  HB2    . GLN   A 1 285 ? 8.116   -7.898  44.533 1.00 19.79  ?  310 GLN   A HB2    1 
ATOM   4652  H  HB3    . GLN   A 1 285 ? 9.150   -8.387  45.636 1.00 19.79  ?  310 GLN   A HB3    1 
ATOM   4653  H  HG2    . GLN   A 1 285 ? 9.981   -9.355  43.837 1.00 19.61  ?  310 GLN   A HG2    1 
ATOM   4654  H  HG3    . GLN   A 1 285 ? 9.060   -10.526 44.390 1.00 19.61  ?  310 GLN   A HG3    1 
ATOM   4655  H  HE21   . GLN   A 1 285 ? 9.129   -11.302 42.156 1.00 19.40  ?  310 GLN   A HE21   1 
ATOM   4656  H  HE22   . GLN   A 1 285 ? 8.173   -10.768 41.147 1.00 19.40  ?  310 GLN   A HE22   1 
ATOM   4657  N  N      . ILE   A 1 286 ? 5.127   -8.916  44.816 1.00 16.28  ?  311 ILE   A N      1 
ATOM   4658  C  CA     . ILE   A 1 286 ? 4.072   -9.090  43.821 1.00 14.92  ?  311 ILE   A CA     1 
ATOM   4659  C  C      . ILE   A 1 286 ? 4.099   -7.819  42.979 1.00 14.80  ?  311 ILE   A C      1 
ATOM   4660  O  O      . ILE   A 1 286 ? 3.956   -6.715  43.522 1.00 16.93  ?  311 ILE   A O      1 
ATOM   4661  C  CB     . ILE   A 1 286 ? 2.694   -9.330  44.465 1.00 17.91  ?  311 ILE   A CB     1 
ATOM   4662  C  CG1    . ILE   A 1 286 ? 2.644   -10.754 45.050 1.00 20.55  ?  311 ILE   A CG1    1 
ATOM   4663  C  CG2    . ILE   A 1 286 ? 1.603   -9.108  43.451 1.00 19.13  ?  311 ILE   A CG2    1 
ATOM   4664  C  CD1    . ILE   A 1 286 ? 1.360   -11.151 45.735 1.00 24.88  ?  311 ILE   A CD1    1 
ATOM   4665  H  H      . ILE   A 1 286 ? 5.004   -8.224  45.312 1.00 19.53  ?  311 ILE   A H      1 
ATOM   4666  H  HA     . ILE   A 1 286 ? 4.247   -9.858  43.254 1.00 17.90  ?  311 ILE   A HA     1 
ATOM   4667  H  HB     . ILE   A 1 286 ? 2.556   -8.698  45.189 1.00 21.49  ?  311 ILE   A HB     1 
ATOM   4668  H  HG12   . ILE   A 1 286 ? 2.787   -11.383 44.326 1.00 24.65  ?  311 ILE   A HG12   1 
ATOM   4669  H  HG13   . ILE   A 1 286 ? 3.354   -10.836 45.706 1.00 24.65  ?  311 ILE   A HG13   1 
ATOM   4670  H  HG21   . ILE   A 1 286 ? 0.770   -9.460  43.801 1.00 22.95  ?  311 ILE   A HG21   1 
ATOM   4671  H  HG22   . ILE   A 1 286 ? 1.516   -8.156  43.285 1.00 22.95  ?  311 ILE   A HG22   1 
ATOM   4672  H  HG23   . ILE   A 1 286 ? 1.838   -9.567  42.630 1.00 22.95  ?  311 ILE   A HG23   1 
ATOM   4673  H  HD11   . ILE   A 1 286 ? 1.504   -11.978 46.222 1.00 29.85  ?  311 ILE   A HD11   1 
ATOM   4674  H  HD12   . ILE   A 1 286 ? 1.099   -10.448 46.350 1.00 29.85  ?  311 ILE   A HD12   1 
ATOM   4675  H  HD13   . ILE   A 1 286 ? 0.670   -11.278 45.065 1.00 29.85  ?  311 ILE   A HD13   1 
ATOM   4676  N  N      . SER   A 1 287 ? 4.350   -7.958  41.676 1.00 13.65  ?  312 SER   A N      1 
ATOM   4677  C  CA     . SER   A 1 287 ? 4.567   -6.773  40.860 1.00 14.16  ?  312 SER   A CA     1 
ATOM   4678  C  C      . SER   A 1 287 ? 4.084   -6.989  39.436 1.00 13.94  ?  312 SER   A C      1 
ATOM   4679  O  O      . SER   A 1 287 ? 3.974   -8.121  38.954 1.00 14.13  ?  312 SER   A O      1 
ATOM   4680  C  CB     . SER   A 1 287 ? 6.049   -6.360  40.856 1.00 14.46  ?  312 SER   A CB     1 
ATOM   4681  O  OG     . SER   A 1 287 ? 6.870   -7.361  40.261 1.00 15.02  ?  312 SER   A OG     1 
ATOM   4682  H  H      . SER   A 1 287 ? 4.399   -8.707  41.258 1.00 16.37  ?  312 SER   A H      1 
ATOM   4683  H  HA     . SER   A 1 287 ? 4.030   -6.055  41.232 1.00 16.99  ?  312 SER   A HA     1 
ATOM   4684  H  HB2    . SER   A 1 287 ? 6.143   -5.537  40.351 1.00 17.35  ?  312 SER   A HB2    1 
ATOM   4685  H  HB3    . SER   A 1 287 ? 6.337   -6.223  41.772 1.00 17.35  ?  312 SER   A HB3    1 
ATOM   4686  H  HG     . SER   A 1 287 ? 6.815   -8.076  40.699 1.00 18.02  ?  312 SER   A HG     1 
ATOM   4687  N  N      . PHE   A 1 288 ? 3.795   -5.862  38.777 1.00 13.92  ?  313 PHE   A N      1 
ATOM   4688  C  CA     . PHE   A 1 288 ? 3.290   -5.799  37.411 1.00 14.00  ?  313 PHE   A CA     1 
ATOM   4689  C  C      . PHE   A 1 288 ? 4.020   -4.690  36.677 1.00 14.00  ?  313 PHE   A C      1 
ATOM   4690  O  O      . PHE   A 1 288 ? 4.246   -3.607  37.232 1.00 15.38  ?  313 PHE   A O      1 
ATOM   4691  C  CB     . PHE   A 1 288 ? 1.758   -5.544  37.387 1.00 15.15  ?  313 PHE   A CB     1 
ATOM   4692  C  CG     . PHE   A 1 288 ? 1.006   -6.547  38.202 1.00 15.05  ?  313 PHE   A CG     1 
ATOM   4693  C  CD1    . PHE   A 1 288 ? 0.618   -7.758  37.645 1.00 15.07  ?  313 PHE   A CD1    1 
ATOM   4694  C  CD2    . PHE   A 1 288 ? 0.779   -6.335  39.549 1.00 16.42  ?  313 PHE   A CD2    1 
ATOM   4695  C  CE1    . PHE   A 1 288 ? -0.009  -8.732  38.412 1.00 15.79  ?  313 PHE   A CE1    1 
ATOM   4696  C  CE2    . PHE   A 1 288 ? 0.147   -7.306  40.322 1.00 16.85  ?  313 PHE   A CE2    1 
ATOM   4697  C  CZ     . PHE   A 1 288 ? -0.243  -8.507  39.743 1.00 16.22  ?  313 PHE   A CZ     1 
ATOM   4698  H  H      . PHE   A 1 288 ? 3.890   -5.080  39.123 1.00 16.69  ?  313 PHE   A H      1 
ATOM   4699  H  HA     . PHE   A 1 288 ? 3.459   -6.636  36.951 1.00 16.79  ?  313 PHE   A HA     1 
ATOM   4700  H  HB2    . PHE   A 1 288 ? 1.576   -4.663  37.749 1.00 18.17  ?  313 PHE   A HB2    1 
ATOM   4701  H  HB3    . PHE   A 1 288 ? 1.441   -5.599  36.472 1.00 18.17  ?  313 PHE   A HB3    1 
ATOM   4702  H  HD1    . PHE   A 1 288 ? 0.782   -7.921  36.744 1.00 18.08  ?  313 PHE   A HD1    1 
ATOM   4703  H  HD2    . PHE   A 1 288 ? 1.050   -5.537  39.942 1.00 19.70  ?  313 PHE   A HD2    1 
ATOM   4704  H  HE1    . PHE   A 1 288 ? -0.270  -9.535  38.023 1.00 18.94  ?  313 PHE   A HE1    1 
ATOM   4705  H  HE2    . PHE   A 1 288 ? -0.014  -7.151  41.224 1.00 20.21  ?  313 PHE   A HE2    1 
ATOM   4706  H  HZ     . PHE   A 1 288 ? -0.662  -9.158  40.258 1.00 19.46  ?  313 PHE   A HZ     1 
ATOM   4707  N  N      . VAL   A 1 289 ? 4.371   -4.966  35.427 1.00 13.65  ?  314 VAL   A N      1 
ATOM   4708  C  CA     . VAL   A 1 289 ? 4.849   -3.965  34.480 1.00 13.57  ?  314 VAL   A CA     1 
ATOM   4709  C  C      . VAL   A 1 289 ? 3.908   -3.995  33.290 1.00 14.18  ?  314 VAL   A C      1 
ATOM   4710  O  O      . VAL   A 1 289 ? 3.796   -5.020  32.606 1.00 15.24  ?  314 VAL   A O      1 
ATOM   4711  C  CB     . VAL   A 1 289 ? 6.296   -4.233  34.037 1.00 14.80  ?  314 VAL   A CB     1 
ATOM   4712  C  CG1    . VAL   A 1 289 ? 6.696   -3.317  32.877 1.00 15.89  ?  314 VAL   A CG1    1 
ATOM   4713  C  CG2    . VAL   A 1 289 ? 7.254   -4.072  35.209 1.00 16.60  ?  314 VAL   A CG2    1 
ATOM   4714  H  H      . VAL   A 1 289 ? 4.339   -5.757  35.091 1.00 16.37  ?  314 VAL   A H      1 
ATOM   4715  H  HA     . VAL   A 1 289 ? 4.820   -3.087  34.890 1.00 16.28  ?  314 VAL   A HA     1 
ATOM   4716  H  HB     . VAL   A 1 289 ? 6.357   -5.148  33.721 1.00 17.75  ?  314 VAL   A HB     1 
ATOM   4717  H  HG11   . VAL   A 1 289 ? 7.660   -3.339  32.776 1.00 19.06  ?  314 VAL   A HG11   1 
ATOM   4718  H  HG12   . VAL   A 1 289 ? 6.270   -3.633  32.065 1.00 19.06  ?  314 VAL   A HG12   1 
ATOM   4719  H  HG13   . VAL   A 1 289 ? 6.403   -2.414  33.074 1.00 19.06  ?  314 VAL   A HG13   1 
ATOM   4720  H  HG21   . VAL   A 1 289 ? 8.156   -4.261  34.909 1.00 19.91  ?  314 VAL   A HG21   1 
ATOM   4721  H  HG22   . VAL   A 1 289 ? 7.199   -3.161  35.539 1.00 19.91  ?  314 VAL   A HG22   1 
ATOM   4722  H  HG23   . VAL   A 1 289 ? 7.002   -4.693  35.910 1.00 19.91  ?  314 VAL   A HG23   1 
ATOM   4723  N  N      . ASN   A 1 290 ? 3.229   -2.883  33.042 1.00 14.37  ?  315 ASN   A N      1 
ATOM   4724  C  CA     . ASN   A 1 290 ? 2.344   -2.781  31.882 1.00 14.89  ?  315 ASN   A CA     1 
ATOM   4725  C  C      . ASN   A 1 290 ? 1.370   -3.957  31.866 1.00 15.31  ?  315 ASN   A C      1 
ATOM   4726  O  O      . ASN   A 1 290 ? 1.093   -4.552  30.825 1.00 16.85  ?  315 ASN   A O      1 
ATOM   4727  C  CB     . ASN   A 1 290 ? 3.165   -2.696  30.590 1.00 15.79  ?  315 ASN   A CB     1 
ATOM   4728  C  CG     . ASN   A 1 290 ? 4.181   -1.551  30.619 1.00 15.17  ?  315 ASN   A CG     1 
ATOM   4729  O  OD1    . ASN   A 1 290 ? 4.200   -0.747  31.564 1.00 16.84  ?  315 ASN   A OD1    1 
ATOM   4730  N  ND2    . ASN   A 1 290 ? 5.041   -1.481  29.591 1.00 15.16  ?  315 ASN   A ND2    1 
ATOM   4731  H  H      . ASN   A 1 290 ? 3.262   -2.174  33.527 1.00 17.24  ?  315 ASN   A H      1 
ATOM   4732  H  HA     . ASN   A 1 290 ? 1.816   -1.969  31.940 1.00 17.86  ?  315 ASN   A HA     1 
ATOM   4733  H  HB2    . ASN   A 1 290 ? 3.650   -3.527  30.466 1.00 18.95  ?  315 ASN   A HB2    1 
ATOM   4734  H  HB3    . ASN   A 1 290 ? 2.565   -2.548  29.842 1.00 18.95  ?  315 ASN   A HB3    1 
ATOM   4735  H  HD21   . ASN   A 1 290 ? 5.630   -0.855  29.564 1.00 18.19  ?  315 ASN   A HD21   1 
ATOM   4736  H  HD22   . ASN   A 1 290 ? 5.004   -2.063  28.958 1.00 18.19  ?  315 ASN   A HD22   1 
ATOM   4737  N  N      . SER   A 1 291 ? 0.861   -4.288  33.059 1.00 16.79  ?  316 SER   A N      1 
ATOM   4738  C  CA     . SER   A 1 291 ? -0.099  -5.349  33.368 1.00 17.85  ?  316 SER   A CA     1 
ATOM   4739  C  C      . SER   A 1 291 ? 0.442   -6.762  33.170 1.00 15.90  ?  316 SER   A C      1 
ATOM   4740  O  O      . SER   A 1 291 ? -0.314  -7.717  33.361 1.00 16.71  ?  316 SER   A O      1 
ATOM   4741  C  CB     . SER   A 1 291 ? -1.422  -5.171  32.604 1.00 20.95  ?  316 SER   A CB     1 
ATOM   4742  O  OG     . SER   A 1 291 ? -2.180  -4.124  33.199 1.00 23.68  ?  316 SER   A OG     1 
ATOM   4743  H  H      . SER   A 1 291 ? 1.082   -3.866  33.775 1.00 20.15  ?  316 SER   A H      1 
ATOM   4744  H  HA     . SER   A 1 291 ? -0.296  -5.278  34.316 1.00 21.42  ?  316 SER   A HA     1 
ATOM   4745  H  HB2    . SER   A 1 291 ? -1.231  -4.944  31.681 1.00 25.13  ?  316 SER   A HB2    1 
ATOM   4746  H  HB3    . SER   A 1 291 ? -1.929  -5.998  32.644 1.00 25.13  ?  316 SER   A HB3    1 
ATOM   4747  H  HG     . SER   A 1 291 ? -2.356  -4.315  33.998 1.00 28.41  ?  316 SER   A HG     1 
ATOM   4748  N  N      . ILE   A 1 292 ? 1.737   -6.926  32.896 1.00 15.12  ?  317 ILE   A N      1 
ATOM   4749  C  CA     . ILE   A 1 292 ? 2.411   -8.226  32.926 1.00 14.48  ?  317 ILE   A CA     1 
ATOM   4750  C  C      . ILE   A 1 292 ? 2.775   -8.577  34.363 1.00 13.56  ?  317 ILE   A C      1 
ATOM   4751  O  O      . ILE   A 1 292 ? 3.344   -7.747  35.073 1.00 14.54  ?  317 ILE   A O      1 
ATOM   4752  C  CB     . ILE   A 1 292 ? 3.696   -8.170  32.079 1.00 15.34  ?  317 ILE   A CB     1 
ATOM   4753  C  CG1    . ILE   A 1 292 ? 3.401   -7.790  30.632 1.00 16.18  ?  317 ILE   A CG1    1 
ATOM   4754  C  CG2    . ILE   A 1 292 ? 4.498   -9.473  32.206 1.00 15.58  ?  317 ILE   A CG2    1 
ATOM   4755  C  CD1    . ILE   A 1 292 ? 4.614   -7.234  29.934 1.00 16.42  ?  317 ILE   A CD1    1 
ATOM   4756  H  H      . ILE   A 1 292 ? 2.264   -6.280  32.682 1.00 18.14  ?  317 ILE   A H      1 
ATOM   4757  H  HA     . ILE   A 1 292 ? 1.806   -8.898  32.577 1.00 17.38  ?  317 ILE   A HA     1 
ATOM   4758  H  HB     . ILE   A 1 292 ? 4.256   -7.460  32.432 1.00 18.41  ?  317 ILE   A HB     1 
ATOM   4759  H  HG12   . ILE   A 1 292 ? 3.108   -8.578  30.149 1.00 19.41  ?  317 ILE   A HG12   1 
ATOM   4760  H  HG13   . ILE   A 1 292 ? 2.706   -7.113  30.616 1.00 19.41  ?  317 ILE   A HG13   1 
ATOM   4761  H  HG21   . ILE   A 1 292 ? 5.146   -9.517  31.485 1.00 18.69  ?  317 ILE   A HG21   1 
ATOM   4762  H  HG22   . ILE   A 1 292 ? 4.955   -9.480  33.062 1.00 18.69  ?  317 ILE   A HG22   1 
ATOM   4763  H  HG23   . ILE   A 1 292 ? 3.889   -10.225 32.151 1.00 18.69  ?  317 ILE   A HG23   1 
ATOM   4764  H  HD11   . ILE   A 1 292 ? 4.376   -7.004  29.022 1.00 19.70  ?  317 ILE   A HD11   1 
ATOM   4765  H  HD12   . ILE   A 1 292 ? 4.916   -6.443  30.407 1.00 19.70  ?  317 ILE   A HD12   1 
ATOM   4766  H  HD13   . ILE   A 1 292 ? 5.314   -7.907  29.933 1.00 19.70  ?  317 ILE   A HD13   1 
ATOM   4767  N  N      . ALA   A 1 293 ? 2.521   -9.818  34.784 1.00 13.55  ?  318 ALA   A N      1 
ATOM   4768  C  CA     . ALA   A 1 293 ? 2.944   -10.265 36.116 1.00 14.23  ?  318 ALA   A CA     1 
ATOM   4769  C  C      . ALA   A 1 293 ? 4.439   -10.597 36.085 1.00 13.98  ?  318 ALA   A C      1 
ATOM   4770  O  O      . ALA   A 1 293 ? 4.844   -11.587 35.473 1.00 15.00  ?  318 ALA   A O      1 
ATOM   4771  C  CB     . ALA   A 1 293 ? 2.130   -11.471 36.576 1.00 15.60  ?  318 ALA   A CB     1 
ATOM   4772  H  H      . ALA   A 1 293 ? 2.109   -10.415 34.322 1.00 16.26  ?  318 ALA   A H      1 
ATOM   4773  H  HA     . ALA   A 1 293 ? 2.798   -9.543  36.747 1.00 17.07  ?  318 ALA   A HA     1 
ATOM   4774  H  HB1    . ALA   A 1 293 ? 2.432   -11.739 37.458 1.00 18.72  ?  318 ALA   A HB1    1 
ATOM   4775  H  HB2    . ALA   A 1 293 ? 1.192   -11.224 36.609 1.00 18.72  ?  318 ALA   A HB2    1 
ATOM   4776  H  HB3    . ALA   A 1 293 ? 2.259   -12.197 35.947 1.00 18.72  ?  318 ALA   A HB3    1 
ATOM   4777  N  N      . THR   A 1 294 ? 5.265   -9.772  36.740 1.00 13.19  ?  319 THR   A N      1 
ATOM   4778  C  CA     . THR   A 1 294 ? 6.722   -9.952  36.717 1.00 13.28  ?  319 THR   A CA     1 
ATOM   4779  C  C      . THR   A 1 294 ? 7.118   -10.792 37.931 1.00 13.88  ?  319 THR   A C      1 
ATOM   4780  O  O      . THR   A 1 294 ? 7.620   -10.306 38.947 1.00 14.56  ?  319 THR   A O      1 
ATOM   4781  C  CB     . THR   A 1 294 ? 7.444   -8.604  36.664 1.00 14.30  ?  319 THR   A CB     1 
ATOM   4782  O  OG1    . THR   A 1 294 ? 6.872   -7.668  37.589 1.00 14.20  ?  319 THR   A OG1    1 
ATOM   4783  C  CG2    . THR   A 1 294 ? 7.348   -8.023  35.260 1.00 14.26  ?  319 THR   A CG2    1 
ATOM   4784  H  H      . THR   A 1 294 ? 5.005   -9.097  37.206 1.00 15.82  ?  319 THR   A H      1 
ATOM   4785  H  HA     . THR   A 1 294 ? 6.973   -10.442 35.918 1.00 15.93  ?  319 THR   A HA     1 
ATOM   4786  H  HB     . THR   A 1 294 ? 8.374   -8.742  36.902 1.00 17.15  ?  319 THR   A HB     1 
ATOM   4787  H  HG1    . THR   A 1 294 ? 6.938   -7.962  38.373 1.00 17.03  ?  319 THR   A HG1    1 
ATOM   4788  H  HG21   . THR   A 1 294 ? 7.787   -7.159  35.227 1.00 17.10  ?  319 THR   A HG21   1 
ATOM   4789  H  HG22   . THR   A 1 294 ? 7.776   -8.617  34.624 1.00 17.10  ?  319 THR   A HG22   1 
ATOM   4790  H  HG23   . THR   A 1 294 ? 6.417   -7.912  35.009 1.00 17.10  ?  319 THR   A HG23   1 
ATOM   4791  N  N      . SER   A 1 295 ? 6.901   -12.104 37.801 1.00 14.13  ?  320 SER   A N      1 
ATOM   4792  C  CA     . SER   A 1 295 ? 7.026   -12.993 38.951 1.00 14.38  ?  320 SER   A CA     1 
ATOM   4793  C  C      . SER   A 1 295 ? 8.470   -13.263 39.353 1.00 14.88  ?  320 SER   A C      1 
ATOM   4794  O  O      . SER   A 1 295 ? 8.690   -13.764 40.459 1.00 17.89  ?  320 SER   A O      1 
ATOM   4795  C  CB     . SER   A 1 295 ? 6.316   -14.324 38.684 1.00 17.44  ?  320 SER   A CB     1 
ATOM   4796  O  OG     . SER   A 1 295 ? 6.733   -14.904 37.475 1.00 19.61  ?  320 SER   A OG     1 
ATOM   4797  H  H      . SER   A 1 295 ? 6.684   -12.495 37.066 1.00 16.95  ?  320 SER   A H      1 
ATOM   4798  H  HA     . SER   A 1 295 ? 6.586   -12.568 39.704 1.00 17.25  ?  320 SER   A HA     1 
ATOM   4799  H  HB2    . SER   A 1 295 ? 6.516   -14.936 39.409 1.00 20.92  ?  320 SER   A HB2    1 
ATOM   4800  H  HB3    . SER   A 1 295 ? 5.360   -14.164 38.639 1.00 20.92  ?  320 SER   A HB3    1 
ATOM   4801  H  HG     . SER   A 1 295 ? 6.519   -14.410 36.830 1.00 23.52  ?  320 SER   A HG     1 
ATOM   4802  N  N      . LYS   A 1 296 ? 9.454   -12.936 38.523 1.00 14.22  ?  321 LYS   A N      1 
ATOM   4803  C  CA     . LYS   A 1 296 ? 10.845  -12.984 38.952 1.00 15.44  ?  321 LYS   A CA     1 
ATOM   4804  C  C      . LYS   A 1 296 ? 11.364  -11.609 39.346 1.00 16.66  ?  321 LYS   A C      1 
ATOM   4805  O  O      . LYS   A 1 296 ? 12.506  -11.499 39.798 1.00 22.03  ?  321 LYS   A O      1 
ATOM   4806  C  CB     . LYS   A 1 296 ? 11.719  -13.611 37.859 1.00 17.61  ?  321 LYS   A CB     1 
ATOM   4807  C  CG     . LYS   A 1 296 ? 11.510  -15.119 37.745 1.00 20.88  ?  321 LYS   A CG     1 
ATOM   4808  C  CD     . LYS   A 1 296 ? 12.284  -15.704 36.573 1.00 26.07  ?  321 LYS   A CD     1 
ATOM   4809  C  CE     . LYS   A 1 296 ? 12.039  -17.192 36.381 1.00 31.56  ?  321 LYS   A CE     1 
ATOM   4810  N  NZ     . LYS   A 1 296 ? 12.314  -17.926 37.621 1.00 35.80  ?  321 LYS   A NZ     1 
ATOM   4811  H  H      . LYS   A 1 296 ? 9.340   -12.684 37.709 1.00 17.06  ?  321 LYS   A H      1 
ATOM   4812  H  HA     . LYS   A 1 296 ? 10.926  -13.561 39.728 1.00 18.52  ?  321 LYS   A HA     1 
ATOM   4813  H  HB2    . LYS   A 1 296 ? 11.497  -13.210 37.005 1.00 21.12  ?  321 LYS   A HB2    1 
ATOM   4814  H  HB3    . LYS   A 1 296 ? 12.653  -13.451 38.068 1.00 21.12  ?  321 LYS   A HB3    1 
ATOM   4815  H  HG2    . LYS   A 1 296 ? 11.818  -15.549 38.558 1.00 25.05  ?  321 LYS   A HG2    1 
ATOM   4816  H  HG3    . LYS   A 1 296 ? 10.567  -15.303 37.609 1.00 25.05  ?  321 LYS   A HG3    1 
ATOM   4817  H  HD2    . LYS   A 1 296 ? 12.015  -15.249 35.759 1.00 31.28  ?  321 LYS   A HD2    1 
ATOM   4818  H  HD3    . LYS   A 1 296 ? 13.233  -15.575 36.727 1.00 31.28  ?  321 LYS   A HD3    1 
ATOM   4819  H  HE2    . LYS   A 1 296 ? 11.112  -17.338 36.135 1.00 37.86  ?  321 LYS   A HE2    1 
ATOM   4820  H  HE3    . LYS   A 1 296 ? 12.624  -17.530 35.685 1.00 37.86  ?  321 LYS   A HE3    1 
ATOM   4821  H  HZ1    . LYS   A 1 296 ? 12.233  -18.801 37.481 1.00 42.96  ?  321 LYS   A HZ1    1 
ATOM   4822  H  HZ2    . LYS   A 1 296 ? 13.142  -17.753 37.899 1.00 42.96  ?  321 LYS   A HZ2    1 
ATOM   4823  H  HZ3    . LYS   A 1 296 ? 11.740  -17.680 38.254 1.00 42.96  ?  321 LYS   A HZ3    1 
ATOM   4824  N  N      . GLY   A 1 297 ? 10.536  -10.573 39.228 1.00 15.44  ?  322 GLY   A N      1 
ATOM   4825  C  CA     . GLY   A 1 297 ? 10.882  -9.239  39.667 1.00 15.18  ?  322 GLY   A CA     1 
ATOM   4826  C  C      . GLY   A 1 297 ? 11.508  -8.411  38.572 1.00 14.88  ?  322 GLY   A C      1 
ATOM   4827  O  O      . GLY   A 1 297 ? 11.066  -8.443  37.419 1.00 15.61  ?  322 GLY   A O      1 
ATOM   4828  H  H      . GLY   A 1 297 ? 9.749   -10.625 38.887 1.00 18.52  ?  322 GLY   A H      1 
ATOM   4829  H  HA2    . GLY   A 1 297 ? 10.081  -8.785  39.972 1.00 18.21  ?  322 GLY   A HA2    1 
ATOM   4830  H  HA3    . GLY   A 1 297 ? 11.511  -9.297  40.403 1.00 18.21  ?  322 GLY   A HA3    1 
ATOM   4831  N  N      . GLY   A 1 298 ? 12.524  -7.649  38.928 1.00 14.90  ?  323 GLY   A N      1 
ATOM   4832  C  CA     . GLY   A 1 298 ? 13.251  -6.845  37.976 1.00 15.97  ?  323 GLY   A CA     1 
ATOM   4833  C  C      . GLY   A 1 298 ? 13.638  -5.521  38.582 1.00 15.86  ?  323 GLY   A C      1 
ATOM   4834  O  O      . GLY   A 1 298 ? 13.468  -5.287  39.780 1.00 16.19  ?  323 GLY   A O      1 
ATOM   4835  H  H      . GLY   A 1 298 ? 12.815  -7.582  39.734 1.00 17.87  ?  323 GLY   A H      1 
ATOM   4836  H  HA2    . GLY   A 1 298 ? 14.056  -7.310  37.701 1.00 19.16  ?  323 GLY   A HA2    1 
ATOM   4837  H  HA3    . GLY   A 1 298 ? 12.698  -6.681  37.195 1.00 19.16  ?  323 GLY   A HA3    1 
ATOM   4838  N  N      . ARG   A 1 299 ? 14.147  -4.629  37.728 1.00 15.85  ?  324 ARG   A N      1 
ATOM   4839  C  CA     . ARG   A 1 299 ? 14.719  -3.384  38.218 1.00 15.66  ?  324 ARG   A CA     1 
ATOM   4840  C  C      . ARG   A 1 299 ? 13.665  -2.422  38.743 1.00 16.13  ?  324 ARG   A C      1 
ATOM   4841  O  O      . ARG   A 1 299 ? 14.006  -1.534  39.529 1.00 17.89  ?  324 ARG   A O      1 
ATOM   4842  C  CB     . ARG   A 1 299 ? 15.545  -2.735  37.109 1.00 17.22  ?  324 ARG   A CB     1 
ATOM   4843  C  CG     . ARG   A 1 299 ? 16.681  -3.655  36.638 1.00 19.73  ?  324 ARG   A CG     1 
ATOM   4844  C  CD     . ARG   A 1 299 ? 17.790  -2.889  35.981 1.00 24.78  ?  324 ARG   A CD     1 
ATOM   4845  N  NE     . ARG   A 1 299 ? 18.788  -3.738  35.340 1.00 27.10  ?  324 ARG   A NE     1 
ATOM   4846  C  CZ     . ARG   A 1 299 ? 19.825  -4.305  35.955 1.00 27.87  ?  324 ARG   A CZ     1 
ATOM   4847  N  NH1    . ARG   A 1 299 ? 20.011  -4.159  37.260 1.00 29.54  ?  324 ARG   A NH1    1 
ATOM   4848  N  NH2    . ARG   A 1 299 ? 20.676  -5.040  35.255 1.00 28.49  ?  324 ARG   A NH2    1 
ATOM   4849  H  H      . ARG   A 1 299 ? 14.170  -4.724  36.874 1.00 19.01  ?  324 ARG   A H      1 
ATOM   4850  H  HA     . ARG   A 1 299 ? 15.315  -3.575  38.959 1.00 18.79  ?  324 ARG   A HA     1 
ATOM   4851  H  HB2    . ARG   A 1 299 ? 14.971  -2.547  36.351 1.00 20.65  ?  324 ARG   A HB2    1 
ATOM   4852  H  HB3    . ARG   A 1 299 ? 15.937  -1.913  37.441 1.00 20.65  ?  324 ARG   A HB3    1 
ATOM   4853  H  HG2    . ARG   A 1 299 ? 17.050  -4.124  37.403 1.00 23.67  ?  324 ARG   A HG2    1 
ATOM   4854  H  HG3    . ARG   A 1 299 ? 16.331  -4.291  35.995 1.00 23.67  ?  324 ARG   A HG3    1 
ATOM   4855  H  HD2    . ARG   A 1 299 ? 17.410  -2.313  35.300 1.00 29.73  ?  324 ARG   A HD2    1 
ATOM   4856  H  HD3    . ARG   A 1 299 ? 18.242  -2.355  36.653 1.00 29.73  ?  324 ARG   A HD3    1 
ATOM   4857  H  HE     . ARG   A 1 299 ? 18.701  -3.884  34.497 1.00 32.51  ?  324 ARG   A HE     1 
ATOM   4858  H  HH11   . ARG   A 1 299 ? 19.458  -3.692  37.723 1.00 35.44  ?  324 ARG   A HH11   1 
ATOM   4859  H  HH12   . ARG   A 1 299 ? 20.685  -4.532  37.642 1.00 35.44  ?  324 ARG   A HH12   1 
ATOM   4860  H  HH21   . ARG   A 1 299 ? 20.558  -5.148  34.411 1.00 34.18  ?  324 ARG   A HH21   1 
ATOM   4861  H  HH22   . ARG   A 1 299 ? 21.348  -5.409  35.646 1.00 34.18  ?  324 ARG   A HH22   1 
ATOM   4862  N  N      . HIS   A 1 300 ? 12.396  -2.586  38.350 1.00 15.84  ?  325 HIS   A N      1 
ATOM   4863  C  CA     . HIS   A 1 300 ? 11.333  -1.778  38.941 1.00 15.74  ?  325 HIS   A CA     1 
ATOM   4864  C  C      . HIS   A 1 300 ? 11.128  -2.142  40.410 1.00 16.50  ?  325 HIS   A C      1 
ATOM   4865  O  O      . HIS   A 1 300 ? 10.915  -1.256  41.249 1.00 18.54  ?  325 HIS   A O      1 
ATOM   4866  C  CB     . HIS   A 1 300 ? 10.030  -1.938  38.147 1.00 16.07  ?  325 HIS   A CB     1 
ATOM   4867  C  CG     . HIS   A 1 300 ? 9.530   -3.349  38.071 1.00 15.64  ?  325 HIS   A CG     1 
ATOM   4868  N  ND1    . HIS   A 1 300 ? 10.311  -4.386  37.610 1.00 15.31  ?  325 HIS   A ND1    1 
ATOM   4869  C  CD2    . HIS   A 1 300 ? 8.326   -3.894  38.375 1.00 15.87  ?  325 HIS   A CD2    1 
ATOM   4870  C  CE1    . HIS   A 1 300 ? 9.619   -5.512  37.651 1.00 14.86  ?  325 HIS   A CE1    1 
ATOM   4871  N  NE2    . HIS   A 1 300 ? 8.413   -5.242  38.118 1.00 14.96  ?  325 HIS   A NE2    1 
ATOM   4872  H  H      . HIS   A 1 300 ? 12.132  -3.149  37.755 1.00 19.00  ?  325 HIS   A H      1 
ATOM   4873  H  HA     . HIS   A 1 300 ? 11.586  -0.843  38.893 1.00 18.88  ?  325 HIS   A HA     1 
ATOM   4874  H  HB2    . HIS   A 1 300 ? 9.341   -1.403  38.571 1.00 19.28  ?  325 HIS   A HB2    1 
ATOM   4875  H  HB3    . HIS   A 1 300 ? 10.179  -1.629  37.240 1.00 19.28  ?  325 HIS   A HB3    1 
ATOM   4876  H  HD2    . HIS   A 1 300 ? 7.581   -3.440  38.697 1.00 19.04  ?  325 HIS   A HD2    1 
ATOM   4877  H  HE1    . HIS   A 1 300 ? 9.928   -6.351  37.395 1.00 17.82  ?  325 HIS   A HE1    1 
ATOM   4878  H  HE2    . HIS   A 1 300 ? 7.784   -5.816  38.241 1.00 17.95  ?  325 HIS   A HE2    1 
ATOM   4879  N  N      . VAL   A 1 301 ? 11.194  -3.433  40.747 1.00 15.75  ?  326 VAL   A N      1 
ATOM   4880  C  CA     . VAL   A 1 301 ? 11.105  -3.831  42.151 1.00 16.06  ?  326 VAL   A CA     1 
ATOM   4881  C  C      . VAL   A 1 301 ? 12.352  -3.380  42.909 1.00 16.95  ?  326 VAL   A C      1 
ATOM   4882  O  O      . VAL   A 1 301 ? 12.253  -2.825  44.009 1.00 19.78  ?  326 VAL   A O      1 
ATOM   4883  C  CB     . VAL   A 1 301 ? 10.883  -5.352  42.283 1.00 16.25  ?  326 VAL   A CB     1 
ATOM   4884  C  CG1    . VAL   A 1 301 ? 10.853  -5.772  43.770 1.00 19.25  ?  326 VAL   A CG1    1 
ATOM   4885  C  CG2    . VAL   A 1 301 ? 9.609   -5.773  41.597 1.00 17.99  ?  326 VAL   A CG2    1 
ATOM   4886  H  H      . VAL   A 1 301 ? 11.289  -4.084  40.192 1.00 18.90  ?  326 VAL   A H      1 
ATOM   4887  H  HA     . VAL   A 1 301 ? 10.335  -3.390  42.541 1.00 19.27  ?  326 VAL   A HA     1 
ATOM   4888  H  HB     . VAL   A 1 301 ? 11.623  -5.806  41.850 1.00 19.49  ?  326 VAL   A HB     1 
ATOM   4889  H  HG11   . VAL   A 1 301 ? 10.542  -6.689  43.833 1.00 23.09  ?  326 VAL   A HG11   1 
ATOM   4890  H  HG12   . VAL   A 1 301 ? 11.748  -5.701  44.136 1.00 23.09  ?  326 VAL   A HG12   1 
ATOM   4891  H  HG13   . VAL   A 1 301 ? 10.251  -5.185  44.252 1.00 23.09  ?  326 VAL   A HG13   1 
ATOM   4892  H  HG21   . VAL   A 1 301 ? 9.484   -6.727  41.720 1.00 21.58  ?  326 VAL   A HG21   1 
ATOM   4893  H  HG22   . VAL   A 1 301 ? 8.865   -5.289  41.988 1.00 21.58  ?  326 VAL   A HG22   1 
ATOM   4894  H  HG23   . VAL   A 1 301 ? 9.676   -5.567  40.651 1.00 21.58  ?  326 VAL   A HG23   1 
ATOM   4895  N  N      . ASP   A 1 302 ? 13.546  -3.609  42.336 1.00 18.35  ?  327 ASP   A N      1 
ATOM   4896  C  CA     . ASP   A 1 302 ? 14.777  -3.185  43.001 1.00 20.07  ?  327 ASP   A CA     1 
ATOM   4897  C  C      . ASP   A 1 302 ? 14.750  -1.687  43.305 1.00 20.23  ?  327 ASP   A C      1 
ATOM   4898  O  O      . ASP   A 1 302 ? 15.141  -1.247  44.396 1.00 22.75  ?  327 ASP   A O      1 
ATOM   4899  C  CB     . ASP   A 1 302 ? 16.011  -3.470  42.129 1.00 19.90  ?  327 ASP   A CB     1 
ATOM   4900  C  CG     . ASP   A 1 302 ? 16.178  -4.942  41.736 1.00 22.37  ?  327 ASP   A CG     1 
ATOM   4901  O  OD1    . ASP   A 1 302 ? 15.588  -5.832  42.389 1.00 23.24  ?  327 ASP   A OD1    1 
ATOM   4902  O  OD2    . ASP   A 1 302 ? 16.942  -5.200  40.770 1.00 23.67  ?  327 ASP   A OD2    1 
ATOM   4903  H  H      . ASP   A 1 302 ? 13.662  -4.000  41.579 1.00 22.01  ?  327 ASP   A H      1 
ATOM   4904  H  HA     . ASP   A 1 302 ? 14.849  -3.695  43.823 1.00 24.08  ?  327 ASP   A HA     1 
ATOM   4905  H  HB2    . ASP   A 1 302 ? 15.937  -2.954  41.310 1.00 23.87  ?  327 ASP   A HB2    1 
ATOM   4906  H  HB3    . ASP   A 1 302 ? 16.805  -3.204  42.618 1.00 23.87  ?  327 ASP   A HB3    1 
ATOM   4907  N  N      . TYR   A 1 303 ? 14.318  -0.895  42.324 1.00 18.97  ?  328 TYR   A N      1 
ATOM   4908  C  CA     . TYR   A 1 303 ? 14.290  0.561   42.437 1.00 21.23  ?  328 TYR   A CA     1 
ATOM   4909  C  C      . TYR   A 1 303 ? 13.446  1.021   43.617 1.00 21.47  ?  328 TYR   A C      1 
ATOM   4910  O  O      . TYR   A 1 303 ? 13.851  1.918   44.364 1.00 23.97  ?  328 TYR   A O      1 
ATOM   4911  C  CB     . TYR   A 1 303 ? 13.774  1.122   41.099 1.00 22.18  ?  328 TYR   A CB     1 
ATOM   4912  C  CG     . TYR   A 1 303 ? 13.529  2.616   40.989 1.00 23.08  ?  328 TYR   A CG     1 
ATOM   4913  C  CD1    . TYR   A 1 303 ? 14.551  3.545   41.177 1.00 25.44  ?  328 TYR   A CD1    1 
ATOM   4914  C  CD2    . TYR   A 1 303 ? 12.278  3.090   40.614 1.00 24.01  ?  328 TYR   A CD2    1 
ATOM   4915  C  CE1    . TYR   A 1 303 ? 14.306  4.902   41.053 1.00 25.10  ?  328 TYR   A CE1    1 
ATOM   4916  C  CE2    . TYR   A 1 303 ? 12.030  4.433   40.476 1.00 25.11  ?  328 TYR   A CE2    1 
ATOM   4917  C  CZ     . TYR   A 1 303 ? 13.040  5.338   40.701 1.00 25.77  ?  328 TYR   A CZ     1 
ATOM   4918  O  OH     . TYR   A 1 303 ? 12.761  6.677   40.556 1.00 29.02  ?  328 TYR   A OH     1 
ATOM   4919  H  H      . TYR   A 1 303 ? 14.028  -1.182  41.567 1.00 22.76  ?  328 TYR   A H      1 
ATOM   4920  H  HA     . TYR   A 1 303 ? 15.182  0.906   42.601 1.00 25.47  ?  328 TYR   A HA     1 
ATOM   4921  H  HB2    . TYR   A 1 303 ? 14.426  0.898   40.416 1.00 26.62  ?  328 TYR   A HB2    1 
ATOM   4922  H  HB3    . TYR   A 1 303 ? 12.929  0.688   40.906 1.00 26.62  ?  328 TYR   A HB3    1 
ATOM   4923  H  HD1    . TYR   A 1 303 ? 15.407  3.249   41.388 1.00 30.52  ?  328 TYR   A HD1    1 
ATOM   4924  H  HD2    . TYR   A 1 303 ? 11.593  2.482   40.452 1.00 28.80  ?  328 TYR   A HD2    1 
ATOM   4925  H  HE1    . TYR   A 1 303 ? 14.988  5.516   41.204 1.00 30.11  ?  328 TYR   A HE1    1 
ATOM   4926  H  HE2    . TYR   A 1 303 ? 11.183  4.729   40.231 1.00 30.13  ?  328 TYR   A HE2    1 
ATOM   4927  H  HH     . TYR   A 1 303 ? 13.448  7.132   40.717 1.00 34.81  ?  328 TYR   A HH     1 
ATOM   4928  N  N      . VAL   A 1 304 ? 12.264  0.426   43.798 1.00 20.87  ?  329 VAL   A N      1 
ATOM   4929  C  CA     . VAL   A 1 304 ? 11.393  0.797   44.912 1.00 22.32  ?  329 VAL   A CA     1 
ATOM   4930  C  C      . VAL   A 1 304 ? 11.906  0.207   46.222 1.00 22.88  ?  329 VAL   A C      1 
ATOM   4931  O  O      . VAL   A 1 304 ? 12.028  0.909   47.236 1.00 22.83  ?  329 VAL   A O      1 
ATOM   4932  C  CB     . VAL   A 1 304 ? 9.948   0.342   44.618 1.00 22.57  ?  329 VAL   A CB     1 
ATOM   4933  C  CG1    . VAL   A 1 304 ? 9.048   0.611   45.816 1.00 25.42  ?  329 VAL   A CG1    1 
ATOM   4934  C  CG2    . VAL   A 1 304 ? 9.417   1.015   43.354 1.00 24.64  ?  329 VAL   A CG2    1 
ATOM   4935  H  H      . VAL   A 1 304 ? 11.946  -0.193  43.293 1.00 25.04  ?  329 VAL   A H      1 
ATOM   4936  H  HA     . VAL   A 1 304 ? 11.399  1.762   45.001 1.00 26.78  ?  329 VAL   A HA     1 
ATOM   4937  H  HB     . VAL   A 1 304 ? 9.945   -0.615  44.460 1.00 27.08  ?  329 VAL   A HB     1 
ATOM   4938  H  HG11   . VAL   A 1 304 ? 8.130   0.415   45.571 1.00 30.50  ?  329 VAL   A HG11   1 
ATOM   4939  H  HG12   . VAL   A 1 304 ? 9.323   0.042   46.551 1.00 30.50  ?  329 VAL   A HG12   1 
ATOM   4940  H  HG13   . VAL   A 1 304 ? 9.131   1.543   46.070 1.00 30.50  ?  329 VAL   A HG13   1 
ATOM   4941  H  HG21   . VAL   A 1 304 ? 8.492   0.754   43.223 1.00 29.57  ?  329 VAL   A HG21   1 
ATOM   4942  H  HG22   . VAL   A 1 304 ? 9.477   1.977   43.459 1.00 29.57  ?  329 VAL   A HG22   1 
ATOM   4943  H  HG23   . VAL   A 1 304 ? 9.952   0.731   42.597 1.00 29.57  ?  329 VAL   A HG23   1 
ATOM   4944  N  N      . ALA   A 1 305 ? 12.222  -1.089  46.221 1.00 22.56  ?  330 ALA   A N      1 
ATOM   4945  C  CA     . ALA   A 1 305 ? 12.600  -1.759  47.461 1.00 23.34  ?  330 ALA   A CA     1 
ATOM   4946  C  C      . ALA   A 1 305 ? 13.893  -1.195  48.031 1.00 25.31  ?  330 ALA   A C      1 
ATOM   4947  O  O      . ALA   A 1 305 ? 14.038  -1.076  49.253 1.00 26.14  ?  330 ALA   A O      1 
ATOM   4948  C  CB     . ALA   A 1 305 ? 12.745  -3.265  47.223 1.00 23.52  ?  330 ALA   A CB     1 
ATOM   4949  H  H      . ALA   A 1 305 ? 12.226  -1.595  45.526 1.00 27.06  ?  330 ALA   A H      1 
ATOM   4950  H  HA     . ALA   A 1 305 ? 11.895  -1.617  48.111 1.00 28.01  ?  330 ALA   A HA     1 
ATOM   4951  H  HB1    . ALA   A 1 305 ? 12.998  -3.693  48.056 1.00 28.21  ?  330 ALA   A HB1    1 
ATOM   4952  H  HB2    . ALA   A 1 305 ? 11.896  -3.618  46.914 1.00 28.21  ?  330 ALA   A HB2    1 
ATOM   4953  H  HB3    . ALA   A 1 305 ? 13.429  -3.414  46.553 1.00 28.21  ?  330 ALA   A HB3    1 
ATOM   4954  N  N      . ASP   A 1 306 ? 14.854  -0.868  47.161 1.00 26.31  ?  331 ASP   A N      1 
ATOM   4955  C  CA     . ASP   A 1 306 ? 16.142  -0.367  47.631 1.00 29.20  ?  331 ASP   A CA     1 
ATOM   4956  C  C      . ASP   A 1 306 ? 16.027  0.993   48.301 1.00 29.19  ?  331 ASP   A C      1 
ATOM   4957  O  O      . ASP   A 1 306 ? 16.818  1.296   49.204 1.00 30.57  ?  331 ASP   A O      1 
ATOM   4958  C  CB     . ASP   A 1 306 ? 17.128  -0.294  46.470 1.00 33.57  ?  331 ASP   A CB     1 
ATOM   4959  C  CG     . ASP   A 1 306 ? 17.553  -1.662  45.994 1.00 38.93  ?  331 ASP   A CG     1 
ATOM   4960  O  OD1    . ASP   A 1 306 ? 17.182  -2.660  46.651 1.00 40.62  ?  331 ASP   A OD1    1 
ATOM   4961  O  OD2    . ASP   A 1 306 ? 18.256  -1.740  44.968 1.00 41.55  ?  331 ASP   A OD2    1 
ATOM   4962  H  H      . ASP   A 1 306 ? 14.785  -0.927  46.306 1.00 31.57  ?  331 ASP   A H      1 
ATOM   4963  H  HA     . ASP   A 1 306 ? 16.486  -0.990  48.290 1.00 35.03  ?  331 ASP   A HA     1 
ATOM   4964  H  HB2    . ASP   A 1 306 ? 16.710  0.168   45.727 1.00 40.27  ?  331 ASP   A HB2    1 
ATOM   4965  H  HB3    . ASP   A 1 306 ? 17.921  0.187   46.756 1.00 40.27  ?  331 ASP   A HB3    1 
ATOM   4966  N  N      . GLN   A 1 307 ? 15.076  1.832   47.871 1.00 28.07  ?  332 GLN   A N      1 
ATOM   4967  C  CA     . GLN   A 1 307 ? 14.854  3.084   48.582 1.00 30.80  ?  332 GLN   A CA     1 
ATOM   4968  C  C      . GLN   A 1 307 ? 14.471  2.807   50.023 1.00 31.53  ?  332 GLN   A C      1 
ATOM   4969  O  O      . GLN   A 1 307 ? 14.924  3.492   50.948 1.00 33.12  ?  332 GLN   A O      1 
ATOM   4970  C  CB     . GLN   A 1 307 ? 13.729  3.896   47.951 1.00 31.37  ?  332 GLN   A CB     1 
ATOM   4971  C  CG     . GLN   A 1 307 ? 14.008  4.529   46.641 1.00 32.06  ?  332 GLN   A CG     1 
ATOM   4972  C  CD     . GLN   A 1 307 ? 12.763  5.179   46.090 1.00 31.13  ?  332 GLN   A CD     1 
ATOM   4973  O  OE1    . GLN   A 1 307 ? 12.157  6.039   46.739 1.00 32.35  ?  332 GLN   A OE1    1 
ATOM   4974  N  NE2    . GLN   A 1 307 ? 12.349  4.750   44.902 1.00 29.53  ?  332 GLN   A NE2    1 
ATOM   4975  H  H      . GLN   A 1 307 ? 14.565  1.699   47.192 1.00 33.68  ?  332 GLN   A H      1 
ATOM   4976  H  HA     . GLN   A 1 307 ? 15.675  3.599   48.529 1.00 36.96  ?  332 GLN   A HA     1 
ATOM   4977  H  HB2    . GLN   A 1 307 ? 12.970  3.306   47.824 1.00 37.64  ?  332 GLN   A HB2    1 
ATOM   4978  H  HB3    . GLN   A 1 307 ? 13.496  4.610   48.565 1.00 37.64  ?  332 GLN   A HB3    1 
ATOM   4979  H  HG2    . GLN   A 1 307 ? 14.691  5.210   46.748 1.00 38.47  ?  332 GLN   A HG2    1 
ATOM   4980  H  HG3    . GLN   A 1 307 ? 14.308  3.854   46.012 1.00 38.47  ?  332 GLN   A HG3    1 
ATOM   4981  H  HE21   . GLN   A 1 307 ? 12.785  4.134   44.491 1.00 35.43  ?  332 GLN   A HE21   1 
ATOM   4982  H  HE22   . GLN   A 1 307 ? 11.644  5.089   44.545 1.00 35.43  ?  332 GLN   A HE22   1 
ATOM   4983  N  N      . ILE   A 1 308 ? 13.586  1.832   50.218 1.00 30.61  ?  333 ILE   A N      1 
ATOM   4984  C  CA     . ILE   A 1 308 ? 13.133  1.481   51.554 1.00 29.28  ?  333 ILE   A CA     1 
ATOM   4985  C  C      . ILE   A 1 308 ? 14.281  0.878   52.348 1.00 29.19  ?  333 ILE   A C      1 
ATOM   4986  O  O      . ILE   A 1 308 ? 14.566  1.302   53.473 1.00 30.66  ?  333 ILE   A O      1 
ATOM   4987  C  CB     . ILE   A 1 308 ? 11.922  0.533   51.462 1.00 29.52  ?  333 ILE   A CB     1 
ATOM   4988  C  CG1    . ILE   A 1 308 ? 10.794  1.226   50.683 1.00 28.39  ?  333 ILE   A CG1    1 
ATOM   4989  C  CG2    . ILE   A 1 308 ? 11.445  0.108   52.832 1.00 30.28  ?  333 ILE   A CG2    1 
ATOM   4990  C  CD1    . ILE   A 1 308 ? 9.714   0.300   50.175 1.00 27.61  ?  333 ILE   A CD1    1 
ATOM   4991  H  H      . ILE   A 1 308 ? 13.234  1.359   49.591 1.00 36.72  ?  333 ILE   A H      1 
ATOM   4992  H  HA     . ILE   A 1 308 ? 12.845  2.281   52.021 1.00 35.14  ?  333 ILE   A HA     1 
ATOM   4993  H  HB     . ILE   A 1 308 ? 12.195  -0.270  50.990 1.00 35.42  ?  333 ILE   A HB     1 
ATOM   4994  H  HG12   . ILE   A 1 308 ? 10.371  1.876   51.266 1.00 34.06  ?  333 ILE   A HG12   1 
ATOM   4995  H  HG13   . ILE   A 1 308 ? 11.180  1.674   49.914 1.00 34.06  ?  333 ILE   A HG13   1 
ATOM   4996  H  HG21   . ILE   A 1 308 ? 10.611  -0.379  52.738 1.00 36.32  ?  333 ILE   A HG21   1 
ATOM   4997  H  HG22   . ILE   A 1 308 ? 12.117  -0.461  53.238 1.00 36.32  ?  333 ILE   A HG22   1 
ATOM   4998  H  HG23   . ILE   A 1 308 ? 11.306  0.898   53.377 1.00 36.32  ?  333 ILE   A HG23   1 
ATOM   4999  H  HD11   . ILE   A 1 308 ? 9.076   0.813   49.654 1.00 33.13  ?  333 ILE   A HD11   1 
ATOM   5000  H  HD12   . ILE   A 1 308 ? 10.120  -0.384  49.619 1.00 33.13  ?  333 ILE   A HD12   1 
ATOM   5001  H  HD13   . ILE   A 1 308 ? 9.268   -0.111  50.932 1.00 33.13  ?  333 ILE   A HD13   1 
ATOM   5002  N  N      . VAL   A 1 309 ? 14.989  -0.088  51.758 1.00 29.46  ?  334 VAL   A N      1 
ATOM   5003  C  CA     . VAL   A 1 309 ? 16.047  -0.781  52.488 1.00 30.86  ?  334 VAL   A CA     1 
ATOM   5004  C  C      . VAL   A 1 309 ? 17.090  0.207   52.989 1.00 31.79  ?  334 VAL   A C      1 
ATOM   5005  O  O      . VAL   A 1 309 ? 17.502  0.157   54.153 1.00 31.65  ?  334 VAL   A O      1 
ATOM   5006  C  CB     . VAL   A 1 309 ? 16.694  -1.870  51.613 1.00 30.40  ?  334 VAL   A CB     1 
ATOM   5007  C  CG1    . VAL   A 1 309 ? 17.939  -2.443  52.305 1.00 31.90  ?  334 VAL   A CG1    1 
ATOM   5008  C  CG2    . VAL   A 1 309 ? 15.702  -2.967  51.341 1.00 29.94  ?  334 VAL   A CG2    1 
ATOM   5009  H  H      . VAL   A 1 309 ? 14.876  -0.356  50.949 1.00 35.35  ?  334 VAL   A H      1 
ATOM   5010  H  HA     . VAL   A 1 309 ? 15.643  -1.212  53.257 1.00 37.02  ?  334 VAL   A HA     1 
ATOM   5011  H  HB     . VAL   A 1 309 ? 16.967  -1.478  50.769 1.00 36.48  ?  334 VAL   A HB     1 
ATOM   5012  H  HG11   . VAL   A 1 309 ? 18.170  -3.289  51.889 1.00 38.28  ?  334 VAL   A HG11   1 
ATOM   5013  H  HG12   . VAL   A 1 309 ? 18.672  -1.816  52.207 1.00 38.28  ?  334 VAL   A HG12   1 
ATOM   5014  H  HG13   . VAL   A 1 309 ? 17.743  -2.580  53.245 1.00 38.28  ?  334 VAL   A HG13   1 
ATOM   5015  H  HG21   . VAL   A 1 309 ? 16.102  -3.613  50.738 1.00 35.92  ?  334 VAL   A HG21   1 
ATOM   5016  H  HG22   . VAL   A 1 309 ? 15.470  -3.398  52.179 1.00 35.92  ?  334 VAL   A HG22   1 
ATOM   5017  H  HG23   . VAL   A 1 309 ? 14.909  -2.583  50.936 1.00 35.92  ?  334 VAL   A HG23   1 
ATOM   5018  N  N      . THR   A 1 310 ? 17.543  1.115   52.119 1.00 32.45  ?  335 THR   A N      1 
ATOM   5019  C  CA     . THR   A 1 310 ? 18.634  2.001   52.514 1.00 34.89  ?  335 THR   A CA     1 
ATOM   5020  C  C      . THR   A 1 310 ? 18.226  2.890   53.683 1.00 36.42  ?  335 THR   A C      1 
ATOM   5021  O  O      . THR   A 1 310 ? 19.029  3.137   54.590 1.00 36.65  ?  335 THR   A O      1 
ATOM   5022  C  CB     . THR   A 1 310 ? 19.102  2.857   51.336 1.00 39.30  ?  335 THR   A CB     1 
ATOM   5023  O  OG1    . THR   A 1 310 ? 18.036  3.697   50.880 1.00 43.94  ?  335 THR   A OG1    1 
ATOM   5024  C  CG2    . THR   A 1 310 ? 19.578  1.983   50.202 1.00 38.29  ?  335 THR   A CG2    1 
ATOM   5025  H  H      . THR   A 1 310 ? 17.245  1.232   51.322 1.00 38.93  ?  335 THR   A H      1 
ATOM   5026  H  HA     . THR   A 1 310 ? 19.383  1.449   52.790 1.00 41.86  ?  335 THR   A HA     1 
ATOM   5027  H  HB     . THR   A 1 310 ? 19.842  3.416   51.623 1.00 47.15  ?  335 THR   A HB     1 
ATOM   5028  H  HG1    . THR   A 1 310 ? 18.302  4.179   50.245 1.00 52.72  ?  335 THR   A HG1    1 
ATOM   5029  H  HG21   . THR   A 1 310 ? 19.561  2.481   49.370 1.00 45.94  ?  335 THR   A HG21   1 
ATOM   5030  H  HG22   . THR   A 1 310 ? 20.485  1.684   50.372 1.00 45.94  ?  335 THR   A HG22   1 
ATOM   5031  H  HG23   . THR   A 1 310 ? 19.001  1.208   50.117 1.00 45.94  ?  335 THR   A HG23   1 
ATOM   5032  N  N      . LYS   A 1 311 ? 16.982  3.375   53.689 1.00 36.44  ?  336 LYS   A N      1 
ATOM   5033  C  CA     . LYS   A 1 311 ? 16.533  4.220   54.793 1.00 38.76  ?  336 LYS   A CA     1 
ATOM   5034  C  C      . LYS   A 1 311 ? 16.419  3.426   56.090 1.00 39.66  ?  336 LYS   A C      1 
ATOM   5035  O  O      . LYS   A 1 311 ? 16.798  3.916   57.163 1.00 41.47  ?  336 LYS   A O      1 
ATOM   5036  C  CB     . LYS   A 1 311 ? 15.193  4.870   54.439 1.00 40.84  ?  336 LYS   A CB     1 
ATOM   5037  C  CG     . LYS   A 1 311 ? 15.275  5.931   53.345 1.00 43.00  ?  336 LYS   A CG     1 
ATOM   5038  C  CD     . LYS   A 1 311 ? 15.802  7.256   53.910 1.00 46.00  ?  336 LYS   A CD     1 
ATOM   5039  C  CE     . LYS   A 1 311 ? 16.120  8.255   52.804 1.00 49.87  ?  336 LYS   A CE     1 
ATOM   5040  N  NZ     . LYS   A 1 311 ? 14.998  8.401   51.836 1.00 53.12  ?  336 LYS   A NZ     1 
ATOM   5041  H  H      . LYS   A 1 311 ? 16.392  3.232   53.080 1.00 43.72  ?  336 LYS   A H      1 
ATOM   5042  H  HA     . LYS   A 1 311 ? 17.184  4.926   54.931 1.00 46.51  ?  336 LYS   A HA     1 
ATOM   5043  H  HB2    . LYS   A 1 311 ? 14.586  4.178   54.133 1.00 49.00  ?  336 LYS   A HB2    1 
ATOM   5044  H  HB3    . LYS   A 1 311 ? 14.837  5.295   55.235 1.00 49.00  ?  336 LYS   A HB3    1 
ATOM   5045  H  HG2    . LYS   A 1 311 ? 15.878  5.631   52.648 1.00 51.60  ?  336 LYS   A HG2    1 
ATOM   5046  H  HG3    . LYS   A 1 311 ? 14.391  6.083   52.976 1.00 51.60  ?  336 LYS   A HG3    1 
ATOM   5047  H  HD2    . LYS   A 1 311 ? 15.130  7.648   54.489 1.00 55.19  ?  336 LYS   A HD2    1 
ATOM   5048  H  HD3    . LYS   A 1 311 ? 16.616  7.089   54.412 1.00 55.19  ?  336 LYS   A HD3    1 
ATOM   5049  H  HE2    . LYS   A 1 311 ? 16.292  9.124   53.200 1.00 59.84  ?  336 LYS   A HE2    1 
ATOM   5050  H  HE3    . LYS   A 1 311 ? 16.902  7.952   52.316 1.00 59.84  ?  336 LYS   A HE3    1 
ATOM   5051  H  HZ1    . LYS   A 1 311 ? 14.850  7.626   51.423 1.00 63.74  ?  336 LYS   A HZ1    1 
ATOM   5052  H  HZ2    . LYS   A 1 311 ? 14.257  8.646   52.264 1.00 63.74  ?  336 LYS   A HZ2    1 
ATOM   5053  H  HZ3    . LYS   A 1 311 ? 15.198  9.019   51.228 1.00 63.74  ?  336 LYS   A HZ3    1 
ATOM   5054  N  N      . LEU   A 1 312 ? 15.901  2.200   56.020 1.00 38.74  ?  337 LEU   A N      1 
ATOM   5055  C  CA     . LEU   A 1 312 ? 15.782  1.404   57.234 1.00 39.35  ?  337 LEU   A CA     1 
ATOM   5056  C  C      . LEU   A 1 312 ? 17.151  0.988   57.759 1.00 39.58  ?  337 LEU   A C      1 
ATOM   5057  O  O      . LEU   A 1 312 ? 17.372  0.958   58.977 1.00 40.05  ?  337 LEU   A O      1 
ATOM   5058  C  CB     . LEU   A 1 312 ? 14.919  0.170   56.986 1.00 38.94  ?  337 LEU   A CB     1 
ATOM   5059  C  CG     . LEU   A 1 312 ? 13.494  0.419   56.504 1.00 41.24  ?  337 LEU   A CG     1 
ATOM   5060  C  CD1    . LEU   A 1 312 ? 12.705  -0.890  56.461 1.00 41.64  ?  337 LEU   A CD1    1 
ATOM   5061  C  CD2    . LEU   A 1 312 ? 12.790  1.422   57.374 1.00 41.69  ?  337 LEU   A CD2    1 
ATOM   5062  H  H      . LEU   A 1 312 ? 15.621  1.819   55.302 1.00 46.48  ?  337 LEU   A H      1 
ATOM   5063  H  HA     . LEU   A 1 312 ? 15.343  1.945   57.909 1.00 47.21  ?  337 LEU   A HA     1 
ATOM   5064  H  HB2    . LEU   A 1 312 ? 15.357  -0.372  56.312 1.00 46.72  ?  337 LEU   A HB2    1 
ATOM   5065  H  HB3    . LEU   A 1 312 ? 14.855  -0.323  57.819 1.00 46.72  ?  337 LEU   A HB3    1 
ATOM   5066  H  HG     . LEU   A 1 312 ? 13.535  0.784   55.606 1.00 49.49  ?  337 LEU   A HG     1 
ATOM   5067  H  HD11   . LEU   A 1 312 ? 11.811  -0.709  56.132 1.00 49.96  ?  337 LEU   A HD11   1 
ATOM   5068  H  HD12   . LEU   A 1 312 ? 13.156  -1.511  55.867 1.00 49.96  ?  337 LEU   A HD12   1 
ATOM   5069  H  HD13   . LEU   A 1 312 ? 12.660  -1.261  57.356 1.00 49.96  ?  337 LEU   A HD13   1 
ATOM   5070  H  HD21   . LEU   A 1 312 ? 11.847  1.429   57.148 1.00 50.02  ?  337 LEU   A HD21   1 
ATOM   5071  H  HD22   . LEU   A 1 312 ? 12.905  1.171   58.303 1.00 50.02  ?  337 LEU   A HD22   1 
ATOM   5072  H  HD23   . LEU   A 1 312 ? 13.174  2.300   57.218 1.00 50.02  ?  337 LEU   A HD23   1 
ATOM   5073  N  N      . VAL   A 1 313 ? 18.080  0.646   56.861 1.00 40.09  ?  338 VAL   A N      1 
ATOM   5074  C  CA     . VAL   A 1 313 ? 19.431  0.307   57.296 1.00 40.95  ?  338 VAL   A CA     1 
ATOM   5075  C  C      . VAL   A 1 313 ? 20.030  1.468   58.079 1.00 44.53  ?  338 VAL   A C      1 
ATOM   5076  O  O      . VAL   A 1 313 ? 20.641  1.275   59.136 1.00 45.70  ?  338 VAL   A O      1 
ATOM   5077  C  CB     . VAL   A 1 313 ? 20.312  -0.071  56.091 1.00 39.51  ?  338 VAL   A CB     1 
ATOM   5078  C  CG1    . VAL   A 1 313 ? 21.795  0.003   56.466 1.00 40.30  ?  338 VAL   A CG1    1 
ATOM   5079  C  CG2    . VAL   A 1 313 ? 19.963  -1.460  55.595 1.00 39.23  ?  338 VAL   A CG2    1 
ATOM   5080  H  H      . VAL   A 1 313 ? 17.953  0.603   56.012 1.00 48.10  ?  338 VAL   A H      1 
ATOM   5081  H  HA     . VAL   A 1 313 ? 19.383  -0.466  57.880 1.00 49.14  ?  338 VAL   A HA     1 
ATOM   5082  H  HB     . VAL   A 1 313 ? 20.147  0.560   55.373 1.00 47.41  ?  338 VAL   A HB     1 
ATOM   5083  H  HG11   . VAL   A 1 313 ? 22.310  -0.499  55.815 1.00 48.35  ?  338 VAL   A HG11   1 
ATOM   5084  H  HG12   . VAL   A 1 313 ? 22.075  0.931   56.465 1.00 48.35  ?  338 VAL   A HG12   1 
ATOM   5085  H  HG13   . VAL   A 1 313 ? 21.916  -0.379  57.349 1.00 48.35  ?  338 VAL   A HG13   1 
ATOM   5086  H  HG21   . VAL   A 1 313 ? 20.442  -1.630  54.769 1.00 47.06  ?  338 VAL   A HG21   1 
ATOM   5087  H  HG22   . VAL   A 1 313 ? 20.223  -2.109  56.267 1.00 47.06  ?  338 VAL   A HG22   1 
ATOM   5088  H  HG23   . VAL   A 1 313 ? 19.007  -1.509  55.440 1.00 47.06  ?  338 VAL   A HG23   1 
ATOM   5089  N  N      . ASP   A 1 314 ? 19.853  2.694   57.575 1.00 47.10  ?  339 ASP   A N      1 
ATOM   5090  C  CA     . ASP   A 1 314 ? 20.392  3.863   58.261 1.00 49.42  ?  339 ASP   A CA     1 
ATOM   5091  C  C      . ASP   A 1 314 ? 19.795  4.005   59.655 1.00 50.79  ?  339 ASP   A C      1 
ATOM   5092  O  O      . ASP   A 1 314 ? 20.502  4.350   60.610 1.00 51.46  ?  339 ASP   A O      1 
ATOM   5093  C  CB     . ASP   A 1 314 ? 20.133  5.127   57.436 1.00 51.92  ?  339 ASP   A CB     1 
ATOM   5094  C  CG     . ASP   A 1 314 ? 21.050  5.235   56.226 1.00 54.68  ?  339 ASP   A CG     1 
ATOM   5095  O  OD1    . ASP   A 1 314 ? 22.028  4.460   56.161 1.00 56.06  ?  339 ASP   A OD1    1 
ATOM   5096  O  OD2    . ASP   A 1 314 ? 20.792  6.079   55.334 1.00 55.00  ?  339 ASP   A OD2    1 
ATOM   5097  H  H      . ASP   A 1 314 ? 19.430  2.870   56.847 1.00 56.52  ?  339 ASP   A H      1 
ATOM   5098  H  HA     . ASP   A 1 314 ? 21.352  3.756   58.352 1.00 59.29  ?  339 ASP   A HA     1 
ATOM   5099  H  HB2    . ASP   A 1 314 ? 19.217  5.116   57.118 1.00 62.30  ?  339 ASP   A HB2    1 
ATOM   5100  H  HB3    . ASP   A 1 314 ? 20.281  5.906   57.995 1.00 62.30  ?  339 ASP   A HB3    1 
ATOM   5101  N  N      . VAL   A 1 315 ? 18.492  3.751   59.796 1.00 51.24  ?  340 VAL   A N      1 
ATOM   5102  C  CA     . VAL   A 1 315 ? 17.877  3.830   61.117 1.00 51.86  ?  340 VAL   A CA     1 
ATOM   5103  C  C      . VAL   A 1 315 ? 18.516  2.818   62.057 1.00 51.65  ?  340 VAL   A C      1 
ATOM   5104  O  O      . VAL   A 1 315 ? 18.795  3.122   63.224 1.00 51.40  ?  340 VAL   A O      1 
ATOM   5105  C  CB     . VAL   A 1 315 ? 16.354  3.623   61.026 1.00 53.09  ?  340 VAL   A CB     1 
ATOM   5106  C  CG1    . VAL   A 1 315 ? 15.766  3.402   62.423 1.00 54.03  ?  340 VAL   A CG1    1 
ATOM   5107  C  CG2    . VAL   A 1 315 ? 15.698  4.821   60.368 1.00 53.39  ?  340 VAL   A CG2    1 
ATOM   5108  H  H      . VAL   A 1 315 ? 17.958  3.537   59.157 1.00 61.48  ?  340 VAL   A H      1 
ATOM   5109  H  HA     . VAL   A 1 315 ? 18.034  4.720   61.469 1.00 62.23  ?  340 VAL   A HA     1 
ATOM   5110  H  HB     . VAL   A 1 315 ? 16.173  2.838   60.485 1.00 63.70  ?  340 VAL   A HB     1 
ATOM   5111  H  HG11   . VAL   A 1 315 ? 14.807  3.546   62.388 1.00 64.83  ?  340 VAL   A HG11   1 
ATOM   5112  H  HG12   . VAL   A 1 315 ? 15.953  2.492   62.704 1.00 64.83  ?  340 VAL   A HG12   1 
ATOM   5113  H  HG13   . VAL   A 1 315 ? 16.173  4.029   63.040 1.00 64.83  ?  340 VAL   A HG13   1 
ATOM   5114  H  HG21   . VAL   A 1 315 ? 14.736  4.697   60.374 1.00 64.06  ?  340 VAL   A HG21   1 
ATOM   5115  H  HG22   . VAL   A 1 315 ? 15.931  5.621   60.865 1.00 64.06  ?  340 VAL   A HG22   1 
ATOM   5116  H  HG23   . VAL   A 1 315 ? 16.016  4.894   59.455 1.00 64.06  ?  340 VAL   A HG23   1 
ATOM   5117  N  N      . VAL   A 1 316 ? 18.752  1.597   61.571 1.00 52.12  ?  341 VAL   A N      1 
ATOM   5118  C  CA     . VAL   A 1 316 ? 19.335  0.566   62.424 1.00 54.01  ?  341 VAL   A CA     1 
ATOM   5119  C  C      . VAL   A 1 316 ? 20.745  0.961   62.841 1.00 56.82  ?  341 VAL   A C      1 
ATOM   5120  O  O      . VAL   A 1 316 ? 21.149  0.752   63.991 1.00 57.92  ?  341 VAL   A O      1 
ATOM   5121  C  CB     . VAL   A 1 316 ? 19.314  -0.799  61.712 1.00 52.99  ?  341 VAL   A CB     1 
ATOM   5122  C  CG1    . VAL   A 1 316 ? 20.140  -1.816  62.489 1.00 53.30  ?  341 VAL   A CG1    1 
ATOM   5123  C  CG2    . VAL   A 1 316 ? 17.881  -1.285  61.554 1.00 52.07  ?  341 VAL   A CG2    1 
ATOM   5124  H  H      . VAL   A 1 316 ? 18.586  1.347   60.765 1.00 62.54  ?  341 VAL   A H      1 
ATOM   5125  H  HA     . VAL   A 1 316 ? 18.794  0.489   63.225 1.00 64.81  ?  341 VAL   A HA     1 
ATOM   5126  H  HB     . VAL   A 1 316 ? 19.705  -0.704  60.829 1.00 63.59  ?  341 VAL   A HB     1 
ATOM   5127  H  HG11   . VAL   A 1 316 ? 19.897  -2.708  62.197 1.00 63.95  ?  341 VAL   A HG11   1 
ATOM   5128  H  HG12   . VAL   A 1 316 ? 21.081  -1.655  62.317 1.00 63.95  ?  341 VAL   A HG12   1 
ATOM   5129  H  HG13   . VAL   A 1 316 ? 19.954  -1.715  63.435 1.00 63.95  ?  341 VAL   A HG13   1 
ATOM   5130  H  HG21   . VAL   A 1 316 ? 17.887  -2.144  61.103 1.00 62.48  ?  341 VAL   A HG21   1 
ATOM   5131  H  HG22   . VAL   A 1 316 ? 17.479  -1.375  62.432 1.00 62.48  ?  341 VAL   A HG22   1 
ATOM   5132  H  HG23   . VAL   A 1 316 ? 17.385  -0.638  61.028 1.00 62.48  ?  341 VAL   A HG23   1 
ATOM   5133  N  N      . LYS   A 1 317 ? 21.512  1.549   61.920 1.00 58.64  ?  342 LYS   A N      1 
ATOM   5134  C  CA     . LYS   A 1 317 ? 22.869  1.965   62.257 1.00 60.62  ?  342 LYS   A CA     1 
ATOM   5135  C  C      . LYS   A 1 317 ? 22.864  3.041   63.341 1.00 61.69  ?  342 LYS   A C      1 
ATOM   5136  O  O      . LYS   A 1 317 ? 23.739  3.053   64.215 1.00 62.63  ?  342 LYS   A O      1 
ATOM   5137  C  CB     . LYS   A 1 317 ? 23.595  2.456   61.006 1.00 60.98  ?  342 LYS   A CB     1 
ATOM   5138  C  CG     . LYS   A 1 317 ? 23.854  1.371   59.966 1.00 61.42  ?  342 LYS   A CG     1 
ATOM   5139  C  CD     . LYS   A 1 317 ? 24.673  0.211   60.544 1.00 61.51  ?  342 LYS   A CD     1 
ATOM   5140  C  CE     . LYS   A 1 317 ? 23.774  -0.881  61.124 1.00 60.75  ?  342 LYS   A CE     1 
ATOM   5141  N  NZ     . LYS   A 1 317 ? 24.496  -1.809  62.041 1.00 60.13  ?  342 LYS   A NZ     1 
ATOM   5142  H  H      . LYS   A 1 317 ? 21.274  1.715   61.110 1.00 70.36  ?  342 LYS   A H      1 
ATOM   5143  H  HA     . LYS   A 1 317 ? 23.356  1.199   62.600 1.00 72.74  ?  342 LYS   A HA     1 
ATOM   5144  H  HB2    . LYS   A 1 317 ? 23.056  3.144   60.585 1.00 73.17  ?  342 LYS   A HB2    1 
ATOM   5145  H  HB3    . LYS   A 1 317 ? 24.454  2.823   61.269 1.00 73.17  ?  342 LYS   A HB3    1 
ATOM   5146  H  HG2    . LYS   A 1 317 ? 23.006  1.018   59.655 1.00 73.70  ?  342 LYS   A HG2    1 
ATOM   5147  H  HG3    . LYS   A 1 317 ? 24.349  1.751   59.223 1.00 73.70  ?  342 LYS   A HG3    1 
ATOM   5148  H  HD2    . LYS   A 1 317 ? 25.214  -0.181  59.840 1.00 73.81  ?  342 LYS   A HD2    1 
ATOM   5149  H  HD3    . LYS   A 1 317 ? 25.244  0.545   61.254 1.00 73.81  ?  342 LYS   A HD3    1 
ATOM   5150  H  HE2    . LYS   A 1 317 ? 23.056  -0.465  61.626 1.00 72.89  ?  342 LYS   A HE2    1 
ATOM   5151  H  HE3    . LYS   A 1 317 ? 23.408  -1.407  60.395 1.00 72.89  ?  342 LYS   A HE3    1 
ATOM   5152  H  HZ1    . LYS   A 1 317 ? 24.872  -1.350  62.704 1.00 72.15  ?  342 LYS   A HZ1    1 
ATOM   5153  H  HZ2    . LYS   A 1 317 ? 23.927  -2.401  62.385 1.00 72.15  ?  342 LYS   A HZ2    1 
ATOM   5154  H  HZ3    . LYS   A 1 317 ? 25.132  -2.245  61.595 1.00 72.15  ?  342 LYS   A HZ3    1 
ATOM   5155  N  N      . LYS   A 1 318 ? 21.879  3.947   63.310 1.00 62.97  ?  343 LYS   A N      1 
ATOM   5156  C  CA     . LYS   A 1 318 ? 21.772  4.959   64.359 1.00 65.69  ?  343 LYS   A CA     1 
ATOM   5157  C  C      . LYS   A 1 318 ? 21.647  4.329   65.742 1.00 67.23  ?  343 LYS   A C      1 
ATOM   5158  O  O      . LYS   A 1 318 ? 22.083  4.918   66.742 1.00 67.49  ?  343 LYS   A O      1 
ATOM   5159  C  CB     . LYS   A 1 318 ? 20.561  5.863   64.111 1.00 67.89  ?  343 LYS   A CB     1 
ATOM   5160  C  CG     . LYS   A 1 318 ? 20.627  6.714   62.852 1.00 69.91  ?  343 LYS   A CG     1 
ATOM   5161  C  CD     . LYS   A 1 318 ? 21.566  7.898   63.021 1.00 71.72  ?  343 LYS   A CD     1 
ATOM   5162  C  CE     . LYS   A 1 318 ? 20.928  9.185   62.509 1.00 73.17  ?  343 LYS   A CE     1 
ATOM   5163  N  NZ     . LYS   A 1 318 ? 21.894  10.002  61.719 1.00 73.93  ?  343 LYS   A NZ     1 
ATOM   5164  H  H      . LYS   A 1 318 ? 21.272  3.994   62.703 1.00 75.56  ?  343 LYS   A H      1 
ATOM   5165  H  HA     . LYS   A 1 318 ? 22.575  5.502   64.333 1.00 78.82  ?  343 LYS   A HA     1 
ATOM   5166  H  HB2    . LYS   A 1 318 ? 19.772  5.304   64.041 1.00 81.46  ?  343 LYS   A HB2    1 
ATOM   5167  H  HB3    . LYS   A 1 318 ? 20.473  6.468   64.864 1.00 81.46  ?  343 LYS   A HB3    1 
ATOM   5168  H  HG2    . LYS   A 1 318 ? 20.951  6.172   62.116 1.00 83.88  ?  343 LYS   A HG2    1 
ATOM   5169  H  HG3    . LYS   A 1 318 ? 19.742  7.054   62.649 1.00 83.88  ?  343 LYS   A HG3    1 
ATOM   5170  H  HD2    . LYS   A 1 318 ? 21.774  8.013   63.961 1.00 86.05  ?  343 LYS   A HD2    1 
ATOM   5171  H  HD3    . LYS   A 1 318 ? 22.380  7.738   62.518 1.00 86.05  ?  343 LYS   A HD3    1 
ATOM   5172  H  HE2    . LYS   A 1 318 ? 20.177  8.964   61.937 1.00 87.79  ?  343 LYS   A HE2    1 
ATOM   5173  H  HE3    . LYS   A 1 318 ? 20.627  9.715   63.263 1.00 87.79  ?  343 LYS   A HE3    1 
ATOM   5174  H  HZ1    . LYS   A 1 318 ? 22.173  9.542   61.010 1.00 88.71  ?  343 LYS   A HZ1    1 
ATOM   5175  H  HZ2    . LYS   A 1 318 ? 21.503  10.751  61.441 1.00 88.71  ?  343 LYS   A HZ2    1 
ATOM   5176  H  HZ3    . LYS   A 1 318 ? 22.597  10.212  62.221 1.00 88.71  ?  343 LYS   A HZ3    1 
ATOM   5177  N  N      . LYS   A 1 319 ? 21.043  3.145   65.821 1.00 68.96  ?  344 LYS   A N      1 
ATOM   5178  C  CA     . LYS   A 1 319 ? 20.733  2.493   67.085 1.00 71.51  ?  344 LYS   A CA     1 
ATOM   5179  C  C      . LYS   A 1 319 ? 21.595  1.259   67.329 1.00 73.02  ?  344 LYS   A C      1 
ATOM   5180  O  O      . LYS   A 1 319 ? 21.168  0.326   68.013 1.00 73.51  ?  344 LYS   A O      1 
ATOM   5181  C  CB     . LYS   A 1 319 ? 19.251  2.116   67.118 1.00 72.32  ?  344 LYS   A CB     1 
ATOM   5182  C  CG     . LYS   A 1 319 ? 18.314  3.263   66.790 1.00 73.29  ?  344 LYS   A CG     1 
ATOM   5183  C  CD     . LYS   A 1 319 ? 16.873  2.787   66.710 1.00 74.27  ?  344 LYS   A CD     1 
ATOM   5184  C  CE     . LYS   A 1 319 ? 15.905  3.959   66.728 1.00 75.18  ?  344 LYS   A CE     1 
ATOM   5185  N  NZ     . LYS   A 1 319 ? 14.560  3.560   66.228 1.00 75.84  ?  344 LYS   A NZ     1 
ATOM   5186  H  H      . LYS   A 1 319 ? 20.797  2.689   65.134 1.00 82.74  ?  344 LYS   A H      1 
ATOM   5187  H  HA     . LYS   A 1 319 ? 20.914  3.116   67.807 1.00 85.81  ?  344 LYS   A HA     1 
ATOM   5188  H  HB2    . LYS   A 1 319 ? 19.096  1.413   66.468 1.00 86.78  ?  344 LYS   A HB2    1 
ATOM   5189  H  HB3    . LYS   A 1 319 ? 19.031  1.800   68.008 1.00 86.78  ?  344 LYS   A HB3    1 
ATOM   5190  H  HG2    . LYS   A 1 319 ? 18.375  3.938   67.483 1.00 87.94  ?  344 LYS   A HG2    1 
ATOM   5191  H  HG3    . LYS   A 1 319 ? 18.558  3.644   65.932 1.00 87.94  ?  344 LYS   A HG3    1 
ATOM   5192  H  HD2    . LYS   A 1 319 ? 16.741  2.294   65.885 1.00 89.11  ?  344 LYS   A HD2    1 
ATOM   5193  H  HD3    . LYS   A 1 319 ? 16.679  2.219   67.472 1.00 89.11  ?  344 LYS   A HD3    1 
ATOM   5194  H  HE2    . LYS   A 1 319 ? 15.810  4.284   67.637 1.00 90.21  ?  344 LYS   A HE2    1 
ATOM   5195  H  HE3    . LYS   A 1 319 ? 16.246  4.666   66.157 1.00 90.21  ?  344 LYS   A HE3    1 
ATOM   5196  H  HZ1    . LYS   A 1 319 ? 14.006  4.256   66.257 1.00 91.00  ?  344 LYS   A HZ1    1 
ATOM   5197  H  HZ2    . LYS   A 1 319 ? 14.620  3.273   65.388 1.00 91.00  ?  344 LYS   A HZ2    1 
ATOM   5198  H  HZ3    . LYS   A 1 319 ? 14.229  2.907   66.733 1.00 91.00  ?  344 LYS   A HZ3    1 
ATOM   5199  N  N      . ASN   A 1 320 ? 22.812  1.244   66.790 1.00 73.38  ?  345 ASN   A N      1 
ATOM   5200  C  CA     . ASN   A 1 320 ? 23.684  0.072   66.894 1.00 73.03  ?  345 ASN   A CA     1 
ATOM   5201  C  C      . ASN   A 1 320 ? 25.164  0.456   66.844 1.00 71.79  ?  345 ASN   A C      1 
ATOM   5202  O  O      . ASN   A 1 320 ? 25.711  1.009   67.807 1.00 70.38  ?  345 ASN   A O      1 
ATOM   5203  C  CB     . ASN   A 1 320 ? 23.341  -0.915  65.768 1.00 73.92  ?  345 ASN   A CB     1 
ATOM   5204  C  CG     . ASN   A 1 320 ? 24.039  -2.253  65.921 1.00 74.37  ?  345 ASN   A CG     1 
ATOM   5205  O  OD1    . ASN   A 1 320 ? 24.568  -2.804  64.953 1.00 74.27  ?  345 ASN   A OD1    1 
ATOM   5206  N  ND2    . ASN   A 1 320 ? 24.044  -2.783  67.140 1.00 74.34  ?  345 ASN   A ND2    1 
ATOM   5207  H  H      . ASN   A 1 320 ? 23.159  1.901   66.358 1.00 88.05  ?  345 ASN   A H      1 
ATOM   5208  H  HA     . ASN   A 1 320 ? 23.540  -0.363  67.749 1.00 87.63  ?  345 ASN   A HA     1 
ATOM   5209  H  HB2    . ASN   A 1 320 ? 22.385  -1.076  65.770 1.00 88.70  ?  345 ASN   A HB2    1 
ATOM   5210  H  HB3    . ASN   A 1 320 ? 23.612  -0.532  64.919 1.00 88.70  ?  345 ASN   A HB3    1 
ATOM   5211  H  HD21   . ASN   A 1 320 ? 24.427  -3.541  67.277 1.00 89.20  ?  345 ASN   A HD21   1 
ATOM   5212  H  HD22   . ASN   A 1 320 ? 23.664  -2.369  67.791 1.00 89.20  ?  345 ASN   A HD22   1 
ATOM   5213  N  N      . ALA   A 1 325 ? 27.005  -3.427  61.433 1.00 58.75  ?  350 ALA   A N      1 
ATOM   5214  C  CA     . ALA   A 1 325 ? 26.734  -4.818  61.763 1.00 58.70  ?  350 ALA   A CA     1 
ATOM   5215  C  C      . ALA   A 1 325 ? 25.629  -5.390  60.864 1.00 58.43  ?  350 ALA   A C      1 
ATOM   5216  O  O      . ALA   A 1 325 ? 25.806  -6.463  60.292 1.00 59.91  ?  350 ALA   A O      1 
ATOM   5217  C  CB     . ALA   A 1 325 ? 26.361  -4.954  63.245 1.00 57.97  ?  350 ALA   A CB     1 
ATOM   5218  H  HA     . ALA   A 1 325 ? 27.536  -5.342  61.614 1.00 70.44  ?  350 ALA   A HA     1 
ATOM   5219  H  HB1    . ALA   A 1 325 ? 26.184  -5.887  63.442 1.00 69.56  ?  350 ALA   A HB1    1 
ATOM   5220  H  HB2    . ALA   A 1 325 ? 27.100  -4.636  63.787 1.00 69.56  ?  350 ALA   A HB2    1 
ATOM   5221  H  HB3    . ALA   A 1 325 ? 25.568  -4.423  63.422 1.00 69.56  ?  350 ALA   A HB3    1 
ATOM   5222  N  N      . VAL   A 1 326 ? 24.497  -4.673  60.715 1.00 56.81  ?  351 VAL   A N      1 
ATOM   5223  C  CA     . VAL   A 1 326 ? 23.377  -5.196  59.933 1.00 54.44  ?  351 VAL   A CA     1 
ATOM   5224  C  C      . VAL   A 1 326 ? 23.653  -5.022  58.444 1.00 51.63  ?  351 VAL   A C      1 
ATOM   5225  O  O      . VAL   A 1 326 ? 24.276  -4.046  58.009 1.00 52.84  ?  351 VAL   A O      1 
ATOM   5226  C  CB     . VAL   A 1 326 ? 22.047  -4.519  60.321 1.00 55.70  ?  351 VAL   A CB     1 
ATOM   5227  C  CG1    . VAL   A 1 326 ? 21.862  -3.201  59.586 1.00 56.66  ?  351 VAL   A CG1    1 
ATOM   5228  C  CG2    . VAL   A 1 326 ? 20.872  -5.441  60.002 1.00 55.47  ?  351 VAL   A CG2    1 
ATOM   5229  H  H      . VAL   A 1 326 ? 24.363  -3.895  61.054 1.00 68.16  ?  351 VAL   A H      1 
ATOM   5230  H  HA     . VAL   A 1 326 ? 23.302  -6.143  60.129 1.00 65.32  ?  351 VAL   A HA     1 
ATOM   5231  H  HB     . VAL   A 1 326 ? 22.070  -4.340  61.274 1.00 66.83  ?  351 VAL   A HB     1 
ATOM   5232  H  HG11   . VAL   A 1 326 ? 21.465  -2.555  60.191 1.00 67.99  ?  351 VAL   A HG11   1 
ATOM   5233  H  HG12   . VAL   A 1 326 ? 22.727  -2.883  59.284 1.00 67.99  ?  351 VAL   A HG12   1 
ATOM   5234  H  HG13   . VAL   A 1 326 ? 21.277  -3.343  58.825 1.00 67.99  ?  351 VAL   A HG13   1 
ATOM   5235  H  HG21   . VAL   A 1 326 ? 20.044  -4.978  60.205 1.00 66.56  ?  351 VAL   A HG21   1 
ATOM   5236  H  HG22   . VAL   A 1 326 ? 20.899  -5.672  59.060 1.00 66.56  ?  351 VAL   A HG22   1 
ATOM   5237  H  HG23   . VAL   A 1 326 ? 20.944  -6.243  60.542 1.00 66.56  ?  351 VAL   A HG23   1 
ATOM   5238  N  N      . LYS   A 1 327 ? 23.153  -5.960  57.648 1.00 47.95  ?  352 LYS   A N      1 
ATOM   5239  C  CA     . LYS   A 1 327 ? 23.362  -5.953  56.210 1.00 45.52  ?  352 LYS   A CA     1 
ATOM   5240  C  C      . LYS   A 1 327 ? 22.034  -5.774  55.489 1.00 41.41  ?  352 LYS   A C      1 
ATOM   5241  O  O      . LYS   A 1 327 ? 20.969  -6.132  56.002 1.00 40.43  ?  352 LYS   A O      1 
ATOM   5242  C  CB     . LYS   A 1 327 ? 24.055  -7.241  55.752 1.00 47.27  ?  352 LYS   A CB     1 
ATOM   5243  C  CG     . LYS   A 1 327 ? 25.354  -7.531  56.504 1.00 49.36  ?  352 LYS   A CG     1 
ATOM   5244  C  CD     . LYS   A 1 327 ? 26.355  -8.279  55.629 1.00 51.65  ?  352 LYS   A CD     1 
ATOM   5245  C  CE     . LYS   A 1 327 ? 27.636  -8.601  56.388 1.00 52.27  ?  352 LYS   A CE     1 
ATOM   5246  N  NZ     . LYS   A 1 327 ? 27.459  -9.771  57.292 1.00 52.88  ?  352 LYS   A NZ     1 
ATOM   5247  H  H      . LYS   A 1 327 ? 22.681  -6.624  57.926 1.00 57.53  ?  352 LYS   A H      1 
ATOM   5248  H  HA     . LYS   A 1 327 ? 23.927  -5.204  55.964 1.00 54.62  ?  352 LYS   A HA     1 
ATOM   5249  H  HB2    . LYS   A 1 327 ? 23.454  -7.988  55.897 1.00 56.72  ?  352 LYS   A HB2    1 
ATOM   5250  H  HB3    . LYS   A 1 327 ? 24.267  -7.163  54.809 1.00 56.72  ?  352 LYS   A HB3    1 
ATOM   5251  H  HG2    . LYS   A 1 327 ? 25.759  -6.694  56.781 1.00 59.22  ?  352 LYS   A HG2    1 
ATOM   5252  H  HG3    . LYS   A 1 327 ? 25.160  -8.079  57.280 1.00 59.22  ?  352 LYS   A HG3    1 
ATOM   5253  H  HD2    . LYS   A 1 327 ? 25.960  -9.113  55.331 1.00 61.98  ?  352 LYS   A HD2    1 
ATOM   5254  H  HD3    . LYS   A 1 327 ? 26.585  -7.729  54.864 1.00 61.98  ?  352 LYS   A HD3    1 
ATOM   5255  H  HE2    . LYS   A 1 327 ? 28.340  -8.809  55.754 1.00 62.72  ?  352 LYS   A HE2    1 
ATOM   5256  H  HE3    . LYS   A 1 327 ? 27.890  -7.836  56.927 1.00 62.72  ?  352 LYS   A HE3    1 
ATOM   5257  H  HZ1    . LYS   A 1 327 ? 26.606  -9.841  57.537 1.00 63.45  ?  352 LYS   A HZ1    1 
ATOM   5258  H  HZ2    . LYS   A 1 327 ? 27.701  -10.519 56.874 1.00 63.45  ?  352 LYS   A HZ2    1 
ATOM   5259  H  HZ3    . LYS   A 1 327 ? 27.961  -9.672  58.020 1.00 63.45  ?  352 LYS   A HZ3    1 
ATOM   5260  N  N      . ALA   A 1 328 ? 22.119  -5.197  54.289 1.00 39.07  ?  353 ALA   A N      1 
ATOM   5261  C  CA     . ALA   A 1 328 ? 20.915  -4.874  53.534 1.00 38.92  ?  353 ALA   A CA     1 
ATOM   5262  C  C      . ALA   A 1 328 ? 20.020  -6.092  53.345 1.00 35.88  ?  353 ALA   A C      1 
ATOM   5263  O  O      . ALA   A 1 328 ? 18.792  -5.991  53.464 1.00 34.04  ?  353 ALA   A O      1 
ATOM   5264  C  CB     . ALA   A 1 328 ? 21.293  -4.281  52.175 1.00 39.84  ?  353 ALA   A CB     1 
ATOM   5265  H  H      . ALA   A 1 328 ? 22.854  -4.986  53.895 1.00 46.88  ?  353 ALA   A H      1 
ATOM   5266  H  HA     . ALA   A 1 328 ? 20.412  -4.210  54.031 1.00 46.69  ?  353 ALA   A HA     1 
ATOM   5267  H  HB1    . ALA   A 1 328 ? 20.482  -4.071  51.686 1.00 47.80  ?  353 ALA   A HB1    1 
ATOM   5268  H  HB2    . ALA   A 1 328 ? 21.813  -3.474  52.317 1.00 47.80  ?  353 ALA   A HB2    1 
ATOM   5269  H  HB3    . ALA   A 1 328 ? 21.818  -4.931  51.682 1.00 47.80  ?  353 ALA   A HB3    1 
ATOM   5270  N  N      . HIS   A 1 329 ? 20.606  -7.250  53.034 1.00 34.13  ?  354 HIS   A N      1 
ATOM   5271  C  CA     . HIS   A 1 329 ? 19.773  -8.416  52.758 1.00 33.90  ?  354 HIS   A CA     1 
ATOM   5272  C  C      . HIS   A 1 329 ? 18.961  -8.814  53.987 1.00 32.50  ?  354 HIS   A C      1 
ATOM   5273  O  O      . HIS   A 1 329 ? 17.862  -9.360  53.849 1.00 32.55  ?  354 HIS   A O      1 
ATOM   5274  C  CB     . HIS   A 1 329 ? 20.626  -9.586  52.249 1.00 35.48  ?  354 HIS   A CB     1 
ATOM   5275  C  CG     . HIS   A 1 329 ? 21.355  -10.335 53.319 1.00 37.04  ?  354 HIS   A CG     1 
ATOM   5276  N  ND1    . HIS   A 1 329 ? 22.653  -10.046 53.678 1.00 37.51  ?  354 HIS   A ND1    1 
ATOM   5277  C  CD2    . HIS   A 1 329 ? 20.971  -11.374 54.097 1.00 38.25  ?  354 HIS   A CD2    1 
ATOM   5278  C  CE1    . HIS   A 1 329 ? 23.035  -10.867 54.640 1.00 37.67  ?  354 HIS   A CE1    1 
ATOM   5279  N  NE2    . HIS   A 1 329 ? 22.032  -11.681 54.915 1.00 39.09  ?  354 HIS   A NE2    1 
ATOM   5280  H  H      . HIS   A 1 329 ? 21.455  -7.381  52.978 1.00 40.94  ?  354 HIS   A H      1 
ATOM   5281  H  HA     . HIS   A 1 329 ? 19.150  -8.197  52.048 1.00 40.68  ?  354 HIS   A HA     1 
ATOM   5282  H  HB2    . HIS   A 1 329 ? 20.046  -10.215 51.794 1.00 42.56  ?  354 HIS   A HB2    1 
ATOM   5283  H  HB3    . HIS   A 1 329 ? 21.289  -9.239  51.631 1.00 42.56  ?  354 HIS   A HB3    1 
ATOM   5284  H  HD2    . HIS   A 1 329 ? 20.145  -11.800 54.081 1.00 45.89  ?  354 HIS   A HD2    1 
ATOM   5285  H  HE1    . HIS   A 1 329 ? 23.868  -10.871 55.053 1.00 45.20  ?  354 HIS   A HE1    1 
ATOM   5286  H  HE2    . HIS   A 1 329 ? 22.041  -12.302 55.510 1.00 46.90  ?  354 HIS   A HE2    1 
ATOM   5287  N  N      . GLN   A 1 330 ? 19.463  -8.516  55.189 1.00 32.94  ?  355 GLN   A N      1 
ATOM   5288  C  CA     . GLN   A 1 330 ? 18.717  -8.833  56.404 1.00 32.60  ?  355 GLN   A CA     1 
ATOM   5289  C  C      . GLN   A 1 330 ? 17.472  -7.969  56.528 1.00 31.01  ?  355 GLN   A C      1 
ATOM   5290  O  O      . GLN   A 1 330 ? 16.409  -8.451  56.934 1.00 32.27  ?  355 GLN   A O      1 
ATOM   5291  C  CB     . GLN   A 1 330 ? 19.608  -8.642  57.628 1.00 35.28  ?  355 GLN   A CB     1 
ATOM   5292  C  CG     . GLN   A 1 330 ? 20.834  -9.512  57.632 1.00 39.30  ?  355 GLN   A CG     1 
ATOM   5293  C  CD     . GLN   A 1 330 ? 21.752  -9.202  58.801 1.00 43.58  ?  355 GLN   A CD     1 
ATOM   5294  O  OE1    . GLN   A 1 330 ? 22.696  -8.423  58.677 1.00 44.98  ?  355 GLN   A OE1    1 
ATOM   5295  N  NE2    . GLN   A 1 330 ? 21.469  -9.806  59.948 1.00 45.57  ?  355 GLN   A NE2    1 
ATOM   5296  H  H      . GLN   A 1 330 ? 20.221  -8.134  55.326 1.00 39.52  ?  355 GLN   A H      1 
ATOM   5297  H  HA     . GLN   A 1 330 ? 18.444  -9.763  56.364 1.00 39.12  ?  355 GLN   A HA     1 
ATOM   5298  H  HB2    . GLN   A 1 330 ? 19.902  -7.718  57.658 1.00 42.32  ?  355 GLN   A HB2    1 
ATOM   5299  H  HB3    . GLN   A 1 330 ? 19.094  -8.852  58.423 1.00 42.32  ?  355 GLN   A HB3    1 
ATOM   5300  H  HG2    . GLN   A 1 330 ? 20.564  -10.442 57.698 1.00 47.16  ?  355 GLN   A HG2    1 
ATOM   5301  H  HG3    . GLN   A 1 330 ? 21.330  -9.368  56.811 1.00 47.16  ?  355 GLN   A HG3    1 
ATOM   5302  H  HE21   . GLN   A 1 330 ? 20.796  -10.339 59.999 1.00 54.68  ?  355 GLN   A HE21   1 
ATOM   5303  H  HE22   . GLN   A 1 330 ? 21.959  -9.664  60.641 1.00 54.68  ?  355 GLN   A HE22   1 
ATOM   5304  N  N      . VAL   A 1 331 ? 17.585  -6.688  56.196 1.00 29.74  ?  356 VAL   A N      1 
ATOM   5305  C  CA     . VAL   A 1 331 ? 16.409  -5.825  56.170 1.00 30.16  ?  356 VAL   A CA     1 
ATOM   5306  C  C      . VAL   A 1 331 ? 15.438  -6.303  55.097 1.00 29.19  ?  356 VAL   A C      1 
ATOM   5307  O  O      . VAL   A 1 331 ? 14.230  -6.432  55.325 1.00 28.90  ?  356 VAL   A O      1 
ATOM   5308  C  CB     . VAL   A 1 331 ? 16.827  -4.360  55.948 1.00 33.10  ?  356 VAL   A CB     1 
ATOM   5309  C  CG1    . VAL   A 1 331 ? 15.600  -3.478  55.744 1.00 33.85  ?  356 VAL   A CG1    1 
ATOM   5310  C  CG2    . VAL   A 1 331 ? 17.666  -3.881  57.132 1.00 35.84  ?  356 VAL   A CG2    1 
ATOM   5311  H  H      . VAL   A 1 331 ? 18.322  -6.298  55.983 1.00 35.68  ?  356 VAL   A H      1 
ATOM   5312  H  HA     . VAL   A 1 331 ? 15.959  -5.879  57.028 1.00 36.18  ?  356 VAL   A HA     1 
ATOM   5313  H  HB     . VAL   A 1 331 ? 17.367  -4.291  55.145 1.00 39.71  ?  356 VAL   A HB     1 
ATOM   5314  H  HG11   . VAL   A 1 331 ? 15.859  -2.548  55.847 1.00 40.61  ?  356 VAL   A HG11   1 
ATOM   5315  H  HG12   . VAL   A 1 331 ? 15.250  -3.626  54.851 1.00 40.61  ?  356 VAL   A HG12   1 
ATOM   5316  H  HG13   . VAL   A 1 331 ? 14.930  -3.710  56.405 1.00 40.61  ?  356 VAL   A HG13   1 
ATOM   5317  H  HG21   . VAL   A 1 331 ? 18.382  -3.316  56.804 1.00 43.00  ?  356 VAL   A HG21   1 
ATOM   5318  H  HG22   . VAL   A 1 331 ? 17.099  -3.379  57.738 1.00 43.00  ?  356 VAL   A HG22   1 
ATOM   5319  H  HG23   . VAL   A 1 331 ? 18.035  -4.653  57.589 1.00 43.00  ?  356 VAL   A HG23   1 
ATOM   5320  N  N      . LYS   A 1 332 ? 15.959  -6.581  53.903 1.00 27.50  ?  357 LYS   A N      1 
ATOM   5321  C  CA     . LYS   A 1 332 ? 15.081  -6.930  52.793 1.00 28.16  ?  357 LYS   A CA     1 
ATOM   5322  C  C      . LYS   A 1 332 ? 14.312  -8.210  53.076 1.00 27.30  ?  357 LYS   A C      1 
ATOM   5323  O  O      . LYS   A 1 332 ? 13.172  -8.362  52.628 1.00 27.88  ?  357 LYS   A O      1 
ATOM   5324  C  CB     . LYS   A 1 332 ? 15.914  -7.037  51.521 1.00 30.25  ?  357 LYS   A CB     1 
ATOM   5325  C  CG     . LYS   A 1 332 ? 15.108  -6.885  50.276 1.00 30.65  ?  357 LYS   A CG     1 
ATOM   5326  C  CD     . LYS   A 1 332 ? 15.987  -6.639  49.075 1.00 31.48  ?  357 LYS   A CD     1 
ATOM   5327  C  CE     . LYS   A 1 332 ? 15.128  -6.644  47.841 1.00 31.74  ?  357 LYS   A CE     1 
ATOM   5328  N  NZ     . LYS   A 1 332 ? 15.918  -6.422  46.623 1.00 33.92  ?  357 LYS   A NZ     1 
ATOM   5329  H  H      . LYS   A 1 332 ? 16.798  -6.574  53.714 1.00 32.99  ?  357 LYS   A H      1 
ATOM   5330  H  HA     . LYS   A 1 332 ? 14.420  -6.233  52.656 1.00 33.79  ?  357 LYS   A HA     1 
ATOM   5331  H  HB2    . LYS   A 1 332 ? 16.588  -6.339  51.527 1.00 36.29  ?  357 LYS   A HB2    1 
ATOM   5332  H  HB3    . LYS   A 1 332 ? 16.339  -7.908  51.496 1.00 36.29  ?  357 LYS   A HB3    1 
ATOM   5333  H  HG2    . LYS   A 1 332 ? 14.600  -7.697  50.121 1.00 36.77  ?  357 LYS   A HG2    1 
ATOM   5334  H  HG3    . LYS   A 1 332 ? 14.506  -6.131  50.373 1.00 36.77  ?  357 LYS   A HG3    1 
ATOM   5335  H  HD2    . LYS   A 1 332 ? 16.423  -5.776  49.155 1.00 37.76  ?  357 LYS   A HD2    1 
ATOM   5336  H  HD3    . LYS   A 1 332 ? 16.652  -7.341  49.001 1.00 37.76  ?  357 LYS   A HD3    1 
ATOM   5337  H  HE2    . LYS   A 1 332 ? 14.685  -7.503  47.763 1.00 38.08  ?  357 LYS   A HE2    1 
ATOM   5338  H  HE3    . LYS   A 1 332 ? 14.468  -5.935  47.907 1.00 38.08  ?  357 LYS   A HE3    1 
ATOM   5339  H  HZ1    . LYS   A 1 332 ? 16.336  -5.638  46.669 1.00 40.70  ?  357 LYS   A HZ1    1 
ATOM   5340  H  HZ2    . LYS   A 1 332 ? 16.523  -7.068  46.531 1.00 40.70  ?  357 LYS   A HZ2    1 
ATOM   5341  H  HZ3    . LYS   A 1 332 ? 15.385  -6.423  45.910 1.00 40.70  ?  357 LYS   A HZ3    1 
ATOM   5342  N  N      . ASN   A 1 333 ? 14.881  -9.121  53.851 1.00 27.44  ?  358 ASN   A N      1 
ATOM   5343  C  CA     . ASN   A 1 333 ? 14.175  -10.385 54.024 1.00 29.32  ?  358 ASN   A CA     1 
ATOM   5344  C  C      . ASN   A 1 333 ? 12.967  -10.270 54.943 1.00 27.71  ?  358 ASN   A C      1 
ATOM   5345  O  O      . ASN   A 1 333 ? 12.197  -11.231 55.027 1.00 28.32  ?  358 ASN   A O      1 
ATOM   5346  C  CB     . ASN   A 1 333 ? 15.160  -11.455 54.482 1.00 35.00  ?  358 ASN   A CB     1 
ATOM   5347  C  CG     . ASN   A 1 333 ? 15.853  -12.137 53.296 1.00 39.92  ?  358 ASN   A CG     1 
ATOM   5348  O  OD1    . ASN   A 1 333 ? 15.222  -12.445 52.260 1.00 41.35  ?  358 ASN   A OD1    1 
ATOM   5349  N  ND2    . ASN   A 1 333 ? 17.159  -12.347 53.421 1.00 41.80  ?  358 ASN   A ND2    1 
ATOM   5350  H  H      . ASN   A 1 333 ? 15.631  -9.038  54.264 1.00 32.92  ?  358 ASN   A H      1 
ATOM   5351  H  HA     . ASN   A 1 333 ? 13.823  -10.688 53.172 1.00 35.18  ?  358 ASN   A HA     1 
ATOM   5352  H  HB2    . ASN   A 1 333 ? 15.842  -11.045 55.037 1.00 42.00  ?  358 ASN   A HB2    1 
ATOM   5353  H  HB3    . ASN   A 1 333 ? 14.684  -12.133 54.986 1.00 42.00  ?  358 ASN   A HB3    1 
ATOM   5354  H  HD21   . ASN   A 1 333 ? 17.597  -12.726 52.786 1.00 50.15  ?  358 ASN   A HD21   1 
ATOM   5355  H  HD22   . ASN   A 1 333 ? 17.567  -12.104 54.139 1.00 50.15  ?  358 ASN   A HD22   1 
ATOM   5356  N  N      . HIS   A 1 334 ? 12.717  -9.108  55.545 1.00 26.93  ?  359 HIS   A N      1 
ATOM   5357  C  CA     . HIS   A 1 334 ? 11.482  -8.869  56.276 1.00 26.66  ?  359 HIS   A CA     1 
ATOM   5358  C  C      . HIS   A 1 334 ? 10.385  -8.203  55.450 1.00 25.42  ?  359 HIS   A C      1 
ATOM   5359  O  O      . HIS   A 1 334 ? 9.299   -7.943  55.986 1.00 26.55  ?  359 HIS   A O      1 
ATOM   5360  C  CB     . HIS   A 1 334 ? 11.759  -7.976  57.480 1.00 30.29  ?  359 HIS   A CB     1 
ATOM   5361  C  CG     . HIS   A 1 334 ? 12.513  -8.650  58.575 1.00 33.81  ?  359 HIS   A CG     1 
ATOM   5362  N  ND1    . HIS   A 1 334 ? 11.890  -9.432  59.520 1.00 36.72  ?  359 HIS   A ND1    1 
ATOM   5363  C  CD2    . HIS   A 1 334 ? 13.828  -8.644  58.894 1.00 36.59  ?  359 HIS   A CD2    1 
ATOM   5364  C  CE1    . HIS   A 1 334 ? 12.789  -9.880  60.378 1.00 38.24  ?  359 HIS   A CE1    1 
ATOM   5365  N  NE2    . HIS   A 1 334 ? 13.973  -9.414  60.023 1.00 38.43  ?  359 HIS   A NE2    1 
ATOM   5366  H  H      . HIS   A 1 334 ? 13.256  -8.438  55.543 1.00 32.31  ?  359 HIS   A H      1 
ATOM   5367  H  HA     . HIS   A 1 334 ? 11.153  -9.732  56.572 1.00 31.99  ?  359 HIS   A HA     1 
ATOM   5368  H  HB2    . HIS   A 1 334 ? 12.282  -7.214  57.188 1.00 36.34  ?  359 HIS   A HB2    1 
ATOM   5369  H  HB3    . HIS   A 1 334 ? 10.912  -7.677  57.847 1.00 36.34  ?  359 HIS   A HB3    1 
ATOM   5370  H  HD2    . HIS   A 1 334 ? 14.506  -8.202  58.436 1.00 43.90  ?  359 HIS   A HD2    1 
ATOM   5371  H  HE1    . HIS   A 1 334 ? 12.617  -10.431 61.108 1.00 45.88  ?  359 HIS   A HE1    1 
ATOM   5372  H  HE2    . HIS   A 1 334 ? 14.713  -9.568  60.432 1.00 46.11  ?  359 HIS   A HE2    1 
ATOM   5373  N  N      . MET   A 1 335 ? 10.627  -7.908  54.180 1.00 23.80  ?  360 MET   A N      1 
ATOM   5374  C  CA     . MET   A 1 335 ? 9.716   -7.089  53.397 1.00 21.92  ?  360 MET   A CA     1 
ATOM   5375  C  C      . MET   A 1 335 ? 8.848   -7.913  52.454 1.00 20.76  ?  360 MET   A C      1 
ATOM   5376  O  O      . MET   A 1 335 ? 9.326   -8.842  51.799 1.00 21.16  ?  360 MET   A O      1 
ATOM   5377  C  CB     . MET   A 1 335 ? 10.505  -6.066  52.574 1.00 23.29  ?  360 MET   A CB     1 
ATOM   5378  C  CG     . MET   A 1 335 ? 11.271  -5.046  53.398 1.00 26.76  ?  360 MET   A CG     1 
ATOM   5379  S  SD     . MET   A 1 335 ? 12.404  -4.060  52.407 1.00 30.13  ?  360 MET   A SD     1 
ATOM   5380  C  CE     . MET   A 1 335 ? 11.355  -3.488  51.076 1.00 29.02  ?  360 MET   A CE     1 
ATOM   5381  H  H      . MET   A 1 335 ? 11.321  -8.174  53.746 1.00 28.55  ?  360 MET   A H      1 
ATOM   5382  H  HA     . MET   A 1 335 ? 9.126   -6.636  54.020 1.00 26.30  ?  360 MET   A HA     1 
ATOM   5383  H  HB2    . MET   A 1 335 ? 11.148  -6.541  52.025 1.00 27.94  ?  360 MET   A HB2    1 
ATOM   5384  H  HB3    . MET   A 1 335 ? 9.883   -5.578  52.010 1.00 27.94  ?  360 MET   A HB3    1 
ATOM   5385  H  HG2    . MET   A 1 335 ? 10.640  -4.444  53.821 1.00 32.11  ?  360 MET   A HG2    1 
ATOM   5386  H  HG3    . MET   A 1 335 ? 11.790  -5.511  54.073 1.00 32.11  ?  360 MET   A HG3    1 
ATOM   5387  H  HE1    . MET   A 1 335 ? 11.842  -2.836  50.548 1.00 34.82  ?  360 MET   A HE1    1 
ATOM   5388  H  HE2    . MET   A 1 335 ? 11.109  -4.245  50.521 1.00 34.82  ?  360 MET   A HE2    1 
ATOM   5389  H  HE3    . MET   A 1 335 ? 10.560  -3.081  51.453 1.00 34.82  ?  360 MET   A HE3    1 
ATOM   5390  N  N      . TRP   A 1 336 ? 7.574   -7.528  52.358 1.00 19.17  ?  361 TRP   A N      1 
ATOM   5391  C  CA     . TRP   A 1 336 ? 6.644   -8.001  51.332 1.00 19.66  ?  361 TRP   A CA     1 
ATOM   5392  C  C      . TRP   A 1 336 ? 6.146   -6.767  50.591 1.00 19.93  ?  361 TRP   A C      1 
ATOM   5393  O  O      . TRP   A 1 336 ? 5.416   -5.951  51.163 1.00 20.80  ?  361 TRP   A O      1 
ATOM   5394  C  CB     . TRP   A 1 336 ? 5.490   -8.770  51.965 1.00 20.36  ?  361 TRP   A CB     1 
ATOM   5395  C  CG     . TRP   A 1 336 ? 4.518   -9.422  51.013 1.00 20.45  ?  361 TRP   A CG     1 
ATOM   5396  C  CD1    . TRP   A 1 336 ? 4.544   -9.420  49.644 1.00 20.53  ?  361 TRP   A CD1    1 
ATOM   5397  C  CD2    . TRP   A 1 336 ? 3.371   -10.192 51.390 1.00 21.03  ?  361 TRP   A CD2    1 
ATOM   5398  N  NE1    . TRP   A 1 336 ? 3.479   -10.144 49.155 1.00 21.86  ?  361 TRP   A NE1    1 
ATOM   5399  C  CE2    . TRP   A 1 336 ? 2.742   -10.622 50.207 1.00 22.10  ?  361 TRP   A CE2    1 
ATOM   5400  C  CE3    . TRP   A 1 336 ? 2.811   -10.547 52.616 1.00 23.24  ?  361 TRP   A CE3    1 
ATOM   5401  C  CZ2    . TRP   A 1 336 ? 1.575   -11.394 50.214 1.00 23.52  ?  361 TRP   A CZ2    1 
ATOM   5402  C  CZ3    . TRP   A 1 336 ? 1.657   -11.318 52.624 1.00 24.60  ?  361 TRP   A CZ3    1 
ATOM   5403  C  CH2    . TRP   A 1 336 ? 1.052   -11.732 51.431 1.00 24.99  ?  361 TRP   A CH2    1 
ATOM   5404  H  H      . TRP   A 1 336 ? 7.210   -6.968  52.900 1.00 23.00  ?  361 TRP   A H      1 
ATOM   5405  H  HA     . TRP   A 1 336 ? 7.091   -8.593  50.706 1.00 23.59  ?  361 TRP   A HA     1 
ATOM   5406  H  HB2    . TRP   A 1 336 ? 5.864   -9.475  52.517 1.00 24.42  ?  361 TRP   A HB2    1 
ATOM   5407  H  HB3    . TRP   A 1 336 ? 4.982   -8.153  52.514 1.00 24.42  ?  361 TRP   A HB3    1 
ATOM   5408  H  HD1    . TRP   A 1 336 ? 5.185   -8.994  49.123 1.00 24.63  ?  361 TRP   A HD1    1 
ATOM   5409  H  HE1    . TRP   A 1 336 ? 3.305   -10.275 48.323 1.00 26.22  ?  361 TRP   A HE1    1 
ATOM   5410  H  HE3    . TRP   A 1 336 ? 3.203   -10.273 53.414 1.00 27.88  ?  361 TRP   A HE3    1 
ATOM   5411  H  HZ2    . TRP   A 1 336 ? 1.171   -11.666 49.422 1.00 28.22  ?  361 TRP   A HZ2    1 
ATOM   5412  H  HZ3    . TRP   A 1 336 ? 1.278   -11.564 53.437 1.00 29.52  ?  361 TRP   A HZ3    1 
ATOM   5413  H  HH2    . TRP   A 1 336 ? 0.279   -12.248 51.467 1.00 29.98  ?  361 TRP   A HH2    1 
ATOM   5414  N  N      . ILE   A 1 337 ? 6.536   -6.612  49.331 1.00 18.05  ?  362 ILE   A N      1 
ATOM   5415  C  CA     . ILE   A 1 337 ? 6.261   -5.393  48.581 1.00 17.30  ?  362 ILE   A CA     1 
ATOM   5416  C  C      . ILE   A 1 337 ? 5.371   -5.708  47.381 1.00 16.90  ?  362 ILE   A C      1 
ATOM   5417  O  O      . ILE   A 1 337 ? 5.486   -6.772  46.762 1.00 16.71  ?  362 ILE   A O      1 
ATOM   5418  C  CB     . ILE   A 1 337 ? 7.587   -4.703  48.174 1.00 18.93  ?  362 ILE   A CB     1 
ATOM   5419  C  CG1    . ILE   A 1 337 ? 7.304   -3.262  47.749 1.00 22.67  ?  362 ILE   A CG1    1 
ATOM   5420  C  CG2    . ILE   A 1 337 ? 8.316   -5.473  47.095 1.00 19.05  ?  362 ILE   A CG2    1 
ATOM   5421  C  CD1    . ILE   A 1 337 ? 8.545   -2.444  47.533 1.00 26.17  ?  362 ILE   A CD1    1 
ATOM   5422  H  H      . ILE   A 1 337 ? 6.966   -7.208  48.883 1.00 21.65  ?  362 ILE   A H      1 
ATOM   5423  H  HA     . ILE   A 1 337 ? 5.750   -4.777  49.129 1.00 20.76  ?  362 ILE   A HA     1 
ATOM   5424  H  HB     . ILE   A 1 337 ? 8.175   -4.691  48.946 1.00 22.70  ?  362 ILE   A HB     1 
ATOM   5425  H  HG12   . ILE   A 1 337 ? 6.808   -3.273  46.916 1.00 27.20  ?  362 ILE   A HG12   1 
ATOM   5426  H  HG13   . ILE   A 1 337 ? 6.780   -2.829  48.442 1.00 27.20  ?  362 ILE   A HG13   1 
ATOM   5427  H  HG21   . ILE   A 1 337 ? 9.213   -5.116  47.004 1.00 22.85  ?  362 ILE   A HG21   1 
ATOM   5428  H  HG22   . ILE   A 1 337 ? 8.355   -6.409  47.347 1.00 22.85  ?  362 ILE   A HG22   1 
ATOM   5429  H  HG23   . ILE   A 1 337 ? 7.835   -5.375  46.258 1.00 22.85  ?  362 ILE   A HG23   1 
ATOM   5430  H  HD11   . ILE   A 1 337 ? 8.349   -1.514  47.728 1.00 31.40  ?  362 ILE   A HD11   1 
ATOM   5431  H  HD12   . ILE   A 1 337 ? 9.243   -2.766  48.126 1.00 31.40  ?  362 ILE   A HD12   1 
ATOM   5432  H  HD13   . ILE   A 1 337 ? 8.828   -2.535  46.610 1.00 31.40  ?  362 ILE   A HD13   1 
ATOM   5433  N  N      . PHE   A 1 338 ? 4.441   -4.790  47.102 1.00 16.92  ?  363 PHE   A N      1 
ATOM   5434  C  CA     . PHE   A 1 338 ? 3.545   -4.823  45.952 1.00 16.31  ?  363 PHE   A CA     1 
ATOM   5435  C  C      . PHE   A 1 338 ? 3.837   -3.589  45.107 1.00 16.96  ?  363 PHE   A C      1 
ATOM   5436  O  O      . PHE   A 1 338 ? 3.866   -2.479  45.643 1.00 18.54  ?  363 PHE   A O      1 
ATOM   5437  C  CB     . PHE   A 1 338 ? 2.066   -4.783  46.386 1.00 16.62  ?  363 PHE   A CB     1 
ATOM   5438  C  CG     . PHE   A 1 338 ? 1.600   -5.985  47.183 1.00 18.07  ?  363 PHE   A CG     1 
ATOM   5439  C  CD1    . PHE   A 1 338 ? 1.978   -6.161  48.505 1.00 20.50  ?  363 PHE   A CD1    1 
ATOM   5440  C  CD2    . PHE   A 1 338 ? 0.731   -6.915  46.613 1.00 19.36  ?  363 PHE   A CD2    1 
ATOM   5441  C  CE1    . PHE   A 1 338 ? 1.532   -7.263  49.235 1.00 21.30  ?  363 PHE   A CE1    1 
ATOM   5442  C  CE2    . PHE   A 1 338 ? 0.270   -8.003  47.343 1.00 20.62  ?  363 PHE   A CE2    1 
ATOM   5443  C  CZ     . PHE   A 1 338 ? 0.667   -8.173  48.654 1.00 20.75  ?  363 PHE   A CZ     1 
ATOM   5444  H  H      . PHE   A 1 338 ? 4.306   -4.100  47.596 1.00 20.30  ?  363 PHE   A H      1 
ATOM   5445  H  HA     . PHE   A 1 338 ? 3.696   -5.634  45.441 1.00 19.57  ?  363 PHE   A HA     1 
ATOM   5446  H  HB2    . PHE   A 1 338 ? 1.929   -3.998  46.938 1.00 19.94  ?  363 PHE   A HB2    1 
ATOM   5447  H  HB3    . PHE   A 1 338 ? 1.513   -4.730  45.591 1.00 19.94  ?  363 PHE   A HB3    1 
ATOM   5448  H  HD1    . PHE   A 1 338 ? 2.536   -5.537  48.911 1.00 24.59  ?  363 PHE   A HD1    1 
ATOM   5449  H  HD2    . PHE   A 1 338 ? 0.456   -6.805  45.731 1.00 23.22  ?  363 PHE   A HD2    1 
ATOM   5450  H  HE1    . PHE   A 1 338 ? 1.817   -7.387  50.111 1.00 25.56  ?  363 PHE   A HE1    1 
ATOM   5451  H  HE2    . PHE   A 1 338 ? -0.307  -8.617  46.949 1.00 24.74  ?  363 PHE   A HE2    1 
ATOM   5452  H  HZ     . PHE   A 1 338 ? 0.354   -8.897  49.146 1.00 24.90  ?  363 PHE   A HZ     1 
ATOM   5453  N  N      . VAL   A 1 339 ? 4.043   -3.771  43.799 1.00 15.83  ?  364 VAL   A N      1 
ATOM   5454  C  CA     . VAL   A 1 339 ? 4.406   -2.673  42.899 1.00 15.57  ?  364 VAL   A CA     1 
ATOM   5455  C  C      . VAL   A 1 339 ? 3.622   -2.816  41.604 1.00 15.24  ?  364 VAL   A C      1 
ATOM   5456  O  O      . VAL   A 1 339 ? 3.705   -3.852  40.939 1.00 17.26  ?  364 VAL   A O      1 
ATOM   5457  C  CB     . VAL   A 1 339 ? 5.918   -2.657  42.587 1.00 15.95  ?  364 VAL   A CB     1 
ATOM   5458  C  CG1    . VAL   A 1 339 ? 6.281   -1.510  41.629 1.00 18.15  ?  364 VAL   A CG1    1 
ATOM   5459  C  CG2    . VAL   A 1 339 ? 6.715   -2.575  43.872 1.00 18.34  ?  364 VAL   A CG2    1 
ATOM   5460  H  H      . VAL   A 1 339 ? 3.976   -4.532  43.404 1.00 18.99  ?  364 VAL   A H      1 
ATOM   5461  H  HA     . VAL   A 1 339 ? 4.155   -1.835  43.317 1.00 18.68  ?  364 VAL   A HA     1 
ATOM   5462  H  HB     . VAL   A 1 339 ? 6.153   -3.484  42.137 1.00 19.13  ?  364 VAL   A HB     1 
ATOM   5463  H  HG11   . VAL   A 1 339 ? 7.246   -1.415  41.602 1.00 21.78  ?  364 VAL   A HG11   1 
ATOM   5464  H  HG12   . VAL   A 1 339 ? 5.944   -1.719  40.744 1.00 21.78  ?  364 VAL   A HG12   1 
ATOM   5465  H  HG13   . VAL   A 1 339 ? 5.877   -0.689  41.952 1.00 21.78  ?  364 VAL   A HG13   1 
ATOM   5466  H  HG21   . VAL   A 1 339 ? 7.656   -2.490  43.655 1.00 22.00  ?  364 VAL   A HG21   1 
ATOM   5467  H  HG22   . VAL   A 1 339 ? 6.421   -1.801  44.377 1.00 22.00  ?  364 VAL   A HG22   1 
ATOM   5468  H  HG23   . VAL   A 1 339 ? 6.566   -3.383  44.388 1.00 22.00  ?  364 VAL   A HG23   1 
ATOM   5469  N  N      . ASN   A 1 340 ? 2.874   -1.784  41.234 1.00 15.94  ?  365 ASN   A N      1 
ATOM   5470  C  CA     . ASN   A 1 340 ? 2.231   -1.702  39.925 1.00 15.60  ?  365 ASN   A CA     1 
ATOM   5471  C  C      . ASN   A 1 340 ? 2.872   -0.553  39.154 1.00 16.05  ?  365 ASN   A C      1 
ATOM   5472  O  O      . ASN   A 1 340 ? 2.793   0.601   39.591 1.00 16.99  ?  365 ASN   A O      1 
ATOM   5473  C  CB     . ASN   A 1 340 ? 0.726   -1.489  40.072 1.00 16.92  ?  365 ASN   A CB     1 
ATOM   5474  C  CG     . ASN   A 1 340 ? -0.018  -1.688  38.775 1.00 16.74  ?  365 ASN   A CG     1 
ATOM   5475  O  OD1    . ASN   A 1 340 ? 0.358   -2.513  37.952 1.00 16.69  ?  365 ASN   A OD1    1 
ATOM   5476  N  ND2    . ASN   A 1 340 ? -1.087  -0.931  38.585 1.00 17.19  ?  365 ASN   A ND2    1 
ATOM   5477  H  H      . ASN   A 1 340 ? 2.720   -1.102  41.734 1.00 19.13  ?  365 ASN   A H      1 
ATOM   5478  H  HA     . ASN   A 1 340 ? 2.371   -2.524  39.430 1.00 18.72  ?  365 ASN   A HA     1 
ATOM   5479  H  HB2    . ASN   A 1 340 ? 0.378   -2.124  40.718 1.00 20.30  ?  365 ASN   A HB2    1 
ATOM   5480  H  HB3    . ASN   A 1 340 ? 0.563   -0.583  40.376 1.00 20.30  ?  365 ASN   A HB3    1 
ATOM   5481  H  HD21   . ASN   A 1 340 ? -1.545  -1.007  37.861 1.00 20.62  ?  365 ASN   A HD21   1 
ATOM   5482  H  HD22   . ASN   A 1 340 ? -1.324  -0.362  39.185 1.00 20.62  ?  365 ASN   A HD22   1 
ATOM   5483  N  N      . ALA   A 1 341 ? 3.515   -0.860  38.022 1.00 16.38  ?  366 ALA   A N      1 
ATOM   5484  C  CA     . ALA   A 1 341 ? 4.288   0.139   37.294 1.00 14.77  ?  366 ALA   A CA     1 
ATOM   5485  C  C      . ALA   A 1 341 ? 3.969   0.160   35.808 1.00 14.71  ?  366 ALA   A C      1 
ATOM   5486  O  O      . ALA   A 1 341 ? 3.654   -0.871  35.208 1.00 16.30  ?  366 ALA   A O      1 
ATOM   5487  C  CB     . ALA   A 1 341 ? 5.809   -0.104  37.449 1.00 17.25  ?  366 ALA   A CB     1 
ATOM   5488  H  H      . ALA   A 1 341 ? 3.515   -1.640  37.661 1.00 19.65  ?  366 ALA   A H      1 
ATOM   5489  H  HA     . ALA   A 1 341 ? 4.039   1.004   37.655 1.00 17.72  ?  366 ALA   A HA     1 
ATOM   5490  H  HB1    . ALA   A 1 341 ? 6.289   0.573   36.948 1.00 20.69  ?  366 ALA   A HB1    1 
ATOM   5491  H  HB2    . ALA   A 1 341 ? 6.043   -0.049  38.389 1.00 20.69  ?  366 ALA   A HB2    1 
ATOM   5492  H  HB3    . ALA   A 1 341 ? 6.024   -0.985  37.105 1.00 20.69  ?  366 ALA   A HB3    1 
ATOM   5493  N  N      . LEU   A 1 342 ? 4.071   1.364   35.224 1.00 15.91  ?  367 LEU   A N      1 
ATOM   5494  C  CA     . LEU   A 1 342 ? 4.032   1.587   33.781 1.00 16.65  ?  367 LEU   A CA     1 
ATOM   5495  C  C      . LEU   A 1 342 ? 5.422   2.050   33.341 1.00 16.96  ?  367 LEU   A C      1 
ATOM   5496  O  O      . LEU   A 1 342 ? 5.902   3.103   33.790 1.00 17.31  ?  367 LEU   A O      1 
ATOM   5497  C  CB     . LEU   A 1 342 ? 2.967   2.621   33.398 1.00 18.05  ?  367 LEU   A CB     1 
ATOM   5498  C  CG     . LEU   A 1 342 ? 1.516   2.150   33.551 1.00 19.26  ?  367 LEU   A CG     1 
ATOM   5499  C  CD1    . LEU   A 1 342 ? 0.528   3.277   33.246 1.00 20.47  ?  367 LEU   A CD1    1 
ATOM   5500  C  CD2    . LEU   A 1 342 ? 1.222   0.950   32.661 1.00 21.43  ?  367 LEU   A CD2    1 
ATOM   5501  H  H      . LEU   A 1 342 ? 4.167   2.094   35.668 1.00 19.08  ?  367 LEU   A H      1 
ATOM   5502  H  HA     . LEU   A 1 342 ? 3.812   0.760   33.325 1.00 19.97  ?  367 LEU   A HA     1 
ATOM   5503  H  HB2    . LEU   A 1 342 ? 3.080   3.400   33.964 1.00 21.65  ?  367 LEU   A HB2    1 
ATOM   5504  H  HB3    . LEU   A 1 342 ? 3.097   2.864   32.468 1.00 21.65  ?  367 LEU   A HB3    1 
ATOM   5505  H  HG     . LEU   A 1 342 ? 1.394   1.880   34.474 1.00 23.11  ?  367 LEU   A HG     1 
ATOM   5506  H  HD11   . LEU   A 1 342 ? -0.376  2.945   33.364 1.00 24.56  ?  367 LEU   A HD11   1 
ATOM   5507  H  HD12   . LEU   A 1 342 ? 0.692   4.014   33.855 1.00 24.56  ?  367 LEU   A HD12   1 
ATOM   5508  H  HD13   . LEU   A 1 342 ? 0.656   3.570   32.330 1.00 24.56  ?  367 LEU   A HD13   1 
ATOM   5509  H  HD21   . LEU   A 1 342 ? 0.265   0.790   32.653 1.00 25.71  ?  367 LEU   A HD21   1 
ATOM   5510  H  HD22   . LEU   A 1 342 ? 1.533   1.140   31.762 1.00 25.71  ?  367 LEU   A HD22   1 
ATOM   5511  H  HD23   . LEU   A 1 342 ? 1.684   0.174   33.014 1.00 25.71  ?  367 LEU   A HD23   1 
ATOM   5512  N  N      . ILE   A 1 343 ? 6.056   1.251   32.479 1.00 16.49  ?  368 ILE   A N      1 
ATOM   5513  C  CA     . ILE   A 1 343 ? 7.450   1.408   32.071 1.00 15.65  ?  368 ILE   A CA     1 
ATOM   5514  C  C      . ILE   A 1 343 ? 7.487   1.584   30.559 1.00 16.54  ?  368 ILE   A C      1 
ATOM   5515  O  O      . ILE   A 1 343 ? 6.854   0.812   29.841 1.00 17.11  ?  368 ILE   A O      1 
ATOM   5516  C  CB     . ILE   A 1 343 ? 8.281   0.173   32.469 1.00 15.77  ?  368 ILE   A CB     1 
ATOM   5517  C  CG1    . ILE   A 1 343 ? 8.173   -0.127  33.961 1.00 18.02  ?  368 ILE   A CG1    1 
ATOM   5518  C  CG2    . ILE   A 1 343 ? 9.712   0.327   31.991 1.00 17.01  ?  368 ILE   A CG2    1 
ATOM   5519  C  CD1    . ILE   A 1 343 ? 8.750   0.918   34.861 1.00 19.18  ?  368 ILE   A CD1    1 
ATOM   5520  H  H      . ILE   A 1 343 ? 5.678   0.578   32.100 1.00 19.78  ?  368 ILE   A H      1 
ATOM   5521  H  HA     . ILE   A 1 343 ? 7.821   2.200   32.490 1.00 18.78  ?  368 ILE   A HA     1 
ATOM   5522  H  HB     . ILE   A 1 343 ? 7.911   -0.604  32.022 1.00 18.92  ?  368 ILE   A HB     1 
ATOM   5523  H  HG12   . ILE   A 1 343 ? 7.234   -0.220  34.188 1.00 21.61  ?  368 ILE   A HG12   1 
ATOM   5524  H  HG13   . ILE   A 1 343 ? 8.641   -0.957  34.141 1.00 21.61  ?  368 ILE   A HG13   1 
ATOM   5525  H  HG21   . ILE   A 1 343 ? 10.270  -0.317  32.453 1.00 20.40  ?  368 ILE   A HG21   1 
ATOM   5526  H  HG22   . ILE   A 1 343 ? 9.744   0.168   31.035 1.00 20.40  ?  368 ILE   A HG22   1 
ATOM   5527  H  HG23   . ILE   A 1 343 ? 10.015  1.228   32.186 1.00 20.40  ?  368 ILE   A HG23   1 
ATOM   5528  H  HD11   . ILE   A 1 343 ? 8.639   0.637   35.783 1.00 23.01  ?  368 ILE   A HD11   1 
ATOM   5529  H  HD12   . ILE   A 1 343 ? 9.693   1.022   34.659 1.00 23.01  ?  368 ILE   A HD12   1 
ATOM   5530  H  HD13   . ILE   A 1 343 ? 8.285   1.755   34.711 1.00 23.01  ?  368 ILE   A HD13   1 
ATOM   5531  N  N      . GLU   A 1 344 ? 8.256   2.553   30.068 1.00 17.16  ?  369 GLU   A N      1 
ATOM   5532  C  CA     . GLU   A 1 344 ? 8.387   2.732   28.623 1.00 17.38  ?  369 GLU   A CA     1 
ATOM   5533  C  C      . GLU   A 1 344 ? 9.296   1.673   28.014 1.00 17.88  ?  369 GLU   A C      1 
ATOM   5534  O  O      . GLU   A 1 344 ? 10.406  1.437   28.498 1.00 18.49  ?  369 GLU   A O      1 
ATOM   5535  C  CB     . GLU   A 1 344 ? 8.930   4.126   28.298 1.00 18.71  ?  369 GLU   A CB     1 
ATOM   5536  C  CG     . GLU   A 1 344 ? 7.922   5.199   28.659 1.00 20.54  ?  369 GLU   A CG     1 
ATOM   5537  C  CD     . GLU   A 1 344 ? 8.378   6.631   28.435 1.00 22.88  ?  369 GLU   A CD     1 
ATOM   5538  O  OE1    . GLU   A 1 344 ? 9.529   6.871   28.003 1.00 23.90  ?  369 GLU   A OE1    1 
ATOM   5539  O  OE2    . GLU   A 1 344 ? 7.540   7.528   28.723 1.00 23.57  ?  369 GLU   A OE2    1 
ATOM   5540  H  H      . GLU   A 1 344 ? 8.706   3.111   30.543 1.00 20.59  ?  369 GLU   A H      1 
ATOM   5541  H  HA     . GLU   A 1 344 ? 7.508   2.637   28.226 1.00 20.85  ?  369 GLU   A HA     1 
ATOM   5542  H  HB2    . GLU   A 1 344 ? 9.742   4.283   28.805 1.00 22.45  ?  369 GLU   A HB2    1 
ATOM   5543  H  HB3    . GLU   A 1 344 ? 9.116   4.186   27.348 1.00 22.45  ?  369 GLU   A HB3    1 
ATOM   5544  H  HG2    . GLU   A 1 344 ? 7.126   5.063   28.122 1.00 24.64  ?  369 GLU   A HG2    1 
ATOM   5545  H  HG3    . GLU   A 1 344 ? 7.706   5.110   29.601 1.00 24.64  ?  369 GLU   A HG3    1 
ATOM   5546  N  N      . ASN   A 1 345 ? 8.817   1.035   26.947 1.00 18.26  ?  370 ASN   A N      1 
ATOM   5547  C  CA     . ASN   A 1 345 ? 9.580   0.096   26.129 1.00 19.30  ?  370 ASN   A CA     1 
ATOM   5548  C  C      . ASN   A 1 345 ? 10.445  -0.837  26.990 1.00 17.73  ?  370 ASN   A C      1 
ATOM   5549  O  O      . ASN   A 1 345 ? 11.662  -0.902  26.816 1.00 18.78  ?  370 ASN   A O      1 
ATOM   5550  C  CB     . ASN   A 1 345 ? 10.432  0.842   25.110 1.00 21.26  ?  370 ASN   A CB     1 
ATOM   5551  C  CG     . ASN   A 1 345 ? 9.590   1.665   24.157 1.00 24.04  ?  370 ASN   A CG     1 
ATOM   5552  O  OD1    . ASN   A 1 345 ? 8.374   1.490   24.072 1.00 24.64  ?  370 ASN   A OD1    1 
ATOM   5553  N  ND2    . ASN   A 1 345 ? 10.229  2.583   23.449 1.00 25.73  ?  370 ASN   A ND2    1 
ATOM   5554  H  H      . ASN   A 1 345 ? 8.011   1.137   26.665 1.00 21.91  ?  370 ASN   A H      1 
ATOM   5555  H  HA     . ASN   A 1 345 ? 8.957   -0.468  25.646 1.00 23.16  ?  370 ASN   A HA     1 
ATOM   5556  H  HB2    . ASN   A 1 345 ? 11.035  1.442   25.576 1.00 25.50  ?  370 ASN   A HB2    1 
ATOM   5557  H  HB3    . ASN   A 1 345 ? 10.940  0.201   24.588 1.00 25.50  ?  370 ASN   A HB3    1 
ATOM   5558  H  HD21   . ASN   A 1 345 ? 9.796   3.076   22.894 1.00 30.87  ?  370 ASN   A HD21   1 
ATOM   5559  H  HD22   . ASN   A 1 345 ? 11.078  2.686   23.544 1.00 30.87  ?  370 ASN   A HD22   1 
ATOM   5560  N  N      . PRO   A 1 346 ? 9.826   -1.603  27.875 1.00 16.93  ?  371 PRO   A N      1 
ATOM   5561  C  CA     . PRO   A 1 346 ? 10.603  -2.462  28.769 1.00 16.32  ?  371 PRO   A CA     1 
ATOM   5562  C  C      . PRO   A 1 346 ? 11.317  -3.593  28.049 1.00 16.77  ?  371 PRO   A C      1 
ATOM   5563  O  O      . PRO   A 1 346 ? 10.896  -4.062  26.988 1.00 18.18  ?  371 PRO   A O      1 
ATOM   5564  C  CB     . PRO   A 1 346 ? 9.542   -3.016  29.731 1.00 16.66  ?  371 PRO   A CB     1 
ATOM   5565  C  CG     . PRO   A 1 346 ? 8.255   -2.968  28.918 1.00 16.19  ?  371 PRO   A CG     1 
ATOM   5566  C  CD     . PRO   A 1 346 ? 8.375   -1.689  28.127 1.00 16.56  ?  371 PRO   A CD     1 
ATOM   5567  H  HA     . PRO   A 1 346 ? 11.260  -1.930  29.245 1.00 19.57  ?  371 PRO   A HA     1 
ATOM   5568  H  HB2    . PRO   A 1 346 ? 9.763   -3.925  29.987 1.00 19.98  ?  371 PRO   A HB2    1 
ATOM   5569  H  HB3    . PRO   A 1 346 ? 9.480   -2.455  30.521 1.00 19.98  ?  371 PRO   A HB3    1 
ATOM   5570  H  HG2    . PRO   A 1 346 ? 8.201   -3.739  28.332 1.00 19.43  ?  371 PRO   A HG2    1 
ATOM   5571  H  HG3    . PRO   A 1 346 ? 7.486   -2.945  29.509 1.00 19.43  ?  371 PRO   A HG3    1 
ATOM   5572  H  HD2    . PRO   A 1 346 ? 7.880   -1.746  27.295 1.00 19.86  ?  371 PRO   A HD2    1 
ATOM   5573  H  HD3    . PRO   A 1 346 ? 8.066   -0.929  28.645 1.00 19.86  ?  371 PRO   A HD3    1 
ATOM   5574  N  N      . THR   A 1 347 ? 12.407  -4.043  28.665 1.00 16.99  ?  372 THR   A N      1 
ATOM   5575  C  CA     . THR   A 1 347 ? 13.144  -5.223  28.253 1.00 16.67  ?  372 THR   A CA     1 
ATOM   5576  C  C      . THR   A 1 347 ? 13.027  -6.283  29.339 1.00 15.30  ?  372 THR   A C      1 
ATOM   5577  O  O      . THR   A 1 347 ? 12.842  -5.969  30.522 1.00 15.80  ?  372 THR   A O      1 
ATOM   5578  C  CB     . THR   A 1 347 ? 14.624  -4.908  27.989 1.00 17.36  ?  372 THR   A CB     1 
ATOM   5579  O  OG1    . THR   A 1 347 ? 15.238  -4.307  29.136 1.00 17.33  ?  372 THR   A OG1    1 
ATOM   5580  C  CG2    . THR   A 1 347 ? 14.761  -3.954  26.812 1.00 18.30  ?  372 THR   A CG2    1 
ATOM   5581  H  H      . THR   A 1 347 ? 12.750  -3.661  29.355 1.00 20.38  ?  372 THR   A H      1 
ATOM   5582  H  HA     . THR   A 1 347 ? 12.773  -5.570  27.427 1.00 20.00  ?  372 THR   A HA     1 
ATOM   5583  H  HB     . THR   A 1 347 ? 15.081  -5.740  27.787 1.00 20.82  ?  372 THR   A HB     1 
ATOM   5584  H  HG1    . THR   A 1 347 ? 15.208  -4.835  29.788 1.00 20.79  ?  372 THR   A HG1    1 
ATOM   5585  H  HG21   . THR   A 1 347 ? 15.698  -3.763  26.647 1.00 21.95  ?  372 THR   A HG21   1 
ATOM   5586  H  HG22   . THR   A 1 347 ? 14.376  -4.352  26.016 1.00 21.95  ?  372 THR   A HG22   1 
ATOM   5587  H  HG23   . THR   A 1 347 ? 14.299  -3.123  27.004 1.00 21.95  ?  372 THR   A HG23   1 
ATOM   5588  N  N      . PHE   A 1 348 ? 13.130  -7.542  28.918 1.00 15.65  ?  373 PHE   A N      1 
ATOM   5589  C  CA     . PHE   A 1 348 ? 13.022  -8.699  29.793 1.00 15.02  ?  373 PHE   A CA     1 
ATOM   5590  C  C      . PHE   A 1 348 ? 14.051  -9.743  29.358 1.00 16.31  ?  373 PHE   A C      1 
ATOM   5591  O  O      . PHE   A 1 348 ? 14.592  -9.674  28.253 1.00 17.72  ?  373 PHE   A O      1 
ATOM   5592  C  CB     . PHE   A 1 348 ? 11.613  -9.317  29.744 1.00 15.96  ?  373 PHE   A CB     1 
ATOM   5593  C  CG     . PHE   A 1 348 ? 10.471  -8.346  30.012 1.00 15.64  ?  373 PHE   A CG     1 
ATOM   5594  C  CD1    . PHE   A 1 348 ? 9.962   -7.532  29.003 1.00 15.58  ?  373 PHE   A CD1    1 
ATOM   5595  C  CD2    . PHE   A 1 348 ? 9.874   -8.289  31.266 1.00 15.18  ?  373 PHE   A CD2    1 
ATOM   5596  C  CE1    . PHE   A 1 348 ? 8.911   -6.664  29.254 1.00 16.59  ?  373 PHE   A CE1    1 
ATOM   5597  C  CE2    . PHE   A 1 348 ? 8.812   -7.437  31.501 1.00 16.18  ?  373 PHE   A CE2    1 
ATOM   5598  C  CZ     . PHE   A 1 348 ? 8.330   -6.634  30.492 1.00 17.10  ?  373 PHE   A CZ     1 
ATOM   5599  H  H      . PHE   A 1 348 ? 13.269  -7.757  28.097 1.00 18.77  ?  373 PHE   A H      1 
ATOM   5600  H  HA     . PHE   A 1 348 ? 13.212  -8.422  30.704 1.00 18.02  ?  373 PHE   A HA     1 
ATOM   5601  H  HB2    . PHE   A 1 348 ? 11.474  -9.692  28.860 1.00 19.15  ?  373 PHE   A HB2    1 
ATOM   5602  H  HB3    . PHE   A 1 348 ? 11.562  -10.018 30.413 1.00 19.15  ?  373 PHE   A HB3    1 
ATOM   5603  H  HD1    . PHE   A 1 348 ? 10.331  -7.571  28.150 1.00 18.69  ?  373 PHE   A HD1    1 
ATOM   5604  H  HD2    . PHE   A 1 348 ? 10.193  -8.829  31.953 1.00 18.21  ?  373 PHE   A HD2    1 
ATOM   5605  H  HE1    . PHE   A 1 348 ? 8.601   -6.103  28.581 1.00 19.90  ?  373 PHE   A HE1    1 
ATOM   5606  H  HE2    . PHE   A 1 348 ? 8.420   -7.407  32.344 1.00 19.41  ?  373 PHE   A HE2    1 
ATOM   5607  H  HZ     . PHE   A 1 348 ? 7.608   -6.069  30.652 1.00 20.52  ?  373 PHE   A HZ     1 
ATOM   5608  N  N      . ASP   A 1 349 ? 14.291  -10.743 30.222 1.00 15.98  ?  374 ASP   A N      1 
ATOM   5609  C  CA     . ASP   A 1 349 ? 15.207  -11.832 29.878 1.00 17.01  ?  374 ASP   A CA     1 
ATOM   5610  C  C      . ASP   A 1 349 ? 14.653  -12.744 28.785 1.00 16.07  ?  374 ASP   A C      1 
ATOM   5611  O  O      . ASP   A 1 349 ? 15.425  -13.390 28.058 1.00 18.37  ?  374 ASP   A O      1 
ATOM   5612  C  CB     . ASP   A 1 349 ? 15.501  -12.725 31.088 1.00 20.39  ?  374 ASP   A CB     1 
ATOM   5613  C  CG     . ASP   A 1 349 ? 16.394  -12.086 32.112 1.00 23.33  ?  374 ASP   A CG     1 
ATOM   5614  O  OD1    . ASP   A 1 349 ? 17.315  -11.325 31.729 1.00 23.29  ?  374 ASP   A OD1    1 
ATOM   5615  O  OD2    . ASP   A 1 349 ? 16.172  -12.365 33.313 1.00 24.25  ?  374 ASP   A OD2    1 
ATOM   5616  H  H      . ASP   A 1 349 ? 13.938  -10.811 31.004 1.00 19.17  ?  374 ASP   A H      1 
ATOM   5617  H  HA     . ASP   A 1 349 ? 16.024  -11.403 29.577 1.00 20.41  ?  374 ASP   A HA     1 
ATOM   5618  H  HB2    . ASP   A 1 349 ? 14.663  -12.946 31.524 1.00 24.46  ?  374 ASP   A HB2    1 
ATOM   5619  H  HB3    . ASP   A 1 349 ? 15.937  -13.535 30.780 1.00 24.46  ?  374 ASP   A HB3    1 
ATOM   5620  N  N      . SER   A 1 350 ? 13.329  -12.864 28.696 1.00 16.02  ?  375 SER   A N      1 
ATOM   5621  C  CA     . SER   A 1 350 ? 12.703  -13.871 27.853 1.00 16.29  ?  375 SER   A CA     1 
ATOM   5622  C  C      . SER   A 1 350 ? 11.340  -13.380 27.374 1.00 15.05  ?  375 SER   A C      1 
ATOM   5623  O  O      . SER   A 1 350 ? 10.792  -12.392 27.872 1.00 15.15  ?  375 SER   A O      1 
ATOM   5624  C  CB     . SER   A 1 350 ? 12.543  -15.197 28.604 1.00 19.94  ?  375 SER   A CB     1 
ATOM   5625  O  OG     . SER   A 1 350 ? 11.484  -15.086 29.530 1.00 22.65  ?  375 SER   A OG     1 
ATOM   5626  H  H      . SER   A 1 350 ? 12.769  -12.367 29.119 1.00 19.22  ?  375 SER   A H      1 
ATOM   5627  H  HA     . SER   A 1 350 ? 13.265  -14.005 27.074 1.00 19.55  ?  375 SER   A HA     1 
ATOM   5628  H  HB2    . SER   A 1 350 ? 12.344  -15.904 27.971 1.00 23.92  ?  375 SER   A HB2    1 
ATOM   5629  H  HB3    . SER   A 1 350 ? 13.365  -15.400 29.079 1.00 23.92  ?  375 SER   A HB3    1 
ATOM   5630  H  HG     . SER   A 1 350 ? 11.652  -14.480 30.088 1.00 27.17  ?  375 SER   A HG     1 
ATOM   5631  N  N      . GLN   A 1 351 ? 10.801  -14.101 26.385 1.00 16.98  ?  376 GLN   A N      1 
ATOM   5632  C  CA     . GLN   A 1 351 ? 9.452   -13.828 25.900 1.00 16.97  ?  376 GLN   A CA     1 
ATOM   5633  C  C      . GLN   A 1 351 ? 8.408   -13.908 27.012 1.00 16.05  ?  376 GLN   A C      1 
ATOM   5634  O  O      . GLN   A 1 351 ? 7.356   -13.259 26.911 1.00 17.10  ?  376 GLN   A O      1 
ATOM   5635  C  CB     . GLN   A 1 351 ? 9.093   -14.814 24.779 1.00 18.74  ?  376 GLN   A CB     1 
ATOM   5636  C  CG     . GLN   A 1 351 ? 7.646   -14.725 24.271 1.00 19.65  ?  376 GLN   A CG     1 
ATOM   5637  C  CD     . GLN   A 1 351 ? 7.316   -13.393 23.592 1.00 20.43  ?  376 GLN   A CD     1 
ATOM   5638  O  OE1    . GLN   A 1 351 ? 8.185   -12.756 22.994 1.00 22.00  ?  376 GLN   A OE1    1 
ATOM   5639  N  NE2    . GLN   A 1 351 ? 6.064   -12.973 23.687 1.00 20.68  ?  376 GLN   A NE2    1 
ATOM   5640  H  H      . GLN   A 1 351 ? 11.195  -14.750 25.981 1.00 20.37  ?  376 GLN   A H      1 
ATOM   5641  H  HA     . GLN   A 1 351 ? 9.434   -12.926 25.544 1.00 20.36  ?  376 GLN   A HA     1 
ATOM   5642  H  HB2    . GLN   A 1 351 ? 9.677   -14.644 24.023 1.00 22.48  ?  376 GLN   A HB2    1 
ATOM   5643  H  HB3    . GLN   A 1 351 ? 9.231   -15.716 25.108 1.00 22.48  ?  376 GLN   A HB3    1 
ATOM   5644  H  HG2    . GLN   A 1 351 ? 7.497   -15.432 23.624 1.00 23.57  ?  376 GLN   A HG2    1 
ATOM   5645  H  HG3    . GLN   A 1 351 ? 7.043   -14.832 25.023 1.00 23.57  ?  376 GLN   A HG3    1 
ATOM   5646  H  HE21   . GLN   A 1 351 ? 5.483   -13.443 24.113 1.00 24.81  ?  376 GLN   A HE21   1 
ATOM   5647  H  HE22   . GLN   A 1 351 ? 5.830   -12.230 23.321 1.00 24.81  ?  376 GLN   A HE22   1 
ATOM   5648  N  N      . THR   A 1 352 ? 8.654   -14.710 28.060 1.00 15.82  ?  377 THR   A N      1 
ATOM   5649  C  CA     . THR   A 1 352 ? 7.644   -14.868 29.104 1.00 15.37  ?  377 THR   A CA     1 
ATOM   5650  C  C      . THR   A 1 352 ? 7.551   -13.641 30.014 1.00 15.67  ?  377 THR   A C      1 
ATOM   5651  O  O      . THR   A 1 352 ? 6.575   -13.515 30.755 1.00 16.66  ?  377 THR   A O      1 
ATOM   5652  C  CB     . THR   A 1 352 ? 7.901   -16.114 29.978 1.00 16.48  ?  377 THR   A CB     1 
ATOM   5653  O  OG1    . THR   A 1 352 ? 9.175   -16.003 30.627 1.00 18.52  ?  377 THR   A OG1    1 
ATOM   5654  C  CG2    . THR   A 1 352 ? 7.812   -17.400 29.154 1.00 17.78  ?  377 THR   A CG2    1 
ATOM   5655  H  H      . THR   A 1 352 ? 9.378   -15.159 28.182 1.00 18.98  ?  377 THR   A H      1 
ATOM   5656  H  HA     . THR   A 1 352 ? 6.795   -15.001 28.654 1.00 18.44  ?  377 THR   A HA     1 
ATOM   5657  H  HB     . THR   A 1 352 ? 7.216   -16.172 30.661 1.00 19.77  ?  377 THR   A HB     1 
ATOM   5658  H  HG1    . THR   A 1 352 ? 9.787   -15.960 30.054 1.00 22.22  ?  377 THR   A HG1    1 
ATOM   5659  H  HG21   . THR   A 1 352 ? 7.959   -18.170 29.725 1.00 21.33  ?  377 THR   A HG21   1 
ATOM   5660  H  HG22   . THR   A 1 352 ? 6.935   -17.473 28.747 1.00 21.33  ?  377 THR   A HG22   1 
ATOM   5661  H  HG23   . THR   A 1 352 ? 8.485   -17.393 28.455 1.00 21.33  ?  377 THR   A HG23   1 
ATOM   5662  N  N      . LYS   A 1 353 ? 8.561   -12.761 29.992 1.00 15.13  ?  378 LYS   A N      1 
ATOM   5663  C  CA     . LYS   A 1 353 ? 8.516   -11.436 30.625 1.00 14.36  ?  378 LYS   A CA     1 
ATOM   5664  C  C      . LYS   A 1 353 ? 8.290   -11.521 32.135 1.00 14.20  ?  378 LYS   A C      1 
ATOM   5665  O  O      . LYS   A 1 353 ? 7.553   -10.721 32.727 1.00 16.09  ?  378 LYS   A O      1 
ATOM   5666  C  CB     . LYS   A 1 353 ? 7.465   -10.540 29.963 1.00 15.49  ?  378 LYS   A CB     1 
ATOM   5667  C  CG     . LYS   A 1 353 ? 7.685   -10.324 28.465 1.00 17.11  ?  378 LYS   A CG     1 
ATOM   5668  C  CD     . LYS   A 1 353 ? 6.506   -9.557  27.864 1.00 20.59  ?  378 LYS   A CD     1 
ATOM   5669  C  CE     . LYS   A 1 353 ? 6.403   -9.657  26.373 1.00 25.17  ?  378 LYS   A CE     1 
ATOM   5670  N  NZ     . LYS   A 1 353 ? 5.126   -9.023  25.872 1.00 26.06  ?  378 LYS   A NZ     1 
ATOM   5671  H  H      . LYS   A 1 353 ? 9.312   -12.914 29.601 1.00 18.15  ?  378 LYS   A H      1 
ATOM   5672  H  HA     . LYS   A 1 353 ? 9.385   -11.024 30.500 1.00 17.23  ?  378 LYS   A HA     1 
ATOM   5673  H  HB2    . LYS   A 1 353 ? 6.592   -10.948 30.077 1.00 18.58  ?  378 LYS   A HB2    1 
ATOM   5674  H  HB3    . LYS   A 1 353 ? 7.483   -9.670  30.392 1.00 18.58  ?  378 LYS   A HB3    1 
ATOM   5675  H  HG2    . LYS   A 1 353 ? 8.495   -9.808  28.325 1.00 20.52  ?  378 LYS   A HG2    1 
ATOM   5676  H  HG3    . LYS   A 1 353 ? 7.757   -11.182 28.019 1.00 20.52  ?  378 LYS   A HG3    1 
ATOM   5677  H  HD2    . LYS   A 1 353 ? 5.683   -9.908  28.239 1.00 24.70  ?  378 LYS   A HD2    1 
ATOM   5678  H  HD3    . LYS   A 1 353 ? 6.599   -8.618  28.089 1.00 24.70  ?  378 LYS   A HD3    1 
ATOM   5679  H  HE2    . LYS   A 1 353 ? 7.154   -9.197  25.966 1.00 30.20  ?  378 LYS   A HE2    1 
ATOM   5680  H  HE3    . LYS   A 1 353 ? 6.404   -10.591 26.112 1.00 30.20  ?  378 LYS   A HE3    1 
ATOM   5681  H  HZ1    . LYS   A 1 353 ? 5.079   -9.094  24.986 1.00 31.26  ?  378 LYS   A HZ1    1 
ATOM   5682  H  HZ2    . LYS   A 1 353 ? 4.422   -9.430  26.233 1.00 31.26  ?  378 LYS   A HZ2    1 
ATOM   5683  H  HZ3    . LYS   A 1 353 ? 5.107   -8.161  26.095 1.00 31.26  ?  378 LYS   A HZ3    1 
ATOM   5684  N  N      . GLU   A 1 354 ? 8.988   -12.455 32.774 1.00 14.89  ?  379 GLU   A N      1 
ATOM   5685  C  CA     . GLU   A 1 354 ? 8.927   -12.594 34.217 1.00 14.85  ?  379 GLU   A CA     1 
ATOM   5686  C  C      . GLU   A 1 354 ? 9.918   -11.707 34.950 1.00 13.57  ?  379 GLU   A C      1 
ATOM   5687  O  O      . GLU   A 1 354 ? 9.682   -11.403 36.125 1.00 14.58  ?  379 GLU   A O      1 
ATOM   5688  C  CB     . GLU   A 1 354 ? 9.147   -14.059 34.602 1.00 17.55  ?  379 GLU   A CB     1 
ATOM   5689  C  CG     . GLU   A 1 354 ? 8.014   -14.939 34.064 1.00 20.42  ?  379 GLU   A CG     1 
ATOM   5690  C  CD     . GLU   A 1 354 ? 8.208   -16.417 34.265 1.00 27.10  ?  379 GLU   A CD     1 
ATOM   5691  O  OE1    . GLU   A 1 354 ? 9.319   -16.832 34.622 1.00 30.77  ?  379 GLU   A OE1    1 
ATOM   5692  O  OE2    . GLU   A 1 354 ? 7.242   -17.176 34.052 1.00 28.72  ?  379 GLU   A OE2    1 
ATOM   5693  H  H      . GLU   A 1 354 ? 9.507   -13.022 32.388 1.00 17.86  ?  379 GLU   A H      1 
ATOM   5694  H  HA     . GLU   A 1 354 ? 8.044   -12.337 34.524 1.00 17.81  ?  379 GLU   A HA     1 
ATOM   5695  H  HB2    . GLU   A 1 354 ? 9.985   -14.370 34.224 1.00 21.05  ?  379 GLU   A HB2    1 
ATOM   5696  H  HB3    . GLU   A 1 354 ? 9.168   -14.140 35.568 1.00 21.05  ?  379 GLU   A HB3    1 
ATOM   5697  H  HG2    . GLU   A 1 354 ? 7.191   -14.691 34.513 1.00 24.50  ?  379 GLU   A HG2    1 
ATOM   5698  H  HG3    . GLU   A 1 354 ? 7.931   -14.785 33.110 1.00 24.50  ?  379 GLU   A HG3    1 
ATOM   5699  N  N      . ASN   A 1 355 ? 10.997  -11.270 34.289 1.00 13.85  ?  380 ASN   A N      1 
ATOM   5700  C  CA     . ASN   A 1 355 ? 12.036  -10.457 34.913 1.00 13.56  ?  380 ASN   A CA     1 
ATOM   5701  C  C      . ASN   A 1 355 ? 12.324  -9.253  34.031 1.00 13.82  ?  380 ASN   A C      1 
ATOM   5702  O  O      . ASN   A 1 355 ? 12.791  -9.408  32.902 1.00 14.37  ?  380 ASN   A O      1 
ATOM   5703  C  CB     . ASN   A 1 355 ? 13.319  -11.254 35.127 1.00 14.81  ?  380 ASN   A CB     1 
ATOM   5704  C  CG     . ASN   A 1 355 ? 14.374  -10.460 35.863 1.00 18.67  ?  380 ASN   A CG     1 
ATOM   5705  O  OD1    . ASN   A 1 355 ? 14.092  -9.789  36.866 1.00 21.61  ?  380 ASN   A OD1    1 
ATOM   5706  N  ND2    . ASN   A 1 355 ? 15.599  -10.527 35.372 1.00 21.38  ?  380 ASN   A ND2    1 
ATOM   5707  H  H      . ASN   A 1 355 ? 11.148  -11.437 33.459 1.00 16.61  ?  380 ASN   A H      1 
ATOM   5708  H  HA     . ASN   A 1 355 ? 11.711  -10.146 35.773 1.00 16.26  ?  380 ASN   A HA     1 
ATOM   5709  H  HB2    . ASN   A 1 355 ? 13.117  -12.046 35.650 1.00 17.77  ?  380 ASN   A HB2    1 
ATOM   5710  H  HB3    . ASN   A 1 355 ? 13.681  -11.510 34.264 1.00 17.77  ?  380 ASN   A HB3    1 
ATOM   5711  H  HD21   . ASN   A 1 355 ? 16.238  -10.095 35.752 1.00 25.65  ?  380 ASN   A HD21   1 
ATOM   5712  H  HD22   . ASN   A 1 355 ? 15.757  -11.003 34.674 1.00 25.65  ?  380 ASN   A HD22   1 
ATOM   5713  N  N      . MET   A 1 356 ? 12.053  -8.055  34.548 1.00 13.21  ?  381 MET   A N      1 
ATOM   5714  C  CA     . MET   A 1 356 ? 12.155  -6.822  33.774 1.00 14.48  ?  381 MET   A CA     1 
ATOM   5715  C  C      . MET   A 1 356 ? 13.521  -6.179  34.016 1.00 15.00  ?  381 MET   A C      1 
ATOM   5716  O  O      . MET   A 1 356 ? 13.840  -5.796  35.144 1.00 15.94  ?  381 MET   A O      1 
ATOM   5717  C  CB     . MET   A 1 356 ? 11.011  -5.883  34.158 1.00 15.28  ?  381 MET   A CB     1 
ATOM   5718  C  CG     . MET   A 1 356 ? 10.645  -4.863  33.093 1.00 16.78  ?  381 MET   A CG     1 
ATOM   5719  S  SD     . MET   A 1 356 ? 11.795  -3.475  32.899 1.00 16.88  ?  381 MET   A SD     1 
ATOM   5720  C  CE     . MET   A 1 356 ? 11.769  -2.787  34.570 1.00 18.23  ?  381 MET   A CE     1 
ATOM   5721  H  H      . MET   A 1 356 ? 11.804  -7.931  35.361 1.00 15.85  ?  381 MET   A H      1 
ATOM   5722  H  HA     . MET   A 1 356 ? 12.087  -7.015  32.826 1.00 17.37  ?  381 MET   A HA     1 
ATOM   5723  H  HB2    . MET   A 1 356 ? 10.221  -6.417  34.335 1.00 18.33  ?  381 MET   A HB2    1 
ATOM   5724  H  HB3    . MET   A 1 356 ? 11.267  -5.395  34.955 1.00 18.33  ?  381 MET   A HB3    1 
ATOM   5725  H  HG2    . MET   A 1 356 ? 10.600  -5.319  32.238 1.00 20.13  ?  381 MET   A HG2    1 
ATOM   5726  H  HG3    . MET   A 1 356 ? 9.779   -4.489  33.316 1.00 20.13  ?  381 MET   A HG3    1 
ATOM   5727  H  HE1    . MET   A 1 356 ? 12.217  -1.927  34.564 1.00 21.88  ?  381 MET   A HE1    1 
ATOM   5728  H  HE2    . MET   A 1 356 ? 10.847  -2.677  34.852 1.00 21.88  ?  381 MET   A HE2    1 
ATOM   5729  H  HE3    . MET   A 1 356 ? 12.228  -3.395  35.169 1.00 21.88  ?  381 MET   A HE3    1 
ATOM   5730  N  N      . THR   A 1 357 ? 14.322  -6.065  32.953 1.00 14.12  ?  382 THR   A N      1 
ATOM   5731  C  CA     . THR   A 1 357 ? 15.748  -5.775  33.053 1.00 15.22  ?  382 THR   A CA     1 
ATOM   5732  C  C      . THR   A 1 357 ? 16.143  -4.340  32.711 1.00 15.45  ?  382 THR   A C      1 
ATOM   5733  O  O      . THR   A 1 357 ? 17.329  -4.003  32.806 1.00 17.02  ?  382 THR   A O      1 
ATOM   5734  C  CB     . THR   A 1 357 ? 16.516  -6.714  32.115 1.00 15.73  ?  382 THR   A CB     1 
ATOM   5735  O  OG1    . THR   A 1 357 ? 16.058  -6.464  30.781 1.00 17.55  ?  382 THR   A OG1    1 
ATOM   5736  C  CG2    . THR   A 1 357 ? 16.291  -8.172  32.469 1.00 15.78  ?  382 THR   A CG2    1 
ATOM   5737  H  H      . THR   A 1 357 ? 14.052  -6.155  32.141 1.00 16.93  ?  382 THR   A H      1 
ATOM   5738  H  HA     . THR   A 1 357 ? 16.008  -5.928  33.975 1.00 18.26  ?  382 THR   A HA     1 
ATOM   5739  H  HB     . THR   A 1 357 ? 17.470  -6.554  32.190 1.00 18.87  ?  382 THR   A HB     1 
ATOM   5740  H  HG1    . THR   A 1 357 ? 16.470  -6.955  30.238 1.00 21.06  ?  382 THR   A HG1    1 
ATOM   5741  H  HG21   . THR   A 1 357 ? 16.829  -8.740  31.895 1.00 18.93  ?  382 THR   A HG21   1 
ATOM   5742  H  HG22   . THR   A 1 357 ? 16.541  -8.332  33.393 1.00 18.93  ?  382 THR   A HG22   1 
ATOM   5743  H  HG23   . THR   A 1 357 ? 15.356  -8.401  32.352 1.00 18.93  ?  382 THR   A HG23   1 
ATOM   5744  N  N      . LEU   A 1 358 ? 15.199  -3.497  32.316 1.00 15.83  ?  383 LEU   A N      1 
ATOM   5745  C  CA     . LEU   A 1 358 ? 15.515  -2.137  31.896 1.00 16.57  ?  383 LEU   A CA     1 
ATOM   5746  C  C      . LEU   A 1 358 ? 16.030  -1.316  33.069 1.00 17.36  ?  383 LEU   A C      1 
ATOM   5747  O  O      . LEU   A 1 358 ? 15.485  -1.381  34.167 1.00 17.84  ?  383 LEU   A O      1 
ATOM   5748  C  CB     . LEU   A 1 358 ? 14.268  -1.475  31.313 1.00 17.37  ?  383 LEU   A CB     1 
ATOM   5749  C  CG     . LEU   A 1 358 ? 14.440  -0.101  30.674 1.00 18.03  ?  383 LEU   A CG     1 
ATOM   5750  C  CD1    . LEU   A 1 358 ? 15.247  -0.214  29.399 1.00 21.05  ?  383 LEU   A CD1    1 
ATOM   5751  C  CD2    . LEU   A 1 358 ? 13.088  0.534   30.373 1.00 17.54  ?  383 LEU   A CD2    1 
ATOM   5752  H  H      . LEU   A 1 358 ? 14.361  -3.687  32.282 1.00 18.99  ?  383 LEU   A H      1 
ATOM   5753  H  HA     . LEU   A 1 358 ? 16.207  -2.160  31.216 1.00 19.88  ?  383 LEU   A HA     1 
ATOM   5754  H  HB2    . LEU   A 1 358 ? 13.913  -2.063  30.628 1.00 20.84  ?  383 LEU   A HB2    1 
ATOM   5755  H  HB3    . LEU   A 1 358 ? 13.623  -1.373  32.030 1.00 20.84  ?  383 LEU   A HB3    1 
ATOM   5756  H  HG     . LEU   A 1 358 ? 14.914  0.472   31.296 1.00 21.64  ?  383 LEU   A HG     1 
ATOM   5757  H  HD11   . LEU   A 1 358 ? 15.304  0.661   28.983 1.00 25.25  ?  383 LEU   A HD11   1 
ATOM   5758  H  HD12   . LEU   A 1 358 ? 16.136  -0.536  29.615 1.00 25.25  ?  383 LEU   A HD12   1 
ATOM   5759  H  HD13   . LEU   A 1 358 ? 14.806  -0.836  28.800 1.00 25.25  ?  383 LEU   A HD13   1 
ATOM   5760  H  HD21   . LEU   A 1 358 ? 13.230  1.396   29.952 1.00 21.04  ?  383 LEU   A HD21   1 
ATOM   5761  H  HD22   . LEU   A 1 358 ? 12.592  -0.048  29.775 1.00 21.04  ?  383 LEU   A HD22   1 
ATOM   5762  H  HD23   . LEU   A 1 358 ? 12.600  0.647   31.204 1.00 21.04  ?  383 LEU   A HD23   1 
ATOM   5763  N  N      . GLN   A 1 359 ? 17.085  -0.536  32.835 1.00 17.43  ?  384 GLN   A N      1 
ATOM   5764  C  CA     A GLN   A 1 359 ? 17.662  0.284   33.894 0.59 18.30  ?  384 GLN   A CA     1 
ATOM   5765  C  CA     B GLN   A 1 359 ? 17.648  0.271   33.903 0.41 18.01  ?  384 GLN   A CA     1 
ATOM   5766  C  C      . GLN   A 1 359 ? 16.729  1.443   34.249 1.00 17.94  ?  384 GLN   A C      1 
ATOM   5767  O  O      . GLN   A 1 359 ? 16.063  2.002   33.376 1.00 18.58  ?  384 GLN   A O      1 
ATOM   5768  C  CB     A GLN   A 1 359 ? 19.010  0.851   33.471 0.59 21.04  ?  384 GLN   A CB     1 
ATOM   5769  C  CB     B GLN   A 1 359 ? 19.028  0.764   33.516 0.41 19.88  ?  384 GLN   A CB     1 
ATOM   5770  C  CG     A GLN   A 1 359 ? 20.119  -0.173  33.301 0.59 23.19  ?  384 GLN   A CG     1 
ATOM   5771  C  CG     B GLN   A 1 359 ? 20.003  -0.385  33.513 0.41 21.44  ?  384 GLN   A CG     1 
ATOM   5772  C  CD     A GLN   A 1 359 ? 20.728  -0.617  34.625 0.59 24.62  ?  384 GLN   A CD     1 
ATOM   5773  C  CD     B GLN   A 1 359 ? 21.397  0.036   33.174 0.41 21.91  ?  384 GLN   A CD     1 
ATOM   5774  O  OE1    A GLN   A 1 359 ? 20.183  -0.373  35.700 0.59 24.48  ?  384 GLN   A OE1    1 
ATOM   5775  O  OE1    B GLN   A 1 359 ? 22.053  0.746   33.938 0.41 23.39  ?  384 GLN   A OE1    1 
ATOM   5776  N  NE2    A GLN   A 1 359 ? 21.866  -1.288  34.542 0.59 25.32  ?  384 GLN   A NE2    1 
ATOM   5777  N  NE2    B GLN   A 1 359 ? 21.866  -0.397  32.012 0.41 22.60  ?  384 GLN   A NE2    1 
ATOM   5778  H  H      . GLN   A 1 359 ? 17.483  -0.462  32.077 1.00 20.91  ?  384 GLN   A H      1 
ATOM   5779  H  HA     . GLN   A 1 359 ? 17.790  -0.270  34.680 1.00 21.61  ?  384 GLN   A HA     1 
ATOM   5780  H  HB2    A GLN   A 1 359 ? 18.899  1.301   32.619 0.59 25.24  ?  384 GLN   A HB2    1 
ATOM   5781  H  HB2    B GLN   A 1 359 ? 18.999  1.151   32.628 0.41 23.85  ?  384 GLN   A HB2    1 
ATOM   5782  H  HB3    A GLN   A 1 359 ? 19.301  1.485   34.145 0.59 25.24  ?  384 GLN   A HB3    1 
ATOM   5783  H  HB3    B GLN   A 1 359 ? 19.328  1.427   34.158 0.41 23.85  ?  384 GLN   A HB3    1 
ATOM   5784  H  HG2    A GLN   A 1 359 ? 19.758  -0.958  32.860 0.59 27.82  ?  384 GLN   A HG2    1 
ATOM   5785  H  HG2    B GLN   A 1 359 ? 20.019  -0.788  34.396 0.41 25.72  ?  384 GLN   A HG2    1 
ATOM   5786  H  HG3    A GLN   A 1 359 ? 20.826  0.215   32.762 0.59 27.82  ?  384 GLN   A HG3    1 
ATOM   5787  H  HG3    B GLN   A 1 359 ? 19.719  -1.039  32.855 0.41 25.72  ?  384 GLN   A HG3    1 
ATOM   5788  H  HE21   A GLN   A 1 359 ? 22.216  -1.447  33.773 0.59 30.38  ?  384 GLN   A HE21   1 
ATOM   5789  H  HE21   B GLN   A 1 359 ? 21.374  -0.888  31.505 0.41 27.11  ?  384 GLN   A HE21   1 
ATOM   5790  H  HE22   A GLN   A 1 359 ? 22.256  -1.564  35.257 0.59 30.38  ?  384 GLN   A HE22   1 
ATOM   5791  H  HE22   B GLN   A 1 359 ? 22.662  -0.186  31.764 0.41 27.11  ?  384 GLN   A HE22   1 
ATOM   5792  N  N      . PRO   A 1 360 ? 16.677  1.836   35.533 1.00 18.79  ?  385 PRO   A N      1 
ATOM   5793  C  CA     . PRO   A 1 360 ? 15.775  2.940   35.922 1.00 20.61  ?  385 PRO   A CA     1 
ATOM   5794  C  C      . PRO   A 1 360 ? 15.965  4.228   35.128 1.00 19.53  ?  385 PRO   A C      1 
ATOM   5795  O  O      . PRO   A 1 360 ? 14.978  4.930   34.865 1.00 20.75  ?  385 PRO   A O      1 
ATOM   5796  C  CB     . PRO   A 1 360 ? 16.100  3.146   37.414 1.00 22.31  ?  385 PRO   A CB     1 
ATOM   5797  C  CG     . PRO   A 1 360 ? 16.501  1.764   37.888 1.00 21.53  ?  385 PRO   A CG     1 
ATOM   5798  C  CD     . PRO   A 1 360 ? 17.262  1.159   36.712 1.00 20.40  ?  385 PRO   A CD     1 
ATOM   5799  H  HA     . PRO   A 1 360 ? 14.857  2.643   35.820 1.00 24.73  ?  385 PRO   A HA     1 
ATOM   5800  H  HB2    . PRO   A 1 360 ? 16.829  3.777   37.515 1.00 26.77  ?  385 PRO   A HB2    1 
ATOM   5801  H  HB3    . PRO   A 1 360 ? 15.316  3.466   37.887 1.00 26.77  ?  385 PRO   A HB3    1 
ATOM   5802  H  HG2    . PRO   A 1 360 ? 17.069  1.834   38.671 1.00 25.83  ?  385 PRO   A HG2    1 
ATOM   5803  H  HG3    . PRO   A 1 360 ? 15.710  1.242   38.096 1.00 25.83  ?  385 PRO   A HG3    1 
ATOM   5804  H  HD2    . PRO   A 1 360 ? 18.211  1.348   36.782 1.00 24.47  ?  385 PRO   A HD2    1 
ATOM   5805  H  HD3    . PRO   A 1 360 ? 17.118  0.201   36.666 1.00 24.47  ?  385 PRO   A HD3    1 
ATOM   5806  N  N      . LYS   A 1 361 ? 17.193  4.559   34.722 1.00 21.79  ?  386 LYS   A N      1 
ATOM   5807  C  CA     . LYS   A 1 361 ? 17.393  5.795   33.976 1.00 24.85  ?  386 LYS   A CA     1 
ATOM   5808  C  C      . LYS   A 1 361 ? 16.602  5.816   32.671 1.00 22.91  ?  386 LYS   A C      1 
ATOM   5809  O  O      . LYS   A 1 361 ? 16.430  6.889   32.076 1.00 25.37  ?  386 LYS   A O      1 
ATOM   5810  C  CB     . LYS   A 1 361 ? 18.875  6.018   33.665 1.00 27.78  ?  386 LYS   A CB     1 
ATOM   5811  C  CG     . LYS   A 1 361 ? 19.535  4.934   32.828 1.00 29.44  ?  386 LYS   A CG     1 
ATOM   5812  C  CD     . LYS   A 1 361 ? 21.047  5.183   32.749 1.00 34.51  ?  386 LYS   A CD     1 
ATOM   5813  C  CE     . LYS   A 1 361 ? 21.769  4.025   32.109 1.00 41.10  ?  386 LYS   A CE     1 
ATOM   5814  N  NZ     . LYS   A 1 361 ? 22.419  4.416   30.829 1.00 45.64  ?  386 LYS   A NZ     1 
ATOM   5815  H  H      . LYS   A 1 361 ? 17.904  4.096   34.862 1.00 26.14  ?  386 LYS   A H      1 
ATOM   5816  H  HA     . LYS   A 1 361 ? 17.092  6.528   34.536 1.00 29.81  ?  386 LYS   A HA     1 
ATOM   5817  H  HB2    . LYS   A 1 361 ? 18.963  6.853   33.179 1.00 33.33  ?  386 LYS   A HB2    1 
ATOM   5818  H  HB3    . LYS   A 1 361 ? 19.358  6.070   34.504 1.00 33.33  ?  386 LYS   A HB3    1 
ATOM   5819  H  HG2    . LYS   A 1 361 ? 19.382  4.067   33.235 1.00 35.33  ?  386 LYS   A HG2    1 
ATOM   5820  H  HG3    . LYS   A 1 361 ? 19.169  4.946   31.929 1.00 35.33  ?  386 LYS   A HG3    1 
ATOM   5821  H  HD2    . LYS   A 1 361 ? 21.214  5.977   32.217 1.00 41.40  ?  386 LYS   A HD2    1 
ATOM   5822  H  HD3    . LYS   A 1 361 ? 21.399  5.304   33.645 1.00 41.40  ?  386 LYS   A HD3    1 
ATOM   5823  H  HE2    . LYS   A 1 361 ? 22.457  3.704   32.713 1.00 49.31  ?  386 LYS   A HE2    1 
ATOM   5824  H  HE3    . LYS   A 1 361 ? 21.134  3.315   31.923 1.00 49.31  ?  386 LYS   A HE3    1 
ATOM   5825  H  HZ1    . LYS   A 1 361 ? 22.845  3.719   30.478 1.00 54.76  ?  386 LYS   A HZ1    1 
ATOM   5826  H  HZ2    . LYS   A 1 361 ? 21.805  4.700   30.250 1.00 54.76  ?  386 LYS   A HZ2    1 
ATOM   5827  H  HZ3    . LYS   A 1 361 ? 23.004  5.071   30.972 1.00 54.76  ?  386 LYS   A HZ3    1 
ATOM   5828  N  N      . SER   A 1 362 ? 16.103  4.661   32.223 1.00 21.26  ?  387 SER   A N      1 
ATOM   5829  C  CA     . SER   A 1 362 ? 15.358  4.560   30.973 1.00 22.19  ?  387 SER   A CA     1 
ATOM   5830  C  C      . SER   A 1 362 ? 13.872  4.276   31.171 1.00 21.12  ?  387 SER   A C      1 
ATOM   5831  O  O      . SER   A 1 362 ? 13.159  4.061   30.186 1.00 21.79  ?  387 SER   A O      1 
ATOM   5832  C  CB     . SER   A 1 362 ? 15.987  3.473   30.091 1.00 22.98  ?  387 SER   A CB     1 
ATOM   5833  O  OG     . SER   A 1 362 ? 17.346  3.775   29.825 1.00 25.75  ?  387 SER   A OG     1 
ATOM   5834  H  H      . SER   A 1 362 ? 16.186  3.911   32.635 1.00 25.51  ?  387 SER   A H      1 
ATOM   5835  H  HA     . SER   A 1 362 ? 15.420  5.412   30.513 1.00 26.62  ?  387 SER   A HA     1 
ATOM   5836  H  HB2    . SER   A 1 362 ? 15.936  2.622   30.552 1.00 27.58  ?  387 SER   A HB2    1 
ATOM   5837  H  HB3    . SER   A 1 362 ? 15.503  3.426   29.252 1.00 27.58  ?  387 SER   A HB3    1 
ATOM   5838  H  HG     . SER   A 1 362 ? 17.686  3.173   29.347 1.00 30.90  ?  387 SER   A HG     1 
ATOM   5839  N  N      . PHE   A 1 363 ? 13.380  4.292   32.414 1.00 19.49  ?  388 PHE   A N      1 
ATOM   5840  C  CA     . PHE   A 1 363 ? 11.986  3.929   32.655 1.00 18.51  ?  388 PHE   A CA     1 
ATOM   5841  C  C      . PHE   A 1 363 ? 11.009  4.896   31.979 1.00 19.53  ?  388 PHE   A C      1 
ATOM   5842  O  O      . PHE   A 1 363 ? 9.866   4.524   31.679 1.00 20.33  ?  388 PHE   A O      1 
ATOM   5843  C  CB     . PHE   A 1 363 ? 11.660  3.940   34.152 1.00 18.50  ?  388 PHE   A CB     1 
ATOM   5844  C  CG     . PHE   A 1 363 ? 12.221  2.796   34.959 1.00 17.70  ?  388 PHE   A CG     1 
ATOM   5845  C  CD1    . PHE   A 1 363 ? 12.784  1.676   34.366 1.00 17.69  ?  388 PHE   A CD1    1 
ATOM   5846  C  CD2    . PHE   A 1 363 ? 12.128  2.838   36.348 1.00 17.92  ?  388 PHE   A CD2    1 
ATOM   5847  C  CE1    . PHE   A 1 363 ? 13.268  0.637   35.142 1.00 18.10  ?  388 PHE   A CE1    1 
ATOM   5848  C  CE2    . PHE   A 1 363 ? 12.592  1.783   37.129 1.00 19.06  ?  388 PHE   A CE2    1 
ATOM   5849  C  CZ     . PHE   A 1 363 ? 13.166  0.690   36.526 1.00 17.30  ?  388 PHE   A CZ     1 
ATOM   5850  H  H      . PHE   A 1 363 ? 13.824  4.505   33.119 1.00 23.38  ?  388 PHE   A H      1 
ATOM   5851  H  HA     . PHE   A 1 363 ? 11.873  3.034   32.300 1.00 22.21  ?  388 PHE   A HA     1 
ATOM   5852  H  HB2    . PHE   A 1 363 ? 12.012  4.760   34.533 1.00 22.19  ?  388 PHE   A HB2    1 
ATOM   5853  H  HB3    . PHE   A 1 363 ? 10.695  3.916   34.252 1.00 22.19  ?  388 PHE   A HB3    1 
ATOM   5854  H  HD1    . PHE   A 1 363 ? 12.837  1.623   33.439 1.00 21.22  ?  388 PHE   A HD1    1 
ATOM   5855  H  HD2    . PHE   A 1 363 ? 11.751  3.581   36.759 1.00 21.50  ?  388 PHE   A HD2    1 
ATOM   5856  H  HE1    . PHE   A 1 363 ? 13.663  -0.100  34.735 1.00 21.71  ?  388 PHE   A HE1    1 
ATOM   5857  H  HE2    . PHE   A 1 363 ? 12.513  1.817   38.055 1.00 22.87  ?  388 PHE   A HE2    1 
ATOM   5858  H  HZ     . PHE   A 1 363 ? 13.487  -0.012  37.044 1.00 20.76  ?  388 PHE   A HZ     1 
ATOM   5859  N  N      . GLY   A 1 364 ? 11.398  6.159   31.826 1.00 19.47  ?  389 GLY   A N      1 
ATOM   5860  C  CA     . GLY   A 1 364 ? 10.486  7.191   31.391 1.00 20.44  ?  389 GLY   A CA     1 
ATOM   5861  C  C      . GLY   A 1 364 ? 9.739   7.901   32.501 1.00 20.58  ?  389 GLY   A C      1 
ATOM   5862  O  O      . GLY   A 1 364 ? 8.951   8.814   32.214 1.00 23.08  ?  389 GLY   A O      1 
ATOM   5863  H  H      . GLY   A 1 364 ? 12.198  6.440   31.972 1.00 23.35  ?  389 GLY   A H      1 
ATOM   5864  H  HA2    . GLY   A 1 364 ? 10.987  7.860   30.899 1.00 24.52  ?  389 GLY   A HA2    1 
ATOM   5865  H  HA3    . GLY   A 1 364 ? 9.827   6.793   30.800 1.00 24.52  ?  389 GLY   A HA3    1 
ATOM   5866  N  N      . SER   A 1 365 ? 9.955   7.510   33.752 1.00 20.54  ?  390 SER   A N      1 
ATOM   5867  C  CA     . SER   A 1 365 ? 9.317   8.126   34.908 1.00 21.74  ?  390 SER   A CA     1 
ATOM   5868  C  C      . SER   A 1 365 ? 10.165  7.760   36.117 1.00 22.12  ?  390 SER   A C      1 
ATOM   5869  O  O      . SER   A 1 365 ? 11.055  6.909   36.037 1.00 22.28  ?  390 SER   A O      1 
ATOM   5870  C  CB     . SER   A 1 365 ? 7.862   7.665   35.068 1.00 22.45  ?  390 SER   A CB     1 
ATOM   5871  O  OG     . SER   A 1 365 ? 7.763   6.273   35.323 1.00 22.97  ?  390 SER   A OG     1 
ATOM   5872  H  H      . SER   A 1 365 ? 10.485  6.868   33.964 1.00 24.64  ?  390 SER   A H      1 
ATOM   5873  H  HA     . SER   A 1 365 ? 9.298   9.091   34.812 1.00 26.08  ?  390 SER   A HA     1 
ATOM   5874  H  HB2    . SER   A 1 365 ? 7.464   8.145   35.811 1.00 26.93  ?  390 SER   A HB2    1 
ATOM   5875  H  HB3    . SER   A 1 365 ? 7.382   7.864   34.249 1.00 26.93  ?  390 SER   A HB3    1 
ATOM   5876  H  HG     . SER   A 1 365 ? 8.092   5.839   34.683 1.00 27.55  ?  390 SER   A HG     1 
ATOM   5877  N  N      . THR   A 1 366 ? 9.904   8.439   37.230 1.00 23.38  ?  391 THR   A N      1 
ATOM   5878  C  CA     . THR   A 1 366 ? 10.546  8.156   38.503 1.00 23.84  ?  391 THR   A CA     1 
ATOM   5879  C  C      . THR   A 1 366 ? 9.494   7.787   39.538 1.00 24.58  ?  391 THR   A C      1 
ATOM   5880  O  O      . THR   A 1 366 ? 8.289   7.964   39.333 1.00 25.87  ?  391 THR   A O      1 
ATOM   5881  C  CB     . THR   A 1 366 ? 11.361  9.360   38.991 1.00 26.94  ?  391 THR   A CB     1 
ATOM   5882  O  OG1    . THR   A 1 366 ? 10.480  10.438  39.318 1.00 29.26  ?  391 THR   A OG1    1 
ATOM   5883  C  CG2    . THR   A 1 366 ? 12.314  9.796   37.911 1.00 28.69  ?  391 THR   A CG2    1 
ATOM   5884  H  H      . THR   A 1 366 ? 9.341   9.087   37.271 1.00 28.05  ?  391 THR   A H      1 
ATOM   5885  H  HA     . THR   A 1 366 ? 11.149  7.404   38.395 1.00 28.61  ?  391 THR   A HA     1 
ATOM   5886  H  HB     . THR   A 1 366 ? 11.871  9.119   39.781 1.00 32.33  ?  391 THR   A HB     1 
ATOM   5887  H  HG1    . THR   A 1 366 ? 10.035  10.661  38.641 1.00 35.11  ?  391 THR   A HG1    1 
ATOM   5888  H  HG21   . THR   A 1 366 ? 12.916  10.475  38.254 1.00 34.42  ?  391 THR   A HG21   1 
ATOM   5889  H  HG22   . THR   A 1 366 ? 12.836  9.038   37.603 1.00 34.42  ?  391 THR   A HG22   1 
ATOM   5890  H  HG23   . THR   A 1 366 ? 11.820  10.163  37.161 1.00 34.42  ?  391 THR   A HG23   1 
ATOM   5891  N  N      . CYS   A 1 367 ? 9.978   7.251   40.664 1.00 24.86  ?  392 CYS   A N      1 
ATOM   5892  C  CA     . CYS   A 1 367 ? 9.136   6.800   41.767 1.00 25.40  ?  392 CYS   A CA     1 
ATOM   5893  C  C      . CYS   A 1 367 ? 9.925   7.042   43.057 1.00 28.74  ?  392 CYS   A C      1 
ATOM   5894  O  O      . CYS   A 1 367 ? 10.500  6.138   43.661 1.00 30.24  ?  392 CYS   A O      1 
ATOM   5895  C  CB     . CYS   A 1 367 ? 8.751   5.326   41.624 1.00 25.09  ?  392 CYS   A CB     1 
ATOM   5896  S  SG     . CYS   A 1 367 ? 7.609   4.730   42.902 1.00 25.55  ?  392 CYS   A SG     1 
ATOM   5897  H  H      . CYS   A 1 367 ? 10.817  7.135   40.813 1.00 29.82  ?  392 CYS   A H      1 
ATOM   5898  H  HA     . CYS   A 1 367 ? 8.323   7.329   41.793 1.00 30.48  ?  392 CYS   A HA     1 
ATOM   5899  H  HB2    . CYS   A 1 367 ? 8.322   5.199   40.764 1.00 30.11  ?  392 CYS   A HB2    1 
ATOM   5900  H  HB3    . CYS   A 1 367 ? 9.556   4.788   41.676 1.00 30.11  ?  392 CYS   A HB3    1 
ATOM   5901  H  HG     . CYS   A 1 367 ? 7.374   3.570   42.705 1.00 30.65  ?  392 CYS   A HG     1 
ATOM   5902  N  N      . GLN   A 1 368 ? 9.976   8.293   43.496 1.00 32.06  ?  393 GLN   A N      1 
ATOM   5903  C  CA     A GLN   A 1 368 ? 10.594  8.623   44.778 0.53 33.19  ?  393 GLN   A CA     1 
ATOM   5904  C  CA     B GLN   A 1 368 ? 10.594  8.623   44.775 0.47 33.15  ?  393 GLN   A CA     1 
ATOM   5905  C  C      . GLN   A 1 368 ? 9.499   8.593   45.841 1.00 32.91  ?  393 GLN   A C      1 
ATOM   5906  O  O      . GLN   A 1 368 ? 8.583   9.423   45.826 1.00 34.56  ?  393 GLN   A O      1 
ATOM   5907  C  CB     A GLN   A 1 368 ? 11.297  9.977   44.747 0.53 35.51  ?  393 GLN   A CB     1 
ATOM   5908  C  CB     B GLN   A 1 368 ? 11.299  9.973   44.709 0.47 35.27  ?  393 GLN   A CB     1 
ATOM   5909  C  CG     A GLN   A 1 368 ? 12.283  10.172  45.917 0.53 38.40  ?  393 GLN   A CG     1 
ATOM   5910  C  CG     B GLN   A 1 368 ? 12.430  10.030  43.666 0.47 37.66  ?  393 GLN   A CG     1 
ATOM   5911  C  CD     A GLN   A 1 368 ? 13.524  9.285   45.809 0.53 42.48  ?  393 GLN   A CD     1 
ATOM   5912  C  CD     B GLN   A 1 368 ? 13.575  9.055   43.943 0.47 40.36  ?  393 GLN   A CD     1 
ATOM   5913  O  OE1    A GLN   A 1 368 ? 14.045  9.056   44.718 0.53 45.23  ?  393 GLN   A OE1    1 
ATOM   5914  O  OE1    B GLN   A 1 368 ? 13.453  7.845   43.722 0.47 40.25  ?  393 GLN   A OE1    1 
ATOM   5915  N  NE2    A GLN   A 1 368 ? 13.993  8.776   46.943 0.53 43.39  ?  393 GLN   A NE2    1 
ATOM   5916  N  NE2    B GLN   A 1 368 ? 14.700  9.586   44.419 0.47 41.87  ?  393 GLN   A NE2    1 
ATOM   5917  H  H      A GLN   A 1 368 ? 9.660   8.971   43.070 0.53 38.47  ?  393 GLN   A H      1 
ATOM   5918  H  H      B GLN   A 1 368 ? 9.660   8.971   43.070 0.47 38.47  ?  393 GLN   A H      1 
ATOM   5919  H  HA     . GLN   A 1 368 ? 11.270  7.958   44.986 1.00 39.77  ?  393 GLN   A HA     1 
ATOM   5920  H  HB2    A GLN   A 1 368 ? 11.797  10.053  43.919 0.53 42.60  ?  393 GLN   A HB2    1 
ATOM   5921  H  HB2    B GLN   A 1 368 ? 10.649  10.655  44.478 0.47 42.32  ?  393 GLN   A HB2    1 
ATOM   5922  H  HB3    A GLN   A 1 368 ? 10.630  10.679  44.798 0.53 42.60  ?  393 GLN   A HB3    1 
ATOM   5923  H  HB3    B GLN   A 1 368 ? 11.687  10.166  45.577 0.47 42.32  ?  393 GLN   A HB3    1 
ATOM   5924  H  HG2    A GLN   A 1 368 ? 12.576  11.096  45.931 0.53 46.07  ?  393 GLN   A HG2    1 
ATOM   5925  H  HG2    B GLN   A 1 368 ? 12.062  9.813   42.795 0.47 45.19  ?  393 GLN   A HG2    1 
ATOM   5926  H  HG3    A GLN   A 1 368 ? 11.832  9.955   46.748 0.53 46.07  ?  393 GLN   A HG3    1 
ATOM   5927  H  HG3    B GLN   A 1 368 ? 12.801  10.926  43.656 0.47 45.19  ?  393 GLN   A HG3    1 
ATOM   5928  H  HE21   A GLN   A 1 368 ? 13.600  8.952   47.687 0.53 52.06  ?  393 GLN   A HE21   1 
ATOM   5929  H  HE21   B GLN   A 1 368 ? 14.751  10.434  44.553 0.47 50.23  ?  393 GLN   A HE21   1 
ATOM   5930  H  HE22   A GLN   A 1 368 ? 14.689  8.272   46.933 0.53 52.06  ?  393 GLN   A HE22   1 
ATOM   5931  H  HE22   B GLN   A 1 368 ? 15.375  9.082   44.591 0.47 50.23  ?  393 GLN   A HE22   1 
ATOM   5932  N  N      . LEU   A 1 369 ? 9.582   7.620   46.748 1.00 31.26  ?  394 LEU   A N      1 
ATOM   5933  C  CA     . LEU   A 1 369 ? 8.588   7.468   47.806 1.00 31.54  ?  394 LEU   A CA     1 
ATOM   5934  C  C      . LEU   A 1 369 ? 8.572   8.693   48.718 1.00 33.69  ?  394 LEU   A C      1 
ATOM   5935  O  O      . LEU   A 1 369 ? 9.608   9.310   48.977 1.00 34.86  ?  394 LEU   A O      1 
ATOM   5936  C  CB     . LEU   A 1 369 ? 8.889   6.202   48.607 1.00 31.00  ?  394 LEU   A CB     1 
ATOM   5937  C  CG     . LEU   A 1 369 ? 8.820   4.906   47.797 1.00 31.09  ?  394 LEU   A CG     1 
ATOM   5938  C  CD1    . LEU   A 1 369 ? 9.477   3.755   48.524 1.00 31.73  ?  394 LEU   A CD1    1 
ATOM   5939  C  CD2    . LEU   A 1 369 ? 7.354   4.601   47.497 1.00 32.39  ?  394 LEU   A CD2    1 
ATOM   5940  H  H      . LEU   A 1 369 ? 10.208  7.031   46.773 1.00 37.51  ?  394 LEU   A H      1 
ATOM   5941  H  HA     . LEU   A 1 369 ? 7.703   7.385   47.418 1.00 37.85  ?  394 LEU   A HA     1 
ATOM   5942  H  HB2    . LEU   A 1 369 ? 9.786   6.274   48.970 1.00 37.20  ?  394 LEU   A HB2    1 
ATOM   5943  H  HB3    . LEU   A 1 369 ? 8.244   6.132   49.328 1.00 37.20  ?  394 LEU   A HB3    1 
ATOM   5944  H  HG     . LEU   A 1 369 ? 9.308   5.013   46.965 1.00 37.31  ?  394 LEU   A HG     1 
ATOM   5945  H  HD11   . LEU   A 1 369 ? 9.397   2.954   47.984 1.00 38.07  ?  394 LEU   A HD11   1 
ATOM   5946  H  HD12   . LEU   A 1 369 ? 10.413  3.965   48.668 1.00 38.07  ?  394 LEU   A HD12   1 
ATOM   5947  H  HD13   . LEU   A 1 369 ? 9.032   3.625   49.376 1.00 38.07  ?  394 LEU   A HD13   1 
ATOM   5948  H  HD21   . LEU   A 1 369 ? 7.295   3.741   47.054 1.00 38.86  ?  394 LEU   A HD21   1 
ATOM   5949  H  HD22   . LEU   A 1 369 ? 6.859   4.579   48.331 1.00 38.86  ?  394 LEU   A HD22   1 
ATOM   5950  H  HD23   . LEU   A 1 369 ? 6.999   5.296   46.920 1.00 38.86  ?  394 LEU   A HD23   1 
ATOM   5951  N  N      . SER   A 1 370 ? 7.382   9.048   49.203 1.00 35.05  ?  395 SER   A N      1 
ATOM   5952  C  CA     . SER   A 1 370 ? 7.229   10.266  49.988 1.00 37.66  ?  395 SER   A CA     1 
ATOM   5953  C  C      . SER   A 1 370 ? 7.886   10.126  51.363 1.00 39.61  ?  395 SER   A C      1 
ATOM   5954  O  O      . SER   A 1 370 ? 8.147   9.023   51.851 1.00 38.78  ?  395 SER   A O      1 
ATOM   5955  C  CB     . SER   A 1 370 ? 5.748   10.614  50.169 1.00 37.65  ?  395 SER   A CB     1 
ATOM   5956  O  OG     . SER   A 1 370 ? 5.106   9.724   51.071 1.00 38.04  ?  395 SER   A OG     1 
ATOM   5957  H  H      . SER   A 1 370 ? 6.654   8.603   49.092 1.00 42.05  ?  395 SER   A H      1 
ATOM   5958  H  HA     . SER   A 1 370 ? 7.664   10.992  49.515 1.00 45.19  ?  395 SER   A HA     1 
ATOM   5959  H  HB2    . SER   A 1 370 ? 5.680   11.516  50.518 1.00 45.17  ?  395 SER   A HB2    1 
ATOM   5960  H  HB3    . SER   A 1 370 ? 5.307   10.558  49.307 1.00 45.17  ?  395 SER   A HB3    1 
ATOM   5961  H  HG     . SER   A 1 370 ? 5.165   8.935   50.788 1.00 45.65  ?  395 SER   A HG     1 
ATOM   5962  N  N      . GLU   A 1 371 ? 8.157   11.280  51.989 1.00 42.25  ?  396 GLU   A N      1 
ATOM   5963  C  CA     . GLU   A 1 371 ? 8.635   11.274  53.370 1.00 44.18  ?  396 GLU   A CA     1 
ATOM   5964  C  C      . GLU   A 1 371 ? 7.611   10.606  54.280 1.00 43.46  ?  396 GLU   A C      1 
ATOM   5965  O  O      . GLU   A 1 371 ? 7.969   9.882   55.214 1.00 44.87  ?  396 GLU   A O      1 
ATOM   5966  C  CB     . GLU   A 1 371 ? 8.938   12.695  53.850 1.00 48.22  ?  396 GLU   A CB     1 
ATOM   5967  C  CG     . GLU   A 1 371 ? 9.881   13.432  52.926 1.00 52.28  ?  396 GLU   A CG     1 
ATOM   5968  C  CD     . GLU   A 1 371 ? 10.427  14.724  53.493 1.00 55.88  ?  396 GLU   A CD     1 
ATOM   5969  O  OE1    . GLU   A 1 371 ? 10.106  15.087  54.650 1.00 57.58  ?  396 GLU   A OE1    1 
ATOM   5970  O  OE2    . GLU   A 1 371 ? 11.193  15.379  52.757 1.00 57.31  ?  396 GLU   A OE2    1 
ATOM   5971  H  H      . GLU   A 1 371 ? 8.072   12.062  51.641 1.00 50.70  ?  396 GLU   A H      1 
ATOM   5972  H  HA     . GLU   A 1 371 ? 9.467   10.777  53.412 1.00 53.01  ?  396 GLU   A HA     1 
ATOM   5973  H  HB2    . GLU   A 1 371 ? 8.109   13.196  53.898 1.00 57.85  ?  396 GLU   A HB2    1 
ATOM   5974  H  HB3    . GLU   A 1 371 ? 9.350   12.651  54.728 1.00 57.85  ?  396 GLU   A HB3    1 
ATOM   5975  H  HG2    . GLU   A 1 371 ? 10.636  12.856  52.729 1.00 62.73  ?  396 GLU   A HG2    1 
ATOM   5976  H  HG3    . GLU   A 1 371 ? 9.407   13.649  52.108 1.00 62.73  ?  396 GLU   A HG3    1 
ATOM   5977  N  N      . LYS   A 1 372 ? 6.321   10.817  54.002 1.00 42.57  ?  397 LYS   A N      1 
ATOM   5978  C  CA     . LYS   A 1 372 ? 5.270   10.171  54.785 1.00 42.78  ?  397 LYS   A CA     1 
ATOM   5979  C  C      . LYS   A 1 372 ? 5.354   8.651   54.686 1.00 40.34  ?  397 LYS   A C      1 
ATOM   5980  O  O      . LYS   A 1 372 ? 5.249   7.943   55.694 1.00 41.73  ?  397 LYS   A O      1 
ATOM   5981  C  CB     . LYS   A 1 372 ? 3.906   10.664  54.305 1.00 44.79  ?  397 LYS   A CB     1 
ATOM   5982  C  CG     . LYS   A 1 372 ? 2.728   10.119  55.075 1.00 47.37  ?  397 LYS   A CG     1 
ATOM   5983  C  CD     . LYS   A 1 372 ? 1.422   10.531  54.415 1.00 50.48  ?  397 LYS   A CD     1 
ATOM   5984  C  CE     . LYS   A 1 372 ? 0.230   10.147  55.276 1.00 52.95  ?  397 LYS   A CE     1 
ATOM   5985  N  NZ     . LYS   A 1 372 ? -1.057  10.560  54.650 1.00 54.30  ?  397 LYS   A NZ     1 
ATOM   5986  H  H      . LYS   A 1 372 ? 6.033   11.324  53.371 1.00 51.08  ?  397 LYS   A H      1 
ATOM   5987  H  HA     . LYS   A 1 372 ? 5.378   10.412  55.718 1.00 51.33  ?  397 LYS   A HA     1 
ATOM   5988  H  HB2    . LYS   A 1 372 ? 3.883   11.631  54.384 1.00 53.74  ?  397 LYS   A HB2    1 
ATOM   5989  H  HB3    . LYS   A 1 372 ? 3.793   10.404  53.378 1.00 53.74  ?  397 LYS   A HB3    1 
ATOM   5990  H  HG2    . LYS   A 1 372 ? 2.773   9.151   55.094 1.00 56.84  ?  397 LYS   A HG2    1 
ATOM   5991  H  HG3    . LYS   A 1 372 ? 2.741   10.470  55.979 1.00 56.84  ?  397 LYS   A HG3    1 
ATOM   5992  H  HD2    . LYS   A 1 372 ? 1.412   11.493  54.289 1.00 60.57  ?  397 LYS   A HD2    1 
ATOM   5993  H  HD3    . LYS   A 1 372 ? 1.338   10.084  53.558 1.00 60.57  ?  397 LYS   A HD3    1 
ATOM   5994  H  HE2    . LYS   A 1 372 ? 0.216   9.184   55.394 1.00 63.53  ?  397 LYS   A HE2    1 
ATOM   5995  H  HE3    . LYS   A 1 372 ? 0.303   10.585  56.139 1.00 63.53  ?  397 LYS   A HE3    1 
ATOM   5996  H  HZ1    . LYS   A 1 372 ? -1.738  10.325  55.171 1.00 65.15  ?  397 LYS   A HZ1    1 
ATOM   5997  H  HZ2    . LYS   A 1 372 ? -1.070  11.443  54.537 1.00 65.15  ?  397 LYS   A HZ2    1 
ATOM   5998  H  HZ3    . LYS   A 1 372 ? -1.150  10.166  53.857 1.00 65.15  ?  397 LYS   A HZ3    1 
ATOM   5999  N  N      . PHE   A 1 373 ? 5.523   8.128   53.471 1.00 37.12  ?  398 PHE   A N      1 
ATOM   6000  C  CA     . PHE   A 1 373 ? 5.637   6.682   53.297 1.00 33.88  ?  398 PHE   A CA     1 
ATOM   6001  C  C      . PHE   A 1 373 ? 6.838   6.135   54.059 1.00 34.43  ?  398 PHE   A C      1 
ATOM   6002  O  O      . PHE   A 1 373 ? 6.743   5.112   54.747 1.00 34.69  ?  398 PHE   A O      1 
ATOM   6003  C  CB     . PHE   A 1 373 ? 5.748   6.354   51.806 1.00 31.76  ?  398 PHE   A CB     1 
ATOM   6004  C  CG     . PHE   A 1 373 ? 5.750   4.882   51.495 1.00 28.96  ?  398 PHE   A CG     1 
ATOM   6005  C  CD1    . PHE   A 1 373 ? 6.912   4.138   51.600 1.00 28.24  ?  398 PHE   A CD1    1 
ATOM   6006  C  CD2    . PHE   A 1 373 ? 4.587   4.237   51.087 1.00 27.57  ?  398 PHE   A CD2    1 
ATOM   6007  C  CE1    . PHE   A 1 373 ? 6.916   2.783   51.316 1.00 26.81  ?  398 PHE   A CE1    1 
ATOM   6008  C  CE2    . PHE   A 1 373 ? 4.587   2.884   50.796 1.00 26.51  ?  398 PHE   A CE2    1 
ATOM   6009  C  CZ     . PHE   A 1 373 ? 5.754   2.156   50.907 1.00 26.74  ?  398 PHE   A CZ     1 
ATOM   6010  H  H      . PHE   A 1 373 ? 5.575   8.582   52.743 1.00 44.53  ?  398 PHE   A H      1 
ATOM   6011  H  HA     . PHE   A 1 373 ? 4.839   6.255   53.647 1.00 40.65  ?  398 PHE   A HA     1 
ATOM   6012  H  HB2    . PHE   A 1 373 ? 4.992   6.751   51.344 1.00 38.11  ?  398 PHE   A HB2    1 
ATOM   6013  H  HB3    . PHE   A 1 373 ? 6.577   6.727   51.467 1.00 38.11  ?  398 PHE   A HB3    1 
ATOM   6014  H  HD1    . PHE   A 1 373 ? 7.700   4.554   51.865 1.00 33.89  ?  398 PHE   A HD1    1 
ATOM   6015  H  HD2    . PHE   A 1 373 ? 3.797   4.723   51.008 1.00 33.08  ?  398 PHE   A HD2    1 
ATOM   6016  H  HE1    . PHE   A 1 373 ? 7.703   2.294   51.399 1.00 32.16  ?  398 PHE   A HE1    1 
ATOM   6017  H  HE2    . PHE   A 1 373 ? 3.801   2.466   50.525 1.00 31.80  ?  398 PHE   A HE2    1 
ATOM   6018  H  HZ     . PHE   A 1 373 ? 5.758   1.247   50.709 1.00 32.08  ?  398 PHE   A HZ     1 
ATOM   6019  N  N      . ILE   A 1 374 ? 7.985   6.800   53.933 1.00 35.82  ?  399 ILE   A N      1 
ATOM   6020  C  CA     . ILE   A 1 374 ? 9.205   6.297   54.553 1.00 38.11  ?  399 ILE   A CA     1 
ATOM   6021  C  C      . ILE   A 1 374 ? 9.079   6.309   56.072 1.00 40.07  ?  399 ILE   A C      1 
ATOM   6022  O  O      . ILE   A 1 374 ? 9.528   5.379   56.751 1.00 40.42  ?  399 ILE   A O      1 
ATOM   6023  C  CB     . ILE   A 1 374 ? 10.414  7.121   54.074 1.00 38.36  ?  399 ILE   A CB     1 
ATOM   6024  C  CG1    . ILE   A 1 374 ? 10.706  6.849   52.595 1.00 37.40  ?  399 ILE   A CG1    1 
ATOM   6025  C  CG2    . ILE   A 1 374 ? 11.647  6.832   54.930 1.00 39.13  ?  399 ILE   A CG2    1 
ATOM   6026  C  CD1    . ILE   A 1 374 ? 11.085  5.412   52.279 1.00 37.66  ?  399 ILE   A CD1    1 
ATOM   6027  H  H      . ILE   A 1 374 ? 8.082   7.536   53.499 1.00 42.98  ?  399 ILE   A H      1 
ATOM   6028  H  HA     . ILE   A 1 374 ? 9.337   5.377   54.277 1.00 45.72  ?  399 ILE   A HA     1 
ATOM   6029  H  HB     . ILE   A 1 374 ? 10.190  8.059   54.173 1.00 46.03  ?  399 ILE   A HB     1 
ATOM   6030  H  HG12   . ILE   A 1 374 ? 9.913   7.063   52.079 1.00 44.88  ?  399 ILE   A HG12   1 
ATOM   6031  H  HG13   . ILE   A 1 374 ? 11.445  7.413   52.317 1.00 44.88  ?  399 ILE   A HG13   1 
ATOM   6032  H  HG21   . ILE   A 1 374 ? 12.439  7.120   54.450 1.00 46.95  ?  399 ILE   A HG21   1 
ATOM   6033  H  HG22   . ILE   A 1 374 ? 11.572  7.318   55.766 1.00 46.95  ?  399 ILE   A HG22   1 
ATOM   6034  H  HG23   . ILE   A 1 374 ? 11.694  5.879   55.105 1.00 46.95  ?  399 ILE   A HG23   1 
ATOM   6035  H  HD11   . ILE   A 1 374 ? 11.405  5.363   51.365 1.00 45.18  ?  399 ILE   A HD11   1 
ATOM   6036  H  HD12   . ILE   A 1 374 ? 11.782  5.127   52.890 1.00 45.18  ?  399 ILE   A HD12   1 
ATOM   6037  H  HD13   . ILE   A 1 374 ? 10.302  4.849   52.385 1.00 45.18  ?  399 ILE   A HD13   1 
ATOM   6038  N  N      . LYS   A 1 375 ? 8.468   7.355   56.632 1.00 42.14  ?  400 LYS   A N      1 
ATOM   6039  C  CA     . LYS   A 1 375 ? 8.284   7.393   58.079 1.00 44.69  ?  400 LYS   A CA     1 
ATOM   6040  C  C      . LYS   A 1 375 ? 7.403   6.243   58.548 1.00 43.95  ?  400 LYS   A C      1 
ATOM   6041  O  O      . LYS   A 1 375 ? 7.676   5.621   59.582 1.00 45.12  ?  400 LYS   A O      1 
ATOM   6042  C  CB     . LYS   A 1 375 ? 7.677   8.728   58.503 1.00 48.61  ?  400 LYS   A CB     1 
ATOM   6043  C  CG     . LYS   A 1 375 ? 8.692   9.824   58.742 1.00 52.64  ?  400 LYS   A CG     1 
ATOM   6044  C  CD     . LYS   A 1 375 ? 8.042   11.032  59.407 1.00 55.66  ?  400 LYS   A CD     1 
ATOM   6045  C  CE     . LYS   A 1 375 ? 9.054   12.146  59.658 1.00 58.41  ?  400 LYS   A CE     1 
ATOM   6046  N  NZ     . LYS   A 1 375 ? 10.176  11.697  60.535 1.00 60.06  ?  400 LYS   A NZ     1 
ATOM   6047  H  H      . LYS   A 1 375 ? 8.159   8.035   56.207 1.00 50.57  ?  400 LYS   A H      1 
ATOM   6048  H  HA     . LYS   A 1 375 ? 9.152   7.310   58.503 1.00 53.63  ?  400 LYS   A HA     1 
ATOM   6049  H  HB2    . LYS   A 1 375 ? 7.076   9.031   57.805 1.00 58.33  ?  400 LYS   A HB2    1 
ATOM   6050  H  HB3    . LYS   A 1 375 ? 7.186   8.597   59.329 1.00 58.33  ?  400 LYS   A HB3    1 
ATOM   6051  H  HG2    . LYS   A 1 375 ? 9.395   9.493   59.323 1.00 63.16  ?  400 LYS   A HG2    1 
ATOM   6052  H  HG3    . LYS   A 1 375 ? 9.070   10.106  57.894 1.00 63.16  ?  400 LYS   A HG3    1 
ATOM   6053  H  HD2    . LYS   A 1 375 ? 7.343   11.380  58.830 1.00 66.79  ?  400 LYS   A HD2    1 
ATOM   6054  H  HD3    . LYS   A 1 375 ? 7.665   10.765  60.260 1.00 66.79  ?  400 LYS   A HD3    1 
ATOM   6055  H  HE2    . LYS   A 1 375 ? 9.428   12.434  58.811 1.00 70.09  ?  400 LYS   A HE2    1 
ATOM   6056  H  HE3    . LYS   A 1 375 ? 8.609   12.890  60.094 1.00 70.09  ?  400 LYS   A HE3    1 
ATOM   6057  H  HZ1    . LYS   A 1 375 ? 10.632  11.045  60.136 1.00 72.06  ?  400 LYS   A HZ1    1 
ATOM   6058  H  HZ2    . LYS   A 1 375 ? 10.726  12.377  60.698 1.00 72.06  ?  400 LYS   A HZ2    1 
ATOM   6059  H  HZ3    . LYS   A 1 375 ? 9.855   11.393  61.308 1.00 72.06  ?  400 LYS   A HZ3    1 
ATOM   6060  N  N      . ALA   A 1 376 ? 6.334   5.953   57.803 1.00 42.19  ?  401 ALA   A N      1 
ATOM   6061  C  CA     . ALA   A 1 376 ? 5.465   4.838   58.162 1.00 40.94  ?  401 ALA   A CA     1 
ATOM   6062  C  C      . ALA   A 1 376 ? 6.200   3.508   58.047 1.00 39.88  ?  401 ALA   A C      1 
ATOM   6063  O  O      . ALA   A 1 376 ? 6.004   2.608   58.872 1.00 40.58  ?  401 ALA   A O      1 
ATOM   6064  C  CB     . ALA   A 1 376 ? 4.220   4.847   57.276 1.00 40.60  ?  401 ALA   A CB     1 
ATOM   6065  H  H      . ALA   A 1 376 ? 6.095   6.381   57.097 1.00 50.62  ?  401 ALA   A H      1 
ATOM   6066  H  HA     . ALA   A 1 376 ? 5.180   4.941   59.083 1.00 49.12  ?  401 ALA   A HA     1 
ATOM   6067  H  HB1    . ALA   A 1 376 ? 3.631   4.128   57.552 1.00 48.72  ?  401 ALA   A HB1    1 
ATOM   6068  H  HB2    . ALA   A 1 376 ? 3.768   5.700   57.375 1.00 48.72  ?  401 ALA   A HB2    1 
ATOM   6069  H  HB3    . ALA   A 1 376 ? 4.488   4.720   56.353 1.00 48.72  ?  401 ALA   A HB3    1 
ATOM   6070  N  N      . ALA   A 1 377 ? 7.051   3.364   57.030 1.00 38.28  ?  402 ALA   A N      1 
ATOM   6071  C  CA     . ALA   A 1 377 ? 7.842   2.144   56.901 1.00 38.64  ?  402 ALA   A CA     1 
ATOM   6072  C  C      . ALA   A 1 377 ? 8.833   1.995   58.048 1.00 42.00  ?  402 ALA   A C      1 
ATOM   6073  O  O      . ALA   A 1 377 ? 9.133   0.872   58.465 1.00 43.47  ?  402 ALA   A O      1 
ATOM   6074  C  CB     . ALA   A 1 377 ? 8.585   2.141   55.565 1.00 36.82  ?  402 ALA   A CB     1 
ATOM   6075  H  H      . ALA   A 1 377 ? 7.186   3.947   56.412 1.00 45.93  ?  402 ALA   A H      1 
ATOM   6076  H  HA     . ALA   A 1 377 ? 7.242   1.382   56.918 1.00 46.36  ?  402 ALA   A HA     1 
ATOM   6077  H  HB1    . ALA   A 1 377 ? 9.104   1.325   55.494 1.00 44.17  ?  402 ALA   A HB1    1 
ATOM   6078  H  HB2    . ALA   A 1 377 ? 7.937   2.185   54.844 1.00 44.17  ?  402 ALA   A HB2    1 
ATOM   6079  H  HB3    . ALA   A 1 377 ? 9.173   2.912   55.529 1.00 44.17  ?  402 ALA   A HB3    1 
ATOM   6080  N  N      . ILE   A 1 378 ? 9.370   3.108   58.550 1.00 44.16  ?  403 ILE   A N      1 
ATOM   6081  C  CA     . ILE   A 1 378 ? 10.310  3.036   59.662 1.00 47.81  ?  403 ILE   A CA     1 
ATOM   6082  C  C      . ILE   A 1 378 ? 9.628   2.504   60.912 1.00 50.67  ?  403 ILE   A C      1 
ATOM   6083  O  O      . ILE   A 1 378 ? 10.249  1.787   61.707 1.00 51.81  ?  403 ILE   A O      1 
ATOM   6084  C  CB     . ILE   A 1 378 ? 10.950  4.417   59.900 1.00 49.06  ?  403 ILE   A CB     1 
ATOM   6085  C  CG1    . ILE   A 1 378 ? 12.036  4.660   58.849 1.00 48.79  ?  403 ILE   A CG1    1 
ATOM   6086  C  CG2    . ILE   A 1 378 ? 11.513  4.518   61.313 1.00 50.20  ?  403 ILE   A CG2    1 
ATOM   6087  C  CD1    . ILE   A 1 378 ? 12.296  6.116   58.547 1.00 48.83  ?  403 ILE   A CD1    1 
ATOM   6088  H  H      . ILE   A 1 378 ? 9.207   3.904   58.268 1.00 52.99  ?  403 ILE   A H      1 
ATOM   6089  H  HA     . ILE   A 1 378 ? 11.019  2.415   59.431 1.00 57.37  ?  403 ILE   A HA     1 
ATOM   6090  H  HB     . ILE   A 1 378 ? 10.271  5.104   59.812 1.00 58.87  ?  403 ILE   A HB     1 
ATOM   6091  H  HG12   . ILE   A 1 378 ? 12.867  4.273   59.166 1.00 58.54  ?  403 ILE   A HG12   1 
ATOM   6092  H  HG13   . ILE   A 1 378 ? 11.766  4.232   58.021 1.00 58.54  ?  403 ILE   A HG13   1 
ATOM   6093  H  HG21   . ILE   A 1 378 ? 12.134  5.261   61.354 1.00 60.24  ?  403 ILE   A HG21   1 
ATOM   6094  H  HG22   . ILE   A 1 378 ? 10.782  4.663   61.934 1.00 60.24  ?  403 ILE   A HG22   1 
ATOM   6095  H  HG23   . ILE   A 1 378 ? 11.971  3.691   61.530 1.00 60.24  ?  403 ILE   A HG23   1 
ATOM   6096  H  HD11   . ILE   A 1 378 ? 12.999  6.180   57.882 1.00 58.59  ?  403 ILE   A HD11   1 
ATOM   6097  H  HD12   . ILE   A 1 378 ? 11.481  6.518   58.208 1.00 58.59  ?  403 ILE   A HD12   1 
ATOM   6098  H  HD13   . ILE   A 1 378 ? 12.571  6.563   59.363 1.00 58.59  ?  403 ILE   A HD13   1 
ATOM   6099  N  N      . GLY   A 1 379 ? 8.350   2.825   61.104 1.00 52.37  ?  404 GLY   A N      1 
ATOM   6100  C  CA     . GLY   A 1 379 ? 7.590   2.312   62.227 1.00 54.92  ?  404 GLY   A CA     1 
ATOM   6101  C  C      . GLY   A 1 379 ? 6.768   1.093   61.859 1.00 57.73  ?  404 GLY   A C      1 
ATOM   6102  O  O      . GLY   A 1 379 ? 5.731   0.804   62.468 1.00 58.51  ?  404 GLY   A O      1 
ATOM   6103  H  H      . GLY   A 1 379 ? 7.899   3.345   60.588 1.00 62.83  ?  404 GLY   A H      1 
ATOM   6104  H  HA2    . GLY   A 1 379 ? 8.199   2.065   62.941 1.00 65.90  ?  404 GLY   A HA2    1 
ATOM   6105  H  HA3    . GLY   A 1 379 ? 6.988   3.001   62.550 1.00 65.90  ?  404 GLY   A HA3    1 
ATOM   6106  N  N      . CYS   A 1 380 ? 7.253   0.358   60.860 1.00 59.71  ?  405 CYS   A N      1 
ATOM   6107  C  CA     . CYS   A 1 380 ? 6.546   -0.775  60.274 1.00 61.65  ?  405 CYS   A CA     1 
ATOM   6108  C  C      . CYS   A 1 380 ? 6.655   -2.044  61.103 1.00 62.06  ?  405 CYS   A C      1 
ATOM   6109  O  O      . CYS   A 1 380 ? 5.808   -2.933  60.955 1.00 62.48  ?  405 CYS   A O      1 
ATOM   6110  C  CB     . CYS   A 1 380 ? 7.113   -0.999  58.868 1.00 62.99  ?  405 CYS   A CB     1 
ATOM   6111  S  SG     . CYS   A 1 380 ? 6.408   -2.294  57.848 1.00 64.09  ?  405 CYS   A SG     1 
ATOM   6112  H  H      . CYS   A 1 380 ? 8.016   0.502   60.491 1.00 71.64  ?  405 CYS   A H      1 
ATOM   6113  H  HA     . CYS   A 1 380 ? 5.598   -0.582  60.209 1.00 73.97  ?  405 CYS   A HA     1 
ATOM   6114  H  HB2    . CYS   A 1 380 ? 7.004   -0.171  58.375 1.00 75.58  ?  405 CYS   A HB2    1 
ATOM   6115  H  HB3    . CYS   A 1 380 ? 8.056   -1.206  58.963 1.00 75.58  ?  405 CYS   A HB3    1 
ATOM   6116  H  HG     . CYS   A 1 380 ? 6.489   -3.339  58.433 1.00 76.90  ?  405 CYS   A HG     1 
ATOM   6117  N  N      . GLY   A 1 381 ? 7.657   -2.142  61.977 1.00 61.06  ?  406 GLY   A N      1 
ATOM   6118  C  CA     . GLY   A 1 381 ? 7.982   -3.376  62.659 1.00 59.97  ?  406 GLY   A CA     1 
ATOM   6119  C  C      . GLY   A 1 381 ? 9.196   -4.099  62.113 1.00 59.00  ?  406 GLY   A C      1 
ATOM   6120  O  O      . GLY   A 1 381 ? 9.634   -5.086  62.718 1.00 59.51  ?  406 GLY   A O      1 
ATOM   6121  H  H      . GLY   A 1 381 ? 8.171   -1.487  62.190 1.00 73.26  ?  406 GLY   A H      1 
ATOM   6122  H  HA2    . GLY   A 1 381 ? 8.149   -3.180  63.594 1.00 71.95  ?  406 GLY   A HA2    1 
ATOM   6123  H  HA3    . GLY   A 1 381 ? 7.224   -3.977  62.593 1.00 71.95  ?  406 GLY   A HA3    1 
ATOM   6124  N  N      . ILE   A 1 382 ? 9.750   -3.644  60.989 1.00 57.14  ?  407 ILE   A N      1 
ATOM   6125  C  CA     . ILE   A 1 382 ? 10.972  -4.253  60.472 1.00 56.07  ?  407 ILE   A CA     1 
ATOM   6126  C  C      . ILE   A 1 382 ? 12.166  -3.836  61.325 1.00 56.65  ?  407 ILE   A C      1 
ATOM   6127  O  O      . ILE   A 1 382 ? 12.947  -4.679  61.785 1.00 55.90  ?  407 ILE   A O      1 
ATOM   6128  C  CB     . ILE   A 1 382 ? 11.171  -3.883  58.991 1.00 54.01  ?  407 ILE   A CB     1 
ATOM   6129  C  CG1    . ILE   A 1 382 ? 10.075  -4.524  58.132 1.00 52.90  ?  407 ILE   A CG1    1 
ATOM   6130  C  CG2    . ILE   A 1 382 ? 12.545  -4.322  58.507 1.00 52.86  ?  407 ILE   A CG2    1 
ATOM   6131  C  CD1    . ILE   A 1 382 ? 9.886   -3.874  56.776 1.00 52.60  ?  407 ILE   A CD1    1 
ATOM   6132  H  H      . ILE   A 1 382 ? 9.442   -2.996  60.514 1.00 68.56  ?  407 ILE   A H      1 
ATOM   6133  H  HA     . ILE   A 1 382 ? 10.889  -5.218  60.527 1.00 67.28  ?  407 ILE   A HA     1 
ATOM   6134  H  HB     . ILE   A 1 382 ? 11.109  -2.918  58.908 1.00 64.81  ?  407 ILE   A HB     1 
ATOM   6135  H  HG12   . ILE   A 1 382 ? 10.303  -5.455  57.983 1.00 63.47  ?  407 ILE   A HG12   1 
ATOM   6136  H  HG13   . ILE   A 1 382 ? 9.232   -4.461  58.608 1.00 63.47  ?  407 ILE   A HG13   1 
ATOM   6137  H  HG21   . ILE   A 1 382 ? 12.551  -4.327  57.537 1.00 63.42  ?  407 ILE   A HG21   1 
ATOM   6138  H  HG22   . ILE   A 1 382 ? 13.210  -3.699  58.838 1.00 63.42  ?  407 ILE   A HG22   1 
ATOM   6139  H  HG23   . ILE   A 1 382 ? 12.728  -5.213  58.844 1.00 63.42  ?  407 ILE   A HG23   1 
ATOM   6140  H  HD11   . ILE   A 1 382 ? 9.160   -4.318  56.311 1.00 63.11  ?  407 ILE   A HD11   1 
ATOM   6141  H  HD12   . ILE   A 1 382 ? 9.674   -2.936  56.902 1.00 63.11  ?  407 ILE   A HD12   1 
ATOM   6142  H  HD13   . ILE   A 1 382 ? 10.707  -3.962  56.267 1.00 63.11  ?  407 ILE   A HD13   1 
ATOM   6143  N  N      . VAL   A 1 383 ? 12.318  -2.527  61.558 1.00 57.74  ?  408 VAL   A N      1 
ATOM   6144  C  CA     . VAL   A 1 383 ? 13.403  -2.048  62.411 1.00 59.10  ?  408 VAL   A CA     1 
ATOM   6145  C  C      . VAL   A 1 383 ? 13.356  -2.756  63.758 1.00 61.41  ?  408 VAL   A C      1 
ATOM   6146  O  O      . VAL   A 1 383 ? 14.391  -3.146  64.311 1.00 61.36  ?  408 VAL   A O      1 
ATOM   6147  C  CB     . VAL   A 1 383 ? 13.324  -0.519  62.583 1.00 58.44  ?  408 VAL   A CB     1 
ATOM   6148  C  CG1    . VAL   A 1 383 ? 14.391  -0.048  63.567 1.00 57.81  ?  408 VAL   A CG1    1 
ATOM   6149  C  CG2    . VAL   A 1 383 ? 13.479  0.187   61.247 1.00 58.09  ?  408 VAL   A CG2    1 
ATOM   6150  H  H      . VAL   A 1 383 ? 11.814  -1.909  61.239 1.00 69.28  ?  408 VAL   A H      1 
ATOM   6151  H  HA     . VAL   A 1 383 ? 14.247  -2.255  61.981 1.00 70.91  ?  408 VAL   A HA     1 
ATOM   6152  H  HB     . VAL   A 1 383 ? 12.452  -0.289  62.938 1.00 70.12  ?  408 VAL   A HB     1 
ATOM   6153  H  HG11   . VAL   A 1 383 ? 14.496  0.913   63.481 1.00 69.37  ?  408 VAL   A HG11   1 
ATOM   6154  H  HG12   . VAL   A 1 383 ? 14.110  -0.271  64.468 1.00 69.37  ?  408 VAL   A HG12   1 
ATOM   6155  H  HG13   . VAL   A 1 383 ? 15.228  -0.492  63.361 1.00 69.37  ?  408 VAL   A HG13   1 
ATOM   6156  H  HG21   . VAL   A 1 383 ? 13.455  1.146   61.393 1.00 69.70  ?  408 VAL   A HG21   1 
ATOM   6157  H  HG22   . VAL   A 1 383 ? 14.329  -0.065  60.853 1.00 69.70  ?  408 VAL   A HG22   1 
ATOM   6158  H  HG23   . VAL   A 1 383 ? 12.752  -0.078  60.664 1.00 69.70  ?  408 VAL   A HG23   1 
ATOM   6159  N  N      . GLU   A 1 384 ? 12.148  -2.937  64.301 1.00 63.75  ?  409 GLU   A N      1 
ATOM   6160  C  CA     . GLU   A 1 384 ? 11.991  -3.639  65.569 1.00 65.77  ?  409 GLU   A CA     1 
ATOM   6161  C  C      . GLU   A 1 384 ? 12.593  -5.036  65.500 1.00 65.71  ?  409 GLU   A C      1 
ATOM   6162  O  O      . GLU   A 1 384 ? 13.485  -5.386  66.282 1.00 66.60  ?  409 GLU   A O      1 
ATOM   6163  C  CB     . GLU   A 1 384 ? 10.510  -3.724  65.945 1.00 67.73  ?  409 GLU   A CB     1 
ATOM   6164  C  CG     . GLU   A 1 384 ? 9.875   -2.404  66.316 1.00 69.94  ?  409 GLU   A CG     1 
ATOM   6165  C  CD     . GLU   A 1 384 ? 8.751   -2.574  67.321 1.00 72.17  ?  409 GLU   A CD     1 
ATOM   6166  O  OE1    . GLU   A 1 384 ? 7.802   -3.334  67.028 1.00 72.97  ?  409 GLU   A OE1    1 
ATOM   6167  O  OE2    . GLU   A 1 384 ? 8.830   -1.963  68.410 1.00 73.01  -1 409 GLU   A OE2    1 
ATOM   6168  H  H      . GLU   A 1 384 ? 11.410  -2.664  63.954 1.00 76.49  ?  409 GLU   A H      1 
ATOM   6169  H  HA     . GLU   A 1 384 ? 12.454  -3.135  66.257 1.00 78.92  ?  409 GLU   A HA     1 
ATOM   6170  H  HB2    . GLU   A 1 384 ? 10.020  -4.081  65.188 1.00 81.27  ?  409 GLU   A HB2    1 
ATOM   6171  H  HB3    . GLU   A 1 384 ? 10.420  -4.316  66.709 1.00 81.27  ?  409 GLU   A HB3    1 
ATOM   6172  H  HG2    . GLU   A 1 384 ? 10.547  -1.825  66.709 1.00 83.93  ?  409 GLU   A HG2    1 
ATOM   6173  H  HG3    . GLU   A 1 384 ? 9.508   -1.991  65.519 1.00 83.93  ?  409 GLU   A HG3    1 
ATOM   6174  N  N      . SER   A 1 385 ? 12.099  -5.858  64.570 1.00 64.46  ?  410 SER   A N      1 
ATOM   6175  C  CA     . SER   A 1 385 ? 12.589  -7.226  64.442 1.00 63.16  ?  410 SER   A CA     1 
ATOM   6176  C  C      . SER   A 1 385 ? 14.109  -7.250  64.371 1.00 62.25  ?  410 SER   A C      1 
ATOM   6177  O  O      . SER   A 1 385 ? 14.770  -7.990  65.108 1.00 62.47  ?  410 SER   A O      1 
ATOM   6178  C  CB     . SER   A 1 385 ? 11.982  -7.882  63.200 1.00 63.25  ?  410 SER   A CB     1 
ATOM   6179  O  OG     . SER   A 1 385 ? 10.571  -7.958  63.303 1.00 63.54  ?  410 SER   A OG     1 
ATOM   6180  H  H      . SER   A 1 385 ? 11.484  -5.648  64.007 1.00 77.34  ?  410 SER   A H      1 
ATOM   6181  H  HA     . SER   A 1 385 ? 12.312  -7.737  65.219 1.00 75.78  ?  410 SER   A HA     1 
ATOM   6182  H  HB2    . SER   A 1 385 ? 12.213  -7.354  62.420 1.00 75.89  ?  410 SER   A HB2    1 
ATOM   6183  H  HB3    . SER   A 1 385 ? 12.340  -8.779  63.111 1.00 75.89  ?  410 SER   A HB3    1 
ATOM   6184  H  HG     . SER   A 1 385 ? 10.251  -8.317  62.614 1.00 76.24  ?  410 SER   A HG     1 
ATOM   6185  N  N      . ILE   A 1 386 ? 14.680  -6.421  63.497 1.00 61.65  ?  411 ILE   A N      1 
ATOM   6186  C  CA     . ILE   A 1 386 ? 16.129  -6.398  63.321 1.00 61.86  ?  411 ILE   A CA     1 
ATOM   6187  C  C      . ILE   A 1 386 ? 16.824  -6.109  64.644 1.00 63.29  ?  411 ILE   A C      1 
ATOM   6188  O  O      . ILE   A 1 386 ? 17.790  -6.783  65.019 1.00 63.88  ?  411 ILE   A O      1 
ATOM   6189  C  CB     . ILE   A 1 386 ? 16.514  -5.365  62.246 1.00 60.85  ?  411 ILE   A CB     1 
ATOM   6190  C  CG1    . ILE   A 1 386 ? 16.160  -5.907  60.864 1.00 60.71  ?  411 ILE   A CG1    1 
ATOM   6191  C  CG2    . ILE   A 1 386 ? 17.987  -5.008  62.352 1.00 60.37  ?  411 ILE   A CG2    1 
ATOM   6192  C  CD1    . ILE   A 1 386 ? 16.018  -4.838  59.826 1.00 61.24  ?  411 ILE   A CD1    1 
ATOM   6193  H  H      . ILE   A 1 386 ? 14.254  -5.867  62.997 1.00 73.98  ?  411 ILE   A H      1 
ATOM   6194  H  HA     . ILE   A 1 386 ? 16.417  -7.274  63.021 1.00 74.22  ?  411 ILE   A HA     1 
ATOM   6195  H  HB     . ILE   A 1 386 ? 16.009  -4.549  62.390 1.00 73.01  ?  411 ILE   A HB     1 
ATOM   6196  H  HG12   . ILE   A 1 386 ? 16.862  -6.511  60.575 1.00 72.84  ?  411 ILE   A HG12   1 
ATOM   6197  H  HG13   . ILE   A 1 386 ? 15.316  -6.382  60.920 1.00 72.84  ?  411 ILE   A HG13   1 
ATOM   6198  H  HG21   . ILE   A 1 386 ? 18.270  -4.589  61.524 1.00 72.43  ?  411 ILE   A HG21   1 
ATOM   6199  H  HG22   . ILE   A 1 386 ? 18.110  -4.394  63.093 1.00 72.43  ?  411 ILE   A HG22   1 
ATOM   6200  H  HG23   . ILE   A 1 386 ? 18.498  -5.818  62.505 1.00 72.43  ?  411 ILE   A HG23   1 
ATOM   6201  H  HD11   . ILE   A 1 386 ? 15.623  -5.222  59.028 1.00 73.48  ?  411 ILE   A HD11   1 
ATOM   6202  H  HD12   . ILE   A 1 386 ? 15.445  -4.135  60.173 1.00 73.48  ?  411 ILE   A HD12   1 
ATOM   6203  H  HD13   . ILE   A 1 386 ? 16.895  -4.478  59.621 1.00 73.48  ?  411 ILE   A HD13   1 
ATOM   6204  N  N      . LEU   A 1 387 ? 16.349  -5.096  65.368 1.00 64.30  ?  412 LEU   A N      1 
ATOM   6205  C  CA     . LEU   A 1 387 ? 17.053  -4.671  66.573 1.00 65.40  ?  412 LEU   A CA     1 
ATOM   6206  C  C      . LEU   A 1 387 ? 16.950  -5.708  67.684 1.00 67.18  ?  412 LEU   A C      1 
ATOM   6207  O  O      . LEU   A 1 387 ? 17.854  -5.802  68.521 1.00 67.19  ?  412 LEU   A O      1 
ATOM   6208  C  CB     . LEU   A 1 387 ? 16.524  -3.314  67.031 1.00 64.65  ?  412 LEU   A CB     1 
ATOM   6209  C  CG     . LEU   A 1 387 ? 17.047  -2.160  66.171 1.00 63.79  ?  412 LEU   A CG     1 
ATOM   6210  C  CD1    . LEU   A 1 387 ? 16.352  -0.849  66.500 1.00 63.61  ?  412 LEU   A CD1    1 
ATOM   6211  C  CD2    . LEU   A 1 387 ? 18.562  -2.011  66.327 1.00 63.03  ?  412 LEU   A CD2    1 
ATOM   6212  H  H      . LEU   A 1 387 ? 15.637  -4.650  65.187 1.00 77.15  ?  412 LEU   A H      1 
ATOM   6213  H  HA     . LEU   A 1 387 ? 17.995  -4.565  66.370 1.00 78.47  ?  412 LEU   A HA     1 
ATOM   6214  H  HB2    . LEU   A 1 387 ? 15.556  -3.317  66.975 1.00 77.57  ?  412 LEU   A HB2    1 
ATOM   6215  H  HB3    . LEU   A 1 387 ? 16.803  -3.159  67.947 1.00 77.57  ?  412 LEU   A HB3    1 
ATOM   6216  H  HG     . LEU   A 1 387 ? 16.852  -2.367  65.244 1.00 76.54  ?  412 LEU   A HG     1 
ATOM   6217  H  HD11   . LEU   A 1 387 ? 16.698  -0.154  65.920 1.00 76.33  ?  412 LEU   A HD11   1 
ATOM   6218  H  HD12   . LEU   A 1 387 ? 15.398  -0.954  66.359 1.00 76.33  ?  412 LEU   A HD12   1 
ATOM   6219  H  HD13   . LEU   A 1 387 ? 16.526  -0.624  67.427 1.00 76.33  ?  412 LEU   A HD13   1 
ATOM   6220  H  HD21   . LEU   A 1 387 ? 18.825  -1.125  66.033 1.00 75.63  ?  412 LEU   A HD21   1 
ATOM   6221  H  HD22   . LEU   A 1 387 ? 18.797  -2.133  67.261 1.00 75.63  ?  412 LEU   A HD22   1 
ATOM   6222  H  HD23   . LEU   A 1 387 ? 19.003  -2.684  65.785 1.00 75.63  ?  412 LEU   A HD23   1 
ATOM   6223  N  N      . ASN   A 1 388 ? 15.873  -6.498  67.712 1.00 68.96  ?  413 ASN   A N      1 
ATOM   6224  C  CA     . ASN   A 1 388 ? 15.857  -7.649  68.606 1.00 71.16  ?  413 ASN   A CA     1 
ATOM   6225  C  C      . ASN   A 1 388 ? 16.961  -8.636  68.242 1.00 71.96  ?  413 ASN   A C      1 
ATOM   6226  O  O      . ASN   A 1 388 ? 17.542  -9.277  69.126 1.00 72.21  ?  413 ASN   A O      1 
ATOM   6227  C  CB     . ASN   A 1 388 ? 14.501  -8.356  68.561 1.00 72.63  ?  413 ASN   A CB     1 
ATOM   6228  C  CG     . ASN   A 1 388 ? 13.358  -7.468  69.014 1.00 73.91  ?  413 ASN   A CG     1 
ATOM   6229  O  OD1    . ASN   A 1 388 ? 13.566  -6.433  69.649 1.00 74.31  ?  413 ASN   A OD1    1 
ATOM   6230  N  ND2    . ASN   A 1 388 ? 12.136  -7.878  68.694 1.00 74.40  ?  413 ASN   A ND2    1 
ATOM   6231  H  H      . ASN   A 1 388 ? 15.164  -6.390  67.238 1.00 82.75  ?  413 ASN   A H      1 
ATOM   6232  H  HA     . ASN   A 1 388 ? 15.995  -7.335  69.513 1.00 85.39  ?  413 ASN   A HA     1 
ATOM   6233  H  HB2    . ASN   A 1 388 ? 14.321  -8.634  67.649 1.00 87.15  ?  413 ASN   A HB2    1 
ATOM   6234  H  HB3    . ASN   A 1 388 ? 14.529  -9.130  69.145 1.00 87.15  ?  413 ASN   A HB3    1 
ATOM   6235  H  HD21   . ASN   A 1 388 ? 11.451  -7.412  68.926 1.00 89.27  ?  413 ASN   A HD21   1 
ATOM   6236  H  HD22   . ASN   A 1 388 ? 12.029  -8.609  68.254 1.00 89.27  ?  413 ASN   A HD22   1 
ATOM   6237  N  N      . TRP   A 1 389 ? 17.268  -8.766  66.947 1.00 72.05  ?  414 TRP   A N      1 
ATOM   6238  C  CA     . TRP   A 1 389 ? 18.269  -9.735  66.517 1.00 71.66  ?  414 TRP   A CA     1 
ATOM   6239  C  C      . TRP   A 1 389 ? 19.670  -9.314  66.949 1.00 71.84  ?  414 TRP   A C      1 
ATOM   6240  O  O      . TRP   A 1 389 ? 20.433  -10.126 67.484 1.00 72.15  ?  414 TRP   A O      1 
ATOM   6241  C  CB     . TRP   A 1 389 ? 18.208  -9.922  64.999 1.00 71.04  ?  414 TRP   A CB     1 
ATOM   6242  C  CG     . TRP   A 1 389 ? 19.302  -10.808 64.487 1.00 70.40  ?  414 TRP   A CG     1 
ATOM   6243  C  CD1    . TRP   A 1 389 ? 19.328  -12.172 64.507 1.00 70.04  ?  414 TRP   A CD1    1 
ATOM   6244  C  CD2    . TRP   A 1 389 ? 20.538  -10.390 63.895 1.00 70.25  ?  414 TRP   A CD2    1 
ATOM   6245  N  NE1    . TRP   A 1 389 ? 20.503  -12.630 63.961 1.00 69.87  ?  414 TRP   A NE1    1 
ATOM   6246  C  CE2    . TRP   A 1 389 ? 21.263  -11.557 63.576 1.00 70.01  ?  414 TRP   A CE2    1 
ATOM   6247  C  CE3    . TRP   A 1 389 ? 21.101  -9.144  63.600 1.00 70.27  ?  414 TRP   A CE3    1 
ATOM   6248  C  CZ2    . TRP   A 1 389 ? 22.521  -11.514 62.977 1.00 70.14  ?  414 TRP   A CZ2    1 
ATOM   6249  C  CZ3    . TRP   A 1 389 ? 22.353  -9.104  63.009 1.00 70.27  ?  414 TRP   A CZ3    1 
ATOM   6250  C  CH2    . TRP   A 1 389 ? 23.050  -10.282 62.705 1.00 70.16  ?  414 TRP   A CH2    1 
ATOM   6251  H  H      . TRP   A 1 389 ? 16.914  -8.310  66.310 1.00 86.45  ?  414 TRP   A H      1 
ATOM   6252  H  HA     . TRP   A 1 389 ? 18.069  -10.589 66.932 1.00 85.98  ?  414 TRP   A HA     1 
ATOM   6253  H  HB2    . TRP   A 1 389 ? 17.358  -10.326 64.763 1.00 85.24  ?  414 TRP   A HB2    1 
ATOM   6254  H  HB3    . TRP   A 1 389 ? 18.295  -9.057  64.569 1.00 85.24  ?  414 TRP   A HB3    1 
ATOM   6255  H  HD1    . TRP   A 1 389 ? 18.649  -12.713 64.841 1.00 84.04  ?  414 TRP   A HD1    1 
ATOM   6256  H  HE1    . TRP   A 1 389 ? 20.726  -13.457 63.875 1.00 83.84  ?  414 TRP   A HE1    1 
ATOM   6257  H  HE3    . TRP   A 1 389 ? 20.644  -8.359  63.798 1.00 84.31  ?  414 TRP   A HE3    1 
ATOM   6258  H  HZ2    . TRP   A 1 389 ? 22.984  -12.294 62.769 1.00 84.16  ?  414 TRP   A HZ2    1 
ATOM   6259  H  HZ3    . TRP   A 1 389 ? 22.737  -8.281  62.809 1.00 84.32  ?  414 TRP   A HZ3    1 
ATOM   6260  H  HH2    . TRP   A 1 389 ? 23.890  -10.225 62.311 1.00 84.19  ?  414 TRP   A HH2    1 
ATOM   6261  N  N      . VAL   A 1 390 ? 20.034  -8.048  66.722 1.00 71.68  ?  415 VAL   A N      1 
ATOM   6262  C  CA     . VAL   A 1 390 ? 21.369  -7.600  67.104 1.00 71.98  ?  415 VAL   A CA     1 
ATOM   6263  C  C      . VAL   A 1 390 ? 21.549  -7.655  68.618 1.00 72.98  ?  415 VAL   A C      1 
ATOM   6264  O  O      . VAL   A 1 390 ? 22.683  -7.714  69.104 1.00 73.06  ?  415 VAL   A O      1 
ATOM   6265  C  CB     . VAL   A 1 390 ? 21.666  -6.183  66.565 1.00 71.31  ?  415 VAL   A CB     1 
ATOM   6266  C  CG1    . VAL   A 1 390 ? 21.475  -6.141  65.051 1.00 70.89  ?  415 VAL   A CG1    1 
ATOM   6267  C  CG2    . VAL   A 1 390 ? 20.807  -5.137  67.257 1.00 71.16  ?  415 VAL   A CG2    1 
ATOM   6268  H  H      . VAL   A 1 390 ? 19.538  -7.447  66.358 1.00 86.01  ?  415 VAL   A H      1 
ATOM   6269  H  HA     . VAL   A 1 390 ? 22.012  -8.198  66.693 1.00 86.38  ?  415 VAL   A HA     1 
ATOM   6270  H  HB     . VAL   A 1 390 ? 22.591  -5.966  66.759 1.00 85.57  ?  415 VAL   A HB     1 
ATOM   6271  H  HG11   . VAL   A 1 390 ? 21.658  -5.242  64.735 1.00 85.06  ?  415 VAL   A HG11   1 
ATOM   6272  H  HG12   . VAL   A 1 390 ? 22.089  -6.768  64.638 1.00 85.06  ?  415 VAL   A HG12   1 
ATOM   6273  H  HG13   . VAL   A 1 390 ? 20.560  -6.385  64.841 1.00 85.06  ?  415 VAL   A HG13   1 
ATOM   6274  H  HG21   . VAL   A 1 390 ? 20.891  -4.296  66.782 1.00 85.39  ?  415 VAL   A HG21   1 
ATOM   6275  H  HG22   . VAL   A 1 390 ? 19.883  -5.431  67.249 1.00 85.39  ?  415 VAL   A HG22   1 
ATOM   6276  H  HG23   . VAL   A 1 390 ? 21.113  -5.032  68.172 1.00 85.39  ?  415 VAL   A HG23   1 
ATOM   6277  N  N      . LYS   A 1 391 ? 20.452  -7.636  69.383 1.00 73.81  ?  416 LYS   A N      1 
ATOM   6278  C  CA     . LYS   A 1 391 ? 20.559  -7.874  70.820 1.00 74.44  ?  416 LYS   A CA     1 
ATOM   6279  C  C      . LYS   A 1 391 ? 21.110  -9.269  71.090 1.00 76.13  ?  416 LYS   A C      1 
ATOM   6280  O  O      . LYS   A 1 391 ? 21.989  -9.449  71.940 1.00 76.18  ?  416 LYS   A O      1 
ATOM   6281  C  CB     . LYS   A 1 391 ? 19.196  -7.692  71.487 1.00 73.13  ?  416 LYS   A CB     1 
ATOM   6282  H  H      . LYS   A 1 391 ? 19.654  -7.491  69.099 1.00 88.57  ?  416 LYS   A H      1 
ATOM   6283  H  HA     . LYS   A 1 391 ? 21.164  -7.223  71.208 1.00 89.32  ?  416 LYS   A HA     1 
ATOM   6284  N  N      . PHE   A 1 392 ? 20.612  -10.263 70.367 1.00 77.82  ?  417 PHE   A N      1 
ATOM   6285  C  CA     . PHE   A 1 392 ? 21.161  -11.613 70.407 1.00 79.44  ?  417 PHE   A CA     1 
ATOM   6286  C  C      . PHE   A 1 392 ? 22.459  -11.667 69.608 1.00 79.49  ?  417 PHE   A C      1 
ATOM   6287  O  O      . PHE   A 1 392 ? 23.396  -12.375 69.977 1.00 79.57  ?  417 PHE   A O      1 
ATOM   6288  C  CB     . PHE   A 1 392 ? 20.125  -12.599 69.863 1.00 80.57  ?  417 PHE   A CB     1 
ATOM   6289  H  H      . PHE   A 1 392 ? 19.942  -10.181 69.834 1.00 93.38  ?  417 PHE   A H      1 
ATOM   6290  H  HA     . PHE   A 1 392 ? 21.366  -11.880 71.317 1.00 95.32  ?  417 PHE   A HA     1 
ATOM   6291  N  N      . ALA   B 1 3   ? 0.974   7.533   10.121 1.00 55.75  ?  28  ALA   B N      1 
ATOM   6292  C  CA     . ALA   B 1 3   ? -0.210  6.870   10.643 1.00 54.16  ?  28  ALA   B CA     1 
ATOM   6293  C  C      . ALA   B 1 3   ? -0.707  5.789   9.690  1.00 49.71  ?  28  ALA   B C      1 
ATOM   6294  O  O      . ALA   B 1 3   ? -1.797  5.251   9.880  1.00 49.00  ?  28  ALA   B O      1 
ATOM   6295  C  CB     . ALA   B 1 3   ? -1.315  7.891   10.907 1.00 55.61  ?  28  ALA   B CB     1 
ATOM   6296  H  HA     . ALA   B 1 3   ? 0.020   6.443   11.484 1.00 64.99  ?  28  ALA   B HA     1 
ATOM   6297  H  HB1    . ALA   B 1 3   ? -2.108  7.426   11.217 1.00 66.72  ?  28  ALA   B HB1    1 
ATOM   6298  H  HB2    . ALA   B 1 3   ? -1.013  8.517   11.583 1.00 66.72  ?  28  ALA   B HB2    1 
ATOM   6299  H  HB3    . ALA   B 1 3   ? -1.512  8.364   10.082 1.00 66.72  ?  28  ALA   B HB3    1 
ATOM   6300  N  N      . SER   B 1 4   ? 0.077   5.475   8.661  1.00 47.28  ?  29  SER   B N      1 
ATOM   6301  C  CA     . SER   B 1 4   ? -0.350  4.451   7.721  1.00 44.35  ?  29  SER   B CA     1 
ATOM   6302  C  C      . SER   B 1 4   ? -0.326  3.082   8.388  1.00 42.05  ?  29  SER   B C      1 
ATOM   6303  O  O      . SER   B 1 4   ? 0.462   2.816   9.302  1.00 39.90  ?  29  SER   B O      1 
ATOM   6304  C  CB     . SER   B 1 4   ? 0.519   4.441   6.463  1.00 44.45  ?  29  SER   B CB     1 
ATOM   6305  O  OG     . SER   B 1 4   ? 1.774   3.824   6.660  1.00 43.95  ?  29  SER   B OG     1 
ATOM   6306  H  H      . SER   B 1 4   ? 0.841   5.833   8.492  1.00 56.73  ?  29  SER   B H      1 
ATOM   6307  H  HA     . SER   B 1 4   ? -1.256  4.645   7.435  1.00 53.22  ?  29  SER   B HA     1 
ATOM   6308  H  HB2    . SER   B 1 4   ? 0.046   3.957   5.768  1.00 53.33  ?  29  SER   B HB2    1 
ATOM   6309  H  HB3    . SER   B 1 4   ? 0.668   5.358   6.186  1.00 53.33  ?  29  SER   B HB3    1 
ATOM   6310  H  HG     . SER   B 1 4   ? 2.233   3.877   5.958  1.00 52.73  ?  29  SER   B HG     1 
ATOM   6311  N  N      . VAL   B 1 5   ? -1.231  2.217   7.933  1.00 42.87  ?  30  VAL   B N      1 
ATOM   6312  C  CA     . VAL   B 1 5   ? -1.279  0.845   8.424  1.00 44.03  ?  30  VAL   B CA     1 
ATOM   6313  C  C      . VAL   B 1 5   ? 0.050   0.138   8.212  1.00 41.65  ?  30  VAL   B C      1 
ATOM   6314  O  O      . VAL   B 1 5   ? 0.444   -0.714  9.018  1.00 40.04  ?  30  VAL   B O      1 
ATOM   6315  C  CB     . VAL   B 1 5   ? -2.451  0.131   7.724  1.00 47.79  ?  30  VAL   B CB     1 
ATOM   6316  C  CG1    . VAL   B 1 5   ? -2.242  -1.350  7.670  1.00 48.25  ?  30  VAL   B CG1    1 
ATOM   6317  C  CG2    . VAL   B 1 5   ? -3.765  0.462   8.435  1.00 49.18  ?  30  VAL   B CG2    1 
ATOM   6318  H  H      . VAL   B 1 5   ? -1.828  2.401   7.342  1.00 51.44  ?  30  VAL   B H      1 
ATOM   6319  H  HA     . VAL   B 1 5   ? -1.434  0.838   9.382  1.00 52.83  ?  30  VAL   B HA     1 
ATOM   6320  H  HB     . VAL   B 1 5   ? -2.500  0.447   6.809  1.00 57.35  ?  30  VAL   B HB     1 
ATOM   6321  H  HG11   . VAL   B 1 5   ? -3.078  -1.779  7.431  1.00 57.89  ?  30  VAL   B HG11   1 
ATOM   6322  H  HG12   . VAL   B 1 5   ? -1.565  -1.549  7.004  1.00 57.89  ?  30  VAL   B HG12   1 
ATOM   6323  H  HG13   . VAL   B 1 5   ? -1.949  -1.660  8.542  1.00 57.89  ?  30  VAL   B HG13   1 
ATOM   6324  H  HG21   . VAL   B 1 5   ? -4.497  0.043   7.956  1.00 59.02  ?  30  VAL   B HG21   1 
ATOM   6325  H  HG22   . VAL   B 1 5   ? -3.726  0.123   9.343  1.00 59.02  ?  30  VAL   B HG22   1 
ATOM   6326  H  HG23   . VAL   B 1 5   ? -3.884  1.424   8.446  1.00 59.02  ?  30  VAL   B HG23   1 
ATOM   6327  N  N      . GLU   B 1 6   ? 0.774   0.491   7.152  1.00 41.37  ?  31  GLU   B N      1 
ATOM   6328  C  CA     . GLU   B 1 6   ? 2.033   -0.181  6.852  1.00 40.62  ?  31  GLU   B CA     1 
ATOM   6329  C  C      . GLU   B 1 6   ? 3.178   0.315   7.728  1.00 39.72  ?  31  GLU   B C      1 
ATOM   6330  O  O      . GLU   B 1 6   ? 4.133   -0.434  7.966  1.00 39.62  ?  31  GLU   B O      1 
ATOM   6331  C  CB     . GLU   B 1 6   ? 2.362   -0.001  5.370  1.00 41.81  ?  31  GLU   B CB     1 
ATOM   6332  C  CG     . GLU   B 1 6   ? 1.383   -0.709  4.436  1.00 42.65  ?  31  GLU   B CG     1 
ATOM   6333  C  CD     . GLU   B 1 6   ? 0.060   0.028   4.265  1.00 43.57  ?  31  GLU   B CD     1 
ATOM   6334  O  OE1    . GLU   B 1 6   ? 0.015   1.267   4.451  1.00 43.64  ?  31  GLU   B OE1    1 
ATOM   6335  O  OE2    . GLU   B 1 6   ? -0.941  -0.647  3.952  1.00 44.17  ?  31  GLU   B OE2    1 
ATOM   6336  H  H      . GLU   B 1 6   ? 0.560   1.111   6.596  1.00 49.64  ?  31  GLU   B H      1 
ATOM   6337  H  HA     . GLU   B 1 6   ? 1.938   -1.131  7.025  1.00 48.74  ?  31  GLU   B HA     1 
ATOM   6338  H  HB2    . GLU   B 1 6   ? 2.343   0.946   5.159  1.00 50.17  ?  31  GLU   B HB2    1 
ATOM   6339  H  HB3    . GLU   B 1 6   ? 3.247   -0.360  5.201  1.00 50.17  ?  31  GLU   B HB3    1 
ATOM   6340  H  HG2    . GLU   B 1 6   ? 1.791   -0.792  3.560  1.00 51.18  ?  31  GLU   B HG2    1 
ATOM   6341  H  HG3    . GLU   B 1 6   ? 1.188   -1.589  4.796  1.00 51.18  ?  31  GLU   B HG3    1 
ATOM   6342  N  N      . ARG   B 1 7   ? 3.105   1.556   8.217  1.00 37.26  ?  32  ARG   B N      1 
ATOM   6343  C  CA     . ARG   B 1 7   ? 4.068   2.016   9.210  1.00 37.40  ?  32  ARG   B CA     1 
ATOM   6344  C  C      . ARG   B 1 7   ? 3.766   1.412   10.577 1.00 35.40  ?  32  ARG   B C      1 
ATOM   6345  O  O      . ARG   B 1 7   ? 4.686   0.997   11.293 1.00 35.45  ?  32  ARG   B O      1 
ATOM   6346  C  CB     . ARG   B 1 7   ? 4.072   3.545   9.304  1.00 40.15  ?  32  ARG   B CB     1 
ATOM   6347  C  CG     . ARG   B 1 7   ? 5.111   4.082   10.291 1.00 45.48  ?  32  ARG   B CG     1 
ATOM   6348  C  CD     . ARG   B 1 7   ? 5.134   5.601   10.381 1.00 50.84  ?  32  ARG   B CD     1 
ATOM   6349  N  NE     . ARG   B 1 7   ? 6.045   6.049   11.433 1.00 56.64  ?  32  ARG   B NE     1 
ATOM   6350  C  CZ     . ARG   B 1 7   ? 6.427   7.310   11.618 1.00 60.73  ?  32  ARG   B CZ     1 
ATOM   6351  N  NH1    . ARG   B 1 7   ? 5.989   8.268   10.812 1.00 62.37  ?  32  ARG   B NH1    1 
ATOM   6352  N  NH2    . ARG   B 1 7   ? 7.254   7.610   12.610 1.00 62.12  ?  32  ARG   B NH2    1 
ATOM   6353  H  H      . ARG   B 1 7   ? 2.515   2.140   7.991  1.00 44.70  ?  32  ARG   B H      1 
ATOM   6354  H  HA     . ARG   B 1 7   ? 4.955   1.739   8.929  1.00 44.87  ?  32  ARG   B HA     1 
ATOM   6355  H  HB2    . ARG   B 1 7   ? 4.273   3.913   8.429  1.00 48.18  ?  32  ARG   B HB2    1 
ATOM   6356  H  HB3    . ARG   B 1 7   ? 3.198   3.844   9.597  1.00 48.18  ?  32  ARG   B HB3    1 
ATOM   6357  H  HG2    . ARG   B 1 7   ? 4.911   3.736   11.175 1.00 54.57  ?  32  ARG   B HG2    1 
ATOM   6358  H  HG3    . ARG   B 1 7   ? 5.991   3.788   10.011 1.00 54.57  ?  32  ARG   B HG3    1 
ATOM   6359  H  HD2    . ARG   B 1 7   ? 5.435   5.970   9.536  1.00 61.01  ?  32  ARG   B HD2    1 
ATOM   6360  H  HD3    . ARG   B 1 7   ? 4.243   5.926   10.586 1.00 61.01  ?  32  ARG   B HD3    1 
ATOM   6361  H  HE     . ARG   B 1 7   ? 6.356   5.455   11.971 1.00 67.96  ?  32  ARG   B HE     1 
ATOM   6362  H  HH11   . ARG   B 1 7   ? 5.455   8.076   10.166 1.00 74.84  ?  32  ARG   B HH11   1 
ATOM   6363  H  HH12   . ARG   B 1 7   ? 6.239   9.082   10.936 1.00 74.84  ?  32  ARG   B HH12   1 
ATOM   6364  H  HH21   . ARG   B 1 7   ? 7.543   6.990   13.131 1.00 74.53  ?  32  ARG   B HH21   1 
ATOM   6365  H  HH22   . ARG   B 1 7   ? 7.503   8.424   12.731 1.00 74.53  ?  32  ARG   B HH22   1 
ATOM   6366  N  N      . ILE   B 1 8   ? 2.482   1.326   10.938 1.00 33.04  ?  33  ILE   B N      1 
ATOM   6367  C  CA     . ILE   B 1 8   ? 2.109   0.867   12.275 1.00 32.60  ?  33  ILE   B CA     1 
ATOM   6368  C  C      . ILE   B 1 8   ? 2.429   -0.608  12.453 1.00 32.42  ?  33  ILE   B C      1 
ATOM   6369  O  O      . ILE   B 1 8   ? 2.988   -1.020  13.476 1.00 31.34  ?  33  ILE   B O      1 
ATOM   6370  C  CB     . ILE   B 1 8   ? 0.617   1.117   12.548 1.00 33.66  ?  33  ILE   B CB     1 
ATOM   6371  C  CG1    . ILE   B 1 8   ? 0.321   2.608   12.617 1.00 35.53  ?  33  ILE   B CG1    1 
ATOM   6372  C  CG2    . ILE   B 1 8   ? 0.188   0.428   13.861 1.00 35.18  ?  33  ILE   B CG2    1 
ATOM   6373  C  CD1    . ILE   B 1 8   ? -1.150  2.893   12.549 1.00 37.19  ?  33  ILE   B CD1    1 
ATOM   6374  H  H      . ILE   B 1 8   ? 1.815   1.525   10.432 1.00 39.64  ?  33  ILE   B H      1 
ATOM   6375  H  HA     . ILE   B 1 8   ? 2.634   1.380   12.910 1.00 39.11  ?  33  ILE   B HA     1 
ATOM   6376  H  HB     . ILE   B 1 8   ? 0.110   0.739   11.812 1.00 40.38  ?  33  ILE   B HB     1 
ATOM   6377  H  HG12   . ILE   B 1 8   ? 0.660   2.962   13.453 1.00 42.63  ?  33  ILE   B HG12   1 
ATOM   6378  H  HG13   . ILE   B 1 8   ? 0.750   3.053   11.869 1.00 42.63  ?  33  ILE   B HG13   1 
ATOM   6379  H  HG21   . ILE   B 1 8   ? -0.663  0.795   14.147 1.00 42.21  ?  33  ILE   B HG21   1 
ATOM   6380  H  HG22   . ILE   B 1 8   ? 0.101   -0.525  13.704 1.00 42.21  ?  33  ILE   B HG22   1 
ATOM   6381  H  HG23   . ILE   B 1 8   ? 0.863   0.592   14.538 1.00 42.21  ?  33  ILE   B HG23   1 
ATOM   6382  H  HD11   . ILE   B 1 8   ? -1.281  3.836   12.367 1.00 44.62  ?  33  ILE   B HD11   1 
ATOM   6383  H  HD12   . ILE   B 1 8   ? -1.543  2.361   11.839 1.00 44.62  ?  33  ILE   B HD12   1 
ATOM   6384  H  HD13   . ILE   B 1 8   ? -1.556  2.660   13.399 1.00 44.62  ?  33  ILE   B HD13   1 
ATOM   6385  N  N      . TYR   B 1 9   ? 2.021   -1.434  11.498 1.00 31.82  ?  34  TYR   B N      1 
ATOM   6386  C  CA     . TYR   B 1 9   ? 2.116   -2.879  11.629 1.00 32.40  ?  34  TYR   B CA     1 
ATOM   6387  C  C      . TYR   B 1 9   ? 3.222   -3.389  10.721 1.00 32.99  ?  34  TYR   B C      1 
ATOM   6388  O  O      . TYR   B 1 9   ? 3.122   -3.274  9.492  1.00 34.90  ?  34  TYR   B O      1 
ATOM   6389  C  CB     . TYR   B 1 9   ? 0.786   -3.539  11.287 1.00 30.84  ?  34  TYR   B CB     1 
ATOM   6390  C  CG     . TYR   B 1 9   ? -0.365  -3.108  12.164 1.00 31.53  ?  34  TYR   B CG     1 
ATOM   6391  C  CD1    . TYR   B 1 9   ? -0.559  -3.673  13.424 1.00 31.03  ?  34  TYR   B CD1    1 
ATOM   6392  C  CD2    . TYR   B 1 9   ? -1.264  -2.136  11.729 1.00 32.40  ?  34  TYR   B CD2    1 
ATOM   6393  C  CE1    . TYR   B 1 9   ? -1.620  -3.293  14.217 1.00 31.01  ?  34  TYR   B CE1    1 
ATOM   6394  C  CE2    . TYR   B 1 9   ? -2.323  -1.744  12.516 1.00 32.77  ?  34  TYR   B CE2    1 
ATOM   6395  C  CZ     . TYR   B 1 9   ? -2.496  -2.326  13.756 1.00 32.75  ?  34  TYR   B CZ     1 
ATOM   6396  O  OH     . TYR   B 1 9   ? -3.554  -1.938  14.539 1.00 34.45  ?  34  TYR   B OH     1 
ATOM   6397  H  H      . TYR   B 1 9   ? 1.679   -1.174  10.753 1.00 38.18  ?  34  TYR   B H      1 
ATOM   6398  H  HA     . TYR   B 1 9   ? 2.349   -3.107  12.542 1.00 38.87  ?  34  TYR   B HA     1 
ATOM   6399  H  HB2    . TYR   B 1 9   ? 0.557   -3.318  10.371 1.00 37.01  ?  34  TYR   B HB2    1 
ATOM   6400  H  HB3    . TYR   B 1 9   ? 0.884   -4.500  11.382 1.00 37.01  ?  34  TYR   B HB3    1 
ATOM   6401  H  HD1    . TYR   B 1 9   ? 0.037   -4.317  13.734 1.00 37.23  ?  34  TYR   B HD1    1 
ATOM   6402  H  HD2    . TYR   B 1 9   ? -1.147  -1.746  10.893 1.00 38.87  ?  34  TYR   B HD2    1 
ATOM   6403  H  HE1    . TYR   B 1 9   ? -1.746  -3.682  15.052 1.00 37.20  ?  34  TYR   B HE1    1 
ATOM   6404  H  HE2    . TYR   B 1 9   ? -2.916  -1.093  12.216 1.00 39.31  ?  34  TYR   B HE2    1 
ATOM   6405  H  HH     . TYR   B 1 9   ? -4.000  -1.345  14.145 1.00 41.33  ?  34  TYR   B HH     1 
ATOM   6406  N  N      . GLN   B 1 10  ? 4.266   -3.944  11.327 1.00 32.20  ?  35  GLN   B N      1 
ATOM   6407  C  CA     . GLN   B 1 10  ? 5.467   -4.321  10.604 1.00 32.49  ?  35  GLN   B CA     1 
ATOM   6408  C  C      . GLN   B 1 10  ? 5.856   -5.763  10.877 1.00 30.75  ?  35  GLN   B C      1 
ATOM   6409  O  O      . GLN   B 1 10  ? 5.689   -6.274  11.989 1.00 30.26  ?  35  GLN   B O      1 
ATOM   6410  C  CB     . GLN   B 1 10  ? 6.630   -3.409  10.979 1.00 36.14  ?  35  GLN   B CB     1 
ATOM   6411  C  CG     . GLN   B 1 10  ? 6.381   -1.964  10.610 1.00 38.97  ?  35  GLN   B CG     1 
ATOM   6412  C  CD     . GLN   B 1 10  ? 7.592   -1.106  10.837 1.00 42.78  ?  35  GLN   B CD     1 
ATOM   6413  O  OE1    . GLN   B 1 10  ? 8.714   -1.603  10.921 1.00 45.79  ?  35  GLN   B OE1    1 
ATOM   6414  N  NE2    . GLN   B 1 10  ? 7.378   0.193   10.955 1.00 42.51  ?  35  GLN   B NE2    1 
ATOM   6415  H  H      . GLN   B 1 10  ? 4.300   -4.114  12.170 1.00 38.64  ?  35  GLN   B H      1 
ATOM   6416  H  HA     . GLN   B 1 10  ? 5.286   -4.250  9.654  1.00 38.99  ?  35  GLN   B HA     1 
ATOM   6417  H  HB2    . GLN   B 1 10  ? 6.770   -3.454  11.938 1.00 43.36  ?  35  GLN   B HB2    1 
ATOM   6418  H  HB3    . GLN   B 1 10  ? 7.427   -3.705  10.512 1.00 43.36  ?  35  GLN   B HB3    1 
ATOM   6419  H  HG2    . GLN   B 1 10  ? 6.144   -1.911  9.671  1.00 46.75  ?  35  GLN   B HG2    1 
ATOM   6420  H  HG3    . GLN   B 1 10  ? 5.658   -1.616  11.155 1.00 46.75  ?  35  GLN   B HG3    1 
ATOM   6421  H  HE21   . GLN   B 1 10  ? 6.577   0.503   10.901 1.00 51.01  ?  35  GLN   B HE21   1 
ATOM   6422  H  HE22   . GLN   B 1 10  ? 8.038   0.728   11.086 1.00 51.01  ?  35  GLN   B HE22   1 
ATOM   6423  N  N      . LYS   B 1 11  ? 6.378   -6.403  9.836  1.00 31.84  ?  36  LYS   B N      1 
ATOM   6424  C  CA     . LYS   B 1 11  ? 6.914   -7.751  9.890  1.00 32.74  ?  36  LYS   B CA     1 
ATOM   6425  C  C      . LYS   B 1 11  ? 8.431   -7.677  9.792  1.00 32.78  ?  36  LYS   B C      1 
ATOM   6426  O  O      . LYS   B 1 11  ? 8.979   -6.928  8.973  1.00 34.63  ?  36  LYS   B O      1 
ATOM   6427  C  CB     . LYS   B 1 11  ? 6.352   -8.610  8.752  1.00 36.23  ?  36  LYS   B CB     1 
ATOM   6428  C  CG     . LYS   B 1 11  ? 6.870   -10.048 8.733  1.00 39.32  ?  36  LYS   B CG     1 
ATOM   6429  C  CD     . LYS   B 1 11  ? 6.352   -10.801 7.522  1.00 43.69  ?  36  LYS   B CD     1 
ATOM   6430  C  CE     . LYS   B 1 11  ? 5.307   -11.843 7.914  1.00 48.37  ?  36  LYS   B CE     1 
ATOM   6431  N  NZ     . LYS   B 1 11  ? 5.132   -12.905 6.865  1.00 50.25  ?  36  LYS   B NZ     1 
ATOM   6432  H  H      . LYS   B 1 11  ? 6.434   -6.056  9.050  1.00 38.20  ?  36  LYS   B H      1 
ATOM   6433  H  HA     . LYS   B 1 11  ? 6.673   -8.177  10.727 1.00 39.29  ?  36  LYS   B HA     1 
ATOM   6434  H  HB2    . LYS   B 1 11  ? 5.387   -8.647  8.839  1.00 43.46  ?  36  LYS   B HB2    1 
ATOM   6435  H  HB3    . LYS   B 1 11  ? 6.594   -8.201  7.907  1.00 43.46  ?  36  LYS   B HB3    1 
ATOM   6436  H  HG2    . LYS   B 1 11  ? 7.839   -10.042 8.698  1.00 47.18  ?  36  LYS   B HG2    1 
ATOM   6437  H  HG3    . LYS   B 1 11  ? 6.569   -10.509 9.532  1.00 47.18  ?  36  LYS   B HG3    1 
ATOM   6438  H  HD2    . LYS   B 1 11  ? 5.941   -10.175 6.906  1.00 52.42  ?  36  LYS   B HD2    1 
ATOM   6439  H  HD3    . LYS   B 1 11  ? 7.090   -11.258 7.088  1.00 52.42  ?  36  LYS   B HD3    1 
ATOM   6440  H  HE2    . LYS   B 1 11  ? 5.584   -12.276 8.737  1.00 58.03  ?  36  LYS   B HE2    1 
ATOM   6441  H  HE3    . LYS   B 1 11  ? 4.453   -11.403 8.042  1.00 58.03  ?  36  LYS   B HE3    1 
ATOM   6442  H  HZ1    . LYS   B 1 11  ? 4.492   -13.473 7.110  1.00 60.29  ?  36  LYS   B HZ1    1 
ATOM   6443  H  HZ2    . LYS   B 1 11  ? 4.906   -12.532 6.089  1.00 60.29  ?  36  LYS   B HZ2    1 
ATOM   6444  H  HZ3    . LYS   B 1 11  ? 5.892   -13.356 6.757  1.00 60.29  ?  36  LYS   B HZ3    1 
ATOM   6445  N  N      . LYS   B 1 12  ? 9.101   -8.462  10.625 1.00 31.99  ?  37  LYS   B N      1 
ATOM   6446  C  CA     . LYS   B 1 12  ? 10.551  -8.507  10.671 1.00 32.57  ?  37  LYS   B CA     1 
ATOM   6447  C  C      . LYS   B 1 12  ? 11.040  -9.886  10.255 1.00 32.74  ?  37  LYS   B C      1 
ATOM   6448  O  O      . LYS   B 1 12  ? 10.391  -10.900 10.530 1.00 32.65  ?  37  LYS   B O      1 
ATOM   6449  C  CB     . LYS   B 1 12  ? 11.064  -8.191  12.084 1.00 33.44  ?  37  LYS   B CB     1 
ATOM   6450  C  CG     . LYS   B 1 12  ? 10.684  -6.801  12.592 1.00 34.97  ?  37  LYS   B CG     1 
ATOM   6451  C  CD     . LYS   B 1 12  ? 11.476  -5.739  11.843 1.00 36.38  ?  37  LYS   B CD     1 
ATOM   6452  C  CE     . LYS   B 1 12  ? 10.986  -4.308  12.114 1.00 39.13  ?  37  LYS   B CE     1 
ATOM   6453  N  NZ     . LYS   B 1 12  ? 11.836  -3.302  11.393 1.00 42.08  ?  37  LYS   B NZ     1 
ATOM   6454  H  H      . LYS   B 1 12  ? 8.725   -8.991  11.189 1.00 38.38  ?  37  LYS   B H      1 
ATOM   6455  H  HA     . LYS   B 1 12  ? 10.915  -7.854  10.053 1.00 39.08  ?  37  LYS   B HA     1 
ATOM   6456  H  HB2    . LYS   B 1 12  ? 10.693  -8.841  12.701 1.00 40.12  ?  37  LYS   B HB2    1 
ATOM   6457  H  HB3    . LYS   B 1 12  ? 12.032  -8.249  12.082 1.00 40.12  ?  37  LYS   B HB3    1 
ATOM   6458  H  HG2    . LYS   B 1 12  ? 9.738   -6.645  12.444 1.00 41.96  ?  37  LYS   B HG2    1 
ATOM   6459  H  HG3    . LYS   B 1 12  ? 10.888  -6.731  13.538 1.00 41.96  ?  37  LYS   B HG3    1 
ATOM   6460  H  HD2    . LYS   B 1 12  ? 12.406  -5.791  12.114 1.00 43.65  ?  37  LYS   B HD2    1 
ATOM   6461  H  HD3    . LYS   B 1 12  ? 11.399  -5.904  10.890 1.00 43.65  ?  37  LYS   B HD3    1 
ATOM   6462  H  HE2    . LYS   B 1 12  ? 10.072  -4.216  11.805 1.00 46.95  ?  37  LYS   B HE2    1 
ATOM   6463  H  HE3    . LYS   B 1 12  ? 11.035  -4.126  13.066 1.00 46.95  ?  37  LYS   B HE3    1 
ATOM   6464  H  HZ1    . LYS   B 1 12  ? 11.541  -2.479  11.561 1.00 50.49  ?  37  LYS   B HZ1    1 
ATOM   6465  H  HZ2    . LYS   B 1 12  ? 12.681  -3.367  11.665 1.00 50.49  ?  37  LYS   B HZ2    1 
ATOM   6466  H  HZ3    . LYS   B 1 12  ? 11.802  -3.447  10.516 1.00 50.49  ?  37  LYS   B HZ3    1 
ATOM   6467  N  N      . THR   B 1 13  ? 12.198  -9.916  9.598  1.00 32.04  ?  38  THR   B N      1 
ATOM   6468  C  CA     . THR   B 1 13  ? 12.886  -11.176 9.378  1.00 31.52  ?  38  THR   B CA     1 
ATOM   6469  C  C      . THR   B 1 13  ? 13.518  -11.631 10.690 1.00 30.98  ?  38  THR   B C      1 
ATOM   6470  O  O      . THR   B 1 13  ? 13.658  -10.853 11.637 1.00 30.91  ?  38  THR   B O      1 
ATOM   6471  C  CB     . THR   B 1 13  ? 13.970  -11.041 8.309  1.00 32.43  ?  38  THR   B CB     1 
ATOM   6472  O  OG1    . THR   B 1 13  ? 15.035  -10.224 8.814  1.00 32.96  ?  38  THR   B OG1    1 
ATOM   6473  C  CG2    . THR   B 1 13  ? 13.414  -10.436 7.015  1.00 34.39  ?  38  THR   B CG2    1 
ATOM   6474  H  H      . THR   B 1 13  ? 12.598  -9.227  9.275  1.00 38.44  ?  38  THR   B H      1 
ATOM   6475  H  HA     . THR   B 1 13  ? 12.251  -11.839 9.065  1.00 37.82  ?  38  THR   B HA     1 
ATOM   6476  H  HB     . THR   B 1 13  ? 14.313  -11.921 8.089  1.00 38.92  ?  38  THR   B HB     1 
ATOM   6477  H  HG1    . THR   B 1 13  ? 15.625  -10.124 8.224  1.00 39.54  ?  38  THR   B HG1    1 
ATOM   6478  H  HG21   . THR   B 1 13  ? 14.103  -10.423 6.332  1.00 41.26  ?  38  THR   B HG21   1 
ATOM   6479  H  HG22   . THR   B 1 13  ? 12.666  -10.965 6.696  1.00 41.26  ?  38  THR   B HG22   1 
ATOM   6480  H  HG23   . THR   B 1 13  ? 13.112  -9.528  7.176  1.00 41.26  ?  38  THR   B HG23   1 
ATOM   6481  N  N      . GLN   B 1 14  ? 13.923  -12.897 10.754 1.00 31.77  ?  39  GLN   B N      1 
ATOM   6482  C  CA     . GLN   B 1 14  ? 14.557  -13.380 11.977 1.00 32.62  ?  39  GLN   B CA     1 
ATOM   6483  C  C      . GLN   B 1 14  ? 15.823  -12.585 12.293 1.00 30.76  ?  39  GLN   B C      1 
ATOM   6484  O  O      . GLN   B 1 14  ? 16.067  -12.222 13.450 1.00 29.81  ?  39  GLN   B O      1 
ATOM   6485  C  CB     . GLN   B 1 14  ? 14.879  -14.868 11.847 1.00 36.39  ?  39  GLN   B CB     1 
ATOM   6486  C  CG     . GLN   B 1 14  ? 13.746  -15.707 11.284 1.00 40.52  ?  39  GLN   B CG     1 
ATOM   6487  C  CD     . GLN   B 1 14  ? 14.212  -17.091 10.843 1.00 44.34  ?  39  GLN   B CD     1 
ATOM   6488  O  OE1    . GLN   B 1 14  ? 14.324  -18.013 11.654 1.00 46.95  ?  39  GLN   B OE1    1 
ATOM   6489  N  NE2    . GLN   B 1 14  ? 14.500  -17.233 9.555  1.00 45.20  ?  39  GLN   B NE2    1 
ATOM   6490  H  H      . GLN   B 1 14  ? 13.846  -13.478 10.125 1.00 38.12  ?  39  GLN   B H      1 
ATOM   6491  H  HA     . GLN   B 1 14  ? 13.938  -13.268 12.716 1.00 39.13  ?  39  GLN   B HA     1 
ATOM   6492  H  HB2    . GLN   B 1 14  ? 15.641  -14.969 11.255 1.00 43.67  ?  39  GLN   B HB2    1 
ATOM   6493  H  HB3    . GLN   B 1 14  ? 15.094  -15.217 12.726 1.00 43.67  ?  39  GLN   B HB3    1 
ATOM   6494  H  HG2    . GLN   B 1 14  ? 13.065  -15.821 11.966 1.00 48.62  ?  39  GLN   B HG2    1 
ATOM   6495  H  HG3    . GLN   B 1 14  ? 13.369  -15.256 10.512 1.00 48.62  ?  39  GLN   B HG3    1 
ATOM   6496  H  HE21   . GLN   B 1 14  ? 14.419  -16.565 9.020  1.00 54.24  ?  39  GLN   B HE21   1 
ATOM   6497  H  HE22   . GLN   B 1 14  ? 14.767  -17.994 9.255  1.00 54.24  ?  39  GLN   B HE22   1 
ATOM   6498  N  N      . LEU   B 1 15  ? 16.648  -12.319 11.273 1.00 30.96  ?  40  LEU   B N      1 
ATOM   6499  C  CA     . LEU   B 1 15  ? 17.883  -11.567 11.478 1.00 31.44  ?  40  LEU   B CA     1 
ATOM   6500  C  C      . LEU   B 1 15  ? 17.598  -10.137 11.921 1.00 30.37  ?  40  LEU   B C      1 
ATOM   6501  O  O      . LEU   B 1 15  ? 18.237  -9.623  12.847 1.00 29.88  ?  40  LEU   B O      1 
ATOM   6502  C  CB     . LEU   B 1 15  ? 18.703  -11.577 10.187 1.00 34.11  ?  40  LEU   B CB     1 
ATOM   6503  C  CG     . LEU   B 1 15  ? 20.008  -10.791 10.197 1.00 37.26  ?  40  LEU   B CG     1 
ATOM   6504  C  CD1    . LEU   B 1 15  ? 20.865  -11.208 11.360 1.00 38.78  ?  40  LEU   B CD1    1 
ATOM   6505  C  CD2    . LEU   B 1 15  ? 20.759  -10.990 8.883  1.00 39.71  ?  40  LEU   B CD2    1 
ATOM   6506  H  H      . LEU   B 1 15  ? 16.514  -12.562 10.459 1.00 37.15  ?  40  LEU   B H      1 
ATOM   6507  H  HA     . LEU   B 1 15  ? 18.402  -11.993 12.178 1.00 37.72  ?  40  LEU   B HA     1 
ATOM   6508  H  HB2    . LEU   B 1 15  ? 18.928  -12.498 9.982  1.00 40.93  ?  40  LEU   B HB2    1 
ATOM   6509  H  HB3    . LEU   B 1 15  ? 18.152  -11.205 9.480  1.00 40.93  ?  40  LEU   B HB3    1 
ATOM   6510  H  HG     . LEU   B 1 15  ? 19.808  -9.846  10.292 1.00 44.70  ?  40  LEU   B HG     1 
ATOM   6511  H  HD11   . LEU   B 1 15  ? 21.748  -10.820 11.258 1.00 46.53  ?  40  LEU   B HD11   1 
ATOM   6512  H  HD12   . LEU   B 1 15  ? 20.458  -10.891 12.182 1.00 46.53  ?  40  LEU   B HD12   1 
ATOM   6513  H  HD13   . LEU   B 1 15  ? 20.928  -12.176 11.375 1.00 46.53  ?  40  LEU   B HD13   1 
ATOM   6514  H  HD21   . LEU   B 1 15  ? 21.581  -10.476 8.908  1.00 47.65  ?  40  LEU   B HD21   1 
ATOM   6515  H  HD22   . LEU   B 1 15  ? 20.961  -11.933 8.774  1.00 47.65  ?  40  LEU   B HD22   1 
ATOM   6516  H  HD23   . LEU   B 1 15  ? 20.201  -10.685 8.150  1.00 47.65  ?  40  LEU   B HD23   1 
ATOM   6517  N  N      . GLU   B 1 16  ? 16.634  -9.480  11.279 1.00 30.26  ?  41  GLU   B N      1 
ATOM   6518  C  CA     . GLU   B 1 16  ? 16.247  -8.140  11.710 1.00 31.41  ?  41  GLU   B CA     1 
ATOM   6519  C  C      . GLU   B 1 16  ? 15.775  -8.135  13.157 1.00 29.79  ?  41  GLU   B C      1 
ATOM   6520  O  O      . GLU   B 1 16  ? 16.043  -7.191  13.911 1.00 29.80  ?  41  GLU   B O      1 
ATOM   6521  C  CB     . GLU   B 1 16  ? 15.144  -7.606  10.806 1.00 34.16  ?  41  GLU   B CB     1 
ATOM   6522  C  CG     . GLU   B 1 16  ? 15.620  -7.240  9.432  1.00 36.12  ?  41  GLU   B CG     1 
ATOM   6523  C  CD     . GLU   B 1 16  ? 14.483  -6.893  8.497  1.00 38.01  ?  41  GLU   B CD     1 
ATOM   6524  O  OE1    . GLU   B 1 16  ? 13.319  -7.223  8.806  1.00 36.23  ?  41  GLU   B OE1    1 
ATOM   6525  O  OE2    . GLU   B 1 16  ? 14.753  -6.285  7.445  1.00 40.84  ?  41  GLU   B OE2    1 
ATOM   6526  H  H      . GLU   B 1 16  ? 16.196  -9.781  10.603 1.00 36.30  ?  41  GLU   B H      1 
ATOM   6527  H  HA     . GLU   B 1 16  ? 17.020  -7.558  11.640 1.00 37.68  ?  41  GLU   B HA     1 
ATOM   6528  H  HB2    . GLU   B 1 16  ? 14.460  -8.288  10.712 1.00 40.99  ?  41  GLU   B HB2    1 
ATOM   6529  H  HB3    . GLU   B 1 16  ? 14.765  -6.810  11.211 1.00 40.99  ?  41  GLU   B HB3    1 
ATOM   6530  H  HG2    . GLU   B 1 16  ? 16.205  -6.469  9.495  1.00 43.34  ?  41  GLU   B HG2    1 
ATOM   6531  H  HG3    . GLU   B 1 16  ? 16.102  -7.992  9.054  1.00 43.34  ?  41  GLU   B HG3    1 
ATOM   6532  N  N      . HIS   B 1 17  ? 15.050  -9.169  13.556 1.00 28.19  ?  42  HIS   B N      1 
ATOM   6533  C  CA     . HIS   B 1 17  ? 14.499  -9.213  14.904 1.00 26.42  ?  42  HIS   B CA     1 
ATOM   6534  C  C      . HIS   B 1 17  ? 15.602  -9.327  15.943 1.00 25.99  ?  42  HIS   B C      1 
ATOM   6535  O  O      . HIS   B 1 17  ? 15.533  -8.693  17.002 1.00 27.87  ?  42  HIS   B O      1 
ATOM   6536  C  CB     . HIS   B 1 17  ? 13.526  -10.383 14.973 1.00 27.33  ?  42  HIS   B CB     1 
ATOM   6537  C  CG     . HIS   B 1 17  ? 12.693  -10.428 16.214 1.00 26.78  ?  42  HIS   B CG     1 
ATOM   6538  N  ND1    . HIS   B 1 17  ? 13.011  -11.216 17.302 1.00 26.15  ?  42  HIS   B ND1    1 
ATOM   6539  C  CD2    . HIS   B 1 17  ? 11.518  -9.829  16.512 1.00 27.09  ?  42  HIS   B CD2    1 
ATOM   6540  C  CE1    . HIS   B 1 17  ? 12.085  -11.066 18.232 1.00 25.34  ?  42  HIS   B CE1    1 
ATOM   6541  N  NE2    . HIS   B 1 17  ? 11.162  -10.239 17.773 1.00 26.20  ?  42  HIS   B NE2    1 
ATOM   6542  H  H      . HIS   B 1 17  ? 14.862  -9.854  13.071 1.00 33.82  ?  42  HIS   B H      1 
ATOM   6543  H  HA     . HIS   B 1 17  ? 14.016  -8.396  15.107 1.00 31.70  ?  42  HIS   B HA     1 
ATOM   6544  H  HB2    . HIS   B 1 17  ? 12.921  -10.326 14.217 1.00 32.79  ?  42  HIS   B HB2    1 
ATOM   6545  H  HB3    . HIS   B 1 17  ? 14.033  -11.209 14.932 1.00 32.79  ?  42  HIS   B HB3    1 
ATOM   6546  H  HD2    . HIS   B 1 17  ? 11.041  -9.248  15.965 1.00 32.50  ?  42  HIS   B HD2    1 
ATOM   6547  H  HE1    . HIS   B 1 17  ? 12.083  -11.474 19.068 1.00 30.41  ?  42  HIS   B HE1    1 
ATOM   6548  H  HE2    . HIS   B 1 17  ? 10.454  -9.996  18.196 1.00 31.44  ?  42  HIS   B HE2    1 
ATOM   6549  N  N      . ILE   B 1 18  ? 16.624  -10.133 15.657 1.00 25.06  ?  43  ILE   B N      1 
ATOM   6550  C  CA     . ILE   B 1 18  ? 17.735  -10.300 16.591 1.00 25.20  ?  43  ILE   B CA     1 
ATOM   6551  C  C      . ILE   B 1 18  ? 18.450  -8.971  16.834 1.00 24.93  ?  43  ILE   B C      1 
ATOM   6552  O  O      . ILE   B 1 18  ? 18.776  -8.627  17.975 1.00 25.51  ?  43  ILE   B O      1 
ATOM   6553  C  CB     . ILE   B 1 18  ? 18.696  -11.385 16.067 1.00 25.64  ?  43  ILE   B CB     1 
ATOM   6554  C  CG1    . ILE   B 1 18  ? 18.013  -12.753 16.139 1.00 25.79  ?  43  ILE   B CG1    1 
ATOM   6555  C  CG2    . ILE   B 1 18  ? 19.982  -11.394 16.871 1.00 26.78  ?  43  ILE   B CG2    1 
ATOM   6556  C  CD1    . ILE   B 1 18  ? 18.642  -13.811 15.276 1.00 25.92  ?  43  ILE   B CD1    1 
ATOM   6557  H  H      . ILE   B 1 18  ? 16.699  -10.591 14.933 1.00 30.07  ?  43  ILE   B H      1 
ATOM   6558  H  HA     . ILE   B 1 18  ? 17.381  -10.594 17.446 1.00 30.23  ?  43  ILE   B HA     1 
ATOM   6559  H  HB     . ILE   B 1 18  ? 18.918  -11.185 15.144 1.00 30.76  ?  43  ILE   B HB     1 
ATOM   6560  H  HG12   . ILE   B 1 18  ? 18.045  -13.067 17.057 1.00 30.94  ?  43  ILE   B HG12   1 
ATOM   6561  H  HG13   . ILE   B 1 18  ? 17.091  -12.653 15.855 1.00 30.94  ?  43  ILE   B HG13   1 
ATOM   6562  H  HG21   . ILE   B 1 18  ? 20.446  -12.231 16.716 1.00 32.13  ?  43  ILE   B HG21   1 
ATOM   6563  H  HG22   . ILE   B 1 18  ? 20.537  -10.650 16.588 1.00 32.13  ?  43  ILE   B HG22   1 
ATOM   6564  H  HG23   . ILE   B 1 18  ? 19.766  -11.305 17.813 1.00 32.13  ?  43  ILE   B HG23   1 
ATOM   6565  H  HD11   . ILE   B 1 18  ? 18.120  -14.626 15.345 1.00 31.10  ?  43  ILE   B HD11   1 
ATOM   6566  H  HD12   . ILE   B 1 18  ? 18.652  -13.503 14.356 1.00 31.10  ?  43  ILE   B HD12   1 
ATOM   6567  H  HD13   . ILE   B 1 18  ? 19.548  -13.971 15.582 1.00 31.10  ?  43  ILE   B HD13   1 
ATOM   6568  N  N      . LEU   B 1 19  ? 18.711  -8.204  15.775 1.00 26.98  ?  44  LEU   B N      1 
ATOM   6569  C  CA     . LEU   B 1 19  ? 19.391  -6.921  15.957 1.00 28.38  ?  44  LEU   B CA     1 
ATOM   6570  C  C      . LEU   B 1 19  ? 18.473  -5.875  16.594 1.00 29.89  ?  44  LEU   B C      1 
ATOM   6571  O  O      . LEU   B 1 19  ? 18.945  -5.020  17.355 1.00 30.84  ?  44  LEU   B O      1 
ATOM   6572  C  CB     . LEU   B 1 19  ? 19.928  -6.421  14.610 1.00 30.63  ?  44  LEU   B CB     1 
ATOM   6573  C  CG     . LEU   B 1 19  ? 21.081  -7.254  14.042 1.00 33.02  ?  44  LEU   B CG     1 
ATOM   6574  C  CD1    . LEU   B 1 19  ? 21.296  -6.970  12.565 1.00 35.69  ?  44  LEU   B CD1    1 
ATOM   6575  C  CD2    . LEU   B 1 19  ? 22.379  -7.002  14.821 1.00 32.48  ?  44  LEU   B CD2    1 
ATOM   6576  H  H      . LEU   B 1 19  ? 18.511  -8.398  14.961 1.00 32.37  ?  44  LEU   B H      1 
ATOM   6577  H  HA     . LEU   B 1 19  ? 20.146  -7.049  16.552 1.00 34.05  ?  44  LEU   B HA     1 
ATOM   6578  H  HB2    . LEU   B 1 19  ? 19.206  -6.439  13.964 1.00 36.75  ?  44  LEU   B HB2    1 
ATOM   6579  H  HB3    . LEU   B 1 19  ? 20.249  -5.513  14.724 1.00 36.75  ?  44  LEU   B HB3    1 
ATOM   6580  H  HG     . LEU   B 1 19  ? 20.846  -8.191  14.134 1.00 39.62  ?  44  LEU   B HG     1 
ATOM   6581  H  HD11   . LEU   B 1 19  ? 22.030  -7.516  12.242 1.00 42.82  ?  44  LEU   B HD11   1 
ATOM   6582  H  HD12   . LEU   B 1 19  ? 20.484  -7.187  12.081 1.00 42.82  ?  44  LEU   B HD12   1 
ATOM   6583  H  HD13   . LEU   B 1 19  ? 21.509  -6.031  12.452 1.00 42.82  ?  44  LEU   B HD13   1 
ATOM   6584  H  HD21   . LEU   B 1 19  ? 23.102  -7.490  14.398 1.00 38.97  ?  44  LEU   B HD21   1 
ATOM   6585  H  HD22   . LEU   B 1 19  ? 22.572  -6.051  14.814 1.00 38.97  ?  44  LEU   B HD22   1 
ATOM   6586  H  HD23   . LEU   B 1 19  ? 22.263  -7.308  15.734 1.00 38.97  ?  44  LEU   B HD23   1 
ATOM   6587  N  N      . LEU   B 1 20  ? 17.169  -5.939  16.320 1.00 29.88  ?  45  LEU   B N      1 
ATOM   6588  C  CA     . LEU   B 1 20  ? 16.223  -4.981  16.884 1.00 30.62  ?  45  LEU   B CA     1 
ATOM   6589  C  C      . LEU   B 1 20  ? 15.862  -5.279  18.334 1.00 29.00  ?  45  LEU   B C      1 
ATOM   6590  O  O      . LEU   B 1 20  ? 15.604  -4.350  19.121 1.00 31.18  ?  45  LEU   B O      1 
ATOM   6591  C  CB     . LEU   B 1 20  ? 14.956  -4.987  16.034 1.00 32.04  ?  45  LEU   B CB     1 
ATOM   6592  C  CG     . LEU   B 1 20  ? 13.887  -3.964  16.380 1.00 35.73  ?  45  LEU   B CG     1 
ATOM   6593  C  CD1    . LEU   B 1 20  ? 14.388  -2.589  15.967 1.00 37.11  ?  45  LEU   B CD1    1 
ATOM   6594  C  CD2    . LEU   B 1 20  ? 12.592  -4.312  15.702 1.00 37.11  ?  45  LEU   B CD2    1 
ATOM   6595  H  H      . LEU   B 1 20  ? 16.807  -6.528  15.809 1.00 35.85  ?  45  LEU   B H      1 
ATOM   6596  H  HA     . LEU   B 1 20  ? 16.626  -4.099  16.866 1.00 36.74  ?  45  LEU   B HA     1 
ATOM   6597  H  HB2    . LEU   B 1 20  ? 15.215  -4.825  15.113 1.00 38.44  ?  45  LEU   B HB2    1 
ATOM   6598  H  HB3    . LEU   B 1 20  ? 14.547  -5.862  16.115 1.00 38.44  ?  45  LEU   B HB3    1 
ATOM   6599  H  HG     . LEU   B 1 20  ? 13.709  -3.958  17.333 1.00 42.87  ?  45  LEU   B HG     1 
ATOM   6600  H  HD11   . LEU   B 1 20  ? 13.690  -1.936  16.132 1.00 44.53  ?  45  LEU   B HD11   1 
ATOM   6601  H  HD12   . LEU   B 1 20  ? 15.176  -2.370  16.488 1.00 44.53  ?  45  LEU   B HD12   1 
ATOM   6602  H  HD13   . LEU   B 1 20  ? 14.610  -2.605  15.023 1.00 44.53  ?  45  LEU   B HD13   1 
ATOM   6603  H  HD21   . LEU   B 1 20  ? 11.932  -3.635  15.917 1.00 44.53  ?  45  LEU   B HD21   1 
ATOM   6604  H  HD22   . LEU   B 1 20  ? 12.736  -4.341  14.743 1.00 44.53  ?  45  LEU   B HD22   1 
ATOM   6605  H  HD23   . LEU   B 1 20  ? 12.293  -5.179  16.018 1.00 44.53  ?  45  LEU   B HD23   1 
ATOM   6606  N  N      . ARG   B 1 21  ? 15.818  -6.563  18.685 1.00 26.31  ?  46  ARG   B N      1 
ATOM   6607  C  CA     . ARG   B 1 21  ? 15.382  -7.038  19.996 1.00 24.67  ?  46  ARG   B CA     1 
ATOM   6608  C  C      . ARG   B 1 21  ? 16.426  -8.016  20.527 1.00 23.92  ?  46  ARG   B C      1 
ATOM   6609  O  O      . ARG   B 1 21  ? 16.162  -9.217  20.651 1.00 24.66  ?  46  ARG   B O      1 
ATOM   6610  C  CB     . ARG   B 1 21  ? 14.015  -7.716  19.890 1.00 26.75  ?  46  ARG   B CB     1 
ATOM   6611  C  CG     . ARG   B 1 21  ? 12.858  -6.804  19.518 1.00 27.51  ?  46  ARG   B CG     1 
ATOM   6612  C  CD     . ARG   B 1 21  ? 12.302  -6.081  20.743 1.00 27.30  ?  46  ARG   B CD     1 
ATOM   6613  N  NE     . ARG   B 1 21  ? 11.278  -5.098  20.394 1.00 27.98  ?  46  ARG   B NE     1 
ATOM   6614  C  CZ     . ARG   B 1 21  ? 11.536  -3.830  20.096 1.00 28.88  ?  46  ARG   B CZ     1 
ATOM   6615  N  NH1    . ARG   B 1 21  ? 12.785  -3.393  20.108 1.00 28.62  ?  46  ARG   B NH1    1 
ATOM   6616  N  NH2    . ARG   B 1 21  ? 10.554  -2.999  19.793 1.00 31.48  ?  46  ARG   B NH2    1 
ATOM   6617  H  H      . ARG   B 1 21  ? 16.045  -7.204  18.158 1.00 31.57  ?  46  ARG   B H      1 
ATOM   6618  H  HA     . ARG   B 1 21  ? 15.314  -6.290  20.610 1.00 29.60  ?  46  ARG   B HA     1 
ATOM   6619  H  HB2    . ARG   B 1 21  ? 14.069  -8.406  19.210 1.00 32.10  ?  46  ARG   B HB2    1 
ATOM   6620  H  HB3    . ARG   B 1 21  ? 13.804  -8.114  20.750 1.00 32.10  ?  46  ARG   B HB3    1 
ATOM   6621  H  HG2    . ARG   B 1 21  ? 13.164  -6.138  18.883 1.00 33.01  ?  46  ARG   B HG2    1 
ATOM   6622  H  HG3    . ARG   B 1 21  ? 12.145  -7.332  19.126 1.00 33.01  ?  46  ARG   B HG3    1 
ATOM   6623  H  HD2    . ARG   B 1 21  ? 11.904  -6.731  21.342 1.00 32.76  ?  46  ARG   B HD2    1 
ATOM   6624  H  HD3    . ARG   B 1 21  ? 13.025  -5.615  21.192 1.00 32.76  ?  46  ARG   B HD3    1 
ATOM   6625  H  HE     . ARG   B 1 21  ? 10.457  -5.357  20.381 1.00 33.57  ?  46  ARG   B HE     1 
ATOM   6626  H  HH11   . ARG   B 1 21  ? 13.427  -3.929  20.308 1.00 34.34  ?  46  ARG   B HH11   1 
ATOM   6627  H  HH12   . ARG   B 1 21  ? 12.955  -2.572  19.915 1.00 34.34  ?  46  ARG   B HH12   1 
ATOM   6628  H  HH21   . ARG   B 1 21  ? 9.740   -3.278  19.789 1.00 37.76  ?  46  ARG   B HH21   1 
ATOM   6629  H  HH22   . ARG   B 1 21  ? 10.728  -2.179  19.601 1.00 37.76  ?  46  ARG   B HH22   1 
ATOM   6630  N  N      . PRO   B 1 22  ? 17.634  -7.536  20.835 1.00 23.42  ?  47  PRO   B N      1 
ATOM   6631  C  CA     . PRO   B 1 22  ? 18.714  -8.464  21.219 1.00 23.20  ?  47  PRO   B CA     1 
ATOM   6632  C  C      . PRO   B 1 22  ? 18.533  -9.118  22.579 1.00 20.66  ?  47  PRO   B C      1 
ATOM   6633  O  O      . PRO   B 1 22  ? 19.133  -10.176 22.824 1.00 20.68  ?  47  PRO   B O      1 
ATOM   6634  C  CB     . PRO   B 1 22  ? 19.969  -7.574  21.200 1.00 25.08  ?  47  PRO   B CB     1 
ATOM   6635  C  CG     . PRO   B 1 22  ? 19.436  -6.170  21.355 1.00 27.55  ?  47  PRO   B CG     1 
ATOM   6636  C  CD     . PRO   B 1 22  ? 18.102  -6.146  20.682 1.00 25.95  ?  47  PRO   B CD     1 
ATOM   6637  H  HA     . PRO   B 1 22  ? 18.791  -9.159  20.547 1.00 27.83  ?  47  PRO   B HA     1 
ATOM   6638  H  HB2    . PRO   B 1 22  ? 20.554  -7.809  21.937 1.00 30.09  ?  47  PRO   B HB2    1 
ATOM   6639  H  HB3    . PRO   B 1 22  ? 20.438  -7.679  20.358 1.00 30.09  ?  47  PRO   B HB3    1 
ATOM   6640  H  HG2    . PRO   B 1 22  ? 19.347  -5.959  22.297 1.00 33.05  ?  47  PRO   B HG2    1 
ATOM   6641  H  HG3    . PRO   B 1 22  ? 20.043  -5.544  20.931 1.00 33.05  ?  47  PRO   B HG3    1 
ATOM   6642  H  HD2    . PRO   B 1 22  ? 17.501  -5.527  21.125 1.00 31.13  ?  47  PRO   B HD2    1 
ATOM   6643  H  HD3    . PRO   B 1 22  ? 18.190  -5.911  19.745 1.00 31.13  ?  47  PRO   B HD3    1 
ATOM   6644  N  N      . ASP   B 1 23  ? 17.708  -8.545  23.459 1.00 20.69  ?  48  ASP   B N      1 
ATOM   6645  C  CA     . ASP   B 1 23  ? 17.747  -8.927  24.869 1.00 20.18  ?  48  ASP   B CA     1 
ATOM   6646  C  C      . ASP   B 1 23  ? 17.407  -10.389 25.113 1.00 20.18  ?  48  ASP   B C      1 
ATOM   6647  O  O      . ASP   B 1 23  ? 18.028  -11.016 25.974 1.00 20.25  ?  48  ASP   B O      1 
ATOM   6648  C  CB     . ASP   B 1 23  ? 16.801  -8.048  25.676 1.00 21.79  ?  48  ASP   B CB     1 
ATOM   6649  C  CG     . ASP   B 1 23  ? 17.228  -6.630  25.669 1.00 24.29  ?  48  ASP   B CG     1 
ATOM   6650  O  OD1    . ASP   B 1 23  ? 17.082  -5.995  24.606 1.00 28.74  ?  48  ASP   B OD1    1 
ATOM   6651  O  OD2    . ASP   B 1 23  ? 17.726  -6.169  26.714 1.00 24.40  ?  48  ASP   B OD2    1 
ATOM   6652  H  H      . ASP   B 1 23  ? 17.125  -7.943  23.267 1.00 24.82  ?  48  ASP   B H      1 
ATOM   6653  H  HA     . ASP   B 1 23  ? 18.659  -8.789  25.169 1.00 24.21  ?  48  ASP   B HA     1 
ATOM   6654  H  HB2    . ASP   B 1 23  ? 15.911  -8.100  25.294 1.00 26.14  ?  48  ASP   B HB2    1 
ATOM   6655  H  HB3    . ASP   B 1 23  ? 16.785  -8.356  26.596 1.00 26.14  ?  48  ASP   B HB3    1 
ATOM   6656  N  N      . THR   B 1 24  ? 16.399  -10.943 24.421 1.00 20.86  ?  49  THR   B N      1 
ATOM   6657  C  CA     . THR   B 1 24  ? 16.075  -12.335 24.714 1.00 21.31  ?  49  THR   B CA     1 
ATOM   6658  C  C      . THR   B 1 24  ? 17.056  -13.296 24.053 1.00 21.64  ?  49  THR   B C      1 
ATOM   6659  O  O      . THR   B 1 24  ? 17.024  -14.496 24.352 1.00 23.06  ?  49  THR   B O      1 
ATOM   6660  C  CB     . THR   B 1 24  ? 14.646  -12.747 24.303 1.00 21.23  ?  49  THR   B CB     1 
ATOM   6661  O  OG1    . THR   B 1 24  ? 14.465  -12.674 22.883 1.00 24.55  ?  49  THR   B OG1    1 
ATOM   6662  C  CG2    . THR   B 1 24  ? 13.600  -11.891 25.013 1.00 20.14  ?  49  THR   B CG2    1 
ATOM   6663  H  H      . THR   B 1 24  ? 15.924  -10.554 23.818 1.00 25.03  ?  49  THR   B H      1 
ATOM   6664  H  HA     . THR   B 1 24  ? 16.103  -12.422 25.680 1.00 25.57  ?  49  THR   B HA     1 
ATOM   6665  H  HB     . THR   B 1 24  ? 14.510  -13.669 24.572 1.00 25.47  ?  49  THR   B HB     1 
ATOM   6666  H  HG1    . THR   B 1 24  ? 14.625  -11.895 22.612 1.00 29.45  ?  49  THR   B HG1    1 
ATOM   6667  H  HG21   . THR   B 1 24  ? 12.709  -12.171 24.752 1.00 24.16  ?  49  THR   B HG21   1 
ATOM   6668  H  HG22   . THR   B 1 24  ? 13.691  -11.985 25.974 1.00 24.16  ?  49  THR   B HG22   1 
ATOM   6669  H  HG23   . THR   B 1 24  ? 13.719  -10.958 24.776 1.00 24.16  ?  49  THR   B HG23   1 
ATOM   6670  N  N      . TYR   B 1 25  ? 17.928  -12.801 23.175 1.00 20.05  ?  50  TYR   B N      1 
ATOM   6671  C  CA     . TYR   B 1 25  ? 18.909  -13.658 22.530 1.00 19.32  ?  50  TYR   B CA     1 
ATOM   6672  C  C      . TYR   B 1 25  ? 20.257  -13.666 23.250 1.00 19.17  ?  50  TYR   B C      1 
ATOM   6673  O  O      . TYR   B 1 25  ? 20.825  -14.741 23.464 1.00 18.81  ?  50  TYR   B O      1 
ATOM   6674  C  CB     . TYR   B 1 25  ? 19.107  -13.229 21.078 1.00 20.44  ?  50  TYR   B CB     1 
ATOM   6675  C  CG     . TYR   B 1 25  ? 17.872  -13.280 20.216 1.00 21.27  ?  50  TYR   B CG     1 
ATOM   6676  C  CD1    . TYR   B 1 25  ? 17.507  -14.456 19.576 1.00 23.03  ?  50  TYR   B CD1    1 
ATOM   6677  C  CD2    . TYR   B 1 25  ? 17.080  -12.151 20.014 1.00 21.82  ?  50  TYR   B CD2    1 
ATOM   6678  C  CE1    . TYR   B 1 25  ? 16.390  -14.516 18.765 1.00 23.40  ?  50  TYR   B CE1    1 
ATOM   6679  C  CE2    . TYR   B 1 25  ? 15.953  -12.199 19.202 1.00 22.40  ?  50  TYR   B CE2    1 
ATOM   6680  C  CZ     . TYR   B 1 25  ? 15.609  -13.391 18.591 1.00 24.41  ?  50  TYR   B CZ     1 
ATOM   6681  O  OH     . TYR   B 1 25  ? 14.504  -13.464 17.769 1.00 27.67  ?  50  TYR   B OH     1 
ATOM   6682  H  H      . TYR   B 1 25  ? 17.968  -11.975 22.939 1.00 24.06  ?  50  TYR   B H      1 
ATOM   6683  H  HA     . TYR   B 1 25  ? 18.563  -14.564 22.543 1.00 23.17  ?  50  TYR   B HA     1 
ATOM   6684  H  HB2    . TYR   B 1 25  ? 19.427  -12.313 21.070 1.00 24.52  ?  50  TYR   B HB2    1 
ATOM   6685  H  HB3    . TYR   B 1 25  ? 19.767  -13.814 20.673 1.00 24.52  ?  50  TYR   B HB3    1 
ATOM   6686  H  HD1    . TYR   B 1 25  ? 18.025  -15.219 19.694 1.00 27.62  ?  50  TYR   B HD1    1 
ATOM   6687  H  HD2    . TYR   B 1 25  ? 17.310  -11.352 20.431 1.00 26.18  ?  50  TYR   B HD2    1 
ATOM   6688  H  HE1    . TYR   B 1 25  ? 16.164  -15.311 18.338 1.00 28.08  ?  50  TYR   B HE1    1 
ATOM   6689  H  HE2    . TYR   B 1 25  ? 15.436  -11.437 19.070 1.00 26.88  ?  50  TYR   B HE2    1 
ATOM   6690  H  HH     . TYR   B 1 25  ? 14.600  -12.948 17.113 1.00 33.20  ?  50  TYR   B HH     1 
ATOM   6691  N  N      . ILE   B 1 26  ? 20.786  -12.497 23.628 1.00 18.11  ?  51  ILE   B N      1 
ATOM   6692  C  CA     . ILE   B 1 26  ? 22.125  -12.404 24.202 1.00 18.54  ?  51  ILE   B CA     1 
ATOM   6693  C  C      . ILE   B 1 26  ? 22.167  -11.659 25.528 1.00 17.06  ?  51  ILE   B C      1 
ATOM   6694  O  O      . ILE   B 1 26  ? 23.244  -11.530 26.113 1.00 18.87  ?  51  ILE   B O      1 
ATOM   6695  C  CB     . ILE   B 1 26  ? 23.126  -11.766 23.211 1.00 19.71  ?  51  ILE   B CB     1 
ATOM   6696  C  CG1    . ILE   B 1 26  ? 22.741  -10.322 22.870 1.00 21.00  ?  51  ILE   B CG1    1 
ATOM   6697  C  CG2    . ILE   B 1 26  ? 23.238  -12.617 21.933 1.00 20.39  ?  51  ILE   B CG2    1 
ATOM   6698  C  CD1    . ILE   B 1 26  ? 23.831  -9.568  22.099 1.00 21.44  ?  51  ILE   B CD1    1 
ATOM   6699  H  H      . ILE   B 1 26  ? 20.382  -11.741 23.561 1.00 21.73  ?  51  ILE   B H      1 
ATOM   6700  H  HA     . ILE   B 1 26  ? 22.424  -13.308 24.387 1.00 22.24  ?  51  ILE   B HA     1 
ATOM   6701  H  HB     . ILE   B 1 26  ? 23.993  -11.742 23.645 1.00 23.65  ?  51  ILE   B HB     1 
ATOM   6702  H  HG12   . ILE   B 1 26  ? 21.941  -10.333 22.321 1.00 25.20  ?  51  ILE   B HG12   1 
ATOM   6703  H  HG13   . ILE   B 1 26  ? 22.571  -9.841  23.695 1.00 25.20  ?  51  ILE   B HG13   1 
ATOM   6704  H  HG21   . ILE   B 1 26  ? 23.934  -12.248 21.368 1.00 24.47  ?  51  ILE   B HG21   1 
ATOM   6705  H  HG22   . ILE   B 1 26  ? 23.460  -13.529 22.179 1.00 24.47  ?  51  ILE   B HG22   1 
ATOM   6706  H  HG23   . ILE   B 1 26  ? 22.388  -12.598 21.466 1.00 24.47  ?  51  ILE   B HG23   1 
ATOM   6707  H  HD11   . ILE   B 1 26  ? 23.556  -8.644  21.987 1.00 25.72  ?  51  ILE   B HD11   1 
ATOM   6708  H  HD12   . ILE   B 1 26  ? 24.659  -9.608  22.603 1.00 25.72  ?  51  ILE   B HD12   1 
ATOM   6709  H  HD13   . ILE   B 1 26  ? 23.951  -9.985  21.232 1.00 25.72  ?  51  ILE   B HD13   1 
ATOM   6710  N  N      . GLY   B 1 27  ? 21.036  -11.172 26.038 1.00 18.12  ?  52  GLY   B N      1 
ATOM   6711  C  CA     . GLY   B 1 27  ? 21.043  -10.325 27.213 1.00 18.93  ?  52  GLY   B CA     1 
ATOM   6712  C  C      . GLY   B 1 27  ? 21.094  -8.858  26.851 1.00 20.19  ?  52  GLY   B C      1 
ATOM   6713  O  O      . GLY   B 1 27  ? 21.034  -8.463  25.684 1.00 21.65  ?  52  GLY   B O      1 
ATOM   6714  H  H      . GLY   B 1 27  ? 20.252  -11.322 25.717 1.00 21.74  ?  52  GLY   B H      1 
ATOM   6715  H  HA2    . GLY   B 1 27  ? 20.240  -10.486 27.733 1.00 22.71  ?  52  GLY   B HA2    1 
ATOM   6716  H  HA3    . GLY   B 1 27  ? 21.818  -10.535 27.757 1.00 22.71  ?  52  GLY   B HA3    1 
ATOM   6717  N  N      . SER   B 1 28  ? 21.211  -8.018  27.878 1.00 20.61  ?  53  SER   B N      1 
ATOM   6718  C  CA     . SER   B 1 28  ? 21.167  -6.577  27.654 1.00 20.79  ?  53  SER   B CA     1 
ATOM   6719  C  C      . SER   B 1 28  ? 22.333  -6.103  26.794 1.00 21.84  ?  53  SER   B C      1 
ATOM   6720  O  O      . SER   B 1 28  ? 23.473  -6.553  26.952 1.00 21.63  ?  53  SER   B O      1 
ATOM   6721  C  CB     . SER   B 1 28  ? 21.206  -5.817  28.982 1.00 23.48  ?  53  SER   B CB     1 
ATOM   6722  O  OG     . SER   B 1 28  ? 21.131  -4.424  28.736 1.00 26.26  ?  53  SER   B OG     1 
ATOM   6723  H  H      . SER   B 1 28  ? 21.316  -8.253  28.699 1.00 24.73  ?  53  SER   B H      1 
ATOM   6724  H  HA     . SER   B 1 28  ? 20.336  -6.379  27.193 1.00 24.94  ?  53  SER   B HA     1 
ATOM   6725  H  HB2    . SER   B 1 28  ? 20.452  -6.088  29.528 1.00 28.17  ?  53  SER   B HB2    1 
ATOM   6726  H  HB3    . SER   B 1 28  ? 22.037  -6.017  29.441 1.00 28.17  ?  53  SER   B HB3    1 
ATOM   6727  H  HG     . SER   B 1 28  ? 21.143  -4.003  29.463 1.00 31.51  ?  53  SER   B HG     1 
ATOM   6728  N  N      . VAL   B 1 29  ? 22.051  -5.150  25.904 1.00 22.15  ?  54  VAL   B N      1 
ATOM   6729  C  CA     . VAL   B 1 29  ? 23.099  -4.491  25.129 1.00 23.98  ?  54  VAL   B CA     1 
ATOM   6730  C  C      . VAL   B 1 29  ? 23.408  -3.100  25.674 1.00 25.53  ?  54  VAL   B C      1 
ATOM   6731  O  O      . VAL   B 1 29  ? 24.104  -2.314  25.020 1.00 26.23  ?  54  VAL   B O      1 
ATOM   6732  C  CB     . VAL   B 1 29  ? 22.731  -4.443  23.636 1.00 26.05  ?  54  VAL   B CB     1 
ATOM   6733  C  CG1    . VAL   B 1 29  ? 22.666  -5.872  23.069 1.00 26.66  ?  54  VAL   B CG1    1 
ATOM   6734  C  CG2    . VAL   B 1 29  ? 21.410  -3.713  23.432 1.00 27.54  ?  54  VAL   B CG2    1 
ATOM   6735  H  H      . VAL   B 1 29  ? 21.257  -4.867  25.732 1.00 26.57  ?  54  VAL   B H      1 
ATOM   6736  H  HA     . VAL   B 1 29  ? 23.914  -5.010  25.208 1.00 28.77  ?  54  VAL   B HA     1 
ATOM   6737  H  HB     . VAL   B 1 29  ? 23.414  -3.952  23.152 1.00 31.25  ?  54  VAL   B HB     1 
ATOM   6738  H  HG11   . VAL   B 1 29  ? 22.446  -5.828  22.125 1.00 31.98  ?  54  VAL   B HG11   1 
ATOM   6739  H  HG12   . VAL   B 1 29  ? 23.528  -6.299  23.189 1.00 31.98  ?  54  VAL   B HG12   1 
ATOM   6740  H  HG13   . VAL   B 1 29  ? 21.982  -6.369  23.545 1.00 31.98  ?  54  VAL   B HG13   1 
ATOM   6741  H  HG21   . VAL   B 1 29  ? 21.240  -3.628  22.480 1.00 33.04  ?  54  VAL   B HG21   1 
ATOM   6742  H  HG22   . VAL   B 1 29  ? 20.699  -4.224  23.850 1.00 33.04  ?  54  VAL   B HG22   1 
ATOM   6743  H  HG23   . VAL   B 1 29  ? 21.469  -2.834  23.837 1.00 33.04  ?  54  VAL   B HG23   1 
ATOM   6744  N  N      . GLU   B 1 30  ? 22.906  -2.786  26.864 1.00 24.16  ?  55  GLU   B N      1 
ATOM   6745  C  CA     . GLU   B 1 30  ? 23.220  -1.567  27.590 1.00 25.14  ?  55  GLU   B CA     1 
ATOM   6746  C  C      . GLU   B 1 30  ? 24.185  -1.888  28.721 1.00 25.77  ?  55  GLU   B C      1 
ATOM   6747  O  O      . GLU   B 1 30  ? 24.293  -3.030  29.174 1.00 25.99  ?  55  GLU   B O      1 
ATOM   6748  C  CB     . GLU   B 1 30  ? 21.948  -0.935  28.157 1.00 27.16  ?  55  GLU   B CB     1 
ATOM   6749  C  CG     . GLU   B 1 30  ? 20.939  -0.531  27.100 1.00 30.03  ?  55  GLU   B CG     1 
ATOM   6750  C  CD     . GLU   B 1 30  ? 21.479  0.472   26.093 1.00 35.49  ?  55  GLU   B CD     1 
ATOM   6751  O  OE1    . GLU   B 1 30  ? 22.223  1.398   26.479 1.00 34.60  ?  55  GLU   B OE1    1 
ATOM   6752  O  OE2    . GLU   B 1 30  ? 21.143  0.334   24.902 1.00 40.22  ?  55  GLU   B OE2    1 
ATOM   6753  H  H      . GLU   B 1 30  ? 22.355  -3.290  27.290 1.00 28.98  ?  55  GLU   B H      1 
ATOM   6754  H  HA     . GLU   B 1 30  ? 23.633  -0.923  26.993 1.00 30.16  ?  55  GLU   B HA     1 
ATOM   6755  H  HB2    . GLU   B 1 30  ? 21.519  -1.575  28.746 1.00 32.59  ?  55  GLU   B HB2    1 
ATOM   6756  H  HB3    . GLU   B 1 30  ? 22.192  -0.138  28.653 1.00 32.59  ?  55  GLU   B HB3    1 
ATOM   6757  H  HG2    . GLU   B 1 30  ? 20.664  -1.323  26.611 1.00 36.03  ?  55  GLU   B HG2    1 
ATOM   6758  H  HG3    . GLU   B 1 30  ? 20.172  -0.129  27.538 1.00 36.03  ?  55  GLU   B HG3    1 
ATOM   6759  N  N      . LEU   B 1 31  ? 24.878  -0.854  29.186 1.00 27.54  ?  56  LEU   B N      1 
ATOM   6760  C  CA     . LEU   B 1 31  ? 25.809  -1.022  30.288 1.00 28.45  ?  56  LEU   B CA     1 
ATOM   6761  C  C      . LEU   B 1 31  ? 25.068  -1.409  31.560 1.00 29.23  ?  56  LEU   B C      1 
ATOM   6762  O  O      . LEU   B 1 31  ? 23.940  -0.973  31.818 1.00 33.59  ?  56  LEU   B O      1 
ATOM   6763  C  CB     . LEU   B 1 31  ? 26.616  0.258   30.509 1.00 31.75  ?  56  LEU   B CB     1 
ATOM   6764  C  CG     . LEU   B 1 31  ? 27.726  0.517   29.486 1.00 34.76  ?  56  LEU   B CG     1 
ATOM   6765  C  CD1    . LEU   B 1 31  ? 28.238  1.947   29.629 1.00 36.87  ?  56  LEU   B CD1    1 
ATOM   6766  C  CD2    . LEU   B 1 31  ? 28.860  -0.475  29.632 1.00 34.09  ?  56  LEU   B CD2    1 
ATOM   6767  H  H      . LEU   B 1 31  ? 24.825  -0.051  28.881 1.00 33.04  ?  56  LEU   B H      1 
ATOM   6768  H  HA     . LEU   B 1 31  ? 26.434  -1.733  30.075 1.00 34.13  ?  56  LEU   B HA     1 
ATOM   6769  H  HB2    . LEU   B 1 31  ? 26.007  1.012   30.473 1.00 38.09  ?  56  LEU   B HB2    1 
ATOM   6770  H  HB3    . LEU   B 1 31  ? 27.033  0.209   31.383 1.00 38.09  ?  56  LEU   B HB3    1 
ATOM   6771  H  HG     . LEU   B 1 31  ? 27.362  0.402   28.594 1.00 41.71  ?  56  LEU   B HG     1 
ATOM   6772  H  HD11   . LEU   B 1 31  ? 28.947  2.094   28.983 1.00 44.23  ?  56  LEU   B HD11   1 
ATOM   6773  H  HD12   . LEU   B 1 31  ? 27.507  2.562   29.463 1.00 44.23  ?  56  LEU   B HD12   1 
ATOM   6774  H  HD13   . LEU   B 1 31  ? 28.579  2.072   30.529 1.00 44.23  ?  56  LEU   B HD13   1 
ATOM   6775  H  HD21   . LEU   B 1 31  ? 29.601  -0.192  29.073 1.00 40.90  ?  56  LEU   B HD21   1 
ATOM   6776  H  HD22   . LEU   B 1 31  ? 29.138  -0.502  30.561 1.00 40.90  ?  56  LEU   B HD22   1 
ATOM   6777  H  HD23   . LEU   B 1 31  ? 28.551  -1.351  29.354 1.00 40.90  ?  56  LEU   B HD23   1 
ATOM   6778  N  N      . VAL   B 1 32  ? 25.700  -2.273  32.332 1.00 24.63  ?  57  VAL   B N      1 
ATOM   6779  C  CA     A VAL   B 1 32  ? 25.251  -2.635  33.666 0.41 24.58  ?  57  VAL   B CA     1 
ATOM   6780  C  CA     B VAL   B 1 32  ? 25.247  -2.622  33.670 0.59 24.36  ?  57  VAL   B CA     1 
ATOM   6781  C  C      . VAL   B 1 32  ? 26.424  -2.440  34.611 1.00 24.51  ?  57  VAL   B C      1 
ATOM   6782  O  O      . VAL   B 1 32  ? 27.575  -2.693  34.237 1.00 23.63  ?  57  VAL   B O      1 
ATOM   6783  C  CB     A VAL   B 1 32  ? 24.738  -4.085  33.712 0.41 25.64  ?  57  VAL   B CB     1 
ATOM   6784  C  CB     B VAL   B 1 32  ? 24.686  -4.053  33.760 0.59 25.46  ?  57  VAL   B CB     1 
ATOM   6785  C  CG1    A VAL   B 1 32  ? 24.664  -4.591  35.143 0.41 26.57  ?  57  VAL   B CG1    1 
ATOM   6786  C  CG1    B VAL   B 1 32  ? 23.733  -4.319  32.604 0.59 26.30  ?  57  VAL   B CG1    1 
ATOM   6787  C  CG2    A VAL   B 1 32  ? 23.378  -4.183  33.031 0.41 25.58  ?  57  VAL   B CG2    1 
ATOM   6788  C  CG2    B VAL   B 1 32  ? 25.796  -5.071  33.814 0.59 25.02  ?  57  VAL   B CG2    1 
ATOM   6789  H  H      . VAL   B 1 32  ? 26.417  -2.684  32.095 1.00 29.55  ?  57  VAL   B H      1 
ATOM   6790  H  HA     . VAL   B 1 32  ? 24.525  -2.055  33.945 1.00 29.23  ?  57  VAL   B HA     1 
ATOM   6791  H  HB     A VAL   B 1 32  ? 25.362  -4.654  33.234 0.41 30.76  ?  57  VAL   B HB     1 
ATOM   6792  H  HB     B VAL   B 1 32  ? 24.183  -4.143  34.584 0.59 30.54  ?  57  VAL   B HB     1 
ATOM   6793  H  HG11   A VAL   B 1 32  ? 24.087  -5.370  35.173 0.41 31.87  ?  57  VAL   B HG11   1 
ATOM   6794  H  HG11   B VAL   B 1 32  ? 23.301  -5.177  32.743 0.59 31.55  ?  57  VAL   B HG11   1 
ATOM   6795  H  HG12   A VAL   B 1 32  ? 25.557  -4.828  35.440 0.41 31.87  ?  57  VAL   B HG12   1 
ATOM   6796  H  HG12   B VAL   B 1 32  ? 23.067  -3.615  32.575 0.59 31.55  ?  57  VAL   B HG12   1 
ATOM   6797  H  HG13   A VAL   B 1 32  ? 24.303  -3.889  35.707 0.41 31.87  ?  57  VAL   B HG13   1 
ATOM   6798  H  HG13   B VAL   B 1 32  ? 24.237  -4.333  31.776 0.59 31.55  ?  57  VAL   B HG13   1 
ATOM   6799  H  HG21   A VAL   B 1 32  ? 23.077  -5.104  33.057 0.41 30.69  ?  57  VAL   B HG21   1 
ATOM   6800  H  HG21   B VAL   B 1 32  ? 25.440  -5.939  33.570 0.59 30.02  ?  57  VAL   B HG21   1 
ATOM   6801  H  HG22   A VAL   B 1 32  ? 22.748  -3.615  33.501 0.41 30.69  ?  57  VAL   B HG22   1 
ATOM   6802  H  HG22   B VAL   B 1 32  ? 26.493  -4.811  33.191 0.59 30.02  ?  57  VAL   B HG22   1 
ATOM   6803  H  HG23   A VAL   B 1 32  ? 23.465  -3.890  32.110 0.41 30.69  ?  57  VAL   B HG23   1 
ATOM   6804  H  HG23   B VAL   B 1 32  ? 26.152  -5.101  34.716 0.59 30.02  ?  57  VAL   B HG23   1 
ATOM   6805  N  N      . THR   B 1 33  ? 26.135  -1.991  35.827 1.00 24.87  ?  58  THR   B N      1 
ATOM   6806  C  CA     . THR   B 1 33  ? 27.133  -1.866  36.879 1.00 25.05  ?  58  THR   B CA     1 
ATOM   6807  C  C      . THR   B 1 33  ? 26.667  -2.716  38.052 1.00 25.93  ?  58  THR   B C      1 
ATOM   6808  O  O      . THR   B 1 33  ? 25.615  -2.444  38.642 1.00 27.42  ?  58  THR   B O      1 
ATOM   6809  C  CB     . THR   B 1 33  ? 27.319  -0.414  37.319 1.00 27.95  ?  58  THR   B CB     1 
ATOM   6810  O  OG1    . THR   B 1 33  ? 27.775  0.369   36.211 1.00 29.28  ?  58  THR   B OG1    1 
ATOM   6811  C  CG2    . THR   B 1 33  ? 28.342  -0.321  38.451 1.00 29.42  ?  58  THR   B CG2    1 
ATOM   6812  H  H      . THR   B 1 33  ? 25.348  -1.747  36.071 1.00 29.84  ?  58  THR   B H      1 
ATOM   6813  H  HA     . THR   B 1 33  ? 27.990  -2.188  36.558 1.00 30.06  ?  58  THR   B HA     1 
ATOM   6814  H  HB     . THR   B 1 33  ? 26.472  -0.065  37.640 1.00 33.53  ?  58  THR   B HB     1 
ATOM   6815  H  HG1    . THR   B 1 33  ? 28.515  0.078   35.938 1.00 35.13  ?  58  THR   B HG1    1 
ATOM   6816  H  HG21   . THR   B 1 33  ? 28.607  0.602   38.584 1.00 35.29  ?  58  THR   B HG21   1 
ATOM   6817  H  HG22   . THR   B 1 33  ? 27.959  -0.661  39.274 1.00 35.29  ?  58  THR   B HG22   1 
ATOM   6818  H  HG23   . THR   B 1 33  ? 29.129  -0.845  38.231 1.00 35.29  ?  58  THR   B HG23   1 
ATOM   6819  N  N      . GLN   B 1 34  ? 27.443  -3.736  38.388 1.00 25.64  ?  59  GLN   B N      1 
ATOM   6820  C  CA     . GLN   B 1 34  ? 27.057  -4.633  39.460 1.00 25.44  ?  59  GLN   B CA     1 
ATOM   6821  C  C      . GLN   B 1 34  ? 28.298  -5.363  39.932 1.00 25.30  ?  59  GLN   B C      1 
ATOM   6822  O  O      . GLN   B 1 34  ? 29.334  -5.360  39.262 1.00 25.12  ?  59  GLN   B O      1 
ATOM   6823  C  CB     . GLN   B 1 34  ? 25.987  -5.628  39.001 1.00 25.73  ?  59  GLN   B CB     1 
ATOM   6824  C  CG     . GLN   B 1 34  ? 26.460  -6.561  37.899 1.00 26.32  ?  59  GLN   B CG     1 
ATOM   6825  C  CD     . GLN   B 1 34  ? 25.329  -7.375  37.286 1.00 28.35  ?  59  GLN   B CD     1 
ATOM   6826  O  OE1    . GLN   B 1 34  ? 24.187  -6.915  37.188 1.00 30.56  ?  59  GLN   B OE1    1 
ATOM   6827  N  NE2    . GLN   B 1 34  ? 25.642  -8.594  36.881 1.00 28.23  ?  59  GLN   B NE2    1 
ATOM   6828  H  H      . GLN   B 1 34  ? 28.192  -3.928  38.011 1.00 30.76  ?  59  GLN   B H      1 
ATOM   6829  H  HA     . GLN   B 1 34  ? 26.696  -4.123  40.201 1.00 30.52  ?  59  GLN   B HA     1 
ATOM   6830  H  HB2    . GLN   B 1 34  ? 25.720  -6.172  39.758 1.00 30.87  ?  59  GLN   B HB2    1 
ATOM   6831  H  HB3    . GLN   B 1 34  ? 25.224  -5.133  38.663 1.00 30.87  ?  59  GLN   B HB3    1 
ATOM   6832  H  HG2    . GLN   B 1 34  ? 26.867  -6.034  37.193 1.00 31.58  ?  59  GLN   B HG2    1 
ATOM   6833  H  HG3    . GLN   B 1 34  ? 27.109  -7.180  38.267 1.00 31.58  ?  59  GLN   B HG3    1 
ATOM   6834  H  HE21   . GLN   B 1 34  ? 26.446  -8.884  36.972 1.00 33.87  ?  59  GLN   B HE21   1 
ATOM   6835  H  HE22   . GLN   B 1 34  ? 25.040  -9.097  36.528 1.00 33.87  ?  59  GLN   B HE22   1 
ATOM   6836  N  N      . GLN   B 1 35  ? 28.184  -5.963  41.109 1.00 26.06  ?  60  GLN   B N      1 
ATOM   6837  C  CA     . GLN   B 1 35  ? 29.263  -6.768  41.657 1.00 27.60  ?  60  GLN   B CA     1 
ATOM   6838  C  C      . GLN   B 1 35  ? 29.298  -8.128  40.976 1.00 27.40  ?  60  GLN   B C      1 
ATOM   6839  O  O      . GLN   B 1 35  ? 28.262  -8.783  40.826 1.00 27.24  ?  60  GLN   B O      1 
ATOM   6840  C  CB     . GLN   B 1 35  ? 29.079  -6.913  43.160 1.00 30.52  ?  60  GLN   B CB     1 
ATOM   6841  C  CG     . GLN   B 1 35  ? 29.047  -5.578  43.865 1.00 38.15  ?  60  GLN   B CG     1 
ATOM   6842  C  CD     . GLN   B 1 35  ? 29.706  -5.651  45.205 1.00 44.20  ?  60  GLN   B CD     1 
ATOM   6843  O  OE1    . GLN   B 1 35  ? 29.041  -5.713  46.235 1.00 46.54  ?  60  GLN   B OE1    1 
ATOM   6844  N  NE2    . GLN   B 1 35  ? 31.030  -5.673  45.202 1.00 46.30  ?  60  GLN   B NE2    1 
ATOM   6845  H  H      . GLN   B 1 35  ? 27.488  -5.919  41.612 1.00 31.27  ?  60  GLN   B H      1 
ATOM   6846  H  HA     . GLN   B 1 35  ? 30.117  -6.338  41.496 1.00 33.11  ?  60  GLN   B HA     1 
ATOM   6847  H  HB2    . GLN   B 1 35  ? 28.240  -7.367  43.335 1.00 36.62  ?  60  GLN   B HB2    1 
ATOM   6848  H  HB3    . GLN   B 1 35  ? 29.817  -7.429  43.522 1.00 36.62  ?  60  GLN   B HB3    1 
ATOM   6849  H  HG2    . GLN   B 1 35  ? 29.518  -4.921  43.329 1.00 45.77  ?  60  GLN   B HG2    1 
ATOM   6850  H  HG3    . GLN   B 1 35  ? 28.125  -5.304  43.992 1.00 45.77  ?  60  GLN   B HG3    1 
ATOM   6851  H  HE21   . GLN   B 1 35  ? 31.459  -5.645  44.457 1.00 55.56  ?  60  GLN   B HE21   1 
ATOM   6852  H  HE22   . GLN   B 1 35  ? 31.461  -5.714  45.945 1.00 55.56  ?  60  GLN   B HE22   1 
ATOM   6853  N  N      . MET   B 1 36  ? 30.505  -8.537  40.573 1.00 25.19  ?  61  MET   B N      1 
ATOM   6854  C  CA     . MET   B 1 36  ? 30.760  -9.783  39.866 1.00 24.56  ?  61  MET   B CA     1 
ATOM   6855  C  C      . MET   B 1 36  ? 32.065  -10.375 40.385 1.00 23.37  ?  61  MET   B C      1 
ATOM   6856  O  O      . MET   B 1 36  ? 32.922  -9.658  40.911 1.00 23.72  ?  61  MET   B O      1 
ATOM   6857  C  CB     . MET   B 1 36  ? 30.939  -9.596  38.347 1.00 24.19  ?  61  MET   B CB     1 
ATOM   6858  C  CG     . MET   B 1 36  ? 29.811  -8.969  37.581 1.00 23.73  ?  61  MET   B CG     1 
ATOM   6859  S  SD     . MET   B 1 36  ? 28.490  -10.122 37.410 1.00 28.42  ?  61  MET   B SD     1 
ATOM   6860  C  CE     . MET   B 1 36  ? 29.167  -11.111 36.062 1.00 25.01  ?  61  MET   B CE     1 
ATOM   6861  H  H      . MET   B 1 36  ? 31.224  -8.085  40.707 1.00 30.23  ?  61  MET   B H      1 
ATOM   6862  H  HA     . MET   B 1 36  ? 29.999  -10.363 40.028 1.00 29.47  ?  61  MET   B HA     1 
ATOM   6863  H  HB2    . MET   B 1 36  ? 31.717  -9.034  38.208 1.00 29.02  ?  61  MET   B HB2    1 
ATOM   6864  H  HB3    . MET   B 1 36  ? 31.088  -10.472 37.957 1.00 29.02  ?  61  MET   B HB3    1 
ATOM   6865  H  HG2    . MET   B 1 36  ? 29.486  -8.190  38.058 1.00 28.47  ?  61  MET   B HG2    1 
ATOM   6866  H  HG3    . MET   B 1 36  ? 30.118  -8.713  36.697 1.00 28.47  ?  61  MET   B HG3    1 
ATOM   6867  H  HE1    . MET   B 1 36  ? 28.436  -11.483 35.545 1.00 30.00  ?  61  MET   B HE1    1 
ATOM   6868  H  HE2    . MET   B 1 36  ? 29.715  -10.543 35.498 1.00 30.00  ?  61  MET   B HE2    1 
ATOM   6869  H  HE3    . MET   B 1 36  ? 29.706  -11.826 36.434 1.00 30.00  ?  61  MET   B HE3    1 
ATOM   6870  N  N      . TRP   B 1 37  ? 32.243  -11.680 40.174 1.00 22.78  ?  62  TRP   B N      1 
ATOM   6871  C  CA     . TRP   B 1 37  ? 33.561  -12.291 40.308 1.00 22.99  ?  62  TRP   B CA     1 
ATOM   6872  C  C      . TRP   B 1 37  ? 34.325  -12.102 39.004 1.00 22.91  ?  62  TRP   B C      1 
ATOM   6873  O  O      . TRP   B 1 37  ? 33.777  -12.324 37.919 1.00 22.90  ?  62  TRP   B O      1 
ATOM   6874  C  CB     . TRP   B 1 37  ? 33.436  -13.780 40.637 1.00 23.19  ?  62  TRP   B CB     1 
ATOM   6875  C  CG     . TRP   B 1 37  ? 32.870  -14.061 41.987 1.00 23.70  ?  62  TRP   B CG     1 
ATOM   6876  C  CD1    . TRP   B 1 37  ? 31.568  -14.363 42.296 1.00 23.03  ?  62  TRP   B CD1    1 
ATOM   6877  C  CD2    . TRP   B 1 37  ? 33.586  -14.071 43.224 1.00 24.80  ?  62  TRP   B CD2    1 
ATOM   6878  N  NE1    . TRP   B 1 37  ? 31.437  -14.556 43.649 1.00 24.01  ?  62  TRP   B NE1    1 
ATOM   6879  C  CE2    . TRP   B 1 37  ? 32.662  -14.389 44.241 1.00 25.67  ?  62  TRP   B CE2    1 
ATOM   6880  C  CE3    . TRP   B 1 37  ? 34.924  -13.855 43.570 1.00 25.96  ?  62  TRP   B CE3    1 
ATOM   6881  C  CZ2    . TRP   B 1 37  ? 33.030  -14.483 45.577 1.00 27.04  ?  62  TRP   B CZ2    1 
ATOM   6882  C  CZ3    . TRP   B 1 37  ? 35.285  -13.951 44.894 1.00 26.48  ?  62  TRP   B CZ3    1 
ATOM   6883  C  CH2    . TRP   B 1 37  ? 34.342  -14.265 45.882 1.00 27.03  ?  62  TRP   B CH2    1 
ATOM   6884  H  H      . TRP   B 1 37  ? 31.618  -12.228 39.954 1.00 27.33  ?  62  TRP   B H      1 
ATOM   6885  H  HA     . TRP   B 1 37  ? 34.050  -11.870 41.032 1.00 27.59  ?  62  TRP   B HA     1 
ATOM   6886  H  HB2    . TRP   B 1 37  ? 32.853  -14.194 39.982 1.00 27.82  ?  62  TRP   B HB2    1 
ATOM   6887  H  HB3    . TRP   B 1 37  ? 34.318  -14.181 40.598 1.00 27.82  ?  62  TRP   B HB3    1 
ATOM   6888  H  HD1    . TRP   B 1 37  ? 30.876  -14.429 41.678 1.00 27.63  ?  62  TRP   B HD1    1 
ATOM   6889  H  HE1    . TRP   B 1 37  ? 30.706  -14.750 44.059 1.00 28.81  ?  62  TRP   B HE1    1 
ATOM   6890  H  HE3    . TRP   B 1 37  ? 35.556  -13.651 42.919 1.00 31.15  ?  62  TRP   B HE3    1 
ATOM   6891  H  HZ2    . TRP   B 1 37  ? 32.407  -14.686 46.237 1.00 32.44  ?  62  TRP   B HZ2    1 
ATOM   6892  H  HZ3    . TRP   B 1 37  ? 36.170  -13.805 45.139 1.00 31.77  ?  62  TRP   B HZ3    1 
ATOM   6893  H  HH2    . TRP   B 1 37  ? 34.617  -14.327 46.768 1.00 32.43  ?  62  TRP   B HH2    1 
ATOM   6894  N  N      . VAL   B 1 38  ? 35.588  -11.677 39.103 1.00 24.42  ?  63  VAL   B N      1 
ATOM   6895  C  CA     . VAL   B 1 38  ? 36.452  -11.467 37.948 1.00 25.09  ?  63  VAL   B CA     1 
ATOM   6896  C  C      . VAL   B 1 38  ? 37.840  -12.017 38.271 1.00 26.35  ?  63  VAL   B C      1 
ATOM   6897  O  O      . VAL   B 1 38  ? 38.157  -12.335 39.418 1.00 27.80  ?  63  VAL   B O      1 
ATOM   6898  C  CB     . VAL   B 1 38  ? 36.551  -9.978  37.547 1.00 25.74  ?  63  VAL   B CB     1 
ATOM   6899  C  CG1    . VAL   B 1 38  ? 35.179  -9.376  37.269 1.00 26.82  ?  63  VAL   B CG1    1 
ATOM   6900  C  CG2    . VAL   B 1 38  ? 37.263  -9.162  38.626 1.00 27.12  ?  63  VAL   B CG2    1 
ATOM   6901  H  H      . VAL   B 1 38  ? 35.973  -11.501 39.852 1.00 29.30  ?  63  VAL   B H      1 
ATOM   6902  H  HA     . VAL   B 1 38  ? 36.093  -11.962 37.195 1.00 30.10  ?  63  VAL   B HA     1 
ATOM   6903  H  HB     . VAL   B 1 38  ? 37.071  -9.934  36.730 1.00 30.88  ?  63  VAL   B HB     1 
ATOM   6904  H  HG11   . VAL   B 1 38  ? 35.287  -8.586  36.716 1.00 32.18  ?  63  VAL   B HG11   1 
ATOM   6905  H  HG12   . VAL   B 1 38  ? 34.634  -10.031 36.806 1.00 32.18  ?  63  VAL   B HG12   1 
ATOM   6906  H  HG13   . VAL   B 1 38  ? 34.763  -9.135  38.111 1.00 32.18  ?  63  VAL   B HG13   1 
ATOM   6907  H  HG21   . VAL   B 1 38  ? 37.115  -8.219  38.457 1.00 32.54  ?  63  VAL   B HG21   1 
ATOM   6908  H  HG22   . VAL   B 1 38  ? 36.902  -9.403  39.493 1.00 32.54  ?  63  VAL   B HG22   1 
ATOM   6909  H  HG23   . VAL   B 1 38  ? 38.212  -9.359  38.596 1.00 32.54  ?  63  VAL   B HG23   1 
ATOM   6910  N  N      . TYR   B 1 39  ? 38.676  -12.133 37.238 1.00 26.09  ?  64  TYR   B N      1 
ATOM   6911  C  CA     . TYR   B 1 39  ? 40.100  -12.410 37.414 1.00 27.22  ?  64  TYR   B CA     1 
ATOM   6912  C  C      . TYR   B 1 39  ? 40.878  -11.189 36.933 1.00 28.89  ?  64  TYR   B C      1 
ATOM   6913  O  O      . TYR   B 1 39  ? 40.961  -10.939 35.725 1.00 29.34  ?  64  TYR   B O      1 
ATOM   6914  C  CB     . TYR   B 1 39  ? 40.550  -13.655 36.658 1.00 28.71  ?  64  TYR   B CB     1 
ATOM   6915  C  CG     . TYR   B 1 39  ? 41.961  -14.077 37.029 1.00 29.67  ?  64  TYR   B CG     1 
ATOM   6916  C  CD1    . TYR   B 1 39  ? 43.071  -13.435 36.492 1.00 31.84  ?  64  TYR   B CD1    1 
ATOM   6917  C  CD2    . TYR   B 1 39  ? 42.180  -15.104 37.939 1.00 30.66  ?  64  TYR   B CD2    1 
ATOM   6918  C  CE1    . TYR   B 1 39  ? 44.346  -13.814 36.844 1.00 32.50  ?  64  TYR   B CE1    1 
ATOM   6919  C  CE2    . TYR   B 1 39  ? 43.461  -15.496 38.283 1.00 32.19  ?  64  TYR   B CE2    1 
ATOM   6920  C  CZ     . TYR   B 1 39  ? 44.537  -14.842 37.742 1.00 32.95  ?  64  TYR   B CZ     1 
ATOM   6921  O  OH     . TYR   B 1 39  ? 45.814  -15.225 38.085 1.00 34.04  ?  64  TYR   B OH     1 
ATOM   6922  H  H      . TYR   B 1 39  ? 38.437  -12.054 36.415 1.00 31.30  ?  64  TYR   B H      1 
ATOM   6923  H  HA     . TYR   B 1 39  ? 40.268  -12.560 38.358 1.00 32.66  ?  64  TYR   B HA     1 
ATOM   6924  H  HB2    . TYR   B 1 39  ? 39.950  -14.388 36.868 1.00 34.45  ?  64  TYR   B HB2    1 
ATOM   6925  H  HB3    . TYR   B 1 39  ? 40.530  -13.472 35.706 1.00 34.45  ?  64  TYR   B HB3    1 
ATOM   6926  H  HD1    . TYR   B 1 39  ? 42.951  -12.740 35.887 1.00 38.20  ?  64  TYR   B HD1    1 
ATOM   6927  H  HD2    . TYR   B 1 39  ? 41.451  -15.535 38.324 1.00 36.79  ?  64  TYR   B HD2    1 
ATOM   6928  H  HE1    . TYR   B 1 39  ? 45.079  -13.376 36.476 1.00 38.99  ?  64  TYR   B HE1    1 
ATOM   6929  H  HE2    . TYR   B 1 39  ? 43.591  -16.200 38.878 1.00 38.62  ?  64  TYR   B HE2    1 
ATOM   6930  H  HH     . TYR   B 1 39  ? 45.786  -15.861 38.633 1.00 40.84  ?  64  TYR   B HH     1 
ATOM   6931  N  N      . ASP   B 1 40  ? 41.445  -10.432 37.874 1.00 29.71  ?  65  ASP   B N      1 
ATOM   6932  C  CA     . ASP   B 1 40  ? 42.232  -9.248  37.549 1.00 30.36  ?  65  ASP   B CA     1 
ATOM   6933  C  C      . ASP   B 1 40  ? 43.716  -9.583  37.404 1.00 31.75  ?  65  ASP   B C      1 
ATOM   6934  O  O      . ASP   B 1 40  ? 44.246  -10.474 38.077 1.00 31.95  ?  65  ASP   B O      1 
ATOM   6935  C  CB     . ASP   B 1 40  ? 42.046  -8.163  38.617 1.00 30.77  ?  65  ASP   B CB     1 
ATOM   6936  C  CG     . ASP   B 1 40  ? 40.743  -7.393  38.456 1.00 31.26  ?  65  ASP   B CG     1 
ATOM   6937  O  OD1    . ASP   B 1 40  ? 40.488  -6.904  37.338 1.00 31.48  ?  65  ASP   B OD1    1 
ATOM   6938  O  OD2    . ASP   B 1 40  ? 39.990  -7.264  39.448 1.00 31.79  ?  65  ASP   B OD2    1 
ATOM   6939  H  H      . ASP   B 1 40  ? 41.387  -10.587 38.717 1.00 35.65  ?  65  ASP   B H      1 
ATOM   6940  H  HA     . ASP   B 1 40  ? 41.926  -8.898  36.697 1.00 36.42  ?  65  ASP   B HA     1 
ATOM   6941  H  HB2    . ASP   B 1 40  ? 42.041  -8.580  39.493 1.00 36.91  ?  65  ASP   B HB2    1 
ATOM   6942  H  HB3    . ASP   B 1 40  ? 42.778  -7.530  38.556 1.00 36.91  ?  65  ASP   B HB3    1 
ATOM   6943  N  N      . GLU   B 1 41  ? 44.380  -8.842  36.505 1.00 32.06  ?  66  GLU   B N      1 
ATOM   6944  C  CA     . GLU   B 1 41  ? 45.782  -9.047  36.168 1.00 35.39  ?  66  GLU   B CA     1 
ATOM   6945  C  C      . GLU   B 1 41  ? 46.741  -8.947  37.343 1.00 35.71  ?  66  GLU   B C      1 
ATOM   6946  O  O      . GLU   B 1 41  ? 47.884  -9.416  37.226 1.00 35.10  ?  66  GLU   B O      1 
ATOM   6947  C  CB     . GLU   B 1 41  ? 46.243  -7.980  35.173 1.00 40.01  ?  66  GLU   B CB     1 
ATOM   6948  C  CG     . GLU   B 1 41  ? 46.012  -8.257  33.743 1.00 44.06  ?  66  GLU   B CG     1 
ATOM   6949  C  CD     . GLU   B 1 41  ? 46.645  -7.190  32.882 1.00 44.49  ?  66  GLU   B CD     1 
ATOM   6950  O  OE1    . GLU   B 1 41  ? 46.703  -6.020  33.325 1.00 44.64  ?  66  GLU   B OE1    1 
ATOM   6951  O  OE2    . GLU   B 1 41  ? 47.088  -7.528  31.769 1.00 45.13  ?  66  GLU   B OE2    1 
ATOM   6952  H  H      . GLU   B 1 41  ? 44.024  -8.194  36.065 1.00 38.46  ?  66  GLU   B H      1 
ATOM   6953  H  HA     . GLU   B 1 41  ? 45.830  -9.940  35.794 1.00 42.46  ?  66  GLU   B HA     1 
ATOM   6954  H  HB2    . GLU   B 1 41  ? 45.776  -7.156  35.380 1.00 48.00  ?  66  GLU   B HB2    1 
ATOM   6955  H  HB3    . GLU   B 1 41  ? 47.198  -7.858  35.286 1.00 48.00  ?  66  GLU   B HB3    1 
ATOM   6956  H  HG2    . GLU   B 1 41  ? 46.404  -9.113  33.512 1.00 52.86  ?  66  GLU   B HG2    1 
ATOM   6957  H  HG3    . GLU   B 1 41  ? 45.058  -8.270  33.566 1.00 52.86  ?  66  GLU   B HG3    1 
ATOM   6958  N  N      . ASP   B 1 42  ? 46.343  -8.276  38.424 1.00 36.68  ?  67  ASP   B N      1 
ATOM   6959  C  CA     . ASP   B 1 42  ? 47.240  -8.042  39.545 1.00 37.98  ?  67  ASP   B CA     1 
ATOM   6960  C  C      . ASP   B 1 42  ? 46.893  -8.824  40.803 1.00 39.60  ?  67  ASP   B C      1 
ATOM   6961  O  O      . ASP   B 1 42  ? 47.811  -9.218  41.524 1.00 41.73  ?  67  ASP   B O      1 
ATOM   6962  C  CB     . ASP   B 1 42  ? 47.317  -6.543  39.894 1.00 39.25  ?  67  ASP   B CB     1 
ATOM   6963  C  CG     . ASP   B 1 42  ? 45.963  -5.898  40.160 1.00 41.49  ?  67  ASP   B CG     1 
ATOM   6964  O  OD1    . ASP   B 1 42  ? 44.899  -6.545  40.038 1.00 40.88  ?  67  ASP   B OD1    1 
ATOM   6965  O  OD2    . ASP   B 1 42  ? 45.981  -4.693  40.487 1.00 44.62  ?  67  ASP   B OD2    1 
ATOM   6966  H  H      . ASP   B 1 42  ? 45.555  -7.947  38.528 1.00 44.01  ?  67  ASP   B H      1 
ATOM   6967  H  HA     . ASP   B 1 42  ? 48.128  -8.319  39.268 1.00 45.57  ?  67  ASP   B HA     1 
ATOM   6968  H  HB2    . ASP   B 1 42  ? 47.856  -6.438  40.694 1.00 47.09  ?  67  ASP   B HB2    1 
ATOM   6969  H  HB3    . ASP   B 1 42  ? 47.728  -6.071  39.153 1.00 47.09  ?  67  ASP   B HB3    1 
ATOM   6970  N  N      . VAL   B 1 43  ? 45.621  -9.096  41.085 1.00 38.27  ?  68  VAL   B N      1 
ATOM   6971  C  CA     A VAL   B 1 43  ? 45.227  -9.769  42.318 0.05 38.41  ?  68  VAL   B CA     1 
ATOM   6972  C  CA     B VAL   B 1 43  ? 45.256  -9.788  42.316 0.95 38.72  ?  68  VAL   B CA     1 
ATOM   6973  C  C      . VAL   B 1 43  ? 44.541  -11.107 42.078 1.00 37.80  ?  68  VAL   B C      1 
ATOM   6974  O  O      . VAL   B 1 43  ? 44.316  -11.850 43.046 1.00 40.94  ?  68  VAL   B O      1 
ATOM   6975  C  CB     A VAL   B 1 43  ? 44.318  -8.864  43.180 0.05 38.99  ?  68  VAL   B CB     1 
ATOM   6976  C  CB     B VAL   B 1 43  ? 44.404  -8.886  43.234 0.95 39.16  ?  68  VAL   B CB     1 
ATOM   6977  C  CG1    A VAL   B 1 43  ? 44.166  -9.429  44.586 0.05 39.17  ?  68  VAL   B CG1    1 
ATOM   6978  C  CG1    B VAL   B 1 43  ? 45.206  -7.662  43.628 0.95 39.49  ?  68  VAL   B CG1    1 
ATOM   6979  C  CG2    A VAL   B 1 43  ? 44.867  -7.444  43.218 0.05 39.22  ?  68  VAL   B CG2    1 
ATOM   6980  C  CG2    B VAL   B 1 43  ? 43.112  -8.487  42.543 0.95 38.40  ?  68  VAL   B CG2    1 
ATOM   6981  H  H      A VAL   B 1 43  ? 44.960  -8.897  40.571 0.05 45.91  ?  68  VAL   B H      1 
ATOM   6982  H  H      B VAL   B 1 43  ? 44.955  -8.889  40.581 0.95 45.91  ?  68  VAL   B H      1 
ATOM   6983  H  HA     A VAL   B 1 43  ? 46.031  -9.955  42.828 0.05 46.08  ?  68  VAL   B HA     1 
ATOM   6984  H  HA     B VAL   B 1 43  ? 46.076  -10.001 42.790 0.95 46.46  ?  68  VAL   B HA     1 
ATOM   6985  H  HB     A VAL   B 1 43  ? 43.434  -8.834  42.780 0.05 46.78  ?  68  VAL   B HB     1 
ATOM   6986  H  HB     B VAL   B 1 43  ? 44.167  -9.374  44.038 0.95 46.98  ?  68  VAL   B HB     1 
ATOM   6987  H  HG11   A VAL   B 1 43  ? 43.813  -8.738  45.167 0.05 47.00  ?  68  VAL   B HG11   1 
ATOM   6988  H  HG11   B VAL   B 1 43  ? 44.683  -7.127  44.245 0.95 47.39  ?  68  VAL   B HG11   1 
ATOM   6989  H  HG12   A VAL   B 1 43  ? 43.556  -10.182 44.559 0.05 47.00  ?  68  VAL   B HG12   1 
ATOM   6990  H  HG12   B VAL   B 1 43  ? 46.029  -7.947  44.053 0.95 47.39  ?  68  VAL   B HG12   1 
ATOM   6991  H  HG13   A VAL   B 1 43  ? 45.035  -9.718  44.905 0.05 47.00  ?  68  VAL   B HG13   1 
ATOM   6992  H  HG13   B VAL   B 1 43  ? 45.406  -7.146  42.831 0.95 47.39  ?  68  VAL   B HG13   1 
ATOM   6993  H  HG21   A VAL   B 1 43  ? 44.448  -6.962  43.948 0.05 47.06  ?  68  VAL   B HG21   1 
ATOM   6994  H  HG21   B VAL   B 1 43  ? 42.626  -7.870  43.113 0.95 46.07  ?  68  VAL   B HG21   1 
ATOM   6995  H  HG22   A VAL   B 1 43  ? 45.827  -7.480  43.355 0.05 47.06  ?  68  VAL   B HG22   1 
ATOM   6996  H  HG22   B VAL   B 1 43  ? 43.324  -8.059  41.698 0.95 46.07  ?  68  VAL   B HG22   1 
ATOM   6997  H  HG23   A VAL   B 1 43  ? 44.669  -7.006  42.376 0.05 47.06  ?  68  VAL   B HG23   1 
ATOM   6998  H  HG23   B VAL   B 1 43  ? 42.579  -9.282  42.387 0.95 46.07  ?  68  VAL   B HG23   1 
ATOM   6999  N  N      . GLY   B 1 44  ? 44.195  -11.442 40.841 1.00 33.75  ?  69  GLY   B N      1 
ATOM   7000  C  CA     . GLY   B 1 44  ? 43.526  -12.699 40.575 1.00 32.58  ?  69  GLY   B CA     1 
ATOM   7001  C  C      . GLY   B 1 44  ? 42.034  -12.675 40.833 1.00 30.66  ?  69  GLY   B C      1 
ATOM   7002  O  O      . GLY   B 1 44  ? 41.358  -11.676 40.562 1.00 29.29  ?  69  GLY   B O      1 
ATOM   7003  H  H      . GLY   B 1 44  ? 44.336  -10.957 40.145 1.00 40.49  ?  69  GLY   B H      1 
ATOM   7004  H  HA2    . GLY   B 1 44  ? 43.665  -12.938 39.645 1.00 39.09  ?  69  GLY   B HA2    1 
ATOM   7005  H  HA3    . GLY   B 1 44  ? 43.915  -13.387 41.138 1.00 39.09  ?  69  GLY   B HA3    1 
ATOM   7006  N  N      . ILE   B 1 45  ? 41.504  -13.789 41.338 1.00 31.19  ?  70  ILE   B N      1 
ATOM   7007  C  CA     . ILE   B 1 45  ? 40.066  -13.920 41.536 1.00 30.96  ?  70  ILE   B CA     1 
ATOM   7008  C  C      . ILE   B 1 45  ? 39.628  -12.987 42.654 1.00 30.89  ?  70  ILE   B C      1 
ATOM   7009  O  O      . ILE   B 1 45  ? 40.195  -13.012 43.753 1.00 32.36  ?  70  ILE   B O      1 
ATOM   7010  C  CB     . ILE   B 1 45  ? 39.707  -15.375 41.875 1.00 31.96  ?  70  ILE   B CB     1 
ATOM   7011  C  CG1    . ILE   B 1 45  ? 40.052  -16.314 40.718 1.00 32.79  ?  70  ILE   B CG1    1 
ATOM   7012  C  CG2    . ILE   B 1 45  ? 38.231  -15.492 42.216 1.00 32.11  ?  70  ILE   B CG2    1 
ATOM   7013  C  CD1    . ILE   B 1 45  ? 39.112  -16.194 39.528 1.00 33.41  ?  70  ILE   B CD1    1 
ATOM   7014  H  H      . ILE   B 1 45  ? 41.956  -14.481 41.574 1.00 37.43  ?  70  ILE   B H      1 
ATOM   7015  H  HA     . ILE   B 1 45  ? 39.608  -13.668 40.719 1.00 37.14  ?  70  ILE   B HA     1 
ATOM   7016  H  HB     . ILE   B 1 45  ? 40.235  -15.636 42.646 1.00 38.35  ?  70  ILE   B HB     1 
ATOM   7017  H  HG12   . ILE   B 1 45  ? 40.948  -16.110 40.408 1.00 39.34  ?  70  ILE   B HG12   1 
ATOM   7018  H  HG13   . ILE   B 1 45  ? 40.011  -17.229 41.036 1.00 39.34  ?  70  ILE   B HG13   1 
ATOM   7019  H  HG21   . ILE   B 1 45  ? 37.964  -16.423 42.153 1.00 38.53  ?  70  ILE   B HG21   1 
ATOM   7020  H  HG22   . ILE   B 1 45  ? 38.089  -15.168 43.119 1.00 38.53  ?  70  ILE   B HG22   1 
ATOM   7021  H  HG23   . ILE   B 1 45  ? 37.718  -14.958 41.589 1.00 38.53  ?  70  ILE   B HG23   1 
ATOM   7022  H  HD11   . ILE   B 1 45  ? 39.496  -16.667 38.773 1.00 40.09  ?  70  ILE   B HD11   1 
ATOM   7023  H  HD12   . ILE   B 1 45  ? 38.255  -16.585 39.762 1.00 40.09  ?  70  ILE   B HD12   1 
ATOM   7024  H  HD13   . ILE   B 1 45  ? 38.998  -15.256 39.308 1.00 40.09  ?  70  ILE   B HD13   1 
ATOM   7025  N  N      . ASN   B 1 46  ? 38.605  -12.173 42.395 1.00 28.92  ?  71  ASN   B N      1 
ATOM   7026  C  CA     . ASN   B 1 46  ? 38.085  -11.286 43.432 1.00 28.55  ?  71  ASN   B CA     1 
ATOM   7027  C  C      . ASN   B 1 46  ? 36.702  -10.787 43.031 1.00 27.04  ?  71  ASN   B C      1 
ATOM   7028  O  O      . ASN   B 1 46  ? 36.309  -10.845 41.865 1.00 26.91  ?  71  ASN   B O      1 
ATOM   7029  C  CB     . ASN   B 1 46  ? 39.064  -10.128 43.716 1.00 29.25  ?  71  ASN   B CB     1 
ATOM   7030  C  CG     . ASN   B 1 46  ? 39.074  -9.070  42.628 1.00 30.46  ?  71  ASN   B CG     1 
ATOM   7031  O  OD1    . ASN   B 1 46  ? 38.605  -7.948  42.833 1.00 31.93  ?  71  ASN   B OD1    1 
ATOM   7032  N  ND2    . ASN   B 1 46  ? 39.638  -9.408  41.474 1.00 29.27  ?  71  ASN   B ND2    1 
ATOM   7033  H  H      . ASN   B 1 46  ? 38.202  -12.116 41.637 1.00 34.70  ?  71  ASN   B H      1 
ATOM   7034  H  HA     . ASN   B 1 46  ? 37.968  -11.783 44.257 1.00 34.25  ?  71  ASN   B HA     1 
ATOM   7035  H  HB2    . ASN   B 1 46  ? 38.809  -9.697  44.547 1.00 35.09  ?  71  ASN   B HB2    1 
ATOM   7036  H  HB3    . ASN   B 1 46  ? 39.962  -10.487 43.790 1.00 35.09  ?  71  ASN   B HB3    1 
ATOM   7037  H  HD21   . ASN   B 1 46  ? 39.667  -8.841  40.828 1.00 35.12  ?  71  ASN   B HD21   1 
ATOM   7038  H  HD22   . ASN   B 1 46  ? 39.973  -10.193 41.373 1.00 35.12  ?  71  ASN   B HD22   1 
ATOM   7039  N  N      . TYR   B 1 47  ? 35.955  -10.333 44.035 1.00 26.39  ?  72  TYR   B N      1 
ATOM   7040  C  CA     . TYR   B 1 47  ? 34.568  -9.900  43.892 1.00 25.74  ?  72  TYR   B CA     1 
ATOM   7041  C  C      . TYR   B 1 47  ? 34.547  -8.385  43.984 1.00 25.87  ?  72  TYR   B C      1 
ATOM   7042  O  O      . TYR   B 1 47  ? 34.969  -7.820  45.002 1.00 27.79  ?  72  TYR   B O      1 
ATOM   7043  C  CB     . TYR   B 1 47  ? 33.697  -10.515 44.984 1.00 27.00  ?  72  TYR   B CB     1 
ATOM   7044  C  CG     . TYR   B 1 47  ? 32.197  -10.342 44.810 1.00 27.30  ?  72  TYR   B CG     1 
ATOM   7045  C  CD1    . TYR   B 1 47  ? 31.508  -11.016 43.804 1.00 27.58  ?  72  TYR   B CD1    1 
ATOM   7046  C  CD2    . TYR   B 1 47  ? 31.459  -9.533  45.673 1.00 29.67  ?  72  TYR   B CD2    1 
ATOM   7047  C  CE1    . TYR   B 1 47  ? 30.130  -10.875 43.650 1.00 28.22  ?  72  TYR   B CE1    1 
ATOM   7048  C  CE2    . TYR   B 1 47  ? 30.068  -9.400  45.528 1.00 28.04  ?  72  TYR   B CE2    1 
ATOM   7049  C  CZ     . TYR   B 1 47  ? 29.417  -10.069 44.508 1.00 28.91  ?  72  TYR   B CZ     1 
ATOM   7050  O  OH     . TYR   B 1 47  ? 28.051  -9.952  44.342 1.00 29.73  ?  72  TYR   B OH     1 
ATOM   7051  H  H      . TYR   B 1 47  ? 36.243  -10.264 44.843 1.00 31.67  ?  72  TYR   B H      1 
ATOM   7052  H  HA     . TYR   B 1 47  ? 34.215  -10.174 43.031 1.00 30.88  ?  72  TYR   B HA     1 
ATOM   7053  H  HB2    . TYR   B 1 47  ? 33.875  -11.468 45.015 1.00 32.40  ?  72  TYR   B HB2    1 
ATOM   7054  H  HB3    . TYR   B 1 47  ? 33.937  -10.105 45.830 1.00 32.40  ?  72  TYR   B HB3    1 
ATOM   7055  H  HD1    . TYR   B 1 47  ? 31.977  -11.570 43.223 1.00 33.09  ?  72  TYR   B HD1    1 
ATOM   7056  H  HD2    . TYR   B 1 47  ? 31.894  -9.075  46.355 1.00 35.60  ?  72  TYR   B HD2    1 
ATOM   7057  H  HE1    . TYR   B 1 47  ? 29.691  -11.327 42.965 1.00 33.86  ?  72  TYR   B HE1    1 
ATOM   7058  H  HE2    . TYR   B 1 47  ? 29.587  -8.864  46.116 1.00 33.64  ?  72  TYR   B HE2    1 
ATOM   7059  H  HH     . TYR   B 1 47  ? 27.732  -9.449  44.935 1.00 35.66  ?  72  TYR   B HH     1 
ATOM   7060  N  N      . ARG   B 1 48  ? 34.070  -7.731  42.927 1.00 25.83  ?  73  ARG   B N      1 
ATOM   7061  C  CA     . ARG   B 1 48  ? 34.089  -6.277  42.900 1.00 25.58  ?  73  ARG   B CA     1 
ATOM   7062  C  C      . ARG   B 1 48  ? 33.060  -5.743  41.917 1.00 25.18  ?  73  ARG   B C      1 
ATOM   7063  O  O      . ARG   B 1 48  ? 32.539  -6.462  41.061 1.00 25.24  ?  73  ARG   B O      1 
ATOM   7064  C  CB     . ARG   B 1 48  ? 35.483  -5.738  42.531 1.00 26.41  ?  73  ARG   B CB     1 
ATOM   7065  C  CG     . ARG   B 1 48  ? 35.927  -5.999  41.073 1.00 27.06  ?  73  ARG   B CG     1 
ATOM   7066  C  CD     . ARG   B 1 48  ? 37.211  -5.247  40.755 1.00 28.22  ?  73  ARG   B CD     1 
ATOM   7067  N  NE     . ARG   B 1 48  ? 37.792  -5.517  39.439 1.00 29.37  ?  73  ARG   B NE     1 
ATOM   7068  C  CZ     . ARG   B 1 48  ? 37.431  -4.915  38.307 1.00 29.79  ?  73  ARG   B CZ     1 
ATOM   7069  N  NH1    . ARG   B 1 48  ? 36.442  -4.031  38.299 1.00 30.15  ?  73  ARG   B NH1    1 
ATOM   7070  N  NH2    . ARG   B 1 48  ? 38.044  -5.226  37.172 1.00 29.34  ?  73  ARG   B NH2    1 
ATOM   7071  H  H      . ARG   B 1 48  ? 33.737  -8.103  42.226 1.00 30.99  ?  73  ARG   B H      1 
ATOM   7072  H  HA     . ARG   B 1 48  ? 33.840  -5.973  43.787 1.00 30.68  ?  73  ARG   B HA     1 
ATOM   7073  H  HB2    . ARG   B 1 48  ? 35.486  -4.778  42.668 1.00 31.68  ?  73  ARG   B HB2    1 
ATOM   7074  H  HB3    . ARG   B 1 48  ? 36.137  -6.158  43.112 1.00 31.68  ?  73  ARG   B HB3    1 
ATOM   7075  H  HG2    . ARG   B 1 48  ? 36.086  -6.948  40.947 1.00 32.46  ?  73  ARG   B HG2    1 
ATOM   7076  H  HG3    . ARG   B 1 48  ? 35.234  -5.696  40.464 1.00 32.46  ?  73  ARG   B HG3    1 
ATOM   7077  H  HD2    . ARG   B 1 48  ? 37.026  -4.296  40.799 1.00 33.86  ?  73  ARG   B HD2    1 
ATOM   7078  H  HD3    . ARG   B 1 48  ? 37.877  -5.487  41.419 1.00 33.86  ?  73  ARG   B HD3    1 
ATOM   7079  H  HE     . ARG   B 1 48  ? 38.414  -6.108  39.394 1.00 35.23  ?  73  ARG   B HE     1 
ATOM   7080  H  HH11   . ARG   B 1 48  ? 36.028  -3.842  39.028 1.00 36.18  ?  73  ARG   B HH11   1 
ATOM   7081  H  HH12   . ARG   B 1 48  ? 36.214  -3.648  37.563 1.00 36.18  ?  73  ARG   B HH12   1 
ATOM   7082  H  HH21   . ARG   B 1 48  ? 38.672  -5.814  37.169 1.00 35.20  ?  73  ARG   B HH21   1 
ATOM   7083  H  HH22   . ARG   B 1 48  ? 37.813  -4.840  36.439 1.00 35.20  ?  73  ARG   B HH22   1 
ATOM   7084  N  N      . GLU   B 1 49  ? 32.806  -4.447  42.028 1.00 25.96  ?  74  GLU   B N      1 
ATOM   7085  C  CA     . GLU   B 1 49  ? 31.966  -3.770  41.054 1.00 26.76  ?  74  GLU   B CA     1 
ATOM   7086  C  C      . GLU   B 1 49  ? 32.634  -3.730  39.685 1.00 26.19  ?  74  GLU   B C      1 
ATOM   7087  O  O      . GLU   B 1 49  ? 33.825  -3.426  39.560 1.00 27.08  ?  74  GLU   B O      1 
ATOM   7088  C  CB     . GLU   B 1 49  ? 31.671  -2.350  41.524 1.00 28.12  ?  74  GLU   B CB     1 
ATOM   7089  C  CG     . GLU   B 1 49  ? 30.611  -1.651  40.705 1.00 32.46  ?  74  GLU   B CG     1 
ATOM   7090  C  CD     . GLU   B 1 49  ? 30.372  -0.239  41.182 1.00 38.46  ?  74  GLU   B CD     1 
ATOM   7091  O  OE1    . GLU   B 1 49  ? 31.049  0.676   40.671 1.00 40.67  ?  74  GLU   B OE1    1 
ATOM   7092  O  OE2    . GLU   B 1 49  ? 29.522  -0.057  42.078 1.00 41.52  ?  74  GLU   B OE2    1 
ATOM   7093  H  H      . GLU   B 1 49  ? 33.106  -3.940  42.654 1.00 31.14  ?  74  GLU   B H      1 
ATOM   7094  H  HA     . GLU   B 1 49  ? 31.129  -4.252  40.965 1.00 32.11  ?  74  GLU   B HA     1 
ATOM   7095  H  HB2    . GLU   B 1 49  ? 31.363  -2.383  42.443 1.00 33.73  ?  74  GLU   B HB2    1 
ATOM   7096  H  HB3    . GLU   B 1 49  ? 32.485  -1.826  41.466 1.00 33.73  ?  74  GLU   B HB3    1 
ATOM   7097  H  HG2    . GLU   B 1 49  ? 30.896  -1.614  39.778 1.00 38.95  ?  74  GLU   B HG2    1 
ATOM   7098  H  HG3    . GLU   B 1 49  ? 29.777  -2.141  40.776 1.00 38.95  ?  74  GLU   B HG3    1 
ATOM   7099  N  N      . VAL   B 1 50  ? 31.838  -4.013  38.652 1.00 26.45  ?  75  VAL   B N      1 
ATOM   7100  C  CA     A VAL   B 1 50  ? 32.288  -3.942  37.271 0.68 26.05  ?  75  VAL   B CA     1 
ATOM   7101  C  CA     B VAL   B 1 50  ? 32.262  -4.000  37.257 0.32 26.75  ?  75  VAL   B CA     1 
ATOM   7102  C  C      . VAL   B 1 50  ? 31.198  -3.276  36.443 1.00 25.88  ?  75  VAL   B C      1 
ATOM   7103  O  O      . VAL   B 1 50  ? 30.013  -3.311  36.781 1.00 26.54  ?  75  VAL   B O      1 
ATOM   7104  C  CB     A VAL   B 1 50  ? 32.623  -5.322  36.667 0.68 27.89  ?  75  VAL   B CB     1 
ATOM   7105  C  CB     B VAL   B 1 50  ? 32.469  -5.441  36.745 0.32 28.89  ?  75  VAL   B CB     1 
ATOM   7106  C  CG1    A VAL   B 1 50  ? 33.864  -5.902  37.311 0.68 31.07  ?  75  VAL   B CG1    1 
ATOM   7107  C  CG1    B VAL   B 1 50  ? 32.557  -5.476  35.243 0.32 29.28  ?  75  VAL   B CG1    1 
ATOM   7108  C  CG2    A VAL   B 1 50  ? 31.446  -6.238  36.825 0.68 26.09  ?  75  VAL   B CG2    1 
ATOM   7109  C  CG2    B VAL   B 1 50  ? 33.717  -6.052  37.367 0.32 30.78  ?  75  VAL   B CG2    1 
ATOM   7110  H  H      A VAL   B 1 50  ? 31.016  -4.252  38.733 0.68 31.73  ?  75  VAL   B H      1 
ATOM   7111  H  H      B VAL   B 1 50  ? 31.009  -4.224  38.742 0.32 31.73  ?  75  VAL   B H      1 
ATOM   7112  H  HA     A VAL   B 1 50  ? 33.094  -3.403  37.247 0.68 31.26  ?  75  VAL   B HA     1 
ATOM   7113  H  HA     B VAL   B 1 50  ? 33.094  -3.512  37.156 0.32 32.09  ?  75  VAL   B HA     1 
ATOM   7114  H  HB     A VAL   B 1 50  ? 32.810  -5.225  35.720 0.68 33.46  ?  75  VAL   B HB     1 
ATOM   7115  H  HB     B VAL   B 1 50  ? 31.702  -5.972  37.009 0.32 34.66  ?  75  VAL   B HB     1 
ATOM   7116  H  HG11   A VAL   B 1 50  ? 33.982  -6.814  37.003 0.68 37.28  ?  75  VAL   B HG11   1 
ATOM   7117  H  HG11   B VAL   B 1 50  ? 33.142  -6.203  34.978 0.32 35.12  ?  75  VAL   B HG11   1 
ATOM   7118  H  HG12   A VAL   B 1 50  ? 34.631  -5.365  37.057 0.68 37.28  ?  75  VAL   B HG12   1 
ATOM   7119  H  HG12   B VAL   B 1 50  ? 31.670  -5.615  34.877 0.32 35.12  ?  75  VAL   B HG12   1 
ATOM   7120  H  HG13   A VAL   B 1 50  ? 33.755  -5.888  38.274 0.68 37.28  ?  75  VAL   B HG13   1 
ATOM   7121  H  HG13   B VAL   B 1 50  ? 32.916  -4.631  34.928 0.32 35.12  ?  75  VAL   B HG13   1 
ATOM   7122  H  HG21   A VAL   B 1 50  ? 31.678  -7.112  36.474 0.68 31.30  ?  75  VAL   B HG21   1 
ATOM   7123  H  HG21   B VAL   B 1 50  ? 33.786  -6.979  37.090 0.32 36.93  ?  75  VAL   B HG21   1 
ATOM   7124  H  HG22   A VAL   B 1 50  ? 31.224  -6.308  37.766 0.68 31.30  ?  75  VAL   B HG22   1 
ATOM   7125  H  HG22   B VAL   B 1 50  ? 34.495  -5.558  37.064 0.32 36.93  ?  75  VAL   B HG22   1 
ATOM   7126  H  HG23   A VAL   B 1 50  ? 30.694  -5.873  36.333 0.68 31.30  ?  75  VAL   B HG23   1 
ATOM   7127  H  HG23   B VAL   B 1 50  ? 33.646  -6.000  38.333 0.32 36.93  ?  75  VAL   B HG23   1 
ATOM   7128  N  N      . THR   B 1 51  ? 31.611  -2.641  35.355 1.00 24.96  ?  76  THR   B N      1 
ATOM   7129  C  CA     . THR   B 1 51  ? 30.687  -2.038  34.399 1.00 25.35  ?  76  THR   B CA     1 
ATOM   7130  C  C      . THR   B 1 51  ? 30.947  -2.703  33.057 1.00 24.30  ?  76  THR   B C      1 
ATOM   7131  O  O      . THR   B 1 51  ? 32.085  -2.707  32.579 1.00 26.15  ?  76  THR   B O      1 
ATOM   7132  C  CB     . THR   B 1 51  ? 30.876  -0.525  34.335 1.00 27.63  ?  76  THR   B CB     1 
ATOM   7133  O  OG1    . THR   B 1 51  ? 30.500  0.042   35.599 1.00 28.70  ?  76  THR   B OG1    1 
ATOM   7134  C  CG2    . THR   B 1 51  ? 30.020  0.078   33.248 1.00 28.26  ?  76  THR   B CG2    1 
ATOM   7135  H  H      . THR   B 1 51  ? 32.439  -2.543  35.143 1.00 29.94  ?  76  THR   B H      1 
ATOM   7136  H  HA     . THR   B 1 51  ? 29.764  -2.196  34.652 1.00 30.42  ?  76  THR   B HA     1 
ATOM   7137  H  HB     . THR   B 1 51  ? 31.803  -0.318  34.136 1.00 33.15  ?  76  THR   B HB     1 
ATOM   7138  H  HG1    . THR   B 1 51  ? 30.987  -0.270  36.209 1.00 34.44  ?  76  THR   B HG1    1 
ATOM   7139  H  HG21   . THR   B 1 51  ? 29.970  1.041   33.360 1.00 33.90  ?  76  THR   B HG21   1 
ATOM   7140  H  HG22   . THR   B 1 51  ? 30.400  -0.118  32.378 1.00 33.90  ?  76  THR   B HG22   1 
ATOM   7141  H  HG23   . THR   B 1 51  ? 29.123  -0.290  33.290 1.00 33.90  ?  76  THR   B HG23   1 
ATOM   7142  N  N      . PHE   B 1 52  ? 29.915  -3.319  32.485 1.00 22.03  ?  77  PHE   B N      1 
ATOM   7143  C  CA     . PHE   B 1 52  ? 30.093  -4.131  31.288 1.00 21.87  ?  77  PHE   B CA     1 
ATOM   7144  C  C      . PHE   B 1 52  ? 28.750  -4.280  30.588 1.00 21.26  ?  77  PHE   B C      1 
ATOM   7145  O  O      . PHE   B 1 52  ? 27.691  -3.979  31.155 1.00 21.23  ?  77  PHE   B O      1 
ATOM   7146  C  CB     . PHE   B 1 52  ? 30.673  -5.515  31.623 1.00 22.14  ?  77  PHE   B CB     1 
ATOM   7147  C  CG     . PHE   B 1 52  ? 29.695  -6.431  32.317 1.00 21.47  ?  77  PHE   B CG     1 
ATOM   7148  C  CD1    . PHE   B 1 52  ? 29.376  -6.239  33.655 1.00 22.10  ?  77  PHE   B CD1    1 
ATOM   7149  C  CD2    . PHE   B 1 52  ? 29.096  -7.479  31.632 1.00 20.30  ?  77  PHE   B CD2    1 
ATOM   7150  C  CE1    . PHE   B 1 52  ? 28.474  -7.080  34.301 1.00 23.88  ?  77  PHE   B CE1    1 
ATOM   7151  C  CE2    . PHE   B 1 52  ? 28.196  -8.319  32.268 1.00 21.65  ?  77  PHE   B CE2    1 
ATOM   7152  C  CZ     . PHE   B 1 52  ? 27.882  -8.116  33.600 1.00 23.18  ?  77  PHE   B CZ     1 
ATOM   7153  H  H      . PHE   B 1 52  ? 29.105  -3.282  32.772 1.00 26.43  ?  77  PHE   B H      1 
ATOM   7154  H  HA     . PHE   B 1 52  ? 30.704  -3.670  30.693 1.00 26.24  ?  77  PHE   B HA     1 
ATOM   7155  H  HB2    . PHE   B 1 52  ? 30.949  -5.946  30.799 1.00 26.56  ?  77  PHE   B HB2    1 
ATOM   7156  H  HB3    . PHE   B 1 52  ? 31.438  -5.400  32.209 1.00 26.56  ?  77  PHE   B HB3    1 
ATOM   7157  H  HD1    . PHE   B 1 52  ? 29.769  -5.540  34.125 1.00 26.52  ?  77  PHE   B HD1    1 
ATOM   7158  H  HD2    . PHE   B 1 52  ? 29.301  -7.619  30.736 1.00 24.35  ?  77  PHE   B HD2    1 
ATOM   7159  H  HE1    . PHE   B 1 52  ? 28.270  -6.946  35.198 1.00 28.65  ?  77  PHE   B HE1    1 
ATOM   7160  H  HE2    . PHE   B 1 52  ? 27.803  -9.019  31.800 1.00 25.97  ?  77  PHE   B HE2    1 
ATOM   7161  H  HZ     . PHE   B 1 52  ? 27.272  -8.676  34.025 1.00 27.81  ?  77  PHE   B HZ     1 
ATOM   7162  N  N      . VAL   B 1 53  ? 28.813  -4.785  29.356 1.00 21.86  ?  78  VAL   B N      1 
ATOM   7163  C  CA     . VAL   B 1 53  ? 27.625  -5.043  28.544 1.00 21.00  ?  78  VAL   B CA     1 
ATOM   7164  C  C      . VAL   B 1 53  ? 27.373  -6.549  28.537 1.00 20.16  ?  78  VAL   B C      1 
ATOM   7165  O  O      . VAL   B 1 53  ? 28.187  -7.295  27.956 1.00 20.50  ?  78  VAL   B O      1 
ATOM   7166  C  CB     . VAL   B 1 53  ? 27.797  -4.505  27.117 1.00 22.35  ?  78  VAL   B CB     1 
ATOM   7167  C  CG1    . VAL   B 1 53  ? 26.528  -4.736  26.313 1.00 23.68  ?  78  VAL   B CG1    1 
ATOM   7168  C  CG2    . VAL   B 1 53  ? 28.145  -3.040  27.147 1.00 23.92  ?  78  VAL   B CG2    1 
ATOM   7169  H  H      . VAL   B 1 53  ? 29.549  -4.990  28.961 1.00 26.22  ?  78  VAL   B H      1 
ATOM   7170  H  HA     . VAL   B 1 53  ? 26.859  -4.609  28.951 1.00 25.20  ?  78  VAL   B HA     1 
ATOM   7171  H  HB     . VAL   B 1 53  ? 28.523  -4.980  26.683 1.00 26.82  ?  78  VAL   B HB     1 
ATOM   7172  H  HG11   . VAL   B 1 53  ? 26.589  -4.246  25.478 1.00 28.41  ?  78  VAL   B HG11   1 
ATOM   7173  H  HG12   . VAL   B 1 53  ? 26.436  -5.685  26.134 1.00 28.41  ?  78  VAL   B HG12   1 
ATOM   7174  H  HG13   . VAL   B 1 53  ? 25.767  -4.421  26.826 1.00 28.41  ?  78  VAL   B HG13   1 
ATOM   7175  H  HG21   . VAL   B 1 53  ? 28.154  -2.699  26.239 1.00 28.69  ?  78  VAL   B HG21   1 
ATOM   7176  H  HG22   . VAL   B 1 53  ? 27.479  -2.568  27.672 1.00 28.69  ?  78  VAL   B HG22   1 
ATOM   7177  H  HG23   . VAL   B 1 53  ? 29.021  -2.932  27.550 1.00 28.69  ?  78  VAL   B HG23   1 
ATOM   7178  N  N      . PRO   B 1 54  ? 26.271  -7.035  29.123 1.00 19.66  ?  79  PRO   B N      1 
ATOM   7179  C  CA     . PRO   B 1 54  ? 26.015  -8.489  29.127 1.00 18.78  ?  79  PRO   B CA     1 
ATOM   7180  C  C      . PRO   B 1 54  ? 26.064  -9.150  27.754 1.00 19.18  ?  79  PRO   B C      1 
ATOM   7181  O  O      . PRO   B 1 54  ? 26.641  -10.236 27.616 1.00 19.31  ?  79  PRO   B O      1 
ATOM   7182  C  CB     . PRO   B 1 54  ? 24.608  -8.581  29.758 1.00 18.86  ?  79  PRO   B CB     1 
ATOM   7183  C  CG     . PRO   B 1 54  ? 24.561  -7.396  30.707 1.00 19.59  ?  79  PRO   B CG     1 
ATOM   7184  C  CD     . PRO   B 1 54  ? 25.280  -6.292  29.932 1.00 19.03  ?  79  PRO   B CD     1 
ATOM   7185  H  HA     . PRO   B 1 54  ? 26.666  -8.925  29.699 1.00 22.53  ?  79  PRO   B HA     1 
ATOM   7186  H  HB2    . PRO   B 1 54  ? 23.927  -8.510  29.071 1.00 22.62  ?  79  PRO   B HB2    1 
ATOM   7187  H  HB3    . PRO   B 1 54  ? 24.509  -9.419  30.237 1.00 22.62  ?  79  PRO   B HB3    1 
ATOM   7188  H  HG2    . PRO   B 1 54  ? 23.642  -7.152  30.896 1.00 23.51  ?  79  PRO   B HG2    1 
ATOM   7189  H  HG3    . PRO   B 1 54  ? 25.025  -7.606  31.532 1.00 23.51  ?  79  PRO   B HG3    1 
ATOM   7190  H  HD2    . PRO   B 1 54  ? 24.660  -5.811  29.362 1.00 22.83  ?  79  PRO   B HD2    1 
ATOM   7191  H  HD3    . PRO   B 1 54  ? 25.721  -5.676  30.538 1.00 22.83  ?  79  PRO   B HD3    1 
ATOM   7192  N  N      . GLY   B 1 55  ? 25.491  -8.517  26.731 1.00 19.76  ?  80  GLY   B N      1 
ATOM   7193  C  CA     . GLY   B 1 55  ? 25.462  -9.137  25.416 1.00 20.05  ?  80  GLY   B CA     1 
ATOM   7194  C  C      . GLY   B 1 55  ? 26.844  -9.416  24.849 1.00 20.42  ?  80  GLY   B C      1 
ATOM   7195  O  O      . GLY   B 1 55  ? 27.050  -10.419 24.157 1.00 20.23  ?  80  GLY   B O      1 
ATOM   7196  H  H      . GLY   B 1 55  ? 25.119  -7.743  26.773 1.00 23.70  ?  80  GLY   B H      1 
ATOM   7197  H  HA2    . GLY   B 1 55  ? 24.985  -9.980  25.473 1.00 24.06  ?  80  GLY   B HA2    1 
ATOM   7198  H  HA3    . GLY   B 1 55  ? 24.997  -8.551  24.799 1.00 24.06  ?  80  GLY   B HA3    1 
ATOM   7199  N  N      . LEU   B 1 56  ? 27.802  -8.522  25.109 1.00 21.27  ?  81  LEU   B N      1 
ATOM   7200  C  CA     . LEU   B 1 56  ? 29.168  -8.745  24.642 1.00 21.95  ?  81  LEU   B CA     1 
ATOM   7201  C  C      . LEU   B 1 56  ? 29.802  -9.938  25.352 1.00 21.22  ?  81  LEU   B C      1 
ATOM   7202  O  O      . LEU   B 1 56  ? 30.433  -10.791 24.720 1.00 22.86  ?  81  LEU   B O      1 
ATOM   7203  C  CB     . LEU   B 1 56  ? 29.998  -7.480  24.848 1.00 23.54  ?  81  LEU   B CB     1 
ATOM   7204  C  CG     . LEU   B 1 56  ? 31.501  -7.579  24.590 1.00 25.80  ?  81  LEU   B CG     1 
ATOM   7205  C  CD1    . LEU   B 1 56  ? 31.791  -8.064  23.173 1.00 27.79  ?  81  LEU   B CD1    1 
ATOM   7206  C  CD2    . LEU   B 1 56  ? 32.177  -6.235  24.841 1.00 28.39  ?  81  LEU   B CD2    1 
ATOM   7207  H  H      . LEU   B 1 56  ? 27.688  -7.790  25.546 1.00 25.52  ?  81  LEU   B H      1 
ATOM   7208  H  HA     . LEU   B 1 56  ? 29.151  -8.941  23.692 1.00 26.33  ?  81  LEU   B HA     1 
ATOM   7209  H  HB2    . LEU   B 1 56  ? 29.654  -6.798  24.251 1.00 28.25  ?  81  LEU   B HB2    1 
ATOM   7210  H  HB3    . LEU   B 1 56  ? 29.889  -7.200  25.770 1.00 28.25  ?  81  LEU   B HB3    1 
ATOM   7211  H  HG     . LEU   B 1 56  ? 31.874  -8.231  25.205 1.00 30.95  ?  81  LEU   B HG     1 
ATOM   7212  H  HD11   . LEU   B 1 56  ? 32.751  -8.060  23.028 1.00 33.34  ?  81  LEU   B HD11   1 
ATOM   7213  H  HD12   . LEU   B 1 56  ? 31.445  -8.964  23.070 1.00 33.34  ?  81  LEU   B HD12   1 
ATOM   7214  H  HD13   . LEU   B 1 56  ? 31.359  -7.469  22.541 1.00 33.34  ?  81  LEU   B HD13   1 
ATOM   7215  H  HD21   . LEU   B 1 56  ? 33.137  -6.343  24.754 1.00 34.07  ?  81  LEU   B HD21   1 
ATOM   7216  H  HD22   . LEU   B 1 56  ? 31.856  -5.594  24.188 1.00 34.07  ?  81  LEU   B HD22   1 
ATOM   7217  H  HD23   . LEU   B 1 56  ? 31.957  -5.934  25.736 1.00 34.07  ?  81  LEU   B HD23   1 
ATOM   7218  N  N      . TYR   B 1 57  ? 29.636  -10.015 26.672 1.00 21.44  ?  82  TYR   B N      1 
ATOM   7219  C  CA     . TYR   B 1 57  ? 30.132  -11.154 27.438 1.00 19.96  ?  82  TYR   B CA     1 
ATOM   7220  C  C      . TYR   B 1 57  ? 29.525  -12.451 26.938 1.00 19.85  ?  82  TYR   B C      1 
ATOM   7221  O  O      . TYR   B 1 57  ? 30.206  -13.481 26.868 1.00 20.78  ?  82  TYR   B O      1 
ATOM   7222  C  CB     . TYR   B 1 57  ? 29.778  -10.943 28.906 1.00 19.45  ?  82  TYR   B CB     1 
ATOM   7223  C  CG     . TYR   B 1 57  ? 30.434  -11.795 29.967 1.00 19.11  ?  82  TYR   B CG     1 
ATOM   7224  C  CD1    . TYR   B 1 57  ? 31.662  -12.396 29.780 1.00 20.34  ?  82  TYR   B CD1    1 
ATOM   7225  C  CD2    . TYR   B 1 57  ? 29.822  -11.951 31.196 1.00 20.74  ?  82  TYR   B CD2    1 
ATOM   7226  C  CE1    . TYR   B 1 57  ? 32.245  -13.135 30.794 1.00 21.69  ?  82  TYR   B CE1    1 
ATOM   7227  C  CE2    . TYR   B 1 57  ? 30.400  -12.688 32.211 1.00 22.36  ?  82  TYR   B CE2    1 
ATOM   7228  C  CZ     . TYR   B 1 57  ? 31.618  -13.259 32.009 1.00 22.36  ?  82  TYR   B CZ     1 
ATOM   7229  O  OH     . TYR   B 1 57  ? 32.209  -13.968 33.027 1.00 24.88  ?  82  TYR   B OH     1 
ATOM   7230  H  H      . TYR   B 1 57  ? 29.238  -9.420  27.149 1.00 25.72  ?  82  TYR   B H      1 
ATOM   7231  H  HA     . TYR   B 1 57  ? 31.095  -11.218 27.346 1.00 23.94  ?  82  TYR   B HA     1 
ATOM   7232  H  HB2    . TYR   B 1 57  ? 29.996  -10.023 29.125 1.00 23.33  ?  82  TYR   B HB2    1 
ATOM   7233  H  HB3    . TYR   B 1 57  ? 28.823  -11.087 28.996 1.00 23.33  ?  82  TYR   B HB3    1 
ATOM   7234  H  HD1    . TYR   B 1 57  ? 32.101  -12.305 28.965 1.00 24.40  ?  82  TYR   B HD1    1 
ATOM   7235  H  HD2    . TYR   B 1 57  ? 28.997  -11.548 31.344 1.00 24.88  ?  82  TYR   B HD2    1 
ATOM   7236  H  HE1    . TYR   B 1 57  ? 33.066  -13.548 30.652 1.00 26.02  ?  82  TYR   B HE1    1 
ATOM   7237  H  HE2    . TYR   B 1 57  ? 29.961  -12.793 33.024 1.00 26.83  ?  82  TYR   B HE2    1 
ATOM   7238  H  HH     . TYR   B 1 57  ? 32.962  -14.250 32.783 1.00 29.85  ?  82  TYR   B HH     1 
ATOM   7239  N  N      . LYS   B 1 58  ? 28.237  -12.413 26.589 1.00 18.94  ?  83  LYS   B N      1 
ATOM   7240  C  CA     . LYS   B 1 58  ? 27.515  -13.615 26.194 1.00 18.51  ?  83  LYS   B CA     1 
ATOM   7241  C  C      . LYS   B 1 58  ? 27.990  -14.153 24.849 1.00 19.99  ?  83  LYS   B C      1 
ATOM   7242  O  O      . LYS   B 1 58  ? 28.072  -15.374 24.674 1.00 20.51  ?  83  LYS   B O      1 
ATOM   7243  C  CB     . LYS   B 1 58  ? 26.011  -13.324 26.180 1.00 18.33  ?  83  LYS   B CB     1 
ATOM   7244  C  CG     . LYS   B 1 58  ? 25.120  -14.479 25.696 1.00 19.82  ?  83  LYS   B CG     1 
ATOM   7245  C  CD     . LYS   B 1 58  ? 25.373  -15.785 26.454 1.00 22.05  ?  83  LYS   B CD     1 
ATOM   7246  C  CE     . LYS   B 1 58  ? 25.210  -15.594 27.938 1.00 22.41  ?  83  LYS   B CE     1 
ATOM   7247  N  NZ     . LYS   B 1 58  ? 25.290  -16.884 28.683 1.00 23.49  ?  83  LYS   B NZ     1 
ATOM   7248  H  H      . LYS   B 1 58  ? 27.758  -11.698 26.573 1.00 22.72  ?  83  LYS   B H      1 
ATOM   7249  H  HA     . LYS   B 1 58  ? 27.684  -14.312 26.847 1.00 22.21  ?  83  LYS   B HA     1 
ATOM   7250  H  HB2    . LYS   B 1 58  ? 25.734  -13.104 27.083 1.00 21.99  ?  83  LYS   B HB2    1 
ATOM   7251  H  HB3    . LYS   B 1 58  ? 25.852  -12.569 25.592 1.00 21.99  ?  83  LYS   B HB3    1 
ATOM   7252  H  HG2    . LYS   B 1 58  ? 24.190  -14.235 25.823 1.00 23.78  ?  83  LYS   B HG2    1 
ATOM   7253  H  HG3    . LYS   B 1 58  ? 25.295  -14.640 24.756 1.00 23.78  ?  83  LYS   B HG3    1 
ATOM   7254  H  HD2    . LYS   B 1 58  ? 24.738  -16.456 26.160 1.00 26.46  ?  83  LYS   B HD2    1 
ATOM   7255  H  HD3    . LYS   B 1 58  ? 26.279  -16.087 26.282 1.00 26.46  ?  83  LYS   B HD3    1 
ATOM   7256  H  HE2    . LYS   B 1 58  ? 25.914  -15.012 28.264 1.00 26.88  ?  83  LYS   B HE2    1 
ATOM   7257  H  HE3    . LYS   B 1 58  ? 24.343  -15.196 28.115 1.00 26.88  ?  83  LYS   B HE3    1 
ATOM   7258  H  HZ1    . LYS   B 1 58  ? 24.650  -17.436 28.405 1.00 28.18  ?  83  LYS   B HZ1    1 
ATOM   7259  H  HZ2    . LYS   B 1 58  ? 26.081  -17.266 28.545 1.00 28.18  ?  83  LYS   B HZ2    1 
ATOM   7260  H  HZ3    . LYS   B 1 58  ? 25.187  -16.739 29.555 1.00 28.18  ?  83  LYS   B HZ3    1 
ATOM   7261  N  N      . ILE   B 1 59  ? 28.307  -13.287 23.878 1.00 20.39  ?  84  ILE   B N      1 
ATOM   7262  C  CA     . ILE   B 1 59  ? 28.692  -13.870 22.591 1.00 22.13  ?  84  ILE   B CA     1 
ATOM   7263  C  C      . ILE   B 1 59  ? 30.035  -14.596 22.729 1.00 23.36  ?  84  ILE   B C      1 
ATOM   7264  O  O      . ILE   B 1 59  ? 30.278  -15.598 22.046 1.00 23.97  ?  84  ILE   B O      1 
ATOM   7265  C  CB     . ILE   B 1 59  ? 28.714  -12.844 21.439 1.00 23.69  ?  84  ILE   B CB     1 
ATOM   7266  C  CG1    . ILE   B 1 59  ? 29.622  -11.652 21.705 1.00 25.12  ?  84  ILE   B CG1    1 
ATOM   7267  C  CG2    . ILE   B 1 59  ? 27.280  -12.367 21.158 1.00 23.77  ?  84  ILE   B CG2    1 
ATOM   7268  C  CD1    . ILE   B 1 59  ? 29.840  -10.782 20.465 1.00 27.22  ?  84  ILE   B CD1    1 
ATOM   7269  H  H      . ILE   B 1 59  ? 28.306  -12.429 23.936 1.00 24.46  ?  84  ILE   B H      1 
ATOM   7270  H  HA     . ILE   B 1 59  ? 28.004  -14.510 22.352 1.00 26.55  ?  84  ILE   B HA     1 
ATOM   7271  H  HB     . ILE   B 1 59  ? 29.085  -13.297 20.666 1.00 28.42  ?  84  ILE   B HB     1 
ATOM   7272  H  HG12   . ILE   B 1 59  ? 29.221  -11.098 22.393 1.00 30.14  ?  84  ILE   B HG12   1 
ATOM   7273  H  HG13   . ILE   B 1 59  ? 30.487  -11.974 22.001 1.00 30.14  ?  84  ILE   B HG13   1 
ATOM   7274  H  HG21   . ILE   B 1 59  ? 27.274  -11.855 20.334 1.00 28.51  ?  84  ILE   B HG21   1 
ATOM   7275  H  HG22   . ILE   B 1 59  ? 26.701  -13.140 21.071 1.00 28.51  ?  84  ILE   B HG22   1 
ATOM   7276  H  HG23   . ILE   B 1 59  ? 26.982  -11.811 21.894 1.00 28.51  ?  84  ILE   B HG23   1 
ATOM   7277  H  HD11   . ILE   B 1 59  ? 30.520  -10.117 20.661 1.00 32.66  ?  84  ILE   B HD11   1 
ATOM   7278  H  HD12   . ILE   B 1 59  ? 30.131  -11.345 19.731 1.00 32.66  ?  84  ILE   B HD12   1 
ATOM   7279  H  HD13   . ILE   B 1 59  ? 29.006  -10.343 20.235 1.00 32.66  ?  84  ILE   B HD13   1 
ATOM   7280  N  N      . PHE   B 1 60  ? 30.909  -14.119 23.628 1.00 22.58  ?  85  PHE   B N      1 
ATOM   7281  C  CA     . PHE   B 1 60  ? 32.135  -14.838 23.990 1.00 23.33  ?  85  PHE   B CA     1 
ATOM   7282  C  C      . PHE   B 1 60  ? 31.803  -16.176 24.645 1.00 22.56  ?  85  PHE   B C      1 
ATOM   7283  O  O      . PHE   B 1 60  ? 32.352  -17.221 24.274 1.00 23.53  ?  85  PHE   B O      1 
ATOM   7284  C  CB     . PHE   B 1 60  ? 32.970  -13.923 24.911 1.00 22.92  ?  85  PHE   B CB     1 
ATOM   7285  C  CG     . PHE   B 1 60  ? 34.152  -14.586 25.552 1.00 23.79  ?  85  PHE   B CG     1 
ATOM   7286  C  CD1    . PHE   B 1 60  ? 35.354  -14.693 24.876 1.00 25.20  ?  85  PHE   B CD1    1 
ATOM   7287  C  CD2    . PHE   B 1 60  ? 34.078  -15.058 26.850 1.00 24.72  ?  85  PHE   B CD2    1 
ATOM   7288  C  CE1    . PHE   B 1 60  ? 36.447  -15.310 25.462 1.00 25.80  ?  85  PHE   B CE1    1 
ATOM   7289  C  CE2    . PHE   B 1 60  ? 35.172  -15.657 27.445 1.00 24.99  ?  85  PHE   B CE2    1 
ATOM   7290  C  CZ     . PHE   B 1 60  ? 36.360  -15.783 26.745 1.00 25.89  ?  85  PHE   B CZ     1 
ATOM   7291  H  H      . PHE   B 1 60  ? 30.814  -13.374 24.047 1.00 27.09  ?  85  PHE   B H      1 
ATOM   7292  H  HA     . PHE   B 1 60  ? 32.665  -15.041 23.203 1.00 27.99  ?  85  PHE   B HA     1 
ATOM   7293  H  HB2    . PHE   B 1 60  ? 33.302  -13.179 24.385 1.00 27.49  ?  85  PHE   B HB2    1 
ATOM   7294  H  HB3    . PHE   B 1 60  ? 32.397  -13.598 25.622 1.00 27.49  ?  85  PHE   B HB3    1 
ATOM   7295  H  HD1    . PHE   B 1 60  ? 35.430  -14.346 24.016 1.00 30.24  ?  85  PHE   B HD1    1 
ATOM   7296  H  HD2    . PHE   B 1 60  ? 33.284  -14.970 27.327 1.00 29.66  ?  85  PHE   B HD2    1 
ATOM   7297  H  HE1    . PHE   B 1 60  ? 37.240  -15.403 24.984 1.00 30.95  ?  85  PHE   B HE1    1 
ATOM   7298  H  HE2    . PHE   B 1 60  ? 35.111  -15.976 28.316 1.00 29.99  ?  85  PHE   B HE2    1 
ATOM   7299  H  HZ     . PHE   B 1 60  ? 37.096  -16.188 27.144 1.00 31.07  ?  85  PHE   B HZ     1 
ATOM   7300  N  N      . ASP   B 1 61  ? 30.865  -16.158 25.600 1.00 21.24  ?  86  ASP   B N      1 
ATOM   7301  C  CA     . ASP   B 1 61  ? 30.416  -17.381 26.263 1.00 21.34  ?  86  ASP   B CA     1 
ATOM   7302  C  C      . ASP   B 1 61  ? 29.905  -18.422 25.272 1.00 21.27  ?  86  ASP   B C      1 
ATOM   7303  O  O      . ASP   B 1 61  ? 30.186  -19.618 25.417 1.00 21.22  ?  86  ASP   B O      1 
ATOM   7304  C  CB     . ASP   B 1 61  ? 29.317  -17.022 27.268 1.00 20.79  ?  86  ASP   B CB     1 
ATOM   7305  C  CG     . ASP   B 1 61  ? 28.885  -18.196 28.128 1.00 22.39  ?  86  ASP   B CG     1 
ATOM   7306  O  OD1    . ASP   B 1 61  ? 29.766  -18.870 28.700 1.00 23.28  ?  86  ASP   B OD1    1 
ATOM   7307  O  OD2    . ASP   B 1 61  ? 27.664  -18.433 28.249 1.00 22.95  ?  86  ASP   B OD2    1 
ATOM   7308  H  H      . ASP   B 1 61  ? 30.472  -15.447 25.883 1.00 25.48  ?  86  ASP   B H      1 
ATOM   7309  H  HA     . ASP   B 1 61  ? 31.168  -17.778 26.731 1.00 25.61  ?  86  ASP   B HA     1 
ATOM   7310  H  HB2    . ASP   B 1 61  ? 29.645  -16.326 27.858 1.00 24.94  ?  86  ASP   B HB2    1 
ATOM   7311  H  HB3    . ASP   B 1 61  ? 28.538  -16.706 26.784 1.00 24.94  ?  86  ASP   B HB3    1 
ATOM   7312  N  N      . GLU   B 1 62  ? 29.122  -17.996 24.283 1.00 20.52  ?  87  GLU   B N      1 
ATOM   7313  C  CA     . GLU   B 1 62  ? 28.555  -18.967 23.354 1.00 21.06  ?  87  GLU   B CA     1 
ATOM   7314  C  C      . GLU   B 1 62  ? 29.653  -19.759 22.654 1.00 21.38  ?  87  GLU   B C      1 
ATOM   7315  O  O      . GLU   B 1 62  ? 29.542  -20.979 22.483 1.00 22.15  ?  87  GLU   B O      1 
ATOM   7316  C  CB     . GLU   B 1 62  ? 27.673  -18.276 22.312 1.00 20.81  ?  87  GLU   B CB     1 
ATOM   7317  C  CG     . GLU   B 1 62  ? 26.384  -17.654 22.857 1.00 20.48  ?  87  GLU   B CG     1 
ATOM   7318  C  CD     . GLU   B 1 62  ? 25.297  -18.666 23.277 1.00 22.91  ?  87  GLU   B CD     1 
ATOM   7319  O  OE1    . GLU   B 1 62  ? 24.207  -18.209 23.698 1.00 26.08  ?  87  GLU   B OE1    1 
ATOM   7320  O  OE2    . GLU   B 1 62  ? 25.517  -19.897 23.210 1.00 23.59  ?  87  GLU   B OE2    1 
ATOM   7321  H  H      . GLU   B 1 62  ? 28.910  -17.176 24.132 1.00 24.62  ?  87  GLU   B H      1 
ATOM   7322  H  HA     . GLU   B 1 62  ? 27.997  -19.578 23.860 1.00 25.27  ?  87  GLU   B HA     1 
ATOM   7323  H  HB2    . GLU   B 1 62  ? 28.187  -17.564 21.900 1.00 24.97  ?  87  GLU   B HB2    1 
ATOM   7324  H  HB3    . GLU   B 1 62  ? 27.418  -18.932 21.644 1.00 24.97  ?  87  GLU   B HB3    1 
ATOM   7325  H  HG2    . GLU   B 1 62  ? 26.605  -17.124 23.638 1.00 24.57  ?  87  GLU   B HG2    1 
ATOM   7326  H  HG3    . GLU   B 1 62  ? 26.002  -17.088 22.168 1.00 24.57  ?  87  GLU   B HG3    1 
ATOM   7327  N  N      . ILE   B 1 63  ? 30.711  -19.080 22.212 1.00 21.75  ?  88  ILE   B N      1 
ATOM   7328  C  CA     . ILE   B 1 63  ? 31.770  -19.783 21.492 1.00 24.51  ?  88  ILE   B CA     1 
ATOM   7329  C  C      . ILE   B 1 63  ? 32.589  -20.641 22.450 1.00 24.87  ?  88  ILE   B C      1 
ATOM   7330  O  O      . ILE   B 1 63  ? 33.019  -21.751 22.107 1.00 25.75  ?  88  ILE   B O      1 
ATOM   7331  C  CB     . ILE   B 1 63  ? 32.658  -18.780 20.735 1.00 25.90  ?  88  ILE   B CB     1 
ATOM   7332  C  CG1    . ILE   B 1 63  ? 31.805  -17.951 19.773 1.00 25.82  ?  88  ILE   B CG1    1 
ATOM   7333  C  CG2    . ILE   B 1 63  ? 33.779  -19.509 19.975 1.00 26.19  ?  88  ILE   B CG2    1 
ATOM   7334  C  CD1    . ILE   B 1 63  ? 30.970  -18.765 18.812 1.00 26.58  ?  88  ILE   B CD1    1 
ATOM   7335  H  H      . ILE   B 1 63  ? 30.837  -18.235 22.314 1.00 26.10  ?  88  ILE   B H      1 
ATOM   7336  H  HA     . ILE   B 1 63  ? 31.358  -20.372 20.840 1.00 29.40  ?  88  ILE   B HA     1 
ATOM   7337  H  HB     . ILE   B 1 63  ? 33.069  -18.185 21.381 1.00 31.07  ?  88  ILE   B HB     1 
ATOM   7338  H  HG12   . ILE   B 1 63  ? 31.200  -17.400 20.293 1.00 30.97  ?  88  ILE   B HG12   1 
ATOM   7339  H  HG13   . ILE   B 1 63  ? 32.394  -17.389 19.245 1.00 30.97  ?  88  ILE   B HG13   1 
ATOM   7340  H  HG21   . ILE   B 1 63  ? 34.223  -18.879 19.386 1.00 31.43  ?  88  ILE   B HG21   1 
ATOM   7341  H  HG22   . ILE   B 1 63  ? 34.414  -19.867 20.615 1.00 31.43  ?  88  ILE   B HG22   1 
ATOM   7342  H  HG23   . ILE   B 1 63  ? 33.391  -20.231 19.456 1.00 31.43  ?  88  ILE   B HG23   1 
ATOM   7343  H  HD11   . ILE   B 1 63  ? 30.613  -18.178 18.128 1.00 31.89  ?  88  ILE   B HD11   1 
ATOM   7344  H  HD12   . ILE   B 1 63  ? 31.530  -19.445 18.405 1.00 31.89  ?  88  ILE   B HD12   1 
ATOM   7345  H  HD13   . ILE   B 1 63  ? 30.244  -19.184 19.301 1.00 31.89  ?  88  ILE   B HD13   1 
ATOM   7346  N  N      . LEU   B 1 64  ? 32.814  -20.147 23.667 1.00 24.08  ?  89  LEU   B N      1 
ATOM   7347  C  CA     . LEU   B 1 64  ? 33.596  -20.900 24.643 1.00 24.14  ?  89  LEU   B CA     1 
ATOM   7348  C  C      . LEU   B 1 64  ? 32.881  -22.176 25.068 1.00 23.00  ?  89  LEU   B C      1 
ATOM   7349  O  O      . LEU   B 1 64  ? 33.503  -23.241 25.150 1.00 25.01  ?  89  LEU   B O      1 
ATOM   7350  C  CB     . LEU   B 1 64  ? 33.880  -20.003 25.843 1.00 26.31  ?  89  LEU   B CB     1 
ATOM   7351  C  CG     . LEU   B 1 64  ? 34.819  -20.464 26.949 1.00 26.78  ?  89  LEU   B CG     1 
ATOM   7352  C  CD1    . LEU   B 1 64  ? 36.209  -20.775 26.424 1.00 27.41  ?  89  LEU   B CD1    1 
ATOM   7353  C  CD2    . LEU   B 1 64  ? 34.865  -19.382 28.047 1.00 29.34  ?  89  LEU   B CD2    1 
ATOM   7354  H  H      . LEU   B 1 64  ? 32.529  -19.386 23.949 1.00 28.89  ?  89  LEU   B H      1 
ATOM   7355  H  HA     . LEU   B 1 64  ? 34.441  -21.166 24.248 1.00 28.96  ?  89  LEU   B HA     1 
ATOM   7356  H  HB2    . LEU   B 1 64  ? 34.258  -19.179 25.498 1.00 31.57  ?  89  LEU   B HB2    1 
ATOM   7357  H  HB3    . LEU   B 1 64  ? 33.029  -19.825 26.272 1.00 31.57  ?  89  LEU   B HB3    1 
ATOM   7358  H  HG     . LEU   B 1 64  ? 34.487  -21.292 27.329 1.00 32.14  ?  89  LEU   B HG     1 
ATOM   7359  H  HD11   . LEU   B 1 64  ? 36.782  -21.012 27.169 1.00 32.89  ?  89  LEU   B HD11   1 
ATOM   7360  H  HD12   . LEU   B 1 64  ? 36.152  -21.516 25.801 1.00 32.89  ?  89  LEU   B HD12   1 
ATOM   7361  H  HD13   . LEU   B 1 64  ? 36.559  -19.990 25.974 1.00 32.89  ?  89  LEU   B HD13   1 
ATOM   7362  H  HD21   . LEU   B 1 64  ? 35.459  -19.677 28.755 1.00 35.20  ?  89  LEU   B HD21   1 
ATOM   7363  H  HD22   . LEU   B 1 64  ? 35.194  -18.555 27.662 1.00 35.20  ?  89  LEU   B HD22   1 
ATOM   7364  H  HD23   . LEU   B 1 64  ? 33.971  -19.251 28.399 1.00 35.20  ?  89  LEU   B HD23   1 
ATOM   7365  N  N      . VAL   B 1 65  ? 31.574  -22.098 25.327 1.00 21.85  ?  90  VAL   B N      1 
ATOM   7366  C  CA     . VAL   B 1 65  ? 30.825  -23.298 25.689 1.00 21.09  ?  90  VAL   B CA     1 
ATOM   7367  C  C      . VAL   B 1 65  ? 30.783  -24.280 24.521 1.00 21.10  ?  90  VAL   B C      1 
ATOM   7368  O  O      . VAL   B 1 65  ? 30.834  -25.496 24.727 1.00 21.91  ?  90  VAL   B O      1 
ATOM   7369  C  CB     . VAL   B 1 65  ? 29.410  -22.923 26.173 1.00 20.18  ?  90  VAL   B CB     1 
ATOM   7370  C  CG1    . VAL   B 1 65  ? 28.517  -24.169 26.327 1.00 21.05  ?  90  VAL   B CG1    1 
ATOM   7371  C  CG2    . VAL   B 1 65  ? 29.478  -22.169 27.503 1.00 20.19  ?  90  VAL   B CG2    1 
ATOM   7372  H  H      . VAL   B 1 65  ? 31.108  -21.376 25.300 1.00 26.22  ?  90  VAL   B H      1 
ATOM   7373  H  HA     . VAL   B 1 65  ? 31.284  -23.733 26.425 1.00 25.30  ?  90  VAL   B HA     1 
ATOM   7374  H  HB     . VAL   B 1 65  ? 29.010  -22.346 25.503 1.00 24.22  ?  90  VAL   B HB     1 
ATOM   7375  H  HG11   . VAL   B 1 65  ? 27.729  -23.931 26.840 1.00 25.25  ?  90  VAL   B HG11   1 
ATOM   7376  H  HG12   . VAL   B 1 65  ? 28.257  -24.481 25.446 1.00 25.25  ?  90  VAL   B HG12   1 
ATOM   7377  H  HG13   . VAL   B 1 65  ? 29.017  -24.860 26.789 1.00 25.25  ?  90  VAL   B HG13   1 
ATOM   7378  H  HG21   . VAL   B 1 65  ? 28.579  -21.934 27.779 1.00 24.22  ?  90  VAL   B HG21   1 
ATOM   7379  H  HG22   . VAL   B 1 65  ? 29.890  -22.740 28.169 1.00 24.22  ?  90  VAL   B HG22   1 
ATOM   7380  H  HG23   . VAL   B 1 65  ? 30.008  -21.365 27.383 1.00 24.22  ?  90  VAL   B HG23   1 
ATOM   7381  N  N      . ASN   B 1 66  ? 30.688  -23.783 23.283 1.00 20.92  ?  91  ASN   B N      1 
ATOM   7382  C  CA     . ASN   B 1 66  ? 30.754  -24.688 22.137 1.00 22.59  ?  91  ASN   B CA     1 
ATOM   7383  C  C      . ASN   B 1 66  ? 32.053  -25.495 22.141 1.00 24.72  ?  91  ASN   B C      1 
ATOM   7384  O  O      . ASN   B 1 66  ? 32.065  -26.669 21.749 1.00 25.21  ?  91  ASN   B O      1 
ATOM   7385  C  CB     . ASN   B 1 66  ? 30.647  -23.927 20.813 1.00 23.23  ?  91  ASN   B CB     1 
ATOM   7386  C  CG     . ASN   B 1 66  ? 29.235  -23.498 20.478 1.00 22.38  ?  91  ASN   B CG     1 
ATOM   7387  O  OD1    . ASN   B 1 66  ? 28.255  -23.966 21.064 1.00 21.22  ?  91  ASN   B OD1    1 
ATOM   7388  N  ND2    . ASN   B 1 66  ? 29.126  -22.599 19.508 1.00 23.44  ?  91  ASN   B ND2    1 
ATOM   7389  H  H      . ASN   B 1 66  ? 30.589  -22.952 23.087 1.00 25.10  ?  91  ASN   B H      1 
ATOM   7390  H  HA     . ASN   B 1 66  ? 29.996  -25.289 22.203 1.00 27.10  ?  91  ASN   B HA     1 
ATOM   7391  H  HB2    . ASN   B 1 66  ? 31.196  -23.129 20.864 1.00 27.87  ?  91  ASN   B HB2    1 
ATOM   7392  H  HB3    . ASN   B 1 66  ? 30.961  -24.500 20.096 1.00 27.87  ?  91  ASN   B HB3    1 
ATOM   7393  H  HD21   . ASN   B 1 66  ? 28.349  -22.314 19.271 1.00 28.12  ?  91  ASN   B HD21   1 
ATOM   7394  H  HD22   . ASN   B 1 66  ? 29.831  -22.301 19.117 1.00 28.12  ?  91  ASN   B HD22   1 
ATOM   7395  N  N      . ALA   B 1 67  ? 33.172  -24.873 22.535 1.00 25.43  ?  92  ALA   B N      1 
ATOM   7396  C  CA     . ALA   B 1 67  ? 34.431  -25.617 22.590 1.00 26.96  ?  92  ALA   B CA     1 
ATOM   7397  C  C      . ALA   B 1 67  ? 34.403  -26.677 23.688 1.00 27.26  ?  92  ALA   B C      1 
ATOM   7398  O  O      . ALA   B 1 67  ? 34.878  -27.798 23.486 1.00 27.69  ?  92  ALA   B O      1 
ATOM   7399  C  CB     . ALA   B 1 67  ? 35.612  -24.667 22.806 1.00 28.02  ?  92  ALA   B CB     1 
ATOM   7400  H  H      . ALA   B 1 67  ? 33.225  -24.047 22.768 1.00 30.51  ?  92  ALA   B H      1 
ATOM   7401  H  HA     . ALA   B 1 67  ? 34.556  -26.060 21.737 1.00 32.34  ?  92  ALA   B HA     1 
ATOM   7402  H  HB1    . ALA   B 1 67  ? 36.432  -25.185 22.839 1.00 33.62  ?  92  ALA   B HB1    1 
ATOM   7403  H  HB2    . ALA   B 1 67  ? 35.649  -24.036 22.070 1.00 33.62  ?  92  ALA   B HB2    1 
ATOM   7404  H  HB3    . ALA   B 1 67  ? 35.487  -24.192 23.643 1.00 33.62  ?  92  ALA   B HB3    1 
ATOM   7405  N  N      . ALA   B 1 68  ? 33.871  -26.336 24.863 1.00 26.17  ?  93  ALA   B N      1 
ATOM   7406  C  CA     . ALA   B 1 68  ? 33.719  -27.332 25.919 1.00 24.77  ?  93  ALA   B CA     1 
ATOM   7407  C  C      . ALA   B 1 68  ? 32.810  -28.472 25.469 1.00 24.70  ?  93  ALA   B C      1 
ATOM   7408  O  O      . ALA   B 1 68  ? 33.040  -29.632 25.830 1.00 24.66  ?  93  ALA   B O      1 
ATOM   7409  C  CB     . ALA   B 1 68  ? 33.183  -26.665 27.186 1.00 24.35  ?  93  ALA   B CB     1 
ATOM   7410  H  H      . ALA   B 1 68  ? 33.595  -25.548 25.070 1.00 31.40  ?  93  ALA   B H      1 
ATOM   7411  H  HA     . ALA   B 1 68  ? 34.585  -27.714 26.130 1.00 29.71  ?  93  ALA   B HA     1 
ATOM   7412  H  HB1    . ALA   B 1 68  ? 33.071  -27.339 27.875 1.00 29.21  ?  93  ALA   B HB1    1 
ATOM   7413  H  HB2    . ALA   B 1 68  ? 33.816  -25.992 27.481 1.00 29.21  ?  93  ALA   B HB2    1 
ATOM   7414  H  HB3    . ALA   B 1 68  ? 32.328  -26.250 26.987 1.00 29.21  ?  93  ALA   B HB3    1 
ATOM   7415  N  N      . ASP   B 1 69  ? 31.772  -28.155 24.680 1.00 24.47  ?  94  ASP   B N      1 
ATOM   7416  C  CA     . ASP   B 1 69  ? 30.860  -29.186 24.187 1.00 24.79  ?  94  ASP   B CA     1 
ATOM   7417  C  C      . ASP   B 1 69  ? 31.595  -30.231 23.351 1.00 26.04  ?  94  ASP   B C      1 
ATOM   7418  O  O      . ASP   B 1 69  ? 31.166  -31.390 23.277 1.00 26.87  ?  94  ASP   B O      1 
ATOM   7419  C  CB     . ASP   B 1 69  ? 29.741  -28.571 23.334 1.00 24.73  ?  94  ASP   B CB     1 
ATOM   7420  C  CG     . ASP   B 1 69  ? 28.668  -27.863 24.151 1.00 26.63  ?  94  ASP   B CG     1 
ATOM   7421  O  OD1    . ASP   B 1 69  ? 28.618  -28.055 25.391 1.00 26.55  ?  94  ASP   B OD1    1 
ATOM   7422  O  OD2    . ASP   B 1 69  ? 27.866  -27.115 23.531 1.00 27.34  ?  94  ASP   B OD2    1 
ATOM   7423  H  H      . ASP   B 1 69  ? 31.578  -27.359 24.420 1.00 29.35  ?  94  ASP   B H      1 
ATOM   7424  H  HA     . ASP   B 1 69  ? 30.458  -29.614 24.959 1.00 29.74  ?  94  ASP   B HA     1 
ATOM   7425  H  HB2    . ASP   B 1 69  ? 30.130  -27.920 22.730 1.00 29.67  ?  94  ASP   B HB2    1 
ATOM   7426  H  HB3    . ASP   B 1 69  ? 29.310  -29.277 22.828 1.00 29.67  ?  94  ASP   B HB3    1 
ATOM   7427  N  N      . ASN   B 1 70  ? 32.681  -29.838 22.684 1.00 27.09  ?  95  ASN   B N      1 
ATOM   7428  C  CA     . ASN   B 1 70  ? 33.375  -30.791 21.829 1.00 28.72  ?  95  ASN   B CA     1 
ATOM   7429  C  C      . ASN   B 1 70  ? 34.071  -31.875 22.641 1.00 30.41  ?  95  ASN   B C      1 
ATOM   7430  O  O      . ASN   B 1 70  ? 34.404  -32.925 22.086 1.00 31.79  ?  95  ASN   B O      1 
ATOM   7431  C  CB     . ASN   B 1 70  ? 34.403  -30.098 20.926 1.00 29.85  ?  95  ASN   B CB     1 
ATOM   7432  C  CG     . ASN   B 1 70  ? 34.709  -30.920 19.675 1.00 32.29  ?  95  ASN   B CG     1 
ATOM   7433  O  OD1    . ASN   B 1 70  ? 33.791  -31.239 18.916 1.00 32.23  ?  95  ASN   B OD1    1 
ATOM   7434  N  ND2    . ASN   B 1 70  ? 35.983  -31.278 19.457 1.00 33.36  ?  95  ASN   B ND2    1 
ATOM   7435  H  H      . ASN   B 1 70  ? 33.024  -29.050 22.710 1.00 32.50  ?  95  ASN   B H      1 
ATOM   7436  H  HA     . ASN   B 1 70  ? 32.715  -31.199 21.248 1.00 34.46  ?  95  ASN   B HA     1 
ATOM   7437  H  HB2    . ASN   B 1 70  ? 34.054  -29.238 20.646 1.00 35.81  ?  95  ASN   B HB2    1 
ATOM   7438  H  HB3    . ASN   B 1 70  ? 35.230  -29.977 21.419 1.00 35.81  ?  95  ASN   B HB3    1 
ATOM   7439  H  HD21   . ASN   B 1 70  ? 36.186  -31.741 18.761 1.00 40.03  ?  95  ASN   B HD21   1 
ATOM   7440  H  HD22   . ASN   B 1 70  ? 36.596  -31.045 20.012 1.00 40.03  ?  95  ASN   B HD22   1 
ATOM   7441  N  N      . LYS   B 1 71  ? 34.307  -31.645 23.936 1.00 31.33  ?  96  LYS   B N      1 
ATOM   7442  C  CA     . LYS   B 1 71  ? 34.897  -32.685 24.773 1.00 31.43  ?  96  LYS   B CA     1 
ATOM   7443  C  C      . LYS   B 1 71  ? 33.907  -33.820 25.016 1.00 31.24  ?  96  LYS   B C      1 
ATOM   7444  O  O      . LYS   B 1 71  ? 34.325  -34.968 25.188 1.00 32.77  ?  96  LYS   B O      1 
ATOM   7445  C  CB     . LYS   B 1 71  ? 35.380  -32.088 26.098 1.00 31.51  ?  96  LYS   B CB     1 
ATOM   7446  C  CG     . LYS   B 1 71  ? 35.922  -33.115 27.087 1.00 31.55  ?  96  LYS   B CG     1 
ATOM   7447  C  CD     . LYS   B 1 71  ? 37.208  -33.784 26.610 1.00 33.40  ?  96  LYS   B CD     1 
ATOM   7448  C  CE     . LYS   B 1 71  ? 37.763  -34.661 27.712 1.00 35.43  ?  96  LYS   B CE     1 
ATOM   7449  N  NZ     . LYS   B 1 71  ? 39.153  -35.128 27.449 1.00 37.33  ?  96  LYS   B NZ     1 
ATOM   7450  H  H      . LYS   B 1 71  ? 34.137  -30.907 24.345 1.00 37.59  ?  96  LYS   B H      1 
ATOM   7451  H  HA     . LYS   B 1 71  ? 35.673  -33.055 24.324 1.00 37.71  ?  96  LYS   B HA     1 
ATOM   7452  H  HB2    . LYS   B 1 71  ? 36.091  -31.455 25.912 1.00 37.80  ?  96  LYS   B HB2    1 
ATOM   7453  H  HB3    . LYS   B 1 71  ? 34.636  -31.634 26.524 1.00 37.80  ?  96  LYS   B HB3    1 
ATOM   7454  H  HG2    . LYS   B 1 71  ? 36.110  -32.673 27.929 1.00 37.85  ?  96  LYS   B HG2    1 
ATOM   7455  H  HG3    . LYS   B 1 71  ? 35.256  -33.809 27.218 1.00 37.85  ?  96  LYS   B HG3    1 
ATOM   7456  H  HD2    . LYS   B 1 71  ? 37.023  -34.336 25.834 1.00 40.07  ?  96  LYS   B HD2    1 
ATOM   7457  H  HD3    . LYS   B 1 71  ? 37.867  -33.108 26.387 1.00 40.07  ?  96  LYS   B HD3    1 
ATOM   7458  H  HE2    . LYS   B 1 71  ? 37.771  -34.157 28.541 1.00 42.51  ?  96  LYS   B HE2    1 
ATOM   7459  H  HE3    . LYS   B 1 71  ? 37.199  -35.444 27.805 1.00 42.51  ?  96  LYS   B HE3    1 
ATOM   7460  H  HZ1    . LYS   B 1 71  ? 39.437  -35.633 28.125 1.00 44.79  ?  96  LYS   B HZ1    1 
ATOM   7461  H  HZ2    . LYS   B 1 71  ? 39.176  -35.608 26.700 1.00 44.79  ?  96  LYS   B HZ2    1 
ATOM   7462  H  HZ3    . LYS   B 1 71  ? 39.697  -34.429 27.362 1.00 44.79  ?  96  LYS   B HZ3    1 
ATOM   7463  N  N      . GLN   B 1 72  ? 32.599  -33.524 25.035 1.00 29.58  ?  97  GLN   B N      1 
ATOM   7464  C  CA     . GLN   B 1 72  ? 31.602  -34.592 25.096 1.00 29.15  ?  97  GLN   B CA     1 
ATOM   7465  C  C      . GLN   B 1 72  ? 31.506  -35.314 23.755 1.00 30.58  ?  97  GLN   B C      1 
ATOM   7466  O  O      . GLN   B 1 72  ? 31.429  -36.549 23.703 1.00 33.10  ?  97  GLN   B O      1 
ATOM   7467  C  CB     . GLN   B 1 72  ? 30.242  -34.019 25.506 1.00 28.82  ?  97  GLN   B CB     1 
ATOM   7468  C  CG     . GLN   B 1 72  ? 30.272  -33.228 26.813 1.00 29.13  ?  97  GLN   B CG     1 
ATOM   7469  C  CD     . GLN   B 1 72  ? 30.758  -34.048 28.008 1.00 31.24  ?  97  GLN   B CD     1 
ATOM   7470  O  OE1    . GLN   B 1 72  ? 30.423  -35.222 28.153 1.00 30.25  ?  97  GLN   B OE1    1 
ATOM   7471  N  NE2    . GLN   B 1 72  ? 31.555  -33.422 28.868 1.00 33.63  ?  97  GLN   B NE2    1 
ATOM   7472  H  H      . GLN   B 1 72  ? 32.273  -32.728 25.013 1.00 35.49  ?  97  GLN   B H      1 
ATOM   7473  H  HA     . GLN   B 1 72  ? 31.864  -35.236 25.772 1.00 34.97  ?  97  GLN   B HA     1 
ATOM   7474  H  HB2    . GLN   B 1 72  ? 29.933  -33.422 24.806 1.00 34.58  ?  97  GLN   B HB2    1 
ATOM   7475  H  HB3    . GLN   B 1 72  ? 29.616  -34.751 25.617 1.00 34.58  ?  97  GLN   B HB3    1 
ATOM   7476  H  HG2    . GLN   B 1 72  ? 30.871  -32.472 26.709 1.00 34.95  ?  97  GLN   B HG2    1 
ATOM   7477  H  HG3    . GLN   B 1 72  ? 29.376  -32.916 27.012 1.00 34.95  ?  97  GLN   B HG3    1 
ATOM   7478  H  HE21   . GLN   B 1 72  ? 31.770  -32.600 28.735 1.00 40.35  ?  97  GLN   B HE21   1 
ATOM   7479  H  HE22   . GLN   B 1 72  ? 31.856  -33.839 29.557 1.00 40.35  ?  97  GLN   B HE22   1 
ATOM   7480  N  N      . ARG   B 1 73  ? 31.556  -34.560 22.657 1.00 30.70  ?  98  ARG   B N      1 
ATOM   7481  C  CA     . ARG   B 1 73  ? 31.548  -35.170 21.332 1.00 32.47  ?  98  ARG   B CA     1 
ATOM   7482  C  C      . ARG   B 1 73  ? 32.762  -36.067 21.112 1.00 34.09  ?  98  ARG   B C      1 
ATOM   7483  O  O      . ARG   B 1 73  ? 32.630  -37.169 20.560 1.00 35.30  ?  98  ARG   B O      1 
ATOM   7484  C  CB     . ARG   B 1 73  ? 31.487  -34.070 20.272 1.00 31.91  ?  98  ARG   B CB     1 
ATOM   7485  C  CG     . ARG   B 1 73  ? 31.621  -34.562 18.835 1.00 33.26  ?  98  ARG   B CG     1 
ATOM   7486  C  CD     . ARG   B 1 73  ? 31.240  -33.452 17.862 1.00 33.80  ?  98  ARG   B CD     1 
ATOM   7487  N  NE     . ARG   B 1 73  ? 31.528  -33.806 16.479 1.00 34.71  ?  98  ARG   B NE     1 
ATOM   7488  C  CZ     . ARG   B 1 73  ? 32.603  -33.404 15.806 1.00 35.62  ?  98  ARG   B CZ     1 
ATOM   7489  N  NH1    . ARG   B 1 73  ? 33.506  -32.620 16.382 1.00 36.32  ?  98  ARG   B NH1    1 
ATOM   7490  N  NH2    . ARG   B 1 73  ? 32.763  -33.791 14.549 1.00 36.52  ?  98  ARG   B NH2    1 
ATOM   7491  H  H      . ARG   B 1 73  ? 31.594  -33.701 22.652 1.00 36.83  ?  98  ARG   B H      1 
ATOM   7492  H  HA     . ARG   B 1 73  ? 30.761  -35.730 21.246 1.00 38.96  ?  98  ARG   B HA     1 
ATOM   7493  H  HB2    . ARG   B 1 73  ? 30.632  -33.617 20.347 1.00 38.29  ?  98  ARG   B HB2    1 
ATOM   7494  H  HB3    . ARG   B 1 73  ? 32.210  -33.444 20.435 1.00 38.29  ?  98  ARG   B HB3    1 
ATOM   7495  H  HG2    . ARG   B 1 73  ? 32.540  -34.824 18.664 1.00 39.91  ?  98  ARG   B HG2    1 
ATOM   7496  H  HG3    . ARG   B 1 73  ? 31.029  -35.317 18.692 1.00 39.91  ?  98  ARG   B HG3    1 
ATOM   7497  H  HD2    . ARG   B 1 73  ? 30.289  -33.276 17.937 1.00 40.55  ?  98  ARG   B HD2    1 
ATOM   7498  H  HD3    . ARG   B 1 73  ? 31.744  -32.652 18.079 1.00 40.55  ?  98  ARG   B HD3    1 
ATOM   7499  H  HE     . ARG   B 1 73  ? 30.964  -34.309 16.069 1.00 41.65  ?  98  ARG   B HE     1 
ATOM   7500  H  HH11   . ARG   B 1 73  ? 33.399  -32.367 17.197 1.00 43.58  ?  98  ARG   B HH11   1 
ATOM   7501  H  HH12   . ARG   B 1 73  ? 34.199  -32.365 15.941 1.00 43.58  ?  98  ARG   B HH12   1 
ATOM   7502  H  HH21   . ARG   B 1 73  ? 32.175  -34.297 14.177 1.00 43.81  ?  98  ARG   B HH21   1 
ATOM   7503  H  HH22   . ARG   B 1 73  ? 33.455  -33.537 14.106 1.00 43.81  ?  98  ARG   B HH22   1 
ATOM   7504  N  N      . ASP   B 1 74  ? 33.947  -35.612 21.518 1.00 33.81  ?  99  ASP   B N      1 
ATOM   7505  C  CA     . ASP   B 1 74  ? 35.188  -36.367 21.342 1.00 35.58  ?  99  ASP   B CA     1 
ATOM   7506  C  C      . ASP   B 1 74  ? 35.988  -36.360 22.638 1.00 36.32  ?  99  ASP   B C      1 
ATOM   7507  O  O      . ASP   B 1 74  ? 36.752  -35.410 22.894 1.00 35.29  ?  99  ASP   B O      1 
ATOM   7508  C  CB     . ASP   B 1 74  ? 36.046  -35.797 20.217 1.00 37.37  ?  99  ASP   B CB     1 
ATOM   7509  C  CG     . ASP   B 1 74  ? 37.349  -36.554 20.044 1.00 39.93  ?  99  ASP   B CG     1 
ATOM   7510  O  OD1    . ASP   B 1 74  ? 37.500  -37.611 20.695 1.00 40.61  ?  99  ASP   B OD1    1 
ATOM   7511  O  OD2    . ASP   B 1 74  ? 38.214  -36.100 19.262 1.00 42.01  ?  99  ASP   B OD2    1 
ATOM   7512  H  H      . ASP   B 1 74  ? 34.061  -34.853 21.906 1.00 40.57  ?  99  ASP   B H      1 
ATOM   7513  H  HA     . ASP   B 1 74  ? 34.947  -37.282 21.127 1.00 42.69  ?  99  ASP   B HA     1 
ATOM   7514  H  HB2    . ASP   B 1 74  ? 35.552  -35.851 19.383 1.00 44.84  ?  99  ASP   B HB2    1 
ATOM   7515  H  HB3    . ASP   B 1 74  ? 36.258  -34.872 20.417 1.00 44.84  ?  99  ASP   B HB3    1 
ATOM   7516  N  N      . PRO   B 1 75  ? 35.861  -37.397 23.469 1.00 39.08  ?  100 PRO   B N      1 
ATOM   7517  C  CA     . PRO   B 1 75  ? 36.589  -37.403 24.749 1.00 40.17  ?  100 PRO   B CA     1 
ATOM   7518  C  C      . PRO   B 1 75  ? 38.100  -37.387 24.606 1.00 39.84  ?  100 PRO   B C      1 
ATOM   7519  O  O      . PRO   B 1 75  ? 38.787  -37.163 25.610 1.00 39.43  ?  100 PRO   B O      1 
ATOM   7520  C  CB     . PRO   B 1 75  ? 36.106  -38.698 25.423 1.00 41.61  ?  100 PRO   B CB     1 
ATOM   7521  C  CG     . PRO   B 1 75  ? 34.747  -38.926 24.838 1.00 41.62  ?  100 PRO   B CG     1 
ATOM   7522  C  CD     . PRO   B 1 75  ? 34.868  -38.486 23.395 1.00 40.90  ?  100 PRO   B CD     1 
ATOM   7523  H  HA     . PRO   B 1 75  ? 36.317  -36.641 25.284 1.00 48.20  ?  100 PRO   B HA     1 
ATOM   7524  H  HB2    . PRO   B 1 75  ? 36.707  -39.429 25.211 1.00 49.92  ?  100 PRO   B HB2    1 
ATOM   7525  H  HB3    . PRO   B 1 75  ? 36.058  -38.576 26.384 1.00 49.92  ?  100 PRO   B HB3    1 
ATOM   7526  H  HG2    . PRO   B 1 75  ? 34.515  -39.866 24.896 1.00 49.94  ?  100 PRO   B HG2    1 
ATOM   7527  H  HG3    . PRO   B 1 75  ? 34.089  -38.393 25.311 1.00 49.94  ?  100 PRO   B HG3    1 
ATOM   7528  H  HD2    . PRO   B 1 75  ? 35.188  -39.211 22.836 1.00 49.07  ?  100 PRO   B HD2    1 
ATOM   7529  H  HD3    . PRO   B 1 75  ? 34.018  -38.159 23.060 1.00 49.07  ?  100 PRO   B HD3    1 
ATOM   7530  N  N      . LYS   B 1 76  ? 38.642  -37.613 23.412 1.00 40.50  ?  101 LYS   B N      1 
ATOM   7531  C  CA     . LYS   B 1 76  ? 40.083  -37.516 23.218 1.00 41.64  ?  101 LYS   B CA     1 
ATOM   7532  C  C      . LYS   B 1 76  ? 40.567  -36.076 23.128 1.00 40.91  ?  101 LYS   B C      1 
ATOM   7533  O  O      . LYS   B 1 76  ? 41.774  -35.840 23.246 1.00 41.48  ?  101 LYS   B O      1 
ATOM   7534  C  CB     . LYS   B 1 76  ? 40.500  -38.284 21.962 1.00 45.59  ?  101 LYS   B CB     1 
ATOM   7535  C  CG     . LYS   B 1 76  ? 40.411  -39.793 22.114 1.00 48.56  ?  101 LYS   B CG     1 
ATOM   7536  C  CD     . LYS   B 1 76  ? 40.999  -40.514 20.909 1.00 51.35  ?  101 LYS   B CD     1 
ATOM   7537  C  CE     . LYS   B 1 76  ? 41.108  -42.015 21.165 1.00 54.13  ?  101 LYS   B CE     1 
ATOM   7538  N  NZ     . LYS   B 1 76  ? 39.993  -42.553 22.007 1.00 55.46  ?  101 LYS   B NZ     1 
ATOM   7539  H  H      . LYS   B 1 76  ? 38.199  -37.822 22.706 1.00 48.59  ?  101 LYS   B H      1 
ATOM   7540  H  HA     . LYS   B 1 76  ? 40.528  -37.931 23.973 1.00 49.97  ?  101 LYS   B HA     1 
ATOM   7541  H  HB2    . LYS   B 1 76  ? 39.918  -38.025 21.230 1.00 54.70  ?  101 LYS   B HB2    1 
ATOM   7542  H  HB3    . LYS   B 1 76  ? 41.419  -38.060 21.750 1.00 54.70  ?  101 LYS   B HB3    1 
ATOM   7543  H  HG2    . LYS   B 1 76  ? 40.906  -40.066 22.902 1.00 58.27  ?  101 LYS   B HG2    1 
ATOM   7544  H  HG3    . LYS   B 1 76  ? 39.481  -40.053 22.200 1.00 58.27  ?  101 LYS   B HG3    1 
ATOM   7545  H  HD2    . LYS   B 1 76  ? 40.426  -40.376 20.139 1.00 61.62  ?  101 LYS   B HD2    1 
ATOM   7546  H  HD3    . LYS   B 1 76  ? 41.887  -40.169 20.728 1.00 61.62  ?  101 LYS   B HD3    1 
ATOM   7547  H  HE2    . LYS   B 1 76  ? 41.091  -42.481 20.315 1.00 64.95  ?  101 LYS   B HE2    1 
ATOM   7548  H  HE3    . LYS   B 1 76  ? 41.942  -42.195 21.626 1.00 64.95  ?  101 LYS   B HE3    1 
ATOM   7549  H  HZ1    . LYS   B 1 76  ? 40.052  -42.229 22.834 1.00 66.55  ?  101 LYS   B HZ1    1 
ATOM   7550  H  HZ2    . LYS   B 1 76  ? 39.208  -42.317 21.659 1.00 66.55  ?  101 LYS   B HZ2    1 
ATOM   7551  H  HZ3    . LYS   B 1 76  ? 40.038  -43.441 22.040 1.00 66.55  ?  101 LYS   B HZ3    1 
ATOM   7552  N  N      . MET   B 1 77  ? 39.663  -35.118 22.920 1.00 39.39  ?  102 MET   B N      1 
ATOM   7553  C  CA     . MET   B 1 77  ? 40.021  -33.708 22.992 1.00 37.83  ?  102 MET   B CA     1 
ATOM   7554  C  C      . MET   B 1 77  ? 40.765  -33.427 24.291 1.00 39.76  ?  102 MET   B C      1 
ATOM   7555  O  O      . MET   B 1 77  ? 40.443  -34.003 25.334 1.00 40.83  ?  102 MET   B O      1 
ATOM   7556  C  CB     . MET   B 1 77  ? 38.760  -32.848 22.906 1.00 36.84  ?  102 MET   B CB     1 
ATOM   7557  C  CG     . MET   B 1 77  ? 39.011  -31.372 23.117 1.00 36.36  ?  102 MET   B CG     1 
ATOM   7558  S  SD     . MET   B 1 77  ? 37.460  -30.442 23.065 1.00 36.99  ?  102 MET   B SD     1 
ATOM   7559  C  CE     . MET   B 1 77  ? 37.909  -28.991 24.018 1.00 37.21  ?  102 MET   B CE     1 
ATOM   7560  H  H      . MET   B 1 77  ? 38.835  -35.261 22.736 1.00 47.26  ?  102 MET   B H      1 
ATOM   7561  H  HA     . MET   B 1 77  ? 40.590  -33.476 22.242 1.00 45.39  ?  102 MET   B HA     1 
ATOM   7562  H  HB2    . MET   B 1 77  ? 38.368  -32.958 22.026 1.00 44.20  ?  102 MET   B HB2    1 
ATOM   7563  H  HB3    . MET   B 1 77  ? 38.136  -33.142 23.587 1.00 44.20  ?  102 MET   B HB3    1 
ATOM   7564  H  HG2    . MET   B 1 77  ? 39.423  -31.235 23.984 1.00 43.62  ?  102 MET   B HG2    1 
ATOM   7565  H  HG3    . MET   B 1 77  ? 39.593  -31.040 22.416 1.00 43.62  ?  102 MET   B HG3    1 
ATOM   7566  H  HE1    . MET   B 1 77  ? 37.179  -28.354 23.987 1.00 44.65  ?  102 MET   B HE1    1 
ATOM   7567  H  HE2    . MET   B 1 77  ? 38.078  -29.255 24.936 1.00 44.65  ?  102 MET   B HE2    1 
ATOM   7568  H  HE3    . MET   B 1 77  ? 38.709  -28.596 23.635 1.00 44.65  ?  102 MET   B HE3    1 
ATOM   7569  N  N      . SER   B 1 78  ? 41.754  -32.525 24.228 1.00 40.20  ?  103 SER   B N      1 
ATOM   7570  C  CA     . SER   B 1 78  ? 42.614  -32.270 25.377 1.00 39.87  ?  103 SER   B CA     1 
ATOM   7571  C  C      . SER   B 1 78  ? 42.824  -30.804 25.758 1.00 39.81  ?  103 SER   B C      1 
ATOM   7572  O  O      . SER   B 1 78  ? 43.207  -30.556 26.910 1.00 40.04  ?  103 SER   B O      1 
ATOM   7573  C  CB     . SER   B 1 78  ? 44.002  -32.899 25.144 1.00 40.72  ?  103 SER   B CB     1 
ATOM   7574  O  OG     . SER   B 1 78  ? 44.592  -32.382 23.960 1.00 42.01  ?  103 SER   B OG     1 
ATOM   7575  H  H      . SER   B 1 78  ? 41.940  -32.054 23.532 1.00 48.23  ?  103 SER   B H      1 
ATOM   7576  H  HA     . SER   B 1 78  ? 42.193  -32.691 26.143 1.00 47.84  ?  103 SER   B HA     1 
ATOM   7577  H  HB2    . SER   B 1 78  ? 44.575  -32.692 25.899 1.00 48.85  ?  103 SER   B HB2    1 
ATOM   7578  H  HB3    . SER   B 1 78  ? 43.904  -33.860 25.056 1.00 48.85  ?  103 SER   B HB3    1 
ATOM   7579  H  HG     . SER   B 1 78  ? 45.345  -32.733 23.837 1.00 50.41  ?  103 SER   B HG     1 
ATOM   7580  N  N      . CYS   B 1 79  ? 42.598  -29.837 24.862 1.00 39.28  ?  104 CYS   B N      1 
ATOM   7581  C  CA     . CYS   B 1 79  ? 42.963  -28.461 25.168 1.00 40.25  ?  104 CYS   B CA     1 
ATOM   7582  C  C      . CYS   B 1 79  ? 41.986  -27.467 24.557 1.00 36.68  ?  104 CYS   B C      1 
ATOM   7583  O  O      . CYS   B 1 79  ? 41.463  -27.679 23.459 1.00 35.59  ?  104 CYS   B O      1 
ATOM   7584  C  CB     . CYS   B 1 79  ? 44.358  -28.080 24.648 1.00 43.83  ?  104 CYS   B CB     1 
ATOM   7585  S  SG     . CYS   B 1 79  ? 45.716  -29.056 25.284 1.00 48.70  ?  104 CYS   B SG     1 
ATOM   7586  H  H      . CYS   B 1 79  ? 42.241  -29.956 24.089 1.00 47.13  ?  104 CYS   B H      1 
ATOM   7587  H  HA     . CYS   B 1 79  ? 42.928  -28.395 26.135 1.00 48.30  ?  104 CYS   B HA     1 
ATOM   7588  H  HB2    . CYS   B 1 79  ? 44.360  -28.178 23.683 1.00 52.59  ?  104 CYS   B HB2    1 
ATOM   7589  H  HB3    . CYS   B 1 79  ? 44.530  -27.156 24.887 1.00 52.59  ?  104 CYS   B HB3    1 
ATOM   7590  H  HG     . CYS   B 1 79  ? 46.740  -28.671 24.790 1.00 58.43  ?  104 CYS   B HG     1 
ATOM   7591  N  N      . ILE   B 1 80  ? 41.792  -26.355 25.264 1.00 34.60  ?  105 ILE   B N      1 
ATOM   7592  C  CA     . ILE   B 1 80  ? 41.150  -25.161 24.729 1.00 34.12  ?  105 ILE   B CA     1 
ATOM   7593  C  C      . ILE   B 1 80  ? 42.123  -24.000 24.891 1.00 35.13  ?  105 ILE   B C      1 
ATOM   7594  O  O      . ILE   B 1 80  ? 42.674  -23.797 25.980 1.00 36.58  ?  105 ILE   B O      1 
ATOM   7595  C  CB     . ILE   B 1 80  ? 39.833  -24.837 25.453 1.00 31.88  ?  105 ILE   B CB     1 
ATOM   7596  C  CG1    . ILE   B 1 80  ? 38.793  -25.939 25.263 1.00 31.17  ?  105 ILE   B CG1    1 
ATOM   7597  C  CG2    . ILE   B 1 80  ? 39.280  -23.503 24.954 1.00 32.16  ?  105 ILE   B CG2    1 
ATOM   7598  C  CD1    . ILE   B 1 80  ? 37.584  -25.792 26.184 1.00 30.78  ?  105 ILE   B CD1    1 
ATOM   7599  H  H      . ILE   B 1 80  ? 42.033  -26.268 26.085 1.00 41.52  ?  105 ILE   B H      1 
ATOM   7600  H  HA     . ILE   B 1 80  ? 40.959  -25.300 23.789 1.00 40.94  ?  105 ILE   B HA     1 
ATOM   7601  H  HB     . ILE   B 1 80  ? 40.027  -24.777 26.402 1.00 38.25  ?  105 ILE   B HB     1 
ATOM   7602  H  HG12   . ILE   B 1 80  ? 38.475  -25.916 24.347 1.00 37.39  ?  105 ILE   B HG12   1 
ATOM   7603  H  HG13   . ILE   B 1 80  ? 39.207  -26.796 25.450 1.00 37.39  ?  105 ILE   B HG13   1 
ATOM   7604  H  HG21   . ILE   B 1 80  ? 38.358  -23.416 25.242 1.00 38.58  ?  105 ILE   B HG21   1 
ATOM   7605  H  HG22   . ILE   B 1 80  ? 39.812  -22.782 25.324 1.00 38.58  ?  105 ILE   B HG22   1 
ATOM   7606  H  HG23   . ILE   B 1 80  ? 39.327  -23.485 23.985 1.00 38.58  ?  105 ILE   B HG23   1 
ATOM   7607  H  HD11   . ILE   B 1 80  ? 37.085  -26.624 26.185 1.00 36.93  ?  105 ILE   B HD11   1 
ATOM   7608  H  HD12   . ILE   B 1 80  ? 37.893  -25.590 27.081 1.00 36.93  ?  105 ILE   B HD12   1 
ATOM   7609  H  HD13   . ILE   B 1 80  ? 37.024  -25.071 25.857 1.00 36.93  ?  105 ILE   B HD13   1 
ATOM   7610  N  N      . ARG   B 1 81  ? 42.315  -23.225 23.823 1.00 34.43  ?  106 ARG   B N      1 
ATOM   7611  C  CA     . ARG   B 1 81  ? 43.204  -22.067 23.845 1.00 35.26  ?  106 ARG   B CA     1 
ATOM   7612  C  C      . ARG   B 1 81  ? 42.423  -20.821 23.452 1.00 36.04  ?  106 ARG   B C      1 
ATOM   7613  O  O      . ARG   B 1 81  ? 41.885  -20.745 22.341 1.00 36.34  ?  106 ARG   B O      1 
ATOM   7614  C  CB     . ARG   B 1 81  ? 44.394  -22.273 22.905 1.00 37.78  ?  106 ARG   B CB     1 
ATOM   7615  C  CG     . ARG   B 1 81  ? 45.226  -23.502 23.221 1.00 39.05  ?  106 ARG   B CG     1 
ATOM   7616  C  CD     . ARG   B 1 81  ? 46.439  -23.639 22.275 1.00 41.15  ?  106 ARG   B CD     1 
ATOM   7617  N  NE     . ARG   B 1 81  ? 47.440  -22.605 22.532 1.00 44.04  ?  106 ARG   B NE     1 
ATOM   7618  C  CZ     . ARG   B 1 81  ? 48.441  -22.726 23.403 1.00 45.67  ?  106 ARG   B CZ     1 
ATOM   7619  N  NH1    . ARG   B 1 81  ? 48.595  -23.842 24.104 1.00 46.17  ?  106 ARG   B NH1    1 
ATOM   7620  N  NH2    . ARG   B 1 81  ? 49.288  -21.724 23.578 1.00 46.74  ?  106 ARG   B NH2    1 
ATOM   7621  H  H      . ARG   B 1 81  ? 41.935  -23.354 23.063 1.00 41.31  ?  106 ARG   B H      1 
ATOM   7622  H  HA     . ARG   B 1 81  ? 43.537  -21.939 24.747 1.00 42.31  ?  106 ARG   B HA     1 
ATOM   7623  H  HB2    . ARG   B 1 81  ? 44.061  -22.367 21.998 1.00 45.33  ?  106 ARG   B HB2    1 
ATOM   7624  H  HB3    . ARG   B 1 81  ? 44.976  -21.499 22.965 1.00 45.33  ?  106 ARG   B HB3    1 
ATOM   7625  H  HG2    . ARG   B 1 81  ? 45.557  -23.438 24.130 1.00 46.85  ?  106 ARG   B HG2    1 
ATOM   7626  H  HG3    . ARG   B 1 81  ? 44.675  -24.294 23.123 1.00 46.85  ?  106 ARG   B HG3    1 
ATOM   7627  H  HD2    . ARG   B 1 81  ? 46.853  -24.505 22.409 1.00 49.38  ?  106 ARG   B HD2    1 
ATOM   7628  H  HD3    . ARG   B 1 81  ? 46.140  -23.552 21.356 1.00 49.38  ?  106 ARG   B HD3    1 
ATOM   7629  H  HE     . ARG   B 1 81  ? 47.379  -21.870 22.091 1.00 52.84  ?  106 ARG   B HE     1 
ATOM   7630  H  HH11   . ARG   B 1 81  ? 48.046  -24.495 23.999 1.00 55.39  ?  106 ARG   B HH11   1 
ATOM   7631  H  HH12   . ARG   B 1 81  ? 49.244  -23.911 24.664 1.00 55.39  ?  106 ARG   B HH12   1 
ATOM   7632  H  HH21   . ARG   B 1 81  ? 49.191  -20.996 23.129 1.00 56.08  ?  106 ARG   B HH21   1 
ATOM   7633  H  HH22   . ARG   B 1 81  ? 49.934  -21.800 24.139 1.00 56.08  ?  106 ARG   B HH22   1 
ATOM   7634  N  N      . VAL   B 1 82  ? 42.369  -19.846 24.359 1.00 33.63  ?  107 VAL   B N      1 
ATOM   7635  C  CA     . VAL   B 1 82  ? 41.665  -18.587 24.147 1.00 33.62  ?  107 VAL   B CA     1 
ATOM   7636  C  C      . VAL   B 1 82  ? 42.688  -17.473 23.982 1.00 34.42  ?  107 VAL   B C      1 
ATOM   7637  O  O      . VAL   B 1 82  ? 43.666  -17.403 24.735 1.00 35.63  ?  107 VAL   B O      1 
ATOM   7638  C  CB     . VAL   B 1 82  ? 40.718  -18.288 25.328 1.00 32.11  ?  107 VAL   B CB     1 
ATOM   7639  C  CG1    . VAL   B 1 82  ? 40.004  -16.956 25.134 1.00 31.68  ?  107 VAL   B CG1    1 
ATOM   7640  C  CG2    . VAL   B 1 82  ? 39.702  -19.425 25.525 1.00 32.01  ?  107 VAL   B CG2    1 
ATOM   7641  H  H      . VAL   B 1 82  ? 42.747  -19.896 25.130 1.00 40.35  ?  107 VAL   B H      1 
ATOM   7642  H  HA     . VAL   B 1 82  ? 41.144  -18.641 23.331 1.00 40.33  ?  107 VAL   B HA     1 
ATOM   7643  H  HB     . VAL   B 1 82  ? 41.253  -18.225 26.135 1.00 38.52  ?  107 VAL   B HB     1 
ATOM   7644  H  HG11   . VAL   B 1 82  ? 39.292  -16.881 25.787 1.00 38.01  ?  107 VAL   B HG11   1 
ATOM   7645  H  HG12   . VAL   B 1 82  ? 40.642  -16.236 25.256 1.00 38.01  ?  107 VAL   B HG12   1 
ATOM   7646  H  HG13   . VAL   B 1 82  ? 39.636  -16.923 24.237 1.00 38.01  ?  107 VAL   B HG13   1 
ATOM   7647  H  HG21   . VAL   B 1 82  ? 39.093  -19.184 26.241 1.00 38.41  ?  107 VAL   B HG21   1 
ATOM   7648  H  HG22   . VAL   B 1 82  ? 39.208  -19.553 24.700 1.00 38.41  ?  107 VAL   B HG22   1 
ATOM   7649  H  HG23   . VAL   B 1 82  ? 40.178  -20.238 25.754 1.00 38.41  ?  107 VAL   B HG23   1 
ATOM   7650  N  N      . THR   B 1 83  ? 42.467  -16.596 23.008 1.00 34.82  ?  108 THR   B N      1 
ATOM   7651  C  CA     . THR   B 1 83  ? 43.267  -15.384 22.868 1.00 35.72  ?  108 THR   B CA     1 
ATOM   7652  C  C      . THR   B 1 83  ? 42.353  -14.163 22.897 1.00 35.91  ?  108 THR   B C      1 
ATOM   7653  O  O      . THR   B 1 83  ? 41.251  -14.181 22.337 1.00 36.19  ?  108 THR   B O      1 
ATOM   7654  C  CB     . THR   B 1 83  ? 44.116  -15.385 21.581 1.00 39.29  ?  108 THR   B CB     1 
ATOM   7655  O  OG1    . THR   B 1 83  ? 43.285  -15.225 20.426 1.00 41.24  ?  108 THR   B OG1    1 
ATOM   7656  C  CG2    . THR   B 1 83  ? 44.928  -16.682 21.467 1.00 39.05  ?  108 THR   B CG2    1 
ATOM   7657  H  H      . THR   B 1 83  ? 41.853  -16.681 22.411 1.00 41.77  ?  108 THR   B H      1 
ATOM   7658  H  HA     . THR   B 1 83  ? 43.884  -15.327 23.615 1.00 42.86  ?  108 THR   B HA     1 
ATOM   7659  H  HB     . THR   B 1 83  ? 44.737  -14.640 21.615 1.00 47.14  ?  108 THR   B HB     1 
ATOM   7660  H  HG1    . THR   B 1 83  ? 43.750  -15.273 19.729 1.00 49.48  ?  108 THR   B HG1    1 
ATOM   7661  H  HG21   . THR   B 1 83  ? 45.439  -16.682 20.642 1.00 46.85  ?  108 THR   B HG21   1 
ATOM   7662  H  HG22   . THR   B 1 83  ? 45.539  -16.758 22.216 1.00 46.85  ?  108 THR   B HG22   1 
ATOM   7663  H  HG23   . THR   B 1 83  ? 44.332  -17.448 21.467 1.00 46.85  ?  108 THR   B HG23   1 
ATOM   7664  N  N      . ILE   B 1 84  ? 42.810  -13.117 23.580 1.00 37.05  ?  109 ILE   B N      1 
ATOM   7665  C  CA     . ILE   B 1 84  ? 42.096  -11.850 23.689 1.00 37.09  ?  109 ILE   B CA     1 
ATOM   7666  C  C      . ILE   B 1 84  ? 43.083  -10.734 23.374 1.00 39.72  ?  109 ILE   B C      1 
ATOM   7667  O  O      . ILE   B 1 84  ? 44.073  -10.567 24.094 1.00 40.04  ?  109 ILE   B O      1 
ATOM   7668  C  CB     . ILE   B 1 84  ? 41.486  -11.652 25.090 1.00 35.68  ?  109 ILE   B CB     1 
ATOM   7669  C  CG1    . ILE   B 1 84  ? 40.520  -12.797 25.413 1.00 34.77  ?  109 ILE   B CG1    1 
ATOM   7670  C  CG2    . ILE   B 1 84  ? 40.815  -10.285 25.183 1.00 36.57  ?  109 ILE   B CG2    1 
ATOM   7671  C  CD1    . ILE   B 1 84  ? 39.960  -12.744 26.830 1.00 35.29  ?  109 ILE   B CD1    1 
ATOM   7672  H  H      . ILE   B 1 84  ? 43.558  -13.118 24.005 1.00 44.45  ?  109 ILE   B H      1 
ATOM   7673  H  HA     . ILE   B 1 84  ? 41.380  -11.823 23.035 1.00 44.51  ?  109 ILE   B HA     1 
ATOM   7674  H  HB     . ILE   B 1 84  ? 42.193  -11.676 25.754 1.00 42.81  ?  109 ILE   B HB     1 
ATOM   7675  H  HG12   . ILE   B 1 84  ? 39.772  -12.757 24.797 1.00 41.72  ?  109 ILE   B HG12   1 
ATOM   7676  H  HG13   . ILE   B 1 84  ? 40.989  -13.639 25.311 1.00 41.72  ?  109 ILE   B HG13   1 
ATOM   7677  H  HG21   . ILE   B 1 84  ? 40.328  -10.229 26.020 1.00 43.88  ?  109 ILE   B HG21   1 
ATOM   7678  H  HG22   . ILE   B 1 84  ? 41.497  -9.596  25.151 1.00 43.88  ?  109 ILE   B HG22   1 
ATOM   7679  H  HG23   . ILE   B 1 84  ? 40.204  -10.181 24.437 1.00 43.88  ?  109 ILE   B HG23   1 
ATOM   7680  H  HD11   . ILE   B 1 84  ? 39.524  -13.588 27.029 1.00 42.34  ?  109 ILE   B HD11   1 
ATOM   7681  H  HD12   . ILE   B 1 84  ? 40.688  -12.593 27.453 1.00 42.34  ?  109 ILE   B HD12   1 
ATOM   7682  H  HD13   . ILE   B 1 84  ? 39.318  -12.019 26.890 1.00 42.34  ?  109 ILE   B HD13   1 
ATOM   7683  N  N      . ASP   B 1 85  ? 42.802  -9.965  22.316 1.00 41.02  ?  110 ASP   B N      1 
ATOM   7684  C  CA     . ASP   B 1 85  ? 43.663  -8.882  21.834 1.00 43.17  ?  110 ASP   B CA     1 
ATOM   7685  C  C      . ASP   B 1 85  ? 42.860  -7.589  21.810 1.00 43.48  ?  110 ASP   B C      1 
ATOM   7686  O  O      . ASP   B 1 85  ? 42.226  -7.256  20.795 1.00 43.90  ?  110 ASP   B O      1 
ATOM   7687  C  CB     . ASP   B 1 85  ? 44.210  -9.212  20.446 1.00 45.61  ?  110 ASP   B CB     1 
ATOM   7688  C  CG     . ASP   B 1 85  ? 45.114  -8.129  19.893 1.00 49.03  ?  110 ASP   B CG     1 
ATOM   7689  O  OD1    . ASP   B 1 85  ? 45.310  -7.090  20.563 1.00 50.51  ?  110 ASP   B OD1    1 
ATOM   7690  O  OD2    . ASP   B 1 85  ? 45.633  -8.329  18.775 1.00 50.78  ?  110 ASP   B OD2    1 
ATOM   7691  H  H      . ASP   B 1 85  ? 42.089  -10.056 21.844 1.00 49.21  ?  110 ASP   B H      1 
ATOM   7692  H  HA     . ASP   B 1 85  ? 44.406  -8.763  22.447 1.00 51.80  ?  110 ASP   B HA     1 
ATOM   7693  H  HB2    . ASP   B 1 85  ? 44.724  -10.033 20.497 1.00 54.73  ?  110 ASP   B HB2    1 
ATOM   7694  H  HB3    . ASP   B 1 85  ? 43.467  -9.323  19.833 1.00 54.73  ?  110 ASP   B HB3    1 
ATOM   7695  N  N      . PRO   B 1 86  ? 42.860  -6.826  22.902 1.00 43.96  ?  111 PRO   B N      1 
ATOM   7696  C  CA     . PRO   B 1 86  ? 42.075  -5.577  22.906 1.00 45.70  ?  111 PRO   B CA     1 
ATOM   7697  C  C      . PRO   B 1 86  ? 42.491  -4.574  21.842 1.00 47.28  ?  111 PRO   B C      1 
ATOM   7698  O  O      . PRO   B 1 86  ? 41.624  -3.904  21.265 1.00 48.29  ?  111 PRO   B O      1 
ATOM   7699  C  CB     . PRO   B 1 86  ? 42.311  -5.024  24.322 1.00 44.92  ?  111 PRO   B CB     1 
ATOM   7700  C  CG     . PRO   B 1 86  ? 42.618  -6.237  25.149 1.00 44.16  ?  111 PRO   B CG     1 
ATOM   7701  C  CD     . PRO   B 1 86  ? 43.399  -7.156  24.236 1.00 43.70  ?  111 PRO   B CD     1 
ATOM   7702  H  HA     . PRO   B 1 86  ? 41.138  -5.794  22.785 1.00 54.83  ?  111 PRO   B HA     1 
ATOM   7703  H  HB2    . PRO   B 1 86  ? 43.058  -4.406  24.318 1.00 53.90  ?  111 PRO   B HB2    1 
ATOM   7704  H  HB3    . PRO   B 1 86  ? 41.511  -4.577  24.642 1.00 53.90  ?  111 PRO   B HB3    1 
ATOM   7705  H  HG2    . PRO   B 1 86  ? 43.149  -5.984  25.920 1.00 52.98  ?  111 PRO   B HG2    1 
ATOM   7706  H  HG3    . PRO   B 1 86  ? 41.792  -6.656  25.437 1.00 52.98  ?  111 PRO   B HG3    1 
ATOM   7707  H  HD2    . PRO   B 1 86  ? 44.349  -6.967  24.283 1.00 52.43  ?  111 PRO   B HD2    1 
ATOM   7708  H  HD3    . PRO   B 1 86  ? 43.235  -8.086  24.456 1.00 52.43  ?  111 PRO   B HD3    1 
ATOM   7709  N  N      . GLU   B 1 87  ? 43.792  -4.440  21.572 1.00 47.39  ?  112 GLU   B N      1 
ATOM   7710  C  CA     . GLU   B 1 87  ? 44.244  -3.407  20.643 1.00 51.12  ?  112 GLU   B CA     1 
ATOM   7711  C  C      . GLU   B 1 87  ? 43.617  -3.588  19.267 1.00 51.01  ?  112 GLU   B C      1 
ATOM   7712  O  O      . GLU   B 1 87  ? 43.171  -2.615  18.648 1.00 51.44  ?  112 GLU   B O      1 
ATOM   7713  C  CB     . GLU   B 1 87  ? 45.770  -3.418  20.547 1.00 54.44  ?  112 GLU   B CB     1 
ATOM   7714  C  CG     . GLU   B 1 87  ? 46.476  -3.081  21.858 1.00 59.13  ?  112 GLU   B CG     1 
ATOM   7715  C  CD     . GLU   B 1 87  ? 46.343  -1.614  22.250 1.00 63.95  ?  112 GLU   B CD     1 
ATOM   7716  O  OE1    . GLU   B 1 87  ? 46.424  -0.739  21.359 1.00 64.69  ?  112 GLU   B OE1    1 
ATOM   7717  O  OE2    . GLU   B 1 87  ? 46.157  -1.339  23.455 1.00 66.36  ?  112 GLU   B OE2    1 
ATOM   7718  H  H      . GLU   B 1 87  ? 44.419  -4.924  21.906 1.00 56.86  ?  112 GLU   B H      1 
ATOM   7719  H  HA     . GLU   B 1 87  ? 43.971  -2.541  20.983 1.00 61.34  ?  112 GLU   B HA     1 
ATOM   7720  H  HB2    . GLU   B 1 87  ? 46.058  -4.304  20.276 1.00 65.32  ?  112 GLU   B HB2    1 
ATOM   7721  H  HB3    . GLU   B 1 87  ? 46.044  -2.763  19.887 1.00 65.32  ?  112 GLU   B HB3    1 
ATOM   7722  H  HG2    . GLU   B 1 87  ? 46.091  -3.616  22.569 1.00 70.95  ?  112 GLU   B HG2    1 
ATOM   7723  H  HG3    . GLU   B 1 87  ? 47.421  -3.281  21.766 1.00 70.95  ?  112 GLU   B HG3    1 
ATOM   7724  N  N      . ASN   B 1 88  ? 43.571  -4.822  18.771 1.00 49.38  ?  113 ASN   B N      1 
ATOM   7725  C  CA     . ASN   B 1 88  ? 42.974  -5.085  17.472 1.00 49.08  ?  113 ASN   B CA     1 
ATOM   7726  C  C      . ASN   B 1 88  ? 41.538  -5.561  17.571 1.00 46.89  ?  113 ASN   B C      1 
ATOM   7727  O  O      . ASN   B 1 88  ? 40.953  -5.940  16.551 1.00 46.85  ?  113 ASN   B O      1 
ATOM   7728  C  CB     . ASN   B 1 88  ? 43.782  -6.118  16.698 1.00 50.79  ?  113 ASN   B CB     1 
ATOM   7729  C  CG     . ASN   B 1 88  ? 45.064  -5.559  16.178 1.00 52.82  ?  113 ASN   B CG     1 
ATOM   7730  O  OD1    . ASN   B 1 88  ? 46.139  -6.003  16.567 1.00 54.96  ?  113 ASN   B OD1    1 
ATOM   7731  N  ND2    . ASN   B 1 88  ? 44.969  -4.568  15.296 1.00 52.67  ?  113 ASN   B ND2    1 
ATOM   7732  H  H      . ASN   B 1 88  ? 43.879  -5.519  19.169 1.00 59.25  ?  113 ASN   B H      1 
ATOM   7733  H  HA     . ASN   B 1 88  ? 42.992  -4.253  16.973 1.00 58.89  ?  113 ASN   B HA     1 
ATOM   7734  H  HB2    . ASN   B 1 88  ? 43.993  -6.862  17.284 1.00 60.94  ?  113 ASN   B HB2    1 
ATOM   7735  H  HB3    . ASN   B 1 88  ? 43.260  -6.429  15.942 1.00 60.94  ?  113 ASN   B HB3    1 
ATOM   7736  H  HD21   . ASN   B 1 88  ? 45.681  -4.214  14.969 1.00 63.20  ?  113 ASN   B HD21   1 
ATOM   7737  H  HD22   . ASN   B 1 88  ? 44.195  -4.281  15.054 1.00 63.20  ?  113 ASN   B HD22   1 
ATOM   7738  N  N      . ASN   B 1 89  ? 40.963  -5.551  18.768 1.00 45.04  ?  114 ASN   B N      1 
ATOM   7739  C  CA     . ASN   B 1 89  ? 39.594  -5.992  18.991 1.00 43.00  ?  114 ASN   B CA     1 
ATOM   7740  C  C      . ASN   B 1 89  ? 39.361  -7.376  18.386 1.00 41.91  ?  114 ASN   B C      1 
ATOM   7741  O  O      . ASN   B 1 89  ? 38.504  -7.578  17.523 1.00 43.13  ?  114 ASN   B O      1 
ATOM   7742  C  CB     . ASN   B 1 89  ? 38.614  -4.981  18.410 1.00 42.81  ?  114 ASN   B CB     1 
ATOM   7743  C  CG     . ASN   B 1 89  ? 37.207  -5.276  18.805 1.00 42.05  ?  114 ASN   B CG     1 
ATOM   7744  O  OD1    . ASN   B 1 89  ? 36.950  -5.641  19.944 1.00 44.63  ?  114 ASN   B OD1    1 
ATOM   7745  N  ND2    . ASN   B 1 89  ? 36.286  -5.158  17.864 1.00 41.54  ?  114 ASN   B ND2    1 
ATOM   7746  H  H      . ASN   B 1 89  ? 41.357  -5.286  19.485 1.00 54.05  ?  114 ASN   B H      1 
ATOM   7747  H  HA     . ASN   B 1 89  ? 39.445  -6.060  19.947 1.00 51.59  ?  114 ASN   B HA     1 
ATOM   7748  H  HB2    . ASN   B 1 89  ? 38.840  -4.095  18.734 1.00 51.36  ?  114 ASN   B HB2    1 
ATOM   7749  H  HB3    . ASN   B 1 89  ? 38.668  -5.004  17.442 1.00 51.36  ?  114 ASN   B HB3    1 
ATOM   7750  H  HD21   . ASN   B 1 89  ? 35.461  -5.319  18.047 1.00 49.84  ?  114 ASN   B HD21   1 
ATOM   7751  H  HD22   . ASN   B 1 89  ? 36.511  -4.921  17.069 1.00 49.84  ?  114 ASN   B HD22   1 
ATOM   7752  N  N      . LEU   B 1 90  ? 40.140  -8.340  18.868 1.00 40.14  ?  115 LEU   B N      1 
ATOM   7753  C  CA     . LEU   B 1 90  ? 40.224  -9.659  18.252 1.00 38.52  ?  115 LEU   B CA     1 
ATOM   7754  C  C      . LEU   B 1 90  ? 40.204  -10.721 19.340 1.00 36.96  ?  115 LEU   B C      1 
ATOM   7755  O  O      . LEU   B 1 90  ? 41.002  -10.663 20.279 1.00 38.21  ?  115 LEU   B O      1 
ATOM   7756  C  CB     . LEU   B 1 90  ? 41.500  -9.773  17.407 1.00 41.15  ?  115 LEU   B CB     1 
ATOM   7757  C  CG     . LEU   B 1 90  ? 41.504  -10.864 16.342 1.00 45.90  ?  115 LEU   B CG     1 
ATOM   7758  C  CD1    . LEU   B 1 90  ? 40.431  -10.596 15.303 1.00 48.29  ?  115 LEU   B CD1    1 
ATOM   7759  C  CD2    . LEU   B 1 90  ? 42.870  -10.946 15.695 1.00 47.87  ?  115 LEU   B CD2    1 
ATOM   7760  H  H      . LEU   B 1 90  ? 40.638  -8.252  19.564 1.00 48.16  ?  115 LEU   B H      1 
ATOM   7761  H  HA     . LEU   B 1 90  ? 39.457  -9.810  17.679 1.00 46.22  ?  115 LEU   B HA     1 
ATOM   7762  H  HB2    . LEU   B 1 90  ? 41.637  -8.928  16.951 1.00 49.37  ?  115 LEU   B HB2    1 
ATOM   7763  H  HB3    . LEU   B 1 90  ? 42.243  -9.953  18.004 1.00 49.37  ?  115 LEU   B HB3    1 
ATOM   7764  H  HG     . LEU   B 1 90  ? 41.308  -11.721 16.754 1.00 55.08  ?  115 LEU   B HG     1 
ATOM   7765  H  HD11   . LEU   B 1 90  ? 40.581  -11.173 14.538 1.00 57.94  ?  115 LEU   B HD11   1 
ATOM   7766  H  HD12   . LEU   B 1 90  ? 39.562  -10.780 15.691 1.00 57.94  ?  115 LEU   B HD12   1 
ATOM   7767  H  HD13   . LEU   B 1 90  ? 40.481  -9.666  15.030 1.00 57.94  ?  115 LEU   B HD13   1 
ATOM   7768  H  HD21   . LEU   B 1 90  ? 42.858  -11.641 15.018 1.00 57.44  ?  115 LEU   B HD21   1 
ATOM   7769  H  HD22   . LEU   B 1 90  ? 43.078  -10.091 15.287 1.00 57.44  ?  115 LEU   B HD22   1 
ATOM   7770  H  HD23   . LEU   B 1 90  ? 43.529  -11.158 16.375 1.00 57.44  ?  115 LEU   B HD23   1 
ATOM   7771  N  N      . ILE   B 1 91  ? 39.278  -11.674 19.221 1.00 35.39  ?  116 ILE   B N      1 
ATOM   7772  C  CA     . ILE   B 1 91  ? 39.189  -12.821 20.119 1.00 34.19  ?  116 ILE   B CA     1 
ATOM   7773  C  C      . ILE   B 1 91  ? 39.191  -14.083 19.267 1.00 33.96  ?  116 ILE   B C      1 
ATOM   7774  O  O      . ILE   B 1 91  ? 38.519  -14.132 18.232 1.00 35.41  ?  116 ILE   B O      1 
ATOM   7775  C  CB     . ILE   B 1 91  ? 37.922  -12.768 21.003 1.00 33.62  ?  116 ILE   B CB     1 
ATOM   7776  C  CG1    . ILE   B 1 91  ? 37.941  -11.510 21.878 1.00 34.25  ?  116 ILE   B CG1    1 
ATOM   7777  C  CG2    . ILE   B 1 91  ? 37.813  -14.045 21.852 1.00 33.41  ?  116 ILE   B CG2    1 
ATOM   7778  C  CD1    . ILE   B 1 91  ? 36.588  -11.182 22.505 1.00 35.47  ?  116 ILE   B CD1    1 
ATOM   7779  H  H      . ILE   B 1 91  ? 38.674  -11.676 18.608 1.00 42.47  ?  116 ILE   B H      1 
ATOM   7780  H  HA     . ILE   B 1 91  ? 39.962  -12.832 20.705 1.00 41.02  ?  116 ILE   B HA     1 
ATOM   7781  H  HB     . ILE   B 1 91  ? 37.139  -12.722 20.433 1.00 40.33  ?  116 ILE   B HB     1 
ATOM   7782  H  HG12   . ILE   B 1 91  ? 38.578  -11.638 22.597 1.00 41.09  ?  116 ILE   B HG12   1 
ATOM   7783  H  HG13   . ILE   B 1 91  ? 38.206  -10.753 21.331 1.00 41.09  ?  116 ILE   B HG13   1 
ATOM   7784  H  HG21   . ILE   B 1 91  ? 37.152  -13.905 22.548 1.00 40.09  ?  116 ILE   B HG21   1 
ATOM   7785  H  HG22   . ILE   B 1 91  ? 37.543  -14.781 21.281 1.00 40.09  ?  116 ILE   B HG22   1 
ATOM   7786  H  HG23   . ILE   B 1 91  ? 38.678  -14.234 22.249 1.00 40.09  ?  116 ILE   B HG23   1 
ATOM   7787  H  HD11   . ILE   B 1 91  ? 36.649  -10.326 22.958 1.00 42.56  ?  116 ILE   B HD11   1 
ATOM   7788  H  HD12   . ILE   B 1 91  ? 35.917  -11.139 21.806 1.00 42.56  ?  116 ILE   B HD12   1 
ATOM   7789  H  HD13   . ILE   B 1 91  ? 36.358  -11.877 23.141 1.00 42.56  ?  116 ILE   B HD13   1 
ATOM   7790  N  N      . SER   B 1 92  ? 39.939  -15.104 19.695 1.00 33.14  ?  117 SER   B N      1 
ATOM   7791  C  CA     . SER   B 1 92  ? 39.900  -16.416 19.055 1.00 32.95  ?  117 SER   B CA     1 
ATOM   7792  C  C      . SER   B 1 92  ? 39.748  -17.490 20.125 1.00 32.82  ?  117 SER   B C      1 
ATOM   7793  O  O      . SER   B 1 92  ? 40.286  -17.363 21.229 1.00 33.48  ?  117 SER   B O      1 
ATOM   7794  C  CB     . SER   B 1 92  ? 41.168  -16.693 18.205 1.00 35.63  ?  117 SER   B CB     1 
ATOM   7795  O  OG     . SER   B 1 92  ? 42.288  -17.013 19.009 1.00 38.60  ?  117 SER   B OG     1 
ATOM   7796  H  H      . SER   B 1 92  ? 40.481  -15.058 20.361 1.00 39.76  ?  117 SER   B H      1 
ATOM   7797  H  HA     . SER   B 1 92  ? 39.135  -16.457 18.459 1.00 39.53  ?  117 SER   B HA     1 
ATOM   7798  H  HB2    . SER   B 1 92  ? 40.987  -17.439 17.611 1.00 42.75  ?  117 SER   B HB2    1 
ATOM   7799  H  HB3    . SER   B 1 92  ? 41.373  -15.899 17.686 1.00 42.75  ?  117 SER   B HB3    1 
ATOM   7800  H  HG     . SER   B 1 92  ? 42.958  -17.160 18.523 1.00 46.32  ?  117 SER   B HG     1 
ATOM   7801  N  N      . ILE   B 1 93  ? 39.000  -18.539 19.802 1.00 32.32  ?  118 ILE   B N      1 
ATOM   7802  C  CA     . ILE   B 1 93  ? 38.854  -19.697 20.674 1.00 31.26  ?  118 ILE   B CA     1 
ATOM   7803  C  C      . ILE   B 1 93  ? 39.130  -20.942 19.844 1.00 33.11  ?  118 ILE   B C      1 
ATOM   7804  O  O      . ILE   B 1 93  ? 38.447  -21.193 18.845 1.00 33.19  ?  118 ILE   B O      1 
ATOM   7805  C  CB     . ILE   B 1 93  ? 37.466  -19.746 21.338 1.00 29.93  ?  118 ILE   B CB     1 
ATOM   7806  C  CG1    . ILE   B 1 93  ? 37.306  -18.496 22.214 1.00 30.30  ?  118 ILE   B CG1    1 
ATOM   7807  C  CG2    . ILE   B 1 93  ? 37.290  -21.042 22.122 1.00 31.00  ?  118 ILE   B CG2    1 
ATOM   7808  C  CD1    . ILE   B 1 93  ? 35.943  -18.345 22.817 1.00 31.96  ?  118 ILE   B CD1    1 
ATOM   7809  H  H      . ILE   B 1 93  ? 38.558  -18.604 19.067 1.00 38.78  ?  118 ILE   B H      1 
ATOM   7810  H  HA     . ILE   B 1 93  ? 39.517  -19.664 21.382 1.00 37.50  ?  118 ILE   B HA     1 
ATOM   7811  H  HB     . ILE   B 1 93  ? 36.768  -19.741 20.664 1.00 35.91  ?  118 ILE   B HB     1 
ATOM   7812  H  HG12   . ILE   B 1 93  ? 37.946  -18.541 22.941 1.00 36.36  ?  118 ILE   B HG12   1 
ATOM   7813  H  HG13   . ILE   B 1 93  ? 37.476  -17.711 21.670 1.00 36.36  ?  118 ILE   B HG13   1 
ATOM   7814  H  HG21   . ILE   B 1 93  ? 36.467  -20.992 22.633 1.00 37.19  ?  118 ILE   B HG21   1 
ATOM   7815  H  HG22   . ILE   B 1 93  ? 37.248  -21.784 21.499 1.00 37.19  ?  118 ILE   B HG22   1 
ATOM   7816  H  HG23   . ILE   B 1 93  ? 38.044  -21.153 22.721 1.00 37.19  ?  118 ILE   B HG23   1 
ATOM   7817  H  HD11   . ILE   B 1 93  ? 35.878  -17.473 23.236 1.00 38.34  ?  118 ILE   B HD11   1 
ATOM   7818  H  HD12   . ILE   B 1 93  ? 35.278  -18.426 22.116 1.00 38.34  ?  118 ILE   B HD12   1 
ATOM   7819  H  HD13   . ILE   B 1 93  ? 35.812  -19.042 23.479 1.00 38.34  ?  118 ILE   B HD13   1 
ATOM   7820  N  N      . TRP   B 1 94  ? 40.128  -21.716 20.266 1.00 33.31  ?  119 TRP   B N      1 
ATOM   7821  C  CA     . TRP   B 1 94  ? 40.645  -22.884 19.558 1.00 35.38  ?  119 TRP   B CA     1 
ATOM   7822  C  C      . TRP   B 1 94  ? 40.474  -24.117 20.433 1.00 35.10  ?  119 TRP   B C      1 
ATOM   7823  O  O      . TRP   B 1 94  ? 40.604  -24.040 21.658 1.00 34.75  ?  119 TRP   B O      1 
ATOM   7824  C  CB     . TRP   B 1 94  ? 42.123  -22.631 19.216 1.00 38.04  ?  119 TRP   B CB     1 
ATOM   7825  C  CG     . TRP   B 1 94  ? 42.910  -23.739 18.542 1.00 40.13  ?  119 TRP   B CG     1 
ATOM   7826  C  CD1    . TRP   B 1 94  ? 43.208  -23.851 17.209 1.00 41.81  ?  119 TRP   B CD1    1 
ATOM   7827  C  CD2    . TRP   B 1 94  ? 43.544  -24.853 19.184 1.00 41.39  ?  119 TRP   B CD2    1 
ATOM   7828  N  NE1    . TRP   B 1 94  ? 43.974  -24.974 16.984 1.00 42.55  ?  119 TRP   B NE1    1 
ATOM   7829  C  CE2    . TRP   B 1 94  ? 44.195  -25.606 18.179 1.00 42.87  ?  119 TRP   B CE2    1 
ATOM   7830  C  CE3    . TRP   B 1 94  ? 43.621  -25.290 20.510 1.00 41.45  ?  119 TRP   B CE3    1 
ATOM   7831  C  CZ2    . TRP   B 1 94  ? 44.900  -26.776 18.459 1.00 43.11  ?  119 TRP   B CZ2    1 
ATOM   7832  C  CZ3    . TRP   B 1 94  ? 44.321  -26.450 20.785 1.00 42.38  ?  119 TRP   B CZ3    1 
ATOM   7833  C  CH2    . TRP   B 1 94  ? 44.960  -27.172 19.767 1.00 43.19  ?  119 TRP   B CH2    1 
ATOM   7834  H  H      . TRP   B 1 94  ? 40.546  -21.576 21.004 1.00 39.96  ?  119 TRP   B H      1 
ATOM   7835  H  HA     . TRP   B 1 94  ? 40.160  -23.059 18.737 1.00 42.45  ?  119 TRP   B HA     1 
ATOM   7836  H  HB2    . TRP   B 1 94  ? 42.160  -21.866 18.621 1.00 45.64  ?  119 TRP   B HB2    1 
ATOM   7837  H  HB3    . TRP   B 1 94  ? 42.586  -22.430 20.044 1.00 45.64  ?  119 TRP   B HB3    1 
ATOM   7838  H  HD1    . TRP   B 1 94  ? 42.932  -23.254 16.551 1.00 50.17  ?  119 TRP   B HD1    1 
ATOM   7839  H  HE1    . TRP   B 1 94  ? 44.266  -25.235 16.218 1.00 51.05  ?  119 TRP   B HE1    1 
ATOM   7840  H  HE3    . TRP   B 1 94  ? 43.210  -24.810 21.192 1.00 49.74  ?  119 TRP   B HE3    1 
ATOM   7841  H  HZ2    . TRP   B 1 94  ? 45.312  -27.266 17.785 1.00 51.73  ?  119 TRP   B HZ2    1 
ATOM   7842  H  HZ3    . TRP   B 1 94  ? 44.370  -26.756 21.662 1.00 50.85  ?  119 TRP   B HZ3    1 
ATOM   7843  H  HH2    . TRP   B 1 94  ? 45.436  -27.940 19.987 1.00 51.82  ?  119 TRP   B HH2    1 
ATOM   7844  N  N      . ASN   B 1 95  ? 40.153  -25.249 19.808 1.00 34.88  ?  120 ASN   B N      1 
ATOM   7845  C  CA     . ASN   B 1 95  ? 40.087  -26.521 20.516 1.00 35.42  ?  120 ASN   B CA     1 
ATOM   7846  C  C      . ASN   B 1 95  ? 40.624  -27.620 19.608 1.00 37.17  ?  120 ASN   B C      1 
ATOM   7847  O  O      . ASN   B 1 95  ? 40.562  -27.520 18.378 1.00 37.14  ?  120 ASN   B O      1 
ATOM   7848  C  CB     . ASN   B 1 95  ? 38.655  -26.872 20.980 1.00 35.74  ?  120 ASN   B CB     1 
ATOM   7849  C  CG     . ASN   B 1 95  ? 37.705  -27.148 19.826 1.00 35.33  ?  120 ASN   B CG     1 
ATOM   7850  O  OD1    . ASN   B 1 95  ? 37.006  -26.246 19.356 1.00 35.77  ?  120 ASN   B OD1    1 
ATOM   7851  N  ND2    . ASN   B 1 95  ? 37.662  -28.402 19.373 1.00 34.70  ?  120 ASN   B ND2    1 
ATOM   7852  H  H      . ASN   B 1 95  ? 39.968  -25.303 18.970 1.00 41.85  ?  120 ASN   B H      1 
ATOM   7853  H  HA     . ASN   B 1 95  ? 40.643  -26.472 21.309 1.00 42.50  ?  120 ASN   B HA     1 
ATOM   7854  H  HB2    . ASN   B 1 95  ? 38.689  -27.667 21.535 1.00 42.88  ?  120 ASN   B HB2    1 
ATOM   7855  H  HB3    . ASN   B 1 95  ? 38.297  -26.128 21.489 1.00 42.88  ?  120 ASN   B HB3    1 
ATOM   7856  H  HD21   . ASN   B 1 95  ? 37.140  -28.606 18.721 1.00 41.63  ?  120 ASN   B HD21   1 
ATOM   7857  H  HD22   . ASN   B 1 95  ? 38.157  -29.007 19.732 1.00 41.63  ?  120 ASN   B HD22   1 
ATOM   7858  N  N      . ASN   B 1 96  ? 41.154  -28.668 20.223 1.00 37.41  ?  121 ASN   B N      1 
ATOM   7859  C  CA     . ASN   B 1 96  ? 41.559  -29.851 19.486 1.00 39.52  ?  121 ASN   B CA     1 
ATOM   7860  C  C      . ASN   B 1 96  ? 40.485  -30.927 19.687 1.00 39.59  ?  121 ASN   B C      1 
ATOM   7861  O  O      . ASN   B 1 96  ? 39.351  -30.627 20.084 1.00 39.53  ?  121 ASN   B O      1 
ATOM   7862  C  CB     . ASN   B 1 96  ? 42.985  -30.278 19.882 1.00 42.06  ?  121 ASN   B CB     1 
ATOM   7863  C  CG     . ASN   B 1 96  ? 43.128  -30.652 21.342 1.00 42.32  ?  121 ASN   B CG     1 
ATOM   7864  O  OD1    . ASN   B 1 96  ? 42.152  -30.741 22.073 1.00 40.39  ?  121 ASN   B OD1    1 
ATOM   7865  N  ND2    . ASN   B 1 96  ? 44.369  -30.910 21.756 1.00 43.08  ?  121 ASN   B ND2    1 
ATOM   7866  H  H      . ASN   B 1 96  ? 41.289  -28.716 21.071 1.00 44.88  ?  121 ASN   B H      1 
ATOM   7867  H  HA     . ASN   B 1 96  ? 41.610  -29.639 18.541 1.00 47.42  ?  121 ASN   B HA     1 
ATOM   7868  H  HB2    . ASN   B 1 96  ? 43.237  -31.052 19.353 1.00 50.46  ?  121 ASN   B HB2    1 
ATOM   7869  H  HB3    . ASN   B 1 96  ? 43.592  -29.543 19.704 1.00 50.46  ?  121 ASN   B HB3    1 
ATOM   7870  H  HD21   . ASN   B 1 96  ? 44.513  -31.127 22.576 1.00 51.69  ?  121 ASN   B HD21   1 
ATOM   7871  H  HD22   . ASN   B 1 96  ? 45.027  -30.858 21.204 1.00 51.69  ?  121 ASN   B HD22   1 
ATOM   7872  N  N      . GLY   B 1 97  ? 40.819  -32.175 19.399 1.00 39.68  ?  122 GLY   B N      1 
ATOM   7873  C  CA     . GLY   B 1 97  ? 39.788  -33.169 19.203 1.00 41.06  ?  122 GLY   B CA     1 
ATOM   7874  C  C      . GLY   B 1 97  ? 39.154  -32.984 17.837 1.00 42.90  ?  122 GLY   B C      1 
ATOM   7875  O  O      . GLY   B 1 97  ? 39.539  -32.118 17.049 1.00 43.63  ?  122 GLY   B O      1 
ATOM   7876  H  H      . GLY   B 1 97  ? 41.624  -32.463 19.313 1.00 47.62  ?  122 GLY   B H      1 
ATOM   7877  H  HA2    . GLY   B 1 97  ? 40.171  -34.058 19.257 1.00 49.26  ?  122 GLY   B HA2    1 
ATOM   7878  H  HA3    . GLY   B 1 97  ? 39.104  -33.077 19.885 1.00 49.26  ?  122 GLY   B HA3    1 
ATOM   7879  N  N      . LYS   B 1 98  ? 38.131  -33.793 17.570 1.00 43.50  ?  123 LYS   B N      1 
ATOM   7880  C  CA     . LYS   B 1 98  ? 37.627  -33.932 16.209 1.00 45.46  ?  123 LYS   B CA     1 
ATOM   7881  C  C      . LYS   B 1 98  ? 37.076  -32.625 15.651 1.00 44.04  ?  123 LYS   B C      1 
ATOM   7882  O  O      . LYS   B 1 98  ? 36.356  -31.881 16.323 1.00 41.83  ?  123 LYS   B O      1 
ATOM   7883  C  CB     . LYS   B 1 98  ? 36.548  -35.019 16.161 1.00 49.13  ?  123 LYS   B CB     1 
ATOM   7884  C  CG     . LYS   B 1 98  ? 37.135  -36.428 16.145 1.00 53.78  ?  123 LYS   B CG     1 
ATOM   7885  C  CD     . LYS   B 1 98  ? 36.064  -37.514 16.129 1.00 56.82  ?  123 LYS   B CD     1 
ATOM   7886  C  CE     . LYS   B 1 98  ? 36.569  -38.805 16.777 1.00 58.91  ?  123 LYS   B CE     1 
ATOM   7887  N  NZ     . LYS   B 1 98  ? 35.455  -39.711 17.192 1.00 59.55  ?  123 LYS   B NZ     1 
ATOM   7888  H  H      . LYS   B 1 98  ? 37.715  -34.269 18.154 1.00 52.19  ?  123 LYS   B H      1 
ATOM   7889  H  HA     . LYS   B 1 98  ? 38.368  -34.190 15.639 1.00 54.54  ?  123 LYS   B HA     1 
ATOM   7890  H  HB2    . LYS   B 1 98  ? 35.982  -34.938 16.945 1.00 58.94  ?  123 LYS   B HB2    1 
ATOM   7891  H  HB3    . LYS   B 1 98  ? 36.019  -34.905 15.356 1.00 58.94  ?  123 LYS   B HB3    1 
ATOM   7892  H  HG2    . LYS   B 1 98  ? 37.682  -36.534 15.351 1.00 64.53  ?  123 LYS   B HG2    1 
ATOM   7893  H  HG3    . LYS   B 1 98  ? 37.677  -36.554 16.940 1.00 64.53  ?  123 LYS   B HG3    1 
ATOM   7894  H  HD2    . LYS   B 1 98  ? 35.287  -37.208 16.623 1.00 68.18  ?  123 LYS   B HD2    1 
ATOM   7895  H  HD3    . LYS   B 1 98  ? 35.818  -37.710 15.211 1.00 68.18  ?  123 LYS   B HD3    1 
ATOM   7896  H  HE2    . LYS   B 1 98  ? 37.124  -39.283 16.142 1.00 70.69  ?  123 LYS   B HE2    1 
ATOM   7897  H  HE3    . LYS   B 1 98  ? 37.085  -38.582 17.567 1.00 70.69  ?  123 LYS   B HE3    1 
ATOM   7898  H  HZ1    . LYS   B 1 98  ? 35.785  -40.441 17.579 1.00 71.45  ?  123 LYS   B HZ1    1 
ATOM   7899  H  HZ2    . LYS   B 1 98  ? 34.922  -39.293 17.770 1.00 71.45  ?  123 LYS   B HZ2    1 
ATOM   7900  H  HZ3    . LYS   B 1 98  ? 34.977  -39.951 16.481 1.00 71.45  ?  123 LYS   B HZ3    1 
ATOM   7901  N  N      . GLY   B 1 99  ? 37.432  -32.359 14.395 1.00 43.30  ?  124 GLY   B N      1 
ATOM   7902  C  CA     . GLY   B 1 99  ? 36.902  -31.229 13.670 1.00 42.15  ?  124 GLY   B CA     1 
ATOM   7903  C  C      . GLY   B 1 99  ? 35.517  -31.505 13.126 1.00 41.79  ?  124 GLY   B C      1 
ATOM   7904  O  O      . GLY   B 1 99  ? 34.980  -32.608 13.217 1.00 43.04  ?  124 GLY   B O      1 
ATOM   7905  H  H      . GLY   B 1 99  ? 37.989  -32.831 13.941 1.00 51.95  ?  124 GLY   B H      1 
ATOM   7906  H  HA2    . GLY   B 1 99  ? 36.854  -30.461 14.260 1.00 50.58  ?  124 GLY   B HA2    1 
ATOM   7907  H  HA3    . GLY   B 1 99  ? 37.489  -31.020 12.926 1.00 50.58  ?  124 GLY   B HA3    1 
ATOM   7908  N  N      . ILE   B 1 100 ? 34.929  -30.465 12.544 1.00 39.54  ?  125 ILE   B N      1 
ATOM   7909  C  CA     . ILE   B 1 100 ? 33.597  -30.546 11.947 1.00 39.11  ?  125 ILE   B CA     1 
ATOM   7910  C  C      . ILE   B 1 100 ? 33.704  -31.180 10.567 1.00 41.20  ?  125 ILE   B C      1 
ATOM   7911  O  O      . ILE   B 1 100 ? 34.630  -30.848 9.816  1.00 42.41  ?  125 ILE   B O      1 
ATOM   7912  C  CB     . ILE   B 1 100 ? 32.955  -29.153 11.867 1.00 38.80  ?  125 ILE   B CB     1 
ATOM   7913  C  CG1    . ILE   B 1 100 ? 32.831  -28.563 13.273 1.00 38.05  ?  125 ILE   B CG1    1 
ATOM   7914  C  CG2    . ILE   B 1 100 ? 31.591  -29.212 11.197 1.00 38.38  ?  125 ILE   B CG2    1 
ATOM   7915  C  CD1    . ILE   B 1 100 ? 32.558  -27.096 13.268 1.00 38.77  ?  125 ILE   B CD1    1 
ATOM   7916  H  H      . ILE   B 1 100 ? 35.286  -29.685 12.480 1.00 47.45  ?  125 ILE   B H      1 
ATOM   7917  H  HA     . ILE   B 1 100 ? 33.036  -31.117 12.494 1.00 46.92  ?  125 ILE   B HA     1 
ATOM   7918  H  HB     . ILE   B 1 100 ? 33.527  -28.586 11.327 1.00 46.55  ?  125 ILE   B HB     1 
ATOM   7919  H  HG12   . ILE   B 1 100 ? 32.100  -29.001 13.735 1.00 45.66  ?  125 ILE   B HG12   1 
ATOM   7920  H  HG13   . ILE   B 1 100 ? 33.662  -28.711 13.751 1.00 45.66  ?  125 ILE   B HG13   1 
ATOM   7921  H  HG21   . ILE   B 1 100 ? 31.204  -28.322 11.189 1.00 46.05  ?  125 ILE   B HG21   1 
ATOM   7922  H  HG22   . ILE   B 1 100 ? 31.699  -29.534 10.288 1.00 46.05  ?  125 ILE   B HG22   1 
ATOM   7923  H  HG23   . ILE   B 1 100 ? 31.019  -29.816 11.696 1.00 46.05  ?  125 ILE   B HG23   1 
ATOM   7924  H  HD11   . ILE   B 1 100 ? 31.685  -26.939 12.876 1.00 46.52  ?  125 ILE   B HD11   1 
ATOM   7925  H  HD12   . ILE   B 1 100 ? 32.575  -26.768 14.181 1.00 46.52  ?  125 ILE   B HD12   1 
ATOM   7926  H  HD13   . ILE   B 1 100 ? 33.241  -26.649 12.744 1.00 46.52  ?  125 ILE   B HD13   1 
ATOM   7927  N  N      . PRO   B 1 101 ? 32.781  -32.065 10.182 1.00 41.65  ?  126 PRO   B N      1 
ATOM   7928  C  CA     . PRO   B 1 101 ? 32.864  -32.681 8.846  1.00 42.77  ?  126 PRO   B CA     1 
ATOM   7929  C  C      . PRO   B 1 101 ? 32.868  -31.648 7.726  1.00 43.46  ?  126 PRO   B C      1 
ATOM   7930  O  O      . PRO   B 1 101 ? 31.973  -30.809 7.626  1.00 44.17  ?  126 PRO   B O      1 
ATOM   7931  C  CB     . PRO   B 1 101 ? 31.609  -33.563 8.778  1.00 43.16  ?  126 PRO   B CB     1 
ATOM   7932  C  CG     . PRO   B 1 101 ? 31.216  -33.797 10.189 1.00 43.11  ?  126 PRO   B CG     1 
ATOM   7933  C  CD     . PRO   B 1 101 ? 31.642  -32.582 10.965 1.00 42.92  ?  126 PRO   B CD     1 
ATOM   7934  H  HA     . PRO   B 1 101 ? 33.667  -33.223 8.787  1.00 51.31  ?  126 PRO   B HA     1 
ATOM   7935  H  HB2    . PRO   B 1 101 ? 30.907  -33.099 8.296  1.00 51.78  ?  126 PRO   B HB2    1 
ATOM   7936  H  HB3    . PRO   B 1 101 ? 31.819  -34.400 8.335  1.00 51.78  ?  126 PRO   B HB3    1 
ATOM   7937  H  HG2    . PRO   B 1 101 ? 30.255  -33.914 10.242 1.00 51.73  ?  126 PRO   B HG2    1 
ATOM   7938  H  HG3    . PRO   B 1 101 ? 31.667  -34.588 10.523 1.00 51.73  ?  126 PRO   B HG3    1 
ATOM   7939  H  HD2    . PRO   B 1 101 ? 30.925  -31.929 11.005 1.00 51.49  ?  126 PRO   B HD2    1 
ATOM   7940  H  HD3    . PRO   B 1 101 ? 31.920  -32.825 11.862 1.00 51.49  ?  126 PRO   B HD3    1 
ATOM   7941  N  N      . VAL   B 1 102 ? 33.854  -31.744 6.846  1.00 43.43  ?  127 VAL   B N      1 
ATOM   7942  C  CA     . VAL   B 1 102 ? 33.992  -30.808 5.730  1.00 45.17  ?  127 VAL   B CA     1 
ATOM   7943  C  C      . VAL   B 1 102 ? 33.388  -31.494 4.507  1.00 45.70  ?  127 VAL   B C      1 
ATOM   7944  O  O      . VAL   B 1 102 ? 34.063  -32.212 3.764  1.00 48.01  ?  127 VAL   B O      1 
ATOM   7945  C  CB     . VAL   B 1 102 ? 35.447  -30.383 5.530  1.00 45.23  ?  127 VAL   B CB     1 
ATOM   7946  C  CG1    . VAL   B 1 102 ? 35.563  -29.398 4.388  1.00 46.08  ?  127 VAL   B CG1    1 
ATOM   7947  C  CG2    . VAL   B 1 102 ? 35.989  -29.766 6.835  1.00 45.82  ?  127 VAL   B CG2    1 
ATOM   7948  H  H      . VAL   B 1 102 ? 34.466  -32.348 6.871  1.00 52.11  ?  127 VAL   B H      1 
ATOM   7949  H  HA     . VAL   B 1 102 ? 33.466  -30.011 5.905  1.00 54.19  ?  127 VAL   B HA     1 
ATOM   7950  H  HB     . VAL   B 1 102 ? 35.982  -31.160 5.306  1.00 54.27  ?  127 VAL   B HB     1 
ATOM   7951  H  HG11   . VAL   B 1 102 ? 36.470  -29.058 4.355  1.00 55.29  ?  127 VAL   B HG11   1 
ATOM   7952  H  HG12   . VAL   B 1 102 ? 35.349  -29.852 3.557  1.00 55.29  ?  127 VAL   B HG12   1 
ATOM   7953  H  HG13   . VAL   B 1 102 ? 34.941  -28.668 4.535  1.00 55.29  ?  127 VAL   B HG13   1 
ATOM   7954  H  HG21   . VAL   B 1 102 ? 36.889  -29.440 6.680  1.00 54.98  ?  127 VAL   B HG21   1 
ATOM   7955  H  HG22   . VAL   B 1 102 ? 35.413  -29.032 7.100  1.00 54.98  ?  127 VAL   B HG22   1 
ATOM   7956  H  HG23   . VAL   B 1 102 ? 35.998  -30.446 7.526  1.00 54.98  ?  127 VAL   B HG23   1 
ATOM   7957  N  N      . VAL   B 1 103 ? 32.090  -31.266 4.302  1.00 45.90  ?  128 VAL   B N      1 
ATOM   7958  C  CA     . VAL   B 1 103 ? 31.328  -31.974 3.271  1.00 46.58  ?  128 VAL   B CA     1 
ATOM   7959  C  C      . VAL   B 1 103 ? 30.004  -31.262 3.066  1.00 47.47  ?  128 VAL   B C      1 
ATOM   7960  O  O      . VAL   B 1 103 ? 29.501  -30.602 3.984  1.00 45.54  ?  128 VAL   B O      1 
ATOM   7961  C  CB     . VAL   B 1 103 ? 31.128  -33.459 3.684  1.00 46.44  ?  128 VAL   B CB     1 
ATOM   7962  C  CG1    . VAL   B 1 103 ? 30.153  -33.555 4.854  1.00 45.87  ?  128 VAL   B CG1    1 
ATOM   7963  C  CG2    . VAL   B 1 103 ? 30.602  -34.265 2.499  1.00 46.57  ?  128 VAL   B CG2    1 
ATOM   7964  H  H      . VAL   B 1 103 ? 31.623  -30.701 4.751  1.00 55.07  ?  128 VAL   B H      1 
ATOM   7965  H  HA     . VAL   B 1 103 ? 31.821  -31.941 2.436  1.00 55.89  ?  128 VAL   B HA     1 
ATOM   7966  H  HB     . VAL   B 1 103 ? 31.981  -33.829 3.961  1.00 55.72  ?  128 VAL   B HB     1 
ATOM   7967  H  HG11   . VAL   B 1 103 ? 30.226  -34.435 5.255  1.00 55.04  ?  128 VAL   B HG11   1 
ATOM   7968  H  HG12   . VAL   B 1 103 ? 30.376  -32.874 5.508  1.00 55.04  ?  128 VAL   B HG12   1 
ATOM   7969  H  HG13   . VAL   B 1 103 ? 29.251  -33.415 4.526  1.00 55.04  ?  128 VAL   B HG13   1 
ATOM   7970  H  HG21   . VAL   B 1 103 ? 30.625  -35.208 2.723  1.00 55.87  ?  128 VAL   B HG21   1 
ATOM   7971  H  HG22   . VAL   B 1 103 ? 29.690  -33.992 2.312  1.00 55.87  ?  128 VAL   B HG22   1 
ATOM   7972  H  HG23   . VAL   B 1 103 ? 31.163  -34.094 1.727  1.00 55.87  ?  128 VAL   B HG23   1 
ATOM   7973  N  N      . GLU   B 1 104 ? 29.413  -31.449 1.884  1.00 48.39  ?  129 GLU   B N      1 
ATOM   7974  C  CA     . GLU   B 1 104 ? 28.116  -30.874 1.567  1.00 49.45  ?  129 GLU   B CA     1 
ATOM   7975  C  C      . GLU   B 1 104 ? 26.989  -31.631 2.261  1.00 49.37  ?  129 GLU   B C      1 
ATOM   7976  O  O      . GLU   B 1 104 ? 26.927  -32.864 2.207  1.00 49.64  ?  129 GLU   B O      1 
ATOM   7977  C  CB     . GLU   B 1 104 ? 27.870  -30.901 0.057  1.00 52.87  ?  129 GLU   B CB     1 
ATOM   7978  C  CG     . GLU   B 1 104 ? 28.667  -29.916 -0.762 1.00 55.84  ?  129 GLU   B CG     1 
ATOM   7979  C  CD     . GLU   B 1 104 ? 28.495  -30.132 -2.263 1.00 58.87  ?  129 GLU   B CD     1 
ATOM   7980  O  OE1    . GLU   B 1 104 ? 29.021  -31.132 -2.798 1.00 59.80  ?  129 GLU   B OE1    1 
ATOM   7981  O  OE2    . GLU   B 1 104 ? 27.830  -29.299 -2.914 1.00 60.48  ?  129 GLU   B OE2    1 
ATOM   7982  H  H      . GLU   B 1 104 ? 29.751  -31.913 1.244  1.00 58.06  ?  129 GLU   B H      1 
ATOM   7983  H  HA     . GLU   B 1 104 ? 28.112  -29.956 1.881  1.00 59.33  ?  129 GLU   B HA     1 
ATOM   7984  H  HB2    . GLU   B 1 104 ? 28.089  -31.788 -0.269 1.00 63.44  ?  129 GLU   B HB2    1 
ATOM   7985  H  HB3    . GLU   B 1 104 ? 26.932  -30.712 -0.100 1.00 63.44  ?  129 GLU   B HB3    1 
ATOM   7986  H  HG2    . GLU   B 1 104 ? 28.371  -29.016 -0.551 1.00 67.00  ?  129 GLU   B HG2    1 
ATOM   7987  H  HG3    . GLU   B 1 104 ? 29.608  -30.014 -0.549 1.00 67.00  ?  129 GLU   B HG3    1 
ATOM   7988  N  N      . HIS   B 1 105 ? 26.073  -30.876 2.867  1.00 47.57  ?  130 HIS   B N      1 
ATOM   7989  C  CA     . HIS   B 1 105 ? 24.874  -31.419 3.497  1.00 47.09  ?  130 HIS   B CA     1 
ATOM   7990  C  C      . HIS   B 1 105 ? 23.846  -31.742 2.421  1.00 48.24  ?  130 HIS   B C      1 
ATOM   7991  O  O      . HIS   B 1 105 ? 23.409  -30.855 1.682  1.00 48.66  ?  130 HIS   B O      1 
ATOM   7992  C  CB     . HIS   B 1 105 ? 24.335  -30.392 4.489  1.00 44.24  ?  130 HIS   B CB     1 
ATOM   7993  C  CG     . HIS   B 1 105 ? 23.394  -30.944 5.512  1.00 43.00  ?  130 HIS   B CG     1 
ATOM   7994  N  ND1    . HIS   B 1 105 ? 22.093  -31.289 5.222  1.00 42.78  ?  130 HIS   B ND1    1 
ATOM   7995  C  CD2    . HIS   B 1 105 ? 23.549  -31.146 6.844  1.00 41.85  ?  130 HIS   B CD2    1 
ATOM   7996  C  CE1    . HIS   B 1 105 ? 21.492  -31.701 6.324  1.00 42.19  ?  130 HIS   B CE1    1 
ATOM   7997  N  NE2    . HIS   B 1 105 ? 22.358  -31.638 7.320  1.00 41.21  ?  130 HIS   B NE2    1 
ATOM   7998  H  H      . HIS   B 1 105 ? 26.126  -30.019 2.928  1.00 57.08  ?  130 HIS   B H      1 
ATOM   7999  H  HA     . HIS   B 1 105 ? 25.074  -32.241 3.972  1.00 56.50  ?  130 HIS   B HA     1 
ATOM   8000  H  HB2    . HIS   B 1 105 ? 25.085  -29.999 4.963  1.00 53.08  ?  130 HIS   B HB2    1 
ATOM   8001  H  HB3    . HIS   B 1 105 ? 23.859  -29.707 3.994  1.00 53.08  ?  130 HIS   B HB3    1 
ATOM   8002  H  HD2    . HIS   B 1 105 ? 24.317  -30.982 7.341  1.00 50.21  ?  130 HIS   B HD2    1 
ATOM   8003  H  HE1    . HIS   B 1 105 ? 20.609  -31.988 6.388  1.00 50.62  ?  130 HIS   B HE1    1 
ATOM   8004  H  HE2    . HIS   B 1 105 ? 22.202  -31.867 8.134  1.00 49.44  ?  130 HIS   B HE2    1 
ATOM   8005  N  N      . LYS   B 1 106 ? 23.439  -33.005 2.337  1.00 49.35  ?  131 LYS   B N      1 
ATOM   8006  C  CA     A LYS   B 1 106 ? 22.602  -33.423 1.220  0.57 49.45  ?  131 LYS   B CA     1 
ATOM   8007  C  CA     B LYS   B 1 106 ? 22.603  -33.426 1.220  0.43 50.28  ?  131 LYS   B CA     1 
ATOM   8008  C  C      . LYS   B 1 106 ? 21.200  -32.838 1.280  1.00 50.56  ?  131 LYS   B C      1 
ATOM   8009  O  O      . LYS   B 1 106 ? 20.508  -32.819 0.256  1.00 52.27  ?  131 LYS   B O      1 
ATOM   8010  C  CB     A LYS   B 1 106 ? 22.519  -34.947 1.172  0.57 48.86  ?  131 LYS   B CB     1 
ATOM   8011  C  CB     B LYS   B 1 106 ? 22.516  -34.954 1.174  0.43 50.97  ?  131 LYS   B CB     1 
ATOM   8012  C  CG     A LYS   B 1 106 ? 23.842  -35.619 0.892  0.57 47.43  ?  131 LYS   B CG     1 
ATOM   8013  C  CG     B LYS   B 1 106 ? 23.863  -35.652 1.239  0.43 51.09  ?  131 LYS   B CG     1 
ATOM   8014  C  CD     A LYS   B 1 106 ? 23.712  -37.130 0.991  0.57 45.86  ?  131 LYS   B CD     1 
ATOM   8015  C  CD     B LYS   B 1 106 ? 24.639  -35.514 -0.062 0.43 50.68  ?  131 LYS   B CD     1 
ATOM   8016  C  CE     A LYS   B 1 106 ? 24.936  -37.828 0.437  0.57 45.61  ?  131 LYS   B CE     1 
ATOM   8017  C  CE     B LYS   B 1 106 ? 26.134  -35.615 0.182  0.43 49.14  ?  131 LYS   B CE     1 
ATOM   8018  N  NZ     A LYS   B 1 106 ? 26.182  -37.474 1.163  0.57 45.46  ?  131 LYS   B NZ     1 
ATOM   8019  N  NZ     B LYS   B 1 106 ? 26.808  -34.325 -0.103 0.43 46.83  ?  131 LYS   B NZ     1 
ATOM   8020  H  H      . LYS   B 1 106 ? 23.627  -33.626 2.901  1.00 59.22  ?  131 LYS   B H      1 
ATOM   8021  H  HA     . LYS   B 1 106 ? 23.016  -33.113 0.400  1.00 60.33  ?  131 LYS   B HA     1 
ATOM   8022  H  HB2    A LYS   B 1 106 ? 22.199  -35.270 2.029  0.57 58.63  ?  131 LYS   B HB2    1 
ATOM   8023  H  HB2    B LYS   B 1 106 ? 21.990  -35.259 1.930  0.43 61.16  ?  131 LYS   B HB2    1 
ATOM   8024  H  HB3    A LYS   B 1 106 ? 21.902  -35.204 0.470  0.57 58.63  ?  131 LYS   B HB3    1 
ATOM   8025  H  HB3    B LYS   B 1 106 ? 22.088  -35.216 0.344  0.43 61.16  ?  131 LYS   B HB3    1 
ATOM   8026  H  HG2    A LYS   B 1 106 ? 24.137  -35.393 -0.004 0.57 56.91  ?  131 LYS   B HG2    1 
ATOM   8027  H  HG2    B LYS   B 1 106 ? 24.393  -35.259 1.950  0.43 61.30  ?  131 LYS   B HG2    1 
ATOM   8028  H  HG3    A LYS   B 1 106 ? 24.500  -35.323 1.541  0.57 56.91  ?  131 LYS   B HG3    1 
ATOM   8029  H  HG3    B LYS   B 1 106 ? 23.726  -36.597 1.410  0.43 61.30  ?  131 LYS   B HG3    1 
ATOM   8030  H  HD2    A LYS   B 1 106 ? 23.611  -37.384 1.922  0.57 55.03  ?  131 LYS   B HD2    1 
ATOM   8031  H  HD2    B LYS   B 1 106 ? 24.378  -36.223 -0.670 0.43 60.81  ?  131 LYS   B HD2    1 
ATOM   8032  H  HD3    A LYS   B 1 106 ? 22.939  -37.421 0.483  0.57 55.03  ?  131 LYS   B HD3    1 
ATOM   8033  H  HD3    B LYS   B 1 106 ? 24.450  -34.650 -0.460 0.43 60.81  ?  131 LYS   B HD3    1 
ATOM   8034  H  HE2    A LYS   B 1 106 ? 24.812  -38.787 0.506  0.57 54.73  ?  131 LYS   B HE2    1 
ATOM   8035  H  HE2    B LYS   B 1 106 ? 26.295  -35.847 1.110  0.43 58.97  ?  131 LYS   B HE2    1 
ATOM   8036  H  HE3    A LYS   B 1 106 ? 25.050  -37.574 -0.493 0.57 54.73  ?  131 LYS   B HE3    1 
ATOM   8037  H  HE3    B LYS   B 1 106 ? 26.511  -36.293 -0.400 0.43 58.97  ?  131 LYS   B HE3    1 
ATOM   8038  H  HZ1    A LYS   B 1 106 ? 26.327  -36.598 1.109  0.57 54.54  ?  131 LYS   B HZ1    1 
ATOM   8039  H  HZ1    B LYS   B 1 106 ? 26.696  -34.105 -0.959 0.43 56.19  ?  131 LYS   B HZ1    1 
ATOM   8040  H  HZ2    A LYS   B 1 106 ? 26.109  -37.702 2.020  0.57 54.54  ?  131 LYS   B HZ2    1 
ATOM   8041  H  HZ2    B LYS   B 1 106 ? 26.463  -33.682 0.407  0.43 56.19  ?  131 LYS   B HZ2    1 
ATOM   8042  H  HZ3    A LYS   B 1 106 ? 26.874  -37.904 0.807  0.57 54.54  ?  131 LYS   B HZ3    1 
ATOM   8043  H  HZ3    B LYS   B 1 106 ? 27.679  -34.392 0.066  0.43 56.19  ?  131 LYS   B HZ3    1 
ATOM   8044  N  N      . VAL   B 1 107 ? 20.765  -32.360 2.439  1.00 49.36  ?  132 VAL   B N      1 
ATOM   8045  C  CA     . VAL   B 1 107 ? 19.431  -31.795 2.593  1.00 49.02  ?  132 VAL   B CA     1 
ATOM   8046  C  C      . VAL   B 1 107 ? 19.455  -30.278 2.495  1.00 48.08  ?  132 VAL   B C      1 
ATOM   8047  O  O      . VAL   B 1 107 ? 18.637  -29.678 1.797  1.00 48.74  ?  132 VAL   B O      1 
ATOM   8048  C  CB     . VAL   B 1 107 ? 18.805  -32.256 3.928  1.00 50.28  ?  132 VAL   B CB     1 
ATOM   8049  C  CG1    . VAL   B 1 107 ? 17.504  -31.521 4.169  1.00 50.86  ?  132 VAL   B CG1    1 
ATOM   8050  C  CG2    . VAL   B 1 107 ? 18.583  -33.754 3.910  1.00 51.65  ?  132 VAL   B CG2    1 
ATOM   8051  H  H      . VAL   B 1 107 ? 21.231  -32.353 3.162  1.00 59.23  ?  132 VAL   B H      1 
ATOM   8052  H  HA     . VAL   B 1 107 ? 18.875  -32.128 1.871  1.00 58.81  ?  132 VAL   B HA     1 
ATOM   8053  H  HB     . VAL   B 1 107 ? 19.410  -32.050 4.658  1.00 60.33  ?  132 VAL   B HB     1 
ATOM   8054  H  HG11   . VAL   B 1 107 ? 16.988  -32.002 4.834  1.00 61.02  ?  132 VAL   B HG11   1 
ATOM   8055  H  HG12   . VAL   B 1 107 ? 17.702  -30.626 4.488  1.00 61.02  ?  132 VAL   B HG12   1 
ATOM   8056  H  HG13   . VAL   B 1 107 ? 17.009  -31.473 3.336  1.00 61.02  ?  132 VAL   B HG13   1 
ATOM   8057  H  HG21   . VAL   B 1 107 ? 18.196  -34.025 4.757  1.00 61.98  ?  132 VAL   B HG21   1 
ATOM   8058  H  HG22   . VAL   B 1 107 ? 17.980  -33.975 3.184  1.00 61.98  ?  132 VAL   B HG22   1 
ATOM   8059  H  HG23   . VAL   B 1 107 ? 19.436  -34.198 3.779  1.00 61.98  ?  132 VAL   B HG23   1 
ATOM   8060  N  N      . GLU   B 1 108 ? 20.378  -29.637 3.203  1.00 47.81  ?  133 GLU   B N      1 
ATOM   8061  C  CA     . GLU   B 1 108 ? 20.494  -28.184 3.170  1.00 46.36  ?  133 GLU   B CA     1 
ATOM   8062  C  C      . GLU   B 1 108 ? 21.468  -27.700 2.102  1.00 46.84  ?  133 GLU   B C      1 
ATOM   8063  O  O      . GLU   B 1 108 ? 21.526  -26.494 1.840  1.00 47.54  ?  133 GLU   B O      1 
ATOM   8064  C  CB     . GLU   B 1 108 ? 20.907  -27.672 4.553  1.00 45.67  ?  133 GLU   B CB     1 
ATOM   8065  C  CG     . GLU   B 1 108 ? 20.040  -28.220 5.686  1.00 46.33  ?  133 GLU   B CG     1 
ATOM   8066  C  CD     . GLU   B 1 108 ? 18.579  -27.819 5.569  1.00 48.57  ?  133 GLU   B CD     1 
ATOM   8067  O  OE1    . GLU   B 1 108 ? 18.295  -26.731 5.021  1.00 49.35  ?  133 GLU   B OE1    1 
ATOM   8068  O  OE2    . GLU   B 1 108 ? 17.714  -28.592 6.034  1.00 50.10  ?  133 GLU   B OE2    1 
ATOM   8069  H  H      . GLU   B 1 108 ? 20.952  -30.023 3.713  1.00 57.36  ?  133 GLU   B H      1 
ATOM   8070  H  HA     . GLU   B 1 108 ? 19.632  -27.790 2.966  1.00 55.62  ?  133 GLU   B HA     1 
ATOM   8071  H  HB2    . GLU   B 1 108 ? 21.824  -27.938 4.725  1.00 54.80  ?  133 GLU   B HB2    1 
ATOM   8072  H  HB3    . GLU   B 1 108 ? 20.834  -26.705 4.564  1.00 54.80  ?  133 GLU   B HB3    1 
ATOM   8073  H  HG2    . GLU   B 1 108 ? 20.085  -29.189 5.676  1.00 55.59  ?  133 GLU   B HG2    1 
ATOM   8074  H  HG3    . GLU   B 1 108 ? 20.375  -27.881 6.531  1.00 55.59  ?  133 GLU   B HG3    1 
ATOM   8075  N  N      . LYS   B 1 109 ? 22.229  -28.608 1.487  1.00 46.09  ?  134 LYS   B N      1 
ATOM   8076  C  CA     . LYS   B 1 109 ? 22.980  -28.332 0.258  1.00 48.05  ?  134 LYS   B CA     1 
ATOM   8077  C  C      . LYS   B 1 109 ? 23.962  -27.169 0.409  1.00 48.47  ?  134 LYS   B C      1 
ATOM   8078  O  O      . LYS   B 1 109 ? 24.045  -26.271 -0.434 1.00 49.63  ?  134 LYS   B O      1 
ATOM   8079  C  CB     . LYS   B 1 109 ? 22.010  -28.103 -0.903 1.00 50.01  ?  134 LYS   B CB     1 
ATOM   8080  C  CG     . LYS   B 1 109 ? 21.556  -29.414 -1.537 1.00 53.58  ?  134 LYS   B CG     1 
ATOM   8081  C  CD     . LYS   B 1 109 ? 20.049  -29.521 -1.587 1.00 55.81  ?  134 LYS   B CD     1 
ATOM   8082  C  CE     . LYS   B 1 109 ? 19.625  -30.920 -1.974 1.00 56.88  ?  134 LYS   B CE     1 
ATOM   8083  N  NZ     . LYS   B 1 109 ? 18.540  -30.889 -2.982 1.00 58.30  ?  134 LYS   B NZ     1 
ATOM   8084  H  H      . LYS   B 1 109 ? 22.330  -29.414 1.769  1.00 55.30  ?  134 LYS   B H      1 
ATOM   8085  H  HA     . LYS   B 1 109 ? 23.531  -29.107 0.062  1.00 57.65  ?  134 LYS   B HA     1 
ATOM   8086  H  HB2    . LYS   B 1 109 ? 21.225  -27.637 -0.574 1.00 60.01  ?  134 LYS   B HB2    1 
ATOM   8087  H  HB3    . LYS   B 1 109 ? 22.449  -27.572 -1.585 1.00 60.01  ?  134 LYS   B HB3    1 
ATOM   8088  H  HG2    . LYS   B 1 109 ? 21.894  -29.464 -2.445 1.00 64.29  ?  134 LYS   B HG2    1 
ATOM   8089  H  HG3    . LYS   B 1 109 ? 21.896  -30.157 -1.015 1.00 64.29  ?  134 LYS   B HG3    1 
ATOM   8090  H  HD2    . LYS   B 1 109 ? 19.680  -29.317 -0.713 1.00 66.97  ?  134 LYS   B HD2    1 
ATOM   8091  H  HD3    . LYS   B 1 109 ? 19.701  -28.900 -2.246 1.00 66.97  ?  134 LYS   B HD3    1 
ATOM   8092  H  HE2    . LYS   B 1 109 ? 20.382  -31.393 -2.353 1.00 68.25  ?  134 LYS   B HE2    1 
ATOM   8093  H  HE3    . LYS   B 1 109 ? 19.301  -31.388 -1.188 1.00 68.25  ?  134 LYS   B HE3    1 
ATOM   8094  H  HZ1    . LYS   B 1 109 ? 18.253  -31.716 -3.146 1.00 69.95  ?  134 LYS   B HZ1    1 
ATOM   8095  H  HZ2    . LYS   B 1 109 ? 17.859  -30.402 -2.681 1.00 69.95  ?  134 LYS   B HZ2    1 
ATOM   8096  H  HZ3    . LYS   B 1 109 ? 18.839  -30.532 -3.740 1.00 69.95  ?  134 LYS   B HZ3    1 
ATOM   8097  N  N      . MET   B 1 110 ? 24.738  -27.219 1.488  1.00 47.34  ?  135 MET   B N      1 
ATOM   8098  C  CA     . MET   B 1 110 ? 25.929  -26.395 1.644  1.00 46.70  ?  135 MET   B CA     1 
ATOM   8099  C  C      . MET   B 1 110 ? 26.882  -27.161 2.553  1.00 44.93  ?  135 MET   B C      1 
ATOM   8100  O  O      . MET   B 1 110 ? 26.502  -28.146 3.196  1.00 44.88  ?  135 MET   B O      1 
ATOM   8101  C  CB     . MET   B 1 110 ? 25.605  -25.003 2.192  1.00 49.02  ?  135 MET   B CB     1 
ATOM   8102  C  CG     . MET   B 1 110 ? 24.956  -24.989 3.538  1.00 49.06  ?  135 MET   B CG     1 
ATOM   8103  S  SD     . MET   B 1 110 ? 24.650  -23.313 4.157  1.00 50.51  ?  135 MET   B SD     1 
ATOM   8104  C  CE     . MET   B 1 110 ? 23.156  -22.889 3.266  1.00 50.68  ?  135 MET   B CE     1 
ATOM   8105  H  H      . MET   B 1 110 ? 24.591  -27.735 2.159  1.00 56.80  ?  135 MET   B H      1 
ATOM   8106  H  HA     . MET   B 1 110 ? 26.347  -26.250 0.781  1.00 56.04  ?  135 MET   B HA     1 
ATOM   8107  H  HB2    . MET   B 1 110 ? 26.432  -24.501 2.262  1.00 58.82  ?  135 MET   B HB2    1 
ATOM   8108  H  HB3    . MET   B 1 110 ? 25.001  -24.563 1.573  1.00 58.82  ?  135 MET   B HB3    1 
ATOM   8109  H  HG2    . MET   B 1 110 ? 24.103  -25.447 3.481  1.00 58.86  ?  135 MET   B HG2    1 
ATOM   8110  H  HG3    . MET   B 1 110 ? 25.535  -25.441 4.171  1.00 58.86  ?  135 MET   B HG3    1 
ATOM   8111  H  HE1    . MET   B 1 110 ? 22.889  -21.989 3.507  1.00 60.81  ?  135 MET   B HE1    1 
ATOM   8112  H  HE2    . MET   B 1 110 ? 23.333  -22.938 2.313  1.00 60.81  ?  135 MET   B HE2    1 
ATOM   8113  H  HE3    . MET   B 1 110 ? 22.457  -23.517 3.505  1.00 60.81  ?  135 MET   B HE3    1 
ATOM   8114  N  N      . TYR   B 1 111 ? 28.136  -26.718 2.581  1.00 43.30  ?  136 TYR   B N      1 
ATOM   8115  C  CA     . TYR   B 1 111 ? 29.127  -27.369 3.429  1.00 42.89  ?  136 TYR   B CA     1 
ATOM   8116  C  C      . TYR   B 1 111 ? 28.741  -27.214 4.893  1.00 41.77  ?  136 TYR   B C      1 
ATOM   8117  O  O      . TYR   B 1 111 ? 28.285  -26.150 5.325  1.00 41.16  ?  136 TYR   B O      1 
ATOM   8118  C  CB     . TYR   B 1 111 ? 30.515  -26.794 3.163  1.00 44.16  ?  136 TYR   B CB     1 
ATOM   8119  C  CG     . TYR   B 1 111 ? 31.229  -27.528 2.045  1.00 47.24  ?  136 TYR   B CG     1 
ATOM   8120  C  CD1    . TYR   B 1 111 ? 30.834  -27.367 0.726  1.00 48.03  ?  136 TYR   B CD1    1 
ATOM   8121  C  CD2    . TYR   B 1 111 ? 32.284  -28.394 2.314  1.00 48.55  ?  136 TYR   B CD2    1 
ATOM   8122  C  CE1    . TYR   B 1 111 ? 31.474  -28.040 -0.298 1.00 48.32  ?  136 TYR   B CE1    1 
ATOM   8123  C  CE2    . TYR   B 1 111 ? 32.928  -29.072 1.298  1.00 50.18  ?  136 TYR   B CE2    1 
ATOM   8124  C  CZ     . TYR   B 1 111 ? 32.521  -28.889 -0.005 1.00 50.36  ?  136 TYR   B CZ     1 
ATOM   8125  O  OH     . TYR   B 1 111 ? 33.163  -29.558 -1.017 1.00 52.41  ?  136 TYR   B OH     1 
ATOM   8126  H  H      . TYR   B 1 111 ? 28.434  -26.052 2.126  1.00 51.95  ?  136 TYR   B H      1 
ATOM   8127  H  HA     . TYR   B 1 111 ? 29.165  -28.317 3.225  1.00 51.46  ?  136 TYR   B HA     1 
ATOM   8128  H  HB2    . TYR   B 1 111 ? 30.431  -25.862 2.909  1.00 52.99  ?  136 TYR   B HB2    1 
ATOM   8129  H  HB3    . TYR   B 1 111 ? 31.051  -26.871 3.968  1.00 52.99  ?  136 TYR   B HB3    1 
ATOM   8130  H  HD1    . TYR   B 1 111 ? 30.127  -26.798 0.526  1.00 57.62  ?  136 TYR   B HD1    1 
ATOM   8131  H  HD2    . TYR   B 1 111 ? 32.561  -28.518 3.193  1.00 58.25  ?  136 TYR   B HD2    1 
ATOM   8132  H  HE1    . TYR   B 1 111 ? 31.200  -27.921 -1.178 1.00 57.97  ?  136 TYR   B HE1    1 
ATOM   8133  H  HE2    . TYR   B 1 111 ? 33.632  -29.648 1.492  1.00 60.21  ?  136 TYR   B HE2    1 
ATOM   8134  H  HH     . TYR   B 1 111 ? 33.768  -30.047 -0.700 1.00 62.88  ?  136 TYR   B HH     1 
ATOM   8135  N  N      . VAL   B 1 112 ? 28.914  -28.296 5.656  1.00 40.31  ?  137 VAL   B N      1 
ATOM   8136  C  CA     . VAL   B 1 112 ? 28.388  -28.337 7.022  1.00 38.36  ?  137 VAL   B CA     1 
ATOM   8137  C  C      . VAL   B 1 112 ? 28.858  -27.150 7.859  1.00 37.69  ?  137 VAL   B C      1 
ATOM   8138  O  O      . VAL   B 1 112 ? 28.033  -26.569 8.579  1.00 36.02  ?  137 VAL   B O      1 
ATOM   8139  C  CB     . VAL   B 1 112 ? 28.720  -29.688 7.675  1.00 38.43  ?  137 VAL   B CB     1 
ATOM   8140  C  CG1    . VAL   B 1 112 ? 28.392  -29.644 9.172  1.00 36.21  ?  137 VAL   B CG1    1 
ATOM   8141  C  CG2    . VAL   B 1 112 ? 27.958  -30.821 6.985  1.00 40.20  ?  137 VAL   B CG2    1 
ATOM   8142  H  H      . VAL   B 1 112 ? 29.326  -29.010 5.410  1.00 48.36  ?  137 VAL   B H      1 
ATOM   8143  H  HA     . VAL   B 1 112 ? 27.422  -28.278 6.960  1.00 46.03  ?  137 VAL   B HA     1 
ATOM   8144  H  HB     . VAL   B 1 112 ? 29.668  -29.865 7.575  1.00 46.11  ?  137 VAL   B HB     1 
ATOM   8145  H  HG11   . VAL   B 1 112 ? 28.354  -30.551 9.514  1.00 43.45  ?  137 VAL   B HG11   1 
ATOM   8146  H  HG12   . VAL   B 1 112 ? 29.086  -29.146 9.633  1.00 43.45  ?  137 VAL   B HG12   1 
ATOM   8147  H  HG13   . VAL   B 1 112 ? 27.535  -29.208 9.295  1.00 43.45  ?  137 VAL   B HG13   1 
ATOM   8148  H  HG21   . VAL   B 1 112 ? 28.186  -31.661 7.412  1.00 48.23  ?  137 VAL   B HG21   1 
ATOM   8149  H  HG22   . VAL   B 1 112 ? 27.005  -30.656 7.067  1.00 48.23  ?  137 VAL   B HG22   1 
ATOM   8150  H  HG23   . VAL   B 1 112 ? 28.210  -30.847 6.049  1.00 48.23  ?  137 VAL   B HG23   1 
ATOM   8151  N  N      . PRO   B 1 113 ? 30.141  -26.766 7.853  1.00 37.98  ?  138 PRO   B N      1 
ATOM   8152  C  CA     . PRO   B 1 113 ? 30.544  -25.614 8.682  1.00 38.44  ?  138 PRO   B CA     1 
ATOM   8153  C  C      . PRO   B 1 113 ? 29.827  -24.329 8.306  1.00 38.11  ?  138 PRO   B C      1 
ATOM   8154  O  O      . PRO   B 1 113 ? 29.526  -23.513 9.185  1.00 37.42  ?  138 PRO   B O      1 
ATOM   8155  C  CB     . PRO   B 1 113 ? 32.059  -25.515 8.438  1.00 38.20  ?  138 PRO   B CB     1 
ATOM   8156  C  CG     . PRO   B 1 113 ? 32.462  -26.903 8.038  1.00 38.49  ?  138 PRO   B CG     1 
ATOM   8157  C  CD     . PRO   B 1 113 ? 31.303  -27.408 7.205  1.00 39.39  ?  138 PRO   B CD     1 
ATOM   8158  H  HA     . PRO   B 1 113 ? 30.383  -25.813 9.618  1.00 46.13  ?  138 PRO   B HA     1 
ATOM   8159  H  HB2    . PRO   B 1 113 ? 32.241  -24.879 7.728  1.00 45.83  ?  138 PRO   B HB2    1 
ATOM   8160  H  HB3    . PRO   B 1 113 ? 32.510  -25.241 9.252  1.00 45.83  ?  138 PRO   B HB3    1 
ATOM   8161  H  HG2    . PRO   B 1 113 ? 33.279  -26.874 7.516  1.00 46.18  ?  138 PRO   B HG2    1 
ATOM   8162  H  HG3    . PRO   B 1 113 ? 32.590  -27.452 8.826  1.00 46.18  ?  138 PRO   B HG3    1 
ATOM   8163  H  HD2    . PRO   B 1 113 ? 31.388  -27.124 6.281  1.00 47.26  ?  138 PRO   B HD2    1 
ATOM   8164  H  HD3    . PRO   B 1 113 ? 31.237  -28.375 7.251  1.00 47.26  ?  138 PRO   B HD3    1 
ATOM   8165  N  N      . ALA   B 1 114 ? 29.553  -24.116 7.015  1.00 38.74  ?  139 ALA   B N      1 
ATOM   8166  C  CA     . ALA   B 1 114 ? 28.830  -22.915 6.603  1.00 38.23  ?  139 ALA   B CA     1 
ATOM   8167  C  C      . ALA   B 1 114 ? 27.375  -22.970 7.059  1.00 37.30  ?  139 ALA   B C      1 
ATOM   8168  O  O      . ALA   B 1 114 ? 26.804  -21.950 7.463  1.00 37.16  ?  139 ALA   B O      1 
ATOM   8169  C  CB     . ALA   B 1 114 ? 28.924  -22.747 5.084  1.00 38.32  ?  139 ALA   B CB     1 
ATOM   8170  H  H      . ALA   B 1 114 ? 29.772  -24.643 6.372  1.00 46.48  ?  139 ALA   B H      1 
ATOM   8171  H  HA     . ALA   B 1 114 ? 29.241  -22.138 7.012  1.00 45.87  ?  139 ALA   B HA     1 
ATOM   8172  H  HB1    . ALA   B 1 114 ? 28.443  -21.946 4.825  1.00 45.98  ?  139 ALA   B HB1    1 
ATOM   8173  H  HB2    . ALA   B 1 114 ? 29.858  -22.669 4.832  1.00 45.98  ?  139 ALA   B HB2    1 
ATOM   8174  H  HB3    . ALA   B 1 114 ? 28.530  -23.523 4.656  1.00 45.98  ?  139 ALA   B HB3    1 
ATOM   8175  N  N      . LEU   B 1 115 ? 26.765  -24.157 7.012  1.00 36.10  ?  140 LEU   B N      1 
ATOM   8176  C  CA     . LEU   B 1 115 ? 25.394  -24.308 7.486  1.00 35.28  ?  140 LEU   B CA     1 
ATOM   8177  C  C      . LEU   B 1 115 ? 25.280  -23.938 8.956  1.00 33.52  ?  140 LEU   B C      1 
ATOM   8178  O  O      . LEU   B 1 115 ? 24.397  -23.167 9.350  1.00 33.97  ?  140 LEU   B O      1 
ATOM   8179  C  CB     . LEU   B 1 115 ? 24.919  -25.744 7.271  1.00 35.36  ?  140 LEU   B CB     1 
ATOM   8180  C  CG     . LEU   B 1 115 ? 23.591  -26.160 7.901  1.00 36.83  ?  140 LEU   B CG     1 
ATOM   8181  C  CD1    . LEU   B 1 115 ? 22.444  -25.483 7.180  1.00 37.45  ?  140 LEU   B CD1    1 
ATOM   8182  C  CD2    . LEU   B 1 115 ? 23.413  -27.673 7.868  1.00 36.92  ?  140 LEU   B CD2    1 
ATOM   8183  H  H      . LEU   B 1 115 ? 27.120  -24.881 6.713  1.00 43.31  ?  140 LEU   B H      1 
ATOM   8184  H  HA     . LEU   B 1 115 ? 24.824  -23.714 6.973  1.00 42.33  ?  140 LEU   B HA     1 
ATOM   8185  H  HB2    . LEU   B 1 115 ? 24.831  -25.886 6.316  1.00 42.43  ?  140 LEU   B HB2    1 
ATOM   8186  H  HB3    . LEU   B 1 115 ? 25.597  -26.336 7.633  1.00 42.43  ?  140 LEU   B HB3    1 
ATOM   8187  H  HG     . LEU   B 1 115 ? 23.586  -25.885 8.831  1.00 44.19  ?  140 LEU   B HG     1 
ATOM   8188  H  HD11   . LEU   B 1 115 ? 21.609  -25.752 7.592  1.00 44.93  ?  140 LEU   B HD11   1 
ATOM   8189  H  HD12   . LEU   B 1 115 ? 22.552  -24.521 7.248  1.00 44.93  ?  140 LEU   B HD12   1 
ATOM   8190  H  HD13   . LEU   B 1 115 ? 22.455  -25.751 6.248  1.00 44.93  ?  140 LEU   B HD13   1 
ATOM   8191  H  HD21   . LEU   B 1 115 ? 22.567  -27.900 8.282  1.00 44.30  ?  140 LEU   B HD21   1 
ATOM   8192  H  HD22   . LEU   B 1 115 ? 23.421  -27.971 6.945  1.00 44.30  ?  140 LEU   B HD22   1 
ATOM   8193  H  HD23   . LEU   B 1 115 ? 24.142  -28.087 8.355  1.00 44.30  ?  140 LEU   B HD23   1 
ATOM   8194  N  N      . ILE   B 1 116 ? 26.163  -24.490 9.793  1.00 33.07  ?  141 ILE   B N      1 
ATOM   8195  C  CA     . ILE   B 1 116 ? 25.929  -24.423 11.236 1.00 30.84  ?  141 ILE   B CA     1 
ATOM   8196  C  C      . ILE   B 1 116 ? 26.526  -23.178 11.878 1.00 31.64  ?  141 ILE   B C      1 
ATOM   8197  O  O      . ILE   B 1 116 ? 26.255  -22.911 13.060 1.00 30.76  ?  141 ILE   B O      1 
ATOM   8198  C  CB     . ILE   B 1 116 ? 26.433  -25.702 11.945 1.00 32.33  ?  141 ILE   B CB     1 
ATOM   8199  C  CG1    . ILE   B 1 116 ? 27.958  -25.817 11.924 1.00 32.72  ?  141 ILE   B CG1    1 
ATOM   8200  C  CG2    . ILE   B 1 116 ? 25.776  -26.941 11.320 1.00 33.08  ?  141 ILE   B CG2    1 
ATOM   8201  C  CD1    . ILE   B 1 116 ? 28.484  -27.150 12.465 1.00 33.14  ?  141 ILE   B CD1    1 
ATOM   8202  H  H      . ILE   B 1 116 ? 26.883  -24.896 9.556  1.00 39.68  ?  141 ILE   B H      1 
ATOM   8203  H  HA     . ILE   B 1 116 ? 24.971  -24.376 11.380 1.00 37.00  ?  141 ILE   B HA     1 
ATOM   8204  H  HB     . ILE   B 1 116 ? 26.175  -25.640 12.878 1.00 38.79  ?  141 ILE   B HB     1 
ATOM   8205  H  HG12   . ILE   B 1 116 ? 28.264  -25.728 11.008 1.00 39.26  ?  141 ILE   B HG12   1 
ATOM   8206  H  HG13   . ILE   B 1 116 ? 28.332  -25.108 12.469 1.00 39.26  ?  141 ILE   B HG13   1 
ATOM   8207  H  HG21   . ILE   B 1 116 ? 25.896  -27.697 11.916 1.00 39.69  ?  141 ILE   B HG21   1 
ATOM   8208  H  HG22   . ILE   B 1 116 ? 24.831  -26.767 11.192 1.00 39.69  ?  141 ILE   B HG22   1 
ATOM   8209  H  HG23   . ILE   B 1 116 ? 26.197  -27.125 10.465 1.00 39.69  ?  141 ILE   B HG23   1 
ATOM   8210  H  HD11   . ILE   B 1 116 ? 29.439  -27.073 12.618 1.00 39.76  ?  141 ILE   B HD11   1 
ATOM   8211  H  HD12   . ILE   B 1 116 ? 28.031  -27.353 13.298 1.00 39.76  ?  141 ILE   B HD12   1 
ATOM   8212  H  HD13   . ILE   B 1 116 ? 28.309  -27.847 11.814 1.00 39.76  ?  141 ILE   B HD13   1 
ATOM   8213  N  N      . PHE   B 1 117 ? 27.287  -22.379 11.137 1.00 30.97  ?  142 PHE   B N      1 
ATOM   8214  C  CA     . PHE   B 1 117 ? 27.738  -21.090 11.634 1.00 30.21  ?  142 PHE   B CA     1 
ATOM   8215  C  C      . PHE   B 1 117 ? 27.091  -19.914 10.924 1.00 30.67  ?  142 PHE   B C      1 
ATOM   8216  O  O      . PHE   B 1 117 ? 27.196  -18.788 11.420 1.00 30.76  ?  142 PHE   B O      1 
ATOM   8217  C  CB     . PHE   B 1 117 ? 29.266  -20.978 11.523 1.00 29.54  ?  142 PHE   B CB     1 
ATOM   8218  C  CG     . PHE   B 1 117 ? 29.990  -21.775 12.562 1.00 31.04  ?  142 PHE   B CG     1 
ATOM   8219  C  CD1    . PHE   B 1 117 ? 30.234  -21.240 13.818 1.00 31.51  ?  142 PHE   B CD1    1 
ATOM   8220  C  CD2    . PHE   B 1 117 ? 30.397  -23.072 12.300 1.00 32.40  ?  142 PHE   B CD2    1 
ATOM   8221  C  CE1    . PHE   B 1 117 ? 30.888  -21.980 14.789 1.00 32.26  ?  142 PHE   B CE1    1 
ATOM   8222  C  CE2    . PHE   B 1 117 ? 31.046  -23.818 13.272 1.00 33.88  ?  142 PHE   B CE2    1 
ATOM   8223  C  CZ     . PHE   B 1 117 ? 31.288  -23.272 14.517 1.00 33.03  ?  142 PHE   B CZ     1 
ATOM   8224  H  H      . PHE   B 1 117 ? 27.554  -22.564 10.341 1.00 37.15  ?  142 PHE   B H      1 
ATOM   8225  H  HA     . PHE   B 1 117 ? 27.511  -21.024 12.575 1.00 36.25  ?  142 PHE   B HA     1 
ATOM   8226  H  HB2    . PHE   B 1 117 ? 29.543  -21.301 10.652 1.00 35.45  ?  142 PHE   B HB2    1 
ATOM   8227  H  HB3    . PHE   B 1 117 ? 29.522  -20.048 11.629 1.00 35.45  ?  142 PHE   B HB3    1 
ATOM   8228  H  HD1    . PHE   B 1 117 ? 29.956  -20.374 14.011 1.00 37.80  ?  142 PHE   B HD1    1 
ATOM   8229  H  HD2    . PHE   B 1 117 ? 30.234  -23.446 11.465 1.00 38.87  ?  142 PHE   B HD2    1 
ATOM   8230  H  HE1    . PHE   B 1 117 ? 31.057  -21.606 15.624 1.00 38.71  ?  142 PHE   B HE1    1 
ATOM   8231  H  HE2    . PHE   B 1 117 ? 31.319  -24.687 13.085 1.00 40.65  ?  142 PHE   B HE2    1 
ATOM   8232  H  HZ     . PHE   B 1 117 ? 31.720  -23.774 15.170 1.00 39.63  ?  142 PHE   B HZ     1 
ATOM   8233  N  N      . GLY   B 1 118 ? 26.417  -20.143 9.795  1.00 31.37  ?  143 GLY   B N      1 
ATOM   8234  C  CA     . GLY   B 1 118 ? 25.901  -19.045 9.008  1.00 31.43  ?  143 GLY   B CA     1 
ATOM   8235  C  C      . GLY   B 1 118 ? 24.408  -19.045 8.757  1.00 32.52  ?  143 GLY   B C      1 
ATOM   8236  O  O      . GLY   B 1 118 ? 23.898  -18.106 8.133  1.00 34.88  ?  143 GLY   B O      1 
ATOM   8237  H  H      . GLY   B 1 118 ? 26.252  -20.923 9.473  1.00 37.63  ?  143 GLY   B H      1 
ATOM   8238  H  HA2    . GLY   B 1 118 ? 26.118  -18.216 9.461  1.00 37.71  ?  143 GLY   B HA2    1 
ATOM   8239  H  HA3    . GLY   B 1 118 ? 26.339  -19.057 8.143  1.00 37.71  ?  143 GLY   B HA3    1 
ATOM   8240  N  N      . GLN   B 1 119 ? 23.704  -20.086 9.209  1.00 31.54  ?  144 GLN   B N      1 
ATOM   8241  C  CA     . GLN   B 1 119 ? 22.254  -20.185 9.093  1.00 31.80  ?  144 GLN   B CA     1 
ATOM   8242  C  C      . GLN   B 1 119 ? 21.638  -20.349 10.475 1.00 30.47  ?  144 GLN   B C      1 
ATOM   8243  O  O      . GLN   B 1 119 ? 22.080  -21.197 11.257 1.00 29.07  ?  144 GLN   B O      1 
ATOM   8244  C  CB     . GLN   B 1 119 ? 21.840  -21.377 8.219  1.00 33.65  ?  144 GLN   B CB     1 
ATOM   8245  C  CG     . GLN   B 1 119 ? 22.472  -21.384 6.835  1.00 37.18  ?  144 GLN   B CG     1 
ATOM   8246  C  CD     . GLN   B 1 119 ? 22.011  -20.226 5.989  1.00 41.64  ?  144 GLN   B CD     1 
ATOM   8247  O  OE1    . GLN   B 1 119 ? 20.826  -19.900 5.962  1.00 44.12  ?  144 GLN   B OE1    1 
ATOM   8248  N  NE2    . GLN   B 1 119 ? 22.945  -19.585 5.306  1.00 43.12  ?  144 GLN   B NE2    1 
ATOM   8249  H  H      . GLN   B 1 119 ? 24.058  -20.766 9.598  1.00 37.84  ?  144 GLN   B H      1 
ATOM   8250  H  HA     . GLN   B 1 119 ? 21.921  -19.367 8.692  1.00 38.15  ?  144 GLN   B HA     1 
ATOM   8251  H  HB2    . GLN   B 1 119 ? 22.103  -22.197 8.667  1.00 40.37  ?  144 GLN   B HB2    1 
ATOM   8252  H  HB3    . GLN   B 1 119 ? 20.877  -21.357 8.103  1.00 40.37  ?  144 GLN   B HB3    1 
ATOM   8253  H  HG2    . GLN   B 1 119 ? 23.436  -21.327 6.925  1.00 44.61  ?  144 GLN   B HG2    1 
ATOM   8254  H  HG3    . GLN   B 1 119 ? 22.230  -22.206 6.379  1.00 44.61  ?  144 GLN   B HG3    1 
ATOM   8255  H  HE21   . GLN   B 1 119 ? 23.766  -19.837 5.359  1.00 51.74  ?  144 GLN   B HE21   1 
ATOM   8256  H  HE22   . GLN   B 1 119 ? 22.732  -18.916 4.808  1.00 51.74  ?  144 GLN   B HE22   1 
ATOM   8257  N  N      . LEU   B 1 120 ? 20.602  -19.565 10.763 1.00 30.45  ?  145 LEU   B N      1 
ATOM   8258  C  CA     . LEU   B 1 120 ? 19.929  -19.674 12.048 1.00 28.79  ?  145 LEU   B CA     1 
ATOM   8259  C  C      . LEU   B 1 120 ? 19.193  -20.999 12.196 1.00 28.78  ?  145 LEU   B C      1 
ATOM   8260  O  O      . LEU   B 1 120 ? 18.712  -21.592 11.223 1.00 28.14  ?  145 LEU   B O      1 
ATOM   8261  C  CB     . LEU   B 1 120 ? 18.929  -18.538 12.232 1.00 28.05  ?  145 LEU   B CB     1 
ATOM   8262  C  CG     . LEU   B 1 120 ? 19.552  -17.149 12.312 1.00 27.99  ?  145 LEU   B CG     1 
ATOM   8263  C  CD1    . LEU   B 1 120 ? 18.461  -16.111 12.178 1.00 29.12  ?  145 LEU   B CD1    1 
ATOM   8264  C  CD2    . LEU   B 1 120 ? 20.288  -16.980 13.619 1.00 29.87  ?  145 LEU   B CD2    1 
ATOM   8265  H  H      . LEU   B 1 120 ? 20.276  -18.969 10.236 1.00 36.54  ?  145 LEU   B H      1 
ATOM   8266  H  HA     . LEU   B 1 120 ? 20.605  -19.620 12.742 1.00 34.54  ?  145 LEU   B HA     1 
ATOM   8267  H  HB2    . LEU   B 1 120 ? 18.318  -18.542 11.479 1.00 33.65  ?  145 LEU   B HB2    1 
ATOM   8268  H  HB3    . LEU   B 1 120 ? 18.442  -18.688 13.057 1.00 33.65  ?  145 LEU   B HB3    1 
ATOM   8269  H  HG     . LEU   B 1 120 ? 20.192  -17.028 11.594 1.00 33.58  ?  145 LEU   B HG     1 
ATOM   8270  H  HD11   . LEU   B 1 120 ? 18.855  -15.228 12.249 1.00 34.94  ?  145 LEU   B HD11   1 
ATOM   8271  H  HD12   . LEU   B 1 120 ? 18.032  -16.214 11.314 1.00 34.94  ?  145 LEU   B HD12   1 
ATOM   8272  H  HD13   . LEU   B 1 120 ? 17.812  -16.242 12.887 1.00 34.94  ?  145 LEU   B HD13   1 
ATOM   8273  H  HD21   . LEU   B 1 120 ? 20.617  -16.070 13.681 1.00 35.84  ?  145 LEU   B HD21   1 
ATOM   8274  H  HD22   . LEU   B 1 120 ? 19.678  -17.162 14.351 1.00 35.84  ?  145 LEU   B HD22   1 
ATOM   8275  H  HD23   . LEU   B 1 120 ? 21.031  -17.603 13.645 1.00 35.84  ?  145 LEU   B HD23   1 
ATOM   8276  N  N      . LEU   B 1 121 ? 19.096  -21.451 13.454 1.00 27.95  ?  146 LEU   B N      1 
ATOM   8277  C  CA     . LEU   B 1 121 ? 18.323  -22.637 13.833 1.00 27.58  ?  146 LEU   B CA     1 
ATOM   8278  C  C      . LEU   B 1 121 ? 18.936  -23.901 13.225 1.00 27.61  ?  146 LEU   B C      1 
ATOM   8279  O  O      . LEU   B 1 121 ? 18.249  -24.721 12.605 1.00 28.34  ?  146 LEU   B O      1 
ATOM   8280  C  CB     . LEU   B 1 121 ? 16.849  -22.484 13.453 1.00 27.83  ?  146 LEU   B CB     1 
ATOM   8281  C  CG     . LEU   B 1 121 ? 16.192  -21.188 13.935 1.00 29.51  ?  146 LEU   B CG     1 
ATOM   8282  C  CD1    . LEU   B 1 121 ? 14.714  -21.174 13.552 1.00 31.07  ?  146 LEU   B CD1    1 
ATOM   8283  C  CD2    . LEU   B 1 121 ? 16.352  -20.955 15.428 1.00 29.96  ?  146 LEU   B CD2    1 
ATOM   8284  H  H      . LEU   B 1 121 ? 19.480  -21.074 14.124 1.00 33.53  ?  146 LEU   B H      1 
ATOM   8285  H  HA     . LEU   B 1 121 ? 18.362  -22.740 14.797 1.00 33.09  ?  146 LEU   B HA     1 
ATOM   8286  H  HB2    . LEU   B 1 121 ? 16.778  -22.505 12.485 1.00 33.39  ?  146 LEU   B HB2    1 
ATOM   8287  H  HB3    . LEU   B 1 121 ? 16.354  -23.223 13.838 1.00 33.39  ?  146 LEU   B HB3    1 
ATOM   8288  H  HG     . LEU   B 1 121 ? 16.647  -20.454 13.495 1.00 35.40  ?  146 LEU   B HG     1 
ATOM   8289  H  HD11   . LEU   B 1 121 ? 14.314  -20.348 13.867 1.00 37.28  ?  146 LEU   B HD11   1 
ATOM   8290  H  HD12   . LEU   B 1 121 ? 14.637  -21.232 12.587 1.00 37.28  ?  146 LEU   B HD12   1 
ATOM   8291  H  HD13   . LEU   B 1 121 ? 14.273  -21.932 13.966 1.00 37.28  ?  146 LEU   B HD13   1 
ATOM   8292  H  HD21   . LEU   B 1 121 ? 15.804  -20.199 15.690 1.00 35.95  ?  146 LEU   B HD21   1 
ATOM   8293  H  HD22   . LEU   B 1 121 ? 16.067  -21.751 15.904 1.00 35.95  ?  146 LEU   B HD22   1 
ATOM   8294  H  HD23   . LEU   B 1 121 ? 17.284  -20.771 15.621 1.00 35.95  ?  146 LEU   B HD23   1 
ATOM   8295  N  N      . THR   B 1 122 ? 20.241  -24.054 13.432 1.00 26.29  ?  147 THR   B N      1 
ATOM   8296  C  CA     . THR   B 1 122 ? 21.000  -25.209 12.977 1.00 25.20  ?  147 THR   B CA     1 
ATOM   8297  C  C      . THR   B 1 122 ? 21.768  -25.793 14.150 1.00 26.18  ?  147 THR   B C      1 
ATOM   8298  O  O      . THR   B 1 122 ? 22.431  -25.055 14.882 1.00 26.46  ?  147 THR   B O      1 
ATOM   8299  C  CB     . THR   B 1 122 ? 21.976  -24.833 11.854 1.00 26.17  ?  147 THR   B CB     1 
ATOM   8300  O  OG1    . THR   B 1 122 ? 22.789  -23.716 12.247 1.00 27.07  ?  147 THR   B OG1    1 
ATOM   8301  C  CG2    . THR   B 1 122 ? 21.203  -24.481 10.595 1.00 27.96  ?  147 THR   B CG2    1 
ATOM   8302  H  H      . THR   B 1 122 ? 20.725  -23.478 13.850 1.00 31.54  ?  147 THR   B H      1 
ATOM   8303  H  HA     . THR   B 1 122 ? 20.387  -25.881 12.640 1.00 30.24  ?  147 THR   B HA     1 
ATOM   8304  H  HB     . THR   B 1 122 ? 22.558  -25.586 11.667 1.00 31.40  ?  147 THR   B HB     1 
ATOM   8305  H  HG1    . THR   B 1 122 ? 22.304  -23.050 12.410 1.00 32.48  ?  147 THR   B HG1    1 
ATOM   8306  H  HG21   . THR   B 1 122 ? 21.817  -24.242 9.884  1.00 33.55  ?  147 THR   B HG21   1 
ATOM   8307  H  HG22   . THR   B 1 122 ? 20.670  -25.240 10.309 1.00 33.55  ?  147 THR   B HG22   1 
ATOM   8308  H  HG23   . THR   B 1 122 ? 20.613  -23.730 10.767 1.00 33.55  ?  147 THR   B HG23   1 
ATOM   8309  N  N      . SER   B 1 123 ? 21.720  -27.117 14.302 1.00 23.93  ?  148 SER   B N      1 
ATOM   8310  C  CA     . SER   B 1 123 ? 22.238  -27.732 15.520 1.00 23.27  ?  148 SER   B CA     1 
ATOM   8311  C  C      . SER   B 1 123 ? 22.414  -29.228 15.322 1.00 24.14  ?  148 SER   B C      1 
ATOM   8312  O  O      . SER   B 1 123 ? 21.698  -29.846 14.526 1.00 24.67  ?  148 SER   B O      1 
ATOM   8313  C  CB     . SER   B 1 123 ? 21.285  -27.489 16.702 1.00 21.87  ?  148 SER   B CB     1 
ATOM   8314  O  OG     . SER   B 1 123 ? 21.839  -27.951 17.921 1.00 22.22  ?  148 SER   B OG     1 
ATOM   8315  H  H      . SER   B 1 123 ? 21.399  -27.667 13.725 1.00 28.71  ?  148 SER   B H      1 
ATOM   8316  H  HA     . SER   B 1 123 ? 23.111  -27.352 15.709 1.00 27.92  ?  148 SER   B HA     1 
ATOM   8317  H  HB2    . SER   B 1 123 ? 21.115  -26.537 16.776 1.00 26.23  ?  148 SER   B HB2    1 
ATOM   8318  H  HB3    . SER   B 1 123 ? 20.455  -27.963 16.536 1.00 26.23  ?  148 SER   B HB3    1 
ATOM   8319  H  HG     . SER   B 1 123 ? 22.564  -27.556 18.075 1.00 26.66  ?  148 SER   B HG     1 
ATOM   8320  N  N      . SER   B 1 124 ? 23.351  -29.803 16.079 1.00 24.80  ?  149 SER   B N      1 
ATOM   8321  C  CA     . SER   B 1 124 ? 23.435  -31.246 16.273 1.00 25.73  ?  149 SER   B CA     1 
ATOM   8322  C  C      . SER   B 1 124 ? 22.702  -31.704 17.536 1.00 23.98  ?  149 SER   B C      1 
ATOM   8323  O  O      . SER   B 1 124 ? 22.752  -32.894 17.878 1.00 24.43  ?  149 SER   B O      1 
ATOM   8324  C  CB     . SER   B 1 124 ? 24.906  -31.689 16.322 1.00 25.88  ?  149 SER   B CB     1 
ATOM   8325  O  OG     . SER   B 1 124 ? 25.628  -31.111 17.402 1.00 26.20  ?  149 SER   B OG     1 
ATOM   8326  H  H      . SER   B 1 124 ? 23.961  -29.365 16.499 1.00 29.75  ?  149 SER   B H      1 
ATOM   8327  H  HA     . SER   B 1 124 ? 23.025  -31.690 15.514 1.00 30.87  ?  149 SER   B HA     1 
ATOM   8328  H  HB2    . SER   B 1 124 ? 24.933  -32.654 16.417 1.00 31.05  ?  149 SER   B HB2    1 
ATOM   8329  H  HB3    . SER   B 1 124 ? 25.334  -31.425 15.492 1.00 31.05  ?  149 SER   B HB3    1 
ATOM   8330  H  HG     . SER   B 1 124 ? 25.630  -30.274 17.331 1.00 31.43  ?  149 SER   B HG     1 
ATOM   8331  N  N      . ASN   B 1 125 ? 21.990  -30.787 18.206 1.00 23.14  ?  150 ASN   B N      1 
ATOM   8332  C  CA     . ASN   B 1 125 ? 21.327  -31.044 19.480 1.00 21.53  ?  150 ASN   B CA     1 
ATOM   8333  C  C      . ASN   B 1 125 ? 19.804  -31.046 19.379 1.00 23.25  ?  150 ASN   B C      1 
ATOM   8334  O  O      . ASN   B 1 125 ? 19.120  -30.890 20.398 1.00 23.92  ?  150 ASN   B O      1 
ATOM   8335  C  CB     . ASN   B 1 125 ? 21.814  -30.011 20.489 1.00 22.13  ?  150 ASN   B CB     1 
ATOM   8336  C  CG     . ASN   B 1 125 ? 23.257  -30.226 20.856 1.00 22.26  ?  150 ASN   B CG     1 
ATOM   8337  O  OD1    . ASN   B 1 125 ? 23.599  -31.246 21.450 1.00 23.58  ?  150 ASN   B OD1    1 
ATOM   8338  N  ND2    . ASN   B 1 125 ? 24.125  -29.304 20.457 1.00 23.27  ?  150 ASN   B ND2    1 
ATOM   8339  H  H      . ASN   B 1 125 ? 21.876  -29.982 17.928 1.00 27.76  ?  150 ASN   B H      1 
ATOM   8340  H  HA     . ASN   B 1 125 ? 21.565  -31.930 19.794 1.00 25.83  ?  150 ASN   B HA     1 
ATOM   8341  H  HB2    . ASN   B 1 125 ? 21.727  -29.124 20.105 1.00 26.55  ?  150 ASN   B HB2    1 
ATOM   8342  H  HB3    . ASN   B 1 125 ? 21.282  -30.077 21.297 1.00 26.55  ?  150 ASN   B HB3    1 
ATOM   8343  H  HD21   . ASN   B 1 125 ? 24.959  -29.389 20.646 1.00 27.92  ?  150 ASN   B HD21   1 
ATOM   8344  H  HD22   . ASN   B 1 125 ? 23.852  -28.622 20.010 1.00 27.92  ?  150 ASN   B HD22   1 
ATOM   8345  N  N      . TYR   B 1 126 ? 19.255  -31.278 18.183 1.00 22.51  ?  151 TYR   B N      1 
ATOM   8346  C  CA     . TYR   B 1 126 ? 17.812  -31.228 18.003 1.00 22.34  ?  151 TYR   B CA     1 
ATOM   8347  C  C      . TYR   B 1 126 ? 17.111  -32.581 18.148 1.00 23.74  ?  151 TYR   B C      1 
ATOM   8348  O  O      . TYR   B 1 126 ? 15.877  -32.612 18.131 1.00 25.85  ?  151 TYR   B O      1 
ATOM   8349  C  CB     . TYR   B 1 126 ? 17.462  -30.643 16.629 1.00 21.43  ?  151 TYR   B CB     1 
ATOM   8350  C  CG     . TYR   B 1 126 ? 17.600  -29.136 16.479 1.00 22.81  ?  151 TYR   B CG     1 
ATOM   8351  C  CD1    . TYR   B 1 126 ? 17.439  -28.261 17.564 1.00 21.15  ?  151 TYR   B CD1    1 
ATOM   8352  C  CD2    . TYR   B 1 126 ? 17.877  -28.585 15.240 1.00 24.44  ?  151 TYR   B CD2    1 
ATOM   8353  C  CE1    . TYR   B 1 126 ? 17.560  -26.869 17.399 1.00 21.42  ?  151 TYR   B CE1    1 
ATOM   8354  C  CE2    . TYR   B 1 126 ? 17.999  -27.227 15.070 1.00 24.18  ?  151 TYR   B CE2    1 
ATOM   8355  C  CZ     . TYR   B 1 126 ? 17.834  -26.365 16.143 1.00 23.09  ?  151 TYR   B CZ     1 
ATOM   8356  O  OH     . TYR   B 1 126 ? 17.947  -25.006 15.946 1.00 25.68  ?  151 TYR   B OH     1 
ATOM   8357  H  H      . TYR   B 1 126 ? 19.698  -31.464 17.470 1.00 27.00  ?  151 TYR   B H      1 
ATOM   8358  H  HA     . TYR   B 1 126 ? 17.459  -30.641 18.690 1.00 26.80  ?  151 TYR   B HA     1 
ATOM   8359  H  HB2    . TYR   B 1 126 ? 18.048  -31.049 15.970 1.00 25.71  ?  151 TYR   B HB2    1 
ATOM   8360  H  HB3    . TYR   B 1 126 ? 16.538  -30.866 16.433 1.00 25.71  ?  151 TYR   B HB3    1 
ATOM   8361  H  HD1    . TYR   B 1 126 ? 17.251  -28.606 18.407 1.00 25.38  ?  151 TYR   B HD1    1 
ATOM   8362  H  HD2    . TYR   B 1 126 ? 17.984  -29.146 14.506 1.00 29.33  ?  151 TYR   B HD2    1 
ATOM   8363  H  HE1    . TYR   B 1 126 ? 17.457  -26.297 18.125 1.00 25.70  ?  151 TYR   B HE1    1 
ATOM   8364  H  HE2    . TYR   B 1 126 ? 18.194  -26.884 14.228 1.00 29.01  ?  151 TYR   B HE2    1 
ATOM   8365  H  HH     . TYR   B 1 126 ? 17.839  -24.601 16.674 1.00 30.80  ?  151 TYR   B HH     1 
ATOM   8366  N  N      . ASP   B 1 127 ? 17.838  -33.690 18.317 1.00 24.45  ?  152 ASP   B N      1 
ATOM   8367  C  CA     . ASP   B 1 127 ? 17.227  -35.014 18.478 1.00 26.36  ?  152 ASP   B CA     1 
ATOM   8368  C  C      . ASP   B 1 127 ? 17.348  -35.437 19.938 1.00 26.79  ?  152 ASP   B C      1 
ATOM   8369  O  O      . ASP   B 1 127 ? 18.379  -35.973 20.356 1.00 28.25  ?  152 ASP   B O      1 
ATOM   8370  C  CB     . ASP   B 1 127 ? 17.896  -36.040 17.559 1.00 29.52  ?  152 ASP   B CB     1 
ATOM   8371  C  CG     . ASP   B 1 127 ? 17.328  -37.445 17.722 1.00 33.38  ?  152 ASP   B CG     1 
ATOM   8372  O  OD1    . ASP   B 1 127 ? 16.397  -37.636 18.530 1.00 33.84  ?  152 ASP   B OD1    1 
ATOM   8373  O  OD2    . ASP   B 1 127 ? 17.824  -38.373 17.042 1.00 36.10  ?  152 ASP   B OD2    1 
ATOM   8374  H  H      . ASP   B 1 127 ? 18.697  -33.700 18.342 1.00 29.34  ?  152 ASP   B H      1 
ATOM   8375  H  HA     . ASP   B 1 127 ? 16.286  -34.949 18.253 1.00 31.63  ?  152 ASP   B HA     1 
ATOM   8376  H  HB2    . ASP   B 1 127 ? 17.766  -35.770 16.637 1.00 35.41  ?  152 ASP   B HB2    1 
ATOM   8377  H  HB3    . ASP   B 1 127 ? 18.844  -36.075 17.764 1.00 35.41  ?  152 ASP   B HB3    1 
ATOM   8378  N  N      . ASP   B 1 128 ? 16.293  -35.235 20.710 1.00 27.09  ?  153 ASP   B N      1 
ATOM   8379  C  CA     . ASP   B 1 128 ? 16.397  -35.511 22.136 1.00 27.37  ?  153 ASP   B CA     1 
ATOM   8380  C  C      . ASP   B 1 128 ? 16.165  -36.975 22.484 1.00 28.90  ?  153 ASP   B C      1 
ATOM   8381  O  O      . ASP   B 1 128 ? 16.148  -37.302 23.673 1.00 30.01  ?  153 ASP   B O      1 
ATOM   8382  C  CB     . ASP   B 1 128 ? 15.453  -34.594 22.909 1.00 29.17  ?  153 ASP   B CB     1 
ATOM   8383  C  CG     . ASP   B 1 128 ? 16.015  -33.185 23.044 1.00 32.11  ?  153 ASP   B CG     1 
ATOM   8384  O  OD1    . ASP   B 1 128 ? 17.156  -32.929 22.593 1.00 33.43  ?  153 ASP   B OD1    1 
ATOM   8385  O  OD2    . ASP   B 1 128 ? 15.324  -32.324 23.610 1.00 34.27  ?  153 ASP   B OD2    1 
ATOM   8386  H  H      . ASP   B 1 128 ? 15.529  -34.948 20.440 1.00 32.50  ?  153 ASP   B H      1 
ATOM   8387  H  HA     . ASP   B 1 128 ? 17.297  -35.305 22.433 1.00 32.84  ?  153 ASP   B HA     1 
ATOM   8388  H  HB2    . ASP   B 1 128 ? 14.605  -34.540 22.441 1.00 35.00  ?  153 ASP   B HB2    1 
ATOM   8389  H  HB3    . ASP   B 1 128 ? 15.317  -34.953 23.800 1.00 35.00  ?  153 ASP   B HB3    1 
ATOM   8390  N  N      . ASP   B 1 129 ? 16.024  -37.863 21.496 1.00 28.76  ?  154 ASP   B N      1 
ATOM   8391  C  CA     . ASP   B 1 129 ? 16.270  -39.279 21.755 1.00 30.57  ?  154 ASP   B CA     1 
ATOM   8392  C  C      . ASP   B 1 129 ? 17.730  -39.531 22.102 1.00 29.67  ?  154 ASP   B C      1 
ATOM   8393  O  O      . ASP   B 1 129 ? 18.041  -40.529 22.764 1.00 31.30  ?  154 ASP   B O      1 
ATOM   8394  C  CB     . ASP   B 1 129 ? 15.868  -40.117 20.542 1.00 34.41  ?  154 ASP   B CB     1 
ATOM   8395  C  CG     . ASP   B 1 129 ? 14.366  -40.232 20.383 1.00 40.71  ?  154 ASP   B CG     1 
ATOM   8396  O  OD1    . ASP   B 1 129 ? 13.620  -39.882 21.323 1.00 42.47  ?  154 ASP   B OD1    1 
ATOM   8397  O  OD2    . ASP   B 1 129 ? 13.931  -40.691 19.309 1.00 43.99  ?  154 ASP   B OD2    1 
ATOM   8398  H  H      . ASP   B 1 129 ? 15.793  -37.674 20.690 1.00 34.50  ?  154 ASP   B H      1 
ATOM   8399  H  HA     . ASP   B 1 129 ? 15.720  -39.568 22.500 1.00 36.68  ?  154 ASP   B HA     1 
ATOM   8400  H  HB2    . ASP   B 1 129 ? 16.224  -39.704 19.739 1.00 41.28  ?  154 ASP   B HB2    1 
ATOM   8401  H  HB3    . ASP   B 1 129 ? 16.228  -41.012 20.642 1.00 41.28  ?  154 ASP   B HB3    1 
ATOM   8402  N  N      . GLU   B 1 130 ? 18.620  -38.647 21.666 1.00 29.00  ?  155 GLU   B N      1 
ATOM   8403  C  CA     . GLU   B 1 130 ? 20.002  -38.657 22.110 1.00 29.26  ?  155 GLU   B CA     1 
ATOM   8404  C  C      . GLU   B 1 130 ? 20.059  -37.902 23.430 1.00 28.55  ?  155 GLU   B C      1 
ATOM   8405  O  O      . GLU   B 1 130 ? 19.702  -36.722 23.492 1.00 27.44  ?  155 GLU   B O      1 
ATOM   8406  C  CB     . GLU   B 1 130 ? 20.900  -38.022 21.057 1.00 31.94  ?  155 GLU   B CB     1 
ATOM   8407  C  CG     . GLU   B 1 130 ? 20.758  -38.687 19.689 1.00 35.83  ?  155 GLU   B CG     1 
ATOM   8408  C  CD     . GLU   B 1 130 ? 21.556  -37.994 18.604 1.00 39.13  ?  155 GLU   B CD     1 
ATOM   8409  O  OE1    . GLU   B 1 130 ? 22.245  -38.685 17.824 1.00 42.28  ?  155 GLU   B OE1    1 
ATOM   8410  O  OE2    . GLU   B 1 130 ? 21.490  -36.752 18.530 1.00 39.32  ?  155 GLU   B OE2    1 
ATOM   8411  H  H      . GLU   B 1 130 ? 18.442  -38.022 21.103 1.00 34.79  ?  155 GLU   B H      1 
ATOM   8412  H  HA     . GLU   B 1 130 ? 20.323  -39.563 22.245 1.00 35.11  ?  155 GLU   B HA     1 
ATOM   8413  H  HB2    . GLU   B 1 130 ? 20.665  -37.085 20.963 1.00 38.32  ?  155 GLU   B HB2    1 
ATOM   8414  H  HB3    . GLU   B 1 130 ? 21.825  -38.104 21.337 1.00 38.32  ?  155 GLU   B HB3    1 
ATOM   8415  H  HG2    . GLU   B 1 130 ? 21.070  -39.603 19.751 1.00 42.99  ?  155 GLU   B HG2    1 
ATOM   8416  H  HG3    . GLU   B 1 130 ? 19.823  -38.672 19.428 1.00 42.99  ?  155 GLU   B HG3    1 
ATOM   8417  N  N      . LYS   B 1 131 ? 20.468  -38.588 24.488 1.00 27.67  ?  156 LYS   B N      1 
ATOM   8418  C  CA     . LYS   B 1 131 ? 20.500  -37.996 25.824 1.00 24.98  ?  156 LYS   B CA     1 
ATOM   8419  C  C      . LYS   B 1 131 ? 21.894  -37.417 26.066 1.00 25.58  ?  156 LYS   B C      1 
ATOM   8420  O  O      . LYS   B 1 131 ? 22.771  -38.045 26.661 1.00 29.70  ?  156 LYS   B O      1 
ATOM   8421  C  CB     . LYS   B 1 131 ? 20.114  -39.043 26.859 1.00 26.42  ?  156 LYS   B CB     1 
ATOM   8422  C  CG     . LYS   B 1 131 ? 18.816  -39.762 26.539 1.00 30.40  ?  156 LYS   B CG     1 
ATOM   8423  C  CD     . LYS   B 1 131 ? 17.643  -38.800 26.497 1.00 32.06  ?  156 LYS   B CD     1 
ATOM   8424  C  CE     . LYS   B 1 131 ? 16.351  -39.542 26.172 1.00 34.26  ?  156 LYS   B CE     1 
ATOM   8425  N  NZ     . LYS   B 1 131 ? 15.181  -38.632 26.036 1.00 35.14  ?  156 LYS   B NZ     1 
ATOM   8426  H  H      . LYS   B 1 131 ? 20.734  -39.405 24.462 1.00 33.20  ?  156 LYS   B H      1 
ATOM   8427  H  HA     . LYS   B 1 131 ? 19.866  -37.263 25.876 1.00 29.97  ?  156 LYS   B HA     1 
ATOM   8428  H  HB2    . LYS   B 1 131 ? 20.819  -39.708 26.909 1.00 31.69  ?  156 LYS   B HB2    1 
ATOM   8429  H  HB3    . LYS   B 1 131 ? 20.008  -38.608 27.720 1.00 31.69  ?  156 LYS   B HB3    1 
ATOM   8430  H  HG2    . LYS   B 1 131 ? 18.891  -40.190 25.671 1.00 36.47  ?  156 LYS   B HG2    1 
ATOM   8431  H  HG3    . LYS   B 1 131 ? 18.640  -40.428 27.222 1.00 36.47  ?  156 LYS   B HG3    1 
ATOM   8432  H  HD2    . LYS   B 1 131 ? 17.544  -38.371 27.361 1.00 38.46  ?  156 LYS   B HD2    1 
ATOM   8433  H  HD3    . LYS   B 1 131 ? 17.796  -38.132 25.810 1.00 38.46  ?  156 LYS   B HD3    1 
ATOM   8434  H  HE2    . LYS   B 1 131 ? 16.461  -40.016 25.333 1.00 41.11  ?  156 LYS   B HE2    1 
ATOM   8435  H  HE3    . LYS   B 1 131 ? 16.160  -40.170 26.886 1.00 41.11  ?  156 LYS   B HE3    1 
ATOM   8436  H  HZ1    . LYS   B 1 131 ? 15.047  -38.191 26.798 1.00 42.16  ?  156 LYS   B HZ1    1 
ATOM   8437  H  HZ2    . LYS   B 1 131 ? 15.327  -38.044 25.384 1.00 42.16  ?  156 LYS   B HZ2    1 
ATOM   8438  H  HZ3    . LYS   B 1 131 ? 14.450  -39.102 25.842 1.00 42.16  ?  156 LYS   B HZ3    1 
ATOM   8439  N  N      . LYS   B 1 132 ? 22.094  -36.184 25.598 1.00 22.97  ?  157 LYS   B N      1 
ATOM   8440  C  CA     . LYS   B 1 132 ? 23.408  -35.556 25.601 1.00 21.13  ?  157 LYS   B CA     1 
ATOM   8441  C  C      . LYS   B 1 132 ? 23.590  -34.623 26.797 1.00 19.57  ?  157 LYS   B C      1 
ATOM   8442  O  O      . LYS   B 1 132 ? 22.635  -34.008 27.274 1.00 21.12  ?  157 LYS   B O      1 
ATOM   8443  C  CB     . LYS   B 1 132 ? 23.634  -34.748 24.316 1.00 24.86  ?  157 LYS   B CB     1 
ATOM   8444  C  CG     . LYS   B 1 132 ? 23.782  -35.566 23.037 1.00 28.43  ?  157 LYS   B CG     1 
ATOM   8445  C  CD     . LYS   B 1 132 ? 24.021  -34.638 21.845 1.00 31.07  ?  157 LYS   B CD     1 
ATOM   8446  C  CE     . LYS   B 1 132 ? 23.906  -35.366 20.517 1.00 32.62  ?  157 LYS   B CE     1 
ATOM   8447  N  NZ     . LYS   B 1 132 ? 25.079  -36.219 20.297 1.00 36.41  ?  157 LYS   B NZ     1 
ATOM   8448  H  H      . LYS   B 1 132 ? 21.473  -35.687 25.270 1.00 27.56  ?  157 LYS   B H      1 
ATOM   8449  H  HA     . LYS   B 1 132 ? 24.072  -36.260 25.663 1.00 25.35  ?  157 LYS   B HA     1 
ATOM   8450  H  HB2    . LYS   B 1 132 ? 22.877  -34.155 24.192 1.00 29.83  ?  157 LYS   B HB2    1 
ATOM   8451  H  HB3    . LYS   B 1 132 ? 24.447  -34.230 24.421 1.00 29.83  ?  157 LYS   B HB3    1 
ATOM   8452  H  HG2    . LYS   B 1 132 ? 24.539  -36.167 23.120 1.00 34.11  ?  157 LYS   B HG2    1 
ATOM   8453  H  HG3    . LYS   B 1 132 ? 22.971  -36.074 22.879 1.00 34.11  ?  157 LYS   B HG3    1 
ATOM   8454  H  HD2    . LYS   B 1 132 ? 23.360  -33.927 21.857 1.00 37.28  ?  157 LYS   B HD2    1 
ATOM   8455  H  HD3    . LYS   B 1 132 ? 24.913  -34.262 21.907 1.00 37.28  ?  157 LYS   B HD3    1 
ATOM   8456  H  HE2    . LYS   B 1 132 ? 23.114  -35.925 20.520 1.00 39.14  ?  157 LYS   B HE2    1 
ATOM   8457  H  HE3    . LYS   B 1 132 ? 23.854  -34.720 19.796 1.00 39.14  ?  157 LYS   B HE3    1 
ATOM   8458  H  HZ1    . LYS   B 1 132 ? 25.009  -36.637 19.515 1.00 43.68  ?  157 LYS   B HZ1    1 
ATOM   8459  H  HZ2    . LYS   B 1 132 ? 25.819  -35.724 20.295 1.00 43.68  ?  157 LYS   B HZ2    1 
ATOM   8460  H  HZ3    . LYS   B 1 132 ? 25.140  -36.826 20.945 1.00 43.68  ?  157 LYS   B HZ3    1 
ATOM   8461  N  N      . VAL   B 1 133 ? 24.845  -34.485 27.241 1.00 20.25  ?  158 VAL   B N      1 
ATOM   8462  C  CA     . VAL   B 1 133 ? 25.187  -33.571 28.329 1.00 20.68  ?  158 VAL   B CA     1 
ATOM   8463  C  C      . VAL   B 1 133 ? 26.043  -32.424 27.798 1.00 21.54  ?  158 VAL   B C      1 
ATOM   8464  O  O      . VAL   B 1 133 ? 26.883  -31.862 28.514 1.00 21.73  ?  158 VAL   B O      1 
ATOM   8465  C  CB     . VAL   B 1 133 ? 25.886  -34.301 29.496 1.00 20.99  ?  158 VAL   B CB     1 
ATOM   8466  C  CG1    . VAL   B 1 133 ? 24.900  -35.256 30.187 1.00 20.81  ?  158 VAL   B CG1    1 
ATOM   8467  C  CG2    . VAL   B 1 133 ? 27.152  -35.040 29.062 1.00 21.36  ?  158 VAL   B CG2    1 
ATOM   8468  H  H      . VAL   B 1 133 ? 25.520  -34.914 26.924 1.00 24.30  ?  158 VAL   B H      1 
ATOM   8469  H  HA     . VAL   B 1 133 ? 24.363  -33.191 28.671 1.00 24.81  ?  158 VAL   B HA     1 
ATOM   8470  H  HB     . VAL   B 1 133 ? 26.174  -33.629 30.133 1.00 25.18  ?  158 VAL   B HB     1 
ATOM   8471  H  HG11   . VAL   B 1 133 ? 25.354  -35.703 30.919 1.00 24.96  ?  158 VAL   B HG11   1 
ATOM   8472  H  HG12   . VAL   B 1 133 ? 24.150  -34.744 30.526 1.00 24.96  ?  158 VAL   B HG12   1 
ATOM   8473  H  HG13   . VAL   B 1 133 ? 24.590  -35.911 29.542 1.00 24.96  ?  158 VAL   B HG13   1 
ATOM   8474  H  HG21   . VAL   B 1 133 ? 27.551  -35.466 29.837 1.00 25.63  ?  158 VAL   B HG21   1 
ATOM   8475  H  HG22   . VAL   B 1 133 ? 26.917  -35.710 28.401 1.00 25.63  ?  158 VAL   B HG22   1 
ATOM   8476  H  HG23   . VAL   B 1 133 ? 27.775  -34.402 28.679 1.00 25.63  ?  158 VAL   B HG23   1 
ATOM   8477  N  N      . THR   B 1 134 ? 25.822  -32.072 26.536 1.00 21.98  ?  159 THR   B N      1 
ATOM   8478  C  CA     . THR   B 1 134 ? 26.325  -30.837 25.964 1.00 21.90  ?  159 THR   B CA     1 
ATOM   8479  C  C      . THR   B 1 134 ? 25.503  -29.648 26.454 1.00 20.13  ?  159 THR   B C      1 
ATOM   8480  O  O      . THR   B 1 134 ? 24.334  -29.775 26.826 1.00 20.93  ?  159 THR   B O      1 
ATOM   8481  C  CB     . THR   B 1 134 ? 26.260  -30.900 24.441 1.00 23.94  ?  159 THR   B CB     1 
ATOM   8482  O  OG1    . THR   B 1 134 ? 24.936  -31.292 24.047 1.00 25.79  ?  159 THR   B OG1    1 
ATOM   8483  C  CG2    . THR   B 1 134 ? 27.255  -31.909 23.907 1.00 26.43  ?  159 THR   B CG2    1 
ATOM   8484  H  H      . THR   B 1 134 ? 25.371  -32.546 25.978 1.00 26.37  ?  159 THR   B H      1 
ATOM   8485  H  HA     . THR   B 1 134 ? 27.248  -30.708 26.233 1.00 26.28  ?  159 THR   B HA     1 
ATOM   8486  H  HB     . THR   B 1 134 ? 26.475  -30.032 24.067 1.00 28.72  ?  159 THR   B HB     1 
ATOM   8487  H  HG1    . THR   B 1 134 ? 24.882  -31.319 23.209 1.00 30.95  ?  159 THR   B HG1    1 
ATOM   8488  H  HG21   . THR   B 1 134 ? 27.214  -31.935 22.939 1.00 31.72  ?  159 THR   B HG21   1 
ATOM   8489  H  HG22   . THR   B 1 134 ? 28.154  -31.664 24.178 1.00 31.72  ?  159 THR   B HG22   1 
ATOM   8490  H  HG23   . THR   B 1 134 ? 27.052  -32.792 24.255 1.00 31.72  ?  159 THR   B HG23   1 
ATOM   8491  N  N      . GLY   B 1 135 ? 26.126  -28.470 26.432 1.00 20.16  ?  160 GLY   B N      1 
ATOM   8492  C  CA     . GLY   B 1 135 ? 25.389  -27.263 26.745 1.00 20.42  ?  160 GLY   B CA     1 
ATOM   8493  C  C      . GLY   B 1 135 ? 24.542  -26.740 25.609 1.00 20.64  ?  160 GLY   B C      1 
ATOM   8494  O  O      . GLY   B 1 135 ? 23.568  -26.021 25.857 1.00 21.06  ?  160 GLY   B O      1 
ATOM   8495  H  H      . GLY   B 1 135 ? 26.957  -28.351 26.242 1.00 24.19  ?  160 GLY   B H      1 
ATOM   8496  H  HA2    . GLY   B 1 135 ? 24.803  -27.441 27.497 1.00 24.49  ?  160 GLY   B HA2    1 
ATOM   8497  H  HA3    . GLY   B 1 135 ? 26.018  -26.567 26.993 1.00 24.49  ?  160 GLY   B HA3    1 
ATOM   8498  N  N      . GLY   B 1 136 ? 24.864  -27.105 24.373 1.00 20.99  ?  161 GLY   B N      1 
ATOM   8499  C  CA     . GLY   B 1 136 ? 24.097  -26.608 23.242 1.00 21.65  ?  161 GLY   B CA     1 
ATOM   8500  C  C      . GLY   B 1 136 ? 22.732  -27.268 23.153 1.00 20.67  ?  161 GLY   B C      1 
ATOM   8501  O  O      . GLY   B 1 136 ? 22.585  -28.480 23.347 1.00 21.13  ?  161 GLY   B O      1 
ATOM   8502  H  H      . GLY   B 1 136 ? 25.512  -27.631 24.166 1.00 25.18  ?  161 GLY   B H      1 
ATOM   8503  H  HA2    . GLY   B 1 136 ? 23.971  -25.651 23.332 1.00 25.97  ?  161 GLY   B HA2    1 
ATOM   8504  H  HA3    . GLY   B 1 136 ? 24.580  -26.787 22.420 1.00 25.97  ?  161 GLY   B HA3    1 
ATOM   8505  N  N      . ARG   B 1 137 ? 21.718  -26.448 22.859 1.00 19.90  ?  162 ARG   B N      1 
ATOM   8506  C  CA     . ARG   B 1 137 ? 20.347  -26.933 22.798 1.00 19.34  ?  162 ARG   B CA     1 
ATOM   8507  C  C      . ARG   B 1 137 ? 19.531  -26.347 21.648 1.00 21.20  ?  162 ARG   B C      1 
ATOM   8508  O  O      . ARG   B 1 137 ? 18.685  -27.045 21.082 1.00 23.33  ?  162 ARG   B O      1 
ATOM   8509  C  CB     . ARG   B 1 137 ? 19.598  -26.619 24.106 1.00 18.94  ?  162 ARG   B CB     1 
ATOM   8510  C  CG     . ARG   B 1 137 ? 20.184  -27.245 25.381 1.00 19.97  ?  162 ARG   B CG     1 
ATOM   8511  C  CD     . ARG   B 1 137 ? 20.160  -28.815 25.389 1.00 20.17  ?  162 ARG   B CD     1 
ATOM   8512  N  NE     . ARG   B 1 137 ? 18.761  -29.236 25.445 1.00 21.72  ?  162 ARG   B NE     1 
ATOM   8513  C  CZ     . ARG   B 1 137 ? 18.177  -30.136 24.665 1.00 22.55  ?  162 ARG   B CZ     1 
ATOM   8514  N  NH1    . ARG   B 1 137 ? 18.873  -30.849 23.782 1.00 24.02  ?  162 ARG   B NH1    1 
ATOM   8515  N  NH2    . ARG   B 1 137 ? 16.869  -30.328 24.796 1.00 24.12  ?  162 ARG   B NH2    1 
ATOM   8516  H  H      . ARG   B 1 137 ? 21.804  -25.608 22.693 1.00 23.87  ?  162 ARG   B H      1 
ATOM   8517  H  HA     . ARG   B 1 137 ? 20.416  -27.890 22.657 1.00 23.21  ?  162 ARG   B HA     1 
ATOM   8518  H  HB2    . ARG   B 1 137 ? 19.598  -25.657 24.232 1.00 22.72  ?  162 ARG   B HB2    1 
ATOM   8519  H  HB3    . ARG   B 1 137 ? 18.688  -26.943 24.019 1.00 22.72  ?  162 ARG   B HB3    1 
ATOM   8520  H  HG2    . ARG   B 1 137 ? 21.108  -26.964 25.470 1.00 23.96  ?  162 ARG   B HG2    1 
ATOM   8521  H  HG3    . ARG   B 1 137 ? 19.669  -26.938 26.144 1.00 23.96  ?  162 ARG   B HG3    1 
ATOM   8522  H  HD2    . ARG   B 1 137 ? 20.568  -29.161 24.580 1.00 24.19  ?  162 ARG   B HD2    1 
ATOM   8523  H  HD3    . ARG   B 1 137 ? 20.629  -29.154 26.168 1.00 24.19  ?  162 ARG   B HD3    1 
ATOM   8524  H  HE     . ARG   B 1 137 ? 18.268  -28.863 26.043 1.00 26.05  ?  162 ARG   B HE     1 
ATOM   8525  H  HH11   . ARG   B 1 137 ? 19.722  -30.732 23.708 1.00 28.82  ?  162 ARG   B HH11   1 
ATOM   8526  H  HH12   . ARG   B 1 137 ? 18.474  -31.427 23.286 1.00 28.82  ?  162 ARG   B HH12   1 
ATOM   8527  H  HH21   . ARG   B 1 137 ? 16.424  -29.874 25.376 1.00 28.94  ?  162 ARG   B HH21   1 
ATOM   8528  H  HH22   . ARG   B 1 137 ? 16.467  -30.905 24.302 1.00 28.94  ?  162 ARG   B HH22   1 
ATOM   8529  N  N      . ASN   B 1 138 ? 19.737  -25.073 21.308 1.00 20.61  ?  163 ASN   B N      1 
ATOM   8530  C  CA     . ASN   B 1 138 ? 18.770  -24.356 20.487 1.00 20.27  ?  163 ASN   B CA     1 
ATOM   8531  C  C      . ASN   B 1 138 ? 19.173  -24.058 19.052 1.00 20.98  ?  163 ASN   B C      1 
ATOM   8532  O  O      . ASN   B 1 138 ? 18.295  -23.686 18.265 1.00 22.86  ?  163 ASN   B O      1 
ATOM   8533  C  CB     . ASN   B 1 138 ? 18.421  -23.022 21.155 1.00 21.05  ?  163 ASN   B CB     1 
ATOM   8534  C  CG     . ASN   B 1 138 ? 17.927  -23.209 22.560 1.00 24.39  ?  163 ASN   B CG     1 
ATOM   8535  O  OD1    . ASN   B 1 138 ? 17.120  -24.105 22.826 1.00 23.63  ?  163 ASN   B OD1    1 
ATOM   8536  N  ND2    . ASN   B 1 138 ? 18.421  -22.382 23.478 1.00 26.64  ?  163 ASN   B ND2    1 
ATOM   8537  H  H      . ASN   B 1 138 ? 20.424  -24.610 21.541 1.00 24.73  ?  163 ASN   B H      1 
ATOM   8538  H  HA     . ASN   B 1 138 ? 17.984  -24.923 20.430 1.00 24.31  ?  163 ASN   B HA     1 
ATOM   8539  H  HB2    . ASN   B 1 138 ? 19.213  -22.463 21.184 1.00 25.25  ?  163 ASN   B HB2    1 
ATOM   8540  H  HB3    . ASN   B 1 138 ? 17.723  -22.583 20.645 1.00 25.25  ?  163 ASN   B HB3    1 
ATOM   8541  H  HD21   . ASN   B 1 138 ? 18.168  -22.449 24.298 1.00 31.97  ?  163 ASN   B HD21   1 
ATOM   8542  H  HD22   . ASN   B 1 138 ? 18.992  -21.779 23.253 1.00 31.97  ?  163 ASN   B HD22   1 
ATOM   8543  N  N      . GLY   B 1 139 ? 20.449  -24.177 18.689 1.00 21.19  ?  164 GLY   B N      1 
ATOM   8544  C  CA     . GLY   B 1 139 ? 20.868  -23.854 17.335 1.00 22.23  ?  164 GLY   B CA     1 
ATOM   8545  C  C      . GLY   B 1 139 ? 21.041  -22.384 17.039 1.00 22.19  ?  164 GLY   B C      1 
ATOM   8546  O  O      . GLY   B 1 139 ? 20.925  -21.991 15.870 1.00 23.80  ?  164 GLY   B O      1 
ATOM   8547  H  H      . GLY   B 1 139 ? 21.084  -24.442 19.206 1.00 25.43  ?  164 GLY   B H      1 
ATOM   8548  H  HA2    . GLY   B 1 139 ? 21.718  -24.290 17.164 1.00 26.67  ?  164 GLY   B HA2    1 
ATOM   8549  H  HA3    . GLY   B 1 139 ? 20.205  -24.201 16.717 1.00 26.67  ?  164 GLY   B HA3    1 
ATOM   8550  N  N      . TYR   B 1 140 ? 21.302  -21.559 18.059 1.00 22.98  ?  165 TYR   B N      1 
ATOM   8551  C  CA     . TYR   B 1 140 ? 21.469  -20.116 17.908 1.00 22.85  ?  165 TYR   B CA     1 
ATOM   8552  C  C      . TYR   B 1 140 ? 22.873  -19.595 18.199 1.00 22.43  ?  165 TYR   B C      1 
ATOM   8553  O  O      . TYR   B 1 140 ? 23.312  -18.656 17.535 1.00 23.24  ?  165 TYR   B O      1 
ATOM   8554  C  CB     . TYR   B 1 140 ? 20.523  -19.363 18.846 1.00 23.46  ?  165 TYR   B CB     1 
ATOM   8555  C  CG     . TYR   B 1 140 ? 19.187  -18.938 18.307 1.00 24.41  ?  165 TYR   B CG     1 
ATOM   8556  C  CD1    . TYR   B 1 140 ? 19.099  -18.060 17.246 1.00 26.08  ?  165 TYR   B CD1    1 
ATOM   8557  C  CD2    . TYR   B 1 140 ? 18.008  -19.370 18.902 1.00 26.63  ?  165 TYR   B CD2    1 
ATOM   8558  C  CE1    . TYR   B 1 140 ? 17.881  -17.649 16.764 1.00 27.69  ?  165 TYR   B CE1    1 
ATOM   8559  C  CE2    . TYR   B 1 140 ? 16.782  -18.949 18.439 1.00 27.76  ?  165 TYR   B CE2    1 
ATOM   8560  C  CZ     . TYR   B 1 140 ? 16.726  -18.092 17.365 1.00 29.00  ?  165 TYR   B CZ     1 
ATOM   8561  O  OH     . TYR   B 1 140 ? 15.505  -17.682 16.887 1.00 31.77  ?  165 TYR   B OH     1 
ATOM   8562  H  H      . TYR   B 1 140 ? 21.389  -21.824 18.872 1.00 27.57  ?  165 TYR   B H      1 
ATOM   8563  H  HA     . TYR   B 1 140 ? 21.251  -19.913 16.985 1.00 27.41  ?  165 TYR   B HA     1 
ATOM   8564  H  HB2    . TYR   B 1 140 ? 20.345  -19.936 19.609 1.00 28.15  ?  165 TYR   B HB2    1 
ATOM   8565  H  HB3    . TYR   B 1 140 ? 20.975  -18.556 19.136 1.00 28.15  ?  165 TYR   B HB3    1 
ATOM   8566  H  HD1    . TYR   B 1 140 ? 19.878  -17.741 16.851 1.00 31.29  ?  165 TYR   B HD1    1 
ATOM   8567  H  HD2    . TYR   B 1 140 ? 18.048  -19.953 19.625 1.00 31.94  ?  165 TYR   B HD2    1 
ATOM   8568  H  HE1    . TYR   B 1 140 ? 17.837  -17.073 16.035 1.00 33.22  ?  165 TYR   B HE1    1 
ATOM   8569  H  HE2    . TYR   B 1 140 ? 16.000  -19.241 18.849 1.00 33.30  ?  165 TYR   B HE2    1 
ATOM   8570  H  HH     . TYR   B 1 140 ? 14.887  -18.045 17.326 1.00 38.12  ?  165 TYR   B HH     1 
ATOM   8571  N  N      . GLY   B 1 141 ? 23.569  -20.152 19.200 1.00 20.86  ?  166 GLY   B N      1 
ATOM   8572  C  CA     . GLY   B 1 141 ? 24.663  -19.436 19.854 1.00 21.16  ?  166 GLY   B CA     1 
ATOM   8573  C  C      . GLY   B 1 141 ? 25.759  -18.933 18.928 1.00 22.23  ?  166 GLY   B C      1 
ATOM   8574  O  O      . GLY   B 1 141 ? 26.233  -17.798 19.062 1.00 22.97  ?  166 GLY   B O      1 
ATOM   8575  H  H      . GLY   B 1 141 ? 23.426  -20.939 19.516 1.00 25.02  ?  166 GLY   B H      1 
ATOM   8576  H  HA2    . GLY   B 1 141 ? 24.296  -18.667 20.318 1.00 25.39  ?  166 GLY   B HA2    1 
ATOM   8577  H  HA3    . GLY   B 1 141 ? 25.076  -20.028 20.502 1.00 25.39  ?  166 GLY   B HA3    1 
ATOM   8578  N  N      . ALA   B 1 142 ? 26.230  -19.787 18.022 1.00 24.20  ?  167 ALA   B N      1 
ATOM   8579  C  CA     . ALA   B 1 142 ? 27.333  -19.389 17.155 1.00 24.55  ?  167 ALA   B CA     1 
ATOM   8580  C  C      . ALA   B 1 142 ? 26.881  -18.329 16.161 1.00 25.78  ?  167 ALA   B C      1 
ATOM   8581  O  O      . ALA   B 1 142 ? 27.653  -17.422 15.815 1.00 27.42  ?  167 ALA   B O      1 
ATOM   8582  C  CB     . ALA   B 1 142 ? 27.895  -20.610 16.429 1.00 25.28  ?  167 ALA   B CB     1 
ATOM   8583  H  H      . ALA   B 1 142 ? 25.935  -20.585 17.892 1.00 29.03  ?  167 ALA   B H      1 
ATOM   8584  H  HA     . ALA   B 1 142 ? 28.045  -19.014 17.696 1.00 29.45  ?  167 ALA   B HA     1 
ATOM   8585  H  HB1    . ALA   B 1 142 ? 28.636  -20.331 15.868 1.00 30.33  ?  167 ALA   B HB1    1 
ATOM   8586  H  HB2    . ALA   B 1 142 ? 28.203  -21.254 17.086 1.00 30.33  ?  167 ALA   B HB2    1 
ATOM   8587  H  HB3    . ALA   B 1 142 ? 27.197  -21.003 15.882 1.00 30.33  ?  167 ALA   B HB3    1 
ATOM   8588  N  N      . LYS   B 1 143 ? 25.636  -18.438 15.682 1.00 25.79  ?  168 LYS   B N      1 
ATOM   8589  C  CA     . LYS   B 1 143 ? 25.101  -17.428 14.772 1.00 25.54  ?  168 LYS   B CA     1 
ATOM   8590  C  C      . LYS   B 1 143 ? 24.921  -16.092 15.488 1.00 25.79  ?  168 LYS   B C      1 
ATOM   8591  O  O      . LYS   B 1 143 ? 25.152  -15.030 14.904 1.00 27.47  ?  168 LYS   B O      1 
ATOM   8592  C  CB     . LYS   B 1 143 ? 23.780  -17.904 14.167 1.00 26.20  ?  168 LYS   B CB     1 
ATOM   8593  C  CG     . LYS   B 1 143 ? 23.910  -18.851 12.956 1.00 26.74  ?  168 LYS   B CG     1 
ATOM   8594  C  CD     . LYS   B 1 143 ? 24.425  -20.246 13.336 1.00 26.10  ?  168 LYS   B CD     1 
ATOM   8595  C  CE     . LYS   B 1 143 ? 23.421  -21.031 14.191 1.00 25.67  ?  168 LYS   B CE     1 
ATOM   8596  N  NZ     . LYS   B 1 143 ? 23.874  -22.424 14.516 1.00 25.94  ?  168 LYS   B NZ     1 
ATOM   8597  H  H      . LYS   B 1 143 ? 25.091  -19.077 15.867 1.00 30.94  ?  168 LYS   B H      1 
ATOM   8598  H  HA     . LYS   B 1 143 ? 25.726  -17.299 14.041 1.00 30.64  ?  168 LYS   B HA     1 
ATOM   8599  H  HB2    . LYS   B 1 143 ? 23.283  -18.378 14.852 1.00 31.44  ?  168 LYS   B HB2    1 
ATOM   8600  H  HB3    . LYS   B 1 143 ? 23.280  -17.126 13.873 1.00 31.44  ?  168 LYS   B HB3    1 
ATOM   8601  H  HG2    . LYS   B 1 143 ? 23.039  -18.957 12.543 1.00 32.08  ?  168 LYS   B HG2    1 
ATOM   8602  H  HG3    . LYS   B 1 143 ? 24.534  -18.466 12.320 1.00 32.08  ?  168 LYS   B HG3    1 
ATOM   8603  H  HD2    . LYS   B 1 143 ? 24.592  -20.754 12.527 1.00 31.32  ?  168 LYS   B HD2    1 
ATOM   8604  H  HD3    . LYS   B 1 143 ? 25.245  -20.154 13.845 1.00 31.32  ?  168 LYS   B HD3    1 
ATOM   8605  H  HE2    . LYS   B 1 143 ? 23.286  -20.560 15.028 1.00 30.80  ?  168 LYS   B HE2    1 
ATOM   8606  H  HE3    . LYS   B 1 143 ? 22.582  -21.097 13.709 1.00 30.80  ?  168 LYS   B HE3    1 
ATOM   8607  H  HZ1    . LYS   B 1 143 ? 24.636  -22.397 14.975 1.00 31.12  ?  168 LYS   B HZ1    1 
ATOM   8608  H  HZ2    . LYS   B 1 143 ? 23.257  -22.839 15.005 1.00 31.12  ?  168 LYS   B HZ2    1 
ATOM   8609  H  HZ3    . LYS   B 1 143 ? 24.005  -22.884 13.765 1.00 31.12  ?  168 LYS   B HZ3    1 
ATOM   8610  N  N      . LEU   B 1 144 ? 24.513  -16.121 16.759 1.00 25.48  ?  169 LEU   B N      1 
ATOM   8611  C  CA     . LEU   B 1 144 ? 24.404  -14.874 17.516 1.00 24.09  ?  169 LEU   B CA     1 
ATOM   8612  C  C      . LEU   B 1 144 ? 25.761  -14.178 17.628 1.00 25.30  ?  169 LEU   B C      1 
ATOM   8613  O  O      . LEU   B 1 144 ? 25.854  -12.959 17.447 1.00 26.34  ?  169 LEU   B O      1 
ATOM   8614  C  CB     . LEU   B 1 144 ? 23.793  -15.146 18.894 1.00 23.25  ?  169 LEU   B CB     1 
ATOM   8615  C  CG     . LEU   B 1 144 ? 22.337  -15.630 18.822 1.00 24.89  ?  169 LEU   B CG     1 
ATOM   8616  C  CD1    . LEU   B 1 144 ? 21.840  -16.017 20.216 1.00 25.00  ?  169 LEU   B CD1    1 
ATOM   8617  C  CD2    . LEU   B 1 144 ? 21.396  -14.612 18.182 1.00 25.91  ?  169 LEU   B CD2    1 
ATOM   8618  H  H      . LEU   B 1 144 ? 24.298  -16.830 17.195 1.00 30.57  ?  169 LEU   B H      1 
ATOM   8619  H  HA     . LEU   B 1 144 ? 23.805  -14.269 17.051 1.00 28.91  ?  169 LEU   B HA     1 
ATOM   8620  H  HB2    . LEU   B 1 144 ? 24.315  -15.831 19.340 1.00 27.89  ?  169 LEU   B HB2    1 
ATOM   8621  H  HB3    . LEU   B 1 144 ? 23.810  -14.326 19.413 1.00 27.89  ?  169 LEU   B HB3    1 
ATOM   8622  H  HG     . LEU   B 1 144 ? 22.320  -16.411 18.246 1.00 29.86  ?  169 LEU   B HG     1 
ATOM   8623  H  HD11   . LEU   B 1 144 ? 20.922  -16.323 20.151 1.00 29.99  ?  169 LEU   B HD11   1 
ATOM   8624  H  HD12   . LEU   B 1 144 ? 22.401  -16.727 20.566 1.00 29.99  ?  169 LEU   B HD12   1 
ATOM   8625  H  HD13   . LEU   B 1 144 ? 21.890  -15.241 20.796 1.00 29.99  ?  169 LEU   B HD13   1 
ATOM   8626  H  HD21   . LEU   B 1 144 ? 20.480  -14.900 18.318 1.00 31.08  ?  169 LEU   B HD21   1 
ATOM   8627  H  HD22   . LEU   B 1 144 ? 21.536  -13.748 18.599 1.00 31.08  ?  169 LEU   B HD22   1 
ATOM   8628  H  HD23   . LEU   B 1 144 ? 21.589  -14.557 17.233 1.00 31.08  ?  169 LEU   B HD23   1 
ATOM   8629  N  N      . CYS   B 1 145 ? 26.833  -14.934 17.879 1.00 24.68  ?  170 CYS   B N      1 
ATOM   8630  C  CA     . CYS   B 1 145 ? 28.155  -14.308 17.916 1.00 25.28  ?  170 CYS   B CA     1 
ATOM   8631  C  C      . CYS   B 1 145 ? 28.497  -13.685 16.561 1.00 27.25  ?  170 CYS   B C      1 
ATOM   8632  O  O      . CYS   B 1 145 ? 28.992  -12.550 16.488 1.00 27.73  ?  170 CYS   B O      1 
ATOM   8633  C  CB     . CYS   B 1 145 ? 29.227  -15.327 18.318 1.00 26.28  ?  170 CYS   B CB     1 
ATOM   8634  S  SG     . CYS   B 1 145 ? 30.863  -14.532 18.561 1.00 28.50  ?  170 CYS   B SG     1 
ATOM   8635  H  H      . CYS   B 1 145 ? 26.823  -15.781 18.025 1.00 29.60  ?  170 CYS   B H      1 
ATOM   8636  H  HA     . CYS   B 1 145 ? 28.144  -13.609 18.588 1.00 30.33  ?  170 CYS   B HA     1 
ATOM   8637  H  HB2    . CYS   B 1 145 ? 28.967  -15.752 19.150 1.00 31.53  ?  170 CYS   B HB2    1 
ATOM   8638  H  HB3    . CYS   B 1 145 ? 29.313  -15.993 17.618 1.00 31.53  ?  170 CYS   B HB3    1 
ATOM   8639  H  HG     . CYS   B 1 145 ? 31.667  -15.374 18.851 1.00 34.19  ?  170 CYS   B HG     1 
ATOM   8640  N  N      . ASN   B 1 146 ? 28.250  -14.430 15.478 1.00 28.72  ?  171 ASN   B N      1 
ATOM   8641  C  CA     . ASN   B 1 146 ? 28.435  -13.929 14.115 1.00 29.33  ?  171 ASN   B CA     1 
ATOM   8642  C  C      . ASN   B 1 146 ? 27.675  -12.622 13.896 1.00 30.04  ?  171 ASN   B C      1 
ATOM   8643  O  O      . ASN   B 1 146 ? 28.237  -11.626 13.421 1.00 31.55  ?  171 ASN   B O      1 
ATOM   8644  C  CB     . ASN   B 1 146 ? 27.960  -15.026 13.148 1.00 29.24  ?  171 ASN   B CB     1 
ATOM   8645  C  CG     . ASN   B 1 146 ? 28.518  -14.887 11.741 1.00 31.27  ?  171 ASN   B CG     1 
ATOM   8646  O  OD1    . ASN   B 1 146 ? 28.964  -13.818 11.325 1.00 32.70  ?  171 ASN   B OD1    1 
ATOM   8647  N  ND2    . ASN   B 1 146 ? 28.476  -15.980 10.995 1.00 31.94  ?  171 ASN   B ND2    1 
ATOM   8648  H  H      . ASN   B 1 146 ? 27.969  -15.242 15.506 1.00 34.45  ?  171 ASN   B H      1 
ATOM   8649  H  HA     . ASN   B 1 146 ? 29.371  -13.737 13.946 1.00 35.18  ?  171 ASN   B HA     1 
ATOM   8650  H  HB2    . ASN   B 1 146 ? 28.240  -15.888 13.493 1.00 35.08  ?  171 ASN   B HB2    1 
ATOM   8651  H  HB3    . ASN   B 1 146 ? 26.993  -14.990 13.087 1.00 35.08  ?  171 ASN   B HB3    1 
ATOM   8652  H  HD21   . ASN   B 1 146 ? 28.777  -15.963 10.190 1.00 38.33  ?  171 ASN   B HD21   1 
ATOM   8653  H  HD22   . ASN   B 1 146 ? 28.147  -16.707 11.316 1.00 38.33  ?  171 ASN   B HD22   1 
ATOM   8654  N  N      . ILE   B 1 147 ? 26.392  -12.609 14.261 1.00 28.77  ?  172 ILE   B N      1 
ATOM   8655  C  CA     . ILE   B 1 147 ? 25.537  -11.450 14.018 1.00 28.73  ?  172 ILE   B CA     1 
ATOM   8656  C  C      . ILE   B 1 147 ? 26.021  -10.214 14.769 1.00 28.46  ?  172 ILE   B C      1 
ATOM   8657  O  O      . ILE   B 1 147 ? 25.837  -9.086  14.295 1.00 29.69  ?  172 ILE   B O      1 
ATOM   8658  C  CB     . ILE   B 1 147 ? 24.077  -11.808 14.390 1.00 28.84  ?  172 ILE   B CB     1 
ATOM   8659  C  CG1    . ILE   B 1 147 ? 23.497  -12.791 13.361 1.00 28.66  ?  172 ILE   B CG1    1 
ATOM   8660  C  CG2    . ILE   B 1 147 ? 23.223  -10.558 14.486 1.00 29.25  ?  172 ILE   B CG2    1 
ATOM   8661  C  CD1    . ILE   B 1 147 ? 22.220  -13.493 13.820 1.00 29.01  ?  172 ILE   B CD1    1 
ATOM   8662  H  H      . ILE   B 1 147 ? 25.992  -13.261 14.653 1.00 34.52  ?  172 ILE   B H      1 
ATOM   8663  H  HA     . ILE   B 1 147 ? 25.580  -11.232 13.074 1.00 34.47  ?  172 ILE   B HA     1 
ATOM   8664  H  HB     . ILE   B 1 147 ? 24.077  -12.237 15.260 1.00 34.60  ?  172 ILE   B HB     1 
ATOM   8665  H  HG12   . ILE   B 1 147 ? 23.289  -12.303 12.548 1.00 34.38  ?  172 ILE   B HG12   1 
ATOM   8666  H  HG13   . ILE   B 1 147 ? 24.159  -13.475 13.176 1.00 34.38  ?  172 ILE   B HG13   1 
ATOM   8667  H  HG21   . ILE   B 1 147 ? 22.287  -10.809 14.432 1.00 35.09  ?  172 ILE   B HG21   1 
ATOM   8668  H  HG22   . ILE   B 1 147 ? 23.399  -10.119 15.333 1.00 35.09  ?  172 ILE   B HG22   1 
ATOM   8669  H  HG23   . ILE   B 1 147 ? 23.449  -9.964  13.753 1.00 35.09  ?  172 ILE   B HG23   1 
ATOM   8670  H  HD11   . ILE   B 1 147 ? 21.982  -14.172 13.169 1.00 34.80  ?  172 ILE   B HD11   1 
ATOM   8671  H  HD12   . ILE   B 1 147 ? 22.380  -13.905 14.684 1.00 34.80  ?  172 ILE   B HD12   1 
ATOM   8672  H  HD13   . ILE   B 1 147 ? 21.508  -12.839 13.891 1.00 34.80  ?  172 ILE   B HD13   1 
ATOM   8673  N  N      . PHE   B 1 148 ? 26.615  -10.390 15.952 1.00 27.20  ?  173 PHE   B N      1 
ATOM   8674  C  CA     . PHE   B 1 148 ? 27.118  -9.262  16.734 1.00 27.34  ?  173 PHE   B CA     1 
ATOM   8675  C  C      . PHE   B 1 148 ? 28.618  -9.052  16.563 1.00 28.55  ?  173 PHE   B C      1 
ATOM   8676  O  O      . PHE   B 1 148 ? 29.252  -8.416  17.413 1.00 29.92  ?  173 PHE   B O      1 
ATOM   8677  C  CB     . PHE   B 1 148 ? 26.696  -9.434  18.199 1.00 27.50  ?  173 PHE   B CB     1 
ATOM   8678  C  CG     . PHE   B 1 148 ? 25.224  -9.218  18.385 1.00 26.26  ?  173 PHE   B CG     1 
ATOM   8679  C  CD1    . PHE   B 1 148 ? 24.709  -7.932  18.527 1.00 27.28  ?  173 PHE   B CD1    1 
ATOM   8680  C  CD2    . PHE   B 1 148 ? 24.345  -10.288 18.332 1.00 27.13  ?  173 PHE   B CD2    1 
ATOM   8681  C  CE1    . PHE   B 1 148 ? 23.343  -7.725  18.649 1.00 27.40  ?  173 PHE   B CE1    1 
ATOM   8682  C  CE2    . PHE   B 1 148 ? 22.981  -10.093 18.459 1.00 27.52  ?  173 PHE   B CE2    1 
ATOM   8683  C  CZ     . PHE   B 1 148 ? 22.473  -8.811  18.609 1.00 27.37  ?  173 PHE   B CZ     1 
ATOM   8684  H  H      . PHE   B 1 148 ? 26.738  -11.156 16.321 1.00 32.63  ?  173 PHE   B H      1 
ATOM   8685  H  HA     . PHE   B 1 148 ? 26.711  -8.438  16.424 1.00 32.81  ?  173 PHE   B HA     1 
ATOM   8686  H  HB2    . PHE   B 1 148 ? 26.910  -10.335 18.489 1.00 32.99  ?  173 PHE   B HB2    1 
ATOM   8687  H  HB3    . PHE   B 1 148 ? 27.169  -8.788  18.745 1.00 32.99  ?  173 PHE   B HB3    1 
ATOM   8688  H  HD1    . PHE   B 1 148 ? 25.288  -7.204  18.540 1.00 32.73  ?  173 PHE   B HD1    1 
ATOM   8689  H  HD2    . PHE   B 1 148 ? 24.676  -11.149 18.209 1.00 32.56  ?  173 PHE   B HD2    1 
ATOM   8690  H  HE1    . PHE   B 1 148 ? 23.009  -6.864  18.756 1.00 32.88  ?  173 PHE   B HE1    1 
ATOM   8691  H  HE2    . PHE   B 1 148 ? 22.404  -10.822 18.444 1.00 33.01  ?  173 PHE   B HE2    1 
ATOM   8692  H  HZ     . PHE   B 1 148 ? 21.556  -8.677  18.683 1.00 32.84  ?  173 PHE   B HZ     1 
ATOM   8693  N  N      . SER   B 1 149 ? 29.174  -9.512  15.439 1.00 30.09  ?  174 SER   B N      1 
ATOM   8694  C  CA     . SER   B 1 149 ? 30.555  -9.260  15.065 1.00 31.30  ?  174 SER   B CA     1 
ATOM   8695  C  C      . SER   B 1 149 ? 30.631  -8.545  13.718 1.00 34.18  ?  174 SER   B C      1 
ATOM   8696  O  O      . SER   B 1 149 ? 29.803  -8.762  12.826 1.00 34.72  ?  174 SER   B O      1 
ATOM   8697  C  CB     . SER   B 1 149 ? 31.361  -10.569 14.969 1.00 32.21  ?  174 SER   B CB     1 
ATOM   8698  O  OG     . SER   B 1 149 ? 31.483  -11.237 16.218 1.00 31.51  ?  174 SER   B OG     1 
ATOM   8699  H  H      . SER   B 1 149 ? 28.751  -9.988  14.862 1.00 36.10  ?  174 SER   B H      1 
ATOM   8700  H  HA     . SER   B 1 149 ? 30.952  -8.687  15.740 1.00 37.55  ?  174 SER   B HA     1 
ATOM   8701  H  HB2    . SER   B 1 149 ? 30.912  -11.162 14.346 1.00 38.64  ?  174 SER   B HB2    1 
ATOM   8702  H  HB3    . SER   B 1 149 ? 32.251  -10.360 14.644 1.00 38.64  ?  174 SER   B HB3    1 
ATOM   8703  H  HG     . SER   B 1 149 ? 30.722  -11.433 16.515 1.00 37.80  ?  174 SER   B HG     1 
ATOM   8704  N  N      . THR   B 1 150 ? 31.652  -7.696  13.567 1.00 34.81  ?  175 THR   B N      1 
ATOM   8705  C  CA     . THR   B 1 150 ? 31.935  -7.118  12.260 1.00 36.34  ?  175 THR   B CA     1 
ATOM   8706  C  C      . THR   B 1 150 ? 32.724  -8.067  11.368 1.00 37.93  ?  175 THR   B C      1 
ATOM   8707  O  O      . THR   B 1 150 ? 32.728  -7.891  10.145 1.00 39.55  ?  175 THR   B O      1 
ATOM   8708  C  CB     . THR   B 1 150 ? 32.717  -5.810  12.390 1.00 38.53  ?  175 THR   B CB     1 
ATOM   8709  O  OG1    . THR   B 1 150 ? 33.954  -6.051  13.072 1.00 38.95  ?  175 THR   B OG1    1 
ATOM   8710  C  CG2    . THR   B 1 150 ? 31.914  -4.786  13.151 1.00 38.18  ?  175 THR   B CG2    1 
ATOM   8711  H  H      . THR   B 1 150 ? 32.182  -7.447  14.197 1.00 41.77  ?  175 THR   B H      1 
ATOM   8712  H  HA     . THR   B 1 150 ? 31.087  -6.914  11.836 1.00 43.60  ?  175 THR   B HA     1 
ATOM   8713  H  HB     . THR   B 1 150 ? 32.902  -5.457  11.506 1.00 46.23  ?  175 THR   B HB     1 
ATOM   8714  H  HG1    . THR   B 1 150 ? 34.385  -5.334  13.147 1.00 46.73  ?  175 THR   B HG1    1 
ATOM   8715  H  HG21   . THR   B 1 150 ? 32.416  -3.958  13.223 1.00 45.81  ?  175 THR   B HG21   1 
ATOM   8716  H  HG22   . THR   B 1 150 ? 31.080  -4.609  12.690 1.00 45.81  ?  175 THR   B HG22   1 
ATOM   8717  H  HG23   . THR   B 1 150 ? 31.718  -5.113  14.043 1.00 45.81  ?  175 THR   B HG23   1 
ATOM   8718  N  N      . LYS   B 1 151 ? 33.411  -9.044  11.959 1.00 37.46  ?  176 LYS   B N      1 
ATOM   8719  C  CA     . LYS   B 1 151 ? 34.135  -10.065 11.213 1.00 38.42  ?  176 LYS   B CA     1 
ATOM   8720  C  C      . LYS   B 1 151 ? 34.133  -11.330 12.056 1.00 36.52  ?  176 LYS   B C      1 
ATOM   8721  O  O      . LYS   B 1 151 ? 34.363  -11.271 13.265 1.00 36.44  ?  176 LYS   B O      1 
ATOM   8722  C  CB     . LYS   B 1 151 ? 35.565  -9.631  10.896 1.00 41.05  ?  176 LYS   B CB     1 
ATOM   8723  C  CG     . LYS   B 1 151 ? 36.267  -10.515 9.871  1.00 43.94  ?  176 LYS   B CG     1 
ATOM   8724  C  CD     . LYS   B 1 151 ? 37.588  -9.902  9.419  1.00 47.84  ?  176 LYS   B CD     1 
ATOM   8725  C  CE     . LYS   B 1 151 ? 38.604  -9.858  10.554 1.00 51.43  ?  176 LYS   B CE     1 
ATOM   8726  N  NZ     . LYS   B 1 151 ? 38.919  -11.219 11.087 1.00 54.01  ?  176 LYS   B NZ     1 
ATOM   8727  H  H      . LYS   B 1 151 ? 33.474  -9.137  12.811 1.00 44.95  ?  176 LYS   B H      1 
ATOM   8728  H  HA     . LYS   B 1 151 ? 33.696  -10.242 10.366 1.00 46.09  ?  176 LYS   B HA     1 
ATOM   8729  H  HB2    . LYS   B 1 151 ? 35.546  -8.728  10.543 1.00 49.26  ?  176 LYS   B HB2    1 
ATOM   8730  H  HB3    . LYS   B 1 151 ? 36.086  -9.656  11.714 1.00 49.26  ?  176 LYS   B HB3    1 
ATOM   8731  H  HG2    . LYS   B 1 151 ? 36.452  -11.382 10.266 1.00 52.72  ?  176 LYS   B HG2    1 
ATOM   8732  H  HG3    . LYS   B 1 151 ? 35.697  -10.620 9.093  1.00 52.72  ?  176 LYS   B HG3    1 
ATOM   8733  H  HD2    . LYS   B 1 151 ? 37.959  -10.435 8.699  1.00 57.40  ?  176 LYS   B HD2    1 
ATOM   8734  H  HD3    . LYS   B 1 151 ? 37.433  -8.994  9.115  1.00 57.40  ?  176 LYS   B HD3    1 
ATOM   8735  H  HE2    . LYS   B 1 151 ? 39.428  -9.464  10.228 1.00 61.71  ?  176 LYS   B HE2    1 
ATOM   8736  H  HE3    . LYS   B 1 151 ? 38.246  -9.325  11.281 1.00 61.71  ?  176 LYS   B HE3    1 
ATOM   8737  H  HZ1    . LYS   B 1 151 ? 39.595  -11.171 11.664 1.00 64.81  ?  176 LYS   B HZ1    1 
ATOM   8738  H  HZ2    . LYS   B 1 151 ? 38.208  -11.555 11.503 1.00 64.81  ?  176 LYS   B HZ2    1 
ATOM   8739  H  HZ3    . LYS   B 1 151 ? 39.147  -11.762 10.420 1.00 64.81  ?  176 LYS   B HZ3    1 
ATOM   8740  N  N      . PHE   B 1 152 ? 33.877  -12.467 11.415 1.00 35.90  ?  177 PHE   B N      1 
ATOM   8741  C  CA     . PHE   B 1 152 ? 33.690  -13.735 12.112 1.00 34.60  ?  177 PHE   B CA     1 
ATOM   8742  C  C      . PHE   B 1 152 ? 34.221  -14.838 11.212 1.00 36.83  ?  177 PHE   B C      1 
ATOM   8743  O  O      . PHE   B 1 152 ? 33.677  -15.053 10.123 1.00 37.28  ?  177 PHE   B O      1 
ATOM   8744  C  CB     . PHE   B 1 152 ? 32.188  -13.931 12.444 1.00 34.59  ?  177 PHE   B CB     1 
ATOM   8745  C  CG     . PHE   B 1 152 ? 31.870  -15.185 13.215 1.00 32.95  ?  177 PHE   B CG     1 
ATOM   8746  C  CD1    . PHE   B 1 152 ? 31.611  -16.372 12.550 1.00 32.62  ?  177 PHE   B CD1    1 
ATOM   8747  C  CD2    . PHE   B 1 152 ? 31.781  -15.165 14.603 1.00 32.92  ?  177 PHE   B CD2    1 
ATOM   8748  C  CE1    . PHE   B 1 152 ? 31.301  -17.524 13.251 1.00 33.15  ?  177 PHE   B CE1    1 
ATOM   8749  C  CE2    . PHE   B 1 152 ? 31.473  -16.317 15.311 1.00 31.96  ?  177 PHE   B CE2    1 
ATOM   8750  C  CZ     . PHE   B 1 152 ? 31.229  -17.498 14.634 1.00 32.60  ?  177 PHE   B CZ     1 
ATOM   8751  H  H      . PHE   B 1 152 ? 33.806  -12.531 10.560 1.00 43.08  ?  177 PHE   B H      1 
ATOM   8752  H  HA     . PHE   B 1 152 ? 34.192  -13.763 12.941 1.00 41.52  ?  177 PHE   B HA     1 
ATOM   8753  H  HB2    . PHE   B 1 152 ? 31.891  -13.177 12.977 1.00 41.51  ?  177 PHE   B HB2    1 
ATOM   8754  H  HB3    . PHE   B 1 152 ? 31.691  -13.966 11.612 1.00 41.51  ?  177 PHE   B HB3    1 
ATOM   8755  H  HD1    . PHE   B 1 152 ? 31.646  -16.395 11.621 1.00 39.14  ?  177 PHE   B HD1    1 
ATOM   8756  H  HD2    . PHE   B 1 152 ? 31.930  -14.370 15.061 1.00 39.50  ?  177 PHE   B HD2    1 
ATOM   8757  H  HE1    . PHE   B 1 152 ? 31.140  -18.318 12.793 1.00 39.77  ?  177 PHE   B HE1    1 
ATOM   8758  H  HE2    . PHE   B 1 152 ? 31.432  -16.295 16.240 1.00 38.35  ?  177 PHE   B HE2    1 
ATOM   8759  H  HZ     . PHE   B 1 152 ? 31.017  -18.271 15.106 1.00 39.11  ?  177 PHE   B HZ     1 
ATOM   8760  N  N      . THR   B 1 153 ? 35.288  -15.513 11.650 1.00 37.04  ?  178 THR   B N      1 
ATOM   8761  C  CA     . THR   B 1 153 ? 35.957  -16.529 10.845 1.00 38.30  ?  178 THR   B CA     1 
ATOM   8762  C  C      . THR   B 1 153 ? 35.876  -17.900 11.494 1.00 38.72  ?  178 THR   B C      1 
ATOM   8763  O  O      . THR   B 1 153 ? 36.137  -18.042 12.695 1.00 38.18  ?  178 THR   B O      1 
ATOM   8764  C  CB     . THR   B 1 153 ? 37.431  -16.173 10.608 1.00 40.22  ?  178 THR   B CB     1 
ATOM   8765  O  OG1    . THR   B 1 153 ? 37.507  -14.904 9.955  1.00 42.28  ?  178 THR   B OG1    1 
ATOM   8766  C  CG2    . THR   B 1 153 ? 38.131  -17.261 9.757  1.00 40.60  ?  178 THR   B CG2    1 
ATOM   8767  H  H      . THR   B 1 153 ? 35.645  -15.395 12.423 1.00 44.44  ?  178 THR   B H      1 
ATOM   8768  H  HA     . THR   B 1 153 ? 35.491  -16.577 9.995  1.00 45.95  ?  178 THR   B HA     1 
ATOM   8769  H  HB     . THR   B 1 153 ? 37.900  -16.125 11.456 1.00 48.26  ?  178 THR   B HB     1 
ATOM   8770  H  HG1    . THR   B 1 153 ? 37.112  -14.938 9.215  1.00 50.73  ?  178 THR   B HG1    1 
ATOM   8771  H  HG21   . THR   B 1 153 ? 38.970  -16.921 9.409  1.00 48.71  ?  178 THR   B HG21   1 
ATOM   8772  H  HG22   . THR   B 1 153 ? 38.311  -18.043 10.302 1.00 48.71  ?  178 THR   B HG22   1 
ATOM   8773  H  HG23   . THR   B 1 153 ? 37.562  -17.518 9.015  1.00 48.71  ?  178 THR   B HG23   1 
ATOM   8774  N  N      . VAL   B 1 154 ? 35.546  -18.900 10.682 1.00 38.54  ?  179 VAL   B N      1 
ATOM   8775  C  CA     . VAL   B 1 154 ? 35.450  -20.296 11.083 1.00 38.40  ?  179 VAL   B CA     1 
ATOM   8776  C  C      . VAL   B 1 154 ? 36.551  -21.057 10.362 1.00 39.32  ?  179 VAL   B C      1 
ATOM   8777  O  O      . VAL   B 1 154 ? 36.611  -21.030 9.130  1.00 40.34  ?  179 VAL   B O      1 
ATOM   8778  C  CB     . VAL   B 1 154 ? 34.079  -20.882 10.713 1.00 38.09  ?  179 VAL   B CB     1 
ATOM   8779  C  CG1    . VAL   B 1 154 ? 34.018  -22.375 11.043 1.00 38.45  ?  179 VAL   B CG1    1 
ATOM   8780  C  CG2    . VAL   B 1 154 ? 32.958  -20.118 11.407 1.00 37.72  ?  179 VAL   B CG2    1 
ATOM   8781  H  H      . VAL   B 1 154 ? 35.364  -18.785 9.849  1.00 46.25  ?  179 VAL   B H      1 
ATOM   8782  H  HA     . VAL   B 1 154 ? 35.584  -20.369 12.040 1.00 46.08  ?  179 VAL   B HA     1 
ATOM   8783  H  HB     . VAL   B 1 154 ? 33.951  -20.788 9.757  1.00 45.70  ?  179 VAL   B HB     1 
ATOM   8784  H  HG11   . VAL   B 1 154 ? 33.094  -22.669 11.004 1.00 46.14  ?  179 VAL   B HG11   1 
ATOM   8785  H  HG12   . VAL   B 1 154 ? 34.549  -22.864 10.395 1.00 46.14  ?  179 VAL   B HG12   1 
ATOM   8786  H  HG13   . VAL   B 1 154 ? 34.372  -22.516 11.935 1.00 46.14  ?  179 VAL   B HG13   1 
ATOM   8787  H  HG21   . VAL   B 1 154 ? 32.108  -20.524 11.175 1.00 45.26  ?  179 VAL   B HG21   1 
ATOM   8788  H  HG22   . VAL   B 1 154 ? 33.094  -20.160 12.366 1.00 45.26  ?  179 VAL   B HG22   1 
ATOM   8789  H  HG23   . VAL   B 1 154 ? 32.975  -19.194 11.111 1.00 45.26  ?  179 VAL   B HG23   1 
ATOM   8790  N  N      . GLU   B 1 155 ? 37.409  -21.752 11.112 1.00 38.90  ?  180 GLU   B N      1 
ATOM   8791  C  CA     . GLU   B 1 155 ? 38.417  -22.639 10.534 1.00 41.19  ?  180 GLU   B CA     1 
ATOM   8792  C  C      . GLU   B 1 155 ? 38.346  -23.975 11.259 1.00 41.49  ?  180 GLU   B C      1 
ATOM   8793  O  O      . GLU   B 1 155 ? 38.397  -24.016 12.492 1.00 40.11  ?  180 GLU   B O      1 
ATOM   8794  C  CB     . GLU   B 1 155 ? 39.829  -22.042 10.639 1.00 43.06  ?  180 GLU   B CB     1 
ATOM   8795  C  CG     . GLU   B 1 155 ? 40.903  -22.883 9.942  1.00 46.26  ?  180 GLU   B CG     1 
ATOM   8796  C  CD     . GLU   B 1 155 ? 42.272  -22.209 9.886  1.00 49.39  ?  180 GLU   B CD     1 
ATOM   8797  O  OE1    . GLU   B 1 155 ? 42.347  -20.961 9.793  1.00 50.18  ?  180 GLU   B OE1    1 
ATOM   8798  O  OE2    . GLU   B 1 155 ? 43.279  -22.947 9.934  1.00 50.86  ?  180 GLU   B OE2    1 
ATOM   8799  H  H      . GLU   B 1 155 ? 37.426  -21.725 11.971 1.00 46.67  ?  180 GLU   B H      1 
ATOM   8800  H  HA     . GLU   B 1 155 ? 38.230  -22.779 9.592  1.00 49.42  ?  180 GLU   B HA     1 
ATOM   8801  H  HB2    . GLU   B 1 155 ? 39.828  -21.163 10.230 1.00 51.67  ?  180 GLU   B HB2    1 
ATOM   8802  H  HB3    . GLU   B 1 155 ? 40.069  -21.972 11.576 1.00 51.67  ?  180 GLU   B HB3    1 
ATOM   8803  H  HG2    . GLU   B 1 155 ? 41.005  -23.720 10.421 1.00 55.50  ?  180 GLU   B HG2    1 
ATOM   8804  H  HG3    . GLU   B 1 155 ? 40.622  -23.056 9.030  1.00 55.50  ?  180 GLU   B HG3    1 
ATOM   8805  N  N      . THR   B 1 156 ? 38.212  -25.063 10.505 1.00 41.52  ?  181 THR   B N      1 
ATOM   8806  C  CA     . THR   B 1 156 ? 38.065  -26.381 11.111 1.00 41.84  ?  181 THR   B CA     1 
ATOM   8807  C  C      . THR   B 1 156 ? 38.645  -27.425 10.171 1.00 43.46  ?  181 THR   B C      1 
ATOM   8808  O  O      . THR   B 1 156 ? 38.417  -27.384 8.960  1.00 42.90  ?  181 THR   B O      1 
ATOM   8809  C  CB     . THR   B 1 156 ? 36.596  -26.682 11.446 1.00 42.56  ?  181 THR   B CB     1 
ATOM   8810  O  OG1    . THR   B 1 156 ? 36.505  -27.934 12.144 1.00 41.53  ?  181 THR   B OG1    1 
ATOM   8811  C  CG2    . THR   B 1 156 ? 35.739  -26.737 10.199 1.00 42.30  ?  181 THR   B CG2    1 
ATOM   8812  H  H      . THR   B 1 156 ? 38.203  -25.063 9.645  1.00 49.82  ?  181 THR   B H      1 
ATOM   8813  H  HA     . THR   B 1 156 ? 38.567  -26.423 11.939 1.00 50.20  ?  181 THR   B HA     1 
ATOM   8814  H  HB     . THR   B 1 156 ? 36.253  -25.969 12.007 1.00 51.07  ?  181 THR   B HB     1 
ATOM   8815  H  HG1    . THR   B 1 156 ? 36.953  -27.900 12.854 1.00 49.83  ?  181 THR   B HG1    1 
ATOM   8816  H  HG21   . THR   B 1 156 ? 34.802  -26.797 10.444 1.00 50.75  ?  181 THR   B HG21   1 
ATOM   8817  H  HG22   . THR   B 1 156 ? 35.875  -25.938 9.667  1.00 50.75  ?  181 THR   B HG22   1 
ATOM   8818  H  HG23   . THR   B 1 156 ? 35.975  -27.513 9.668  1.00 50.75  ?  181 THR   B HG23   1 
ATOM   8819  N  N      . ALA   B 1 157 ? 39.414  -28.345 10.743 1.00 43.98  ?  182 ALA   B N      1 
ATOM   8820  C  CA     . ALA   B 1 157 ? 40.188  -29.319 9.986  1.00 45.41  ?  182 ALA   B CA     1 
ATOM   8821  C  C      . ALA   B 1 157 ? 39.740  -30.723 10.353 1.00 46.66  ?  182 ALA   B C      1 
ATOM   8822  O  O      . ALA   B 1 157 ? 39.665  -31.071 11.537 1.00 46.40  ?  182 ALA   B O      1 
ATOM   8823  C  CB     . ALA   B 1 157 ? 41.682  -29.134 10.259 1.00 45.15  ?  182 ALA   B CB     1 
ATOM   8824  H  H      . ALA   B 1 157 ? 39.505  -28.427 11.594 1.00 52.78  ?  182 ALA   B H      1 
ATOM   8825  H  HA     . ALA   B 1 157 ? 40.031  -29.204 9.036  1.00 54.49  ?  182 ALA   B HA     1 
ATOM   8826  H  HB1    . ALA   B 1 157 ? 42.182  -29.761 9.714  1.00 54.17  ?  182 ALA   B HB1    1 
ATOM   8827  H  HB2    . ALA   B 1 157 ? 41.934  -28.225 10.032 1.00 54.17  ?  182 ALA   B HB2    1 
ATOM   8828  H  HB3    . ALA   B 1 157 ? 41.854  -29.300 11.199 1.00 54.17  ?  182 ALA   B HB3    1 
ATOM   8829  N  N      . SER   B 1 158 ? 39.457  -31.527 9.333  1.00 47.18  ?  183 SER   B N      1 
ATOM   8830  C  CA     . SER   B 1 158 ? 38.897  -32.865 9.508  1.00 46.47  ?  183 SER   B CA     1 
ATOM   8831  C  C      . SER   B 1 158 ? 39.771  -33.876 8.774  1.00 48.58  ?  183 SER   B C      1 
ATOM   8832  O  O      . SER   B 1 158 ? 39.676  -33.982 7.550  1.00 48.94  ?  183 SER   B O      1 
ATOM   8833  C  CB     . SER   B 1 158 ? 37.472  -32.922 8.988  1.00 46.99  ?  183 SER   B CB     1 
ATOM   8834  O  OG     . SER   B 1 158 ? 36.955  -34.240 9.080  1.00 48.57  ?  183 SER   B OG     1 
ATOM   8835  H  H      . SER   B 1 158 ? 39.585  -31.315 8.510  1.00 56.61  ?  183 SER   B H      1 
ATOM   8836  H  HA     . SER   B 1 158 ? 38.912  -33.084 10.453 1.00 55.76  ?  183 SER   B HA     1 
ATOM   8837  H  HB2    . SER   B 1 158 ? 36.918  -32.328 9.519  1.00 56.38  ?  183 SER   B HB2    1 
ATOM   8838  H  HB3    . SER   B 1 158 ? 37.463  -32.643 8.059  1.00 56.38  ?  183 SER   B HB3    1 
ATOM   8839  H  HG     . SER   B 1 158 ? 36.139  -34.243 8.882  1.00 58.28  ?  183 SER   B HG     1 
ATOM   8840  N  N      . ARG   B 1 159 ? 40.592  -34.622 9.519  1.00 49.08  ?  184 ARG   B N      1 
ATOM   8841  C  CA     . ARG   B 1 159 ? 41.388  -35.679 8.899  1.00 50.89  ?  184 ARG   B CA     1 
ATOM   8842  C  C      . ARG   B 1 159 ? 40.505  -36.753 8.276  1.00 51.92  ?  184 ARG   B C      1 
ATOM   8843  O  O      . ARG   B 1 159 ? 40.898  -37.369 7.276  1.00 52.11  ?  184 ARG   B O      1 
ATOM   8844  C  CB     . ARG   B 1 159 ? 42.336  -36.300 9.928  1.00 52.40  ?  184 ARG   B CB     1 
ATOM   8845  C  CG     . ARG   B 1 159 ? 43.364  -37.302 9.352  1.00 55.86  ?  184 ARG   B CG     1 
ATOM   8846  C  CD     . ARG   B 1 159 ? 44.545  -37.432 10.309 1.00 59.52  ?  184 ARG   B CD     1 
ATOM   8847  N  NE     . ARG   B 1 159 ? 45.359  -38.623 10.107 1.00 64.43  ?  184 ARG   B NE     1 
ATOM   8848  C  CZ     . ARG   B 1 159 ? 46.192  -39.109 11.023 1.00 67.58  ?  184 ARG   B CZ     1 
ATOM   8849  N  NH1    . ARG   B 1 159 ? 46.310  -38.504 12.200 1.00 69.23  ?  184 ARG   B NH1    1 
ATOM   8850  N  NH2    . ARG   B 1 159 ? 46.895  -40.202 10.765 1.00 68.92  ?  184 ARG   B NH2    1 
ATOM   8851  H  H      . ARG   B 1 159 ? 40.703  -34.537 10.367 1.00 58.89  ?  184 ARG   B H      1 
ATOM   8852  H  HA     . ARG   B 1 159 ? 41.928  -35.288 8.195  1.00 61.07  ?  184 ARG   B HA     1 
ATOM   8853  H  HB2    . ARG   B 1 159 ? 42.834  -35.586 10.356 1.00 62.87  ?  184 ARG   B HB2    1 
ATOM   8854  H  HB3    . ARG   B 1 159 ? 41.805  -36.775 10.587 1.00 62.87  ?  184 ARG   B HB3    1 
ATOM   8855  H  HG2    . ARG   B 1 159 ? 42.950  -38.172 9.245  1.00 67.02  ?  184 ARG   B HG2    1 
ATOM   8856  H  HG3    . ARG   B 1 159 ? 43.690  -36.982 8.496  1.00 67.02  ?  184 ARG   B HG3    1 
ATOM   8857  H  HD2    . ARG   B 1 159 ? 45.122  -36.660 10.196 1.00 71.42  ?  184 ARG   B HD2    1 
ATOM   8858  H  HD3    . ARG   B 1 159 ? 44.205  -37.461 11.218 1.00 71.42  ?  184 ARG   B HD3    1 
ATOM   8859  H  HE     . ARG   B 1 159 ? 45.297  -39.034 9.354  1.00 77.31  ?  184 ARG   B HE     1 
ATOM   8860  H  HH11   . ARG   B 1 159 ? 45.849  -37.798 12.369 1.00 83.07  ?  184 ARG   B HH11   1 
ATOM   8861  H  HH12   . ARG   B 1 159 ? 46.849  -38.818 12.792 1.00 83.07  ?  184 ARG   B HH12   1 
ATOM   8862  H  HH21   . ARG   B 1 159 ? 46.814  -40.598 10.006 1.00 82.69  ?  184 ARG   B HH21   1 
ATOM   8863  H  HH22   . ARG   B 1 159 ? 47.434  -40.516 11.358 1.00 82.69  ?  184 ARG   B HH22   1 
ATOM   8864  N  N      . GLU   B 1 160 ? 39.317  -36.996 8.847  1.00 52.62  ?  185 GLU   B N      1 
ATOM   8865  C  CA     . GLU   B 1 160 ? 38.409  -37.984 8.266  1.00 53.45  ?  185 GLU   B CA     1 
ATOM   8866  C  C      . GLU   B 1 160 ? 38.070  -37.626 6.822  1.00 53.48  ?  185 GLU   B C      1 
ATOM   8867  O  O      . GLU   B 1 160 ? 38.145  -38.471 5.925  1.00 52.91  ?  185 GLU   B O      1 
ATOM   8868  C  CB     . GLU   B 1 160 ? 37.123  -38.108 9.093  1.00 54.65  ?  185 GLU   B CB     1 
ATOM   8869  C  CG     . GLU   B 1 160 ? 36.125  -39.114 8.490  1.00 55.11  ?  185 GLU   B CG     1 
ATOM   8870  C  CD     . GLU   B 1 160 ? 34.858  -39.294 9.311  1.00 56.01  ?  185 GLU   B CD     1 
ATOM   8871  O  OE1    . GLU   B 1 160 ? 34.761  -38.704 10.404 1.00 55.25  ?  185 GLU   B OE1    1 
ATOM   8872  O  OE2    . GLU   B 1 160 ? 33.957  -40.034 8.860  1.00 57.24  ?  185 GLU   B OE2    1 
ATOM   8873  H  H      . GLU   B 1 160 ? 39.021  -36.609 9.556  1.00 63.13  ?  185 GLU   B H      1 
ATOM   8874  H  HA     . GLU   B 1 160 ? 38.855  -38.846 8.284  1.00 64.14  ?  185 GLU   B HA     1 
ATOM   8875  H  HB2    . GLU   B 1 160 ? 37.350  -38.409 9.987  1.00 65.57  ?  185 GLU   B HB2    1 
ATOM   8876  H  HB3    . GLU   B 1 160 ? 36.689  -37.242 9.134  1.00 65.57  ?  185 GLU   B HB3    1 
ATOM   8877  H  HG2    . GLU   B 1 160 ? 35.865  -38.804 7.609  1.00 66.13  ?  185 GLU   B HG2    1 
ATOM   8878  H  HG3    . GLU   B 1 160 ? 36.558  -39.980 8.423  1.00 66.13  ?  185 GLU   B HG3    1 
ATOM   8879  N  N      . TYR   B 1 161 ? 37.684  -36.378 6.578  1.00 52.54  ?  186 TYR   B N      1 
ATOM   8880  C  CA     . TYR   B 1 161 ? 37.394  -35.907 5.229  1.00 52.71  ?  186 TYR   B CA     1 
ATOM   8881  C  C      . TYR   B 1 161 ? 38.638  -35.395 4.513  1.00 52.82  ?  186 TYR   B C      1 
ATOM   8882  O  O      . TYR   B 1 161 ? 38.529  -34.920 3.379  1.00 52.52  ?  186 TYR   B O      1 
ATOM   8883  C  CB     . TYR   B 1 161 ? 36.304  -34.828 5.292  1.00 53.11  ?  186 TYR   B CB     1 
ATOM   8884  C  CG     . TYR   B 1 161 ? 34.961  -35.415 5.688  1.00 53.43  ?  186 TYR   B CG     1 
ATOM   8885  C  CD1    . TYR   B 1 161 ? 34.651  -35.659 7.021  1.00 52.46  ?  186 TYR   B CD1    1 
ATOM   8886  C  CD2    . TYR   B 1 161 ? 34.022  -35.767 4.725  1.00 54.00  ?  186 TYR   B CD2    1 
ATOM   8887  C  CE1    . TYR   B 1 161 ? 33.440  -36.220 7.380  1.00 53.88  ?  186 TYR   B CE1    1 
ATOM   8888  C  CE2    . TYR   B 1 161 ? 32.807  -36.323 5.076  1.00 54.86  ?  186 TYR   B CE2    1 
ATOM   8889  C  CZ     . TYR   B 1 161 ? 32.521  -36.548 6.402  1.00 55.07  ?  186 TYR   B CZ     1 
ATOM   8890  O  OH     . TYR   B 1 161 ? 31.312  -37.104 6.746  1.00 56.73  ?  186 TYR   B OH     1 
ATOM   8891  H  H      . TYR   B 1 161 ? 37.581  -35.778 7.185  1.00 63.04  ?  186 TYR   B H      1 
ATOM   8892  H  HA     . TYR   B 1 161 ? 37.043  -36.634 4.691  1.00 63.25  ?  186 TYR   B HA     1 
ATOM   8893  H  HB2    . TYR   B 1 161 ? 36.552  -34.160 5.950  1.00 63.73  ?  186 TYR   B HB2    1 
ATOM   8894  H  HB3    . TYR   B 1 161 ? 36.212  -34.415 4.419  1.00 63.73  ?  186 TYR   B HB3    1 
ATOM   8895  H  HD1    . TYR   B 1 161 ? 35.268  -35.442 7.682  1.00 62.95  ?  186 TYR   B HD1    1 
ATOM   8896  H  HD2    . TYR   B 1 161 ? 34.216  -35.625 3.826  1.00 64.80  ?  186 TYR   B HD2    1 
ATOM   8897  H  HE1    . TYR   B 1 161 ? 33.244  -36.375 8.276  1.00 64.64  ?  186 TYR   B HE1    1 
ATOM   8898  H  HE2    . TYR   B 1 161 ? 32.186  -36.543 4.420  1.00 65.82  ?  186 TYR   B HE2    1 
ATOM   8899  H  HH     . TYR   B 1 161 ? 30.758  -36.995 6.124  1.00 68.07  ?  186 TYR   B HH     1 
ATOM   8900  N  N      . LYS   B 1 162 ? 39.809  -35.498 5.145  1.00 53.68  ?  187 LYS   B N      1 
ATOM   8901  C  CA     . LYS   B 1 162 ? 41.084  -35.057 4.565  1.00 54.45  ?  187 LYS   B CA     1 
ATOM   8902  C  C      . LYS   B 1 162 ? 40.996  -33.646 3.983  1.00 53.75  ?  187 LYS   B C      1 
ATOM   8903  O  O      . LYS   B 1 162 ? 41.614  -33.326 2.965  1.00 54.15  ?  187 LYS   B O      1 
ATOM   8904  C  CB     . LYS   B 1 162 ? 41.574  -36.073 3.523  1.00 58.17  ?  187 LYS   B CB     1 
ATOM   8905  C  CG     . LYS   B 1 162 ? 41.918  -37.427 4.148  1.00 61.39  ?  187 LYS   B CG     1 
ATOM   8906  C  CD     . LYS   B 1 162 ? 42.398  -38.446 3.133  1.00 65.36  ?  187 LYS   B CD     1 
ATOM   8907  C  CE     . LYS   B 1 162 ? 42.814  -39.748 3.816  1.00 67.62  ?  187 LYS   B CE     1 
ATOM   8908  N  NZ     . LYS   B 1 162 ? 43.350  -40.755 2.853  1.00 69.19  ?  187 LYS   B NZ     1 
ATOM   8909  H  H      . LYS   B 1 162 ? 39.896  -35.829 5.934  1.00 64.41  ?  187 LYS   B H      1 
ATOM   8910  H  HA     . LYS   B 1 162 ? 41.742  -35.011 5.276  1.00 65.34  ?  187 LYS   B HA     1 
ATOM   8911  H  HB2    . LYS   B 1 162 ? 40.876  -36.213 2.864  1.00 69.80  ?  187 LYS   B HB2    1 
ATOM   8912  H  HB3    . LYS   B 1 162 ? 42.372  -35.726 3.093  1.00 69.80  ?  187 LYS   B HB3    1 
ATOM   8913  H  HG2    . LYS   B 1 162 ? 42.624  -37.303 4.802  1.00 73.66  ?  187 LYS   B HG2    1 
ATOM   8914  H  HG3    . LYS   B 1 162 ? 41.127  -37.786 4.579  1.00 73.66  ?  187 LYS   B HG3    1 
ATOM   8915  H  HD2    . LYS   B 1 162 ? 41.682  -38.643 2.508  1.00 78.42  ?  187 LYS   B HD2    1 
ATOM   8916  H  HD3    . LYS   B 1 162 ? 43.165  -38.091 2.656  1.00 78.42  ?  187 LYS   B HD3    1 
ATOM   8917  H  HE2    . LYS   B 1 162 ? 43.507  -39.557 4.468  1.00 81.14  ?  187 LYS   B HE2    1 
ATOM   8918  H  HE3    . LYS   B 1 162 ? 42.042  -40.136 4.257  1.00 81.14  ?  187 LYS   B HE3    1 
ATOM   8919  H  HZ1    . LYS   B 1 162 ? 43.580  -41.498 3.285  1.00 83.03  ?  187 LYS   B HZ1    1 
ATOM   8920  H  HZ2    . LYS   B 1 162 ? 42.731  -40.954 2.245  1.00 83.03  ?  187 LYS   B HZ2    1 
ATOM   8921  H  HZ3    . LYS   B 1 162 ? 44.067  -40.428 2.438  1.00 83.03  ?  187 LYS   B HZ3    1 
ATOM   8922  N  N      . LYS   B 1 163 ? 40.270  -32.769 4.665  1.00 52.20  ?  188 LYS   B N      1 
ATOM   8923  C  CA     . LYS   B 1 163 ? 40.143  -31.395 4.205  1.00 51.27  ?  188 LYS   B CA     1 
ATOM   8924  C  C      . LYS   B 1 163 ? 40.102  -30.442 5.390  1.00 50.23  ?  188 LYS   B C      1 
ATOM   8925  O  O      . LYS   B 1 163 ? 39.693  -30.814 6.493  1.00 50.06  ?  188 LYS   B O      1 
ATOM   8926  C  CB     . LYS   B 1 163 ? 38.878  -31.195 3.359  1.00 52.50  ?  188 LYS   B CB     1 
ATOM   8927  C  CG     . LYS   B 1 163 ? 38.886  -31.880 2.012  1.00 55.18  ?  188 LYS   B CG     1 
ATOM   8928  C  CD     . LYS   B 1 163 ? 37.691  -31.427 1.188  1.00 57.83  ?  188 LYS   B CD     1 
ATOM   8929  C  CE     . LYS   B 1 163 ? 37.650  -32.130 -0.153 1.00 60.64  ?  188 LYS   B CE     1 
ATOM   8930  N  NZ     . LYS   B 1 163 ? 36.454  -31.733 -0.950 1.00 62.48  ?  188 LYS   B NZ     1 
ATOM   8931  H  H      . LYS   B 1 163 ? 39.846  -32.945 5.392  1.00 62.63  ?  188 LYS   B H      1 
ATOM   8932  H  HA     . LYS   B 1 163 ? 40.922  -31.178 3.670  1.00 61.52  ?  188 LYS   B HA     1 
ATOM   8933  H  HB2    . LYS   B 1 163 ? 38.120  -31.541 3.855  1.00 62.99  ?  188 LYS   B HB2    1 
ATOM   8934  H  HB3    . LYS   B 1 163 ? 38.765  -30.245 3.199  1.00 62.99  ?  188 LYS   B HB3    1 
ATOM   8935  H  HG2    . LYS   B 1 163 ? 39.698  -31.651 1.534  1.00 66.22  ?  188 LYS   B HG2    1 
ATOM   8936  H  HG3    . LYS   B 1 163 ? 38.833  -32.841 2.134  1.00 66.22  ?  188 LYS   B HG3    1 
ATOM   8937  H  HD2    . LYS   B 1 163 ? 36.873  -31.633 1.667  1.00 69.39  ?  188 LYS   B HD2    1 
ATOM   8938  H  HD3    . LYS   B 1 163 ? 37.752  -30.472 1.031  1.00 69.39  ?  188 LYS   B HD3    1 
ATOM   8939  H  HE2    . LYS   B 1 163 ? 38.444  -31.899 -0.660 1.00 72.76  ?  188 LYS   B HE2    1 
ATOM   8940  H  HE3    . LYS   B 1 163 ? 37.615  -33.089 -0.010 1.00 72.76  ?  188 LYS   B HE3    1 
ATOM   8941  H  HZ1    . LYS   B 1 163 ? 36.452  -32.160 -1.731 1.00 74.97  ?  188 LYS   B HZ1    1 
ATOM   8942  H  HZ2    . LYS   B 1 163 ? 35.710  -31.939 -0.507 1.00 74.97  ?  188 LYS   B HZ2    1 
ATOM   8943  H  HZ3    . LYS   B 1 163 ? 36.466  -30.856 -1.102 1.00 74.97  ?  188 LYS   B HZ3    1 
ATOM   8944  N  N      . MET   B 1 164 ? 40.546  -29.209 5.147  1.00 48.66  ?  189 MET   B N      1 
ATOM   8945  C  CA     . MET   B 1 164 ? 40.374  -28.104 6.080  1.00 49.65  ?  189 MET   B CA     1 
ATOM   8946  C  C      . MET   B 1 164 ? 39.473  -27.048 5.452  1.00 49.04  ?  189 MET   B C      1 
ATOM   8947  O  O      . MET   B 1 164 ? 39.589  -26.747 4.259  1.00 49.07  ?  189 MET   B O      1 
ATOM   8948  C  CB     . MET   B 1 164 ? 41.714  -27.460 6.470  1.00 52.22  ?  189 MET   B CB     1 
ATOM   8949  C  CG     . MET   B 1 164 ? 41.581  -26.325 7.499  1.00 55.51  ?  189 MET   B CG     1 
ATOM   8950  S  SD     . MET   B 1 164 ? 41.771  -24.660 6.820  1.00 58.06  ?  189 MET   B SD     1 
ATOM   8951  C  CE     . MET   B 1 164 ? 43.458  -24.724 6.222  1.00 59.28  ?  189 MET   B CE     1 
ATOM   8952  H  H      . MET   B 1 164 ? 40.960  -28.985 4.428  1.00 58.39  ?  189 MET   B H      1 
ATOM   8953  H  HA     . MET   B 1 164 ? 39.968  -28.448 6.891  1.00 59.57  ?  189 MET   B HA     1 
ATOM   8954  H  HB2    . MET   B 1 164 ? 42.287  -28.142 6.854  1.00 62.66  ?  189 MET   B HB2    1 
ATOM   8955  H  HB3    . MET   B 1 164 ? 42.125  -27.091 5.673  1.00 62.66  ?  189 MET   B HB3    1 
ATOM   8956  H  HG2    . MET   B 1 164 ? 40.701  -26.376 7.903  1.00 66.60  ?  189 MET   B HG2    1 
ATOM   8957  H  HG3    . MET   B 1 164 ? 42.265  -26.442 8.177  1.00 66.60  ?  189 MET   B HG3    1 
ATOM   8958  H  HE1    . MET   B 1 164 ? 43.719  -23.841 5.916  1.00 71.13  ?  189 MET   B HE1    1 
ATOM   8959  H  HE2    . MET   B 1 164 ? 44.039  -25.009 6.944  1.00 71.13  ?  189 MET   B HE2    1 
ATOM   8960  H  HE3    . MET   B 1 164 ? 43.508  -25.356 5.487  1.00 71.13  ?  189 MET   B HE3    1 
ATOM   8961  N  N      . PHE   B 1 165 ? 38.603  -26.466 6.275  1.00 46.27  ?  190 PHE   B N      1 
ATOM   8962  C  CA     . PHE   B 1 165 ? 37.607  -25.485 5.862  1.00 45.54  ?  190 PHE   B CA     1 
ATOM   8963  C  C      . PHE   B 1 165 ? 37.938  -24.143 6.500  1.00 46.12  ?  190 PHE   B C      1 
ATOM   8964  O  O      . PHE   B 1 165 ? 38.314  -24.088 7.674  1.00 46.19  ?  190 PHE   B O      1 
ATOM   8965  C  CB     . PHE   B 1 165 ? 36.195  -25.933 6.300  1.00 44.76  ?  190 PHE   B CB     1 
ATOM   8966  C  CG     . PHE   B 1 165 ? 35.122  -24.875 6.138  1.00 44.25  ?  190 PHE   B CG     1 
ATOM   8967  C  CD1    . PHE   B 1 165 ? 35.006  -23.823 7.044  1.00 43.91  ?  190 PHE   B CD1    1 
ATOM   8968  C  CD2    . PHE   B 1 165 ? 34.206  -24.957 5.105  1.00 43.47  ?  190 PHE   B CD2    1 
ATOM   8969  C  CE1    . PHE   B 1 165 ? 34.028  -22.864 6.894  1.00 42.62  ?  190 PHE   B CE1    1 
ATOM   8970  C  CE2    . PHE   B 1 165 ? 33.219  -24.001 4.961  1.00 43.04  ?  190 PHE   B CE2    1 
ATOM   8971  C  CZ     . PHE   B 1 165 ? 33.131  -22.954 5.857  1.00 42.79  ?  190 PHE   B CZ     1 
ATOM   8972  H  H      . PHE   B 1 165 ? 38.570  -26.634 7.117  1.00 55.52  ?  190 PHE   B H      1 
ATOM   8973  H  HA     . PHE   B 1 165 ? 37.613  -25.383 4.898  1.00 54.64  ?  190 PHE   B HA     1 
ATOM   8974  H  HB2    . PHE   B 1 165 ? 35.935  -26.699 5.765  1.00 53.70  ?  190 PHE   B HB2    1 
ATOM   8975  H  HB3    . PHE   B 1 165 ? 36.226  -26.178 7.238  1.00 53.70  ?  190 PHE   B HB3    1 
ATOM   8976  H  HD1    . PHE   B 1 165 ? 35.597  -23.768 7.760  1.00 52.69  ?  190 PHE   B HD1    1 
ATOM   8977  H  HD2    . PHE   B 1 165 ? 34.256  -25.663 4.502  1.00 52.16  ?  190 PHE   B HD2    1 
ATOM   8978  H  HE1    . PHE   B 1 165 ? 33.975  -22.156 7.495  1.00 51.14  ?  190 PHE   B HE1    1 
ATOM   8979  H  HE2    . PHE   B 1 165 ? 32.612  -24.063 4.258  1.00 51.64  ?  190 PHE   B HE2    1 
ATOM   8980  H  HZ     . PHE   B 1 165 ? 32.466  -22.311 5.759  1.00 51.34  ?  190 PHE   B HZ     1 
ATOM   8981  N  N      . LYS   B 1 166 ? 37.781  -23.061 5.738  1.00 45.17  ?  191 LYS   B N      1 
ATOM   8982  C  CA     . LYS   B 1 166 ? 37.888  -21.725 6.310  1.00 46.44  ?  191 LYS   B CA     1 
ATOM   8983  C  C      . LYS   B 1 166 ? 36.967  -20.767 5.570  1.00 45.80  ?  191 LYS   B C      1 
ATOM   8984  O  O      . LYS   B 1 166 ? 36.993  -20.707 4.340  1.00 46.52  ?  191 LYS   B O      1 
ATOM   8985  C  CB     . LYS   B 1 166 ? 39.332  -21.214 6.251  1.00 48.40  ?  191 LYS   B CB     1 
ATOM   8986  C  CG     . LYS   B 1 166 ? 39.472  -19.756 6.648  1.00 50.86  ?  191 LYS   B CG     1 
ATOM   8987  C  CD     . LYS   B 1 166 ? 40.930  -19.347 6.753  1.00 52.31  ?  191 LYS   B CD     1 
ATOM   8988  C  CE     . LYS   B 1 166 ? 41.060  -17.850 6.935  1.00 54.18  ?  191 LYS   B CE     1 
ATOM   8989  N  NZ     . LYS   B 1 166 ? 42.462  -17.468 7.243  1.00 55.15  ?  191 LYS   B NZ     1 
ATOM   8990  H  H      . LYS   B 1 166 ? 37.613  -23.077 4.895  1.00 54.19  ?  191 LYS   B H      1 
ATOM   8991  H  HA     . LYS   B 1 166 ? 37.602  -21.758 7.237  1.00 55.72  ?  191 LYS   B HA     1 
ATOM   8992  H  HB2    . LYS   B 1 166 ? 39.876  -21.741 6.856  1.00 58.07  ?  191 LYS   B HB2    1 
ATOM   8993  H  HB3    . LYS   B 1 166 ? 39.660  -21.307 5.343  1.00 58.07  ?  191 LYS   B HB3    1 
ATOM   8994  H  HG2    . LYS   B 1 166 ? 39.045  -19.198 5.979  1.00 61.02  ?  191 LYS   B HG2    1 
ATOM   8995  H  HG3    . LYS   B 1 166 ? 39.053  -19.616 7.512  1.00 61.02  ?  191 LYS   B HG3    1 
ATOM   8996  H  HD2    . LYS   B 1 166 ? 41.335  -19.785 7.517  1.00 62.77  ?  191 LYS   B HD2    1 
ATOM   8997  H  HD3    . LYS   B 1 166 ? 41.395  -19.599 5.940  1.00 62.77  ?  191 LYS   B HD3    1 
ATOM   8998  H  HE2    . LYS   B 1 166 ? 40.792  -17.401 6.117  1.00 65.01  ?  191 LYS   B HE2    1 
ATOM   8999  H  HE3    . LYS   B 1 166 ? 40.495  -17.564 7.670  1.00 65.01  ?  191 LYS   B HE3    1 
ATOM   9000  H  HZ1    . LYS   B 1 166 ? 42.524  -16.586 7.340  1.00 66.17  ?  191 LYS   B HZ1    1 
ATOM   9001  H  HZ2    . LYS   B 1 166 ? 42.726  -17.861 7.996  1.00 66.17  ?  191 LYS   B HZ2    1 
ATOM   9002  H  HZ3    . LYS   B 1 166 ? 42.999  -17.724 6.581  1.00 66.17  ?  191 LYS   B HZ3    1 
ATOM   9003  N  N      . GLN   B 1 167 ? 36.168  -20.011 6.317  1.00 45.53  ?  192 GLN   B N      1 
ATOM   9004  C  CA     . GLN   B 1 167 ? 35.316  -19.004 5.706  1.00 43.92  ?  192 GLN   B CA     1 
ATOM   9005  C  C      . GLN   B 1 167 ? 35.085  -17.875 6.695  1.00 43.45  ?  192 GLN   B C      1 
ATOM   9006  O  O      . GLN   B 1 167 ? 35.082  -18.088 7.910  1.00 42.44  ?  192 GLN   B O      1 
ATOM   9007  C  CB     . GLN   B 1 167 ? 33.974  -19.589 5.255  1.00 45.65  ?  192 GLN   B CB     1 
ATOM   9008  C  CG     . GLN   B 1 167 ? 33.115  -18.598 4.491  1.00 48.00  ?  192 GLN   B CG     1 
ATOM   9009  C  CD     . GLN   B 1 167 ? 31.998  -19.263 3.707  1.00 50.17  ?  192 GLN   B CD     1 
ATOM   9010  O  OE1    . GLN   B 1 167 ? 31.570  -20.376 4.022  1.00 49.52  ?  192 GLN   B OE1    1 
ATOM   9011  N  NE2    . GLN   B 1 167 ? 31.527  -18.583 2.669  1.00 51.92  ?  192 GLN   B NE2    1 
ATOM   9012  H  H      . GLN   B 1 167 ? 36.104  -20.064 7.173  1.00 54.63  ?  192 GLN   B H      1 
ATOM   9013  H  HA     . GLN   B 1 167 ? 35.765  -18.640 4.927  1.00 52.70  ?  192 GLN   B HA     1 
ATOM   9014  H  HB2    . GLN   B 1 167 ? 34.142  -20.348 4.675  1.00 54.77  ?  192 GLN   B HB2    1 
ATOM   9015  H  HB3    . GLN   B 1 167 ? 33.477  -19.873 6.038  1.00 54.77  ?  192 GLN   B HB3    1 
ATOM   9016  H  HG2    . GLN   B 1 167 ? 32.711  -17.980 5.121  1.00 57.59  ?  192 GLN   B HG2    1 
ATOM   9017  H  HG3    . GLN   B 1 167 ? 33.674  -18.114 3.864  1.00 57.59  ?  192 GLN   B HG3    1 
ATOM   9018  H  HE21   . GLN   B 1 167 ? 31.854  -17.812 2.475  1.00 62.30  ?  192 GLN   B HE21   1 
ATOM   9019  H  HE22   . GLN   B 1 167 ? 30.894  -18.914 2.190  1.00 62.30  ?  192 GLN   B HE22   1 
ATOM   9020  N  N      . THR   B 1 168 ? 34.895  -16.671 6.158  1.00 43.41  ?  193 THR   B N      1 
ATOM   9021  C  CA     . THR   B 1 168 ? 34.700  -15.470 6.955  1.00 42.93  ?  193 THR   B CA     1 
ATOM   9022  C  C      . THR   B 1 168 ? 33.372  -14.806 6.607  1.00 42.92  ?  193 THR   B C      1 
ATOM   9023  O  O      . THR   B 1 168 ? 32.988  -14.724 5.434  1.00 45.52  ?  193 THR   B O      1 
ATOM   9024  C  CB     . THR   B 1 168 ? 35.848  -14.465 6.741  1.00 42.28  ?  193 THR   B CB     1 
ATOM   9025  O  OG1    . THR   B 1 168 ? 37.084  -15.013 7.213  1.00 43.19  ?  193 THR   B OG1    1 
ATOM   9026  C  CG2    . THR   B 1 168 ? 35.570  -13.175 7.491  1.00 40.94  ?  193 THR   B CG2    1 
ATOM   9027  H  H      . THR   B 1 168 ? 34.875  -16.525 5.311  1.00 52.09  ?  193 THR   B H      1 
ATOM   9028  H  HA     . THR   B 1 168 ? 34.674  -15.719 7.892  1.00 51.51  ?  193 THR   B HA     1 
ATOM   9029  H  HB     . THR   B 1 168 ? 35.922  -14.272 5.793  1.00 50.73  ?  193 THR   B HB     1 
ATOM   9030  H  HG1    . THR   B 1 168 ? 37.709  -14.467 7.082  1.00 51.83  ?  193 THR   B HG1    1 
ATOM   9031  H  HG21   . THR   B 1 168 ? 36.382  -12.649 7.559  1.00 49.12  ?  193 THR   B HG21   1 
ATOM   9032  H  HG22   . THR   B 1 168 ? 34.898  -12.656 7.022  1.00 49.12  ?  193 THR   B HG22   1 
ATOM   9033  H  HG23   . THR   B 1 168 ? 35.248  -13.373 8.384  1.00 49.12  ?  193 THR   B HG23   1 
ATOM   9034  N  N      . TRP   B 1 169 ? 32.680  -14.347 7.645  1.00 39.28  ?  194 TRP   B N      1 
ATOM   9035  C  CA     . TRP   B 1 169 ? 31.470  -13.551 7.534  1.00 38.76  ?  194 TRP   B CA     1 
ATOM   9036  C  C      . TRP   B 1 169 ? 31.798  -12.140 8.001  1.00 38.77  ?  194 TRP   B C      1 
ATOM   9037  O  O      . TRP   B 1 169 ? 32.737  -11.938 8.784  1.00 39.04  ?  194 TRP   B O      1 
ATOM   9038  C  CB     . TRP   B 1 169 ? 30.333  -14.123 8.388  1.00 38.48  ?  194 TRP   B CB     1 
ATOM   9039  C  CG     . TRP   B 1 169 ? 29.698  -15.367 7.841  1.00 37.37  ?  194 TRP   B CG     1 
ATOM   9040  C  CD1    . TRP   B 1 169 ? 28.513  -15.457 7.178  1.00 36.39  ?  194 TRP   B CD1    1 
ATOM   9041  C  CD2    . TRP   B 1 169 ? 30.209  -16.700 7.936  1.00 37.19  ?  194 TRP   B CD2    1 
ATOM   9042  N  NE1    . TRP   B 1 169 ? 28.254  -16.764 6.846  1.00 37.42  ?  194 TRP   B NE1    1 
ATOM   9043  C  CE2    . TRP   B 1 169 ? 29.281  -17.548 7.301  1.00 37.71  ?  194 TRP   B CE2    1 
ATOM   9044  C  CE3    . TRP   B 1 169 ? 31.363  -17.257 8.490  1.00 37.02  ?  194 TRP   B CE3    1 
ATOM   9045  C  CZ2    . TRP   B 1 169 ? 29.475  -18.926 7.200  1.00 38.42  ?  194 TRP   B CZ2    1 
ATOM   9046  C  CZ3    . TRP   B 1 169 ? 31.550  -18.621 8.401  1.00 38.41  ?  194 TRP   B CZ3    1 
ATOM   9047  C  CH2    . TRP   B 1 169 ? 30.611  -19.441 7.759  1.00 38.72  ?  194 TRP   B CH2    1 
ATOM   9048  H  H      . TRP   B 1 169 ? 32.905  -14.493 8.462  1.00 47.13  ?  194 TRP   B H      1 
ATOM   9049  H  HA     . TRP   B 1 169 ? 31.156  -13.537 6.616  1.00 46.50  ?  194 TRP   B HA     1 
ATOM   9050  H  HB2    . TRP   B 1 169 ? 30.686  -14.338 9.265  1.00 46.17  ?  194 TRP   B HB2    1 
ATOM   9051  H  HB3    . TRP   B 1 169 ? 29.638  -13.451 8.465  1.00 46.17  ?  194 TRP   B HB3    1 
ATOM   9052  H  HD1    . TRP   B 1 169 ? 27.958  -14.737 6.979  1.00 43.66  ?  194 TRP   B HD1    1 
ATOM   9053  H  HE1    . TRP   B 1 169 ? 27.561  -17.045 6.421  1.00 44.89  ?  194 TRP   B HE1    1 
ATOM   9054  H  HE3    . TRP   B 1 169 ? 31.994  -16.719 8.912  1.00 44.41  ?  194 TRP   B HE3    1 
ATOM   9055  H  HZ2    . TRP   B 1 169 ? 28.857  -19.472 6.770  1.00 46.10  ?  194 TRP   B HZ2    1 
ATOM   9056  H  HZ3    . TRP   B 1 169 ? 32.312  -19.004 8.773  1.00 46.08  ?  194 TRP   B HZ3    1 
ATOM   9057  H  HH2    . TRP   B 1 169 ? 30.765  -20.357 7.713  1.00 46.46  ?  194 TRP   B HH2    1 
ATOM   9058  N  N      . MET   B 1 170 ? 31.027  -11.168 7.519  1.00 38.96  ?  195 MET   B N      1 
ATOM   9059  C  CA     . MET   B 1 170 ? 31.254  -9.776  7.863  1.00 40.20  ?  195 MET   B CA     1 
ATOM   9060  C  C      . MET   B 1 170 ? 29.927  -9.060  8.055  1.00 39.99  ?  195 MET   B C      1 
ATOM   9061  O  O      . MET   B 1 170 ? 28.875  -9.520  7.603  1.00 39.92  ?  195 MET   B O      1 
ATOM   9062  C  CB     . MET   B 1 170 ? 32.049  -9.034  6.779  1.00 42.73  ?  195 MET   B CB     1 
ATOM   9063  C  CG     . MET   B 1 170 ? 33.360  -9.679  6.416  1.00 45.76  ?  195 MET   B CG     1 
ATOM   9064  S  SD     . MET   B 1 170 ? 33.189  -11.058 5.257  1.00 49.53  ?  195 MET   B SD     1 
ATOM   9065  C  CE     . MET   B 1 170 ? 34.856  -11.130 4.594  1.00 49.58  ?  195 MET   B CE     1 
ATOM   9066  H  H      . MET   B 1 170 ? 30.363  -11.295 6.987  1.00 46.75  ?  195 MET   B H      1 
ATOM   9067  H  HA     . MET   B 1 170 ? 31.755  -9.760  8.693  1.00 48.24  ?  195 MET   B HA     1 
ATOM   9068  H  HB2    . MET   B 1 170 ? 31.510  -8.993  5.974  1.00 51.26  ?  195 MET   B HB2    1 
ATOM   9069  H  HB3    . MET   B 1 170 ? 32.242  -8.138  7.096  1.00 51.26  ?  195 MET   B HB3    1 
ATOM   9070  H  HG2    . MET   B 1 170 ? 33.932  -9.014  6.003  1.00 54.90  ?  195 MET   B HG2    1 
ATOM   9071  H  HG3    . MET   B 1 170 ? 33.775  -10.020 7.223  1.00 54.90  ?  195 MET   B HG3    1 
ATOM   9072  H  HE1    . MET   B 1 170 ? 34.933  -11.904 4.015  1.00 59.49  ?  195 MET   B HE1    1 
ATOM   9073  H  HE2    . MET   B 1 170 ? 35.030  -10.320 4.089  1.00 59.49  ?  195 MET   B HE2    1 
ATOM   9074  H  HE3    . MET   B 1 170 ? 35.485  -11.203 5.329  1.00 59.49  ?  195 MET   B HE3    1 
ATOM   9075  N  N      . ASP   B 1 171 ? 30.002  -7.909  8.725  1.00 40.07  ?  196 ASP   B N      1 
ATOM   9076  C  CA     . ASP   B 1 171 ? 28.910  -6.940  8.798  1.00 40.33  ?  196 ASP   B CA     1 
ATOM   9077  C  C      . ASP   B 1 171 ? 27.642  -7.563  9.380  1.00 39.05  ?  196 ASP   B C      1 
ATOM   9078  O  O      . ASP   B 1 171 ? 26.560  -7.531  8.788  1.00 39.64  ?  196 ASP   B O      1 
ATOM   9079  C  CB     . ASP   B 1 171 ? 28.651  -6.332  7.417  1.00 42.32  ?  196 ASP   B CB     1 
ATOM   9080  C  CG     . ASP   B 1 171 ? 29.886  -5.669  6.836  1.00 45.62  ?  196 ASP   B CG     1 
ATOM   9081  O  OD1    . ASP   B 1 171 ? 30.770  -5.244  7.612  1.00 46.44  ?  196 ASP   B OD1    1 
ATOM   9082  O  OD2    . ASP   B 1 171 ? 29.974  -5.579  5.597  1.00 47.43  ?  196 ASP   B OD2    1 
ATOM   9083  H  H      . ASP   B 1 171 ? 30.701  -7.659  9.160  1.00 48.07  ?  196 ASP   B H      1 
ATOM   9084  H  HA     . ASP   B 1 171 ? 29.172  -6.229  9.404  1.00 48.39  ?  196 ASP   B HA     1 
ATOM   9085  H  HB2    . ASP   B 1 171 ? 28.370  -7.033  6.809  1.00 50.78  ?  196 ASP   B HB2    1 
ATOM   9086  H  HB3    . ASP   B 1 171 ? 27.956  -5.659  7.492  1.00 50.78  ?  196 ASP   B HB3    1 
ATOM   9087  N  N      . ASN   B 1 172 ? 27.793  -8.107  10.585 1.00 37.42  ?  197 ASN   B N      1 
ATOM   9088  C  CA     . ASN   B 1 172 ? 26.665  -8.660  11.327 1.00 36.10  ?  197 ASN   B CA     1 
ATOM   9089  C  C      . ASN   B 1 172 ? 26.010  -9.800  10.547 1.00 36.69  ?  197 ASN   B C      1 
ATOM   9090  O  O      . ASN   B 1 172 ? 24.788  -9.868  10.403 1.00 36.90  ?  197 ASN   B O      1 
ATOM   9091  C  CB     . ASN   B 1 172 ? 25.658  -7.555  11.653 1.00 35.79  ?  197 ASN   B CB     1 
ATOM   9092  C  CG     . ASN   B 1 172 ? 26.314  -6.325  12.264 1.00 37.09  ?  197 ASN   B CG     1 
ATOM   9093  O  OD1    . ASN   B 1 172 ? 26.341  -5.258  11.657 1.00 39.19  ?  197 ASN   B OD1    1 
ATOM   9094  N  ND2    . ASN   B 1 172 ? 26.866  -6.482  13.463 1.00 37.31  ?  197 ASN   B ND2    1 
ATOM   9095  H  H      . ASN   B 1 172 ? 28.545  -8.167  10.998 1.00 44.90  ?  197 ASN   B H      1 
ATOM   9096  H  HA     . ASN   B 1 172 ? 26.985  -9.035  12.162 1.00 43.31  ?  197 ASN   B HA     1 
ATOM   9097  H  HB2    . ASN   B 1 172 ? 25.211  -7.283  10.836 1.00 42.94  ?  197 ASN   B HB2    1 
ATOM   9098  H  HB3    . ASN   B 1 172 ? 25.009  -7.896  12.288 1.00 42.94  ?  197 ASN   B HB3    1 
ATOM   9099  H  HD21   . ASN   B 1 172 ? 27.250  -5.817  13.850 1.00 44.77  ?  197 ASN   B HD21   1 
ATOM   9100  H  HD22   . ASN   B 1 172 ? 26.840  -7.249  13.851 1.00 44.77  ?  197 ASN   B HD22   1 
ATOM   9101  N  N      . MET   B 1 173 ? 26.848  -10.708 10.043 1.00 38.22  ?  198 MET   B N      1 
ATOM   9102  C  CA     . MET   B 1 173 ? 26.405  -11.859 9.253  1.00 38.12  ?  198 MET   B CA     1 
ATOM   9103  C  C      . MET   B 1 173 ? 25.612  -11.418 8.024  1.00 40.85  ?  198 MET   B C      1 
ATOM   9104  O  O      . MET   B 1 173 ? 24.735  -12.139 7.539  1.00 42.33  ?  198 MET   B O      1 
ATOM   9105  C  CB     . MET   B 1 173 ? 25.595  -12.851 10.104 1.00 37.10  ?  198 MET   B CB     1 
ATOM   9106  C  CG     . MET   B 1 173 ? 25.717  -14.297 9.605  1.00 35.92  ?  198 MET   B CG     1 
ATOM   9107  S  SD     . MET   B 1 173 ? 25.008  -15.543 10.709 1.00 37.59  ?  198 MET   B SD     1 
ATOM   9108  C  CE     . MET   B 1 173 ? 23.263  -15.249 10.467 1.00 39.06  ?  198 MET   B CE     1 
ATOM   9109  H  H      . MET   B 1 173 ? 27.701  -10.677 10.148 1.00 45.86  ?  198 MET   B H      1 
ATOM   9110  H  HA     . MET   B 1 173 ? 27.193  -12.333 8.944  1.00 45.73  ?  198 MET   B HA     1 
ATOM   9111  H  HB2    . MET   B 1 173 ? 25.919  -12.820 11.018 1.00 44.51  ?  198 MET   B HB2    1 
ATOM   9112  H  HB3    . MET   B 1 173 ? 24.659  -12.600 10.075 1.00 44.51  ?  198 MET   B HB3    1 
ATOM   9113  H  HG2    . MET   B 1 173 ? 25.260  -14.369 8.753  1.00 43.10  ?  198 MET   B HG2    1 
ATOM   9114  H  HG3    . MET   B 1 173 ? 26.658  -14.507 9.495  1.00 43.10  ?  198 MET   B HG3    1 
ATOM   9115  H  HE1    . MET   B 1 173 ? 22.759  -15.869 11.017 1.00 46.87  ?  198 MET   B HE1    1 
ATOM   9116  H  HE2    . MET   B 1 173 ? 23.057  -14.336 10.724 1.00 46.87  ?  198 MET   B HE2    1 
ATOM   9117  H  HE3    . MET   B 1 173 ? 23.046  -15.386 9.531  1.00 46.87  ?  198 MET   B HE3    1 
ATOM   9118  N  N      . GLY   B 1 174 ? 25.944  -10.245 7.486  1.00 40.77  ?  199 GLY   B N      1 
ATOM   9119  C  CA     . GLY   B 1 174 ? 25.277  -9.731  6.307  1.00 42.51  ?  199 GLY   B CA     1 
ATOM   9120  C  C      . GLY   B 1 174 ? 25.903  -10.179 5.003  1.00 44.16  ?  199 GLY   B C      1 
ATOM   9121  O  O      . GLY   B 1 174 ? 25.286  -10.053 3.939  1.00 45.10  ?  199 GLY   B O      1 
ATOM   9122  H  H      . GLY   B 1 174 ? 26.558  -9.727  7.793  1.00 48.91  ?  199 GLY   B H      1 
ATOM   9123  H  HA2    . GLY   B 1 174 ? 24.354  -10.029 6.313  1.00 51.01  ?  199 GLY   B HA2    1 
ATOM   9124  H  HA3    . GLY   B 1 174 ? 25.296  -8.762  6.332  1.00 51.01  ?  199 GLY   B HA3    1 
ATOM   9125  N  N      . ARG   B 1 175 ? 27.128  -10.697 5.061  1.00 46.11  ?  200 ARG   B N      1 
ATOM   9126  C  CA     . ARG   B 1 175 ? 27.800  -11.199 3.867  1.00 46.88  ?  200 ARG   B CA     1 
ATOM   9127  C  C      . ARG   B 1 175 ? 28.913  -12.148 4.291  1.00 46.46  ?  200 ARG   B C      1 
ATOM   9128  O  O      . ARG   B 1 175 ? 29.279  -12.224 5.466  1.00 45.23  ?  200 ARG   B O      1 
ATOM   9129  C  CB     . ARG   B 1 175 ? 28.347  -10.048 3.011  1.00 47.83  ?  200 ARG   B CB     1 
ATOM   9130  C  CG     . ARG   B 1 175 ? 29.403  -9.195  3.697  1.00 49.16  ?  200 ARG   B CG     1 
ATOM   9131  C  CD     . ARG   B 1 175 ? 29.758  -7.936  2.887  1.00 50.94  ?  200 ARG   B CD     1 
ATOM   9132  N  NE     . ARG   B 1 175 ? 30.846  -7.201  3.528  1.00 51.87  ?  200 ARG   B NE     1 
ATOM   9133  C  CZ     . ARG   B 1 175 ? 32.138  -7.419  3.297  1.00 53.68  ?  200 ARG   B CZ     1 
ATOM   9134  N  NH1    . ARG   B 1 175 ? 32.515  -8.343  2.422  1.00 54.27  ?  200 ARG   B NH1    1 
ATOM   9135  N  NH2    . ARG   B 1 175 ? 33.057  -6.713  3.941  1.00 54.44  ?  200 ARG   B NH2    1 
ATOM   9136  H  H      . ARG   B 1 175 ? 27.592  -10.768 5.781  1.00 55.32  ?  200 ARG   B H      1 
ATOM   9137  H  HA     . ARG   B 1 175 ? 27.166  -11.702 3.333  1.00 56.25  ?  200 ARG   B HA     1 
ATOM   9138  H  HB2    . ARG   B 1 175 ? 28.748  -10.423 2.211  1.00 57.39  ?  200 ARG   B HB2    1 
ATOM   9139  H  HB3    . ARG   B 1 175 ? 27.610  -9.465  2.771  1.00 57.39  ?  200 ARG   B HB3    1 
ATOM   9140  H  HG2    . ARG   B 1 175 ? 29.069  -8.912  4.563  1.00 58.99  ?  200 ARG   B HG2    1 
ATOM   9141  H  HG3    . ARG   B 1 175 ? 30.212  -9.719  3.809  1.00 58.99  ?  200 ARG   B HG3    1 
ATOM   9142  H  HD2    . ARG   B 1 175 ? 30.042  -8.193  1.995  1.00 61.12  ?  200 ARG   B HD2    1 
ATOM   9143  H  HD3    . ARG   B 1 175 ? 28.983  -7.355  2.833  1.00 61.12  ?  200 ARG   B HD3    1 
ATOM   9144  H  HE     . ARG   B 1 175 ? 30.637  -6.587  4.092  1.00 62.24  ?  200 ARG   B HE     1 
ATOM   9145  H  HH11   . ARG   B 1 175 ? 31.923  -8.804  2.002  1.00 65.12  ?  200 ARG   B HH11   1 
ATOM   9146  H  HH12   . ARG   B 1 175 ? 33.351  -8.481  2.276  1.00 65.12  ?  200 ARG   B HH12   1 
ATOM   9147  H  HH21   . ARG   B 1 175 ? 32.819  -6.113  4.509  1.00 65.32  ?  200 ARG   B HH21   1 
ATOM   9148  H  HH22   . ARG   B 1 175 ? 33.892  -6.855  3.791  1.00 65.32  ?  200 ARG   B HH22   1 
ATOM   9149  N  N      . ALA   B 1 176 ? 29.445  -12.884 3.319  1.00 47.61  ?  201 ALA   B N      1 
ATOM   9150  C  CA     . ALA   B 1 176 ? 30.540  -13.803 3.586  1.00 48.55  ?  201 ALA   B CA     1 
ATOM   9151  C  C      . ALA   B 1 176 ? 31.555  -13.729 2.458  1.00 50.17  ?  201 ALA   B C      1 
ATOM   9152  O  O      . ALA   B 1 176 ? 31.211  -13.440 1.309  1.00 51.87  ?  201 ALA   B O      1 
ATOM   9153  C  CB     . ALA   B 1 176 ? 30.049  -15.249 3.743  1.00 48.75  ?  201 ALA   B CB     1 
ATOM   9154  H  H      . ALA   B 1 176 ? 29.187  -12.867 2.499  1.00 57.13  ?  201 ALA   B H      1 
ATOM   9155  H  HA     . ALA   B 1 176 ? 30.980  -13.540 4.409  1.00 58.25  ?  201 ALA   B HA     1 
ATOM   9156  H  HB1    . ALA   B 1 176 ? 30.810  -15.823 3.921  1.00 58.49  ?  201 ALA   B HB1    1 
ATOM   9157  H  HB2    . ALA   B 1 176 ? 29.423  -15.291 4.483  1.00 58.49  ?  201 ALA   B HB2    1 
ATOM   9158  H  HB3    . ALA   B 1 176 ? 29.611  -15.524 2.923  1.00 58.49  ?  201 ALA   B HB3    1 
ATOM   9159  N  N      . GLY   B 1 177 ? 32.820  -13.970 2.812  1.00 50.03  ?  202 GLY   B N      1 
ATOM   9160  C  CA     . GLY   B 1 177 ? 33.863  -14.132 1.828  1.00 51.55  ?  202 GLY   B CA     1 
ATOM   9161  C  C      . GLY   B 1 177 ? 33.845  -15.522 1.240  1.00 52.61  ?  202 GLY   B C      1 
ATOM   9162  O  O      . GLY   B 1 177 ? 32.977  -16.343 1.530  1.00 53.56  ?  202 GLY   B O      1 
ATOM   9163  H  H      . GLY   B 1 177 ? 33.091  -14.044 3.624  1.00 60.03  ?  202 GLY   B H      1 
ATOM   9164  H  HA2    . GLY   B 1 177 ? 33.738  -13.490 1.112  1.00 61.86  ?  202 GLY   B HA2    1 
ATOM   9165  H  HA3    . GLY   B 1 177 ? 34.727  -13.981 2.242  1.00 61.86  ?  202 GLY   B HA3    1 
ATOM   9166  N  N      . GLU   B 1 178 ? 34.833  -15.788 0.392  1.00 52.65  ?  203 GLU   B N      1 
ATOM   9167  C  CA     . GLU   B 1 178 ? 34.892  -17.068 -0.297 1.00 53.39  ?  203 GLU   B CA     1 
ATOM   9168  C  C      . GLU   B 1 178 ? 35.321  -18.179 0.653  1.00 53.44  ?  203 GLU   B C      1 
ATOM   9169  O  O      . GLU   B 1 178 ? 36.209  -17.999 1.491  1.00 53.29  ?  203 GLU   B O      1 
ATOM   9170  C  CB     . GLU   B 1 178 ? 35.858  -16.991 -1.478 1.00 54.28  ?  203 GLU   B CB     1 
ATOM   9171  C  CG     . GLU   B 1 178 ? 35.465  -15.959 -2.520 1.00 56.21  ?  203 GLU   B CG     1 
ATOM   9172  C  CD     . GLU   B 1 178 ? 34.012  -16.089 -2.953 1.00 57.57  ?  203 GLU   B CD     1 
ATOM   9173  O  OE1    . GLU   B 1 178 ? 33.575  -17.224 -3.245 1.00 58.06  ?  203 GLU   B OE1    1 
ATOM   9174  O  OE2    . GLU   B 1 178 ? 33.305  -15.058 -2.985 1.00 58.08  ?  203 GLU   B OE2    1 
ATOM   9175  H  H      . GLU   B 1 178 ? 35.474  -15.249 0.200  1.00 63.17  ?  203 GLU   B H      1 
ATOM   9176  H  HA     . GLU   B 1 178 ? 34.009  -17.285 -0.636 1.00 64.06  ?  203 GLU   B HA     1 
ATOM   9177  H  HB2    . GLU   B 1 178 ? 36.739  -16.757 -1.146 1.00 65.13  ?  203 GLU   B HB2    1 
ATOM   9178  H  HB3    . GLU   B 1 178 ? 35.888  -17.857 -1.914 1.00 65.13  ?  203 GLU   B HB3    1 
ATOM   9179  H  HG2    . GLU   B 1 178 ? 35.589  -15.071 -2.148 1.00 67.44  ?  203 GLU   B HG2    1 
ATOM   9180  H  HG3    . GLU   B 1 178 ? 36.024  -16.071 -3.304 1.00 67.44  ?  203 GLU   B HG3    1 
ATOM   9181  N  N      . MET   B 1 179 ? 34.685  -19.339 0.508  1.00 54.25  ?  204 MET   B N      1 
ATOM   9182  C  CA     . MET   B 1 179 ? 35.081  -20.524 1.256  1.00 54.69  ?  204 MET   B CA     1 
ATOM   9183  C  C      . MET   B 1 179 ? 36.421  -21.039 0.741  1.00 52.83  ?  204 MET   B C      1 
ATOM   9184  O  O      . MET   B 1 179 ? 36.666  -21.078 -0.468 1.00 53.05  ?  204 MET   B O      1 
ATOM   9185  C  CB     . MET   B 1 179 ? 34.001  -21.603 1.123  1.00 56.84  ?  204 MET   B CB     1 
ATOM   9186  C  CG     . MET   B 1 179 ? 34.339  -22.929 1.774  1.00 58.68  ?  204 MET   B CG     1 
ATOM   9187  S  SD     . MET   B 1 179 ? 33.146  -24.255 1.438  1.00 61.12  ?  204 MET   B SD     1 
ATOM   9188  C  CE     . MET   B 1 179 ? 31.689  -23.344 0.921  1.00 62.01  ?  204 MET   B CE     1 
ATOM   9189  H  H      . MET   B 1 179 ? 34.018  -19.465 -0.020 1.00 65.09  ?  204 MET   B H      1 
ATOM   9190  H  HA     . MET   B 1 179 ? 35.169  -20.309 2.198  1.00 65.63  ?  204 MET   B HA     1 
ATOM   9191  H  HB2    . MET   B 1 179 ? 33.187  -21.275 1.536  1.00 68.20  ?  204 MET   B HB2    1 
ATOM   9192  H  HB3    . MET   B 1 179 ? 33.851  -21.772 0.180  1.00 68.20  ?  204 MET   B HB3    1 
ATOM   9193  H  HG2    . MET   B 1 179 ? 35.203  -23.223 1.448  1.00 70.41  ?  204 MET   B HG2    1 
ATOM   9194  H  HG3    . MET   B 1 179 ? 34.372  -22.802 2.735  1.00 70.41  ?  204 MET   B HG3    1 
ATOM   9195  H  HE1    . MET   B 1 179 ? 30.967  -23.970 0.759  1.00 74.40  ?  204 MET   B HE1    1 
ATOM   9196  H  HE2    . MET   B 1 179 ? 31.438  -22.725 1.625  1.00 74.40  ?  204 MET   B HE2    1 
ATOM   9197  H  HE3    . MET   B 1 179 ? 31.893  -22.856 0.108  1.00 74.40  ?  204 MET   B HE3    1 
ATOM   9198  N  N      . GLU   B 1 180 ? 37.301  -21.419 1.662  1.00 51.56  ?  205 GLU   B N      1 
ATOM   9199  C  CA     . GLU   B 1 180 ? 38.602  -21.968 1.315  1.00 52.06  ?  205 GLU   B CA     1 
ATOM   9200  C  C      . GLU   B 1 180 ? 38.685  -23.410 1.793  1.00 51.47  ?  205 GLU   B C      1 
ATOM   9201  O  O      . GLU   B 1 180 ? 38.453  -23.690 2.974  1.00 50.81  ?  205 GLU   B O      1 
ATOM   9202  C  CB     . GLU   B 1 180 ? 39.742  -21.143 1.926  1.00 53.93  ?  205 GLU   B CB     1 
ATOM   9203  C  CG     . GLU   B 1 180 ? 39.789  -19.713 1.418  1.00 57.22  ?  205 GLU   B CG     1 
ATOM   9204  C  CD     . GLU   B 1 180 ? 40.727  -18.834 2.218  1.00 59.81  ?  205 GLU   B CD     1 
ATOM   9205  O  OE1    . GLU   B 1 180 ? 41.446  -19.358 3.095  1.00 60.94  ?  205 GLU   B OE1    1 
ATOM   9206  O  OE2    . GLU   B 1 180 ? 40.739  -17.612 1.970  1.00 60.54  ?  205 GLU   B OE2    1 
ATOM   9207  H  H      . GLU   B 1 180 ? 37.161  -21.366 2.509  1.00 61.87  ?  205 GLU   B H      1 
ATOM   9208  H  HA     . GLU   B 1 180 ? 38.705  -21.958 0.350  1.00 62.46  ?  205 GLU   B HA     1 
ATOM   9209  H  HB2    . GLU   B 1 180 ? 39.626  -21.113 2.889  1.00 64.71  ?  205 GLU   B HB2    1 
ATOM   9210  H  HB3    . GLU   B 1 180 ? 40.587  -21.565 1.706  1.00 64.71  ?  205 GLU   B HB3    1 
ATOM   9211  H  HG2    . GLU   B 1 180 ? 40.093  -19.715 0.497  1.00 68.66  ?  205 GLU   B HG2    1 
ATOM   9212  H  HG3    . GLU   B 1 180 ? 38.900  -19.329 1.472  1.00 68.66  ?  205 GLU   B HG3    1 
ATOM   9213  N  N      . LEU   B 1 181 ? 38.994  -24.320 0.870  1.00 50.13  ?  206 LEU   B N      1 
ATOM   9214  C  CA     . LEU   B 1 181 ? 39.201  -25.730 1.176  1.00 51.24  ?  206 LEU   B CA     1 
ATOM   9215  C  C      . LEU   B 1 181 ? 40.630  -26.117 0.813  1.00 52.20  ?  206 LEU   B C      1 
ATOM   9216  O  O      . LEU   B 1 181 ? 41.125  -25.744 -0.252 1.00 52.19  ?  206 LEU   B O      1 
ATOM   9217  C  CB     . LEU   B 1 181 ? 38.216  -26.609 0.408  1.00 51.00  ?  206 LEU   B CB     1 
ATOM   9218  C  CG     . LEU   B 1 181 ? 36.740  -26.347 0.702  1.00 51.01  ?  206 LEU   B CG     1 
ATOM   9219  C  CD1    . LEU   B 1 181 ? 35.855  -27.091 -0.286 1.00 51.62  ?  206 LEU   B CD1    1 
ATOM   9220  C  CD2    . LEU   B 1 181 ? 36.425  -26.748 2.142  1.00 51.07  ?  206 LEU   B CD2    1 
ATOM   9221  H  H      . LEU   B 1 181 ? 39.091  -24.137 0.035  1.00 60.15  ?  206 LEU   B H      1 
ATOM   9222  H  HA     . LEU   B 1 181 ? 39.069  -25.884 2.125  1.00 61.48  ?  206 LEU   B HA     1 
ATOM   9223  H  HB2    . LEU   B 1 181 ? 38.353  -26.463 -0.541 1.00 61.20  ?  206 LEU   B HB2    1 
ATOM   9224  H  HB3    . LEU   B 1 181 ? 38.396  -27.536 0.631  1.00 61.20  ?  206 LEU   B HB3    1 
ATOM   9225  H  HG     . LEU   B 1 181 ? 36.549  -25.401 0.602  1.00 61.21  ?  206 LEU   B HG     1 
ATOM   9226  H  HD11   . LEU   B 1 181 ? 34.926  -26.907 -0.077 1.00 61.93  ?  206 LEU   B HD11   1 
ATOM   9227  H  HD12   . LEU   B 1 181 ? 36.059  -26.787 -1.184 1.00 61.93  ?  206 LEU   B HD12   1 
ATOM   9228  H  HD13   . LEU   B 1 181 ? 36.029  -28.042 -0.212 1.00 61.93  ?  206 LEU   B HD13   1 
ATOM   9229  H  HD21   . LEU   B 1 181 ? 35.468  -26.687 2.285  1.00 61.27  ?  206 LEU   B HD21   1 
ATOM   9230  H  HD22   . LEU   B 1 181 ? 36.724  -27.659 2.289  1.00 61.27  ?  206 LEU   B HD22   1 
ATOM   9231  H  HD23   . LEU   B 1 181 ? 36.889  -26.146 2.746  1.00 61.27  ?  206 LEU   B HD23   1 
ATOM   9232  N  N      . LYS   B 1 182 ? 41.296  -26.854 1.691  1.00 53.16  ?  207 LYS   B N      1 
ATOM   9233  C  CA     . LYS   B 1 182 ? 42.666  -27.289 1.469  1.00 54.44  ?  207 LYS   B CA     1 
ATOM   9234  C  C      . LYS   B 1 182 ? 42.845  -28.701 1.996  1.00 52.94  ?  207 LYS   B C      1 
ATOM   9235  O  O      . LYS   B 1 182 ? 42.220  -29.076 2.990  1.00 52.09  ?  207 LYS   B O      1 
ATOM   9236  C  CB     . LYS   B 1 182 ? 43.671  -26.342 2.156  1.00 57.74  ?  207 LYS   B CB     1 
ATOM   9237  C  CG     . LYS   B 1 182 ? 43.843  -24.995 1.456  1.00 60.50  ?  207 LYS   B CG     1 
ATOM   9238  C  CD     . LYS   B 1 182 ? 44.110  -23.875 2.449  1.00 62.63  ?  207 LYS   B CD     1 
ATOM   9239  C  CE     . LYS   B 1 182 ? 44.425  -22.553 1.750  1.00 63.88  ?  207 LYS   B CE     1 
ATOM   9240  N  NZ     . LYS   B 1 182 ? 43.451  -22.203 0.674  1.00 64.82  ?  207 LYS   B NZ     1 
ATOM   9241  H  H      . LYS   B 1 182 ? 40.967  -27.120 2.440  1.00 63.78  ?  207 LYS   B H      1 
ATOM   9242  H  HA     . LYS   B 1 182 ? 42.855  -27.302 0.518  1.00 65.33  ?  207 LYS   B HA     1 
ATOM   9243  H  HB2    . LYS   B 1 182 ? 43.363  -26.166 3.059  1.00 69.29  ?  207 LYS   B HB2    1 
ATOM   9244  H  HB3    . LYS   B 1 182 ? 44.538  -26.774 2.179  1.00 69.29  ?  207 LYS   B HB3    1 
ATOM   9245  H  HG2    . LYS   B 1 182 ? 44.594  -25.046 0.845  1.00 72.60  ?  207 LYS   B HG2    1 
ATOM   9246  H  HG3    . LYS   B 1 182 ? 43.032  -24.782 0.968  1.00 72.60  ?  207 LYS   B HG3    1 
ATOM   9247  H  HD2    . LYS   B 1 182 ? 43.325  -23.744 3.002  1.00 75.15  ?  207 LYS   B HD2    1 
ATOM   9248  H  HD3    . LYS   B 1 182 ? 44.870  -24.113 3.002  1.00 75.15  ?  207 LYS   B HD3    1 
ATOM   9249  H  HE2    . LYS   B 1 182 ? 44.411  -21.839 2.407  1.00 76.65  ?  207 LYS   B HE2    1 
ATOM   9250  H  HE3    . LYS   B 1 182 ? 45.305  -22.614 1.345  1.00 76.65  ?  207 LYS   B HE3    1 
ATOM   9251  H  HZ1    . LYS   B 1 182 ? 43.470  -22.820 0.033  1.00 77.78  ?  207 LYS   B HZ1    1 
ATOM   9252  H  HZ2    . LYS   B 1 182 ? 42.628  -22.162 1.010  1.00 77.78  ?  207 LYS   B HZ2    1 
ATOM   9253  H  HZ3    . LYS   B 1 182 ? 43.658  -21.413 0.320  1.00 77.78  ?  207 LYS   B HZ3    1 
ATOM   9254  N  N      . PRO   B 1 183 ? 43.675  -29.514 1.337  1.00 52.84  ?  208 PRO   B N      1 
ATOM   9255  C  CA     . PRO   B 1 183 ? 43.892  -30.878 1.836  1.00 54.04  ?  208 PRO   B CA     1 
ATOM   9256  C  C      . PRO   B 1 183 ? 44.492  -30.860 3.234  1.00 54.78  ?  208 PRO   B C      1 
ATOM   9257  O  O      . PRO   B 1 183 ? 45.280  -29.980 3.590  1.00 55.22  ?  208 PRO   B O      1 
ATOM   9258  C  CB     . PRO   B 1 183 ? 44.860  -31.492 0.816  1.00 54.42  ?  208 PRO   B CB     1 
ATOM   9259  C  CG     . PRO   B 1 183 ? 44.714  -30.636 -0.404 1.00 54.53  ?  208 PRO   B CG     1 
ATOM   9260  C  CD     . PRO   B 1 183 ? 44.456  -29.254 0.110  1.00 54.21  ?  208 PRO   B CD     1 
ATOM   9261  H  HA     . PRO   B 1 183 ? 43.063  -31.382 1.838  1.00 64.85  ?  208 PRO   B HA     1 
ATOM   9262  H  HB2    . PRO   B 1 183 ? 45.767  -31.460 1.158  1.00 65.29  ?  208 PRO   B HB2    1 
ATOM   9263  H  HB3    . PRO   B 1 183 ? 44.608  -32.410 0.630  1.00 65.29  ?  208 PRO   B HB3    1 
ATOM   9264  H  HG2    . PRO   B 1 183 ? 45.531  -30.663 -0.926 1.00 65.43  ?  208 PRO   B HG2    1 
ATOM   9265  H  HG3    . PRO   B 1 183 ? 43.968  -30.950 -0.940 1.00 65.43  ?  208 PRO   B HG3    1 
ATOM   9266  H  HD2    . PRO   B 1 183 ? 45.287  -28.798 0.316  1.00 65.04  ?  208 PRO   B HD2    1 
ATOM   9267  H  HD3    . PRO   B 1 183 ? 43.941  -28.735 -0.527 1.00 65.04  ?  208 PRO   B HD3    1 
ATOM   9268  N  N      . PHE   B 1 184 ? 44.112  -31.849 4.032  1.00 53.75  ?  209 PHE   B N      1 
ATOM   9269  C  CA     . PHE   B 1 184 ? 44.525  -31.889 5.425  1.00 53.99  ?  209 PHE   B CA     1 
ATOM   9270  C  C      . PHE   B 1 184 ? 44.786  -33.324 5.843  1.00 56.19  ?  209 PHE   B C      1 
ATOM   9271  O  O      . PHE   B 1 184 ? 44.021  -34.228 5.496  1.00 57.16  ?  209 PHE   B O      1 
ATOM   9272  C  CB     . PHE   B 1 184 ? 43.456  -31.246 6.328  1.00 51.28  ?  209 PHE   B CB     1 
ATOM   9273  C  CG     . PHE   B 1 184 ? 43.818  -31.240 7.779  1.00 49.79  ?  209 PHE   B CG     1 
ATOM   9274  C  CD1    . PHE   B 1 184 ? 44.727  -30.325 8.271  1.00 49.20  ?  209 PHE   B CD1    1 
ATOM   9275  C  CD2    . PHE   B 1 184 ? 43.255  -32.153 8.653  1.00 49.27  ?  209 PHE   B CD2    1 
ATOM   9276  C  CE1    . PHE   B 1 184 ? 45.074  -30.323 9.601  1.00 49.70  ?  209 PHE   B CE1    1 
ATOM   9277  C  CE2    . PHE   B 1 184 ? 43.598  -32.153 9.988  1.00 49.24  ?  209 PHE   B CE2    1 
ATOM   9278  C  CZ     . PHE   B 1 184 ? 44.507  -31.236 10.462 1.00 49.52  ?  209 PHE   B CZ     1 
ATOM   9279  H  H      . PHE   B 1 184 ? 43.616  -32.508 3.789  1.00 64.50  ?  209 PHE   B H      1 
ATOM   9280  H  HA     . PHE   B 1 184 ? 45.357  -31.402 5.539  1.00 64.78  ?  209 PHE   B HA     1 
ATOM   9281  H  HB2    . PHE   B 1 184 ? 43.326  -30.326 6.051  1.00 61.53  ?  209 PHE   B HB2    1 
ATOM   9282  H  HB3    . PHE   B 1 184 ? 42.628  -31.742 6.231  1.00 61.53  ?  209 PHE   B HB3    1 
ATOM   9283  H  HD1    . PHE   B 1 184 ? 45.109  -29.702 7.695  1.00 59.04  ?  209 PHE   B HD1    1 
ATOM   9284  H  HD2    . PHE   B 1 184 ? 42.638  -32.773 8.336  1.00 59.11  ?  209 PHE   B HD2    1 
ATOM   9285  H  HE1    . PHE   B 1 184 ? 45.692  -29.704 9.919  1.00 59.63  ?  209 PHE   B HE1    1 
ATOM   9286  H  HE2    . PHE   B 1 184 ? 43.215  -32.772 10.567 1.00 59.08  ?  209 PHE   B HE2    1 
ATOM   9287  H  HZ     . PHE   B 1 184 ? 44.738  -31.233 11.363 1.00 59.42  ?  209 PHE   B HZ     1 
ATOM   9288  N  N      . ASN   B 1 185 ? 45.859  -33.522 6.609  1.00 57.80  ?  210 ASN   B N      1 
ATOM   9289  C  CA     . ASN   B 1 185 ? 46.185  -34.841 7.130  1.00 60.38  ?  210 ASN   B CA     1 
ATOM   9290  C  C      . ASN   B 1 185 ? 46.776  -34.802 8.536  1.00 60.71  ?  210 ASN   B C      1 
ATOM   9291  O  O      . ASN   B 1 185 ? 47.453  -35.754 8.938  1.00 62.42  ?  210 ASN   B O      1 
ATOM   9292  C  CB     . ASN   B 1 185 ? 47.181  -35.545 6.208  1.00 64.28  ?  210 ASN   B CB     1 
ATOM   9293  C  CG     . ASN   B 1 185 ? 48.525  -34.837 6.168  1.00 69.56  ?  210 ASN   B CG     1 
ATOM   9294  O  OD1    . ASN   B 1 185 ? 49.368  -35.031 7.047  1.00 71.86  ?  210 ASN   B OD1    1 
ATOM   9295  N  ND2    . ASN   B 1 185 ? 48.723  -33.997 5.156  1.00 71.42  ?  210 ASN   B ND2    1 
ATOM   9296  H  H      . ASN   B 1 185 ? 46.413  -32.906 6.840  1.00 69.35  ?  210 ASN   B H      1 
ATOM   9297  H  HA     . ASN   B 1 185 ? 45.362  -35.352 7.172  1.00 72.45  ?  210 ASN   B HA     1 
ATOM   9298  H  HB2    . ASN   B 1 185 ? 47.325  -36.450 6.527  1.00 77.13  ?  210 ASN   B HB2    1 
ATOM   9299  H  HB3    . ASN   B 1 185 ? 46.822  -35.565 5.307  1.00 77.13  ?  210 ASN   B HB3    1 
ATOM   9300  H  HD21   . ASN   B 1 185 ? 49.468  -33.572 5.090  1.00 85.70  ?  210 ASN   B HD21   1 
ATOM   9301  H  HD22   . ASN   B 1 185 ? 48.107  -33.878 4.568  1.00 85.70  ?  210 ASN   B HD22   1 
ATOM   9302  N  N      . GLY   B 1 186 ? 46.542  -33.733 9.296  1.00 58.71  ?  211 GLY   B N      1 
ATOM   9303  C  CA     . GLY   B 1 186 ? 47.196  -33.570 10.582 1.00 57.59  ?  211 GLY   B CA     1 
ATOM   9304  C  C      . GLY   B 1 186 ? 46.271  -33.755 11.769 1.00 56.13  ?  211 GLY   B C      1 
ATOM   9305  O  O      . GLY   B 1 186 ? 45.306  -34.519 11.684 1.00 56.66  ?  211 GLY   B O      1 
ATOM   9306  H  H      . GLY   B 1 186 ? 46.009  -33.092 9.085  1.00 70.45  ?  211 GLY   B H      1 
ATOM   9307  H  HA2    . GLY   B 1 186 ? 47.912  -34.220 10.656 1.00 69.10  ?  211 GLY   B HA2    1 
ATOM   9308  H  HA3    . GLY   B 1 186 ? 47.573  -32.677 10.633 1.00 69.10  ?  211 GLY   B HA3    1 
ATOM   9309  N  N      . GLU   B 1 187 ? 46.563  -33.072 12.880 1.00 55.24  ?  212 GLU   B N      1 
ATOM   9310  C  CA     . GLU   B 1 187 ? 45.727  -33.131 14.073 1.00 54.89  ?  212 GLU   B CA     1 
ATOM   9311  C  C      . GLU   B 1 187 ? 44.504  -32.235 13.921 1.00 51.43  ?  212 GLU   B C      1 
ATOM   9312  O  O      . GLU   B 1 187 ? 44.627  -31.061 13.559 1.00 51.63  ?  212 GLU   B O      1 
ATOM   9313  C  CB     . GLU   B 1 187 ? 46.531  -32.705 15.302 1.00 58.05  ?  212 GLU   B CB     1 
ATOM   9314  C  CG     . GLU   B 1 187 ? 47.678  -33.637 15.641 1.00 61.61  ?  212 GLU   B CG     1 
ATOM   9315  C  CD     . GLU   B 1 187 ? 47.452  -34.367 16.948 1.00 64.48  ?  212 GLU   B CD     1 
ATOM   9316  O  OE1    . GLU   B 1 187 ? 46.978  -33.730 17.915 1.00 65.27  ?  212 GLU   B OE1    1 
ATOM   9317  O  OE2    . GLU   B 1 187 ? 47.736  -35.582 17.001 1.00 65.59  ?  212 GLU   B OE2    1 
ATOM   9318  H  H      . GLU   B 1 187 ? 47.250  -32.562 12.966 1.00 66.28  ?  212 GLU   B H      1 
ATOM   9319  H  HA     . GLU   B 1 187 ? 45.420  -34.043 14.196 1.00 65.86  ?  212 GLU   B HA     1 
ATOM   9320  H  HB2    . GLU   B 1 187 ? 46.904  -31.824 15.140 1.00 69.66  ?  212 GLU   B HB2    1 
ATOM   9321  H  HB3    . GLU   B 1 187 ? 45.936  -32.678 16.068 1.00 69.66  ?  212 GLU   B HB3    1 
ATOM   9322  H  HG2    . GLU   B 1 187 ? 47.770  -34.298 14.937 1.00 73.93  ?  212 GLU   B HG2    1 
ATOM   9323  H  HG3    . GLU   B 1 187 ? 48.495  -33.121 15.720 1.00 73.93  ?  212 GLU   B HG3    1 
ATOM   9324  N  N      . ASP   B 1 188 ? 43.325  -32.787 14.210 1.00 48.59  ?  213 ASP   B N      1 
ATOM   9325  C  CA     . ASP   B 1 188 ? 42.091  -32.027 14.068 1.00 45.91  ?  213 ASP   B CA     1 
ATOM   9326  C  C      . ASP   B 1 188 ? 42.062  -30.842 15.028 1.00 44.39  ?  213 ASP   B C      1 
ATOM   9327  O  O      . ASP   B 1 188 ? 42.648  -30.877 16.116 1.00 44.05  ?  213 ASP   B O      1 
ATOM   9328  C  CB     . ASP   B 1 188 ? 40.868  -32.908 14.333 1.00 45.55  ?  213 ASP   B CB     1 
ATOM   9329  C  CG     . ASP   B 1 188 ? 40.467  -33.727 13.127 1.00 46.06  ?  213 ASP   B CG     1 
ATOM   9330  O  OD1    . ASP   B 1 188 ? 41.329  -33.953 12.249 1.00 45.75  ?  213 ASP   B OD1    1 
ATOM   9331  O  OD2    . ASP   B 1 188 ? 39.289  -34.139 13.059 1.00 46.15  ?  213 ASP   B OD2    1 
ATOM   9332  H  H      . ASP   B 1 188 ? 43.216  -33.593 14.489 1.00 58.30  ?  213 ASP   B H      1 
ATOM   9333  H  HA     . ASP   B 1 188 ? 42.043  -31.695 13.158 1.00 55.09  ?  213 ASP   B HA     1 
ATOM   9334  H  HB2    . ASP   B 1 188 ? 41.070  -33.519 15.058 1.00 54.66  ?  213 ASP   B HB2    1 
ATOM   9335  H  HB3    . ASP   B 1 188 ? 40.118  -32.343 14.575 1.00 54.66  ?  213 ASP   B HB3    1 
ATOM   9336  N  N      . TYR   B 1 189 ? 41.357  -29.789 14.618 1.00 42.86  ?  214 TYR   B N      1 
ATOM   9337  C  CA     . TYR   B 1 189 ? 41.134  -28.623 15.463 1.00 42.83  ?  214 TYR   B CA     1 
ATOM   9338  C  C      . TYR   B 1 189 ? 40.013  -27.781 14.866 1.00 41.40  ?  214 TYR   B C      1 
ATOM   9339  O  O      . TYR   B 1 189 ? 39.682  -27.900 13.684 1.00 41.08  ?  214 TYR   B O      1 
ATOM   9340  C  CB     . TYR   B 1 189 ? 42.409  -27.781 15.594 1.00 43.70  ?  214 TYR   B CB     1 
ATOM   9341  C  CG     . TYR   B 1 189 ? 42.814  -27.143 14.283 1.00 45.41  ?  214 TYR   B CG     1 
ATOM   9342  C  CD1    . TYR   B 1 189 ? 43.598  -27.829 13.366 1.00 46.75  ?  214 TYR   B CD1    1 
ATOM   9343  C  CD2    . TYR   B 1 189 ? 42.395  -25.860 13.956 1.00 46.30  ?  214 TYR   B CD2    1 
ATOM   9344  C  CE1    . TYR   B 1 189 ? 43.958  -27.257 12.168 1.00 47.81  ?  214 TYR   B CE1    1 
ATOM   9345  C  CE2    . TYR   B 1 189 ? 42.753  -25.279 12.757 1.00 46.82  ?  214 TYR   B CE2    1 
ATOM   9346  C  CZ     . TYR   B 1 189 ? 43.535  -25.981 11.868 1.00 48.15  ?  214 TYR   B CZ     1 
ATOM   9347  O  OH     . TYR   B 1 189 ? 43.895  -25.413 10.667 1.00 49.43  ?  214 TYR   B OH     1 
ATOM   9348  H  H      . TYR   B 1 189 ? 40.992  -29.727 13.842 1.00 51.42  ?  214 TYR   B H      1 
ATOM   9349  H  HA     . TYR   B 1 189 ? 40.855  -28.918 16.344 1.00 51.39  ?  214 TYR   B HA     1 
ATOM   9350  H  HB2    . TYR   B 1 189 ? 42.258  -27.074 16.241 1.00 52.44  ?  214 TYR   B HB2    1 
ATOM   9351  H  HB3    . TYR   B 1 189 ? 43.137  -28.351 15.890 1.00 52.44  ?  214 TYR   B HB3    1 
ATOM   9352  H  HD1    . TYR   B 1 189 ? 43.885  -28.690 13.566 1.00 56.09  ?  214 TYR   B HD1    1 
ATOM   9353  H  HD2    . TYR   B 1 189 ? 41.864  -25.386 14.555 1.00 55.55  ?  214 TYR   B HD2    1 
ATOM   9354  H  HE1    . TYR   B 1 189 ? 44.484  -27.730 11.564 1.00 57.36  ?  214 TYR   B HE1    1 
ATOM   9355  H  HE2    . TYR   B 1 189 ? 42.467  -24.418 12.551 1.00 56.18  ?  214 TYR   B HE2    1 
ATOM   9356  H  HH     . TYR   B 1 189 ? 43.564  -24.643 10.603 1.00 59.31  ?  214 TYR   B HH     1 
ATOM   9357  N  N      . THR   B 1 190 ? 39.435  -26.925 15.696 1.00 39.11  ?  215 THR   B N      1 
ATOM   9358  C  CA     . THR   B 1 190 ? 38.506  -25.902 15.234 1.00 38.61  ?  215 THR   B CA     1 
ATOM   9359  C  C      . THR   B 1 190 ? 38.942  -24.589 15.867 1.00 37.06  ?  215 THR   B C      1 
ATOM   9360  O  O      . THR   B 1 190 ? 39.354  -24.568 17.033 1.00 35.65  ?  215 THR   B O      1 
ATOM   9361  C  CB     . THR   B 1 190 ? 37.049  -26.223 15.601 1.00 38.43  ?  215 THR   B CB     1 
ATOM   9362  O  OG1    . THR   B 1 190 ? 36.578  -27.352 14.845 1.00 37.45  ?  215 THR   B OG1    1 
ATOM   9363  C  CG2    . THR   B 1 190 ? 36.146  -25.033 15.303 1.00 39.04  ?  215 THR   B CG2    1 
ATOM   9364  H  H      . THR   B 1 190 ? 39.567  -26.916 16.545 1.00 46.92  ?  215 THR   B H      1 
ATOM   9365  H  HA     . THR   B 1 190 ? 38.530  -25.828 14.267 1.00 46.32  ?  215 THR   B HA     1 
ATOM   9366  H  HB     . THR   B 1 190 ? 37.007  -26.426 16.548 1.00 46.11  ?  215 THR   B HB     1 
ATOM   9367  H  HG1    . THR   B 1 190 ? 37.073  -28.016 14.983 1.00 44.93  ?  215 THR   B HG1    1 
ATOM   9368  H  HG21   . THR   B 1 190 ? 35.219  -25.317 15.281 1.00 46.84  ?  215 THR   B HG21   1 
ATOM   9369  H  HG22   . THR   B 1 190 ? 36.252  -24.356 15.990 1.00 46.84  ?  215 THR   B HG22   1 
ATOM   9370  H  HG23   . THR   B 1 190 ? 36.378  -24.647 14.444 1.00 46.84  ?  215 THR   B HG23   1 
ATOM   9371  N  N      . CYS   B 1 191 ? 38.877  -23.501 15.101 1.00 38.46  ?  216 CYS   B N      1 
ATOM   9372  C  CA     . CYS   B 1 191 ? 39.260  -22.188 15.610 1.00 39.91  ?  216 CYS   B CA     1 
ATOM   9373  C  C      . CYS   B 1 191 ? 38.269  -21.142 15.128 1.00 38.02  ?  216 CYS   B C      1 
ATOM   9374  O  O      . CYS   B 1 191 ? 38.066  -20.988 13.919 1.00 38.61  ?  216 CYS   B O      1 
ATOM   9375  C  CB     . CYS   B 1 191 ? 40.678  -21.802 15.174 1.00 42.71  ?  216 CYS   B CB     1 
ATOM   9376  S  SG     . CYS   B 1 191 ? 41.263  -20.280 15.958 1.00 46.13  ?  216 CYS   B SG     1 
ATOM   9377  H  H      . CYS   B 1 191 ? 38.614  -23.499 14.282 1.00 46.15  ?  216 CYS   B H      1 
ATOM   9378  H  HA     . CYS   B 1 191 ? 39.226  -22.218 16.579 1.00 47.88  ?  216 CYS   B HA     1 
ATOM   9379  H  HB2    . CYS   B 1 191 ? 41.288  -22.517 15.414 1.00 51.25  ?  216 CYS   B HB2    1 
ATOM   9380  H  HB3    . CYS   B 1 191 ? 40.687  -21.667 14.213 1.00 51.25  ?  216 CYS   B HB3    1 
ATOM   9381  H  HG     . CYS   B 1 191 ? 42.366  -20.032 15.555 1.00 55.35  ?  216 CYS   B HG     1 
ATOM   9382  N  N      . ILE   B 1 192 ? 37.656  -20.437 16.077 1.00 35.13  ?  217 ILE   B N      1 
ATOM   9383  C  CA     . ILE   B 1 192 ? 36.723  -19.350 15.804 1.00 34.57  ?  217 ILE   B CA     1 
ATOM   9384  C  C      . ILE   B 1 192 ? 37.408  -18.046 16.191 1.00 34.39  ?  217 ILE   B C      1 
ATOM   9385  O  O      . ILE   B 1 192 ? 37.848  -17.896 17.338 1.00 34.44  ?  217 ILE   B O      1 
ATOM   9386  C  CB     . ILE   B 1 192 ? 35.409  -19.518 16.587 1.00 35.04  ?  217 ILE   B CB     1 
ATOM   9387  C  CG1    . ILE   B 1 192 ? 34.869  -20.946 16.467 1.00 35.79  ?  217 ILE   B CG1    1 
ATOM   9388  C  CG2    . ILE   B 1 192 ? 34.397  -18.462 16.143 1.00 36.46  ?  217 ILE   B CG2    1 
ATOM   9389  C  CD1    . ILE   B 1 192 ? 34.668  -21.448 15.062 1.00 36.34  ?  217 ILE   B CD1    1 
ATOM   9390  H  H      . ILE   B 1 192 ? 37.769  -20.577 16.917 1.00 42.14  ?  217 ILE   B H      1 
ATOM   9391  H  HA     . ILE   B 1 192 ? 36.520  -19.332 14.855 1.00 41.47  ?  217 ILE   B HA     1 
ATOM   9392  H  HB     . ILE   B 1 192 ? 35.584  -19.376 17.531 1.00 42.05  ?  217 ILE   B HB     1 
ATOM   9393  H  HG12   . ILE   B 1 192 ? 35.496  -21.546 16.900 1.00 42.94  ?  217 ILE   B HG12   1 
ATOM   9394  H  HG13   . ILE   B 1 192 ? 34.009  -20.985 16.913 1.00 42.94  ?  217 ILE   B HG13   1 
ATOM   9395  H  HG21   . ILE   B 1 192 ? 33.544  -18.644 16.568 1.00 43.74  ?  217 ILE   B HG21   1 
ATOM   9396  H  HG22   . ILE   B 1 192 ? 34.718  -17.586 16.408 1.00 43.74  ?  217 ILE   B HG22   1 
ATOM   9397  H  HG23   . ILE   B 1 192 ? 34.301  -18.502 15.179 1.00 43.74  ?  217 ILE   B HG23   1 
ATOM   9398  H  HD11   . ILE   B 1 192 ? 34.231  -22.313 15.096 1.00 43.61  ?  217 ILE   B HD11   1 
ATOM   9399  H  HD12   . ILE   B 1 192 ? 34.113  -20.816 14.578 1.00 43.61  ?  217 ILE   B HD12   1 
ATOM   9400  H  HD13   . ILE   B 1 192 ? 35.532  -21.530 14.629 1.00 43.61  ?  217 ILE   B HD13   1 
ATOM   9401  N  N      . THR   B 1 193 ? 37.494  -17.104 15.246 1.00 35.22  ?  218 THR   B N      1 
ATOM   9402  C  CA     . THR   B 1 193 ? 38.140  -15.810 15.460 1.00 36.15  ?  218 THR   B CA     1 
ATOM   9403  C  C      . THR   B 1 193 ? 37.135  -14.725 15.095 1.00 36.44  ?  218 THR   B C      1 
ATOM   9404  O  O      . THR   B 1 193 ? 36.614  -14.726 13.975 1.00 37.35  ?  218 THR   B O      1 
ATOM   9405  C  CB     . THR   B 1 193 ? 39.403  -15.634 14.593 1.00 37.53  ?  218 THR   B CB     1 
ATOM   9406  O  OG1    . THR   B 1 193 ? 40.329  -16.702 14.820 1.00 37.78  ?  218 THR   B OG1    1 
ATOM   9407  C  CG2    . THR   B 1 193 ? 40.080  -14.293 14.900 1.00 38.63  ?  218 THR   B CG2    1 
ATOM   9408  H  H      . THR   B 1 193 ? 37.176  -17.197 14.452 1.00 42.26  ?  218 THR   B H      1 
ATOM   9409  H  HA     . THR   B 1 193 ? 38.402  -15.734 16.391 1.00 43.37  ?  218 THR   B HA     1 
ATOM   9410  H  HB     . THR   B 1 193 ? 39.145  -15.646 13.658 1.00 45.03  ?  218 THR   B HB     1 
ATOM   9411  H  HG1    . THR   B 1 193 ? 39.960  -17.440 14.664 1.00 45.33  ?  218 THR   B HG1    1 
ATOM   9412  H  HG21   . THR   B 1 193 ? 40.961  -14.265 14.494 1.00 46.36  ?  218 THR   B HG21   1 
ATOM   9413  H  HG22   . THR   B 1 193 ? 39.548  -13.563 14.547 1.00 46.36  ?  218 THR   B HG22   1 
ATOM   9414  H  HG23   . THR   B 1 193 ? 40.173  -14.180 15.859 1.00 46.36  ?  218 THR   B HG23   1 
ATOM   9415  N  N      . PHE   B 1 194 ? 36.863  -13.795 16.012 1.00 36.21  ?  219 PHE   B N      1 
ATOM   9416  C  CA     . PHE   B 1 194 ? 35.852  -12.785 15.735 1.00 36.35  ?  219 PHE   B CA     1 
ATOM   9417  C  C      . PHE   B 1 194 ? 36.251  -11.427 16.290 1.00 36.55  ?  219 PHE   B C      1 
ATOM   9418  O  O      . PHE   B 1 194 ? 37.016  -11.314 17.251 1.00 35.88  ?  219 PHE   B O      1 
ATOM   9419  C  CB     . PHE   B 1 194 ? 34.444  -13.194 16.269 1.00 35.99  ?  219 PHE   B CB     1 
ATOM   9420  C  CG     . PHE   B 1 194 ? 34.350  -13.357 17.769 1.00 36.17  ?  219 PHE   B CG     1 
ATOM   9421  C  CD1    . PHE   B 1 194 ? 34.777  -14.523 18.388 1.00 37.50  ?  219 PHE   B CD1    1 
ATOM   9422  C  CD2    . PHE   B 1 194 ? 33.782  -12.364 18.553 1.00 36.15  ?  219 PHE   B CD2    1 
ATOM   9423  C  CE1    . PHE   B 1 194 ? 34.666  -14.678 19.768 1.00 36.97  ?  219 PHE   B CE1    1 
ATOM   9424  C  CE2    . PHE   B 1 194 ? 33.677  -12.514 19.928 1.00 36.75  ?  219 PHE   B CE2    1 
ATOM   9425  C  CZ     . PHE   B 1 194 ? 34.112  -13.672 20.532 1.00 36.20  ?  219 PHE   B CZ     1 
ATOM   9426  H  H      . PHE   B 1 194 ? 37.243  -13.733 16.782 1.00 43.45  ?  219 PHE   B H      1 
ATOM   9427  H  HA     . PHE   B 1 194 ? 35.795  -12.684 14.772 1.00 43.62  ?  219 PHE   B HA     1 
ATOM   9428  H  HB2    . PHE   B 1 194 ? 33.808  -12.509 16.011 1.00 43.18  ?  219 PHE   B HB2    1 
ATOM   9429  H  HB3    . PHE   B 1 194 ? 34.199  -14.042 15.869 1.00 43.18  ?  219 PHE   B HB3    1 
ATOM   9430  H  HD1    . PHE   B 1 194 ? 35.140  -15.209 17.876 1.00 44.99  ?  219 PHE   B HD1    1 
ATOM   9431  H  HD2    . PHE   B 1 194 ? 33.467  -11.587 18.151 1.00 43.38  ?  219 PHE   B HD2    1 
ATOM   9432  H  HE1    . PHE   B 1 194 ? 34.966  -15.459 20.174 1.00 44.36  ?  219 PHE   B HE1    1 
ATOM   9433  H  HE2    . PHE   B 1 194 ? 33.312  -11.830 20.442 1.00 44.09  ?  219 PHE   B HE2    1 
ATOM   9434  H  HZ     . PHE   B 1 194 ? 34.031  -13.776 21.453 1.00 43.43  ?  219 PHE   B HZ     1 
ATOM   9435  N  N      . GLN   B 1 195 ? 35.742  -10.393 15.626 1.00 36.19  ?  220 GLN   B N      1 
ATOM   9436  C  CA     . GLN   B 1 195 ? 35.868  -9.007  16.055 1.00 36.98  ?  220 GLN   B CA     1 
ATOM   9437  C  C      . GLN   B 1 195 ? 34.496  -8.525  16.499 1.00 35.52  ?  220 GLN   B C      1 
ATOM   9438  O  O      . GLN   B 1 195 ? 33.630  -8.263  15.648 1.00 35.47  ?  220 GLN   B O      1 
ATOM   9439  C  CB     . GLN   B 1 195 ? 36.395  -8.147  14.909 1.00 39.84  ?  220 GLN   B CB     1 
ATOM   9440  C  CG     . GLN   B 1 195 ? 37.785  -8.489  14.487 1.00 43.55  ?  220 GLN   B CG     1 
ATOM   9441  C  CD     . GLN   B 1 195 ? 38.370  -7.404  13.613 1.00 47.10  ?  220 GLN   B CD     1 
ATOM   9442  O  OE1    . GLN   B 1 195 ? 38.027  -7.284  12.438 1.00 50.90  ?  220 GLN   B OE1    1 
ATOM   9443  N  NE2    . GLN   B 1 195 ? 39.226  -6.580  14.198 1.00 46.69  ?  220 GLN   B NE2    1 
ATOM   9444  H  H      . GLN   B 1 195 ? 35.300  -10.474 14.892 1.00 43.42  ?  220 GLN   B H      1 
ATOM   9445  H  HA     . GLN   B 1 195 ? 36.487  -8.936  16.798 1.00 44.37  ?  220 GLN   B HA     1 
ATOM   9446  H  HB2    . GLN   B 1 195 ? 35.815  -8.265  14.140 1.00 47.81  ?  220 GLN   B HB2    1 
ATOM   9447  H  HB3    . GLN   B 1 195 ? 36.391  -7.219  15.189 1.00 47.81  ?  220 GLN   B HB3    1 
ATOM   9448  H  HG2    . GLN   B 1 195 ? 38.346  -8.586  15.272 1.00 52.25  ?  220 GLN   B HG2    1 
ATOM   9449  H  HG3    . GLN   B 1 195 ? 37.775  -9.317  13.982 1.00 52.25  ?  220 GLN   B HG3    1 
ATOM   9450  H  HE21   . GLN   B 1 195 ? 39.420  -6.681  15.029 1.00 56.03  ?  220 GLN   B HE21   1 
ATOM   9451  H  HE22   . GLN   B 1 195 ? 39.589  -5.945  13.746 1.00 56.03  ?  220 GLN   B HE22   1 
ATOM   9452  N  N      . PRO   B 1 196 ? 34.233  -8.420  17.807 1.00 34.04  ?  221 PRO   B N      1 
ATOM   9453  C  CA     . PRO   B 1 196 ? 32.906  -7.973  18.253 1.00 34.18  ?  221 PRO   B CA     1 
ATOM   9454  C  C      . PRO   B 1 196 ? 32.551  -6.607  17.685 1.00 34.43  ?  221 PRO   B C      1 
ATOM   9455  O  O      . PRO   B 1 196 ? 33.404  -5.729  17.558 1.00 34.48  ?  221 PRO   B O      1 
ATOM   9456  C  CB     . PRO   B 1 196 ? 33.027  -7.895  19.783 1.00 36.33  ?  221 PRO   B CB     1 
ATOM   9457  C  CG     . PRO   B 1 196 ? 34.324  -8.434  20.155 1.00 37.22  ?  221 PRO   B CG     1 
ATOM   9458  C  CD     . PRO   B 1 196 ? 35.166  -8.646  18.926 1.00 34.76  ?  221 PRO   B CD     1 
ATOM   9459  H  HA     . PRO   B 1 196 ? 32.240  -8.631  18.001 1.00 41.01  ?  221 PRO   B HA     1 
ATOM   9460  H  HB2    . PRO   B 1 196 ? 32.955  -6.968  20.061 1.00 43.58  ?  221 PRO   B HB2    1 
ATOM   9461  H  HB3    . PRO   B 1 196 ? 32.316  -8.418  20.186 1.00 43.58  ?  221 PRO   B HB3    1 
ATOM   9462  H  HG2    . PRO   B 1 196 ? 34.762  -7.805  20.749 1.00 44.66  ?  221 PRO   B HG2    1 
ATOM   9463  H  HG3    . PRO   B 1 196 ? 34.189  -9.280  20.609 1.00 44.66  ?  221 PRO   B HG3    1 
ATOM   9464  H  HD2    . PRO   B 1 196 ? 35.896  -8.007  18.897 1.00 41.71  ?  221 PRO   B HD2    1 
ATOM   9465  H  HD3    . PRO   B 1 196 ? 35.516  -9.550  18.902 1.00 41.71  ?  221 PRO   B HD3    1 
ATOM   9466  N  N      . ASP   B 1 197 ? 31.270  -6.415  17.385 1.00 33.69  ?  222 ASP   B N      1 
ATOM   9467  C  CA     . ASP   B 1 197 ? 30.793  -5.135  16.860 1.00 34.40  ?  222 ASP   B CA     1 
ATOM   9468  C  C      . ASP   B 1 197 ? 30.576  -4.204  18.046 1.00 33.95  ?  222 ASP   B C      1 
ATOM   9469  O  O      . ASP   B 1 197 ? 29.475  -4.084  18.585 1.00 33.68  ?  222 ASP   B O      1 
ATOM   9470  C  CB     . ASP   B 1 197 ? 29.523  -5.317  16.047 1.00 35.64  ?  222 ASP   B CB     1 
ATOM   9471  C  CG     . ASP   B 1 197 ? 29.112  -4.053  15.316 1.00 36.87  ?  222 ASP   B CG     1 
ATOM   9472  O  OD1    . ASP   B 1 197 ? 29.646  -2.960  15.625 1.00 37.17  ?  222 ASP   B OD1    1 
ATOM   9473  O  OD2    . ASP   B 1 197 ? 28.254  -4.165  14.416 1.00 37.79  ?  222 ASP   B OD2    1 
ATOM   9474  H  H      . ASP   B 1 197 ? 30.656  -7.010  17.476 1.00 40.43  ?  222 ASP   B H      1 
ATOM   9475  H  HA     . ASP   B 1 197 ? 31.466  -4.750  16.276 1.00 41.28  ?  222 ASP   B HA     1 
ATOM   9476  H  HB2    . ASP   B 1 197 ? 29.667  -6.013  15.387 1.00 42.77  ?  222 ASP   B HB2    1 
ATOM   9477  H  HB3    . ASP   B 1 197 ? 28.799  -5.568  16.642 1.00 42.77  ?  222 ASP   B HB3    1 
ATOM   9478  N  N      . LEU   B 1 198 ? 31.652  -3.529  18.454 1.00 33.73  ?  223 LEU   B N      1 
ATOM   9479  C  CA     . LEU   B 1 198 ? 31.592  -2.706  19.654 1.00 35.44  ?  223 LEU   B CA     1 
ATOM   9480  C  C      . LEU   B 1 198 ? 30.608  -1.553  19.504 1.00 36.67  ?  223 LEU   B C      1 
ATOM   9481  O  O      . LEU   B 1 198 ? 30.097  -1.067  20.517 1.00 37.99  ?  223 LEU   B O      1 
ATOM   9482  C  CB     . LEU   B 1 198 ? 32.993  -2.202  20.010 1.00 37.22  ?  223 LEU   B CB     1 
ATOM   9483  C  CG     . LEU   B 1 198 ? 33.955  -3.306  20.476 1.00 39.23  ?  223 LEU   B CG     1 
ATOM   9484  C  CD1    . LEU   B 1 198 ? 35.278  -2.694  20.962 1.00 41.08  ?  223 LEU   B CD1    1 
ATOM   9485  C  CD2    . LEU   B 1 198 ? 33.365  -4.220  21.560 1.00 40.47  ?  223 LEU   B CD2    1 
ATOM   9486  H  H      . LEU   B 1 198 ? 32.415  -3.533  18.058 1.00 40.47  ?  223 LEU   B H      1 
ATOM   9487  H  HA     . LEU   B 1 198 ? 31.286  -3.244  20.401 1.00 42.52  ?  223 LEU   B HA     1 
ATOM   9488  H  HB2    . LEU   B 1 198 ? 33.381  -1.784  19.226 1.00 44.66  ?  223 LEU   B HB2    1 
ATOM   9489  H  HB3    . LEU   B 1 198 ? 32.916  -1.555  20.728 1.00 44.66  ?  223 LEU   B HB3    1 
ATOM   9490  H  HG     . LEU   B 1 198 ? 34.123  -3.873  19.708 1.00 47.06  ?  223 LEU   B HG     1 
ATOM   9491  H  HD11   . LEU   B 1 198 ? 35.872  -3.408  21.240 1.00 49.29  ?  223 LEU   B HD11   1 
ATOM   9492  H  HD12   . LEU   B 1 198 ? 35.680  -2.193  20.235 1.00 49.29  ?  223 LEU   B HD12   1 
ATOM   9493  H  HD13   . LEU   B 1 198 ? 35.097  -2.104  21.710 1.00 49.29  ?  223 LEU   B HD13   1 
ATOM   9494  H  HD21   . LEU   B 1 198 ? 34.082  -4.734  21.964 1.00 48.56  ?  223 LEU   B HD21   1 
ATOM   9495  H  HD22   . LEU   B 1 198 ? 32.931  -3.673  22.233 1.00 48.56  ?  223 LEU   B HD22   1 
ATOM   9496  H  HD23   . LEU   B 1 198 ? 32.719  -4.818  21.151 1.00 48.56  ?  223 LEU   B HD23   1 
ATOM   9497  N  N      . SER   B 1 199 ? 30.282  -1.134  18.276 1.00 38.54  ?  224 SER   B N      1 
ATOM   9498  C  CA     . SER   B 1 199 ? 29.291  -0.071  18.128 1.00 41.57  ?  224 SER   B CA     1 
ATOM   9499  C  C      . SER   B 1 199 ? 27.900  -0.529  18.564 1.00 41.41  ?  224 SER   B C      1 
ATOM   9500  O  O      . SER   B 1 199 ? 27.132  0.280   19.103 1.00 41.25  ?  224 SER   B O      1 
ATOM   9501  C  CB     . SER   B 1 199 ? 29.244  0.427   16.682 1.00 45.08  ?  224 SER   B CB     1 
ATOM   9502  O  OG     . SER   B 1 199 ? 28.736  -0.578  15.824 1.00 47.87  ?  224 SER   B OG     1 
ATOM   9503  H  H      . SER   B 1 199 ? 30.609  -1.439  17.541 1.00 46.25  ?  224 SER   B H      1 
ATOM   9504  H  HA     . SER   B 1 199 ? 29.561  0.671   18.691 1.00 49.87  ?  224 SER   B HA     1 
ATOM   9505  H  HB2    . SER   B 1 199 ? 28.667  1.206   16.634 1.00 54.09  ?  224 SER   B HB2    1 
ATOM   9506  H  HB3    . SER   B 1 199 ? 30.141  0.662   16.398 1.00 54.09  ?  224 SER   B HB3    1 
ATOM   9507  H  HG     . SER   B 1 199 ? 29.232  -1.256  15.852 1.00 57.44  ?  224 SER   B HG     1 
ATOM   9508  N  N      . LYS   B 1 200 ? 27.564  -1.808  18.342 1.00 40.25  ?  225 LYS   B N      1 
ATOM   9509  C  CA     . LYS   B 1 200 ? 26.296  -2.359  18.800 1.00 39.72  ?  225 LYS   B CA     1 
ATOM   9510  C  C      . LYS   B 1 200 ? 26.214  -2.416  20.318 1.00 36.52  ?  225 LYS   B C      1 
ATOM   9511  O  O      . LYS   B 1 200 ? 25.123  -2.607  20.869 1.00 37.28  ?  225 LYS   B O      1 
ATOM   9512  C  CB     . LYS   B 1 200 ? 26.091  -3.782  18.273 1.00 43.34  ?  225 LYS   B CB     1 
ATOM   9513  C  CG     . LYS   B 1 200 ? 26.118  -3.928  16.771 1.00 46.07  ?  225 LYS   B CG     1 
ATOM   9514  C  CD     . LYS   B 1 200 ? 24.733  -3.744  16.162 1.00 47.41  ?  225 LYS   B CD     1 
ATOM   9515  C  CE     . LYS   B 1 200 ? 24.801  -3.737  14.640 1.00 47.90  ?  225 LYS   B CE     1 
ATOM   9516  N  NZ     . LYS   B 1 200 ? 25.842  -2.793  14.125 1.00 48.78  ?  225 LYS   B NZ     1 
ATOM   9517  H  H      . LYS   B 1 200 ? 28.059  -2.375  17.926 1.00 48.30  ?  225 LYS   B H      1 
ATOM   9518  H  HA     . LYS   B 1 200 ? 25.591  -1.793  18.451 1.00 47.66  ?  225 LYS   B HA     1 
ATOM   9519  H  HB2    . LYS   B 1 200 ? 26.796  -4.345  18.630 1.00 52.00  ?  225 LYS   B HB2    1 
ATOM   9520  H  HB3    . LYS   B 1 200 ? 25.227  -4.100  18.578 1.00 52.00  ?  225 LYS   B HB3    1 
ATOM   9521  H  HG2    . LYS   B 1 200 ? 26.708  -3.256  16.394 1.00 55.28  ?  225 LYS   B HG2    1 
ATOM   9522  H  HG3    . LYS   B 1 200 ? 26.436  -4.815  16.541 1.00 55.28  ?  225 LYS   B HG3    1 
ATOM   9523  H  HD2    . LYS   B 1 200 ? 24.158  -4.474  16.440 1.00 56.89  ?  225 LYS   B HD2    1 
ATOM   9524  H  HD3    . LYS   B 1 200 ? 24.361  -2.898  16.457 1.00 56.89  ?  225 LYS   B HD3    1 
ATOM   9525  H  HE2    . LYS   B 1 200 ? 25.020  -4.628  14.327 1.00 57.47  ?  225 LYS   B HE2    1 
ATOM   9526  H  HE3    . LYS   B 1 200 ? 23.941  -3.462  14.284 1.00 57.47  ?  225 LYS   B HE3    1 
ATOM   9527  H  HZ1    . LYS   B 1 200 ? 26.655  -3.108  14.304 1.00 58.53  ?  225 LYS   B HZ1    1 
ATOM   9528  H  HZ2    . LYS   B 1 200 ? 25.757  -2.697  13.244 1.00 58.53  ?  225 LYS   B HZ2    1 
ATOM   9529  H  HZ3    . LYS   B 1 200 ? 25.749  -1.996  14.511 1.00 58.53  ?  225 LYS   B HZ3    1 
ATOM   9530  N  N      . PHE   B 1 201 ? 27.355  -2.308  20.994 1.00 31.75  ?  226 PHE   B N      1 
ATOM   9531  C  CA     . PHE   B 1 201 ? 27.434  -2.359  22.445 1.00 28.86  ?  226 PHE   B CA     1 
ATOM   9532  C  C      . PHE   B 1 201 ? 27.841  -1.012  23.042 1.00 30.20  ?  226 PHE   B C      1 
ATOM   9533  O  O      . PHE   B 1 201 ? 28.012  -0.913  24.262 1.00 29.71  ?  226 PHE   B O      1 
ATOM   9534  C  CB     . PHE   B 1 201 ? 28.415  -3.460  22.867 1.00 28.41  ?  226 PHE   B CB     1 
ATOM   9535  C  CG     . PHE   B 1 201 ? 28.055  -4.849  22.352 1.00 27.39  ?  226 PHE   B CG     1 
ATOM   9536  C  CD1    . PHE   B 1 201 ? 26.855  -5.445  22.711 1.00 27.94  ?  226 PHE   B CD1    1 
ATOM   9537  C  CD2    . PHE   B 1 201 ? 28.930  -5.567  21.541 1.00 27.70  ?  226 PHE   B CD2    1 
ATOM   9538  C  CE1    . PHE   B 1 201 ? 26.517  -6.707  22.258 1.00 27.97  ?  226 PHE   B CE1    1 
ATOM   9539  C  CE2    . PHE   B 1 201 ? 28.597  -6.844  21.090 1.00 26.40  ?  226 PHE   B CE2    1 
ATOM   9540  C  CZ     . PHE   B 1 201 ? 27.385  -7.412  21.456 1.00 27.32  ?  226 PHE   B CZ     1 
ATOM   9541  H  H      . PHE   B 1 201 ? 28.121  -2.200  20.619 1.00 38.09  ?  226 PHE   B H      1 
ATOM   9542  H  HA     . PHE   B 1 201 ? 26.564  -2.587  22.808 1.00 34.62  ?  226 PHE   B HA     1 
ATOM   9543  H  HB2    . PHE   B 1 201 ? 29.296  -3.238  22.525 1.00 34.08  ?  226 PHE   B HB2    1 
ATOM   9544  H  HB3    . PHE   B 1 201 ? 28.436  -3.501  23.836 1.00 34.08  ?  226 PHE   B HB3    1 
ATOM   9545  H  HD1    . PHE   B 1 201 ? 26.266  -4.987  23.267 1.00 33.52  ?  226 PHE   B HD1    1 
ATOM   9546  H  HD2    . PHE   B 1 201 ? 29.745  -5.191  21.297 1.00 33.23  ?  226 PHE   B HD2    1 
ATOM   9547  H  HE1    . PHE   B 1 201 ? 25.699  -7.081  22.496 1.00 33.55  ?  226 PHE   B HE1    1 
ATOM   9548  H  HE2    . PHE   B 1 201 ? 29.186  -7.315  20.545 1.00 31.67  ?  226 PHE   B HE2    1 
ATOM   9549  H  HZ     . PHE   B 1 201 ? 27.160  -8.265  21.161 1.00 32.77  ?  226 PHE   B HZ     1 
ATOM   9550  N  N      . LYS   B 1 202 ? 27.964  0.029   22.211 1.00 32.79  ?  227 LYS   B N      1 
ATOM   9551  C  CA     . LYS   B 1 202 ? 28.357  1.380   22.631 1.00 33.76  ?  227 LYS   B CA     1 
ATOM   9552  C  C      . LYS   B 1 202 ? 29.645  1.375   23.452 1.00 33.69  ?  227 LYS   B C      1 
ATOM   9553  O  O      . LYS   B 1 202 ? 29.774  2.083   24.456 1.00 32.90  ?  227 LYS   B O      1 
ATOM   9554  C  CB     . LYS   B 1 202 ? 27.234  2.073   23.406 1.00 36.19  ?  227 LYS   B CB     1 
ATOM   9555  C  CG     . LYS   B 1 202 ? 25.899  2.111   22.684 1.00 38.94  ?  227 LYS   B CG     1 
ATOM   9556  C  CD     . LYS   B 1 202 ? 24.938  3.056   23.381 1.00 43.52  ?  227 LYS   B CD     1 
ATOM   9557  C  CE     . LYS   B 1 202 ? 23.490  2.615   23.259 1.00 46.86  ?  227 LYS   B CE     1 
ATOM   9558  N  NZ     . LYS   B 1 202 ? 22.603  3.507   24.074 1.00 48.69  ?  227 LYS   B NZ     1 
ATOM   9559  H  H      . LYS   B 1 202 ? 27.818  -0.023  21.365 1.00 39.34  ?  227 LYS   B H      1 
ATOM   9560  H  HA     . LYS   B 1 202 ? 28.533  1.889   21.824 1.00 40.50  ?  227 LYS   B HA     1 
ATOM   9561  H  HB2    . LYS   B 1 202 ? 27.100  1.602   24.244 1.00 43.42  ?  227 LYS   B HB2    1 
ATOM   9562  H  HB3    . LYS   B 1 202 ? 27.499  2.990   23.580 1.00 43.42  ?  227 LYS   B HB3    1 
ATOM   9563  H  HG2    . LYS   B 1 202 ? 26.031  2.422   21.775 1.00 46.72  ?  227 LYS   B HG2    1 
ATOM   9564  H  HG3    . LYS   B 1 202 ? 25.508  1.224   22.677 1.00 46.72  ?  227 LYS   B HG3    1 
ATOM   9565  H  HD2    . LYS   B 1 202 ? 25.161  3.095   24.324 1.00 52.22  ?  227 LYS   B HD2    1 
ATOM   9566  H  HD3    . LYS   B 1 202 ? 25.018  3.937   22.984 1.00 52.22  ?  227 LYS   B HD3    1 
ATOM   9567  H  HE2    . LYS   B 1 202 ? 23.211  2.666   22.332 1.00 56.22  ?  227 LYS   B HE2    1 
ATOM   9568  H  HE3    . LYS   B 1 202 ? 23.398  1.706   23.584 1.00 56.22  ?  227 LYS   B HE3    1 
ATOM   9569  H  HZ1    . LYS   B 1 202 ? 22.669  4.346   23.787 1.00 58.42  ?  227 LYS   B HZ1    1 
ATOM   9570  H  HZ2    . LYS   B 1 202 ? 21.756  3.242   24.002 1.00 58.42  ?  227 LYS   B HZ2    1 
ATOM   9571  H  HZ3    . LYS   B 1 202 ? 22.844  3.475   24.931 1.00 58.42  ?  227 LYS   B HZ3    1 
ATOM   9572  N  N      . MET   B 1 203 ? 30.627  0.604   22.997 1.00 34.30  ?  228 MET   B N      1 
ATOM   9573  C  CA     A MET   B 1 203 ? 31.916  0.546   23.656 0.58 35.02  ?  228 MET   B CA     1 
ATOM   9574  C  CA     B MET   B 1 203 ? 31.922  0.489   23.655 0.42 35.65  ?  228 MET   B CA     1 
ATOM   9575  C  C      . MET   B 1 203 ? 33.019  1.008   22.728 1.00 36.05  ?  228 MET   B C      1 
ATOM   9576  O  O      . MET   B 1 203 ? 32.904  0.921   21.502 1.00 36.91  ?  228 MET   B O      1 
ATOM   9577  C  CB     A MET   B 1 203 ? 32.223  -0.851  24.115 0.58 33.50  ?  228 MET   B CB     1 
ATOM   9578  C  CB     B MET   B 1 203 ? 32.237  -0.973  24.049 0.42 35.79  ?  228 MET   B CB     1 
ATOM   9579  C  CG     A MET   B 1 203 ? 31.330  -1.293  25.210 0.58 31.58  ?  228 MET   B CG     1 
ATOM   9580  C  CG     B MET   B 1 203 ? 31.262  -1.643  25.040 0.42 35.75  ?  228 MET   B CG     1 
ATOM   9581  S  SD     A MET   B 1 203 ? 31.622  -3.041  25.378 0.58 27.83  ?  228 MET   B SD     1 
ATOM   9582  S  SD     B MET   B 1 203 ? 31.609  -1.456  26.814 0.42 34.52  ?  228 MET   B SD     1 
ATOM   9583  C  CE     A MET   B 1 203 ? 33.396  -3.090  25.639 0.58 26.82  ?  228 MET   B CE     1 
ATOM   9584  C  CE     B MET   B 1 203 ? 33.322  -1.974  26.922 0.42 33.93  ?  228 MET   B CE     1 
ATOM   9585  H  H      A MET   B 1 203 ? 30.565  0.103   22.301 0.58 41.15  ?  228 MET   B H      1 
ATOM   9586  H  H      B MET   B 1 203 ? 30.564  0.124   22.287 0.42 41.15  ?  228 MET   B H      1 
ATOM   9587  H  HA     A MET   B 1 203 ? 31.890  1.135   24.427 0.58 42.02  ?  228 MET   B HA     1 
ATOM   9588  H  HA     B MET   B 1 203 ? 31.906  1.019   24.467 0.42 42.77  ?  228 MET   B HA     1 
ATOM   9589  H  HB2    A MET   B 1 203 ? 32.112  -1.462  23.370 0.58 40.20  ?  228 MET   B HB2    1 
ATOM   9590  H  HB2    B MET   B 1 203 ? 32.234  -1.510  23.241 0.42 42.94  ?  228 MET   B HB2    1 
ATOM   9591  H  HB3    A MET   B 1 203 ? 33.137  -0.885  24.439 0.58 40.20  ?  228 MET   B HB3    1 
ATOM   9592  H  HB3    B MET   B 1 203 ? 33.116  -0.992  24.458 0.42 42.94  ?  228 MET   B HB3    1 
ATOM   9593  H  HG2    A MET   B 1 203 ? 31.551  -0.839  26.038 0.58 37.89  ?  228 MET   B HG2    1 
ATOM   9594  H  HG2    B MET   B 1 203 ? 30.380  -1.271  24.887 0.42 42.90  ?  228 MET   B HG2    1 
ATOM   9595  H  HG3    A MET   B 1 203 ? 30.401  -1.133  24.981 0.58 37.89  ?  228 MET   B HG3    1 
ATOM   9596  H  HG3    B MET   B 1 203 ? 31.258  -2.595  24.856 0.42 42.90  ?  228 MET   B HG3    1 
ATOM   9597  H  HE1    A MET   B 1 203 ? 33.633  -3.939  26.044 0.58 32.18  ?  228 MET   B HE1    1 
ATOM   9598  H  HE1    B MET   B 1 203 ? 33.567  -2.063  27.856 0.42 40.70  ?  228 MET   B HE1    1 
ATOM   9599  H  HE2    A MET   B 1 203 ? 33.844  -2.996  24.784 0.58 32.18  ?  228 MET   B HE2    1 
ATOM   9600  H  HE2    B MET   B 1 203 ? 33.423  -2.826  26.470 0.42 40.70  ?  228 MET   B HE2    1 
ATOM   9601  H  HE3    A MET   B 1 203 ? 33.649  -2.361  26.227 0.58 32.18  ?  228 MET   B HE3    1 
ATOM   9602  H  HE3    B MET   B 1 203 ? 33.881  -1.305  26.496 0.42 40.70  ?  228 MET   B HE3    1 
ATOM   9603  N  N      . GLN   B 1 204 ? 34.097  1.511   23.334 1.00 37.99  ?  229 GLN   B N      1 
ATOM   9604  C  CA     . GLN   B 1 204 ? 35.246  1.997   22.583 1.00 41.86  ?  229 GLN   B CA     1 
ATOM   9605  C  C      . GLN   B 1 204 ? 36.310  0.923   22.389 1.00 41.79  ?  229 GLN   B C      1 
ATOM   9606  O  O      . GLN   B 1 204 ? 36.985  0.910   21.352 1.00 42.49  ?  229 GLN   B O      1 
ATOM   9607  C  CB     . GLN   B 1 204 ? 35.847  3.206   23.300 1.00 45.87  ?  229 GLN   B CB     1 
ATOM   9608  C  CG     . GLN   B 1 204 ? 36.617  4.143   22.396 1.00 50.07  ?  229 GLN   B CG     1 
ATOM   9609  C  CD     . GLN   B 1 204 ? 36.479  5.602   22.804 1.00 51.76  ?  229 GLN   B CD     1 
ATOM   9610  O  OE1    . GLN   B 1 204 ? 36.061  5.918   23.919 1.00 53.05  ?  229 GLN   B OE1    1 
ATOM   9611  N  NE2    . GLN   B 1 204 ? 36.818  6.498   21.889 1.00 50.78  ?  229 GLN   B NE2    1 
ATOM   9612  H  H      . GLN   B 1 204 ? 34.184  1.580   24.187 1.00 45.58  ?  229 GLN   B H      1 
ATOM   9613  H  HA     . GLN   B 1 204 ? 34.961  2.285   21.701 1.00 50.23  ?  229 GLN   B HA     1 
ATOM   9614  H  HB2    . GLN   B 1 204 ? 35.127  3.715   23.706 1.00 55.03  ?  229 GLN   B HB2    1 
ATOM   9615  H  HB3    . GLN   B 1 204 ? 36.457  2.889   23.984 1.00 55.03  ?  229 GLN   B HB3    1 
ATOM   9616  H  HG2    . GLN   B 1 204 ? 37.559  3.911   22.429 1.00 60.07  ?  229 GLN   B HG2    1 
ATOM   9617  H  HG3    . GLN   B 1 204 ? 36.285  4.053   21.490 1.00 60.07  ?  229 GLN   B HG3    1 
ATOM   9618  H  HE21   . GLN   B 1 204 ? 37.097  6.241   21.117 1.00 60.93  ?  229 GLN   B HE21   1 
ATOM   9619  H  HE22   . GLN   B 1 204 ? 36.759  7.338   22.066 1.00 60.93  ?  229 GLN   B HE22   1 
ATOM   9620  N  N      . SER   B 1 205 ? 36.470  0.017   23.351 1.00 40.03  ?  230 SER   B N      1 
ATOM   9621  C  CA     . SER   B 1 205 ? 37.452  -1.054  23.244 1.00 38.70  ?  230 SER   B CA     1 
ATOM   9622  C  C      . SER   B 1 205 ? 37.086  -2.138  24.248 1.00 37.07  ?  230 SER   B C      1 
ATOM   9623  O  O      . SER   B 1 205 ? 36.163  -1.979  25.050 1.00 36.05  ?  230 SER   B O      1 
ATOM   9624  C  CB     . SER   B 1 205 ? 38.870  -0.539  23.505 1.00 41.59  ?  230 SER   B CB     1 
ATOM   9625  O  OG     . SER   B 1 205 ? 39.021  -0.187  24.870 1.00 42.92  ?  230 SER   B OG     1 
ATOM   9626  H  H      . SER   B 1 205 ? 36.017  0.003   24.081 1.00 48.04  ?  230 SER   B H      1 
ATOM   9627  H  HA     . SER   B 1 205 ? 37.418  -1.430  22.351 1.00 46.43  ?  230 SER   B HA     1 
ATOM   9628  H  HB2    . SER   B 1 205 ? 39.508  -1.235  23.283 1.00 49.90  ?  230 SER   B HB2    1 
ATOM   9629  H  HB3    . SER   B 1 205 ? 39.030  0.245   22.955 1.00 49.90  ?  230 SER   B HB3    1 
ATOM   9630  H  HG     . SER   B 1 205 ? 39.801  0.092   25.010 1.00 51.49  ?  230 SER   B HG     1 
ATOM   9631  N  N      . LEU   B 1 206 ? 37.829  -3.245  24.199 1.00 35.88  ?  231 LEU   B N      1 
ATOM   9632  C  CA     . LEU   B 1 206 ? 37.712  -4.319  25.189 1.00 33.49  ?  231 LEU   B CA     1 
ATOM   9633  C  C      . LEU   B 1 206 ? 38.491  -3.884  26.425 1.00 33.71  ?  231 LEU   B C      1 
ATOM   9634  O  O      . LEU   B 1 206 ? 39.707  -4.076  26.520 1.00 36.45  ?  231 LEU   B O      1 
ATOM   9635  C  CB     . LEU   B 1 206 ? 38.256  -5.629  24.638 1.00 33.41  ?  231 LEU   B CB     1 
ATOM   9636  C  CG     . LEU   B 1 206 ? 37.522  -6.254  23.454 1.00 34.16  ?  231 LEU   B CG     1 
ATOM   9637  C  CD1    . LEU   B 1 206 ? 38.304  -7.446  22.923 1.00 34.21  ?  231 LEU   B CD1    1 
ATOM   9638  C  CD2    . LEU   B 1 206 ? 36.111  -6.653  23.865 1.00 36.10  ?  231 LEU   B CD2    1 
ATOM   9639  H  H      . LEU   B 1 206 ? 38.417  -3.401  23.592 1.00 43.06  ?  231 LEU   B H      1 
ATOM   9640  H  HA     . LEU   B 1 206 ? 36.779  -4.450  25.420 1.00 40.18  ?  231 LEU   B HA     1 
ATOM   9641  H  HB2    . LEU   B 1 206 ? 39.170  -5.474  24.352 1.00 40.08  ?  231 LEU   B HB2    1 
ATOM   9642  H  HB3    . LEU   B 1 206 ? 38.239  -6.283  25.355 1.00 40.08  ?  231 LEU   B HB3    1 
ATOM   9643  H  HG     . LEU   B 1 206 ? 37.448  -5.607  22.734 1.00 40.99  ?  231 LEU   B HG     1 
ATOM   9644  H  HD11   . LEU   B 1 206 ? 37.818  -7.837  22.180 1.00 41.05  ?  231 LEU   B HD11   1 
ATOM   9645  H  HD12   . LEU   B 1 206 ? 39.176  -7.145  22.626 1.00 41.05  ?  231 LEU   B HD12   1 
ATOM   9646  H  HD13   . LEU   B 1 206 ? 38.403  -8.100  23.633 1.00 41.05  ?  231 LEU   B HD13   1 
ATOM   9647  H  HD21   . LEU   B 1 206 ? 35.687  -7.119  23.128 1.00 43.31  ?  231 LEU   B HD21   1 
ATOM   9648  H  HD22   . LEU   B 1 206 ? 36.161  -7.234  24.640 1.00 43.31  ?  231 LEU   B HD22   1 
ATOM   9649  H  HD23   . LEU   B 1 206 ? 35.608  -5.853  24.084 1.00 43.31  ?  231 LEU   B HD23   1 
ATOM   9650  N  N      . ASP   B 1 207 ? 37.781  -3.288  27.390 1.00 31.16  ?  232 ASP   B N      1 
ATOM   9651  C  CA     . ASP   B 1 207 ? 38.417  -2.632  28.524 1.00 30.30  ?  232 ASP   B CA     1 
ATOM   9652  C  C      . ASP   B 1 207 ? 38.710  -3.608  29.668 1.00 30.58  ?  232 ASP   B C      1 
ATOM   9653  O  O      . ASP   B 1 207 ? 38.495  -4.819  29.568 1.00 30.23  ?  232 ASP   B O      1 
ATOM   9654  C  CB     . ASP   B 1 207 ? 37.571  -1.432  28.993 1.00 30.56  ?  232 ASP   B CB     1 
ATOM   9655  C  CG     . ASP   B 1 207 ? 36.174  -1.809  29.512 1.00 32.55  ?  232 ASP   B CG     1 
ATOM   9656  O  OD1    . ASP   B 1 207 ? 35.845  -3.003  29.665 1.00 32.60  ?  232 ASP   B OD1    1 
ATOM   9657  O  OD2    . ASP   B 1 207 ? 35.391  -0.867  29.782 1.00 35.19  ?  232 ASP   B OD2    1 
ATOM   9658  H  H      . ASP   B 1 207 ? 36.922  -3.253  27.406 1.00 37.38  ?  232 ASP   B H      1 
ATOM   9659  H  HA     . ASP   B 1 207 ? 39.278  -2.300  28.224 1.00 36.35  ?  232 ASP   B HA     1 
ATOM   9660  H  HB2    . ASP   B 1 207 ? 38.041  -0.984  29.713 1.00 36.67  ?  232 ASP   B HB2    1 
ATOM   9661  H  HB3    . ASP   B 1 207 ? 37.452  -0.825  28.245 1.00 36.67  ?  232 ASP   B HB3    1 
ATOM   9662  N  N      . LYS   B 1 208 ? 39.255  -3.053  30.761 1.00 29.77  ?  233 LYS   B N      1 
ATOM   9663  C  CA     . LYS   B 1 208 ? 39.749  -3.869  31.866 1.00 30.27  ?  233 LYS   B CA     1 
ATOM   9664  C  C      . LYS   B 1 208 ? 38.663  -4.781  32.409 1.00 28.73  ?  233 LYS   B C      1 
ATOM   9665  O  O      . LYS   B 1 208 ? 38.914  -5.959  32.685 1.00 28.26  ?  233 LYS   B O      1 
ATOM   9666  C  CB     . LYS   B 1 208 ? 40.271  -2.961  32.984 1.00 33.10  ?  233 LYS   B CB     1 
ATOM   9667  C  CG     . LYS   B 1 208 ? 40.684  -3.679  34.271 1.00 35.57  ?  233 LYS   B CG     1 
ATOM   9668  C  CD     . LYS   B 1 208 ? 40.962  -2.682  35.394 1.00 39.25  ?  233 LYS   B CD     1 
ATOM   9669  C  CE     . LYS   B 1 208 ? 41.619  -3.348  36.587 1.00 41.99  ?  233 LYS   B CE     1 
ATOM   9670  N  NZ     . LYS   B 1 208 ? 41.895  -2.367  37.671 1.00 45.09  ?  233 LYS   B NZ     1 
ATOM   9671  H  H      . LYS   B 1 208 ? 39.348  -2.206  30.883 1.00 35.72  ?  233 LYS   B H      1 
ATOM   9672  H  HA     . LYS   B 1 208 ? 40.478  -4.421  31.543 1.00 36.32  ?  233 LYS   B HA     1 
ATOM   9673  H  HB2    . LYS   B 1 208 ? 41.050  -2.487  32.654 1.00 39.71  ?  233 LYS   B HB2    1 
ATOM   9674  H  HB3    . LYS   B 1 208 ? 39.572  -2.330  33.216 1.00 39.71  ?  233 LYS   B HB3    1 
ATOM   9675  H  HG2    . LYS   B 1 208 ? 39.969  -4.269  34.555 1.00 42.68  ?  233 LYS   B HG2    1 
ATOM   9676  H  HG3    . LYS   B 1 208 ? 41.492  -4.191  34.109 1.00 42.68  ?  233 LYS   B HG3    1 
ATOM   9677  H  HD2    . LYS   B 1 208 ? 41.556  -1.989  35.067 1.00 47.10  ?  233 LYS   B HD2    1 
ATOM   9678  H  HD3    . LYS   B 1 208 ? 40.125  -2.290  35.688 1.00 47.10  ?  233 LYS   B HD3    1 
ATOM   9679  H  HE2    . LYS   B 1 208 ? 41.030  -4.033  36.939 1.00 50.38  ?  233 LYS   B HE2    1 
ATOM   9680  H  HE3    . LYS   B 1 208 ? 42.461  -3.743  36.312 1.00 50.38  ?  233 LYS   B HE3    1 
ATOM   9681  H  HZ1    . LYS   B 1 208 ? 42.288  -2.774  38.358 1.00 54.10  ?  233 LYS   B HZ1    1 
ATOM   9682  H  HZ2    . LYS   B 1 208 ? 42.433  -1.724  37.370 1.00 54.10  ?  233 LYS   B HZ2    1 
ATOM   9683  H  HZ3    . LYS   B 1 208 ? 41.134  -1.999  37.950 1.00 54.10  ?  233 LYS   B HZ3    1 
ATOM   9684  N  N      . ASP   B 1 209 ? 37.461  -4.251  32.587 1.00 27.59  ?  234 ASP   B N      1 
ATOM   9685  C  CA     . ASP   B 1 209 ? 36.411  -5.027  33.230 1.00 26.20  ?  234 ASP   B CA     1 
ATOM   9686  C  C      . ASP   B 1 209 ? 35.954  -6.189  32.355 1.00 25.31  ?  234 ASP   B C      1 
ATOM   9687  O  O      . ASP   B 1 209 ? 35.781  -7.312  32.845 1.00 25.33  ?  234 ASP   B O      1 
ATOM   9688  C  CB     . ASP   B 1 209 ? 35.223  -4.123  33.573 1.00 26.90  ?  234 ASP   B CB     1 
ATOM   9689  C  CG     . ASP   B 1 209 ? 35.443  -3.290  34.831 1.00 27.95  ?  234 ASP   B CG     1 
ATOM   9690  O  OD1    . ASP   B 1 209 ? 36.479  -3.437  35.510 1.00 29.33  ?  234 ASP   B OD1    1 
ATOM   9691  O  OD2    . ASP   B 1 209 ? 34.542  -2.483  35.153 1.00 27.85  ?  234 ASP   B OD2    1 
ATOM   9692  H  H      . ASP   B 1 209 ? 37.230  -3.457  32.349 1.00 33.10  ?  234 ASP   B H      1 
ATOM   9693  H  HA     . ASP   B 1 209 ? 36.767  -5.394  34.054 1.00 31.43  ?  234 ASP   B HA     1 
ATOM   9694  H  HB2    . ASP   B 1 209 ? 35.069  -3.513  32.835 1.00 32.28  ?  234 ASP   B HB2    1 
ATOM   9695  H  HB3    . ASP   B 1 209 ? 34.439  -4.676  33.716 1.00 32.28  ?  234 ASP   B HB3    1 
ATOM   9696  N  N      . ILE   B 1 210 ? 35.726  -5.947  31.064 1.00 25.64  ?  235 ILE   B N      1 
ATOM   9697  C  CA     . ILE   B 1 210 ? 35.216  -7.045  30.245 1.00 25.38  ?  235 ILE   B CA     1 
ATOM   9698  C  C      . ILE   B 1 210 ? 36.298  -8.105  30.064 1.00 24.70  ?  235 ILE   B C      1 
ATOM   9699  O  O      . ILE   B 1 210 ? 35.995  -9.304  30.055 1.00 24.88  ?  235 ILE   B O      1 
ATOM   9700  C  CB     . ILE   B 1 210 ? 34.657  -6.546  28.897 1.00 26.52  ?  235 ILE   B CB     1 
ATOM   9701  C  CG1    . ILE   B 1 210 ? 33.920  -7.688  28.159 1.00 25.91  ?  235 ILE   B CG1    1 
ATOM   9702  C  CG2    . ILE   B 1 210 ? 35.758  -5.932  28.013 1.00 28.01  ?  235 ILE   B CG2    1 
ATOM   9703  C  CD1    . ILE   B 1 210 ? 32.689  -8.278  28.867 1.00 26.59  ?  235 ILE   B CD1    1 
ATOM   9704  H  H      . ILE   B 1 210 ? 35.852  -5.198  30.660 1.00 30.76  ?  235 ILE   B H      1 
ATOM   9705  H  HA     . ILE   B 1 210 ? 34.467  -7.447  30.713 1.00 30.45  ?  235 ILE   B HA     1 
ATOM   9706  H  HB     . ILE   B 1 210 ? 34.017  -5.842  29.088 1.00 31.82  ?  235 ILE   B HB     1 
ATOM   9707  H  HG12   . ILE   B 1 210 ? 33.619  -7.349  27.301 1.00 31.09  ?  235 ILE   B HG12   1 
ATOM   9708  H  HG13   . ILE   B 1 210 ? 34.548  -8.416  28.026 1.00 31.09  ?  235 ILE   B HG13   1 
ATOM   9709  H  HG21   . ILE   B 1 210 ? 35.348  -5.538  27.227 1.00 33.60  ?  235 ILE   B HG21   1 
ATOM   9710  H  HG22   . ILE   B 1 210 ? 36.226  -5.250  28.520 1.00 33.60  ?  235 ILE   B HG22   1 
ATOM   9711  H  HG23   . ILE   B 1 210 ? 36.377  -6.630  27.748 1.00 33.60  ?  235 ILE   B HG23   1 
ATOM   9712  H  HD11   . ILE   B 1 210 ? 32.225  -8.870  28.255 1.00 31.90  ?  235 ILE   B HD11   1 
ATOM   9713  H  HD12   . ILE   B 1 210 ? 32.981  -8.773  29.649 1.00 31.90  ?  235 ILE   B HD12   1 
ATOM   9714  H  HD13   . ILE   B 1 210 ? 32.102  -7.554  29.135 1.00 31.90  ?  235 ILE   B HD13   1 
ATOM   9715  N  N      . VAL   B 1 211 ? 37.571  -7.702  29.962 1.00 25.11  ?  236 VAL   B N      1 
ATOM   9716  C  CA     . VAL   B 1 211 ? 38.645  -8.691  29.883 1.00 25.61  ?  236 VAL   B CA     1 
ATOM   9717  C  C      . VAL   B 1 211 ? 38.701  -9.528  31.155 1.00 25.49  ?  236 VAL   B C      1 
ATOM   9718  O  O      . VAL   B 1 211 ? 38.866  -10.751 31.099 1.00 26.14  ?  236 VAL   B O      1 
ATOM   9719  C  CB     . VAL   B 1 211 ? 40.000  -8.017  29.606 1.00 26.17  ?  236 VAL   B CB     1 
ATOM   9720  C  CG1    . VAL   B 1 211 ? 41.155  -9.015  29.790 1.00 27.62  ?  236 VAL   B CG1    1 
ATOM   9721  C  CG2    . VAL   B 1 211 ? 40.018  -7.457  28.207 1.00 27.86  ?  236 VAL   B CG2    1 
ATOM   9722  H  H      . VAL   B 1 211 ? 37.830  -6.882  29.936 1.00 30.13  ?  236 VAL   B H      1 
ATOM   9723  H  HA     . VAL   B 1 211 ? 38.445  -9.279  29.138 1.00 30.72  ?  236 VAL   B HA     1 
ATOM   9724  H  HB     . VAL   B 1 211 ? 40.125  -7.293  30.239 1.00 31.40  ?  236 VAL   B HB     1 
ATOM   9725  H  HG11   . VAL   B 1 211 ? 41.948  -8.664  29.355 1.00 33.14  ?  236 VAL   B HG11   1 
ATOM   9726  H  HG12   . VAL   B 1 211 ? 41.323  -9.134  30.738 1.00 33.14  ?  236 VAL   B HG12   1 
ATOM   9727  H  HG13   . VAL   B 1 211 ? 40.907  -9.863  29.390 1.00 33.14  ?  236 VAL   B HG13   1 
ATOM   9728  H  HG21   . VAL   B 1 211 ? 40.868  -7.015  28.055 1.00 33.42  ?  236 VAL   B HG21   1 
ATOM   9729  H  HG22   . VAL   B 1 211 ? 39.905  -8.183  27.575 1.00 33.42  ?  236 VAL   B HG22   1 
ATOM   9730  H  HG23   . VAL   B 1 211 ? 39.293  -6.820  28.113 1.00 33.42  ?  236 VAL   B HG23   1 
ATOM   9731  N  N      . ALA   B 1 212 ? 38.572  -8.893  32.321 1.00 25.07  ?  237 ALA   B N      1 
ATOM   9732  C  CA     . ALA   B 1 212 ? 38.650  -9.641  33.573 1.00 24.87  ?  237 ALA   B CA     1 
ATOM   9733  C  C      . ALA   B 1 212 ? 37.488  -10.616 33.734 1.00 24.06  ?  237 ALA   B C      1 
ATOM   9734  O  O      . ALA   B 1 212 ? 37.658  -11.676 34.351 1.00 23.92  ?  237 ALA   B O      1 
ATOM   9735  C  CB     . ALA   B 1 212 ? 38.693  -8.674  34.753 1.00 26.14  ?  237 ALA   B CB     1 
ATOM   9736  H  H      . ALA   B 1 212 ? 38.442  -8.048  32.412 1.00 30.08  ?  237 ALA   B H      1 
ATOM   9737  H  HA     . ALA   B 1 212 ? 39.470  -10.159 33.570 1.00 29.83  ?  237 ALA   B HA     1 
ATOM   9738  H  HB1    . ALA   B 1 212 ? 38.820  -9.179  35.571 1.00 31.36  ?  237 ALA   B HB1    1 
ATOM   9739  H  HB2    . ALA   B 1 212 ? 39.430  -8.055  34.628 1.00 31.36  ?  237 ALA   B HB2    1 
ATOM   9740  H  HB3    . ALA   B 1 212 ? 37.855  -8.186  34.793 1.00 31.36  ?  237 ALA   B HB3    1 
ATOM   9741  N  N      . LEU   B 1 213 ? 36.304  -10.259 33.221 1.00 23.11  ?  238 LEU   B N      1 
ATOM   9742  C  CA     . LEU   B 1 213 ? 35.182  -11.194 33.183 1.00 21.44  ?  238 LEU   B CA     1 
ATOM   9743  C  C      . LEU   B 1 213 ? 35.440  -12.355 32.232 1.00 22.10  ?  238 LEU   B C      1 
ATOM   9744  O  O      . LEU   B 1 213 ? 35.095  -13.505 32.535 1.00 22.24  ?  238 LEU   B O      1 
ATOM   9745  C  CB     . LEU   B 1 213 ? 33.911  -10.464 32.746 1.00 23.55  ?  238 LEU   B CB     1 
ATOM   9746  C  CG     . LEU   B 1 213 ? 33.291  -9.550  33.793 1.00 23.13  ?  238 LEU   B CG     1 
ATOM   9747  C  CD1    . LEU   B 1 213 ? 32.303  -8.592  33.161 1.00 23.88  ?  238 LEU   B CD1    1 
ATOM   9748  C  CD2    . LEU   B 1 213 ? 32.591  -10.395 34.852 1.00 22.79  ?  238 LEU   B CD2    1 
ATOM   9749  H  H      . LEU   B 1 213 ? 36.129  -9.484  32.890 1.00 27.73  ?  238 LEU   B H      1 
ATOM   9750  H  HA     . LEU   B 1 213 ? 35.059  -11.549 34.077 1.00 25.72  ?  238 LEU   B HA     1 
ATOM   9751  H  HB2    . LEU   B 1 213 ? 34.123  -9.917  31.974 1.00 28.25  ?  238 LEU   B HB2    1 
ATOM   9752  H  HB3    . LEU   B 1 213 ? 33.244  -11.127 32.510 1.00 28.25  ?  238 LEU   B HB3    1 
ATOM   9753  H  HG     . LEU   B 1 213 ? 33.989  -9.022  34.211 1.00 27.75  ?  238 LEU   B HG     1 
ATOM   9754  H  HD11   . LEU   B 1 213 ? 31.907  -8.043  33.855 1.00 28.65  ?  238 LEU   B HD11   1 
ATOM   9755  H  HD12   . LEU   B 1 213 ? 32.771  -8.032  32.522 1.00 28.65  ?  238 LEU   B HD12   1 
ATOM   9756  H  HD13   . LEU   B 1 213 ? 31.613  -9.103  32.709 1.00 28.65  ?  238 LEU   B HD13   1 
ATOM   9757  H  HD21   . LEU   B 1 213 ? 32.197  -9.807  35.515 1.00 27.34  ?  238 LEU   B HD21   1 
ATOM   9758  H  HD22   . LEU   B 1 213 ? 31.900  -10.926 34.426 1.00 27.34  ?  238 LEU   B HD22   1 
ATOM   9759  H  HD23   . LEU   B 1 213 ? 33.243  -10.977 35.272 1.00 27.34  ?  238 LEU   B HD23   1 
ATOM   9760  N  N      . MET   B 1 214 ? 36.005  -12.068 31.058 1.00 23.14  ?  239 MET   B N      1 
ATOM   9761  C  CA     . MET   B 1 214 ? 36.264  -13.121 30.084 1.00 24.28  ?  239 MET   B CA     1 
ATOM   9762  C  C      . MET   B 1 214 ? 37.337  -14.077 30.586 1.00 24.30  ?  239 MET   B C      1 
ATOM   9763  O  O      . MET   B 1 214 ? 37.230  -15.293 30.399 1.00 25.04  ?  239 MET   B O      1 
ATOM   9764  C  CB     . MET   B 1 214 ? 36.675  -12.500 28.749 1.00 24.46  ?  239 MET   B CB     1 
ATOM   9765  C  CG     . MET   B 1 214 ? 35.535  -11.831 27.989 1.00 25.80  ?  239 MET   B CG     1 
ATOM   9766  S  SD     . MET   B 1 214 ? 36.091  -10.999 26.480 1.00 31.05  ?  239 MET   B SD     1 
ATOM   9767  C  CE     . MET   B 1 214 ? 34.526  -10.472 25.784 1.00 32.30  ?  239 MET   B CE     1 
ATOM   9768  H  H      . MET   B 1 214 ? 36.243  -11.281 30.806 1.00 27.77  ?  239 MET   B H      1 
ATOM   9769  H  HA     . MET   B 1 214 ? 35.446  -13.622 29.938 1.00 29.13  ?  239 MET   B HA     1 
ATOM   9770  H  HB2    . MET   B 1 214 ? 37.352  -11.825 28.917 1.00 29.35  ?  239 MET   B HB2    1 
ATOM   9771  H  HB3    . MET   B 1 214 ? 37.037  -13.198 28.181 1.00 29.35  ?  239 MET   B HB3    1 
ATOM   9772  H  HG2    . MET   B 1 214 ? 34.885  -12.506 27.737 1.00 30.95  ?  239 MET   B HG2    1 
ATOM   9773  H  HG3    . MET   B 1 214 ? 35.119  -11.168 28.561 1.00 30.95  ?  239 MET   B HG3    1 
ATOM   9774  H  HE1    . MET   B 1 214 ? 34.697  -9.927  25.000 1.00 38.75  ?  239 MET   B HE1    1 
ATOM   9775  H  HE2    . MET   B 1 214 ? 34.011  -11.256 25.536 1.00 38.75  ?  239 MET   B HE2    1 
ATOM   9776  H  HE3    . MET   B 1 214 ? 34.043  -9.955  26.448 1.00 38.75  ?  239 MET   B HE3    1 
ATOM   9777  N  N      . VAL   B 1 215 ? 38.379  -13.543 31.223 1.00 25.04  ?  240 VAL   B N      1 
ATOM   9778  C  CA     . VAL   B 1 215 ? 39.429  -14.394 31.773 1.00 25.41  ?  240 VAL   B CA     1 
ATOM   9779  C  C      . VAL   B 1 215 ? 38.869  -15.277 32.880 1.00 24.56  ?  240 VAL   B C      1 
ATOM   9780  O  O      . VAL   B 1 215 ? 39.193  -16.474 32.967 1.00 24.69  ?  240 VAL   B O      1 
ATOM   9781  C  CB     . VAL   B 1 215 ? 40.600  -13.524 32.260 1.00 27.31  ?  240 VAL   B CB     1 
ATOM   9782  C  CG1    . VAL   B 1 215 ? 41.582  -14.350 33.047 1.00 27.99  ?  240 VAL   B CG1    1 
ATOM   9783  C  CG2    . VAL   B 1 215 ? 41.298  -12.858 31.070 1.00 27.82  ?  240 VAL   B CG2    1 
ATOM   9784  H  H      . VAL   B 1 215 ? 38.500  -12.701 31.348 1.00 30.05  ?  240 VAL   B H      1 
ATOM   9785  H  HA     . VAL   B 1 215 ? 39.762  -14.980 31.075 1.00 30.49  ?  240 VAL   B HA     1 
ATOM   9786  H  HB     . VAL   B 1 215 ? 40.254  -12.829 32.842 1.00 32.77  ?  240 VAL   B HB     1 
ATOM   9787  H  HG11   . VAL   B 1 215 ? 42.402  -13.845 33.159 1.00 33.58  ?  240 VAL   B HG11   1 
ATOM   9788  H  HG12   . VAL   B 1 215 ? 41.199  -14.555 33.915 1.00 33.58  ?  240 VAL   B HG12   1 
ATOM   9789  H  HG13   . VAL   B 1 215 ? 41.763  -15.171 32.563 1.00 33.58  ?  240 VAL   B HG13   1 
ATOM   9790  H  HG21   . VAL   B 1 215 ? 42.006  -12.283 31.400 1.00 33.38  ?  240 VAL   B HG21   1 
ATOM   9791  H  HG22   . VAL   B 1 215 ? 41.670  -13.546 30.497 1.00 33.38  ?  240 VAL   B HG22   1 
ATOM   9792  H  HG23   . VAL   B 1 215 ? 40.648  -12.333 30.577 1.00 33.38  ?  240 VAL   B HG23   1 
ATOM   9793  N  N      . ARG   B 1 216 ? 37.998  -14.720 33.724 1.00 23.98  ?  241 ARG   B N      1 
ATOM   9794  C  CA     . ARG   B 1 216 ? 37.409  -15.549 34.766 1.00 24.14  ?  241 ARG   B CA     1 
ATOM   9795  C  C      . ARG   B 1 216 ? 36.557  -16.655 34.160 1.00 23.64  ?  241 ARG   B C      1 
ATOM   9796  O  O      . ARG   B 1 216 ? 36.532  -17.779 34.671 1.00 23.62  ?  241 ARG   B O      1 
ATOM   9797  C  CB     . ARG   B 1 216 ? 36.545  -14.741 35.730 1.00 24.01  ?  241 ARG   B CB     1 
ATOM   9798  C  CG     . ARG   B 1 216 ? 36.327  -15.496 37.047 1.00 22.95  ?  241 ARG   B CG     1 
ATOM   9799  C  CD     . ARG   B 1 216 ? 34.871  -15.478 37.539 1.00 22.14  ?  241 ARG   B CD     1 
ATOM   9800  N  NE     . ARG   B 1 216 ? 33.975  -16.161 36.615 1.00 21.39  ?  241 ARG   B NE     1 
ATOM   9801  C  CZ     . ARG   B 1 216 ? 33.003  -15.578 35.914 1.00 21.12  ?  241 ARG   B CZ     1 
ATOM   9802  N  NH1    . ARG   B 1 216 ? 32.743  -14.278 36.010 1.00 22.79  ?  241 ARG   B NH1    1 
ATOM   9803  N  NH2    . ARG   B 1 216 ? 32.280  -16.323 35.096 1.00 22.70  ?  241 ARG   B NH2    1 
ATOM   9804  H  H      . ARG   B 1 216 ? 37.745  -13.898 33.713 1.00 28.77  ?  241 ARG   B H      1 
ATOM   9805  H  HA     . ARG   B 1 216 ? 38.143  -15.927 35.274 1.00 28.96  ?  241 ARG   B HA     1 
ATOM   9806  H  HB2    . ARG   B 1 216 ? 36.985  -13.899 35.927 1.00 28.81  ?  241 ARG   B HB2    1 
ATOM   9807  H  HB3    . ARG   B 1 216 ? 35.679  -14.575 35.325 1.00 28.81  ?  241 ARG   B HB3    1 
ATOM   9808  H  HG2    . ARG   B 1 216 ? 36.586  -16.422 36.923 1.00 27.53  ?  241 ARG   B HG2    1 
ATOM   9809  H  HG3    . ARG   B 1 216 ? 36.876  -15.088 37.736 1.00 27.53  ?  241 ARG   B HG3    1 
ATOM   9810  H  HD2    . ARG   B 1 216 ? 34.818  -15.925 38.398 1.00 26.56  ?  241 ARG   B HD2    1 
ATOM   9811  H  HD3    . ARG   B 1 216 ? 34.574  -14.558 37.625 1.00 26.56  ?  241 ARG   B HD3    1 
ATOM   9812  H  HE     . ARG   B 1 216 ? 34.082  -17.008 36.514 1.00 25.67  ?  241 ARG   B HE     1 
ATOM   9813  H  HH11   . ARG   B 1 216 ? 33.208  -13.785 36.539 1.00 27.34  ?  241 ARG   B HH11   1 
ATOM   9814  H  HH12   . ARG   B 1 216 ? 32.108  -13.931 35.545 1.00 27.34  ?  241 ARG   B HH12   1 
ATOM   9815  H  HH21   . ARG   B 1 216 ? 32.441  -17.165 35.026 1.00 27.23  ?  241 ARG   B HH21   1 
ATOM   9816  H  HH22   . ARG   B 1 216 ? 31.648  -15.966 34.635 1.00 27.23  ?  241 ARG   B HH22   1 
ATOM   9817  N  N      . ARG   B 1 217 ? 35.809  -16.342 33.100 1.00 22.28  ?  242 ARG   B N      1 
ATOM   9818  C  CA     . ARG   B 1 217 ? 34.996  -17.375 32.465 1.00 22.28  ?  242 ARG   B CA     1 
ATOM   9819  C  C      . ARG   B 1 217 ? 35.876  -18.511 31.943 1.00 23.05  ?  242 ARG   B C      1 
ATOM   9820  O  O      . ARG   B 1 217 ? 35.475  -19.676 32.008 1.00 22.66  ?  242 ARG   B O      1 
ATOM   9821  C  CB     . ARG   B 1 217 ? 34.142  -16.751 31.355 1.00 21.66  ?  242 ARG   B CB     1 
ATOM   9822  C  CG     . ARG   B 1 217 ? 33.029  -17.636 30.827 1.00 20.99  ?  242 ARG   B CG     1 
ATOM   9823  C  CD     . ARG   B 1 217 ? 31.758  -17.707 31.763 1.00 19.90  ?  242 ARG   B CD     1 
ATOM   9824  N  NE     . ARG   B 1 217 ? 30.965  -18.725 31.117 1.00 19.83  ?  242 ARG   B NE     1 
ATOM   9825  C  CZ     . ARG   B 1 217 ? 30.993  -20.021 31.420 1.00 20.75  ?  242 ARG   B CZ     1 
ATOM   9826  N  NH1    . ARG   B 1 217 ? 31.661  -20.477 32.473 1.00 21.72  ?  242 ARG   B NH1    1 
ATOM   9827  N  NH2    . ARG   B 1 217 ? 30.319  -20.863 30.659 1.00 20.21  ?  242 ARG   B NH2    1 
ATOM   9828  H  H      . ARG   B 1 217 ? 35.756  -15.563 32.741 1.00 26.73  ?  242 ARG   B H      1 
ATOM   9829  H  HA     . ARG   B 1 217 ? 34.380  -17.760 33.108 1.00 26.73  ?  242 ARG   B HA     1 
ATOM   9830  H  HB2    . ARG   B 1 217 ? 33.732  -15.943 31.700 1.00 25.99  ?  242 ARG   B HB2    1 
ATOM   9831  H  HB3    . ARG   B 1 217 ? 34.721  -16.536 30.607 1.00 25.99  ?  242 ARG   B HB3    1 
ATOM   9832  H  HG2    . ARG   B 1 217 ? 32.740  -17.293 29.967 1.00 25.18  ?  242 ARG   B HG2    1 
ATOM   9833  H  HG3    . ARG   B 1 217 ? 33.370  -18.538 30.726 1.00 25.18  ?  242 ARG   B HG3    1 
ATOM   9834  H  HD2    . ARG   B 1 217 ? 31.994  -17.976 32.665 1.00 23.87  ?  242 ARG   B HD2    1 
ATOM   9835  H  HD3    . ARG   B 1 217 ? 31.282  -16.862 31.783 1.00 23.87  ?  242 ARG   B HD3    1 
ATOM   9836  H  HE     . ARG   B 1 217 ? 30.434  -18.475 30.488 1.00 23.79  ?  242 ARG   B HE     1 
ATOM   9837  H  HH11   . ARG   B 1 217 ? 32.091  -19.931 32.979 1.00 26.06  ?  242 ARG   B HH11   1 
ATOM   9838  H  HH12   . ARG   B 1 217 ? 31.664  -21.319 32.649 1.00 26.06  ?  242 ARG   B HH12   1 
ATOM   9839  H  HH21   . ARG   B 1 217 ? 29.874  -20.571 29.983 1.00 24.24  ?  242 ARG   B HH21   1 
ATOM   9840  H  HH22   . ARG   B 1 217 ? 30.324  -21.704 30.839 1.00 24.24  ?  242 ARG   B HH22   1 
ATOM   9841  N  N      . ALA   B 1 218 ? 37.088  -18.201 31.471 1.00 24.16  ?  243 ALA   B N      1 
ATOM   9842  C  CA     . ALA   B 1 218 ? 38.006  -19.256 31.040 1.00 26.57  ?  243 ALA   B CA     1 
ATOM   9843  C  C      . ALA   B 1 218 ? 38.450  -20.117 32.218 1.00 25.77  ?  243 ALA   B C      1 
ATOM   9844  O  O      . ALA   B 1 218 ? 38.550  -21.347 32.092 1.00 26.23  ?  243 ALA   B O      1 
ATOM   9845  C  CB     . ALA   B 1 218 ? 39.212  -18.638 30.327 1.00 26.95  ?  243 ALA   B CB     1 
ATOM   9846  H  H      . ALA   B 1 218 ? 37.396  -17.402 31.391 1.00 28.99  ?  243 ALA   B H      1 
ATOM   9847  H  HA     . ALA   B 1 218 ? 37.551  -19.834 30.408 1.00 31.88  ?  243 ALA   B HA     1 
ATOM   9848  H  HB1    . ALA   B 1 218 ? 39.814  -19.347 30.053 1.00 32.34  ?  243 ALA   B HB1    1 
ATOM   9849  H  HB2    . ALA   B 1 218 ? 38.901  -18.149 29.549 1.00 32.34  ?  243 ALA   B HB2    1 
ATOM   9850  H  HB3    . ALA   B 1 218 ? 39.665  -18.036 30.937 1.00 32.34  ?  243 ALA   B HB3    1 
ATOM   9851  N  N      . TYR   B 1 219 ? 38.696  -19.493 33.376 1.00 24.97  ?  244 TYR   B N      1 
ATOM   9852  C  CA     . TYR   B 1 219 ? 38.940  -20.257 34.595 1.00 25.57  ?  244 TYR   B CA     1 
ATOM   9853  C  C      . TYR   B 1 219 ? 37.764  -21.172 34.917 1.00 25.84  ?  244 TYR   B C      1 
ATOM   9854  O  O      . TYR   B 1 219 ? 37.963  -22.325 35.316 1.00 26.18  ?  244 TYR   B O      1 
ATOM   9855  C  CB     . TYR   B 1 219 ? 39.220  -19.312 35.772 1.00 26.98  ?  244 TYR   B CB     1 
ATOM   9856  C  CG     . TYR   B 1 219 ? 40.686  -18.959 35.931 1.00 29.66  ?  244 TYR   B CG     1 
ATOM   9857  C  CD1    . TYR   B 1 219 ? 41.240  -17.883 35.249 1.00 29.90  ?  244 TYR   B CD1    1 
ATOM   9858  C  CD2    . TYR   B 1 219 ? 41.516  -19.707 36.748 1.00 30.92  ?  244 TYR   B CD2    1 
ATOM   9859  C  CE1    . TYR   B 1 219 ? 42.586  -17.556 35.377 1.00 30.26  ?  244 TYR   B CE1    1 
ATOM   9860  C  CE2    . TYR   B 1 219 ? 42.870  -19.388 36.886 1.00 30.38  ?  244 TYR   B CE2    1 
ATOM   9861  C  CZ     . TYR   B 1 219 ? 43.400  -18.305 36.201 1.00 31.19  ?  244 TYR   B CZ     1 
ATOM   9862  O  OH     . TYR   B 1 219 ? 44.740  -17.994 36.333 1.00 33.43  ?  244 TYR   B OH     1 
ATOM   9863  H  H      . TYR   B 1 219 ? 38.725  -18.639 33.477 1.00 29.96  ?  244 TYR   B H      1 
ATOM   9864  H  HA     . TYR   B 1 219 ? 39.727  -20.808 34.461 1.00 30.67  ?  244 TYR   B HA     1 
ATOM   9865  H  HB2    . TYR   B 1 219 ? 38.730  -18.486 35.634 1.00 32.37  ?  244 TYR   B HB2    1 
ATOM   9866  H  HB3    . TYR   B 1 219 ? 38.927  -19.738 36.592 1.00 32.37  ?  244 TYR   B HB3    1 
ATOM   9867  H  HD1    . TYR   B 1 219 ? 40.698  -17.369 34.694 1.00 35.87  ?  244 TYR   B HD1    1 
ATOM   9868  H  HD2    . TYR   B 1 219 ? 41.168  -20.433 37.213 1.00 37.09  ?  244 TYR   B HD2    1 
ATOM   9869  H  HE1    . TYR   B 1 219 ? 42.936  -16.833 34.908 1.00 36.30  ?  244 TYR   B HE1    1 
ATOM   9870  H  HE2    . TYR   B 1 219 ? 43.415  -19.902 37.437 1.00 36.45  ?  244 TYR   B HE2    1 
ATOM   9871  H  HH     . TYR   B 1 219 ? 45.105  -18.518 36.879 1.00 40.11  ?  244 TYR   B HH     1 
ATOM   9872  N  N      . ASP   B 1 220 ? 36.530  -20.675 34.741 1.00 24.16  ?  245 ASP   B N      1 
ATOM   9873  C  CA     . ASP   B 1 220 ? 35.355  -21.504 34.976 1.00 23.11  ?  245 ASP   B CA     1 
ATOM   9874  C  C      . ASP   B 1 220 ? 35.441  -22.797 34.165 1.00 22.88  ?  245 ASP   B C      1 
ATOM   9875  O  O      . ASP   B 1 220 ? 35.160  -23.892 34.661 1.00 22.98  ?  245 ASP   B O      1 
ATOM   9876  C  CB     . ASP   B 1 220 ? 34.061  -20.815 34.529 1.00 21.14  ?  245 ASP   B CB     1 
ATOM   9877  C  CG     . ASP   B 1 220 ? 33.659  -19.582 35.328 1.00 21.48  ?  245 ASP   B CG     1 
ATOM   9878  O  OD1    . ASP   B 1 220 ? 34.272  -19.214 36.366 1.00 21.20  ?  245 ASP   B OD1    1 
ATOM   9879  O  OD2    . ASP   B 1 220 ? 32.643  -18.961 34.934 1.00 22.18  ?  245 ASP   B OD2    1 
ATOM   9880  H  H      . ASP   B 1 220 ? 36.355  -19.871 34.489 1.00 28.99  ?  245 ASP   B H      1 
ATOM   9881  H  HA     . ASP   B 1 220 ? 35.324  -21.666 35.932 1.00 27.72  ?  245 ASP   B HA     1 
ATOM   9882  H  HB2    . ASP   B 1 220 ? 34.167  -20.537 33.606 1.00 25.37  ?  245 ASP   B HB2    1 
ATOM   9883  H  HB3    . ASP   B 1 220 ? 33.335  -21.454 34.602 1.00 25.37  ?  245 ASP   B HB3    1 
ATOM   9884  N  N      . ILE   B 1 221 ? 35.731  -22.656 32.865 1.00 24.06  ?  246 ILE   B N      1 
ATOM   9885  C  CA     . ILE   B 1 221 ? 35.832  -23.803 31.969 1.00 24.47  ?  246 ILE   B CA     1 
ATOM   9886  C  C      . ILE   B 1 221 ? 36.900  -24.767 32.460 1.00 25.53  ?  246 ILE   B C      1 
ATOM   9887  O  O      . ILE   B 1 221 ? 36.709  -25.989 32.444 1.00 27.21  ?  246 ILE   B O      1 
ATOM   9888  C  CB     . ILE   B 1 221 ? 36.123  -23.317 30.535 1.00 25.75  ?  246 ILE   B CB     1 
ATOM   9889  C  CG1    . ILE   B 1 221 ? 34.973  -22.444 30.017 1.00 25.83  ?  246 ILE   B CG1    1 
ATOM   9890  C  CG2    . ILE   B 1 221 ? 36.383  -24.496 29.619 1.00 27.19  ?  246 ILE   B CG2    1 
ATOM   9891  C  CD1    . ILE   B 1 221 ? 33.646  -23.198 29.816 1.00 26.31  ?  246 ILE   B CD1    1 
ATOM   9892  H  H      . ILE   B 1 221 ? 35.873  -21.901 32.479 1.00 28.86  ?  246 ILE   B H      1 
ATOM   9893  H  HA     . ILE   B 1 221 ? 34.986  -24.277 31.966 1.00 29.36  ?  246 ILE   B HA     1 
ATOM   9894  H  HB     . ILE   B 1 221 ? 36.923  -22.769 30.550 1.00 30.90  ?  246 ILE   B HB     1 
ATOM   9895  H  HG12   . ILE   B 1 221 ? 34.813  -21.733 30.656 1.00 30.99  ?  246 ILE   B HG12   1 
ATOM   9896  H  HG13   . ILE   B 1 221 ? 35.231  -22.069 29.161 1.00 30.99  ?  246 ILE   B HG13   1 
ATOM   9897  H  HG21   . ILE   B 1 221 ? 36.274  -24.211 28.698 1.00 32.63  ?  246 ILE   B HG21   1 
ATOM   9898  H  HG22   . ILE   B 1 221 ? 37.289  -24.813 29.762 1.00 32.63  ?  246 ILE   B HG22   1 
ATOM   9899  H  HG23   . ILE   B 1 221 ? 35.750  -25.201 29.824 1.00 32.63  ?  246 ILE   B HG23   1 
ATOM   9900  H  HD11   . ILE   B 1 221 ? 32.979  -22.578 29.482 1.00 31.56  ?  246 ILE   B HD11   1 
ATOM   9901  H  HD12   . ILE   B 1 221 ? 33.784  -23.913 29.175 1.00 31.56  ?  246 ILE   B HD12   1 
ATOM   9902  H  HD13   . ILE   B 1 221 ? 33.360  -23.566 30.666 1.00 31.56  ?  246 ILE   B HD13   1 
ATOM   9903  N  N      . ALA   B 1 222 ? 38.049  -24.235 32.884 1.00 26.01  ?  247 ALA   B N      1 
ATOM   9904  C  CA     . ALA   B 1 222 ? 39.112  -25.084 33.414 1.00 27.64  ?  247 ALA   B CA     1 
ATOM   9905  C  C      . ALA   B 1 222 ? 38.641  -25.853 34.642 1.00 29.09  ?  247 ALA   B C      1 
ATOM   9906  O  O      . ALA   B 1 222 ? 39.029  -27.013 34.838 1.00 31.11  ?  247 ALA   B O      1 
ATOM   9907  C  CB     . ALA   B 1 222 ? 40.333  -24.222 33.738 1.00 28.15  ?  247 ALA   B CB     1 
ATOM   9908  H  H      . ALA   B 1 222 ? 38.235  -23.395 32.875 1.00 31.20  ?  247 ALA   B H      1 
ATOM   9909  H  HA     . ALA   B 1 222 ? 39.376  -25.736 32.746 1.00 33.16  ?  247 ALA   B HA     1 
ATOM   9910  H  HB1    . ALA   B 1 222 ? 41.043  -24.792 34.073 1.00 33.77  ?  247 ALA   B HB1    1 
ATOM   9911  H  HB2    . ALA   B 1 222 ? 40.625  -23.771 32.930 1.00 33.77  ?  247 ALA   B HB2    1 
ATOM   9912  H  HB3    . ALA   B 1 222 ? 40.088  -23.568 34.411 1.00 33.77  ?  247 ALA   B HB3    1 
ATOM   9913  N  N      . GLY   B 1 223 ? 37.770  -25.239 35.455 1.00 27.80  ?  248 GLY   B N      1 
ATOM   9914  C  CA     . GLY   B 1 223 ? 37.303  -25.903 36.662 1.00 28.54  ?  248 GLY   B CA     1 
ATOM   9915  C  C      . GLY   B 1 223 ? 36.127  -26.837 36.477 1.00 27.00  ?  248 GLY   B C      1 
ATOM   9916  O  O      . GLY   B 1 223 ? 35.944  -27.761 37.275 1.00 29.24  ?  248 GLY   B O      1 
ATOM   9917  H  H      . GLY   B 1 223 ? 37.445  -24.453 35.327 1.00 33.35  ?  248 GLY   B H      1 
ATOM   9918  H  HA2    . GLY   B 1 223 ? 38.034  -26.422 37.031 1.00 34.24  ?  248 GLY   B HA2    1 
ATOM   9919  H  HA3    . GLY   B 1 223 ? 37.041  -25.225 37.305 1.00 34.24  ?  248 GLY   B HA3    1 
ATOM   9920  N  N      . SER   B 1 224 ? 35.303  -26.621 35.448 1.00 24.99  ?  249 SER   B N      1 
ATOM   9921  C  CA     . SER   B 1 224 ? 34.071  -27.389 35.284 1.00 25.09  ?  249 SER   B CA     1 
ATOM   9922  C  C      . SER   B 1 224 ? 34.218  -28.565 34.329 1.00 27.26  ?  249 SER   B C      1 
ATOM   9923  O  O      . SER   B 1 224 ? 33.447  -29.528 34.430 1.00 26.96  ?  249 SER   B O      1 
ATOM   9924  C  CB     . SER   B 1 224 ? 32.939  -26.478 34.787 1.00 25.18  ?  249 SER   B CB     1 
ATOM   9925  O  OG     . SER   B 1 224 ? 33.171  -26.020 33.466 1.00 25.26  ?  249 SER   B OG     1 
ATOM   9926  H  H      . SER   B 1 224 ? 35.438  -26.035 34.833 1.00 29.99  ?  249 SER   B H      1 
ATOM   9927  H  HA     . SER   B 1 224 ? 33.808  -27.742 36.148 1.00 30.10  ?  249 SER   B HA     1 
ATOM   9928  H  HB2    . SER   B 1 224 ? 32.107  -26.977 34.802 1.00 30.21  ?  249 SER   B HB2    1 
ATOM   9929  H  HB3    . SER   B 1 224 ? 32.875  -25.710 35.376 1.00 30.21  ?  249 SER   B HB3    1 
ATOM   9930  H  HG     . SER   B 1 224 ? 33.887  -25.582 33.435 1.00 30.31  ?  249 SER   B HG     1 
ATOM   9931  N  N      . THR   B 1 225 ? 35.185  -28.512 33.423 1.00 29.47  ?  250 THR   B N      1 
ATOM   9932  C  CA     . THR   B 1 225 ? 35.448  -29.619 32.519 1.00 30.84  ?  250 THR   B CA     1 
ATOM   9933  C  C      . THR   B 1 225 ? 36.393  -30.629 33.168 1.00 32.35  ?  250 THR   B C      1 
ATOM   9934  O  O      . THR   B 1 225 ? 37.062  -30.350 34.163 1.00 34.05  ?  250 THR   B O      1 
ATOM   9935  C  CB     . THR   B 1 225 ? 36.072  -29.125 31.211 1.00 31.93  ?  250 THR   B CB     1 
ATOM   9936  O  OG1    . THR   B 1 225 ? 37.332  -28.501 31.489 1.00 32.06  ?  250 THR   B OG1    1 
ATOM   9937  C  CG2    . THR   B 1 225 ? 35.160  -28.143 30.526 1.00 31.28  ?  250 THR   B CG2    1 
ATOM   9938  H  H      . THR   B 1 225 ? 35.708  -27.838 33.311 1.00 35.35  ?  250 THR   B H      1 
ATOM   9939  H  HA     . THR   B 1 225 ? 34.608  -30.057 32.313 1.00 37.00  ?  250 THR   B HA     1 
ATOM   9940  H  HB     . THR   B 1 225 ? 36.209  -29.875 30.613 1.00 38.30  ?  250 THR   B HB     1 
ATOM   9941  H  HG1    . THR   B 1 225 ? 37.219  -27.836 31.991 1.00 38.47  ?  250 THR   B HG1    1 
ATOM   9942  H  HG21   . THR   B 1 225 ? 35.536  -27.883 29.670 1.00 37.53  ?  250 THR   B HG21   1 
ATOM   9943  H  HG22   . THR   B 1 225 ? 34.290  -28.545 30.378 1.00 37.53  ?  250 THR   B HG22   1 
ATOM   9944  H  HG23   . THR   B 1 225 ? 35.051  -27.351 31.075 1.00 37.53  ?  250 THR   B HG23   1 
ATOM   9945  N  N      . LYS   B 1 226 ? 36.431  -31.819 32.593 1.00 34.25  ?  251 LYS   B N      1 
ATOM   9946  C  CA     A LYS   B 1 226 ? 37.337  -32.879 33.013 0.48 36.95  ?  251 LYS   B CA     1 
ATOM   9947  C  CA     B LYS   B 1 226 ? 37.343  -32.875 33.013 0.52 36.81  ?  251 LYS   B CA     1 
ATOM   9948  C  C      . LYS   B 1 226 ? 38.348  -33.117 31.901 1.00 37.99  ?  251 LYS   B C      1 
ATOM   9949  O  O      . LYS   B 1 226 ? 37.971  -33.218 30.730 1.00 39.20  ?  251 LYS   B O      1 
ATOM   9950  C  CB     A LYS   B 1 226 ? 36.547  -34.149 33.324 0.48 37.66  ?  251 LYS   B CB     1 
ATOM   9951  C  CB     B LYS   B 1 226 ? 36.591  -34.161 33.340 0.52 37.25  ?  251 LYS   B CB     1 
ATOM   9952  C  CG     A LYS   B 1 226 ? 37.360  -35.348 33.777 0.48 38.56  ?  251 LYS   B CG     1 
ATOM   9953  C  CG     B LYS   B 1 226 ? 35.573  -34.013 34.459 0.52 38.12  ?  251 LYS   B CG     1 
ATOM   9954  C  CD     A LYS   B 1 226 ? 36.513  -36.620 33.674 0.48 40.01  ?  251 LYS   B CD     1 
ATOM   9955  C  CD     B LYS   B 1 226 ? 36.225  -33.585 35.767 0.52 38.71  ?  251 LYS   B CD     1 
ATOM   9956  C  CE     A LYS   B 1 226 ? 37.312  -37.873 34.008 0.48 41.33  ?  251 LYS   B CE     1 
ATOM   9957  C  CE     B LYS   B 1 226 ? 35.173  -33.271 36.826 0.52 38.55  ?  251 LYS   B CE     1 
ATOM   9958  N  NZ     A LYS   B 1 226 ? 37.515  -38.041 35.475 0.48 42.68  ?  251 LYS   B NZ     1 
ATOM   9959  N  NZ     B LYS   B 1 226 ? 34.133  -32.346 36.316 0.52 36.18  ?  251 LYS   B NZ     1 
ATOM   9960  H  H      . LYS   B 1 226 ? 35.922  -32.045 31.938 1.00 41.09  ?  251 LYS   B H      1 
ATOM   9961  H  HA     . LYS   B 1 226 ? 37.824  -32.626 33.813 1.00 44.16  ?  251 LYS   B HA     1 
ATOM   9962  H  HB2    A LYS   B 1 226 ? 35.916  -33.947 34.033 0.48 45.18  ?  251 LYS   B HB2    1 
ATOM   9963  H  HB2    B LYS   B 1 226 ? 36.116  -34.454 32.546 0.52 44.70  ?  251 LYS   B HB2    1 
ATOM   9964  H  HB3    A LYS   B 1 226 ? 36.071  -34.414 32.521 0.48 45.18  ?  251 LYS   B HB3    1 
ATOM   9965  H  HB3    B LYS   B 1 226 ? 37.232  -34.836 33.611 0.52 44.70  ?  251 LYS   B HB3    1 
ATOM   9966  H  HG2    A LYS   B 1 226 ? 38.142  -35.447 33.211 0.48 46.27  ?  251 LYS   B HG2    1 
ATOM   9967  H  HG2    B LYS   B 1 226 ? 34.921  -33.340 34.210 0.52 45.73  ?  251 LYS   B HG2    1 
ATOM   9968  H  HG3    A LYS   B 1 226 ? 37.633  -35.228 34.701 0.48 46.27  ?  251 LYS   B HG3    1 
ATOM   9969  H  HG3    B LYS   B 1 226 ? 35.133  -34.865 34.604 0.52 45.73  ?  251 LYS   B HG3    1 
ATOM   9970  H  HD2    A LYS   B 1 226 ? 35.771  -36.560 34.296 0.48 48.01  ?  251 LYS   B HD2    1 
ATOM   9971  H  HD2    B LYS   B 1 226 ? 36.788  -34.302 36.098 0.52 46.44  ?  251 LYS   B HD2    1 
ATOM   9972  H  HD3    A LYS   B 1 226 ? 36.179  -36.707 32.768 0.48 48.01  ?  251 LYS   B HD3    1 
ATOM   9973  H  HD3    B LYS   B 1 226 ? 36.757  -32.788 35.617 0.52 46.44  ?  251 LYS   B HD3    1 
ATOM   9974  H  HE2    A LYS   B 1 226 ? 36.835  -38.651 33.679 0.48 49.59  ?  251 LYS   B HE2    1 
ATOM   9975  H  HE2    B LYS   B 1 226 ? 34.739  -34.094 37.100 0.52 46.26  ?  251 LYS   B HE2    1 
ATOM   9976  H  HE3    A LYS   B 1 226 ? 38.184  -37.816 33.587 0.48 49.59  ?  251 LYS   B HE3    1 
ATOM   9977  H  HE3    B LYS   B 1 226 ? 35.603  -32.853 37.589 0.52 46.26  ?  251 LYS   B HE3    1 
ATOM   9978  H  HZ1    A LYS   B 1 226 ? 37.979  -38.784 35.635 0.48 51.21  ?  251 LYS   B HZ1    1 
ATOM   9979  H  HZ1    B LYS   B 1 226 ? 33.642  -32.038 36.991 0.52 43.41  ?  251 LYS   B HZ1    1 
ATOM   9980  H  HZ2    A LYS   B 1 226 ? 37.963  -37.345 35.801 0.48 51.21  ?  251 LYS   B HZ2    1 
ATOM   9981  H  HZ2    B LYS   B 1 226 ? 34.515  -31.659 35.899 0.52 43.41  ?  251 LYS   B HZ2    1 
ATOM   9982  H  HZ3    A LYS   B 1 226 ? 36.728  -38.097 35.887 0.48 51.21  ?  251 LYS   B HZ3    1 
ATOM   9983  H  HZ3    B LYS   B 1 226 ? 33.601  -32.772 35.743 0.52 43.41  ?  251 LYS   B HZ3    1 
ATOM   9984  N  N      . ASP   B 1 227 ? 39.627  -33.179 32.269 1.00 40.16  ?  252 ASP   B N      1 
ATOM   9985  C  CA     . ASP   B 1 227 ? 40.698  -33.545 31.342 1.00 42.29  ?  252 ASP   B CA     1 
ATOM   9986  C  C      . ASP   B 1 227 ? 40.778  -32.612 30.136 1.00 40.84  ?  252 ASP   B C      1 
ATOM   9987  O  O      . ASP   B 1 227 ? 40.998  -33.049 29.004 1.00 41.90  ?  252 ASP   B O      1 
ATOM   9988  C  CB     . ASP   B 1 227 ? 40.525  -34.994 30.883 1.00 45.79  ?  252 ASP   B CB     1 
ATOM   9989  C  CG     . ASP   B 1 227 ? 40.546  -35.972 32.033 1.00 49.42  ?  252 ASP   B CG     1 
ATOM   9990  O  OD1    . ASP   B 1 227 ? 41.356  -35.774 32.963 1.00 49.87  ?  252 ASP   B OD1    1 
ATOM   9991  O  OD2    . ASP   B 1 227 ? 39.747  -36.931 32.014 1.00 51.89  ?  252 ASP   B OD2    1 
ATOM   9992  H  H      . ASP   B 1 227 ? 39.906  -33.011 33.065 1.00 48.18  ?  252 ASP   B H      1 
ATOM   9993  H  HA     . ASP   B 1 227 ? 41.541  -33.453 31.813 1.00 50.74  ?  252 ASP   B HA     1 
ATOM   9994  H  HB2    . ASP   B 1 227 ? 39.673  -35.083 30.428 1.00 54.94  ?  252 ASP   B HB2    1 
ATOM   9995  H  HB3    . ASP   B 1 227 ? 41.249  -35.224 30.279 1.00 54.94  ?  252 ASP   B HB3    1 
ATOM   9996  N  N      . VAL   B 1 228 ? 40.625  -31.316 30.380 1.00 38.62  ?  253 VAL   B N      1 
ATOM   9997  C  CA     . VAL   B 1 228 ? 40.824  -30.294 29.360 1.00 37.35  ?  253 VAL   B CA     1 
ATOM   9998  C  C      . VAL   B 1 228 ? 41.734  -29.232 29.961 1.00 36.97  ?  253 VAL   B C      1 
ATOM   9999  O  O      . VAL   B 1 228 ? 41.407  -28.647 30.999 1.00 38.86  ?  253 VAL   B O      1 
ATOM   10000 C  CB     . VAL   B 1 228 ? 39.497  -29.673 28.891 1.00 37.40  ?  253 VAL   B CB     1 
ATOM   10001 C  CG1    . VAL   B 1 228 ? 39.759  -28.529 27.920 1.00 38.75  ?  253 VAL   B CG1    1 
ATOM   10002 C  CG2    . VAL   B 1 228 ? 38.615  -30.733 28.237 1.00 37.74  ?  253 VAL   B CG2    1 
ATOM   10003 H  H      . VAL   B 1 228 ? 40.401  -30.997 31.146 1.00 46.34  ?  253 VAL   B H      1 
ATOM   10004 H  HA     . VAL   B 1 228 ? 41.261  -30.683 28.587 1.00 44.81  ?  253 VAL   B HA     1 
ATOM   10005 H  HB     . VAL   B 1 228 ? 39.027  -29.317 29.661 1.00 44.88  ?  253 VAL   B HB     1 
ATOM   10006 H  HG11   . VAL   B 1 228 ? 38.934  -28.311 27.459 1.00 46.49  ?  253 VAL   B HG11   1 
ATOM   10007 H  HG12   . VAL   B 1 228 ? 40.073  -27.758 28.418 1.00 46.49  ?  253 VAL   B HG12   1 
ATOM   10008 H  HG13   . VAL   B 1 228 ? 40.432  -28.806 27.280 1.00 46.49  ?  253 VAL   B HG13   1 
ATOM   10009 H  HG21   . VAL   B 1 228 ? 37.791  -30.318 27.936 1.00 45.28  ?  253 VAL   B HG21   1 
ATOM   10010 H  HG22   . VAL   B 1 228 ? 39.088  -31.115 27.481 1.00 45.28  ?  253 VAL   B HG22   1 
ATOM   10011 H  HG23   . VAL   B 1 228 ? 38.418  -31.425 28.887 1.00 45.28  ?  253 VAL   B HG23   1 
ATOM   10012 N  N      . LYS   B 1 229 ? 42.881  -28.999 29.337 1.00 37.99  ?  254 LYS   B N      1 
ATOM   10013 C  CA     . LYS   B 1 229 ? 43.744  -27.890 29.721 1.00 38.50  ?  254 LYS   B CA     1 
ATOM   10014 C  C      . LYS   B 1 229 ? 43.289  -26.624 29.003 1.00 38.58  ?  254 LYS   B C      1 
ATOM   10015 O  O      . LYS   B 1 229 ? 42.973  -26.655 27.811 1.00 39.91  ?  254 LYS   B O      1 
ATOM   10016 C  CB     . LYS   B 1 229 ? 45.207  -28.187 29.399 1.00 42.33  ?  254 LYS   B CB     1 
ATOM   10017 C  CG     . LYS   B 1 229 ? 45.844  -29.166 30.366 1.00 45.87  ?  254 LYS   B CG     1 
ATOM   10018 C  CD     . LYS   B 1 229 ? 46.056  -30.518 29.723 1.00 50.15  ?  254 LYS   B CD     1 
ATOM   10019 C  CE     . LYS   B 1 229 ? 47.210  -30.498 28.738 1.00 52.44  ?  254 LYS   B CE     1 
ATOM   10020 N  NZ     . LYS   B 1 229 ? 47.394  -31.840 28.103 1.00 54.63  ?  254 LYS   B NZ     1 
ATOM   10021 H  H      . LYS   B 1 229 ? 43.183  -29.471 28.684 1.00 45.58  ?  254 LYS   B H      1 
ATOM   10022 H  HA     . LYS   B 1 229 ? 43.685  -27.747 30.678 1.00 46.19  ?  254 LYS   B HA     1 
ATOM   10023 H  HB2    . LYS   B 1 229 ? 45.262  -28.568 28.508 1.00 50.78  ?  254 LYS   B HB2    1 
ATOM   10024 H  HB3    . LYS   B 1 229 ? 45.712  -27.359 29.436 1.00 50.78  ?  254 LYS   B HB3    1 
ATOM   10025 H  HG2    . LYS   B 1 229 ? 46.707  -28.825 30.649 1.00 55.04  ?  254 LYS   B HG2    1 
ATOM   10026 H  HG3    . LYS   B 1 229 ? 45.265  -29.282 31.136 1.00 55.04  ?  254 LYS   B HG3    1 
ATOM   10027 H  HD2    . LYS   B 1 229 ? 46.254  -31.172 30.411 1.00 60.18  ?  254 LYS   B HD2    1 
ATOM   10028 H  HD3    . LYS   B 1 229 ? 45.252  -30.773 29.244 1.00 60.18  ?  254 LYS   B HD3    1 
ATOM   10029 H  HE2    . LYS   B 1 229 ? 47.028  -29.850 28.039 1.00 62.92  ?  254 LYS   B HE2    1 
ATOM   10030 H  HE3    . LYS   B 1 229 ? 48.028  -30.263 29.203 1.00 62.92  ?  254 LYS   B HE3    1 
ATOM   10031 H  HZ1    . LYS   B 1 229 ? 48.074  -31.815 27.529 1.00 65.55  ?  254 LYS   B HZ1    1 
ATOM   10032 H  HZ2    . LYS   B 1 229 ? 47.565  -32.451 28.727 1.00 65.55  ?  254 LYS   B HZ2    1 
ATOM   10033 H  HZ3    . LYS   B 1 229 ? 46.655  -32.073 27.665 1.00 65.55  ?  254 LYS   B HZ3    1 
ATOM   10034 N  N      . VAL   B 1 230 ? 43.245  -25.515 29.736 1.00 36.63  ?  255 VAL   B N      1 
ATOM   10035 C  CA     . VAL   B 1 230 ? 42.761  -24.244 29.211 1.00 34.99  ?  255 VAL   B CA     1 
ATOM   10036 C  C      . VAL   B 1 230 ? 43.906  -23.240 29.248 1.00 36.04  ?  255 VAL   B C      1 
ATOM   10037 O  O      . VAL   B 1 230 ? 44.596  -23.113 30.267 1.00 36.76  ?  255 VAL   B O      1 
ATOM   10038 C  CB     . VAL   B 1 230 ? 41.542  -23.736 30.005 1.00 34.98  ?  255 VAL   B CB     1 
ATOM   10039 C  CG1    . VAL   B 1 230 ? 41.057  -22.411 29.447 1.00 35.55  ?  255 VAL   B CG1    1 
ATOM   10040 C  CG2    . VAL   B 1 230 ? 40.410  -24.779 29.969 1.00 35.80  ?  255 VAL   B CG2    1 
ATOM   10041 H  H      . VAL   B 1 230 ? 43.497  -25.475 30.558 1.00 43.95  ?  255 VAL   B H      1 
ATOM   10042 H  HA     . VAL   B 1 230 ? 42.494  -24.355 28.285 1.00 41.99  ?  255 VAL   B HA     1 
ATOM   10043 H  HB     . VAL   B 1 230 ? 41.804  -23.597 30.928 1.00 41.97  ?  255 VAL   B HB     1 
ATOM   10044 H  HG11   . VAL   B 1 230 ? 40.195  -22.200 29.839 1.00 42.65  ?  255 VAL   B HG11   1 
ATOM   10045 H  HG12   . VAL   B 1 230 ? 41.700  -21.720 29.671 1.00 42.65  ?  255 VAL   B HG12   1 
ATOM   10046 H  HG13   . VAL   B 1 230 ? 40.973  -22.486 28.484 1.00 42.65  ?  255 VAL   B HG13   1 
ATOM   10047 H  HG21   . VAL   B 1 230 ? 39.637  -24.422 30.432 1.00 42.95  ?  255 VAL   B HG21   1 
ATOM   10048 H  HG22   . VAL   B 1 230 ? 40.185  -24.968 29.045 1.00 42.95  ?  255 VAL   B HG22   1 
ATOM   10049 H  HG23   . VAL   B 1 230 ? 40.714  -25.589 30.408 1.00 42.95  ?  255 VAL   B HG23   1 
ATOM   10050 N  N      . PHE   B 1 231 ? 44.101  -22.532 28.138 1.00 36.16  ?  256 PHE   B N      1 
ATOM   10051 C  CA     . PHE   B 1 231 ? 45.121  -21.501 28.016 1.00 37.11  ?  256 PHE   B CA     1 
ATOM   10052 C  C      . PHE   B 1 231 ? 44.478  -20.167 27.649 1.00 36.81  ?  256 PHE   B C      1 
ATOM   10053 O  O      . PHE   B 1 231 ? 43.492  -20.122 26.905 1.00 36.77  ?  256 PHE   B O      1 
ATOM   10054 C  CB     . PHE   B 1 231 ? 46.156  -21.883 26.948 1.00 38.02  ?  256 PHE   B CB     1 
ATOM   10055 C  CG     . PHE   B 1 231 ? 46.873  -23.186 27.214 1.00 39.81  ?  256 PHE   B CG     1 
ATOM   10056 C  CD1    . PHE   B 1 231 ? 46.241  -24.401 27.000 1.00 39.72  ?  256 PHE   B CD1    1 
ATOM   10057 C  CD2    . PHE   B 1 231 ? 48.188  -23.194 27.652 1.00 41.00  ?  256 PHE   B CD2    1 
ATOM   10058 C  CE1    . PHE   B 1 231 ? 46.903  -25.603 27.236 1.00 39.80  ?  256 PHE   B CE1    1 
ATOM   10059 C  CE2    . PHE   B 1 231 ? 48.858  -24.388 27.890 1.00 41.12  ?  256 PHE   B CE2    1 
ATOM   10060 C  CZ     . PHE   B 1 231 ? 48.213  -25.597 27.680 1.00 40.85  ?  256 PHE   B CZ     1 
ATOM   10061 H  H      . PHE   B 1 231 ? 43.638  -22.637 27.420 1.00 43.39  ?  256 PHE   B H      1 
ATOM   10062 H  HA     . PHE   B 1 231 ? 45.573  -21.395 28.868 1.00 44.53  ?  256 PHE   B HA     1 
ATOM   10063 H  HB2    . PHE   B 1 231 ? 45.704  -21.965 26.093 1.00 45.61  ?  256 PHE   B HB2    1 
ATOM   10064 H  HB3    . PHE   B 1 231 ? 46.826  -21.183 26.902 1.00 45.61  ?  256 PHE   B HB3    1 
ATOM   10065 H  HD1    . PHE   B 1 231 ? 45.363  -24.413 26.694 1.00 47.66  ?  256 PHE   B HD1    1 
ATOM   10066 H  HD2    . PHE   B 1 231 ? 48.630  -22.387 27.789 1.00 49.19  ?  256 PHE   B HD2    1 
ATOM   10067 H  HE1    . PHE   B 1 231 ? 46.464  -26.411 27.094 1.00 47.75  ?  256 PHE   B HE1    1 
ATOM   10068 H  HE2    . PHE   B 1 231 ? 49.738  -24.376 28.189 1.00 49.33  ?  256 PHE   B HE2    1 
ATOM   10069 H  HZ     . PHE   B 1 231 ? 48.658  -26.399 27.837 1.00 49.02  ?  256 PHE   B HZ     1 
ATOM   10070 N  N      . LEU   B 1 232 ? 45.042  -19.082 28.177 1.00 35.68  ?  257 LEU   B N      1 
ATOM   10071 C  CA     . LEU   B 1 232 ? 44.593  -17.720 27.891 1.00 36.07  ?  257 LEU   B CA     1 
ATOM   10072 C  C      . LEU   B 1 232 ? 45.824  -16.931 27.463 1.00 36.94  ?  257 LEU   B C      1 
ATOM   10073 O  O      . LEU   B 1 232 ? 46.730  -16.706 28.272 1.00 38.52  ?  257 LEU   B O      1 
ATOM   10074 C  CB     . LEU   B 1 232 ? 43.927  -17.097 29.116 1.00 35.47  ?  257 LEU   B CB     1 
ATOM   10075 C  CG     . LEU   B 1 232 ? 43.098  -15.810 29.014 1.00 34.72  ?  257 LEU   B CG     1 
ATOM   10076 C  CD1    . LEU   B 1 232 ? 43.933  -14.625 28.553 1.00 35.42  ?  257 LEU   B CD1    1 
ATOM   10077 C  CD2    . LEU   B 1 232 ? 41.878  -16.024 28.106 1.00 35.84  ?  257 LEU   B CD2    1 
ATOM   10078 H  H      . LEU   B 1 232 ? 45.708  -19.110 28.720 1.00 42.81  ?  257 LEU   B H      1 
ATOM   10079 H  HA     . LEU   B 1 232 ? 43.947  -17.715 27.168 1.00 43.27  ?  257 LEU   B HA     1 
ATOM   10080 H  HB2    . LEU   B 1 232 ? 43.327  -17.767 29.480 1.00 42.56  ?  257 LEU   B HB2    1 
ATOM   10081 H  HB3    . LEU   B 1 232 ? 44.633  -16.904 29.752 1.00 42.56  ?  257 LEU   B HB3    1 
ATOM   10082 H  HG     . LEU   B 1 232 ? 42.776  -15.587 29.901 1.00 41.65  ?  257 LEU   B HG     1 
ATOM   10083 H  HD11   . LEU   B 1 232 ? 43.388  -13.823 28.586 1.00 42.50  ?  257 LEU   B HD11   1 
ATOM   10084 H  HD12   . LEU   B 1 232 ? 44.698  -14.529 29.142 1.00 42.50  ?  257 LEU   B HD12   1 
ATOM   10085 H  HD13   . LEU   B 1 232 ? 44.232  -14.784 27.644 1.00 42.50  ?  257 LEU   B HD13   1 
ATOM   10086 H  HD21   . LEU   B 1 232 ? 41.361  -15.204 28.073 1.00 43.00  ?  257 LEU   B HD21   1 
ATOM   10087 H  HD22   . LEU   B 1 232 ? 42.184  -16.259 27.216 1.00 43.00  ?  257 LEU   B HD22   1 
ATOM   10088 H  HD23   . LEU   B 1 232 ? 41.336  -16.742 28.469 1.00 43.00  ?  257 LEU   B HD23   1 
ATOM   10089 N  N      . ASN   B 1 233 ? 45.858  -16.503 26.198 1.00 36.38  ?  258 ASN   B N      1 
ATOM   10090 C  CA     . ASN   B 1 233 ? 47.029  -15.823 25.633 1.00 37.41  ?  258 ASN   B CA     1 
ATOM   10091 C  C      . ASN   B 1 233 ? 48.302  -16.618 25.915 1.00 38.69  ?  258 ASN   B C      1 
ATOM   10092 O  O      . ASN   B 1 233 ? 49.355  -16.064 26.243 1.00 37.85  ?  258 ASN   B O      1 
ATOM   10093 C  CB     . ASN   B 1 233 ? 47.146  -14.393 26.162 1.00 37.91  ?  258 ASN   B CB     1 
ATOM   10094 C  CG     . ASN   B 1 233 ? 46.087  -13.476 25.588 1.00 39.09  ?  258 ASN   B CG     1 
ATOM   10095 O  OD1    . ASN   B 1 233 ? 45.267  -13.888 24.773 1.00 40.48  ?  258 ASN   B OD1    1 
ATOM   10096 N  ND2    . ASN   B 1 233 ? 46.092  -12.227 26.022 1.00 40.15  ?  258 ASN   B ND2    1 
ATOM   10097 H  H      . ASN   B 1 233 ? 45.210  -16.596 25.641 1.00 43.65  ?  258 ASN   B H      1 
ATOM   10098 H  HA     . ASN   B 1 233 ? 46.920  -15.770 24.671 1.00 44.89  ?  258 ASN   B HA     1 
ATOM   10099 H  HB2    . ASN   B 1 233 ? 47.045  -14.402 27.127 1.00 45.49  ?  258 ASN   B HB2    1 
ATOM   10100 H  HB3    . ASN   B 1 233 ? 48.015  -14.036 25.922 1.00 45.49  ?  258 ASN   B HB3    1 
ATOM   10101 H  HD21   . ASN   B 1 233 ? 45.511  -11.666 25.726 1.00 48.17  ?  258 ASN   B HD21   1 
ATOM   10102 H  HD22   . ASN   B 1 233 ? 46.677  -11.975 26.600 1.00 48.17  ?  258 ASN   B HD22   1 
ATOM   10103 N  N      . GLY   B 1 234 ? 48.194  -17.941 25.770 1.00 39.51  ?  259 GLY   B N      1 
ATOM   10104 C  CA     . GLY   B 1 234 ? 49.306  -18.847 25.943 1.00 39.77  ?  259 GLY   B CA     1 
ATOM   10105 C  C      . GLY   B 1 234 ? 49.583  -19.242 27.373 1.00 40.13  ?  259 GLY   B C      1 
ATOM   10106 O  O      . GLY   B 1 234 ? 50.420  -20.123 27.605 1.00 40.80  ?  259 GLY   B O      1 
ATOM   10107 H  H      . GLY   B 1 234 ? 47.460  -18.340 25.566 1.00 47.41  ?  259 GLY   B H      1 
ATOM   10108 H  HA2    . GLY   B 1 234 ? 49.127  -19.657 25.441 1.00 47.72  ?  259 GLY   B HA2    1 
ATOM   10109 H  HA3    . GLY   B 1 234 ? 50.106  -18.427 25.591 1.00 47.72  ?  259 GLY   B HA3    1 
ATOM   10110 N  N      . ASN   B 1 235 ? 48.905  -18.627 28.337 1.00 39.84  ?  260 ASN   B N      1 
ATOM   10111 C  CA     . ASN   B 1 235 ? 49.162  -18.852 29.754 1.00 40.33  ?  260 ASN   B CA     1 
ATOM   10112 C  C      . ASN   B 1 235 ? 48.243  -19.971 30.238 1.00 41.25  ?  260 ASN   B C      1 
ATOM   10113 O  O      . ASN   B 1 235 ? 47.021  -19.817 30.258 1.00 40.32  ?  260 ASN   B O      1 
ATOM   10114 C  CB     . ASN   B 1 235 ? 48.930  -17.570 30.551 1.00 40.35  ?  260 ASN   B CB     1 
ATOM   10115 C  CG     . ASN   B 1 235 ? 49.805  -16.420 30.076 1.00 40.61  ?  260 ASN   B CG     1 
ATOM   10116 O  OD1    . ASN   B 1 235 ? 51.006  -16.583 29.875 1.00 39.83  ?  260 ASN   B OD1    1 
ATOM   10117 N  ND2    . ASN   B 1 235 ? 49.205  -15.248 29.897 1.00 41.15  ?  260 ASN   B ND2    1 
ATOM   10118 H  H      . ASN   B 1 235 ? 48.274  -18.061 28.191 1.00 47.80  ?  260 ASN   B H      1 
ATOM   10119 H  HA     . ASN   B 1 235 ? 50.083  -19.129 29.879 1.00 48.39  ?  260 ASN   B HA     1 
ATOM   10120 H  HB2    . ASN   B 1 235 ? 48.003  -17.301 30.456 1.00 48.41  ?  260 ASN   B HB2    1 
ATOM   10121 H  HB3    . ASN   B 1 235 ? 49.133  -17.736 31.485 1.00 48.41  ?  260 ASN   B HB3    1 
ATOM   10122 H  HD21   . ASN   B 1 235 ? 49.659  -14.569 29.629 1.00 49.37  ?  260 ASN   B HD21   1 
ATOM   10123 H  HD22   . ASN   B 1 235 ? 48.362  -15.169 30.049 1.00 49.37  ?  260 ASN   B HD22   1 
ATOM   10124 N  N      . LYS   B 1 236 ? 48.828  -21.097 30.623 1.00 43.11  ?  261 LYS   B N      1 
ATOM   10125 C  CA     . LYS   B 1 236 ? 48.049  -22.203 31.161 1.00 46.10  ?  261 LYS   B CA     1 
ATOM   10126 C  C      . LYS   B 1 236 ? 47.340  -21.780 32.442 1.00 44.63  ?  261 LYS   B C      1 
ATOM   10127 O  O      . LYS   B 1 236 ? 47.946  -21.178 33.329 1.00 46.55  ?  261 LYS   B O      1 
ATOM   10128 C  CB     . LYS   B 1 236 ? 48.992  -23.381 31.413 1.00 49.39  ?  261 LYS   B CB     1 
ATOM   10129 C  CG     . LYS   B 1 236 ? 48.439  -24.469 32.294 1.00 51.30  ?  261 LYS   B CG     1 
ATOM   10130 C  CD     . LYS   B 1 236 ? 47.232  -25.123 31.664 1.00 51.51  ?  261 LYS   B CD     1 
ATOM   10131 C  CE     . LYS   B 1 236 ? 47.020  -26.513 32.228 1.00 52.90  ?  261 LYS   B CE     1 
ATOM   10132 N  NZ     . LYS   B 1 236 ? 48.224  -27.351 32.001 1.00 53.84  ?  261 LYS   B NZ     1 
ATOM   10133 H  H      . LYS   B 1 236 ? 49.674  -21.247 30.583 1.00 51.72  ?  261 LYS   B H      1 
ATOM   10134 H  HA     . LYS   B 1 236 ? 47.365  -22.481 30.533 1.00 55.32  ?  261 LYS   B HA     1 
ATOM   10135 H  HB2    . LYS   B 1 236 ? 49.213  -23.784 30.558 1.00 59.26  ?  261 LYS   B HB2    1 
ATOM   10136 H  HB3    . LYS   B 1 236 ? 49.796  -23.044 31.838 1.00 59.26  ?  261 LYS   B HB3    1 
ATOM   10137 H  HG2    . LYS   B 1 236 ? 49.118  -25.148 32.432 1.00 61.55  ?  261 LYS   B HG2    1 
ATOM   10138 H  HG3    . LYS   B 1 236 ? 48.172  -24.089 33.145 1.00 61.55  ?  261 LYS   B HG3    1 
ATOM   10139 H  HD2    . LYS   B 1 236 ? 46.442  -24.592 31.850 1.00 61.80  ?  261 LYS   B HD2    1 
ATOM   10140 H  HD3    . LYS   B 1 236 ? 47.365  -25.196 30.706 1.00 61.80  ?  261 LYS   B HD3    1 
ATOM   10141 H  HE2    . LYS   B 1 236 ? 46.858  -26.456 33.182 1.00 63.47  ?  261 LYS   B HE2    1 
ATOM   10142 H  HE3    . LYS   B 1 236 ? 46.264  -26.931 31.787 1.00 63.47  ?  261 LYS   B HE3    1 
ATOM   10143 H  HZ1    . LYS   B 1 236 ? 48.856  -27.141 32.590 1.00 64.60  ?  261 LYS   B HZ1    1 
ATOM   10144 H  HZ2    . LYS   B 1 236 ? 48.017  -28.212 32.093 1.00 64.60  ?  261 LYS   B HZ2    1 
ATOM   10145 H  HZ3    . LYS   B 1 236 ? 48.538  -27.216 31.179 1.00 64.60  ?  261 LYS   B HZ3    1 
ATOM   10146 N  N      . LEU   B 1 237 ? 46.047  -22.083 32.544 1.00 41.28  ?  262 LEU   B N      1 
ATOM   10147 C  CA     . LEU   B 1 237 ? 45.308  -21.730 33.756 1.00 39.01  ?  262 LEU   B CA     1 
ATOM   10148 C  C      . LEU   B 1 237 ? 45.521  -22.810 34.811 1.00 39.57  ?  262 LEU   B C      1 
ATOM   10149 O  O      . LEU   B 1 237 ? 45.194  -23.978 34.564 1.00 41.17  ?  262 LEU   B O      1 
ATOM   10150 C  CB     . LEU   B 1 237 ? 43.828  -21.536 33.448 1.00 36.20  ?  262 LEU   B CB     1 
ATOM   10151 C  CG     . LEU   B 1 237 ? 43.520  -20.529 32.335 1.00 34.80  ?  262 LEU   B CG     1 
ATOM   10152 C  CD1    . LEU   B 1 237 ? 42.000  -20.268 32.220 1.00 33.82  ?  262 LEU   B CD1    1 
ATOM   10153 C  CD2    . LEU   B 1 237 ? 44.255  -19.209 32.542 1.00 36.81  ?  262 LEU   B CD2    1 
ATOM   10154 H  H      . LEU   B 1 237 ? 45.584  -22.483 31.939 1.00 49.53  ?  262 LEU   B H      1 
ATOM   10155 H  HA     . LEU   B 1 237 ? 45.636  -20.891 34.116 1.00 46.80  ?  262 LEU   B HA     1 
ATOM   10156 H  HB2    . LEU   B 1 237 ? 43.457  -22.391 33.177 1.00 43.43  ?  262 LEU   B HB2    1 
ATOM   10157 H  HB3    . LEU   B 1 237 ? 43.386  -21.223 34.253 1.00 43.43  ?  262 LEU   B HB3    1 
ATOM   10158 H  HG     . LEU   B 1 237 ? 43.833  -20.917 31.503 1.00 41.75  ?  262 LEU   B HG     1 
ATOM   10159 H  HD11   . LEU   B 1 237 ? 41.841  -19.641 31.497 1.00 40.57  ?  262 LEU   B HD11   1 
ATOM   10160 H  HD12   . LEU   B 1 237 ? 41.549  -21.107 32.037 1.00 40.57  ?  262 LEU   B HD12   1 
ATOM   10161 H  HD13   . LEU   B 1 237 ? 41.680  -19.896 33.057 1.00 40.57  ?  262 LEU   B HD13   1 
ATOM   10162 H  HD21   . LEU   B 1 237 ? 43.897  -18.549 31.927 1.00 44.17  ?  262 LEU   B HD21   1 
ATOM   10163 H  HD22   . LEU   B 1 237 ? 44.123  -18.914 33.456 1.00 44.17  ?  262 LEU   B HD22   1 
ATOM   10164 H  HD23   . LEU   B 1 237 ? 45.200  -19.343 32.370 1.00 44.17  ?  262 LEU   B HD23   1 
ATOM   10165 N  N      . PRO   B 1 238 ? 46.052  -22.472 35.994 1.00 39.53  ?  263 PRO   B N      1 
ATOM   10166 C  CA     . PRO   B 1 238 ? 46.464  -23.530 36.943 1.00 39.94  ?  263 PRO   B CA     1 
ATOM   10167 C  C      . PRO   B 1 238 ? 45.324  -24.047 37.811 1.00 40.58  ?  263 PRO   B C      1 
ATOM   10168 O  O      . PRO   B 1 238 ? 45.296  -23.880 39.032 1.00 42.71  ?  263 PRO   B O      1 
ATOM   10169 C  CB     . PRO   B 1 238 ? 47.551  -22.823 37.764 1.00 40.70  ?  263 PRO   B CB     1 
ATOM   10170 C  CG     . PRO   B 1 238 ? 47.115  -21.391 37.780 1.00 40.30  ?  263 PRO   B CG     1 
ATOM   10171 C  CD     . PRO   B 1 238 ? 46.480  -21.130 36.436 1.00 39.07  ?  263 PRO   B CD     1 
ATOM   10172 H  HA     . PRO   B 1 238 ? 46.846  -24.273 36.450 1.00 47.92  ?  263 PRO   B HA     1 
ATOM   10173 H  HB2    . PRO   B 1 238 ? 47.584  -23.190 38.661 1.00 48.84  ?  263 PRO   B HB2    1 
ATOM   10174 H  HB3    . PRO   B 1 238 ? 48.414  -22.923 37.333 1.00 48.84  ?  263 PRO   B HB3    1 
ATOM   10175 H  HG2    . PRO   B 1 238 ? 46.473  -21.254 38.494 1.00 48.35  ?  263 PRO   B HG2    1 
ATOM   10176 H  HG3    . PRO   B 1 238 ? 47.886  -20.817 37.912 1.00 48.35  ?  263 PRO   B HG3    1 
ATOM   10177 H  HD2    . PRO   B 1 238 ? 45.718  -20.536 36.524 1.00 46.88  ?  263 PRO   B HD2    1 
ATOM   10178 H  HD3    . PRO   B 1 238 ? 47.125  -20.752 35.818 1.00 46.88  ?  263 PRO   B HD3    1 
ATOM   10179 N  N      . VAL   B 1 239 ? 44.362  -24.699 37.163 1.00 38.73  ?  264 VAL   B N      1 
ATOM   10180 C  CA     . VAL   B 1 239 ? 43.228  -25.336 37.820 1.00 38.41  ?  264 VAL   B CA     1 
ATOM   10181 C  C      . VAL   B 1 239 ? 43.295  -26.824 37.507 1.00 41.34  ?  264 VAL   B C      1 
ATOM   10182 O  O      . VAL   B 1 239 ? 43.436  -27.207 36.340 1.00 44.19  ?  264 VAL   B O      1 
ATOM   10183 C  CB     . VAL   B 1 239 ? 41.893  -24.744 37.333 1.00 36.73  ?  264 VAL   B CB     1 
ATOM   10184 C  CG1    . VAL   B 1 239 ? 40.743  -25.348 38.098 1.00 36.34  ?  264 VAL   B CG1    1 
ATOM   10185 C  CG2    . VAL   B 1 239 ? 41.900  -23.233 37.465 1.00 37.19  ?  264 VAL   B CG2    1 
ATOM   10186 H  H      . VAL   B 1 239 ? 44.345  -24.788 36.307 1.00 46.47  ?  264 VAL   B H      1 
ATOM   10187 H  HA     . VAL   B 1 239 ? 43.289  -25.210 38.779 1.00 46.09  ?  264 VAL   B HA     1 
ATOM   10188 H  HB     . VAL   B 1 239 ? 41.775  -24.958 36.394 1.00 44.07  ?  264 VAL   B HB     1 
ATOM   10189 H  HG11   . VAL   B 1 239 ? 39.928  -24.874 37.869 1.00 43.61  ?  264 VAL   B HG11   1 
ATOM   10190 H  HG12   . VAL   B 1 239 ? 40.660  -26.284 37.857 1.00 43.61  ?  264 VAL   B HG12   1 
ATOM   10191 H  HG13   . VAL   B 1 239 ? 40.918  -25.265 39.049 1.00 43.61  ?  264 VAL   B HG13   1 
ATOM   10192 H  HG21   . VAL   B 1 239 ? 41.018  -22.893 37.244 1.00 44.63  ?  264 VAL   B HG21   1 
ATOM   10193 H  HG22   . VAL   B 1 239 ? 42.126  -22.997 38.378 1.00 44.63  ?  264 VAL   B HG22   1 
ATOM   10194 H  HG23   . VAL   B 1 239 ? 42.558  -22.866 36.855 1.00 44.63  ?  264 VAL   B HG23   1 
ATOM   10195 N  N      . LYS   B 1 240 ? 43.203  -27.668 38.533 1.00 42.75  ?  265 LYS   B N      1 
ATOM   10196 C  CA     . LYS   B 1 240 ? 43.207  -29.103 38.272 1.00 49.56  ?  265 LYS   B CA     1 
ATOM   10197 C  C      . LYS   B 1 240 ? 41.775  -29.633 38.332 1.00 50.81  ?  265 LYS   B C      1 
ATOM   10198 O  O      . LYS   B 1 240 ? 41.220  -30.017 37.299 1.00 54.37  ?  265 LYS   B O      1 
ATOM   10199 C  CB     . LYS   B 1 240 ? 44.200  -29.833 39.191 1.00 54.82  ?  265 LYS   B CB     1 
ATOM   10200 C  CG     . LYS   B 1 240 ? 43.995  -29.819 40.696 1.00 58.99  ?  265 LYS   B CG     1 
ATOM   10201 C  CD     . LYS   B 1 240 ? 45.094  -30.712 41.304 1.00 62.22  ?  265 LYS   B CD     1 
ATOM   10202 C  CE     . LYS   B 1 240 ? 45.034  -30.863 42.814 1.00 64.31  ?  265 LYS   B CE     1 
ATOM   10203 N  NZ     . LYS   B 1 240 ? 46.159  -31.741 43.283 1.00 65.33  ?  265 LYS   B NZ     1 
ATOM   10204 H  H      . LYS   B 1 240 ? 43.139  -27.439 39.359 1.00 51.30  ?  265 LYS   B H      1 
ATOM   10205 H  HA     . LYS   B 1 240 ? 43.528  -29.253 37.369 1.00 59.47  ?  265 LYS   B HA     1 
ATOM   10206 H  HB2    . LYS   B 1 240 ? 44.201  -30.767 38.929 1.00 65.78  ?  265 LYS   B HB2    1 
ATOM   10207 H  HB3    . LYS   B 1 240 ? 45.075  -29.444 39.036 1.00 65.78  ?  265 LYS   B HB3    1 
ATOM   10208 H  HG2    . LYS   B 1 240 ? 44.082  -28.916 41.042 1.00 70.78  ?  265 LYS   B HG2    1 
ATOM   10209 H  HG3    . LYS   B 1 240 ? 43.123  -30.178 40.923 1.00 70.78  ?  265 LYS   B HG3    1 
ATOM   10210 H  HD2    . LYS   B 1 240 ? 45.018  -31.600 40.920 1.00 74.66  ?  265 LYS   B HD2    1 
ATOM   10211 H  HD3    . LYS   B 1 240 ? 45.958  -30.329 41.085 1.00 74.66  ?  265 LYS   B HD3    1 
ATOM   10212 H  HE2    . LYS   B 1 240 ? 45.121  -29.993 43.233 1.00 77.17  ?  265 LYS   B HE2    1 
ATOM   10213 H  HE3    . LYS   B 1 240 ? 44.192  -31.272 43.068 1.00 77.17  ?  265 LYS   B HE3    1 
ATOM   10214 H  HZ1    . LYS   B 1 240 ? 46.126  -31.831 44.168 1.00 78.39  ?  265 LYS   B HZ1    1 
ATOM   10215 H  HZ2    . LYS   B 1 240 ? 46.095  -32.546 42.908 1.00 78.39  ?  265 LYS   B HZ2    1 
ATOM   10216 H  HZ3    . LYS   B 1 240 ? 46.941  -31.380 43.059 1.00 78.39  ?  265 LYS   B HZ3    1 
ATOM   10217 N  N      . GLY   B 1 241 ? 41.140  -29.622 39.507 1.00 47.00  ?  266 GLY   B N      1 
ATOM   10218 C  CA     . GLY   B 1 241 ? 39.782  -30.094 39.648 1.00 41.39  ?  266 GLY   B CA     1 
ATOM   10219 C  C      . GLY   B 1 241 ? 38.809  -29.005 40.076 1.00 37.39  ?  266 GLY   B C      1 
ATOM   10220 O  O      . GLY   B 1 241 ? 39.198  -27.869 40.364 1.00 37.41  ?  266 GLY   B O      1 
ATOM   10221 H  H      . GLY   B 1 241 ? 41.429  -29.189 40.199 1.00 56.39  ?  266 GLY   B H      1 
ATOM   10222 H  HA2    . GLY   B 1 241 ? 39.479  -30.466 38.805 1.00 49.66  ?  266 GLY   B HA2    1 
ATOM   10223 H  HA3    . GLY   B 1 241 ? 39.780  -30.792 40.321 1.00 49.66  ?  266 GLY   B HA3    1 
ATOM   10224 N  N      . PHE   B 1 242 ? 37.523  -29.372 40.115 1.00 34.12  ?  267 PHE   B N      1 
ATOM   10225 C  CA     . PHE   B 1 242 ? 36.514  -28.431 40.596 1.00 31.50  ?  267 PHE   B CA     1 
ATOM   10226 C  C      . PHE   B 1 242 ? 36.824  -27.978 42.018 1.00 32.08  ?  267 PHE   B C      1 
ATOM   10227 O  O      . PHE   B 1 242 ? 36.576  -26.822 42.372 1.00 32.45  ?  267 PHE   B O      1 
ATOM   10228 C  CB     . PHE   B 1 242 ? 35.116  -29.056 40.532 1.00 28.51  ?  267 PHE   B CB     1 
ATOM   10229 C  CG     . PHE   B 1 242 ? 33.997  -28.076 40.788 1.00 26.31  ?  267 PHE   B CG     1 
ATOM   10230 C  CD1    . PHE   B 1 242 ? 33.803  -26.981 39.960 1.00 26.54  ?  267 PHE   B CD1    1 
ATOM   10231 C  CD2    . PHE   B 1 242 ? 33.128  -28.250 41.855 1.00 26.34  ?  267 PHE   B CD2    1 
ATOM   10232 C  CE1    . PHE   B 1 242 ? 32.767  -26.071 40.205 1.00 25.48  ?  267 PHE   B CE1    1 
ATOM   10233 C  CE2    . PHE   B 1 242 ? 32.088  -27.349 42.093 1.00 26.12  ?  267 PHE   B CE2    1 
ATOM   10234 C  CZ     . PHE   B 1 242 ? 31.902  -26.270 41.261 1.00 25.45  ?  267 PHE   B CZ     1 
ATOM   10235 H  H      . PHE   B 1 242 ? 37.218  -30.140 39.876 1.00 40.93  ?  267 PHE   B H      1 
ATOM   10236 H  HA     . PHE   B 1 242 ? 36.513  -27.654 40.016 1.00 37.80  ?  267 PHE   B HA     1 
ATOM   10237 H  HB2    . PHE   B 1 242 ? 34.984  -29.431 39.647 1.00 34.20  ?  267 PHE   B HB2    1 
ATOM   10238 H  HB3    . PHE   B 1 242 ? 35.057  -29.754 41.202 1.00 34.20  ?  267 PHE   B HB3    1 
ATOM   10239 H  HD1    . PHE   B 1 242 ? 34.368  -26.849 39.233 1.00 31.85  ?  267 PHE   B HD1    1 
ATOM   10240 H  HD2    . PHE   B 1 242 ? 33.240  -28.979 42.421 1.00 31.60  ?  267 PHE   B HD2    1 
ATOM   10241 H  HE1    . PHE   B 1 242 ? 32.662  -25.329 39.654 1.00 30.57  ?  267 PHE   B HE1    1 
ATOM   10242 H  HE2    . PHE   B 1 242 ? 31.518  -27.480 42.817 1.00 31.34  ?  267 PHE   B HE2    1 
ATOM   10243 H  HZ     . PHE   B 1 242 ? 31.199  -25.679 41.410 1.00 30.53  ?  267 PHE   B HZ     1 
ATOM   10244 N  N      . ARG   B 1 243 ? 37.385  -28.858 42.843 1.00 32.28  ?  268 ARG   B N      1 
ATOM   10245 C  CA     . ARG   B 1 243 ? 37.663  -28.470 44.220 1.00 34.82  ?  268 ARG   B CA     1 
ATOM   10246 C  C      . ARG   B 1 243 ? 38.725  -27.376 44.281 1.00 34.56  ?  268 ARG   B C      1 
ATOM   10247 O  O      . ARG   B 1 243 ? 38.609  -26.440 45.082 1.00 35.24  ?  268 ARG   B O      1 
ATOM   10248 C  CB     . ARG   B 1 243 ? 38.083  -29.695 45.035 1.00 38.05  ?  268 ARG   B CB     1 
ATOM   10249 C  CG     . ARG   B 1 243 ? 38.479  -29.386 46.467 1.00 42.59  ?  268 ARG   B CG     1 
ATOM   10250 C  CD     . ARG   B 1 243 ? 37.316  -28.816 47.258 1.00 46.77  ?  268 ARG   B CD     1 
ATOM   10251 N  NE     . ARG   B 1 243 ? 37.771  -27.945 48.339 1.00 51.25  ?  268 ARG   B NE     1 
ATOM   10252 C  CZ     . ARG   B 1 243 ? 37.905  -28.320 49.608 1.00 53.90  ?  268 ARG   B CZ     1 
ATOM   10253 N  NH1    . ARG   B 1 243 ? 37.616  -29.562 49.977 1.00 55.45  ?  268 ARG   B NH1    1 
ATOM   10254 N  NH2    . ARG   B 1 243 ? 38.326  -27.442 50.508 1.00 53.73  ?  268 ARG   B NH2    1 
ATOM   10255 H  H      . ARG   B 1 243 ? 37.609  -29.662 42.636 1.00 38.73  ?  268 ARG   B H      1 
ATOM   10256 H  HA     . ARG   B 1 243 ? 36.853  -28.117 44.620 1.00 41.77  ?  268 ARG   B HA     1 
ATOM   10257 H  HB2    . ARG   B 1 243 ? 37.340  -30.318 45.063 1.00 45.65  ?  268 ARG   B HB2    1 
ATOM   10258 H  HB3    . ARG   B 1 243 ? 38.846  -30.108 44.601 1.00 45.65  ?  268 ARG   B HB3    1 
ATOM   10259 H  HG2    . ARG   B 1 243 ? 38.772  -30.202 46.902 1.00 51.10  ?  268 ARG   B HG2    1 
ATOM   10260 H  HG3    . ARG   B 1 243 ? 39.196  -28.733 46.468 1.00 51.10  ?  268 ARG   B HG3    1 
ATOM   10261 H  HD2    . ARG   B 1 243 ? 36.751  -28.296 46.666 1.00 56.11  ?  268 ARG   B HD2    1 
ATOM   10262 H  HD3    . ARG   B 1 243 ? 36.808  -29.544 47.648 1.00 56.11  ?  268 ARG   B HD3    1 
ATOM   10263 H  HE     . ARG   B 1 243 ? 37.965  -27.131 48.140 1.00 61.49  ?  268 ARG   B HE     1 
ATOM   10264 H  HH11   . ARG   B 1 243 ? 37.340  -30.131 49.394 1.00 66.53  ?  268 ARG   B HH11   1 
ATOM   10265 H  HH12   . ARG   B 1 243 ? 37.705  -29.798 50.800 1.00 66.53  ?  268 ARG   B HH12   1 
ATOM   10266 H  HH21   . ARG   B 1 243 ? 38.511  -26.637 50.270 1.00 64.47  ?  268 ARG   B HH21   1 
ATOM   10267 H  HH22   . ARG   B 1 243 ? 38.415  -27.678 51.330 1.00 64.47  ?  268 ARG   B HH22   1 
ATOM   10268 N  N      . SER   B 1 244 ? 39.762  -27.469 43.441 1.00 34.20  ?  269 SER   B N      1 
ATOM   10269 C  CA     . SER   B 1 244 ? 40.780  -26.423 43.410 1.00 35.08  ?  269 SER   B CA     1 
ATOM   10270 C  C      . SER   B 1 244 ? 40.236  -25.129 42.815 1.00 33.50  ?  269 SER   B C      1 
ATOM   10271 O  O      . SER   B 1 244 ? 40.699  -24.041 43.175 1.00 33.82  ?  269 SER   B O      1 
ATOM   10272 C  CB     . SER   B 1 244 ? 42.005  -26.892 42.618 1.00 39.23  ?  269 SER   B CB     1 
ATOM   10273 O  OG     . SER   B 1 244 ? 41.729  -26.983 41.227 1.00 41.44  ?  269 SER   B OG     1 
ATOM   10274 H  H      . SER   B 1 244 ? 39.894  -28.117 42.890 1.00 41.03  ?  269 SER   B H      1 
ATOM   10275 H  HA     . SER   B 1 244 ? 41.064  -26.245 44.320 1.00 42.08  ?  269 SER   B HA     1 
ATOM   10276 H  HB2    . SER   B 1 244 ? 42.725  -26.256 42.752 1.00 47.07  ?  269 SER   B HB2    1 
ATOM   10277 H  HB3    . SER   B 1 244 ? 42.270  -27.767 42.942 1.00 47.07  ?  269 SER   B HB3    1 
ATOM   10278 H  HG     . SER   B 1 244 ? 41.076  -27.495 41.097 1.00 49.72  ?  269 SER   B HG     1 
ATOM   10279 N  N      . TYR   B 1 245 ? 39.270  -25.223 41.894 1.00 32.51  ?  270 TYR   B N      1 
ATOM   10280 C  CA     . TYR   B 1 245 ? 38.589  -24.030 41.393 1.00 31.42  ?  270 TYR   B CA     1 
ATOM   10281 C  C      . TYR   B 1 245 ? 37.844  -23.336 42.532 1.00 30.99  ?  270 TYR   B C      1 
ATOM   10282 O  O      . TYR   B 1 245 ? 37.997  -22.126 42.751 1.00 31.16  ?  270 TYR   B O      1 
ATOM   10283 C  CB     . TYR   B 1 245 ? 37.642  -24.426 40.234 1.00 31.00  ?  270 TYR   B CB     1 
ATOM   10284 C  CG     . TYR   B 1 245 ? 36.679  -23.338 39.787 1.00 30.93  ?  270 TYR   B CG     1 
ATOM   10285 C  CD1    . TYR   B 1 245 ? 37.056  -22.378 38.866 1.00 31.14  ?  270 TYR   B CD1    1 
ATOM   10286 C  CD2    . TYR   B 1 245 ? 35.381  -23.276 40.291 1.00 30.13  ?  270 TYR   B CD2    1 
ATOM   10287 C  CE1    . TYR   B 1 245 ? 36.181  -21.361 38.482 1.00 27.91  ?  270 TYR   B CE1    1 
ATOM   10288 C  CE2    . TYR   B 1 245 ? 34.503  -22.279 39.901 1.00 30.41  ?  270 TYR   B CE2    1 
ATOM   10289 C  CZ     . TYR   B 1 245 ? 34.905  -21.319 38.996 1.00 29.90  ?  270 TYR   B CZ     1 
ATOM   10290 O  OH     . TYR   B 1 245 ? 34.034  -20.325 38.613 1.00 29.83  ?  270 TYR   B OH     1 
ATOM   10291 H  H      . TYR   B 1 245 ? 38.995  -25.960 41.547 1.00 39.00  ?  270 TYR   B H      1 
ATOM   10292 H  HA     . TYR   B 1 245 ? 39.232  -23.398 41.035 1.00 37.70  ?  270 TYR   B HA     1 
ATOM   10293 H  HB2    . TYR   B 1 245 ? 38.183  -24.668 39.466 1.00 37.20  ?  270 TYR   B HB2    1 
ATOM   10294 H  HB3    . TYR   B 1 245 ? 37.110  -25.186 40.518 1.00 37.20  ?  270 TYR   B HB3    1 
ATOM   10295 H  HD1    . TYR   B 1 245 ? 37.909  -22.410 38.495 1.00 37.36  ?  270 TYR   B HD1    1 
ATOM   10296 H  HD2    . TYR   B 1 245 ? 35.099  -23.918 40.902 1.00 36.15  ?  270 TYR   B HD2    1 
ATOM   10297 H  HE1    . TYR   B 1 245 ? 36.459  -20.712 37.877 1.00 33.49  ?  270 TYR   B HE1    1 
ATOM   10298 H  HE2    . TYR   B 1 245 ? 33.640  -22.258 40.249 1.00 36.49  ?  270 TYR   B HE2    1 
ATOM   10299 H  HH     . TYR   B 1 245 ? 34.384  -19.851 38.015 1.00 35.79  ?  270 TYR   B HH     1 
ATOM   10300 N  N      . VAL   B 1 246 ? 37.062  -24.104 43.296 1.00 30.24  ?  271 VAL   B N      1 
ATOM   10301 C  CA     . VAL   B 1 246 ? 36.329  -23.538 44.424 1.00 30.96  ?  271 VAL   B CA     1 
ATOM   10302 C  C      . VAL   B 1 246 ? 37.289  -22.852 45.395 1.00 32.95  ?  271 VAL   B C      1 
ATOM   10303 O  O      . VAL   B 1 246 ? 36.984  -21.788 45.944 1.00 33.69  ?  271 VAL   B O      1 
ATOM   10304 C  CB     . VAL   B 1 246 ? 35.501  -24.639 45.118 1.00 30.12  ?  271 VAL   B CB     1 
ATOM   10305 C  CG1    . VAL   B 1 246 ? 34.880  -24.105 46.400 1.00 31.50  ?  271 VAL   B CG1    1 
ATOM   10306 C  CG2    . VAL   B 1 246 ? 34.396  -25.202 44.182 1.00 28.57  ?  271 VAL   B CG2    1 
ATOM   10307 H  H      . VAL   B 1 246 ? 36.942  -24.948 43.182 1.00 36.28  ?  271 VAL   B H      1 
ATOM   10308 H  HA     . VAL   B 1 246 ? 35.716  -22.864 44.092 1.00 37.15  ?  271 VAL   B HA     1 
ATOM   10309 H  HB     . VAL   B 1 246 ? 36.099  -25.370 45.338 1.00 36.14  ?  271 VAL   B HB     1 
ATOM   10310 H  HG11   . VAL   B 1 246 ? 34.180  -24.711 46.688 1.00 37.80  ?  271 VAL   B HG11   1 
ATOM   10311 H  HG12   . VAL   B 1 246 ? 35.567  -24.045 47.082 1.00 37.80  ?  271 VAL   B HG12   1 
ATOM   10312 H  HG13   . VAL   B 1 246 ? 34.507  -23.226 46.228 1.00 37.80  ?  271 VAL   B HG13   1 
ATOM   10313 H  HG21   . VAL   B 1 246 ? 33.947  -25.936 44.630 1.00 34.28  ?  271 VAL   B HG21   1 
ATOM   10314 H  HG22   . VAL   B 1 246 ? 33.760  -24.496 43.984 1.00 34.28  ?  271 VAL   B HG22   1 
ATOM   10315 H  HG23   . VAL   B 1 246 ? 34.807  -25.517 43.362 1.00 34.28  ?  271 VAL   B HG23   1 
ATOM   10316 N  N      . ASP   B 1 247 ? 38.466  -23.435 45.613 1.00 34.38  ?  272 ASP   B N      1 
ATOM   10317 C  CA     . ASP   B 1 247 ? 39.376  -22.856 46.589 1.00 36.89  ?  272 ASP   B CA     1 
ATOM   10318 C  C      . ASP   B 1 247 ? 39.865  -21.478 46.181 1.00 37.09  ?  272 ASP   B C      1 
ATOM   10319 O  O      . ASP   B 1 247 ? 40.232  -20.685 47.052 1.00 37.47  ?  272 ASP   B O      1 
ATOM   10320 C  CB     . ASP   B 1 247 ? 40.556  -23.798 46.805 1.00 40.71  ?  272 ASP   B CB     1 
ATOM   10321 C  CG     . ASP   B 1 247 ? 40.207  -24.965 47.711 1.00 47.12  ?  272 ASP   B CG     1 
ATOM   10322 O  OD1    . ASP   B 1 247 ? 39.291  -24.821 48.553 1.00 49.83  ?  272 ASP   B OD1    1 
ATOM   10323 O  OD2    . ASP   B 1 247 ? 40.856  -26.025 47.588 1.00 50.28  ?  272 ASP   B OD2    1 
ATOM   10324 H  H      . ASP   B 1 247 ? 38.751  -24.145 45.219 1.00 41.25  ?  272 ASP   B H      1 
ATOM   10325 H  HA     . ASP   B 1 247 ? 38.913  -22.756 47.436 1.00 44.26  ?  272 ASP   B HA     1 
ATOM   10326 H  HB2    . ASP   B 1 247 ? 40.839  -24.155 45.949 1.00 48.85  ?  272 ASP   B HB2    1 
ATOM   10327 H  HB3    . ASP   B 1 247 ? 41.285  -23.306 47.216 1.00 48.85  ?  272 ASP   B HB3    1 
ATOM   10328 N  N      . MET   B 1 248 ? 39.865  -21.171 44.891 1.00 35.19  ?  273 MET   B N      1 
ATOM   10329 C  CA     . MET   B 1 248 ? 40.288  -19.845 44.471 1.00 35.23  ?  273 MET   B CA     1 
ATOM   10330 C  C      . MET   B 1 248 ? 39.351  -18.773 45.006 1.00 35.02  ?  273 MET   B C      1 
ATOM   10331 O  O      . MET   B 1 248 ? 39.768  -17.623 45.200 1.00 35.05  ?  273 MET   B O      1 
ATOM   10332 C  CB     . MET   B 1 248 ? 40.346  -19.779 42.951 1.00 36.26  ?  273 MET   B CB     1 
ATOM   10333 C  CG     . MET   B 1 248 ? 41.305  -20.770 42.329 1.00 38.75  ?  273 MET   B CG     1 
ATOM   10334 S  SD     . MET   B 1 248 ? 41.458  -20.467 40.563 1.00 42.06  ?  273 MET   B SD     1 
ATOM   10335 C  CE     . MET   B 1 248 ? 42.470  -18.984 40.558 1.00 45.34  ?  273 MET   B CE     1 
ATOM   10336 H  H      . MET   B 1 248 ? 39.632  -21.700 44.254 1.00 42.22  ?  273 MET   B H      1 
ATOM   10337 H  HA     . MET   B 1 248 ? 41.181  -19.679 44.811 1.00 42.27  ?  273 MET   B HA     1 
ATOM   10338 H  HB2    . MET   B 1 248 ? 39.462  -19.963 42.597 1.00 43.51  ?  273 MET   B HB2    1 
ATOM   10339 H  HB3    . MET   B 1 248 ? 40.630  -18.890 42.689 1.00 43.51  ?  273 MET   B HB3    1 
ATOM   10340 H  HG2    . MET   B 1 248 ? 42.180  -20.675 42.737 1.00 46.49  ?  273 MET   B HG2    1 
ATOM   10341 H  HG3    . MET   B 1 248 ? 40.973  -21.671 42.462 1.00 46.49  ?  273 MET   B HG3    1 
ATOM   10342 H  HE1    . MET   B 1 248 ? 42.633  -18.716 39.640 1.00 54.40  ?  273 MET   B HE1    1 
ATOM   10343 H  HE2    . MET   B 1 248 ? 42.000  -18.279 41.030 1.00 54.40  ?  273 MET   B HE2    1 
ATOM   10344 H  HE3    . MET   B 1 248 ? 43.312  -19.175 41.001 1.00 54.40  ?  273 MET   B HE3    1 
ATOM   10345 N  N      . TYR   B 1 249 ? 38.079  -19.131 45.233 1.00 33.05  ?  274 TYR   B N      1 
ATOM   10346 C  CA     . TYR   B 1 249 ? 37.096  -18.189 45.749 1.00 33.66  ?  274 TYR   B CA     1 
ATOM   10347 C  C      . TYR   B 1 249 ? 37.205  -18.022 47.253 1.00 39.38  ?  274 TYR   B C      1 
ATOM   10348 O  O      . TYR   B 1 249 ? 36.825  -16.975 47.784 1.00 40.72  ?  274 TYR   B O      1 
ATOM   10349 C  CB     . TYR   B 1 249 ? 35.675  -18.655 45.412 1.00 31.64  ?  274 TYR   B CB     1 
ATOM   10350 C  CG     . TYR   B 1 249 ? 35.320  -18.494 43.963 1.00 29.64  ?  274 TYR   B CG     1 
ATOM   10351 C  CD1    . TYR   B 1 249 ? 35.688  -19.449 43.028 1.00 29.34  ?  274 TYR   B CD1    1 
ATOM   10352 C  CD2    . TYR   B 1 249 ? 34.632  -17.379 43.527 1.00 29.90  ?  274 TYR   B CD2    1 
ATOM   10353 C  CE1    . TYR   B 1 249 ? 35.385  -19.292 41.698 1.00 28.58  ?  274 TYR   B CE1    1 
ATOM   10354 C  CE2    . TYR   B 1 249 ? 34.308  -17.218 42.201 1.00 29.48  ?  274 TYR   B CE2    1 
ATOM   10355 C  CZ     . TYR   B 1 249 ? 34.680  -18.174 41.295 1.00 29.73  ?  274 TYR   B CZ     1 
ATOM   10356 O  OH     . TYR   B 1 249 ? 34.343  -17.995 39.976 1.00 31.86  ?  274 TYR   B OH     1 
ATOM   10357 H  H      . TYR   B 1 249 ? 37.764  -19.919 45.092 1.00 39.66  ?  274 TYR   B H      1 
ATOM   10358 H  HA     . TYR   B 1 249 ? 37.252  -17.332 45.322 1.00 40.39  ?  274 TYR   B HA     1 
ATOM   10359 H  HB2    . TYR   B 1 249 ? 35.593  -19.595 45.636 1.00 37.96  ?  274 TYR   B HB2    1 
ATOM   10360 H  HB3    . TYR   B 1 249 ? 35.044  -18.134 45.933 1.00 37.96  ?  274 TYR   B HB3    1 
ATOM   10361 H  HD1    . TYR   B 1 249 ? 36.148  -20.208 43.306 1.00 35.20  ?  274 TYR   B HD1    1 
ATOM   10362 H  HD2    . TYR   B 1 249 ? 34.383  -16.727 44.141 1.00 35.87  ?  274 TYR   B HD2    1 
ATOM   10363 H  HE1    . TYR   B 1 249 ? 35.650  -19.931 41.077 1.00 34.29  ?  274 TYR   B HE1    1 
ATOM   10364 H  HE2    . TYR   B 1 249 ? 33.839  -16.465 41.922 1.00 35.37  ?  274 TYR   B HE2    1 
ATOM   10365 H  HH     . TYR   B 1 249 ? 34.627  -18.639 39.517 1.00 38.22  ?  274 TYR   B HH     1 
ATOM   10366 N  N      . LEU   B 1 250 ? 37.694  -19.038 47.950 1.00 43.18  ?  275 LEU   B N      1 
ATOM   10367 C  CA     . LEU   B 1 250 ? 37.677  -19.054 49.403 1.00 48.31  ?  275 LEU   B CA     1 
ATOM   10368 C  C      . LEU   B 1 250 ? 39.052  -18.936 50.028 1.00 56.28  ?  275 LEU   B C      1 
ATOM   10369 O  O      . LEU   B 1 250 ? 39.161  -18.450 51.149 1.00 57.18  ?  275 LEU   B O      1 
ATOM   10370 C  CB     . LEU   B 1 250 ? 37.024  -20.343 49.909 1.00 46.65  ?  275 LEU   B CB     1 
ATOM   10371 C  CG     . LEU   B 1 250 ? 35.776  -20.839 49.178 1.00 46.23  ?  275 LEU   B CG     1 
ATOM   10372 C  CD1    . LEU   B 1 250 ? 35.471  -22.271 49.602 1.00 47.54  ?  275 LEU   B CD1    1 
ATOM   10373 C  CD2    . LEU   B 1 250 ? 34.587  -19.936 49.443 1.00 45.02  ?  275 LEU   B CD2    1 
ATOM   10374 H  H      . LEU   B 1 250 ? 38.045  -19.740 47.597 1.00 51.81  ?  275 LEU   B H      1 
ATOM   10375 H  HA     . LEU   B 1 250 ? 37.145  -18.305 49.713 1.00 57.96  ?  275 LEU   B HA     1 
ATOM   10376 H  HB2    . LEU   B 1 250 ? 37.684  -21.052 49.849 1.00 55.98  ?  275 LEU   B HB2    1 
ATOM   10377 H  HB3    . LEU   B 1 250 ? 36.770  -20.203 50.834 1.00 55.98  ?  275 LEU   B HB3    1 
ATOM   10378 H  HG     . LEU   B 1 250 ? 35.938  -20.821 48.222 1.00 55.47  ?  275 LEU   B HG     1 
ATOM   10379 H  HD11   . LEU   B 1 250 ? 34.675  -22.575 49.140 1.00 57.04  ?  275 LEU   B HD11   1 
ATOM   10380 H  HD12   . LEU   B 1 250 ? 36.225  -22.836 49.369 1.00 57.04  ?  275 LEU   B HD12   1 
ATOM   10381 H  HD13   . LEU   B 1 250 ? 35.326  -22.292 50.561 1.00 57.04  ?  275 LEU   B HD13   1 
ATOM   10382 H  HD21   . LEU   B 1 250 ? 33.815  -20.282 48.968 1.00 54.01  ?  275 LEU   B HD21   1 
ATOM   10383 H  HD22   . LEU   B 1 250 ? 34.409  -19.921 50.397 1.00 54.01  ?  275 LEU   B HD22   1 
ATOM   10384 H  HD23   . LEU   B 1 250 ? 34.793  -19.041 49.131 1.00 54.01  ?  275 LEU   B HD23   1 
ATOM   10385 N  N      . LYS   B 1 251 ? 40.100  -19.337 49.303 1.00 63.41  ?  276 LYS   B N      1 
ATOM   10386 C  CA     . LYS   B 1 251 ? 41.418  -19.596 49.870 1.00 71.82  ?  276 LYS   B CA     1 
ATOM   10387 C  C      . LYS   B 1 251 ? 41.816  -18.661 51.003 1.00 77.79  ?  276 LYS   B C      1 
ATOM   10388 O  O      . LYS   B 1 251 ? 42.483  -19.087 51.953 1.00 78.62  ?  276 LYS   B O      1 
ATOM   10389 C  CB     . LYS   B 1 251 ? 42.496  -19.510 48.762 1.00 74.03  ?  276 LYS   B CB     1 
ATOM   10390 C  CG     . LYS   B 1 251 ? 42.734  -18.084 48.234 1.00 76.17  ?  276 LYS   B CG     1 
ATOM   10391 C  CD     . LYS   B 1 251 ? 44.046  -17.942 47.440 1.00 77.85  ?  276 LYS   B CD     1 
ATOM   10392 C  CE     . LYS   B 1 251 ? 45.237  -18.522 48.194 1.00 79.00  ?  276 LYS   B CE     1 
ATOM   10393 N  NZ     . LYS   B 1 251 ? 46.505  -17.770 47.968 1.00 79.48  ?  276 LYS   B NZ     1 
ATOM   10394 H  H      . LYS   B 1 251 ? 40.069  -19.470 48.454 1.00 76.09  ?  276 LYS   B H      1 
ATOM   10395 H  HA     . LYS   B 1 251 ? 41.376  -20.488 50.249 1.00 86.18  ?  276 LYS   B HA     1 
ATOM   10396 H  HB2    . LYS   B 1 251 ? 43.336  -19.837 49.120 1.00 88.83  ?  276 LYS   B HB2    1 
ATOM   10397 H  HB3    . LYS   B 1 251 ? 42.217  -20.060 48.014 1.00 88.83  ?  276 LYS   B HB3    1 
ATOM   10398 H  HG2    . LYS   B 1 251 ? 42.002  -17.840 47.645 1.00 91.40  ?  276 LYS   B HG2    1 
ATOM   10399 H  HG3    . LYS   B 1 251 ? 42.773  -17.472 48.985 1.00 91.40  ?  276 LYS   B HG3    1 
ATOM   10400 H  HD2    . LYS   B 1 251 ? 43.962  -18.416 46.597 1.00 93.42  ?  276 LYS   B HD2    1 
ATOM   10401 H  HD3    . LYS   B 1 251 ? 44.221  -17.002 47.276 1.00 93.42  ?  276 LYS   B HD3    1 
ATOM   10402 H  HE2    . LYS   B 1 251 ? 45.046  -18.502 49.145 1.00 94.80  ?  276 LYS   B HE2    1 
ATOM   10403 H  HE3    . LYS   B 1 251 ? 45.378  -19.437 47.903 1.00 94.80  ?  276 LYS   B HE3    1 
ATOM   10404 H  HZ1    . LYS   B 1 251 ? 46.423  -16.938 48.271 1.00 95.37  ?  276 LYS   B HZ1    1 
ATOM   10405 H  HZ2    . LYS   B 1 251 ? 47.176  -18.169 48.395 1.00 95.37  ?  276 LYS   B HZ2    1 
ATOM   10406 H  HZ3    . LYS   B 1 251 ? 46.691  -17.744 47.098 1.00 95.37  ?  276 LYS   B HZ3    1 
ATOM   10407 N  N      . ASP   B 1 252 ? 41.414  -17.393 50.921 1.00 82.21  ?  277 ASP   B N      1 
ATOM   10408 C  CA     . ASP   B 1 252 ? 42.020  -16.361 51.744 1.00 86.17  ?  277 ASP   B CA     1 
ATOM   10409 C  C      . ASP   B 1 252 ? 41.054  -15.589 52.627 1.00 86.72  ?  277 ASP   B C      1 
ATOM   10410 O  O      . ASP   B 1 252 ? 41.519  -14.813 53.470 1.00 87.72  ?  277 ASP   B O      1 
ATOM   10411 C  CB     . ASP   B 1 252 ? 42.769  -15.355 50.853 1.00 89.14  ?  277 ASP   B CB     1 
ATOM   10412 C  CG     . ASP   B 1 252 ? 41.827  -14.493 50.039 1.00 91.44  ?  277 ASP   B CG     1 
ATOM   10413 O  OD1    . ASP   B 1 252 ? 42.019  -13.259 50.007 1.00 92.29  ?  277 ASP   B OD1    1 
ATOM   10414 O  OD2    . ASP   B 1 252 ? 40.877  -15.053 49.451 1.00 92.03  ?  277 ASP   B OD2    1 
ATOM   10415 H  H      . ASP   B 1 252 ? 40.794  -17.112 50.395 1.00 98.64  ?  277 ASP   B H      1 
ATOM   10416 H  HA     . ASP   B 1 252 ? 42.654  -16.795 52.336 1.00 103.40 ?  277 ASP   B HA     1 
ATOM   10417 H  HB2    . ASP   B 1 252 ? 43.303  -14.771 51.414 1.00 106.97 ?  277 ASP   B HB2    1 
ATOM   10418 H  HB3    . ASP   B 1 252 ? 43.342  -15.839 50.238 1.00 106.97 ?  277 ASP   B HB3    1 
ATOM   10419 N  N      . LYS   B 1 253 ? 39.745  -15.760 52.476 1.00 85.86  ?  278 LYS   B N      1 
ATOM   10420 C  CA     . LYS   B 1 253 ? 38.827  -15.028 53.334 1.00 85.13  ?  278 LYS   B CA     1 
ATOM   10421 C  C      . LYS   B 1 253 ? 38.426  -15.861 54.546 1.00 83.92  ?  278 LYS   B C      1 
ATOM   10422 O  O      . LYS   B 1 253 ? 38.396  -17.094 54.507 1.00 82.82  ?  278 LYS   B O      1 
ATOM   10423 C  CB     . LYS   B 1 253 ? 37.580  -14.569 52.571 1.00 85.56  ?  278 LYS   B CB     1 
ATOM   10424 C  CG     . LYS   B 1 253 ? 36.863  -15.610 51.742 1.00 85.54  ?  278 LYS   B CG     1 
ATOM   10425 C  CD     . LYS   B 1 253 ? 36.234  -14.935 50.520 1.00 85.39  ?  278 LYS   B CD     1 
ATOM   10426 C  CE     . LYS   B 1 253 ? 37.311  -14.527 49.513 1.00 85.05  ?  278 LYS   B CE     1 
ATOM   10427 N  NZ     . LYS   B 1 253 ? 36.913  -13.376 48.649 1.00 84.67  ?  278 LYS   B NZ     1 
ATOM   10428 H  H      . LYS   B 1 253 ? 39.377  -16.281 51.900 1.00 103.03 ?  278 LYS   B H      1 
ATOM   10429 H  HA     . LYS   B 1 253 ? 39.280  -14.231 53.653 1.00 102.15 ?  278 LYS   B HA     1 
ATOM   10430 H  HB2    . LYS   B 1 253 ? 36.940  -14.233 53.219 1.00 102.66 ?  278 LYS   B HB2    1 
ATOM   10431 H  HB3    . LYS   B 1 253 ? 37.843  -13.858 51.966 1.00 102.66 ?  278 LYS   B HB3    1 
ATOM   10432 H  HG2    . LYS   B 1 253 ? 37.493  -16.283 51.440 1.00 102.65 ?  278 LYS   B HG2    1 
ATOM   10433 H  HG3    . LYS   B 1 253 ? 36.161  -16.025 52.268 1.00 102.65 ?  278 LYS   B HG3    1 
ATOM   10434 H  HD2    . LYS   B 1 253 ? 35.624  -15.553 50.086 1.00 102.47 ?  278 LYS   B HD2    1 
ATOM   10435 H  HD3    . LYS   B 1 253 ? 35.756  -14.139 50.799 1.00 102.47 ?  278 LYS   B HD3    1 
ATOM   10436 H  HE2    . LYS   B 1 253 ? 38.112  -14.271 49.997 1.00 102.05 ?  278 LYS   B HE2    1 
ATOM   10437 H  HE3    . LYS   B 1 253 ? 37.500  -15.281 48.933 1.00 102.05 ?  278 LYS   B HE3    1 
ATOM   10438 H  HZ1    . LYS   B 1 253 ? 36.165  -13.571 48.208 1.00 101.60 ?  278 LYS   B HZ1    1 
ATOM   10439 H  HZ2    . LYS   B 1 253 ? 36.772  -12.654 49.150 1.00 101.60 ?  278 LYS   B HZ2    1 
ATOM   10440 H  HZ3    . LYS   B 1 253 ? 37.557  -13.199 48.062 1.00 101.60 ?  278 LYS   B HZ3    1 
ATOM   10441 N  N      . LEU   B 1 254 ? 38.142  -15.156 55.636 1.00 84.39  ?  279 LEU   B N      1 
ATOM   10442 C  CA     . LEU   B 1 254 ? 37.767  -15.731 56.915 1.00 85.08  ?  279 LEU   B CA     1 
ATOM   10443 C  C      . LEU   B 1 254 ? 36.372  -15.231 57.263 1.00 87.67  ?  279 LEU   B C      1 
ATOM   10444 O  O      . LEU   B 1 254 ? 35.915  -14.202 56.757 1.00 87.87  ?  279 LEU   B O      1 
ATOM   10445 C  CB     . LEU   B 1 254 ? 38.760  -15.340 58.013 1.00 83.50  ?  279 LEU   B CB     1 
ATOM   10446 C  CG     . LEU   B 1 254 ? 40.272  -15.482 57.815 1.00 81.82  ?  279 LEU   B CG     1 
ATOM   10447 C  CD1    . LEU   B 1 254 ? 40.689  -16.930 57.570 1.00 81.14  ?  279 LEU   B CD1    1 
ATOM   10448 C  CD2    . LEU   B 1 254 ? 40.801  -14.590 56.689 1.00 81.35  ?  279 LEU   B CD2    1 
ATOM   10449 H  H      . LEU   B 1 254 ? 38.161  -14.297 55.657 1.00 101.26 ?  279 LEU   B H      1 
ATOM   10450 H  HA     . LEU   B 1 254 ? 37.759  -16.699 56.866 1.00 102.09 ?  279 LEU   B HA     1 
ATOM   10451 H  HB2    . LEU   B 1 254 ? 38.608  -14.402 58.207 1.00 100.19 ?  279 LEU   B HB2    1 
ATOM   10452 H  HB3    . LEU   B 1 254 ? 38.545  -15.879 58.790 1.00 100.19 ?  279 LEU   B HB3    1 
ATOM   10453 H  HG     . LEU   B 1 254 ? 40.682  -15.188 58.643 1.00 98.18  ?  279 LEU   B HG     1 
ATOM   10454 H  HD11   . LEU   B 1 254 ? 41.641  -16.957 57.387 1.00 97.36  ?  279 LEU   B HD11   1 
ATOM   10455 H  HD12   . LEU   B 1 254 ? 40.489  -17.454 58.361 1.00 97.36  ?  279 LEU   B HD12   1 
ATOM   10456 H  HD13   . LEU   B 1 254 ? 40.196  -17.276 56.810 1.00 97.36  ?  279 LEU   B HD13   1 
ATOM   10457 H  HD21   . LEU   B 1 254 ? 41.747  -14.427 56.833 1.00 97.61  ?  279 LEU   B HD21   1 
ATOM   10458 H  HD22   . LEU   B 1 254 ? 40.668  -15.040 55.840 1.00 97.61  ?  279 LEU   B HD22   1 
ATOM   10459 H  HD23   . LEU   B 1 254 ? 40.316  -13.750 56.697 1.00 97.61  ?  279 LEU   B HD23   1 
ATOM   10460 N  N      . ASP   B 1 255 ? 35.689  -15.966 58.136 1.00 90.09  ?  280 ASP   B N      1 
ATOM   10461 C  CA     . ASP   B 1 255 ? 34.354  -15.547 58.548 1.00 92.54  ?  280 ASP   B CA     1 
ATOM   10462 C  C      . ASP   B 1 255 ? 34.406  -14.228 59.308 1.00 94.28  ?  280 ASP   B C      1 
ATOM   10463 O  O      . ASP   B 1 255 ? 35.501  -13.704 59.568 1.00 94.02  ?  280 ASP   B O      1 
ATOM   10464 C  CB     . ASP   B 1 255 ? 33.681  -16.636 59.399 1.00 93.06  ?  280 ASP   B CB     1 
ATOM   10465 C  CG     . ASP   B 1 255 ? 34.533  -17.074 60.571 1.00 93.52  ?  280 ASP   B CG     1 
ATOM   10466 O  OD1    . ASP   B 1 255 ? 35.018  -16.200 61.318 1.00 93.71  ?  280 ASP   B OD1    1 
ATOM   10467 O  OD2    . ASP   B 1 255 ? 34.711  -18.296 60.759 1.00 93.66  ?  280 ASP   B OD2    1 
ATOM   10468 H  H      . ASP   B 1 255 ? 35.970  -16.695 58.495 1.00 108.10 ?  280 ASP   B H      1 
ATOM   10469 H  HA     . ASP   B 1 255 ? 33.811  -15.411 57.756 1.00 111.05 ?  280 ASP   B HA     1 
ATOM   10470 H  HB2    . ASP   B 1 255 ? 32.844  -16.292 59.748 1.00 111.67 ?  280 ASP   B HB2    1 
ATOM   10471 H  HB3    . ASP   B 1 255 ? 33.514  -17.413 58.842 1.00 111.67 ?  280 ASP   B HB3    1 
ATOM   10472 N  N      . GLU   B 1 256 ? 33.247  -13.675 59.649 1.00 95.75  ?  281 GLU   B N      1 
ATOM   10473 C  CA     . GLU   B 1 256 ? 33.211  -12.397 60.338 1.00 96.83  ?  281 GLU   B CA     1 
ATOM   10474 C  C      . GLU   B 1 256 ? 33.771  -12.486 61.749 1.00 97.17  ?  281 GLU   B C      1 
ATOM   10475 O  O      . GLU   B 1 256 ? 34.233  -11.470 62.278 1.00 97.28  ?  281 GLU   B O      1 
ATOM   10476 C  CB     . GLU   B 1 256 ? 31.774  -11.870 60.371 1.00 97.44  ?  281 GLU   B CB     1 
ATOM   10477 C  CG     . GLU   B 1 256 ? 31.095  -11.898 59.012 1.00 97.87  ?  281 GLU   B CG     1 
ATOM   10478 C  CD     . GLU   B 1 256 ? 29.965  -10.900 58.901 1.00 98.09  ?  281 GLU   B CD     1 
ATOM   10479 O  OE1    . GLU   B 1 256 ? 29.096  -10.874 59.798 1.00 98.28  ?  281 GLU   B OE1    1 
ATOM   10480 O  OE2    . GLU   B 1 256 ? 29.953  -10.132 57.915 1.00 97.99  ?  281 GLU   B OE2    1 
ATOM   10481 H  H      . GLU   B 1 256 ? 32.474  -14.019 59.494 1.00 114.90 ?  281 GLU   B H      1 
ATOM   10482 H  HA     . GLU   B 1 256 ? 33.754  -11.758 59.850 1.00 116.19 ?  281 GLU   B HA     1 
ATOM   10483 H  HB2    . GLU   B 1 256 ? 31.253  -12.419 60.976 1.00 116.92 ?  281 GLU   B HB2    1 
ATOM   10484 H  HB3    . GLU   B 1 256 ? 31.784  -10.951 60.681 1.00 116.92 ?  281 GLU   B HB3    1 
ATOM   10485 H  HG2    . GLU   B 1 256 ? 31.749  -11.687 58.327 1.00 117.44 ?  281 GLU   B HG2    1 
ATOM   10486 H  HG3    . GLU   B 1 256 ? 30.728  -12.783 58.860 1.00 117.44 ?  281 GLU   B HG3    1 
ATOM   10487 N  N      . THR   B 1 257 ? 33.753  -13.673 62.356 1.00 97.17  ?  282 THR   B N      1 
ATOM   10488 C  CA     . THR   B 1 257 ? 34.353  -13.845 63.672 1.00 96.78  ?  282 THR   B CA     1 
ATOM   10489 C  C      . THR   B 1 257 ? 35.875  -13.926 63.598 1.00 95.17  ?  282 THR   B C      1 
ATOM   10490 O  O      . THR   B 1 257 ? 36.555  -13.535 64.553 1.00 95.42  ?  282 THR   B O      1 
ATOM   10491 C  CB     . THR   B 1 257 ? 33.793  -15.097 64.355 1.00 97.75  ?  282 THR   B CB     1 
ATOM   10492 O  OG1    . THR   B 1 257 ? 33.939  -16.230 63.489 1.00 98.20  ?  282 THR   B OG1    1 
ATOM   10493 C  CG2    . THR   B 1 257 ? 32.317  -14.905 64.708 1.00 97.88  ?  282 THR   B CG2    1 
ATOM   10494 H  H      . THR   B 1 257 ? 33.403  -14.387 62.029 1.00 116.59 ?  282 THR   B H      1 
ATOM   10495 H  HA     . THR   B 1 257 ? 34.119  -13.080 64.222 1.00 116.13 ?  282 THR   B HA     1 
ATOM   10496 H  HB     . THR   B 1 257 ? 34.282  -15.260 65.177 1.00 117.29 ?  282 THR   B HB     1 
ATOM   10497 H  HG1    . THR   B 1 257 ? 34.751  -16.353 63.311 1.00 117.84 ?  282 THR   B HG1    1 
ATOM   10498 H  HG21   . THR   B 1 257 ? 31.974  -15.701 65.143 1.00 117.44 ?  282 THR   B HG21   1 
ATOM   10499 H  HG22   . THR   B 1 257 ? 32.215  -14.149 65.307 1.00 117.44 ?  282 THR   B HG22   1 
ATOM   10500 H  HG23   . THR   B 1 257 ? 31.802  -14.740 63.902 1.00 117.44 ?  282 THR   B HG23   1 
ATOM   10501 N  N      . GLY   B 1 258 ? 36.425  -14.432 62.493 1.00 92.85  ?  283 GLY   B N      1 
ATOM   10502 C  CA     . GLY   B 1 258 ? 37.858  -14.367 62.282 1.00 89.87  ?  283 GLY   B CA     1 
ATOM   10503 C  C      . GLY   B 1 258 ? 38.548  -15.651 61.866 1.00 86.91  ?  283 GLY   B C      1 
ATOM   10504 O  O      . GLY   B 1 258 ? 39.739  -15.630 61.543 1.00 86.97  ?  283 GLY   B O      1 
ATOM   10505 H  H      . GLY   B 1 258 ? 35.988  -14.815 61.860 1.00 111.41 ?  283 GLY   B H      1 
ATOM   10506 H  HA2    . GLY   B 1 258 ? 38.033  -13.711 61.589 1.00 107.84 ?  283 GLY   B HA2    1 
ATOM   10507 H  HA3    . GLY   B 1 258 ? 38.274  -14.073 63.108 1.00 107.84 ?  283 GLY   B HA3    1 
ATOM   10508 N  N      . ASN   B 1 259 ? 37.832  -16.768 61.865 1.00 83.48  ?  284 ASN   B N      1 
ATOM   10509 C  CA     . ASN   B 1 259 ? 38.443  -18.048 61.541 1.00 79.54  ?  284 ASN   B CA     1 
ATOM   10510 C  C      . ASN   B 1 259 ? 38.270  -18.380 60.061 1.00 77.44  ?  284 ASN   B C      1 
ATOM   10511 O  O      . ASN   B 1 259 ? 37.417  -17.825 59.366 1.00 77.76  ?  284 ASN   B O      1 
ATOM   10512 C  CB     . ASN   B 1 259 ? 37.848  -19.164 62.400 1.00 77.79  ?  284 ASN   B CB     1 
ATOM   10513 C  CG     . ASN   B 1 259 ? 38.284  -19.074 63.848 1.00 77.33  ?  284 ASN   B CG     1 
ATOM   10514 O  OD1    . ASN   B 1 259 ? 39.309  -18.466 64.162 1.00 77.55  ?  284 ASN   B OD1    1 
ATOM   10515 N  ND2    . ASN   B 1 259 ? 37.510  -19.684 64.739 1.00 77.16  ?  284 ASN   B ND2    1 
ATOM   10516 H  H      . ASN   B 1 259 ? 36.993  -16.809 62.048 1.00 100.17 ?  284 ASN   B H      1 
ATOM   10517 H  HA     . ASN   B 1 259 ? 39.394  -17.997 61.726 1.00 95.44  ?  284 ASN   B HA     1 
ATOM   10518 H  HB2    . ASN   B 1 259 ? 36.880  -19.104 62.372 1.00 93.34  ?  284 ASN   B HB2    1 
ATOM   10519 H  HB3    . ASN   B 1 259 ? 38.137  -20.022 62.051 1.00 93.34  ?  284 ASN   B HB3    1 
ATOM   10520 H  HD21   . ASN   B 1 259 ? 37.716  -19.661 65.574 1.00 92.59  ?  284 ASN   B HD21   1 
ATOM   10521 H  HD22   . ASN   B 1 259 ? 36.804  -20.101 64.481 1.00 92.59  ?  284 ASN   B HD22   1 
ATOM   10522 N  N      . SER   B 1 260 ? 39.107  -19.299 59.584 1.00 74.52  ?  285 SER   B N      1 
ATOM   10523 C  CA     . SER   B 1 260 ? 39.067  -19.686 58.182 1.00 71.69  ?  285 SER   B CA     1 
ATOM   10524 C  C      . SER   B 1 260 ? 37.798  -20.478 57.885 1.00 67.71  ?  285 SER   B C      1 
ATOM   10525 O  O      . SER   B 1 260 ? 37.226  -21.136 58.761 1.00 68.02  ?  285 SER   B O      1 
ATOM   10526 C  CB     . SER   B 1 260 ? 40.298  -20.511 57.818 1.00 72.09  ?  285 SER   B CB     1 
ATOM   10527 O  OG     . SER   B 1 260 ? 40.437  -20.595 56.411 1.00 72.18  ?  285 SER   B OG     1 
ATOM   10528 H  H      . SER   B 1 260 ? 39.702  -19.710 60.050 1.00 89.42  ?  285 SER   B H      1 
ATOM   10529 H  HA     . SER   B 1 260 ? 39.067  -18.891 57.626 1.00 86.03  ?  285 SER   B HA     1 
ATOM   10530 H  HB2    . SER   B 1 260 ? 41.086  -20.086 58.190 1.00 86.50  ?  285 SER   B HB2    1 
ATOM   10531 H  HB3    . SER   B 1 260 ? 40.200  -21.405 58.181 1.00 86.50  ?  285 SER   B HB3    1 
ATOM   10532 H  HG     . SER   B 1 260 ? 41.138  -21.015 56.216 1.00 86.61  ?  285 SER   B HG     1 
ATOM   10533 N  N      . LEU   B 1 261 ? 37.357  -20.407 56.631 1.00 63.49  ?  286 LEU   B N      1 
ATOM   10534 C  CA     . LEU   B 1 261 ? 36.101  -21.038 56.253 1.00 59.96  ?  286 LEU   B CA     1 
ATOM   10535 C  C      . LEU   B 1 261 ? 36.257  -22.556 56.220 1.00 56.74  ?  286 LEU   B C      1 
ATOM   10536 O  O      . LEU   B 1 261 ? 37.227  -23.084 55.668 1.00 55.77  ?  286 LEU   B O      1 
ATOM   10537 C  CB     . LEU   B 1 261 ? 35.629  -20.525 54.893 1.00 60.62  ?  286 LEU   B CB     1 
ATOM   10538 C  CG     . LEU   B 1 261 ? 35.135  -19.078 54.803 1.00 61.79  ?  286 LEU   B CG     1 
ATOM   10539 C  CD1    . LEU   B 1 261 ? 34.468  -18.814 53.449 1.00 61.54  ?  286 LEU   B CD1    1 
ATOM   10540 C  CD2    . LEU   B 1 261 ? 34.174  -18.725 55.934 1.00 62.71  ?  286 LEU   B CD2    1 
ATOM   10541 H  H      . LEU   B 1 261 ? 37.763  -20.003 55.989 1.00 76.18  ?  286 LEU   B H      1 
ATOM   10542 H  HA     . LEU   B 1 261 ? 35.424  -20.814 56.910 1.00 71.95  ?  286 LEU   B HA     1 
ATOM   10543 H  HB2    . LEU   B 1 261 ? 36.371  -20.605 54.274 1.00 72.74  ?  286 LEU   B HB2    1 
ATOM   10544 H  HB3    . LEU   B 1 261 ? 34.894  -21.089 54.604 1.00 72.74  ?  286 LEU   B HB3    1 
ATOM   10545 H  HG     . LEU   B 1 261 ? 35.909  -18.500 54.890 1.00 74.14  ?  286 LEU   B HG     1 
ATOM   10546 H  HD11   . LEU   B 1 261 ? 34.172  -17.891 53.417 1.00 73.85  ?  286 LEU   B HD11   1 
ATOM   10547 H  HD12   . LEU   B 1 261 ? 35.113  -18.978 52.742 1.00 73.85  ?  286 LEU   B HD12   1 
ATOM   10548 H  HD13   . LEU   B 1 261 ? 33.709  -19.409 53.349 1.00 73.85  ?  286 LEU   B HD13   1 
ATOM   10549 H  HD21   . LEU   B 1 261 ? 33.784  -17.855 55.757 1.00 75.24  ?  286 LEU   B HD21   1 
ATOM   10550 H  HD22   . LEU   B 1 261 ? 33.477  -19.398 55.978 1.00 75.24  ?  286 LEU   B HD22   1 
ATOM   10551 H  HD23   . LEU   B 1 261 ? 34.665  -18.703 56.770 1.00 75.24  ?  286 LEU   B HD23   1 
ATOM   10552 N  N      . LYS   B 1 262 ? 35.307  -23.251 56.842 1.00 55.65  ?  287 LYS   B N      1 
ATOM   10553 C  CA     . LYS   B 1 262 ? 35.182  -24.698 56.721 1.00 53.74  ?  287 LYS   B CA     1 
ATOM   10554 C  C      . LYS   B 1 262 ? 34.449  -25.031 55.428 1.00 47.88  ?  287 LYS   B C      1 
ATOM   10555 O  O      . LYS   B 1 262 ? 33.421  -24.419 55.122 1.00 47.52  ?  287 LYS   B O      1 
ATOM   10556 C  CB     . LYS   B 1 262 ? 34.412  -25.244 57.922 1.00 56.85  ?  287 LYS   B CB     1 
ATOM   10557 C  CG     . LYS   B 1 262 ? 34.560  -26.727 58.188 1.00 59.46  ?  287 LYS   B CG     1 
ATOM   10558 C  CD     . LYS   B 1 262 ? 34.743  -26.986 59.689 1.00 60.75  ?  287 LYS   B CD     1 
ATOM   10559 C  CE     . LYS   B 1 262 ? 33.564  -26.481 60.529 1.00 60.83  ?  287 LYS   B CE     1 
ATOM   10560 N  NZ     . LYS   B 1 262 ? 33.796  -26.693 62.002 1.00 61.04  ?  287 LYS   B NZ     1 
ATOM   10561 H  H      . LYS   B 1 262 ? 34.711  -22.899 57.351 1.00 66.78  ?  287 LYS   B H      1 
ATOM   10562 H  HA     . LYS   B 1 262 ? 36.057  -25.117 56.699 1.00 64.49  ?  287 LYS   B HA     1 
ATOM   10563 H  HB2    . LYS   B 1 262 ? 34.720  -24.779 58.716 1.00 68.22  ?  287 LYS   B HB2    1 
ATOM   10564 H  HB3    . LYS   B 1 262 ? 33.468  -25.070 57.781 1.00 68.22  ?  287 LYS   B HB3    1 
ATOM   10565 H  HG2    . LYS   B 1 262 ? 33.763  -27.192 57.888 1.00 71.34  ?  287 LYS   B HG2    1 
ATOM   10566 H  HG3    . LYS   B 1 262 ? 35.338  -27.066 57.718 1.00 71.34  ?  287 LYS   B HG3    1 
ATOM   10567 H  HD2    . LYS   B 1 262 ? 34.828  -27.940 59.837 1.00 72.89  ?  287 LYS   B HD2    1 
ATOM   10568 H  HD3    . LYS   B 1 262 ? 35.543  -26.530 59.993 1.00 72.89  ?  287 LYS   B HD3    1 
ATOM   10569 H  HE2    . LYS   B 1 262 ? 33.444  -25.531 60.373 1.00 72.99  ?  287 LYS   B HE2    1 
ATOM   10570 H  HE3    . LYS   B 1 262 ? 32.761  -26.963 60.275 1.00 72.99  ?  287 LYS   B HE3    1 
ATOM   10571 H  HZ1    . LYS   B 1 262 ? 33.098  -26.395 62.466 1.00 73.24  ?  287 LYS   B HZ1    1 
ATOM   10572 H  HZ2    . LYS   B 1 262 ? 33.907  -27.559 62.171 1.00 73.24  ?  287 LYS   B HZ2    1 
ATOM   10573 H  HZ3    . LYS   B 1 262 ? 34.525  -26.252 62.262 1.00 73.24  ?  287 LYS   B HZ3    1 
ATOM   10574 N  N      . VAL   B 1 263 ? 34.974  -25.989 54.664 1.00 43.68  ?  288 VAL   B N      1 
ATOM   10575 C  CA     . VAL   B 1 263 ? 34.390  -26.386 53.387 1.00 40.80  ?  288 VAL   B CA     1 
ATOM   10576 C  C      . VAL   B 1 263 ? 34.082  -27.876 53.422 1.00 37.87  ?  288 VAL   B C      1 
ATOM   10577 O  O      . VAL   B 1 263 ? 34.956  -28.685 53.752 1.00 38.11  ?  288 VAL   B O      1 
ATOM   10578 C  CB     . VAL   B 1 263 ? 35.329  -26.053 52.204 1.00 40.73  ?  288 VAL   B CB     1 
ATOM   10579 C  CG1    . VAL   B 1 263 ? 34.699  -26.461 50.876 1.00 41.10  ?  288 VAL   B CG1    1 
ATOM   10580 C  CG2    . VAL   B 1 263 ? 35.677  -24.567 52.207 1.00 41.42  ?  288 VAL   B CG2    1 
ATOM   10581 H  H      . VAL   B 1 263 ? 35.682  -26.432 54.870 1.00 52.41  ?  288 VAL   B H      1 
ATOM   10582 H  HA     . VAL   B 1 263 ? 33.553  -25.910 53.265 1.00 48.95  ?  288 VAL   B HA     1 
ATOM   10583 H  HB     . VAL   B 1 263 ? 36.150  -26.559 52.306 1.00 48.87  ?  288 VAL   B HB     1 
ATOM   10584 H  HG11   . VAL   B 1 263 ? 35.221  -26.084 50.150 1.00 49.31  ?  288 VAL   B HG11   1 
ATOM   10585 H  HG12   . VAL   B 1 263 ? 34.695  -27.429 50.812 1.00 49.31  ?  288 VAL   B HG12   1 
ATOM   10586 H  HG13   . VAL   B 1 263 ? 33.790  -26.123 50.840 1.00 49.31  ?  288 VAL   B HG13   1 
ATOM   10587 H  HG21   . VAL   B 1 263 ? 36.223  -24.369 51.430 1.00 49.69  ?  288 VAL   B HG21   1 
ATOM   10588 H  HG22   . VAL   B 1 263 ? 34.856  -24.051 52.174 1.00 49.69  ?  288 VAL   B HG22   1 
ATOM   10589 H  HG23   . VAL   B 1 263 ? 36.167  -24.359 53.018 1.00 49.69  ?  288 VAL   B HG23   1 
ATOM   10590 N  N      . ILE   B 1 264 ? 32.830  -28.223 53.115 1.00 35.92  ?  289 ILE   B N      1 
ATOM   10591 C  CA     . ILE   B 1 264 ? 32.367  -29.600 52.982 1.00 35.53  ?  289 ILE   B CA     1 
ATOM   10592 C  C      . ILE   B 1 264 ? 32.326  -29.927 51.496 1.00 33.00  ?  289 ILE   B C      1 
ATOM   10593 O  O      . ILE   B 1 264 ? 31.810  -29.133 50.698 1.00 34.18  ?  289 ILE   B O      1 
ATOM   10594 C  CB     . ILE   B 1 264 ? 30.973  -29.774 53.607 1.00 37.75  ?  289 ILE   B CB     1 
ATOM   10595 C  CG1    . ILE   B 1 264 ? 30.891  -29.112 54.985 1.00 39.97  ?  289 ILE   B CG1    1 
ATOM   10596 C  CG2    . ILE   B 1 264 ? 30.622  -31.241 53.740 1.00 38.43  ?  289 ILE   B CG2    1 
ATOM   10597 C  CD1    . ILE   B 1 264 ? 32.018  -29.480 55.904 1.00 41.12  ?  289 ILE   B CD1    1 
ATOM   10598 H  H      . ILE   B 1 264 ? 32.205  -27.650 52.973 1.00 43.10  ?  289 ILE   B H      1 
ATOM   10599 H  HA     . ILE   B 1 264 ? 32.982  -30.201 53.432 1.00 42.63  ?  289 ILE   B HA     1 
ATOM   10600 H  HB     . ILE   B 1 264 ? 30.341  -29.340 53.012 1.00 45.30  ?  289 ILE   B HB     1 
ATOM   10601 H  HG12   . ILE   B 1 264 ? 30.907  -28.149 54.869 1.00 47.95  ?  289 ILE   B HG12   1 
ATOM   10602 H  HG13   . ILE   B 1 264 ? 30.063  -29.382 55.411 1.00 47.95  ?  289 ILE   B HG13   1 
ATOM   10603 H  HG21   . ILE   B 1 264 ? 29.721  -31.320 54.091 1.00 46.11  ?  289 ILE   B HG21   1 
ATOM   10604 H  HG22   . ILE   B 1 264 ? 30.674  -31.659 52.866 1.00 46.11  ?  289 ILE   B HG22   1 
ATOM   10605 H  HG23   . ILE   B 1 264 ? 31.251  -31.663 54.345 1.00 46.11  ?  289 ILE   B HG23   1 
ATOM   10606 H  HD11   . ILE   B 1 264 ? 31.809  -29.170 56.799 1.00 49.34  ?  289 ILE   B HD11   1 
ATOM   10607 H  HD12   . ILE   B 1 264 ? 32.124  -30.444 55.904 1.00 49.34  ?  289 ILE   B HD12   1 
ATOM   10608 H  HD13   . ILE   B 1 264 ? 32.833  -29.058 55.590 1.00 49.34  ?  289 ILE   B HD13   1 
ATOM   10609 N  N      . HIS   B 1 265 ? 32.828  -31.103 51.119 1.00 30.80  ?  290 HIS   B N      1 
ATOM   10610 C  CA     . HIS   B 1 265 ? 32.984  -31.463 49.716 1.00 31.08  ?  290 HIS   B CA     1 
ATOM   10611 C  C      . HIS   B 1 265 ? 32.612  -32.915 49.469 1.00 30.37  ?  290 HIS   B C      1 
ATOM   10612 O  O      . HIS   B 1 265 ? 32.932  -33.786 50.280 1.00 31.39  ?  290 HIS   B O      1 
ATOM   10613 C  CB     . HIS   B 1 265 ? 34.440  -31.220 49.281 1.00 33.19  ?  290 HIS   B CB     1 
ATOM   10614 C  CG     . HIS   B 1 265 ? 34.797  -31.830 47.966 1.00 35.02  ?  290 HIS   B CG     1 
ATOM   10615 N  ND1    . HIS   B 1 265 ? 35.641  -32.915 47.847 1.00 38.28  ?  290 HIS   B ND1    1 
ATOM   10616 C  CD2    . HIS   B 1 265 ? 34.429  -31.499 46.707 1.00 35.26  ?  290 HIS   B CD2    1 
ATOM   10617 C  CE1    . HIS   B 1 265 ? 35.771  -33.228 46.570 1.00 39.17  ?  290 HIS   B CE1    1 
ATOM   10618 N  NE2    . HIS   B 1 265 ? 35.048  -32.382 45.857 1.00 36.87  ?  290 HIS   B NE2    1 
ATOM   10619 H  H      . HIS   B 1 265 ? 33.086  -31.715 51.666 1.00 36.95  ?  290 HIS   B H      1 
ATOM   10620 H  HA     . HIS   B 1 265 ? 32.376  -30.931 49.178 1.00 37.29  ?  290 HIS   B HA     1 
ATOM   10621 H  HB2    . HIS   B 1 265 ? 34.588  -30.264 49.211 1.00 39.82  ?  290 HIS   B HB2    1 
ATOM   10622 H  HB3    . HIS   B 1 265 ? 35.031  -31.599 49.951 1.00 39.82  ?  290 HIS   B HB3    1 
ATOM   10623 H  HD2    . HIS   B 1 265 ? 33.863  -30.803 46.463 1.00 42.30  ?  290 HIS   B HD2    1 
ATOM   10624 H  HE1    . HIS   B 1 265 ? 36.284  -33.925 46.231 1.00 47.00  ?  290 HIS   B HE1    1 
ATOM   10625 H  HE2    . HIS   B 1 265 ? 34.977  -32.384 45.000 1.00 44.24  ?  290 HIS   B HE2    1 
ATOM   10626 N  N      . GLU   B 1 266 ? 31.954  -33.177 48.339 1.00 29.04  ?  291 GLU   B N      1 
ATOM   10627 C  CA     . GLU   B 1 266 ? 31.779  -34.546 47.864 1.00 29.31  ?  291 GLU   B CA     1 
ATOM   10628 C  C      . GLU   B 1 266 ? 31.715  -34.563 46.339 1.00 28.38  ?  291 GLU   B C      1 
ATOM   10629 O  O      . GLU   B 1 266 ? 30.955  -33.801 45.733 1.00 26.40  ?  291 GLU   B O      1 
ATOM   10630 C  CB     . GLU   B 1 266 ? 30.504  -35.201 48.441 1.00 30.10  ?  291 GLU   B CB     1 
ATOM   10631 C  CG     . GLU   B 1 266 ? 30.353  -36.668 48.025 1.00 31.21  ?  291 GLU   B CG     1 
ATOM   10632 C  CD     . GLU   B 1 266 ? 29.042  -37.349 48.437 1.00 35.54  ?  291 GLU   B CD     1 
ATOM   10633 O  OE1    . GLU   B 1 266 ? 28.214  -36.765 49.166 1.00 36.48  ?  291 GLU   B OE1    1 
ATOM   10634 O  OE2    . GLU   B 1 266 ? 28.838  -38.502 48.001 1.00 38.51  ?  291 GLU   B OE2    1 
ATOM   10635 H  H      . GLU   B 1 266 ? 31.601  -32.579 47.832 1.00 34.84  ?  291 GLU   B H      1 
ATOM   10636 H  HA     . GLU   B 1 266 ? 32.550  -35.062 48.147 1.00 35.17  ?  291 GLU   B HA     1 
ATOM   10637 H  HB2    . GLU   B 1 266 ? 30.541  -35.165 49.409 1.00 36.12  ?  291 GLU   B HB2    1 
ATOM   10638 H  HB3    . GLU   B 1 266 ? 29.727  -34.716 48.120 1.00 36.12  ?  291 GLU   B HB3    1 
ATOM   10639 H  HG2    . GLU   B 1 266 ? 30.410  -36.718 47.058 1.00 37.45  ?  291 GLU   B HG2    1 
ATOM   10640 H  HG3    . GLU   B 1 266 ? 31.077  -37.174 48.426 1.00 37.45  ?  291 GLU   B HG3    1 
ATOM   10641 N  N      . GLN   B 1 267 ? 32.514  -35.425 45.719 1.00 28.89  ?  292 GLN   B N      1 
ATOM   10642 C  CA     . GLN   B 1 267 ? 32.279  -35.815 44.330 1.00 30.36  ?  292 GLN   B CA     1 
ATOM   10643 C  C      . GLN   B 1 267 ? 31.323  -37.002 44.411 1.00 28.85  ?  292 GLN   B C      1 
ATOM   10644 O  O      . GLN   B 1 267 ? 31.724  -38.115 44.771 1.00 29.25  ?  292 GLN   B O      1 
ATOM   10645 C  CB     . GLN   B 1 267 ? 33.566  -36.154 43.594 1.00 33.54  ?  292 GLN   B CB     1 
ATOM   10646 C  CG     . GLN   B 1 267 ? 33.298  -36.484 42.123 1.00 36.33  ?  292 GLN   B CG     1 
ATOM   10647 C  CD     . GLN   B 1 267 ? 34.552  -36.512 41.276 1.00 40.94  ?  292 GLN   B CD     1 
ATOM   10648 O  OE1    . GLN   B 1 267 ? 34.574  -35.998 40.155 1.00 43.79  ?  292 GLN   B OE1    1 
ATOM   10649 N  NE2    . GLN   B 1 267 ? 35.602  -37.128 41.799 1.00 41.88  ?  292 GLN   B NE2    1 
ATOM   10650 H  H      . GLN   B 1 267 ? 33.199  -35.798 46.081 1.00 34.66  ?  292 GLN   B H      1 
ATOM   10651 H  HA     . GLN   B 1 267 ? 31.879  -35.085 43.832 1.00 36.43  ?  292 GLN   B HA     1 
ATOM   10652 H  HB2    . GLN   B 1 267 ? 34.168  -35.394 43.633 1.00 40.24  ?  292 GLN   B HB2    1 
ATOM   10653 H  HB3    . GLN   B 1 267 ? 33.980  -36.926 44.011 1.00 40.24  ?  292 GLN   B HB3    1 
ATOM   10654 H  HG2    . GLN   B 1 267 ? 32.883  -37.359 42.068 1.00 43.58  ?  292 GLN   B HG2    1 
ATOM   10655 H  HG3    . GLN   B 1 267 ? 32.705  -35.812 41.754 1.00 43.58  ?  292 GLN   B HG3    1 
ATOM   10656 H  HE21   . GLN   B 1 267 ? 35.546  -37.484 42.580 1.00 50.25  ?  292 GLN   B HE21   1 
ATOM   10657 H  HE22   . GLN   B 1 267 ? 36.339  -37.172 41.358 1.00 50.25  ?  292 GLN   B HE22   1 
ATOM   10658 N  N      . VAL   B 1 268 ? 30.040  -36.742 44.136 1.00 28.44  ?  293 VAL   B N      1 
ATOM   10659 C  CA     . VAL   B 1 268 ? 28.997  -37.733 44.385 1.00 29.11  ?  293 VAL   B CA     1 
ATOM   10660 C  C      . VAL   B 1 268 ? 29.069  -38.857 43.362 1.00 29.24  ?  293 VAL   B C      1 
ATOM   10661 O  O      . VAL   B 1 268 ? 28.948  -40.040 43.709 1.00 30.02  ?  293 VAL   B O      1 
ATOM   10662 C  CB     . VAL   B 1 268 ? 27.616  -37.049 44.381 1.00 29.22  ?  293 VAL   B CB     1 
ATOM   10663 C  CG1    . VAL   B 1 268 ? 26.514  -38.064 44.650 1.00 29.76  ?  293 VAL   B CG1    1 
ATOM   10664 C  CG2    . VAL   B 1 268 ? 27.583  -35.897 45.388 1.00 29.81  ?  293 VAL   B CG2    1 
ATOM   10665 H  H      . VAL   B 1 268 ? 29.751  -36.003 43.806 1.00 34.12  ?  293 VAL   B H      1 
ATOM   10666 H  HA     . VAL   B 1 268 ? 29.142  -38.125 45.261 1.00 34.93  ?  293 VAL   B HA     1 
ATOM   10667 H  HB     . VAL   B 1 268 ? 27.451  -36.670 43.504 1.00 35.05  ?  293 VAL   B HB     1 
ATOM   10668 H  HG11   . VAL   B 1 268 ? 25.685  -37.591 44.827 1.00 35.71  ?  293 VAL   B HG11   1 
ATOM   10669 H  HG12   . VAL   B 1 268 ? 26.410  -38.631 43.870 1.00 35.71  ?  293 VAL   B HG12   1 
ATOM   10670 H  HG13   . VAL   B 1 268 ? 26.759  -38.601 45.419 1.00 35.71  ?  293 VAL   B HG13   1 
ATOM   10671 H  HG21   . VAL   B 1 268 ? 26.676  -35.558 45.451 1.00 35.76  ?  293 VAL   B HG21   1 
ATOM   10672 H  HG22   . VAL   B 1 268 ? 27.874  -36.226 46.254 1.00 35.76  ?  293 VAL   B HG22   1 
ATOM   10673 H  HG23   . VAL   B 1 268 ? 28.179  -35.195 45.084 1.00 35.76  ?  293 VAL   B HG23   1 
ATOM   10674 N  N      . ASN   B 1 269 ? 29.254  -38.508 42.092 1.00 28.10  ?  294 ASN   B N      1 
ATOM   10675 C  CA     . ASN   B 1 269 ? 29.422  -39.469 41.008 1.00 28.52  ?  294 ASN   B CA     1 
ATOM   10676 C  C      . ASN   B 1 269 ? 30.060  -38.724 39.840 1.00 27.70  ?  294 ASN   B C      1 
ATOM   10677 O  O      . ASN   B 1 269 ? 30.502  -37.579 39.984 1.00 27.37  ?  294 ASN   B O      1 
ATOM   10678 C  CB     . ASN   B 1 269 ? 28.085  -40.118 40.636 1.00 27.50  ?  294 ASN   B CB     1 
ATOM   10679 C  CG     . ASN   B 1 269 ? 27.009  -39.098 40.320 1.00 26.02  ?  294 ASN   B CG     1 
ATOM   10680 O  OD1    . ASN   B 1 269 ? 27.223  -38.192 39.513 1.00 25.14  ?  294 ASN   B OD1    1 
ATOM   10681 N  ND2    . ASN   B 1 269 ? 25.844  -39.236 40.954 1.00 27.43  ?  294 ASN   B ND2    1 
ATOM   10682 H  H      . ASN   B 1 269 ? 29.288  -37.692 41.824 1.00 33.71  ?  294 ASN   B H      1 
ATOM   10683 H  HA     . ASN   B 1 269 ? 30.021  -40.177 41.292 1.00 34.21  ?  294 ASN   B HA     1 
ATOM   10684 H  HB2    . ASN   B 1 269 ? 28.211  -40.675 39.852 1.00 32.99  ?  294 ASN   B HB2    1 
ATOM   10685 H  HB3    . ASN   B 1 269 ? 27.777  -40.659 41.381 1.00 32.99  ?  294 ASN   B HB3    1 
ATOM   10686 H  HD21   . ASN   B 1 269 ? 25.205  -38.680 40.805 1.00 32.91  ?  294 ASN   B HD21   1 
ATOM   10687 H  HD22   . ASN   B 1 269 ? 25.732  -39.881 41.512 1.00 32.91  ?  294 ASN   B HD22   1 
ATOM   10688 N  N      . HIS   B 1 270 ? 30.101  -39.369 38.673 1.00 28.46  ?  295 HIS   B N      1 
ATOM   10689 C  CA     . HIS   B 1 270 ? 30.774  -38.792 37.517 1.00 29.30  ?  295 HIS   B CA     1 
ATOM   10690 C  C      . HIS   B 1 270 ? 30.057  -37.574 36.941 1.00 27.73  ?  295 HIS   B C      1 
ATOM   10691 O  O      . HIS   B 1 270 ? 30.623  -36.910 36.065 1.00 29.34  ?  295 HIS   B O      1 
ATOM   10692 C  CB     . HIS   B 1 270 ? 30.940  -39.861 36.427 1.00 33.34  ?  295 HIS   B CB     1 
ATOM   10693 C  CG     . HIS   B 1 270 ? 29.651  -40.346 35.835 1.00 37.66  ?  295 HIS   B CG     1 
ATOM   10694 N  ND1    . HIS   B 1 270 ? 28.523  -40.596 36.589 1.00 39.70  ?  295 HIS   B ND1    1 
ATOM   10695 C  CD2    . HIS   B 1 270 ? 29.316  -40.629 34.554 1.00 39.58  ?  295 HIS   B CD2    1 
ATOM   10696 C  CE1    . HIS   B 1 270 ? 27.549  -41.006 35.796 1.00 40.57  ?  295 HIS   B CE1    1 
ATOM   10697 N  NE2    . HIS   B 1 270 ? 28.004  -41.036 34.556 1.00 40.71  ?  295 HIS   B NE2    1 
ATOM   10698 H  H      . HIS   B 1 270 ? 29.748  -40.140 38.529 1.00 34.15  ?  295 HIS   B H      1 
ATOM   10699 H  HA     . HIS   B 1 270 ? 31.656  -38.499 37.793 1.00 35.15  ?  295 HIS   B HA     1 
ATOM   10700 H  HB2    . HIS   B 1 270 ? 31.473  -39.489 35.707 1.00 40.00  ?  295 HIS   B HB2    1 
ATOM   10701 H  HB3    . HIS   B 1 270 ? 31.393  -40.628 36.812 1.00 40.00  ?  295 HIS   B HB3    1 
ATOM   10702 H  HD2    . HIS   B 1 270 ? 29.871  -40.562 33.811 1.00 47.49  ?  295 HIS   B HD2    1 
ATOM   10703 H  HE1    . HIS   B 1 270 ? 26.689  -41.235 36.065 1.00 48.67  ?  295 HIS   B HE1    1 
ATOM   10704 H  HE2    . HIS   B 1 270 ? 27.552  -41.271 33.863 1.00 48.85  ?  295 HIS   B HE2    1 
ATOM   10705 N  N      . ARG   B 1 271 ? 28.855  -37.250 37.419 1.00 24.94  ?  296 ARG   B N      1 
ATOM   10706 C  CA     . ARG   B 1 271 ? 28.092  -36.132 36.885 1.00 22.50  ?  296 ARG   B CA     1 
ATOM   10707 C  C      . ARG   B 1 271 ? 27.757  -35.058 37.912 1.00 22.73  ?  296 ARG   B C      1 
ATOM   10708 O  O      . ARG   B 1 271 ? 27.140  -34.052 37.540 1.00 22.36  ?  296 ARG   B O      1 
ATOM   10709 C  CB     . ARG   B 1 271 ? 26.802  -36.655 36.232 1.00 22.10  ?  296 ARG   B CB     1 
ATOM   10710 C  CG     . ARG   B 1 271 ? 27.058  -37.408 34.926 1.00 23.80  ?  296 ARG   B CG     1 
ATOM   10711 C  CD     . ARG   B 1 271 ? 25.785  -37.652 34.155 1.00 25.28  ?  296 ARG   B CD     1 
ATOM   10712 N  NE     . ARG   B 1 271 ? 26.056  -38.273 32.863 1.00 25.91  ?  296 ARG   B NE     1 
ATOM   10713 C  CZ     . ARG   B 1 271 ? 25.116  -38.638 32.001 1.00 27.26  ?  296 ARG   B CZ     1 
ATOM   10714 N  NH1    . ARG   B 1 271 ? 23.836  -38.452 32.294 1.00 25.13  ?  296 ARG   B NH1    1 
ATOM   10715 N  NH2    . ARG   B 1 271 ? 25.460  -39.186 30.845 1.00 31.82  ?  296 ARG   B NH2    1 
ATOM   10716 H  H      . ARG   B 1 271 ? 28.460  -37.669 38.057 1.00 29.92  ?  296 ARG   B H      1 
ATOM   10717 H  HA     . ARG   B 1 271 ? 28.624  -35.696 36.201 1.00 27.00  ?  296 ARG   B HA     1 
ATOM   10718 H  HB2    . ARG   B 1 271 ? 26.362  -37.263 36.847 1.00 26.51  ?  296 ARG   B HB2    1 
ATOM   10719 H  HB3    . ARG   B 1 271 ? 26.221  -35.904 36.036 1.00 26.51  ?  296 ARG   B HB3    1 
ATOM   10720 H  HG2    . ARG   B 1 271 ? 27.655  -36.886 34.368 1.00 28.55  ?  296 ARG   B HG2    1 
ATOM   10721 H  HG3    . ARG   B 1 271 ? 27.460  -38.268 35.127 1.00 28.55  ?  296 ARG   B HG3    1 
ATOM   10722 H  HD2    . ARG   B 1 271 ? 25.209  -38.245 34.663 1.00 30.33  ?  296 ARG   B HD2    1 
ATOM   10723 H  HD3    . ARG   B 1 271 ? 25.336  -36.807 33.999 1.00 30.33  ?  296 ARG   B HD3    1 
ATOM   10724 H  HE     . ARG   B 1 271 ? 26.877  -38.410 32.646 1.00 31.08  ?  296 ARG   B HE     1 
ATOM   10725 H  HH11   . ARG   B 1 271 ? 23.614  -38.094 33.043 1.00 30.15  ?  296 ARG   B HH11   1 
ATOM   10726 H  HH12   . ARG   B 1 271 ? 23.228  -38.690 31.734 1.00 30.15  ?  296 ARG   B HH12   1 
ATOM   10727 H  HH21   . ARG   B 1 271 ? 26.291  -39.303 30.655 1.00 38.18  ?  296 ARG   B HH21   1 
ATOM   10728 H  HH22   . ARG   B 1 271 ? 24.853  -39.424 30.284 1.00 38.18  ?  296 ARG   B HH22   1 
ATOM   10729 N  N      . TRP   B 1 272 ? 28.174  -35.214 39.174 1.00 23.54  ?  297 TRP   B N      1 
ATOM   10730 C  CA     . TRP   B 1 272 ? 27.845  -34.256 40.221 1.00 21.99  ?  297 TRP   B CA     1 
ATOM   10731 C  C      . TRP   B 1 272 ? 28.984  -34.078 41.214 1.00 22.25  ?  297 TRP   B C      1 
ATOM   10732 O  O      . TRP   B 1 272 ? 29.496  -35.058 41.766 1.00 22.78  ?  297 TRP   B O      1 
ATOM   10733 C  CB     . TRP   B 1 272 ? 26.603  -34.696 41.012 1.00 21.74  ?  297 TRP   B CB     1 
ATOM   10734 C  CG     . TRP   B 1 272 ? 25.348  -34.710 40.237 1.00 20.89  ?  297 TRP   B CG     1 
ATOM   10735 C  CD1    . TRP   B 1 272 ? 24.904  -35.708 39.435 1.00 21.74  ?  297 TRP   B CD1    1 
ATOM   10736 C  CD2    . TRP   B 1 272 ? 24.349  -33.675 40.191 1.00 20.15  ?  297 TRP   B CD2    1 
ATOM   10737 N  NE1    . TRP   B 1 272 ? 23.689  -35.370 38.884 1.00 21.30  ?  297 TRP   B NE1    1 
ATOM   10738 C  CE2    . TRP   B 1 272 ? 23.328  -34.124 39.325 1.00 20.45  ?  297 TRP   B CE2    1 
ATOM   10739 C  CE3    . TRP   B 1 272 ? 24.219  -32.420 40.794 1.00 20.06  ?  297 TRP   B CE3    1 
ATOM   10740 C  CZ2    . TRP   B 1 272 ? 22.189  -33.357 39.045 1.00 20.63  ?  297 TRP   B CZ2    1 
ATOM   10741 C  CZ3    . TRP   B 1 272 ? 23.086  -31.662 40.522 1.00 20.41  ?  297 TRP   B CZ3    1 
ATOM   10742 C  CH2    . TRP   B 1 272 ? 22.085  -32.136 39.655 1.00 19.62  ?  297 TRP   B CH2    1 
ATOM   10743 H  H      . TRP   B 1 272 ? 28.653  -35.874 39.445 1.00 28.24  ?  297 TRP   B H      1 
ATOM   10744 H  HA     . TRP   B 1 272 ? 27.695  -33.405 39.780 1.00 26.38  ?  297 TRP   B HA     1 
ATOM   10745 H  HB2    . TRP   B 1 272 ? 26.752  -35.596 41.342 1.00 26.09  ?  297 TRP   B HB2    1 
ATOM   10746 H  HB3    . TRP   B 1 272 ? 26.480  -34.086 41.756 1.00 26.09  ?  297 TRP   B HB3    1 
ATOM   10747 H  HD1    . TRP   B 1 272 ? 25.356  -36.506 39.279 1.00 26.08  ?  297 TRP   B HD1    1 
ATOM   10748 H  HE1    . TRP   B 1 272 ? 23.230  -35.862 38.349 1.00 25.55  ?  297 TRP   B HE1    1 
ATOM   10749 H  HE3    . TRP   B 1 272 ? 24.878  -32.098 41.367 1.00 24.06  ?  297 TRP   B HE3    1 
ATOM   10750 H  HZ2    . TRP   B 1 272 ? 21.530  -33.666 38.467 1.00 24.75  ?  297 TRP   B HZ2    1 
ATOM   10751 H  HZ3    . TRP   B 1 272 ? 22.988  -30.828 40.920 1.00 24.48  ?  297 TRP   B HZ3    1 
ATOM   10752 H  HH2    . TRP   B 1 272 ? 21.336  -31.609 39.493 1.00 23.54  ?  297 TRP   B HH2    1 
ATOM   10753 N  N      . GLU   B 1 273 ? 29.328  -32.824 41.494 1.00 22.02  ?  298 GLU   B N      1 
ATOM   10754 C  CA     . GLU   B 1 273 ? 30.308  -32.480 42.519 1.00 22.87  ?  298 GLU   B CA     1 
ATOM   10755 C  C      . GLU   B 1 273 ? 29.808  -31.244 43.256 1.00 22.61  ?  298 GLU   B C      1 
ATOM   10756 O  O      . GLU   B 1 273 ? 29.305  -30.301 42.633 1.00 23.10  ?  298 GLU   B O      1 
ATOM   10757 C  CB     . GLU   B 1 273 ? 31.696  -32.263 41.890 1.00 24.44  ?  298 GLU   B CB     1 
ATOM   10758 C  CG     . GLU   B 1 273 ? 32.846  -32.175 42.897 1.00 26.88  ?  298 GLU   B CG     1 
ATOM   10759 C  CD     . GLU   B 1 273 ? 34.249  -32.297 42.279 1.00 29.83  ?  298 GLU   B CD     1 
ATOM   10760 O  OE1    . GLU   B 1 273 ? 34.403  -32.470 41.047 1.00 29.75  ?  298 GLU   B OE1    1 
ATOM   10761 O  OE2    . GLU   B 1 273 ? 35.211  -32.227 43.065 1.00 32.14  ?  298 GLU   B OE2    1 
ATOM   10762 H  H      . GLU   B 1 273 ? 28.998  -32.138 41.094 1.00 26.41  ?  298 GLU   B H      1 
ATOM   10763 H  HA     . GLU   B 1 273 ? 30.406  -33.186 43.177 1.00 27.43  ?  298 GLU   B HA     1 
ATOM   10764 H  HB2    . GLU   B 1 273 ? 31.884  -33.006 41.296 1.00 29.32  ?  298 GLU   B HB2    1 
ATOM   10765 H  HB3    . GLU   B 1 273 ? 31.681  -31.433 41.390 1.00 29.32  ?  298 GLU   B HB3    1 
ATOM   10766 H  HG2    . GLU   B 1 273 ? 32.799  -31.316 43.346 1.00 32.25  ?  298 GLU   B HG2    1 
ATOM   10767 H  HG3    . GLU   B 1 273 ? 32.748  -32.893 43.542 1.00 32.25  ?  298 GLU   B HG3    1 
ATOM   10768 N  N      . VAL   B 1 274 ? 29.934  -31.264 44.585 1.00 23.42  ?  299 VAL   B N      1 
ATOM   10769 C  CA     . VAL   B 1 274 ? 29.325  -30.257 45.444 1.00 23.74  ?  299 VAL   B CA     1 
ATOM   10770 C  C      . VAL   B 1 274 ? 30.302  -29.810 46.523 1.00 24.80  ?  299 VAL   B C      1 
ATOM   10771 O  O      . VAL   B 1 274 ? 30.968  -30.635 47.160 1.00 25.28  ?  299 VAL   B O      1 
ATOM   10772 C  CB     . VAL   B 1 274 ? 28.028  -30.793 46.100 1.00 25.15  ?  299 VAL   B CB     1 
ATOM   10773 C  CG1    . VAL   B 1 274 ? 27.428  -29.743 47.025 1.00 25.90  ?  299 VAL   B CG1    1 
ATOM   10774 C  CG2    . VAL   B 1 274 ? 27.022  -31.242 45.045 1.00 25.81  ?  299 VAL   B CG2    1 
ATOM   10775 H  H      . VAL   B 1 274 ? 30.376  -31.863 45.016 1.00 28.10  ?  299 VAL   B H      1 
ATOM   10776 H  HA     . VAL   B 1 274 ? 29.123  -29.482 44.897 1.00 28.48  ?  299 VAL   B HA     1 
ATOM   10777 H  HB     . VAL   B 1 274 ? 28.249  -31.573 46.633 1.00 30.17  ?  299 VAL   B HB     1 
ATOM   10778 H  HG11   . VAL   B 1 274 ? 26.520  -30.001 47.249 1.00 31.07  ?  299 VAL   B HG11   1 
ATOM   10779 H  HG12   . VAL   B 1 274 ? 27.964  -29.690 47.832 1.00 31.07  ?  299 VAL   B HG12   1 
ATOM   10780 H  HG13   . VAL   B 1 274 ? 27.426  -28.886 46.571 1.00 31.07  ?  299 VAL   B HG13   1 
ATOM   10781 H  HG21   . VAL   B 1 274 ? 26.207  -31.527 45.488 1.00 30.97  ?  299 VAL   B HG21   1 
ATOM   10782 H  HG22   . VAL   B 1 274 ? 26.833  -30.497 44.452 1.00 30.97  ?  299 VAL   B HG22   1 
ATOM   10783 H  HG23   . VAL   B 1 274 ? 27.400  -31.979 44.541 1.00 30.97  ?  299 VAL   B HG23   1 
ATOM   10784 N  N      . CYS   B 1 275 ? 30.367  -28.498 46.745 1.00 26.27  ?  300 CYS   B N      1 
ATOM   10785 C  CA     . CYS   B 1 275 ? 31.046  -27.937 47.905 1.00 27.27  ?  300 CYS   B CA     1 
ATOM   10786 C  C      . CYS   B 1 275 ? 30.083  -27.018 48.649 1.00 26.84  ?  300 CYS   B C      1 
ATOM   10787 O  O      . CYS   B 1 275 ? 29.254  -26.341 48.037 1.00 27.03  ?  300 CYS   B O      1 
ATOM   10788 C  CB     . CYS   B 1 275 ? 32.287  -27.128 47.530 1.00 29.71  ?  300 CYS   B CB     1 
ATOM   10789 S  SG     . CYS   B 1 275 ? 33.636  -28.044 46.761 1.00 32.77  ?  300 CYS   B SG     1 
ATOM   10790 H  H      . CYS   B 1 275 ? 30.018  -27.906 46.229 1.00 31.52  ?  300 CYS   B H      1 
ATOM   10791 H  HA     . CYS   B 1 275 ? 31.323  -28.666 48.481 1.00 32.71  ?  300 CYS   B HA     1 
ATOM   10792 H  HB2    . CYS   B 1 275 ? 32.018  -26.437 46.904 1.00 35.65  ?  300 CYS   B HB2    1 
ATOM   10793 H  HB3    . CYS   B 1 275 ? 32.640  -26.725 48.338 1.00 35.65  ?  300 CYS   B HB3    1 
ATOM   10794 H  HG     . CYS   B 1 275 ? 34.534  -27.287 46.518 1.00 39.32  ?  300 CYS   B HG     1 
ATOM   10795 N  N      . LEU   B 1 276 ? 30.223  -26.964 49.970 1.00 27.66  ?  301 LEU   B N      1 
ATOM   10796 C  CA     . LEU   B 1 276 ? 29.377  -26.117 50.798 1.00 28.25  ?  301 LEU   B CA     1 
ATOM   10797 C  C      . LEU   B 1 276 ? 30.234  -25.396 51.824 1.00 27.86  ?  301 LEU   B C      1 
ATOM   10798 O  O      . LEU   B 1 276 ? 31.075  -26.017 52.482 1.00 28.24  ?  301 LEU   B O      1 
ATOM   10799 C  CB     . LEU   B 1 276 ? 28.296  -26.936 51.515 1.00 29.41  ?  301 LEU   B CB     1 
ATOM   10800 C  CG     . LEU   B 1 276 ? 27.443  -26.198 52.548 1.00 31.55  ?  301 LEU   B CG     1 
ATOM   10801 C  CD1    . LEU   B 1 276 ? 26.502  -25.212 51.873 1.00 30.65  ?  301 LEU   B CD1    1 
ATOM   10802 C  CD2    . LEU   B 1 276 ? 26.661  -27.187 53.417 1.00 33.86  ?  301 LEU   B CD2    1 
ATOM   10803 H  H      . LEU   B 1 276 ? 30.808  -27.413 50.413 1.00 33.18  ?  301 LEU   B H      1 
ATOM   10804 H  HA     . LEU   B 1 276 ? 28.945  -25.455 50.235 1.00 33.90  ?  301 LEU   B HA     1 
ATOM   10805 H  HB2    . LEU   B 1 276 ? 27.690  -27.284 50.843 1.00 35.29  ?  301 LEU   B HB2    1 
ATOM   10806 H  HB3    . LEU   B 1 276 ? 28.733  -27.667 51.978 1.00 35.29  ?  301 LEU   B HB3    1 
ATOM   10807 H  HG     . LEU   B 1 276 ? 28.032  -25.692 53.130 1.00 37.85  ?  301 LEU   B HG     1 
ATOM   10808 H  HD11   . LEU   B 1 276 ? 25.972  -24.766 52.552 1.00 36.77  ?  301 LEU   B HD11   1 
ATOM   10809 H  HD12   . LEU   B 1 276 ? 27.027  -24.561 51.382 1.00 36.77  ?  301 LEU   B HD12   1 
ATOM   10810 H  HD13   . LEU   B 1 276 ? 25.921  -25.696 51.265 1.00 36.77  ?  301 LEU   B HD13   1 
ATOM   10811 H  HD21   . LEU   B 1 276 ? 26.084  -26.691 54.019 1.00 40.62  ?  301 LEU   B HD21   1 
ATOM   10812 H  HD22   . LEU   B 1 276 ? 26.127  -27.759 52.843 1.00 40.62  ?  301 LEU   B HD22   1 
ATOM   10813 H  HD23   . LEU   B 1 276 ? 27.288  -27.724 53.927 1.00 40.62  ?  301 LEU   B HD23   1 
ATOM   10814 N  N      . THR   B 1 277 ? 30.024  -24.091 51.956 1.00 28.62  ?  302 THR   B N      1 
ATOM   10815 C  CA     . THR   B 1 277 ? 30.599  -23.332 53.054 1.00 30.17  ?  302 THR   B CA     1 
ATOM   10816 C  C      . THR   B 1 277 ? 29.557  -22.315 53.512 1.00 31.52  ?  302 THR   B C      1 
ATOM   10817 O  O      . THR   B 1 277 ? 28.405  -22.335 53.068 1.00 31.04  ?  302 THR   B O      1 
ATOM   10818 C  CB     . THR   B 1 277 ? 31.927  -22.674 52.648 1.00 32.17  ?  302 THR   B CB     1 
ATOM   10819 O  OG1    . THR   B 1 277 ? 32.578  -22.161 53.819 1.00 33.24  ?  302 THR   B OG1    1 
ATOM   10820 C  CG2    . THR   B 1 277 ? 31.705  -21.549 51.642 1.00 32.50  ?  302 THR   B CG2    1 
ATOM   10821 H  H      . THR   B 1 277 ? 29.547  -23.621 51.416 1.00 34.34  ?  302 THR   B H      1 
ATOM   10822 H  HA     . THR   B 1 277 ? 30.785  -23.942 53.785 1.00 36.20  ?  302 THR   B HA     1 
ATOM   10823 H  HB     . THR   B 1 277 ? 32.496  -23.334 52.223 1.00 38.60  ?  302 THR   B HB     1 
ATOM   10824 H  HG1    . THR   B 1 277 ? 32.728  -22.785 54.361 1.00 39.89  ?  302 THR   B HG1    1 
ATOM   10825 H  HG21   . THR   B 1 277 ? 32.554  -21.267 51.267 1.00 38.99  ?  302 THR   B HG21   1 
ATOM   10826 H  HG22   . THR   B 1 277 ? 31.129  -21.855 50.924 1.00 38.99  ?  302 THR   B HG22   1 
ATOM   10827 H  HG23   . THR   B 1 277 ? 31.287  -20.791 52.080 1.00 38.99  ?  302 THR   B HG23   1 
ATOM   10828 N  N      . MET   B 1 278 ? 29.959  -21.423 54.417 1.00 35.54  ?  303 MET   B N      1 
ATOM   10829 C  CA     . MET   B 1 278 ? 29.046  -20.438 54.974 1.00 38.64  ?  303 MET   B CA     1 
ATOM   10830 C  C      . MET   B 1 278 ? 29.120  -19.130 54.200 1.00 35.56  ?  303 MET   B C      1 
ATOM   10831 O  O      . MET   B 1 278 ? 30.160  -18.769 53.638 1.00 36.39  ?  303 MET   B O      1 
ATOM   10832 C  CB     . MET   B 1 278 ? 29.350  -20.170 56.451 1.00 44.75  ?  303 MET   B CB     1 
ATOM   10833 C  CG     . MET   B 1 278 ? 28.674  -21.137 57.420 1.00 51.69  ?  303 MET   B CG     1 
ATOM   10834 S  SD     . MET   B 1 278 ? 28.822  -20.605 59.142 1.00 59.00  ?  303 MET   B SD     1 
ATOM   10835 C  CE     . MET   B 1 278 ? 28.107  -21.998 60.013 1.00 60.86  ?  303 MET   B CE     1 
ATOM   10836 H  H      . MET   B 1 278 ? 30.761  -21.371 54.723 1.00 42.64  ?  303 MET   B H      1 
ATOM   10837 H  HA     . MET   B 1 278 ? 28.146  -20.794 54.915 1.00 46.36  ?  303 MET   B HA     1 
ATOM   10838 H  HB2    . MET   B 1 278 ? 30.308  -20.241 56.588 1.00 53.69  ?  303 MET   B HB2    1 
ATOM   10839 H  HB3    . MET   B 1 278 ? 29.049  -19.275 56.672 1.00 53.69  ?  303 MET   B HB3    1 
ATOM   10840 H  HG2    . MET   B 1 278 ? 27.730  -21.196 57.203 1.00 62.03  ?  303 MET   B HG2    1 
ATOM   10841 H  HG3    . MET   B 1 278 ? 29.088  -22.010 57.338 1.00 62.03  ?  303 MET   B HG3    1 
ATOM   10842 H  HE1    . MET   B 1 278 ? 27.154  -21.848 60.120 1.00 73.03  ?  303 MET   B HE1    1 
ATOM   10843 H  HE2    . MET   B 1 278 ? 28.259  -22.805 59.497 1.00 73.03  ?  303 MET   B HE2    1 
ATOM   10844 H  HE3    . MET   B 1 278 ? 28.529  -22.077 60.883 1.00 73.03  ?  303 MET   B HE3    1 
ATOM   10845 N  N      . SER   B 1 279 ? 27.995  -18.423 54.178 1.00 32.45  ?  304 SER   B N      1 
ATOM   10846 C  CA     . SER   B 1 279 ? 27.887  -17.126 53.539 1.00 32.48  ?  304 SER   B CA     1 
ATOM   10847 C  C      . SER   B 1 279 ? 27.543  -16.065 54.571 1.00 34.54  ?  304 SER   B C      1 
ATOM   10848 O  O      . SER   B 1 279 ? 26.757  -16.319 55.489 1.00 34.70  ?  304 SER   B O      1 
ATOM   10849 C  CB     . SER   B 1 279 ? 26.805  -17.116 52.462 1.00 30.78  ?  304 SER   B CB     1 
ATOM   10850 O  OG     . SER   B 1 279 ? 26.583  -15.783 52.033 1.00 30.57  ?  304 SER   B OG     1 
ATOM   10851 H  H      . SER   B 1 279 ? 27.260  -18.687 54.540 1.00 38.93  ?  304 SER   B H      1 
ATOM   10852 H  HA     . SER   B 1 279 ? 28.741  -16.913 53.131 1.00 38.97  ?  304 SER   B HA     1 
ATOM   10853 H  HB2    . SER   B 1 279 ? 27.097  -17.653 51.709 1.00 36.93  ?  304 SER   B HB2    1 
ATOM   10854 H  HB3    . SER   B 1 279 ? 25.983  -17.478 52.829 1.00 36.93  ?  304 SER   B HB3    1 
ATOM   10855 H  HG     . SER   B 1 279 ? 26.016  -15.771 51.413 1.00 36.68  ?  304 SER   B HG     1 
ATOM   10856 N  N      . GLU   B 1 280 ? 28.117  -14.873 54.403 1.00 35.83  ?  305 GLU   B N      1 
ATOM   10857 C  CA     . GLU   B 1 280 ? 27.735  -13.697 55.171 1.00 38.44  ?  305 GLU   B CA     1 
ATOM   10858 C  C      . GLU   B 1 280 ? 26.868  -12.737 54.365 1.00 37.61  ?  305 GLU   B C      1 
ATOM   10859 O  O      . GLU   B 1 280 ? 26.535  -11.650 54.858 1.00 38.74  ?  305 GLU   B O      1 
ATOM   10860 C  CB     . GLU   B 1 280 ? 28.986  -12.973 55.674 1.00 43.35  ?  305 GLU   B CB     1 
ATOM   10861 C  CG     . GLU   B 1 280 ? 29.967  -13.887 56.392 1.00 49.59  ?  305 GLU   B CG     1 
ATOM   10862 C  CD     . GLU   B 1 280 ? 29.338  -14.595 57.579 1.00 55.54  ?  305 GLU   B CD     1 
ATOM   10863 O  OE1    . GLU   B 1 280 ? 28.560  -13.947 58.314 1.00 58.07  ?  305 GLU   B OE1    1 
ATOM   10864 O  OE2    . GLU   B 1 280 ? 29.616  -15.799 57.773 1.00 58.08  ?  305 GLU   B OE2    1 
ATOM   10865 H  H      . GLU   B 1 280 ? 28.744  -14.721 53.835 1.00 42.99  ?  305 GLU   B H      1 
ATOM   10866 H  HA     . GLU   B 1 280 ? 27.225  -13.982 55.946 1.00 46.12  ?  305 GLU   B HA     1 
ATOM   10867 H  HB2    . GLU   B 1 280 ? 29.446  -12.580 54.915 1.00 52.01  ?  305 GLU   B HB2    1 
ATOM   10868 H  HB3    . GLU   B 1 280 ? 28.717  -12.278 56.295 1.00 52.01  ?  305 GLU   B HB3    1 
ATOM   10869 H  HG2    . GLU   B 1 280 ? 30.284  -14.562 55.772 1.00 59.50  ?  305 GLU   B HG2    1 
ATOM   10870 H  HG3    . GLU   B 1 280 ? 30.712  -13.358 56.718 1.00 59.50  ?  305 GLU   B HG3    1 
ATOM   10871 N  N      . LYS   B 1 281 ? 26.489  -13.121 53.140 1.00 35.76  ?  306 LYS   B N      1 
ATOM   10872 C  CA     . LYS   B 1 281 ? 25.762  -12.250 52.226 1.00 35.07  ?  306 LYS   B CA     1 
ATOM   10873 C  C      . LYS   B 1 281 ? 24.374  -12.777 51.872 1.00 31.23  ?  306 LYS   B C      1 
ATOM   10874 O  O      . LYS   B 1 281 ? 23.804  -12.356 50.863 1.00 31.35  ?  306 LYS   B O      1 
ATOM   10875 C  CB     . LYS   B 1 281 ? 26.555  -12.057 50.930 1.00 38.27  ?  306 LYS   B CB     1 
ATOM   10876 C  CG     . LYS   B 1 281 ? 27.902  -11.396 51.075 1.00 42.28  ?  306 LYS   B CG     1 
ATOM   10877 C  CD     . LYS   B 1 281 ? 28.611  -11.362 49.727 1.00 45.32  ?  306 LYS   B CD     1 
ATOM   10878 C  CE     . LYS   B 1 281 ? 29.965  -10.684 49.823 1.00 47.79  ?  306 LYS   B CE     1 
ATOM   10879 N  NZ     . LYS   B 1 281 ? 30.939  -11.301 48.879 1.00 49.78  ?  306 LYS   B NZ     1 
ATOM   10880 H  H      . LYS   B 1 281 ? 26.647  -13.901 52.814 1.00 42.91  ?  306 LYS   B H      1 
ATOM   10881 H  HA     . LYS   B 1 281 ? 25.654  -11.396 52.671 1.00 42.08  ?  306 LYS   B HA     1 
ATOM   10882 H  HB2    . LYS   B 1 281 ? 26.704  -12.929 50.532 1.00 45.92  ?  306 LYS   B HB2    1 
ATOM   10883 H  HB3    . LYS   B 1 281 ? 26.027  -11.505 50.331 1.00 45.92  ?  306 LYS   B HB3    1 
ATOM   10884 H  HG2    . LYS   B 1 281 ? 27.788  -10.486 51.390 1.00 50.73  ?  306 LYS   B HG2    1 
ATOM   10885 H  HG3    . LYS   B 1 281 ? 28.447  -11.898 51.701 1.00 50.73  ?  306 LYS   B HG3    1 
ATOM   10886 H  HD2    . LYS   B 1 281 ? 28.747  -12.270 49.413 1.00 54.38  ?  306 LYS   B HD2    1 
ATOM   10887 H  HD3    . LYS   B 1 281 ? 28.068  -10.870 49.091 1.00 54.38  ?  306 LYS   B HD3    1 
ATOM   10888 H  HE2    . LYS   B 1 281 ? 29.872  -9.744  49.599 1.00 57.35  ?  306 LYS   B HE2    1 
ATOM   10889 H  HE3    . LYS   B 1 281 ? 30.310  -10.777 50.725 1.00 57.35  ?  306 LYS   B HE3    1 
ATOM   10890 H  HZ1    . LYS   B 1 281 ? 31.725  -10.889 48.939 1.00 59.73  ?  306 LYS   B HZ1    1 
ATOM   10891 H  HZ2    . LYS   B 1 281 ? 31.048  -12.162 49.075 1.00 59.73  ?  306 LYS   B HZ2    1 
ATOM   10892 H  HZ3    . LYS   B 1 281 ? 30.639  -11.231 48.044 1.00 59.73  ?  306 LYS   B HZ3    1 
ATOM   10893 N  N      . GLY   B 1 282 ? 23.811  -13.677 52.674 1.00 29.05  ?  307 GLY   B N      1 
ATOM   10894 C  CA     . GLY   B 1 282 ? 22.603  -14.372 52.278 1.00 26.99  ?  307 GLY   B CA     1 
ATOM   10895 C  C      . GLY   B 1 282 ? 22.967  -15.567 51.421 1.00 25.22  ?  307 GLY   B C      1 
ATOM   10896 O  O      . GLY   B 1 282 ? 24.137  -15.858 51.176 1.00 25.66  ?  307 GLY   B O      1 
ATOM   10897 H  H      . GLY   B 1 282 ? 24.113  -13.899 53.448 1.00 34.85  ?  307 GLY   B H      1 
ATOM   10898 H  HA2    . GLY   B 1 282 ? 22.123  -14.678 53.063 1.00 32.38  ?  307 GLY   B HA2    1 
ATOM   10899 H  HA3    . GLY   B 1 282 ? 22.029  -13.778 51.769 1.00 32.38  ?  307 GLY   B HA3    1 
ATOM   10900 N  N      . PHE   B 1 283 ? 21.948  -16.288 50.968 1.00 24.07  ?  308 PHE   B N      1 
ATOM   10901 C  CA     . PHE   B 1 283 ? 22.202  -17.438 50.113 1.00 24.01  ?  308 PHE   B CA     1 
ATOM   10902 C  C      . PHE   B 1 283 ? 23.043  -17.046 48.901 1.00 23.90  ?  308 PHE   B C      1 
ATOM   10903 O  O      . PHE   B 1 283 ? 22.750  -16.061 48.219 1.00 25.62  ?  308 PHE   B O      1 
ATOM   10904 C  CB     . PHE   B 1 283 ? 20.884  -18.069 49.646 1.00 24.38  ?  308 PHE   B CB     1 
ATOM   10905 C  CG     . PHE   B 1 283 ? 21.086  -19.294 48.812 1.00 23.36  ?  308 PHE   B CG     1 
ATOM   10906 C  CD1    . PHE   B 1 283 ? 21.648  -20.433 49.372 1.00 23.93  ?  308 PHE   B CD1    1 
ATOM   10907 C  CD2    . PHE   B 1 283 ? 20.740  -19.312 47.469 1.00 24.05  ?  308 PHE   B CD2    1 
ATOM   10908 C  CE1    . PHE   B 1 283 ? 21.854  -21.566 48.614 1.00 23.95  ?  308 PHE   B CE1    1 
ATOM   10909 C  CE2    . PHE   B 1 283 ? 20.951  -20.439 46.709 1.00 23.23  ?  308 PHE   B CE2    1 
ATOM   10910 C  CZ     . PHE   B 1 283 ? 21.512  -21.569 47.284 1.00 22.30  ?  308 PHE   B CZ     1 
ATOM   10911 H  H      . PHE   B 1 283 ? 21.119  -16.135 51.137 1.00 28.88  ?  308 PHE   B H      1 
ATOM   10912 H  HA     . PHE   B 1 283 ? 22.690  -18.098 50.630 1.00 28.80  ?  308 PHE   B HA     1 
ATOM   10913 H  HB2    . PHE   B 1 283 ? 20.362  -18.319 50.425 1.00 29.25  ?  308 PHE   B HB2    1 
ATOM   10914 H  HB3    . PHE   B 1 283 ? 20.397  -17.421 49.114 1.00 29.25  ?  308 PHE   B HB3    1 
ATOM   10915 H  HD1    . PHE   B 1 283 ? 21.889  -20.431 50.270 1.00 28.70  ?  308 PHE   B HD1    1 
ATOM   10916 H  HD2    . PHE   B 1 283 ? 20.362  -18.557 47.079 1.00 28.85  ?  308 PHE   B HD2    1 
ATOM   10917 H  HE1    . PHE   B 1 283 ? 22.223  -22.326 49.003 1.00 28.73  ?  308 PHE   B HE1    1 
ATOM   10918 H  HE2    . PHE   B 1 283 ? 20.718  -20.443 45.809 1.00 27.87  ?  308 PHE   B HE2    1 
ATOM   10919 H  HZ     . PHE   B 1 283 ? 21.656  -22.329 46.768 1.00 26.75  ?  308 PHE   B HZ     1 
ATOM   10920 N  N      . GLN   B 1 284 ? 24.084  -17.841 48.633 1.00 23.71  ?  309 GLN   B N      1 
ATOM   10921 C  CA     . GLN   B 1 284 ? 24.918  -17.683 47.451 1.00 22.95  ?  309 GLN   B CA     1 
ATOM   10922 C  C      . GLN   B 1 284 ? 25.084  -19.038 46.786 1.00 21.65  ?  309 GLN   B C      1 
ATOM   10923 O  O      . GLN   B 1 284 ? 25.223  -20.057 47.469 1.00 22.53  ?  309 GLN   B O      1 
ATOM   10924 C  CB     . GLN   B 1 284 ? 26.318  -17.148 47.767 1.00 25.34  ?  309 GLN   B CB     1 
ATOM   10925 C  CG     . GLN   B 1 284 ? 26.390  -15.749 48.299 1.00 27.18  ?  309 GLN   B CG     1 
ATOM   10926 C  CD     . GLN   B 1 284 ? 27.829  -15.311 48.453 1.00 27.94  ?  309 GLN   B CD     1 
ATOM   10927 O  OE1    . GLN   B 1 284 ? 28.496  -14.978 47.473 1.00 28.90  ?  309 GLN   B OE1    1 
ATOM   10928 N  NE2    . GLN   B 1 284 ? 28.326  -15.344 49.682 1.00 28.28  ?  309 GLN   B NE2    1 
ATOM   10929 H  H      . GLN   B 1 284 ? 24.329  -18.493 49.137 1.00 28.45  ?  309 GLN   B H      1 
ATOM   10930 H  HA     . GLN   B 1 284 ? 24.478  -17.055 46.857 1.00 27.54  ?  309 GLN   B HA     1 
ATOM   10931 H  HB2    . GLN   B 1 284 ? 26.719  -17.727 48.433 1.00 30.40  ?  309 GLN   B HB2    1 
ATOM   10932 H  HB3    . GLN   B 1 284 ? 26.841  -17.169 46.950 1.00 30.40  ?  309 GLN   B HB3    1 
ATOM   10933 H  HG2    . GLN   B 1 284 ? 25.947  -15.144 47.683 1.00 32.61  ?  309 GLN   B HG2    1 
ATOM   10934 H  HG3    . GLN   B 1 284 ? 25.960  -15.710 49.168 1.00 32.61  ?  309 GLN   B HG3    1 
ATOM   10935 H  HE21   . GLN   B 1 284 ? 27.835  -15.605 50.338 1.00 33.93  ?  309 GLN   B HE21   1 
ATOM   10936 H  HE22   . GLN   B 1 284 ? 29.140  -15.104 49.823 1.00 33.93  ?  309 GLN   B HE22   1 
ATOM   10937 N  N      . GLN   B 1 285 ? 25.107  -19.046 45.461 1.00 19.89  ?  310 GLN   B N      1 
ATOM   10938 C  CA     . GLN   B 1 285 ? 25.398  -20.255 44.710 1.00 19.08  ?  310 GLN   B CA     1 
ATOM   10939 C  C      . GLN   B 1 285 ? 26.287  -19.898 43.532 1.00 19.20  ?  310 GLN   B C      1 
ATOM   10940 O  O      . GLN   B 1 285 ? 26.061  -18.896 42.849 1.00 20.00  ?  310 GLN   B O      1 
ATOM   10941 C  CB     . GLN   B 1 285 ? 24.108  -20.944 44.234 1.00 19.14  ?  310 GLN   B CB     1 
ATOM   10942 C  CG     . GLN   B 1 285 ? 23.251  -20.116 43.289 1.00 19.40  ?  310 GLN   B CG     1 
ATOM   10943 C  CD     . GLN   B 1 285 ? 23.669  -20.274 41.839 1.00 18.84  ?  310 GLN   B CD     1 
ATOM   10944 O  OE1    . GLN   B 1 285 ? 24.356  -21.227 41.488 1.00 20.40  ?  310 GLN   B OE1    1 
ATOM   10945 N  NE2    . GLN   B 1 285 ? 23.236  -19.352 40.989 1.00 18.56  ?  310 GLN   B NE2    1 
ATOM   10946 H  H      . GLN   B 1 285 ? 24.956  -18.356 44.970 1.00 23.86  ?  310 GLN   B H      1 
ATOM   10947 H  HA     . GLN   B 1 285 ? 25.878  -20.889 45.265 1.00 22.89  ?  310 GLN   B HA     1 
ATOM   10948 H  HB2    . GLN   B 1 285 ? 24.349  -21.761 43.769 1.00 22.96  ?  310 GLN   B HB2    1 
ATOM   10949 H  HB3    . GLN   B 1 285 ? 23.567  -21.153 45.012 1.00 22.96  ?  310 GLN   B HB3    1 
ATOM   10950 H  HG2    . GLN   B 1 285 ? 22.327  -20.399 43.368 1.00 23.28  ?  310 GLN   B HG2    1 
ATOM   10951 H  HG3    . GLN   B 1 285 ? 23.333  -19.179 43.525 1.00 23.28  ?  310 GLN   B HG3    1 
ATOM   10952 H  HE21   . GLN   B 1 285 ? 22.744  -18.705 41.271 1.00 22.26  ?  310 GLN   B HE21   1 
ATOM   10953 H  HE22   . GLN   B 1 285 ? 23.448  -19.401 40.157 1.00 22.26  ?  310 GLN   B HE22   1 
ATOM   10954 N  N      . ILE   B 1 286 ? 27.312  -20.716 43.317 1.00 19.25  ?  311 ILE   B N      1 
ATOM   10955 C  CA     . ILE   B 1 286 ? 28.073  -20.743 42.072 1.00 19.27  ?  311 ILE   B CA     1 
ATOM   10956 C  C      . ILE   B 1 286 ? 27.876  -22.125 41.471 1.00 19.16  ?  311 ILE   B C      1 
ATOM   10957 O  O      . ILE   B 1 286 ? 28.179  -23.136 42.119 1.00 20.58  ?  311 ILE   B O      1 
ATOM   10958 C  CB     . ILE   B 1 286 ? 29.557  -20.406 42.304 1.00 20.55  ?  311 ILE   B CB     1 
ATOM   10959 C  CG1    . ILE   B 1 286 ? 29.676  -18.909 42.640 1.00 22.93  ?  311 ILE   B CG1    1 
ATOM   10960 C  CG2    . ILE   B 1 286 ? 30.397  -20.810 41.104 1.00 20.42  ?  311 ILE   B CG2    1 
ATOM   10961 C  CD1    . ILE   B 1 286 ? 31.069  -18.447 42.977 1.00 25.91  ?  311 ILE   B CD1    1 
ATOM   10962 H  H      . ILE   B 1 286 ? 27.595  -21.284 43.897 1.00 23.10  ?  311 ILE   B H      1 
ATOM   10963 H  HA     . ILE   B 1 286 ? 27.730  -20.089 41.443 1.00 23.11  ?  311 ILE   B HA     1 
ATOM   10964 H  HB     . ILE   B 1 286 ? 29.901  -20.913 43.055 1.00 24.65  ?  311 ILE   B HB     1 
ATOM   10965 H  HG12   . ILE   B 1 286 ? 29.377  -18.396 41.873 1.00 27.51  ?  311 ILE   B HG12   1 
ATOM   10966 H  HG13   . ILE   B 1 286 ? 29.113  -18.719 43.406 1.00 27.51  ?  311 ILE   B HG13   1 
ATOM   10967 H  HG21   . ILE   B 1 286 ? 31.278  -20.413 41.188 1.00 24.50  ?  311 ILE   B HG21   1 
ATOM   10968 H  HG22   . ILE   B 1 286 ? 30.471  -21.777 41.081 1.00 24.50  ?  311 ILE   B HG22   1 
ATOM   10969 H  HG23   . ILE   B 1 286 ? 29.966  -20.491 40.295 1.00 24.50  ?  311 ILE   B HG23   1 
ATOM   10970 H  HD11   . ILE   B 1 286 ? 31.023  -17.557 43.359 1.00 31.08  ?  311 ILE   B HD11   1 
ATOM   10971 H  HD12   . ILE   B 1 286 ? 31.459  -19.062 43.618 1.00 31.08  ?  311 ILE   B HD12   1 
ATOM   10972 H  HD13   . ILE   B 1 286 ? 31.602  -18.433 42.167 1.00 31.08  ?  311 ILE   B HD13   1 
ATOM   10973 N  N      . SER   B 1 287 ? 27.325  -22.179 40.261 1.00 17.51  ?  312 SER   B N      1 
ATOM   10974 C  CA     . SER   B 1 287 ? 26.978  -23.468 39.681 1.00 17.10  ?  312 SER   B CA     1 
ATOM   10975 C  C      . SER   B 1 287 ? 27.142  -23.458 38.170 1.00 16.37  ?  312 SER   B C      1 
ATOM   10976 O  O      . SER   B 1 287 ? 27.123  -22.411 37.515 1.00 17.52  ?  312 SER   B O      1 
ATOM   10977 C  CB     . SER   B 1 287 ? 25.539  -23.870 40.060 1.00 17.11  ?  312 SER   B CB     1 
ATOM   10978 O  OG     . SER   B 1 287 ? 24.577  -22.984 39.506 1.00 18.57  ?  312 SER   B OG     1 
ATOM   10979 H  H      . SER   B 1 287 ? 27.148  -21.496 39.768 1.00 21.01  ?  312 SER   B H      1 
ATOM   10980 H  HA     . SER   B 1 287 ? 27.602  -24.129 40.020 1.00 20.51  ?  312 SER   B HA     1 
ATOM   10981 H  HB2    . SER   B 1 287 ? 25.367  -24.764 39.726 1.00 20.53  ?  312 SER   B HB2    1 
ATOM   10982 H  HB3    . SER   B 1 287 ? 25.456  -23.855 41.026 1.00 20.53  ?  312 SER   B HB3    1 
ATOM   10983 H  HG     . SER   B 1 287 ? 24.713  -22.203 39.783 1.00 22.27  ?  312 SER   B HG     1 
ATOM   10984 N  N      . PHE   B 1 288 ? 27.324  -24.674 37.642 1.00 17.74  ?  313 PHE   B N      1 
ATOM   10985 C  CA     . PHE   B 1 288 ? 27.498  -24.951 36.222 1.00 17.35  ?  313 PHE   B CA     1 
ATOM   10986 C  C      . PHE   B 1 288 ? 26.670  -26.167 35.832 1.00 16.94  ?  313 PHE   B C      1 
ATOM   10987 O  O      . PHE   B 1 288 ? 26.614  -27.166 36.566 1.00 19.24  ?  313 PHE   B O      1 
ATOM   10988 C  CB     . PHE   B 1 288 ? 28.998  -25.184 35.875 1.00 19.36  ?  313 PHE   B CB     1 
ATOM   10989 C  CG     . PHE   B 1 288 ? 29.882  -24.079 36.374 1.00 20.45  ?  313 PHE   B CG     1 
ATOM   10990 C  CD1    . PHE   B 1 288 ? 30.103  -22.954 35.598 1.00 20.77  ?  313 PHE   B CD1    1 
ATOM   10991 C  CD2    . PHE   B 1 288 ? 30.429  -24.131 37.648 1.00 22.09  ?  313 PHE   B CD2    1 
ATOM   10992 C  CE1    . PHE   B 1 288 ? 30.865  -21.901 36.072 1.00 19.89  ?  313 PHE   B CE1    1 
ATOM   10993 C  CE2    . PHE   B 1 288 ? 31.192  -23.083 38.129 1.00 22.88  ?  313 PHE   B CE2    1 
ATOM   10994 C  CZ     . PHE   B 1 288 ? 31.404  -21.963 37.339 1.00 21.40  ?  313 PHE   B CZ     1 
ATOM   10995 H  H      . PHE   B 1 288 ? 27.351  -25.391 38.116 1.00 21.28  ?  313 PHE   B H      1 
ATOM   10996 H  HA     . PHE   B 1 288 ? 27.178  -24.198 35.701 1.00 20.82  ?  313 PHE   B HA     1 
ATOM   10997 H  HB2    . PHE   B 1 288 ? 29.293  -26.013 36.284 1.00 23.22  ?  313 PHE   B HB2    1 
ATOM   10998 H  HB3    . PHE   B 1 288 ? 29.096  -25.237 34.912 1.00 23.22  ?  313 PHE   B HB3    1 
ATOM   10999 H  HD1    . PHE   B 1 288 ? 29.734  -22.905 34.746 1.00 24.92  ?  313 PHE   B HD1    1 
ATOM   11000 H  HD2    . PHE   B 1 288 ? 30.282  -24.877 38.183 1.00 26.50  ?  313 PHE   B HD2    1 
ATOM   11001 H  HE1    . PHE   B 1 288 ? 31.012  -21.154 35.538 1.00 23.87  ?  313 PHE   B HE1    1 
ATOM   11002 H  HE2    . PHE   B 1 288 ? 31.561  -23.128 38.981 1.00 27.45  ?  313 PHE   B HE2    1 
ATOM   11003 H  HZ     . PHE   B 1 288 ? 31.912  -21.255 37.663 1.00 25.67  ?  313 PHE   B HZ     1 
ATOM   11004 N  N      . VAL   B 1 289 ? 26.007  -26.051 34.680 1.00 15.97  ?  314 VAL   B N      1 
ATOM   11005 C  CA     . VAL   B 1 289 ? 25.345  -27.167 34.007 1.00 16.17  ?  314 VAL   B CA     1 
ATOM   11006 C  C      . VAL   B 1 289 ? 25.986  -27.327 32.635 1.00 16.48  ?  314 VAL   B C      1 
ATOM   11007 O  O      . VAL   B 1 289 ? 25.898  -26.421 31.797 1.00 17.45  ?  314 VAL   B O      1 
ATOM   11008 C  CB     . VAL   B 1 289 ? 23.826  -26.942 33.869 1.00 17.08  ?  314 VAL   B CB     1 
ATOM   11009 C  CG1    . VAL   B 1 289 ? 23.215  -28.017 32.956 1.00 17.45  ?  314 VAL   B CG1    1 
ATOM   11010 C  CG2    . VAL   B 1 289 ? 23.170  -26.903 35.245 1.00 18.71  ?  314 VAL   B CG2    1 
ATOM   11011 H  H      . VAL   B 1 289 ? 25.925  -25.308 34.255 1.00 19.15  ?  314 VAL   B H      1 
ATOM   11012 H  HA     . VAL   B 1 289 ? 25.490  -27.977 34.519 1.00 19.40  ?  314 VAL   B HA     1 
ATOM   11013 H  HB     . VAL   B 1 289 ? 23.655  -26.084 33.452 1.00 20.49  ?  314 VAL   B HB     1 
ATOM   11014 H  HG11   . VAL   B 1 289 ? 22.255  -28.043 33.097 1.00 20.93  ?  314 VAL   B HG11   1 
ATOM   11015 H  HG12   . VAL   B 1 289 ? 23.407  -27.793 32.032 1.00 20.93  ?  314 VAL   B HG12   1 
ATOM   11016 H  HG13   . VAL   B 1 289 ? 23.605  -28.878 33.176 1.00 20.93  ?  314 VAL   B HG13   1 
ATOM   11017 H  HG21   . VAL   B 1 289 ? 22.220  -26.738 35.137 1.00 22.45  ?  314 VAL   B HG21   1 
ATOM   11018 H  HG22   . VAL   B 1 289 ? 23.310  -27.755 35.687 1.00 22.45  ?  314 VAL   B HG22   1 
ATOM   11019 H  HG23   . VAL   B 1 289 ? 23.572  -26.190 35.766 1.00 22.45  ?  314 VAL   B HG23   1 
ATOM   11020 N  N      . ASN   B 1 290 ? 26.630  -28.476 32.403 1.00 17.32  ?  315 ASN   B N      1 
ATOM   11021 C  CA     . ASN   B 1 290 ? 27.276  -28.756 31.115 1.00 18.17  ?  315 ASN   B CA     1 
ATOM   11022 C  C      . ASN   B 1 290 ? 28.188  -27.591 30.721 1.00 19.00  ?  315 ASN   B C      1 
ATOM   11023 O  O      . ASN   B 1 290 ? 28.222  -27.149 29.570 1.00 19.03  ?  315 ASN   B O      1 
ATOM   11024 C  CB     . ASN   B 1 290 ? 26.229  -29.068 30.040 1.00 18.27  ?  315 ASN   B CB     1 
ATOM   11025 C  CG     . ASN   B 1 290 ? 25.245  -30.153 30.482 1.00 17.80  ?  315 ASN   B CG     1 
ATOM   11026 O  OD1    . ASN   B 1 290 ? 25.434  -30.794 31.518 1.00 18.20  ?  315 ASN   B OD1    1 
ATOM   11027 N  ND2    . ASN   B 1 290 ? 24.186  -30.352 29.700 1.00 17.72  ?  315 ASN   B ND2    1 
ATOM   11028 H  H      . ASN   B 1 290 ? 26.707  -29.111 32.978 1.00 20.78  ?  315 ASN   B H      1 
ATOM   11029 H  HA     . ASN   B 1 290 ? 27.838  -29.543 31.193 1.00 21.80  ?  315 ASN   B HA     1 
ATOM   11030 H  HB2    . ASN   B 1 290 ? 25.723  -28.263 29.846 1.00 21.91  ?  315 ASN   B HB2    1 
ATOM   11031 H  HB3    . ASN   B 1 290 ? 26.679  -29.378 29.238 1.00 21.91  ?  315 ASN   B HB3    1 
ATOM   11032 H  HD21   . ASN   B 1 290 ? 23.605  -30.951 29.907 1.00 21.25  ?  315 ASN   B HD21   1 
ATOM   11033 H  HD22   . ASN   B 1 290 ? 24.084  -29.882 28.987 1.00 21.25  ?  315 ASN   B HD22   1 
ATOM   11034 N  N      . SER   B 1 291 ? 28.913  -27.080 31.726 1.00 19.65  ?  316 SER   B N      1 
ATOM   11035 C  CA     . SER   B 1 291 ? 29.893  -25.993 31.684 1.00 20.30  ?  316 SER   B CA     1 
ATOM   11036 C  C      . SER   B 1 291 ? 29.298  -24.615 31.397 1.00 18.94  ?  316 SER   B C      1 
ATOM   11037 O  O      . SER   B 1 291 ? 30.061  -23.656 31.248 1.00 20.12  ?  316 SER   B O      1 
ATOM   11038 C  CB     . SER   B 1 291 ? 31.032  -26.284 30.689 1.00 22.61  ?  316 SER   B CB     1 
ATOM   11039 O  OG     . SER   B 1 291 ? 31.929  -27.263 31.217 1.00 23.51  ?  316 SER   B OG     1 
ATOM   11040 H  H      . SER   B 1 291 ? 28.844  -27.384 32.527 1.00 23.57  ?  316 SER   B H      1 
ATOM   11041 H  HA     . SER   B 1 291 ? 30.275  -25.934 32.574 1.00 24.35  ?  316 SER   B HA     1 
ATOM   11042 H  HB2    . SER   B 1 291 ? 30.652  -26.618 29.862 1.00 27.12  ?  316 SER   B HB2    1 
ATOM   11043 H  HB3    . SER   B 1 291 ? 31.523  -25.465 30.521 1.00 27.12  ?  316 SER   B HB3    1 
ATOM   11044 H  HG     . SER   B 1 291 ? 31.514  -27.975 31.380 1.00 28.21  ?  316 SER   B HG     1 
ATOM   11045 N  N      . ILE   B 1 292 ? 27.971  -24.484 31.363 1.00 18.47  ?  317 ILE   B N      1 
ATOM   11046 C  CA     . ILE   B 1 292 ? 27.284  -23.194 31.345 1.00 17.09  ?  317 ILE   B CA     1 
ATOM   11047 C  C      . ILE   B 1 292 ? 27.260  -22.626 32.758 1.00 17.24  ?  317 ILE   B C      1 
ATOM   11048 O  O      . ILE   B 1 292 ? 26.896  -23.339 33.694 1.00 18.02  ?  317 ILE   B O      1 
ATOM   11049 C  CB     . ILE   B 1 292 ? 25.844  -23.373 30.835 1.00 15.87  ?  317 ILE   B CB     1 
ATOM   11050 C  CG1    . ILE   B 1 292 ? 25.809  -23.946 29.419 1.00 17.73  ?  317 ILE   B CG1    1 
ATOM   11051 C  CG2    . ILE   B 1 292 ? 25.053  -22.061 30.944 1.00 16.04  ?  317 ILE   B CG2    1 
ATOM   11052 C  CD1    . ILE   B 1 292 ? 24.498  -24.618 29.113 1.00 18.96  ?  317 ILE   B CD1    1 
ATOM   11053 H  H      . ILE   B 1 292 ? 27.428  -25.151 31.349 1.00 22.16  ?  317 ILE   B H      1 
ATOM   11054 H  HA     . ILE   B 1 292 ? 27.766  -22.584 30.764 1.00 20.50  ?  317 ILE   B HA     1 
ATOM   11055 H  HB     . ILE   B 1 292 ? 25.412  -24.024 31.409 1.00 19.04  ?  317 ILE   B HB     1 
ATOM   11056 H  HG12   . ILE   B 1 292 ? 25.937  -23.227 28.781 1.00 21.27  ?  317 ILE   B HG12   1 
ATOM   11057 H  HG13   . ILE   B 1 292 ? 26.516  -24.604 29.324 1.00 21.27  ?  317 ILE   B HG13   1 
ATOM   11058 H  HG21   . ILE   B 1 292 ? 24.259  -22.124 30.389 1.00 19.25  ?  317 ILE   B HG21   1 
ATOM   11059 H  HG22   . ILE   B 1 292 ? 24.799  -21.922 31.870 1.00 19.25  ?  317 ILE   B HG22   1 
ATOM   11060 H  HG23   . ILE   B 1 292 ? 25.612  -21.329 30.640 1.00 19.25  ?  317 ILE   B HG23   1 
ATOM   11061 H  HD11   . ILE   B 1 292 ? 24.431  -24.758 28.156 1.00 22.75  ?  317 ILE   B HD11   1 
ATOM   11062 H  HD12   . ILE   B 1 292 ? 24.465  -25.470 29.575 1.00 22.75  ?  317 ILE   B HD12   1 
ATOM   11063 H  HD13   . ILE   B 1 292 ? 23.773  -24.049 29.416 1.00 22.75  ?  317 ILE   B HD13   1 
ATOM   11064 N  N      . ALA   B 1 293 ? 27.590  -21.338 32.919 1.00 16.75  ?  318 ALA   B N      1 
ATOM   11065 C  CA     . ALA   B 1 293 ? 27.451  -20.671 34.219 1.00 16.50  ?  318 ALA   B CA     1 
ATOM   11066 C  C      . ALA   B 1 293 ? 25.980  -20.356 34.473 1.00 16.83  ?  318 ALA   B C      1 
ATOM   11067 O  O      . ALA   B 1 293 ? 25.412  -19.458 33.842 1.00 17.82  ?  318 ALA   B O      1 
ATOM   11068 C  CB     . ALA   B 1 293 ? 28.283  -19.393 34.289 1.00 17.01  ?  318 ALA   B CB     1 
ATOM   11069 H  H      . ALA   B 1 293 ? 27.894  -20.832 32.293 1.00 20.10  ?  318 ALA   B H      1 
ATOM   11070 H  HA     . ALA   B 1 293 ? 27.771  -21.280 34.902 1.00 19.80  ?  318 ALA   B HA     1 
ATOM   11071 H  HB1    . ALA   B 1 293 ? 28.148  -18.975 35.154 1.00 20.41  ?  318 ALA   B HB1    1 
ATOM   11072 H  HB2    . ALA   B 1 293 ? 29.219  -19.619 34.174 1.00 20.41  ?  318 ALA   B HB2    1 
ATOM   11073 H  HB3    . ALA   B 1 293 ? 27.999  -18.791 33.583 1.00 20.41  ?  318 ALA   B HB3    1 
ATOM   11074 N  N      . THR   B 1 294 ? 25.353  -21.076 35.404 1.00 14.64  ?  319 THR   B N      1 
ATOM   11075 C  CA     . THR   B 1 294 ? 23.928  -20.868 35.682 1.00 14.39  ?  319 THR   B CA     1 
ATOM   11076 C  C      . THR   B 1 294 ? 23.802  -19.855 36.824 1.00 14.77  ?  319 THR   B C      1 
ATOM   11077 O  O      . THR   B 1 294 ? 23.539  -20.179 37.983 1.00 15.89  ?  319 THR   B O      1 
ATOM   11078 C  CB     . THR   B 1 294 ? 23.233  -22.195 35.976 1.00 15.32  ?  319 THR   B CB     1 
ATOM   11079 O  OG1    . THR   B 1 294 ? 23.999  -22.988 36.886 1.00 16.82  ?  319 THR   B OG1    1 
ATOM   11080 C  CG2    . THR   B 1 294 ? 23.054  -22.996 34.688 1.00 16.42  ?  319 THR   B CG2    1 
ATOM   11081 H  H      . THR   B 1 294 ? 25.725  -21.685 35.883 1.00 17.56  ?  319 THR   B H      1 
ATOM   11082 H  HA     . THR   B 1 294 ? 23.497  -20.486 34.901 1.00 17.26  ?  319 THR   B HA     1 
ATOM   11083 H  HB     . THR   B 1 294 ? 22.368  -22.002 36.370 1.00 18.38  ?  319 THR   B HB     1 
ATOM   11084 H  HG1    . THR   B 1 294 ? 24.105  -22.573 37.609 1.00 20.18  ?  319 THR   B HG1    1 
ATOM   11085 H  HG21   . THR   B 1 294 ? 22.608  -23.836 34.879 1.00 19.70  ?  319 THR   B HG21   1 
ATOM   11086 H  HG22   . THR   B 1 294 ? 22.519  -22.492 34.055 1.00 19.70  ?  319 THR   B HG22   1 
ATOM   11087 H  HG23   . THR   B 1 294 ? 23.919  -23.183 34.290 1.00 19.70  ?  319 THR   B HG23   1 
ATOM   11088 N  N      . SER   B 1 295 ? 23.986  -18.580 36.467 1.00 15.32  ?  320 SER   B N      1 
ATOM   11089 C  CA     . SER   B 1 295 ? 24.085  -17.524 37.471 1.00 16.24  ?  320 SER   B CA     1 
ATOM   11090 C  C      . SER   B 1 295 ? 22.745  -17.140 38.110 1.00 16.96  ?  320 SER   B C      1 
ATOM   11091 O  O      . SER   B 1 295 ? 22.765  -16.448 39.134 1.00 18.59  ?  320 SER   B O      1 
ATOM   11092 C  CB     . SER   B 1 295 ? 24.747  -16.290 36.846 1.00 19.18  ?  320 SER   B CB     1 
ATOM   11093 O  OG     . SER   B 1 295 ? 24.077  -15.863 35.671 1.00 22.63  ?  320 SER   B OG     1 
ATOM   11094 H  H      . SER   B 1 295 ? 24.056  -18.306 35.655 1.00 18.38  ?  320 SER   B H      1 
ATOM   11095 H  HA     . SER   B 1 295 ? 24.648  -17.843 38.194 1.00 19.48  ?  320 SER   B HA     1 
ATOM   11096 H  HB2    . SER   B 1 295 ? 24.732  -15.568 37.493 1.00 23.02  ?  320 SER   B HB2    1 
ATOM   11097 H  HB3    . SER   B 1 295 ? 25.664  -16.511 36.618 1.00 23.02  ?  320 SER   B HB3    1 
ATOM   11098 H  HG     . SER   B 1 295 ? 24.119  -16.462 35.083 1.00 27.15  ?  320 SER   B HG     1 
ATOM   11099 N  N      . LYS   B 1 296 ? 21.609  -17.579 37.581 1.00 16.29  ?  321 LYS   B N      1 
ATOM   11100 C  CA     . LYS   B 1 296 ? 20.342  -17.444 38.296 1.00 16.91  ?  321 LYS   B CA     1 
ATOM   11101 C  C      . LYS   B 1 296 ? 19.932  -18.741 38.976 1.00 19.07  ?  321 LYS   B C      1 
ATOM   11102 O  O      . LYS   B 1 296 ? 18.899  -18.779 39.652 1.00 24.18  ?  321 LYS   B O      1 
ATOM   11103 C  CB     . LYS   B 1 296 ? 19.239  -16.968 37.358 1.00 17.92  ?  321 LYS   B CB     1 
ATOM   11104 C  CG     . LYS   B 1 296 ? 19.409  -15.524 36.887 1.00 20.97  ?  321 LYS   B CG     1 
ATOM   11105 C  CD     . LYS   B 1 296 ? 18.287  -15.177 35.911 1.00 26.06  ?  321 LYS   B CD     1 
ATOM   11106 C  CE     . LYS   B 1 296 ? 18.429  -13.830 35.260 1.00 31.87  ?  321 LYS   B CE     1 
ATOM   11107 N  NZ     . LYS   B 1 296 ? 18.744  -12.839 36.274 1.00 35.12  ?  321 LYS   B NZ     1 
ATOM   11108 H  H      . LYS   B 1 296 ? 21.544  -17.958 36.811 1.00 19.54  ?  321 LYS   B H      1 
ATOM   11109 H  HA     . LYS   B 1 296 ? 20.438  -16.761 38.979 1.00 20.29  ?  321 LYS   B HA     1 
ATOM   11110 H  HB2    . LYS   B 1 296 ? 19.232  -17.537 36.572 1.00 21.50  ?  321 LYS   B HB2    1 
ATOM   11111 H  HB3    . LYS   B 1 296 ? 18.389  -17.030 37.821 1.00 21.50  ?  321 LYS   B HB3    1 
ATOM   11112 H  HG2    . LYS   B 1 296 ? 19.362  -14.922 37.646 1.00 25.16  ?  321 LYS   B HG2    1 
ATOM   11113 H  HG3    . LYS   B 1 296 ? 20.261  -15.423 36.435 1.00 25.16  ?  321 LYS   B HG3    1 
ATOM   11114 H  HD2    . LYS   B 1 296 ? 18.271  -15.843 35.206 1.00 31.26  ?  321 LYS   B HD2    1 
ATOM   11115 H  HD3    . LYS   B 1 296 ? 17.444  -15.183 36.391 1.00 31.26  ?  321 LYS   B HD3    1 
ATOM   11116 H  HE2    . LYS   B 1 296 ? 19.147  -13.853 34.609 1.00 38.24  ?  321 LYS   B HE2    1 
ATOM   11117 H  HE3    . LYS   B 1 296 ? 17.596  -13.583 34.828 1.00 38.24  ?  321 LYS   B HE3    1 
ATOM   11118 H  HZ1    . LYS   B 1 296 ? 18.144  -12.873 36.930 1.00 42.14  ?  321 LYS   B HZ1    1 
ATOM   11119 H  HZ2    . LYS   B 1 296 ? 19.552  -12.996 36.612 1.00 42.14  ?  321 LYS   B HZ2    1 
ATOM   11120 H  HZ3    . LYS   B 1 296 ? 18.735  -12.024 35.916 1.00 42.14  ?  321 LYS   B HZ3    1 
ATOM   11121 N  N      . GLY   B 1 297 ? 20.726  -19.796 38.817 1.00 17.99  ?  322 GLY   B N      1 
ATOM   11122 C  CA     . GLY   B 1 297 ? 20.513  -21.035 39.523 1.00 16.69  ?  322 GLY   B CA     1 
ATOM   11123 C  C      . GLY   B 1 297 ? 19.687  -22.010 38.722 1.00 16.19  ?  322 GLY   B C      1 
ATOM   11124 O  O      . GLY   B 1 297 ? 19.908  -22.178 37.519 1.00 16.10  ?  322 GLY   B O      1 
ATOM   11125 H  H      . GLY   B 1 297 ? 21.408  -19.812 38.292 1.00 21.58  ?  322 GLY   B H      1 
ATOM   11126 H  HA2    . GLY   B 1 297 ? 21.370  -21.446 39.718 1.00 20.02  ?  322 GLY   B HA2    1 
ATOM   11127 H  HA3    . GLY   B 1 297 ? 20.052  -20.854 40.357 1.00 20.02  ?  322 GLY   B HA3    1 
ATOM   11128 N  N      . GLY   B 1 298 ? 18.774  -22.696 39.387 1.00 16.89  ?  323 GLY   B N      1 
ATOM   11129 C  CA     . GLY   B 1 298 ? 17.892  -23.637 38.737 1.00 17.26  ?  323 GLY   B CA     1 
ATOM   11130 C  C      . GLY   B 1 298 ? 17.640  -24.858 39.598 1.00 17.75  ?  323 GLY   B C      1 
ATOM   11131 O  O      . GLY   B 1 298 ? 18.052  -24.941 40.753 1.00 18.72  ?  323 GLY   B O      1 
ATOM   11132 H  H      . GLY   B 1 298 ? 18.646  -22.629 40.234 1.00 20.26  ?  323 GLY   B H      1 
ATOM   11133 H  HA2    . GLY   B 1 298 ? 17.041  -23.210 38.552 1.00 20.71  ?  323 GLY   B HA2    1 
ATOM   11134 H  HA3    . GLY   B 1 298 ? 18.288  -23.927 37.900 1.00 20.71  ?  323 GLY   B HA3    1 
ATOM   11135 N  N      . ARG   B 1 299 ? 16.962  -25.837 38.998 1.00 17.13  ?  324 ARG   B N      1 
ATOM   11136 C  CA     . ARG   B 1 299 ? 16.514  -26.996 39.757 1.00 17.50  ?  324 ARG   B CA     1 
ATOM   11137 C  C      . ARG   B 1 299 ? 17.665  -27.893 40.178 1.00 17.76  ?  324 ARG   B C      1 
ATOM   11138 O  O      . ARG   B 1 299 ? 17.498  -28.668 41.128 1.00 19.92  ?  324 ARG   B O      1 
ATOM   11139 C  CB     . ARG   B 1 299 ? 15.487  -27.784 38.947 1.00 19.22  ?  324 ARG   B CB     1 
ATOM   11140 C  CG     . ARG   B 1 299 ? 14.306  -26.934 38.555 1.00 20.58  ?  324 ARG   B CG     1 
ATOM   11141 C  CD     . ARG   B 1 299 ? 13.076  -27.765 38.332 1.00 22.08  ?  324 ARG   B CD     1 
ATOM   11142 N  NE     . ARG   B 1 299 ? 11.963  -26.993 37.779 1.00 23.33  ?  324 ARG   B NE     1 
ATOM   11143 C  CZ     . ARG   B 1 299 ? 11.087  -26.302 38.506 1.00 25.22  ?  324 ARG   B CZ     1 
ATOM   11144 N  NH1    . ARG   B 1 299 ? 11.189  -26.257 39.826 1.00 26.60  ?  324 ARG   B NH1    1 
ATOM   11145 N  NH2    . ARG   B 1 299 ? 10.104  -25.648 37.908 1.00 27.06  ?  324 ARG   B NH2    1 
ATOM   11146 H  H      . ARG   B 1 299 ? 16.754  -25.852 38.164 1.00 20.55  ?  324 ARG   B H      1 
ATOM   11147 H  HA     . ARG   B 1 299 ? 16.076  -26.691 40.567 1.00 20.99  ?  324 ARG   B HA     1 
ATOM   11148 H  HB2    . ARG   B 1 299 ? 15.905  -28.115 38.137 1.00 23.06  ?  324 ARG   B HB2    1 
ATOM   11149 H  HB3    . ARG   B 1 299 ? 15.162  -28.527 39.480 1.00 23.06  ?  324 ARG   B HB3    1 
ATOM   11150 H  HG2    . ARG   B 1 299 ? 14.119  -26.297 39.262 1.00 24.69  ?  324 ARG   B HG2    1 
ATOM   11151 H  HG3    . ARG   B 1 299 ? 14.508  -26.464 37.731 1.00 24.69  ?  324 ARG   B HG3    1 
ATOM   11152 H  HD2    . ARG   B 1 299 ? 13.286  -28.479 37.709 1.00 26.48  ?  324 ARG   B HD2    1 
ATOM   11153 H  HD3    . ARG   B 1 299 ? 12.790  -28.139 39.181 1.00 26.48  ?  324 ARG   B HD3    1 
ATOM   11154 H  HE     . ARG   B 1 299 ? 11.867  -26.986 36.924 1.00 27.99  ?  324 ARG   B HE     1 
ATOM   11155 H  HH11   . ARG   B 1 299 ? 11.825  -26.678 40.223 1.00 31.92  ?  324 ARG   B HH11   1 
ATOM   11156 H  HH12   . ARG   B 1 299 ? 10.618  -25.807 40.287 1.00 31.92  ?  324 ARG   B HH12   1 
ATOM   11157 H  HH21   . ARG   B 1 299 ? 10.031  -25.670 37.051 1.00 32.46  ?  324 ARG   B HH21   1 
ATOM   11158 H  HH22   . ARG   B 1 299 ? 9.538   -25.201 38.376 1.00 32.46  ?  324 ARG   B HH22   1 
ATOM   11159 N  N      . HIS   B 1 300 ? 18.830  -27.788 39.527 1.00 17.78  ?  325 HIS   B N      1 
ATOM   11160 C  CA     . HIS   B 1 300 ? 19.996  -28.530 39.997 1.00 19.23  ?  325 HIS   B CA     1 
ATOM   11161 C  C      . HIS   B 1 300 ? 20.503  -27.976 41.324 1.00 20.29  ?  325 HIS   B C      1 
ATOM   11162 O  O      . HIS   B 1 300 ? 20.890  -28.742 42.211 1.00 21.18  ?  325 HIS   B O      1 
ATOM   11163 C  CB     . HIS   B 1 300 ? 21.108  -28.510 38.950 1.00 18.13  ?  325 HIS   B CB     1 
ATOM   11164 C  CG     . HIS   B 1 300 ? 21.566  -27.139 38.564 1.00 16.85  ?  325 HIS   B CG     1 
ATOM   11165 N  ND1    . HIS   B 1 300 ? 20.706  -26.157 38.115 1.00 16.94  ?  325 HIS   B ND1    1 
ATOM   11166 C  CD2    . HIS   B 1 300 ? 22.802  -26.588 38.555 1.00 17.00  ?  325 HIS   B CD2    1 
ATOM   11167 C  CE1    . HIS   B 1 300 ? 21.391  -25.062 37.848 1.00 17.82  ?  325 HIS   B CE1    1 
ATOM   11168 N  NE2    . HIS   B 1 300 ? 22.667  -25.300 38.099 1.00 16.89  ?  325 HIS   B NE2    1 
ATOM   11169 H  H      . HIS   B 1 300 ? 18.965  -27.304 38.829 1.00 21.32  ?  325 HIS   B H      1 
ATOM   11170 H  HA     . HIS   B 1 300 ? 19.735  -29.455 40.131 1.00 23.07  ?  325 HIS   B HA     1 
ATOM   11171 H  HB2    . HIS   B 1 300 ? 21.875  -28.987 39.303 1.00 21.75  ?  325 HIS   B HB2    1 
ATOM   11172 H  HB3    . HIS   B 1 300 ? 20.786  -28.948 38.147 1.00 21.75  ?  325 HIS   B HB3    1 
ATOM   11173 H  HD2    . HIS   B 1 300 ? 23.595  -27.004 38.809 1.00 20.39  ?  325 HIS   B HD2    1 
ATOM   11174 H  HE1    . HIS   B 1 300 ? 21.038  -24.261 37.535 1.00 21.38  ?  325 HIS   B HE1    1 
ATOM   11175 H  HE2    . HIS   B 1 300 ? 23.309  -24.738 37.994 1.00 20.26  ?  325 HIS   B HE2    1 
ATOM   11176 N  N      . VAL   B 1 301 ? 20.517  -26.647 41.476 1.00 19.33  ?  326 VAL   B N      1 
ATOM   11177 C  CA     . VAL   B 1 301 ? 20.889  -26.059 42.760 1.00 19.32  ?  326 VAL   B CA     1 
ATOM   11178 C  C      . VAL   B 1 301 ? 19.838  -26.377 43.810 1.00 19.38  ?  326 VAL   B C      1 
ATOM   11179 O  O      . VAL   B 1 301 ? 20.171  -26.748 44.946 1.00 20.32  ?  326 VAL   B O      1 
ATOM   11180 C  CB     . VAL   B 1 301 ? 21.100  -24.540 42.610 1.00 20.96  ?  326 VAL   B CB     1 
ATOM   11181 C  CG1    . VAL   B 1 301 ? 21.438  -23.919 43.958 1.00 21.02  ?  326 VAL   B CG1    1 
ATOM   11182 C  CG2    . VAL   B 1 301 ? 22.204  -24.256 41.609 1.00 22.46  ?  326 VAL   B CG2    1 
ATOM   11183 H  H      . VAL   B 1 301 ? 20.318  -26.078 40.863 1.00 23.19  ?  326 VAL   B H      1 
ATOM   11184 H  HA     . VAL   B 1 301 ? 21.729  -26.449 43.047 1.00 23.18  ?  326 VAL   B HA     1 
ATOM   11185 H  HB     . VAL   B 1 301 ? 20.281  -24.138 42.282 1.00 25.14  ?  326 VAL   B HB     1 
ATOM   11186 H  HG11   . VAL   B 1 301 ? 21.755  -23.013 43.818 1.00 25.21  ?  326 VAL   B HG11   1 
ATOM   11187 H  HG12   . VAL   B 1 301 ? 20.640  -23.908 44.509 1.00 25.21  ?  326 VAL   B HG12   1 
ATOM   11188 H  HG13   . VAL   B 1 301 ? 22.128  -24.449 44.386 1.00 25.21  ?  326 VAL   B HG13   1 
ATOM   11189 H  HG21   . VAL   B 1 301 ? 22.360  -23.300 41.573 1.00 26.94  ?  326 VAL   B HG21   1 
ATOM   11190 H  HG22   . VAL   B 1 301 ? 23.012  -24.713 41.892 1.00 26.94  ?  326 VAL   B HG22   1 
ATOM   11191 H  HG23   . VAL   B 1 301 ? 21.930  -24.580 40.736 1.00 26.94  ?  326 VAL   B HG23   1 
ATOM   11192 N  N      . ASP   B 1 302 ? 18.555  -26.240 43.455 1.00 19.46  ?  327 ASP   B N      1 
ATOM   11193 C  CA     . ASP   B 1 302 ? 17.485  -26.535 44.402 1.00 20.59  ?  327 ASP   B CA     1 
ATOM   11194 C  C      . ASP   B 1 302 ? 17.577  -27.975 44.893 1.00 21.71  ?  327 ASP   B C      1 
ATOM   11195 O  O      . ASP   B 1 302 ? 17.394  -28.263 46.084 1.00 22.67  ?  327 ASP   B O      1 
ATOM   11196 C  CB     . ASP   B 1 302 ? 16.107  -26.352 43.752 1.00 22.21  ?  327 ASP   B CB     1 
ATOM   11197 C  CG     . ASP   B 1 302 ? 15.847  -24.956 43.221 1.00 23.88  ?  327 ASP   B CG     1 
ATOM   11198 O  OD1    . ASP   B 1 302 ? 16.558  -23.997 43.590 1.00 26.15  ?  327 ASP   B OD1    1 
ATOM   11199 O  OD2    . ASP   B 1 302 ? 14.870  -24.829 42.442 1.00 25.52  ?  327 ASP   B OD2    1 
ATOM   11200 H  H      . ASP   B 1 302 ? 18.285  -25.981 42.680 1.00 23.34  ?  327 ASP   B H      1 
ATOM   11201 H  HA     . ASP   B 1 302 ? 17.574  -25.916 45.142 1.00 24.70  ?  327 ASP   B HA     1 
ATOM   11202 H  HB2    . ASP   B 1 302 ? 16.030  -26.968 43.007 1.00 26.65  ?  327 ASP   B HB2    1 
ATOM   11203 H  HB3    . ASP   B 1 302 ? 15.424  -26.545 44.414 1.00 26.65  ?  327 ASP   B HB3    1 
ATOM   11204 N  N      . TYR   B 1 303 ? 17.817  -28.899 43.963 1.00 22.42  ?  328 TYR   B N      1 
ATOM   11205 C  CA     . TYR   B 1 303 ? 17.835  -30.327 44.267 1.00 21.95  ?  328 TYR   B CA     1 
ATOM   11206 C  C      . TYR   B 1 303 ? 18.898  -30.658 45.301 1.00 22.00  ?  328 TYR   B C      1 
ATOM   11207 O  O      . TYR   B 1 303 ? 18.646  -31.448 46.218 1.00 24.69  ?  328 TYR   B O      1 
ATOM   11208 C  CB     . TYR   B 1 303 ? 18.032  -31.073 42.937 1.00 23.59  ?  328 TYR   B CB     1 
ATOM   11209 C  CG     . TYR   B 1 303 ? 18.216  -32.566 42.975 1.00 24.69  ?  328 TYR   B CG     1 
ATOM   11210 C  CD1    . TYR   B 1 303 ? 17.233  -33.409 43.478 1.00 26.67  ?  328 TYR   B CD1    1 
ATOM   11211 C  CD2    . TYR   B 1 303 ? 19.360  -33.137 42.443 1.00 25.82  ?  328 TYR   B CD2    1 
ATOM   11212 C  CE1    . TYR   B 1 303 ? 17.415  -34.780 43.492 1.00 28.73  ?  328 TYR   B CE1    1 
ATOM   11213 C  CE2    . TYR   B 1 303 ? 19.548  -34.485 42.446 1.00 27.36  ?  328 TYR   B CE2    1 
ATOM   11214 C  CZ     . TYR   B 1 303 ? 18.582  -35.308 42.975 1.00 29.41  ?  328 TYR   B CZ     1 
ATOM   11215 O  OH     . TYR   B 1 303 ? 18.810  -36.667 42.956 1.00 32.67  ?  328 TYR   B OH     1 
ATOM   11216 H  H      . TYR   B 1 303 ? 17.976  -28.723 43.137 1.00 26.90  ?  328 TYR   B H      1 
ATOM   11217 H  HA     . TYR   B 1 303 ? 16.997  -30.620 44.660 1.00 26.33  ?  328 TYR   B HA     1 
ATOM   11218 H  HB2    . TYR   B 1 303 ? 17.250  -30.905 42.388 1.00 28.30  ?  328 TYR   B HB2    1 
ATOM   11219 H  HB3    . TYR   B 1 303 ? 18.822  -30.708 42.510 1.00 28.30  ?  328 TYR   B HB3    1 
ATOM   11220 H  HD1    . TYR   B 1 303 ? 16.443  -33.048 43.809 1.00 31.99  ?  328 TYR   B HD1    1 
ATOM   11221 H  HD2    . TYR   B 1 303 ? 20.014  -32.587 42.075 1.00 30.98  ?  328 TYR   B HD2    1 
ATOM   11222 H  HE1    . TYR   B 1 303 ? 16.761  -35.339 43.845 1.00 34.47  ?  328 TYR   B HE1    1 
ATOM   11223 H  HE2    . TYR   B 1 303 ? 20.327  -34.848 42.091 1.00 32.82  ?  328 TYR   B HE2    1 
ATOM   11224 H  HH     . TYR   B 1 303 ? 18.165  -37.071 43.311 1.00 39.20  ?  328 TYR   B HH     1 
ATOM   11225 N  N      . VAL   B 1 304 ? 20.076  -30.037 45.188 1.00 22.20  ?  329 VAL   B N      1 
ATOM   11226 C  CA     . VAL   B 1 304 ? 21.162  -30.277 46.134 1.00 23.36  ?  329 VAL   B CA     1 
ATOM   11227 C  C      . VAL   B 1 304 ? 20.939  -29.497 47.423 1.00 24.32  ?  329 VAL   B C      1 
ATOM   11228 O  O      . VAL   B 1 304 ? 21.021  -30.044 48.530 1.00 24.09  ?  329 VAL   B O      1 
ATOM   11229 C  CB     . VAL   B 1 304 ? 22.513  -29.903 45.488 1.00 24.99  ?  329 VAL   B CB     1 
ATOM   11230 C  CG1    . VAL   B 1 304 ? 23.647  -30.044 46.509 1.00 27.17  ?  329 VAL   B CG1    1 
ATOM   11231 C  CG2    . VAL   B 1 304 ? 22.787  -30.750 44.266 1.00 26.09  ?  329 VAL   B CG2    1 
ATOM   11232 H  H      . VAL   B 1 304 ? 20.270  -29.472 44.569 1.00 26.64  ?  329 VAL   B H      1 
ATOM   11233 H  HA     . VAL   B 1 304 ? 21.175  -31.222 46.353 1.00 28.02  ?  329 VAL   B HA     1 
ATOM   11234 H  HB     . VAL   B 1 304 ? 22.471  -28.978 45.200 1.00 29.98  ?  329 VAL   B HB     1 
ATOM   11235 H  HG11   . VAL   B 1 304 ? 24.496  -29.922 46.057 1.00 32.60  ?  329 VAL   B HG11   1 
ATOM   11236 H  HG12   . VAL   B 1 304 ? 23.539  -29.369 47.197 1.00 32.60  ?  329 VAL   B HG12   1 
ATOM   11237 H  HG13   . VAL   B 1 304 ? 23.608  -30.929 46.905 1.00 32.60  ?  329 VAL   B HG13   1 
ATOM   11238 H  HG21   . VAL   B 1 304 ? 23.655  -30.511 43.905 1.00 31.31  ?  329 VAL   B HG21   1 
ATOM   11239 H  HG22   . VAL   B 1 304 ? 22.781  -31.685 44.522 1.00 31.31  ?  329 VAL   B HG22   1 
ATOM   11240 H  HG23   . VAL   B 1 304 ? 22.097  -30.583 43.605 1.00 31.31  ?  329 VAL   B HG23   1 
ATOM   11241 N  N      . ALA   B 1 305 ? 20.658  -28.201 47.301 1.00 23.60  ?  330 ALA   B N      1 
ATOM   11242 C  CA     . ALA   B 1 305 ? 20.526  -27.374 48.494 1.00 25.44  ?  330 ALA   B CA     1 
ATOM   11243 C  C      . ALA   B 1 305 ? 19.388  -27.856 49.383 1.00 26.84  ?  330 ALA   B C      1 
ATOM   11244 O  O      . ALA   B 1 305 ? 19.500  -27.816 50.613 1.00 27.41  ?  330 ALA   B O      1 
ATOM   11245 C  CB     . ALA   B 1 305 ? 20.313  -25.911 48.110 1.00 26.21  ?  330 ALA   B CB     1 
ATOM   11246 H  H      . ALA   B 1 305 ? 20.543  -27.786 46.557 1.00 28.32  ?  330 ALA   B H      1 
ATOM   11247 H  HA     . ALA   B 1 305 ? 21.352  -27.436 48.998 1.00 30.52  ?  330 ALA   B HA     1 
ATOM   11248 H  HB1    . ALA   B 1 305 ? 20.226  -25.382 48.918 1.00 31.44  ?  330 ALA   B HB1    1 
ATOM   11249 H  HB2    . ALA   B 1 305 ? 21.077  -25.605 47.595 1.00 31.44  ?  330 ALA   B HB2    1 
ATOM   11250 H  HB3    . ALA   B 1 305 ? 19.505  -25.838 47.578 1.00 31.44  ?  330 ALA   B HB3    1 
ATOM   11251 N  N      . ASP   B 1 306 ? 18.277  -28.302 48.785 1.00 29.02  ?  331 ASP   B N      1 
ATOM   11252 C  CA     . ASP   B 1 306 ? 17.126  -28.710 49.583 1.00 30.96  ?  331 ASP   B CA     1 
ATOM   11253 C  C      . ASP   B 1 306 ? 17.416  -29.944 50.427 1.00 29.96  ?  331 ASP   B C      1 
ATOM   11254 O  O      . ASP   B 1 306 ? 16.840  -30.085 51.516 1.00 29.70  ?  331 ASP   B O      1 
ATOM   11255 C  CB     . ASP   B 1 306 ? 15.925  -28.989 48.674 1.00 34.10  ?  331 ASP   B CB     1 
ATOM   11256 C  CG     . ASP   B 1 306 ? 15.318  -27.726 48.086 1.00 38.63  ?  331 ASP   B CG     1 
ATOM   11257 O  OD1    . ASP   B 1 306 ? 15.674  -26.614 48.540 1.00 40.39  ?  331 ASP   B OD1    1 
ATOM   11258 O  OD2    . ASP   B 1 306 ? 14.487  -27.856 47.160 1.00 40.32  ?  331 ASP   B OD2    1 
ATOM   11259 H  H      . ASP   B 1 306 ? 18.169  -28.375 47.935 1.00 34.81  ?  331 ASP   B H      1 
ATOM   11260 H  HA     . ASP   B 1 306 ? 16.904  -27.978 50.180 1.00 37.15  ?  331 ASP   B HA     1 
ATOM   11261 H  HB2    . ASP   B 1 306 ? 16.211  -29.554 47.939 1.00 40.91  ?  331 ASP   B HB2    1 
ATOM   11262 H  HB3    . ASP   B 1 306 ? 15.238  -29.439 49.190 1.00 40.91  ?  331 ASP   B HB3    1 
ATOM   11263 N  N      . GLN   B 1 307 ? 18.267  -30.850 49.935 1.00 30.21  ?  332 GLN   B N      1 
ATOM   11264 C  CA     . GLN   B 1 307 ? 18.665  -31.999 50.738 1.00 30.44  ?  332 GLN   B CA     1 
ATOM   11265 C  C      . GLN   B 1 307 ? 19.315  -31.551 52.029 1.00 31.51  ?  332 GLN   B C      1 
ATOM   11266 O  O      . GLN   B 1 307 ? 19.080  -32.135 53.099 1.00 32.97  ?  332 GLN   B O      1 
ATOM   11267 C  CB     . GLN   B 1 307 ? 19.672  -32.855 49.983 1.00 31.18  ?  332 GLN   B CB     1 
ATOM   11268 C  CG     . GLN   B 1 307 ? 19.105  -33.709 48.918 1.00 30.99  ?  332 GLN   B CG     1 
ATOM   11269 C  CD     . GLN   B 1 307 ? 20.195  -34.435 48.178 1.00 29.98  ?  332 GLN   B CD     1 
ATOM   11270 O  OE1    . GLN   B 1 307 ? 20.948  -35.212 48.765 1.00 29.48  ?  332 GLN   B OE1    1 
ATOM   11271 N  NE2    . GLN   B 1 307 ? 20.299  -34.171 46.883 1.00 29.30  ?  332 GLN   B NE2    1 
ATOM   11272 H  H      . GLN   B 1 307 ? 18.621  -30.820 49.151 1.00 36.24  ?  332 GLN   B H      1 
ATOM   11273 H  HA     . GLN   B 1 307 ? 17.870  -32.522 50.923 1.00 36.52  ?  332 GLN   B HA     1 
ATOM   11274 H  HB2    . GLN   B 1 307 ? 20.322  -32.268 49.567 1.00 37.41  ?  332 GLN   B HB2    1 
ATOM   11275 H  HB3    . GLN   B 1 307 ? 20.113  -33.441 50.619 1.00 37.41  ?  332 GLN   B HB3    1 
ATOM   11276 H  HG2    . GLN   B 1 307 ? 18.510  -34.366 49.312 1.00 37.18  ?  332 GLN   B HG2    1 
ATOM   11277 H  HG3    . GLN   B 1 307 ? 18.618  -33.157 48.286 1.00 37.18  ?  332 GLN   B HG3    1 
ATOM   11278 H  HE21   . GLN   B 1 307 ? 19.760  -33.611 46.514 1.00 35.15  ?  332 GLN   B HE21   1 
ATOM   11279 H  HE22   . GLN   B 1 307 ? 20.905  -34.559 46.413 1.00 35.15  ?  332 GLN   B HE22   1 
ATOM   11280 N  N      . ILE   B 1 308 ? 20.190  -30.555 51.922 1.00 30.15  ?  333 ILE   B N      1 
ATOM   11281 C  CA     . ILE   B 1 308 ? 20.892  -30.024 53.078 1.00 29.20  ?  333 ILE   B CA     1 
ATOM   11282 C  C      . ILE   B 1 308 ? 19.912  -29.310 53.995 1.00 30.54  ?  333 ILE   B C      1 
ATOM   11283 O  O      . ILE   B 1 308 ? 19.865  -29.573 55.200 1.00 31.59  ?  333 ILE   B O      1 
ATOM   11284 C  CB     . ILE   B 1 308 ? 22.027  -29.096 52.606 1.00 29.25  ?  333 ILE   B CB     1 
ATOM   11285 C  CG1    . ILE   B 1 308 ? 23.058  -29.893 51.795 1.00 29.45  ?  333 ILE   B CG1    1 
ATOM   11286 C  CG2    . ILE   B 1 308 ? 22.685  -28.405 53.783 1.00 30.47  ?  333 ILE   B CG2    1 
ATOM   11287 C  CD1    . ILE   B 1 308 ? 23.952  -29.043 50.923 1.00 29.88  ?  333 ILE   B CD1    1 
ATOM   11288 H  H      . ILE   B 1 308 ? 20.396  -30.167 51.183 1.00 36.17  ?  333 ILE   B H      1 
ATOM   11289 H  HA     . ILE   B 1 308 ? 21.288  -30.751 53.583 1.00 35.03  ?  333 ILE   B HA     1 
ATOM   11290 H  HB     . ILE   B 1 308 ? 21.645  -28.412 52.034 1.00 35.09  ?  333 ILE   B HB     1 
ATOM   11291 H  HG12   . ILE   B 1 308 ? 23.627  -30.381 52.410 1.00 35.33  ?  333 ILE   B HG12   1 
ATOM   11292 H  HG13   . ILE   B 1 308 ? 22.586  -30.512 51.216 1.00 35.33  ?  333 ILE   B HG13   1 
ATOM   11293 H  HG21   . ILE   B 1 308 ? 23.525  -28.016 53.491 1.00 36.56  ?  333 ILE   B HG21   1 
ATOM   11294 H  HG22   . ILE   B 1 308 ? 22.095  -27.710 54.111 1.00 36.56  ?  333 ILE   B HG22   1 
ATOM   11295 H  HG23   . ILE   B 1 308 ? 22.849  -29.058 54.481 1.00 36.56  ?  333 ILE   B HG23   1 
ATOM   11296 H  HD11   . ILE   B 1 308 ? 24.570  -29.620 50.448 1.00 35.85  ?  333 ILE   B HD11   1 
ATOM   11297 H  HD12   . ILE   B 1 308 ? 23.403  -28.554 50.290 1.00 35.85  ?  333 ILE   B HD12   1 
ATOM   11298 H  HD13   . ILE   B 1 308 ? 24.443  -28.423 51.484 1.00 35.85  ?  333 ILE   B HD13   1 
ATOM   11299 N  N      . VAL   B 1 309 ? 19.083  -28.431 53.428 1.00 29.64  ?  334 VAL   B N      1 
ATOM   11300 C  CA     . VAL   B 1 309 ? 18.166  -27.637 54.241 1.00 31.65  ?  334 VAL   B CA     1 
ATOM   11301 C  C      . VAL   B 1 309 ? 17.222  -28.538 55.028 1.00 33.42  ?  334 VAL   B C      1 
ATOM   11302 O  O      . VAL   B 1 309 ? 16.997  -28.333 56.227 1.00 34.03  ?  334 VAL   B O      1 
ATOM   11303 C  CB     . VAL   B 1 309 ? 17.386  -26.647 53.353 1.00 32.65  ?  334 VAL   B CB     1 
ATOM   11304 C  CG1    . VAL   B 1 309 ? 16.246  -25.997 54.143 1.00 35.31  ?  334 VAL   B CG1    1 
ATOM   11305 C  CG2    . VAL   B 1 309 ? 18.333  -25.597 52.782 1.00 33.43  ?  334 VAL   B CG2    1 
ATOM   11306 H  H      . VAL   B 1 309 ? 19.034  -28.278 52.584 1.00 35.56  ?  334 VAL   B H      1 
ATOM   11307 H  HA     . VAL   B 1 309 ? 18.689  -27.127 54.879 1.00 37.98  ?  334 VAL   B HA     1 
ATOM   11308 H  HB     . VAL   B 1 309 ? 16.989  -27.128 52.610 1.00 39.17  ?  334 VAL   B HB     1 
ATOM   11309 H  HG11   . VAL   B 1 309 ? 15.962  -25.192 53.683 1.00 42.37  ?  334 VAL   B HG11   1 
ATOM   11310 H  HG12   . VAL   B 1 309 ? 15.506  -26.622 54.201 1.00 42.37  ?  334 VAL   B HG12   1 
ATOM   11311 H  HG13   . VAL   B 1 309 ? 16.563  -25.776 55.032 1.00 42.37  ?  334 VAL   B HG13   1 
ATOM   11312 H  HG21   . VAL   B 1 309 ? 17.831  -24.997 52.210 1.00 40.11  ?  334 VAL   B HG21   1 
ATOM   11313 H  HG22   . VAL   B 1 309 ? 18.732  -25.101 53.513 1.00 40.11  ?  334 VAL   B HG22   1 
ATOM   11314 H  HG23   . VAL   B 1 309 ? 19.025  -26.042 52.268 1.00 40.11  ?  334 VAL   B HG23   1 
ATOM   11315 N  N      . THR   B 1 310 ? 16.644  -29.540 54.367 1.00 35.09  ?  335 THR   B N      1 
ATOM   11316 C  CA     . THR   B 1 310 ? 15.663  -30.384 55.044 1.00 38.13  ?  335 THR   B CA     1 
ATOM   11317 C  C      . THR   B 1 310 ? 16.287  -31.111 56.227 1.00 39.96  ?  335 THR   B C      1 
ATOM   11318 O  O      . THR   B 1 310 ? 15.660  -31.254 57.287 1.00 40.75  ?  335 THR   B O      1 
ATOM   11319 C  CB     . THR   B 1 310 ? 15.063  -31.379 54.053 1.00 40.06  ?  335 THR   B CB     1 
ATOM   11320 O  OG1    . THR   B 1 310 ? 14.436  -30.662 52.984 1.00 41.69  ?  335 THR   B OG1    1 
ATOM   11321 C  CG2    . THR   B 1 310 ? 14.029  -32.256 54.743 1.00 40.69  ?  335 THR   B CG2    1 
ATOM   11322 H  H      . THR   B 1 310 ? 16.798  -29.748 53.547 1.00 42.10  ?  335 THR   B H      1 
ATOM   11323 H  HA     . THR   B 1 310 ? 14.945  -29.825 55.381 1.00 45.75  ?  335 THR   B HA     1 
ATOM   11324 H  HB     . THR   B 1 310 ? 15.762  -31.951 53.698 1.00 48.06  ?  335 THR   B HB     1 
ATOM   11325 H  HG1    . THR   B 1 310 ? 14.115  -31.201 52.425 1.00 50.02  ?  335 THR   B HG1    1 
ATOM   11326 H  HG21   . THR   B 1 310 ? 13.503  -32.733 54.081 1.00 48.82  ?  335 THR   B HG21   1 
ATOM   11327 H  HG22   . THR   B 1 310 ? 14.471  -32.901 55.317 1.00 48.82  ?  335 THR   B HG22   1 
ATOM   11328 H  HG23   . THR   B 1 310 ? 13.436  -31.709 55.282 1.00 48.82  ?  335 THR   B HG23   1 
ATOM   11329 N  N      . LYS   B 1 311 ? 17.528  -31.572 56.073 1.00 41.25  ?  336 LYS   B N      1 
ATOM   11330 C  CA     . LYS   B 1 311 ? 18.183  -32.274 57.169 1.00 42.97  ?  336 LYS   B CA     1 
ATOM   11331 C  C      . LYS   B 1 311 ? 18.511  -31.326 58.316 1.00 41.43  ?  336 LYS   B C      1 
ATOM   11332 O  O      . LYS   B 1 311 ? 18.321  -31.673 59.487 1.00 41.70  ?  336 LYS   B O      1 
ATOM   11333 C  CB     . LYS   B 1 311 ? 19.446  -32.965 56.664 1.00 45.43  ?  336 LYS   B CB     1 
ATOM   11334 C  CG     . LYS   B 1 311 ? 19.180  -34.225 55.852 1.00 49.41  ?  336 LYS   B CG     1 
ATOM   11335 C  CD     . LYS   B 1 311 ? 18.517  -35.308 56.708 1.00 52.94  ?  336 LYS   B CD     1 
ATOM   11336 C  CE     . LYS   B 1 311 ? 18.621  -36.691 56.065 1.00 56.05  ?  336 LYS   B CE     1 
ATOM   11337 N  NZ     . LYS   B 1 311 ? 18.211  -36.695 54.630 1.00 57.91  ?  336 LYS   B NZ     1 
ATOM   11338 H  H      . LYS   B 1 311 ? 18.000  -31.492 55.359 1.00 49.50  ?  336 LYS   B H      1 
ATOM   11339 H  HA     . LYS   B 1 311 ? 17.582  -32.955 57.508 1.00 51.55  ?  336 LYS   B HA     1 
ATOM   11340 H  HB2    . LYS   B 1 311 ? 19.933  -32.346 56.098 1.00 54.51  ?  336 LYS   B HB2    1 
ATOM   11341 H  HB3    . LYS   B 1 311 ? 19.989  -33.215 57.427 1.00 54.51  ?  336 LYS   B HB3    1 
ATOM   11342 H  HG2    . LYS   B 1 311 ? 18.587  -34.013 55.114 1.00 59.29  ?  336 LYS   B HG2    1 
ATOM   11343 H  HG3    . LYS   B 1 311 ? 20.019  -34.574 55.514 1.00 59.29  ?  336 LYS   B HG3    1 
ATOM   11344 H  HD2    . LYS   B 1 311 ? 18.954  -35.343 57.574 1.00 63.52  ?  336 LYS   B HD2    1 
ATOM   11345 H  HD3    . LYS   B 1 311 ? 17.577  -35.096 56.820 1.00 63.52  ?  336 LYS   B HD3    1 
ATOM   11346 H  HE2    . LYS   B 1 311 ? 19.541  -36.994 56.115 1.00 67.26  ?  336 LYS   B HE2    1 
ATOM   11347 H  HE3    . LYS   B 1 311 ? 18.043  -37.306 56.543 1.00 67.26  ?  336 LYS   B HE3    1 
ATOM   11348 H  HZ1    . LYS   B 1 311 ? 18.252  -37.522 54.305 1.00 69.49  ?  336 LYS   B HZ1    1 
ATOM   11349 H  HZ2    . LYS   B 1 311 ? 17.378  -36.394 54.550 1.00 69.49  ?  336 LYS   B HZ2    1 
ATOM   11350 H  HZ3    . LYS   B 1 311 ? 18.754  -36.172 54.157 1.00 69.49  ?  336 LYS   B HZ3    1 
ATOM   11351 N  N      . LEU   B 1 312 ? 19.000  -30.123 58.005 1.00 40.07  ?  337 LEU   B N      1 
ATOM   11352 C  CA     . LEU   B 1 312 ? 19.343  -29.192 59.074 1.00 40.55  ?  337 LEU   B CA     1 
ATOM   11353 C  C      . LEU   B 1 312 ? 18.091  -28.728 59.809 1.00 41.78  ?  337 LEU   B C      1 
ATOM   11354 O  O      . LEU   B 1 312 ? 18.109  -28.553 61.033 1.00 41.86  ?  337 LEU   B O      1 
ATOM   11355 C  CB     . LEU   B 1 312 ? 20.109  -27.991 58.526 1.00 41.63  ?  337 LEU   B CB     1 
ATOM   11356 C  CG     . LEU   B 1 312 ? 21.407  -28.217 57.757 1.00 44.43  ?  337 LEU   B CG     1 
ATOM   11357 C  CD1    . LEU   B 1 312 ? 22.380  -27.052 58.022 1.00 44.73  ?  337 LEU   B CD1    1 
ATOM   11358 C  CD2    . LEU   B 1 312 ? 22.071  -29.527 58.065 1.00 45.35  ?  337 LEU   B CD2    1 
ATOM   11359 H  H      . LEU   B 1 312 ? 19.138  -29.833 57.207 1.00 48.08  ?  337 LEU   B H      1 
ATOM   11360 H  HA     . LEU   B 1 312 ? 19.925  -29.649 59.701 1.00 48.65  ?  337 LEU   B HA     1 
ATOM   11361 H  HB2    . LEU   B 1 312 ? 19.514  -27.519 57.924 1.00 49.95  ?  337 LEU   B HB2    1 
ATOM   11362 H  HB3    . LEU   B 1 312 ? 20.336  -27.425 59.281 1.00 49.95  ?  337 LEU   B HB3    1 
ATOM   11363 H  HG     . LEU   B 1 312 ? 21.178  -28.251 56.814 1.00 53.31  ?  337 LEU   B HG     1 
ATOM   11364 H  HD11   . LEU   B 1 312 ? 23.180  -27.182 57.490 1.00 53.67  ?  337 LEU   B HD11   1 
ATOM   11365 H  HD12   . LEU   B 1 312 ? 21.950  -26.219 57.776 1.00 53.67  ?  337 LEU   B HD12   1 
ATOM   11366 H  HD13   . LEU   B 1 312 ? 22.608  -27.041 58.965 1.00 53.67  ?  337 LEU   B HD13   1 
ATOM   11367 H  HD21   . LEU   B 1 312 ? 22.947  -29.542 57.649 1.00 54.41  ?  337 LEU   B HD21   1 
ATOM   11368 H  HD22   . LEU   B 1 312 ? 22.159  -29.618 59.026 1.00 54.41  ?  337 LEU   B HD22   1 
ATOM   11369 H  HD23   . LEU   B 1 312 ? 21.526  -30.248 57.713 1.00 54.41  ?  337 LEU   B HD23   1 
ATOM   11370 N  N      . VAL   B 1 313 ? 16.993  -28.524 59.082 1.00 43.33  ?  338 VAL   B N      1 
ATOM   11371 C  CA     . VAL   B 1 313 ? 15.739  -28.166 59.737 1.00 46.64  ?  338 VAL   B CA     1 
ATOM   11372 C  C      . VAL   B 1 313 ? 15.276  -29.302 60.641 1.00 50.31  ?  338 VAL   B C      1 
ATOM   11373 O  O      . VAL   B 1 313 ? 14.757  -29.066 61.739 1.00 51.18  ?  338 VAL   B O      1 
ATOM   11374 C  CB     . VAL   B 1 313 ? 14.675  -27.793 58.689 1.00 46.52  ?  338 VAL   B CB     1 
ATOM   11375 C  CG1    . VAL   B 1 313 ? 13.298  -27.697 59.337 1.00 46.51  ?  338 VAL   B CG1    1 
ATOM   11376 C  CG2    . VAL   B 1 313 ? 15.059  -26.483 58.012 1.00 46.12  ?  338 VAL   B CG2    1 
ATOM   11377 H  H      . VAL   B 1 313 ? 16.948  -28.586 58.225 1.00 51.99  ?  338 VAL   B H      1 
ATOM   11378 H  HA     . VAL   B 1 313 ? 15.890  -27.386 60.294 1.00 55.96  ?  338 VAL   B HA     1 
ATOM   11379 H  HB     . VAL   B 1 313 ? 14.629  -28.485 58.010 1.00 55.82  ?  338 VAL   B HB     1 
ATOM   11380 H  HG11   . VAL   B 1 313 ? 12.707  -27.200 58.750 1.00 55.80  ?  338 VAL   B HG11   1 
ATOM   11381 H  HG12   . VAL   B 1 313 ? 12.951  -28.592 59.476 1.00 55.80  ?  338 VAL   B HG12   1 
ATOM   11382 H  HG13   . VAL   B 1 313 ? 13.381  -27.238 60.187 1.00 55.80  ?  338 VAL   B HG13   1 
ATOM   11383 H  HG21   . VAL   B 1 313 ? 14.396  -26.270 57.336 1.00 55.33  ?  338 VAL   B HG21   1 
ATOM   11384 H  HG22   . VAL   B 1 313 ? 15.089  -25.780 58.679 1.00 55.33  ?  338 VAL   B HG22   1 
ATOM   11385 H  HG23   . VAL   B 1 313 ? 15.931  -26.584 57.599 1.00 55.33  ?  338 VAL   B HG23   1 
ATOM   11386 N  N      . ASP   B 1 314 ? 15.463  -30.550 60.200 1.00 53.56  ?  339 ASP   B N      1 
ATOM   11387 C  CA     . ASP   B 1 314 ? 15.109  -31.693 61.038 1.00 56.85  ?  339 ASP   B CA     1 
ATOM   11388 C  C      . ASP   B 1 314 ? 15.863  -31.655 62.362 1.00 56.75  ?  339 ASP   B C      1 
ATOM   11389 O  O      . ASP   B 1 314 ? 15.322  -32.031 63.410 1.00 55.85  ?  339 ASP   B O      1 
ATOM   11390 C  CB     . ASP   B 1 314 ? 15.415  -33.005 60.312 1.00 60.51  ?  339 ASP   B CB     1 
ATOM   11391 C  CG     . ASP   B 1 314 ? 14.481  -33.271 59.148 1.00 63.99  ?  339 ASP   B CG     1 
ATOM   11392 O  OD1    . ASP   B 1 314 ? 13.544  -32.473 58.936 1.00 64.71  ?  339 ASP   B OD1    1 
ATOM   11393 O  OD2    . ASP   B 1 314 ? 14.689  -34.283 58.443 1.00 65.89  ?  339 ASP   B OD2    1 
ATOM   11394 H  H      . ASP   B 1 314 ? 15.789  -30.758 59.431 1.00 64.26  ?  339 ASP   B H      1 
ATOM   11395 H  HA     . ASP   B 1 314 ? 14.156  -31.655 61.216 1.00 68.21  ?  339 ASP   B HA     1 
ATOM   11396 H  HB2    . ASP   B 1 314 ? 16.320  -32.970 59.966 1.00 72.61  ?  339 ASP   B HB2    1 
ATOM   11397 H  HB3    . ASP   B 1 314 ? 15.327  -33.740 60.939 1.00 72.61  ?  339 ASP   B HB3    1 
ATOM   11398 N  N      . VAL   B 1 315 ? 17.120  -31.211 62.331 1.00 57.53  ?  340 VAL   B N      1 
ATOM   11399 C  CA     . VAL   B 1 315 ? 17.948  -31.224 63.533 1.00 58.89  ?  340 VAL   B CA     1 
ATOM   11400 C  C      . VAL   B 1 315 ? 17.485  -30.156 64.514 1.00 60.39  ?  340 VAL   B C      1 
ATOM   11401 O  O      . VAL   B 1 315 ? 17.310  -30.424 65.709 1.00 60.09  ?  340 VAL   B O      1 
ATOM   11402 C  CB     . VAL   B 1 315 ? 19.429  -31.040 63.158 1.00 59.13  ?  340 VAL   B CB     1 
ATOM   11403 C  CG1    . VAL   B 1 315 ? 20.274  -30.787 64.394 1.00 59.55  ?  340 VAL   B CG1    1 
ATOM   11404 C  CG2    . VAL   B 1 315 ? 19.930  -32.261 62.406 1.00 58.87  ?  340 VAL   B CG2    1 
ATOM   11405 H  H      . VAL   B 1 315 ? 17.513  -30.900 61.632 1.00 69.04  ?  340 VAL   B H      1 
ATOM   11406 H  HA     . VAL   B 1 315 ? 17.848  -32.086 63.966 1.00 70.66  ?  340 VAL   B HA     1 
ATOM   11407 H  HB     . VAL   B 1 315 ? 19.514  -30.265 62.581 1.00 70.95  ?  340 VAL   B HB     1 
ATOM   11408 H  HG11   . VAL   B 1 315 ? 21.212  -30.841 64.152 1.00 71.45  ?  340 VAL   B HG11   1 
ATOM   11409 H  HG12   . VAL   B 1 315 ? 20.072  -29.903 64.739 1.00 71.45  ?  340 VAL   B HG12   1 
ATOM   11410 H  HG13   . VAL   B 1 315 ? 20.065  -31.459 65.062 1.00 71.45  ?  340 VAL   B HG13   1 
ATOM   11411 H  HG21   . VAL   B 1 315 ? 20.824  -32.477 62.714 1.00 70.64  ?  340 VAL   B HG21   1 
ATOM   11412 H  HG22   . VAL   B 1 315 ? 19.332  -33.005 62.579 1.00 70.64  ?  340 VAL   B HG22   1 
ATOM   11413 H  HG23   . VAL   B 1 315 ? 19.946  -32.063 61.457 1.00 70.64  ?  340 VAL   B HG23   1 
ATOM   11414 N  N      . VAL   B 1 316 ? 17.292  -28.926 64.034 1.00 62.59  ?  341 VAL   B N      1 
ATOM   11415 C  CA     . VAL   B 1 316 ? 16.865  -27.858 64.927 1.00 65.72  ?  341 VAL   B CA     1 
ATOM   11416 C  C      . VAL   B 1 316 ? 15.503  -28.164 65.536 1.00 69.28  ?  341 VAL   B C      1 
ATOM   11417 O  O      . VAL   B 1 316 ? 15.185  -27.665 66.620 1.00 69.19  ?  341 VAL   B O      1 
ATOM   11418 C  CB     . VAL   B 1 316 ? 16.857  -26.505 64.188 1.00 65.27  ?  341 VAL   B CB     1 
ATOM   11419 C  CG1    . VAL   B 1 316 ? 18.254  -26.182 63.671 1.00 63.97  ?  341 VAL   B CG1    1 
ATOM   11420 C  CG2    . VAL   B 1 316 ? 15.853  -26.520 63.054 1.00 66.40  ?  341 VAL   B CG2    1 
ATOM   11421 H  H      . VAL   B 1 316 ? 17.401  -28.693 63.214 1.00 75.10  ?  341 VAL   B H      1 
ATOM   11422 H  HA     . VAL   B 1 316 ? 17.506  -27.787 65.652 1.00 78.86  ?  341 VAL   B HA     1 
ATOM   11423 H  HB     . VAL   B 1 316 ? 16.592  -25.806 64.807 1.00 78.32  ?  341 VAL   B HB     1 
ATOM   11424 H  HG11   . VAL   B 1 316 ? 18.248  -25.295 63.279 1.00 76.75  ?  341 VAL   B HG11   1 
ATOM   11425 H  HG12   . VAL   B 1 316 ? 18.879  -26.212 64.412 1.00 76.75  ?  341 VAL   B HG12   1 
ATOM   11426 H  HG13   . VAL   B 1 316 ? 18.502  -26.839 63.002 1.00 76.75  ?  341 VAL   B HG13   1 
ATOM   11427 H  HG21   . VAL   B 1 316 ? 15.952  -25.708 62.533 1.00 79.68  ?  341 VAL   B HG21   1 
ATOM   11428 H  HG22   . VAL   B 1 316 ? 16.020  -27.295 62.494 1.00 79.68  ?  341 VAL   B HG22   1 
ATOM   11429 H  HG23   . VAL   B 1 316 ? 14.958  -26.567 63.425 1.00 79.68  ?  341 VAL   B HG23   1 
ATOM   11430 N  N      . LYS   B 1 317 ? 14.690  -28.993 64.872 1.00 72.80  ?  342 LYS   B N      1 
ATOM   11431 C  CA     . LYS   B 1 317 ? 13.433  -29.427 65.474 1.00 76.61  ?  342 LYS   B CA     1 
ATOM   11432 C  C      . LYS   B 1 317 ? 13.689  -30.352 66.662 1.00 79.19  ?  342 LYS   B C      1 
ATOM   11433 O  O      . LYS   B 1 317 ? 13.121  -30.162 67.744 1.00 78.75  ?  342 LYS   B O      1 
ATOM   11434 C  CB     . LYS   B 1 317 ? 12.557  -30.128 64.435 1.00 77.58  ?  342 LYS   B CB     1 
ATOM   11435 C  CG     . LYS   B 1 317 ? 12.010  -29.222 63.335 1.00 78.56  ?  342 LYS   B CG     1 
ATOM   11436 C  CD     . LYS   B 1 317 ? 11.255  -28.023 63.899 1.00 79.37  ?  342 LYS   B CD     1 
ATOM   11437 C  CE     . LYS   B 1 317 ? 12.163  -26.804 64.022 1.00 80.02  ?  342 LYS   B CE     1 
ATOM   11438 N  NZ     . LYS   B 1 317 ? 11.708  -25.868 65.091 1.00 80.30  ?  342 LYS   B NZ     1 
ATOM   11439 H  H      . LYS   B 1 317 ? 14.842  -29.309 64.087 1.00 87.35  ?  342 LYS   B H      1 
ATOM   11440 H  HA     . LYS   B 1 317 ? 12.955  -28.645 65.789 1.00 91.93  ?  342 LYS   B HA     1 
ATOM   11441 H  HB2    . LYS   B 1 317 ? 13.083  -30.820 64.006 1.00 93.09  ?  342 LYS   B HB2    1 
ATOM   11442 H  HB3    . LYS   B 1 317 ? 11.797  -30.523 64.890 1.00 93.09  ?  342 LYS   B HB3    1 
ATOM   11443 H  HG2    . LYS   B 1 317 ? 12.747  -28.890 62.800 1.00 94.27  ?  342 LYS   B HG2    1 
ATOM   11444 H  HG3    . LYS   B 1 317 ? 11.398  -29.730 62.779 1.00 94.27  ?  342 LYS   B HG3    1 
ATOM   11445 H  HD2    . LYS   B 1 317 ? 10.519  -27.799 63.308 1.00 95.24  ?  342 LYS   B HD2    1 
ATOM   11446 H  HD3    . LYS   B 1 317 ? 10.916  -28.242 64.781 1.00 95.24  ?  342 LYS   B HD3    1 
ATOM   11447 H  HE2    . LYS   B 1 317 ? 13.062  -27.097 64.239 1.00 96.02  ?  342 LYS   B HE2    1 
ATOM   11448 H  HE3    . LYS   B 1 317 ? 12.166  -26.323 63.180 1.00 96.02  ?  342 LYS   B HE3    1 
ATOM   11449 H  HZ1    . LYS   B 1 317 ? 10.928  -26.141 65.422 1.00 96.35  ?  342 LYS   B HZ1    1 
ATOM   11450 H  HZ2    . LYS   B 1 317 ? 12.307  -25.842 65.748 1.00 96.35  ?  342 LYS   B HZ2    1 
ATOM   11451 H  HZ3    . LYS   B 1 317 ? 11.609  -25.049 64.756 1.00 96.35  ?  342 LYS   B HZ3    1 
ATOM   11452 N  N      . LYS   B 1 318 ? 14.542  -31.365 66.476 1.00 82.21  ?  343 LYS   B N      1 
ATOM   11453 C  CA     . LYS   B 1 318 ? 14.879  -32.263 67.576 1.00 84.79  ?  343 LYS   B CA     1 
ATOM   11454 C  C      . LYS   B 1 318 ? 15.352  -31.496 68.804 1.00 85.81  ?  343 LYS   B C      1 
ATOM   11455 O  O      . LYS   B 1 318 ? 15.083  -31.906 69.939 1.00 85.92  ?  343 LYS   B O      1 
ATOM   11456 C  CB     . LYS   B 1 318 ? 15.961  -33.256 67.139 1.00 86.05  ?  343 LYS   B CB     1 
ATOM   11457 C  CG     . LYS   B 1 318 ? 15.433  -34.497 66.436 1.00 86.81  ?  343 LYS   B CG     1 
ATOM   11458 C  CD     . LYS   B 1 318 ? 16.548  -35.497 66.125 1.00 87.50  ?  343 LYS   B CD     1 
ATOM   11459 C  CE     . LYS   B 1 318 ? 17.580  -34.916 65.163 1.00 87.81  ?  343 LYS   B CE     1 
ATOM   11460 N  NZ     . LYS   B 1 318 ? 18.183  -35.964 64.290 1.00 87.86  ?  343 LYS   B NZ     1 
ATOM   11461 H  H      . LYS   B 1 318 ? 14.932  -31.550 65.732 1.00 98.65  ?  343 LYS   B H      1 
ATOM   11462 H  HA     . LYS   B 1 318 ? 14.085  -32.766 67.816 1.00 101.74 ?  343 LYS   B HA     1 
ATOM   11463 H  HB2    . LYS   B 1 318 ? 16.563  -32.806 66.525 1.00 103.25 ?  343 LYS   B HB2    1 
ATOM   11464 H  HB3    . LYS   B 1 318 ? 16.447  -33.549 67.926 1.00 103.25 ?  343 LYS   B HB3    1 
ATOM   11465 H  HG2    . LYS   B 1 318 ? 14.784  -34.936 67.008 1.00 104.17 ?  343 LYS   B HG2    1 
ATOM   11466 H  HG3    . LYS   B 1 318 ? 15.017  -34.238 65.600 1.00 104.17 ?  343 LYS   B HG3    1 
ATOM   11467 H  HD2    . LYS   B 1 318 ? 17.002  -35.737 66.949 1.00 105.00 ?  343 LYS   B HD2    1 
ATOM   11468 H  HD3    . LYS   B 1 318 ? 16.163  -36.288 65.716 1.00 105.00 ?  343 LYS   B HD3    1 
ATOM   11469 H  HE2    . LYS   B 1 318 ? 17.151  -34.258 64.594 1.00 105.37 ?  343 LYS   B HE2    1 
ATOM   11470 H  HE3    . LYS   B 1 318 ? 18.292  -34.500 65.673 1.00 105.37 ?  343 LYS   B HE3    1 
ATOM   11471 H  HZ1    . LYS   B 1 318 ? 18.784  -35.597 63.745 1.00 105.42 ?  343 LYS   B HZ1    1 
ATOM   11472 H  HZ2    . LYS   B 1 318 ? 18.586  -36.581 64.789 1.00 105.42 ?  343 LYS   B HZ2    1 
ATOM   11473 H  HZ3    . LYS   B 1 318 ? 17.551  -36.354 63.801 1.00 105.42 ?  343 LYS   B HZ3    1 
ATOM   11474 N  N      . LYS   B 1 319 ? 16.050  -30.382 68.597 1.00 86.57  ?  344 LYS   B N      1 
ATOM   11475 C  CA     . LYS   B 1 319 ? 16.641  -29.595 69.676 1.00 87.73  ?  344 LYS   B CA     1 
ATOM   11476 C  C      . LYS   B 1 319 ? 15.848  -28.325 69.950 1.00 89.67  ?  344 LYS   B C      1 
ATOM   11477 O  O      . LYS   B 1 319 ? 16.420  -27.276 70.255 1.00 89.98  ?  344 LYS   B O      1 
ATOM   11478 C  CB     . LYS   B 1 319 ? 18.091  -29.266 69.334 1.00 87.09  ?  344 LYS   B CB     1 
ATOM   11479 C  CG     . LYS   B 1 319 ? 18.920  -30.491 68.967 1.00 86.84  ?  344 LYS   B CG     1 
ATOM   11480 C  CD     . LYS   B 1 319 ? 20.336  -30.106 68.575 1.00 86.69  ?  344 LYS   B CD     1 
ATOM   11481 C  CE     . LYS   B 1 319 ? 21.211  -31.333 68.382 1.00 86.81  ?  344 LYS   B CE     1 
ATOM   11482 N  NZ     . LYS   B 1 319 ? 22.634  -31.040 68.715 1.00 87.04  ?  344 LYS   B NZ     1 
ATOM   11483 H  H      . LYS   B 1 319 ? 16.199  -30.052 67.817 1.00 103.88 ?  344 LYS   B H      1 
ATOM   11484 H  HA     . LYS   B 1 319 ? 16.635  -30.121 70.492 1.00 105.27 ?  344 LYS   B HA     1 
ATOM   11485 H  HB2    . LYS   B 1 319 ? 18.104  -28.660 68.577 1.00 104.50 ?  344 LYS   B HB2    1 
ATOM   11486 H  HB3    . LYS   B 1 319 ? 18.506  -28.845 70.103 1.00 104.50 ?  344 LYS   B HB3    1 
ATOM   11487 H  HG2    . LYS   B 1 319 ? 18.966  -31.088 69.730 1.00 104.20 ?  344 LYS   B HG2    1 
ATOM   11488 H  HG3    . LYS   B 1 319 ? 18.508  -30.944 68.215 1.00 104.20 ?  344 LYS   B HG3    1 
ATOM   11489 H  HD2    . LYS   B 1 319 ? 20.316  -29.611 67.741 1.00 104.02 ?  344 LYS   B HD2    1 
ATOM   11490 H  HD3    . LYS   B 1 319 ? 20.727  -29.561 69.276 1.00 104.02 ?  344 LYS   B HD3    1 
ATOM   11491 H  HE2    . LYS   B 1 319 ? 20.900  -32.045 68.963 1.00 104.17 ?  344 LYS   B HE2    1 
ATOM   11492 H  HE3    . LYS   B 1 319 ? 21.166  -31.618 67.455 1.00 104.17 ?  344 LYS   B HE3    1 
ATOM   11493 H  HZ1    . LYS   B 1 319 ? 23.132  -31.767 68.587 1.00 104.45 ?  344 LYS   B HZ1    1 
ATOM   11494 H  HZ2    . LYS   B 1 319 ? 22.939  -30.385 68.196 1.00 104.45 ?  344 LYS   B HZ2    1 
ATOM   11495 H  HZ3    . LYS   B 1 319 ? 22.702  -30.790 69.566 1.00 104.45 ?  344 LYS   B HZ3    1 
ATOM   11496 N  N      . ASN   B 1 320 ? 14.524  -28.397 69.856 1.00 91.11  ?  345 ASN   B N      1 
ATOM   11497 C  CA     . ASN   B 1 320 ? 13.677  -27.227 70.062 1.00 92.51  ?  345 ASN   B CA     1 
ATOM   11498 C  C      . ASN   B 1 320 ? 12.222  -27.638 70.266 1.00 92.66  ?  345 ASN   B C      1 
ATOM   11499 O  O      . ASN   B 1 320 ? 11.913  -28.451 71.139 1.00 92.73  ?  345 ASN   B O      1 
ATOM   11500 C  CB     . ASN   B 1 320 ? 13.803  -26.273 68.872 1.00 93.46  ?  345 ASN   B CB     1 
ATOM   11501 C  CG     . ASN   B 1 320 ? 12.933  -25.041 69.016 1.00 94.03  ?  345 ASN   B CG     1 
ATOM   11502 O  OD1    . ASN   B 1 320 ? 12.115  -24.738 68.147 1.00 94.37  ?  345 ASN   B OD1    1 
ATOM   11503 N  ND2    . ASN   B 1 320 ? 13.104  -24.322 70.120 1.00 94.08  ?  345 ASN   B ND2    1 
ATOM   11504 H  H      . ASN   B 1 320 ? 14.090  -29.116 69.672 1.00 109.33 ?  345 ASN   B H      1 
ATOM   11505 H  HA     . ASN   B 1 320 ? 13.964  -26.755 70.858 1.00 111.01 ?  345 ASN   B HA     1 
ATOM   11506 H  HB2    . ASN   B 1 320 ? 14.725  -25.982 68.796 1.00 112.15 ?  345 ASN   B HB2    1 
ATOM   11507 H  HB3    . ASN   B 1 320 ? 13.534  -26.737 68.064 1.00 112.15 ?  345 ASN   B HB3    1 
ATOM   11508 H  HD21   . ASN   B 1 320 ? 12.634  -23.614 70.249 1.00 112.89 ?  345 ASN   B HD21   1 
ATOM   11509 H  HD22   . ASN   B 1 320 ? 13.684  -24.566 70.706 1.00 112.89 ?  345 ASN   B HD22   1 
ATOM   11510 N  N      . ALA   B 1 325 ? 9.315   -24.320 64.239 1.00 62.05  ?  350 ALA   B N      1 
ATOM   11511 C  CA     . ALA   B 1 325 ? 9.487   -22.884 64.435 1.00 62.77  ?  350 ALA   B CA     1 
ATOM   11512 C  C      . ALA   B 1 325 ? 10.523  -22.315 63.464 1.00 62.81  ?  350 ALA   B C      1 
ATOM   11513 O  O      . ALA   B 1 325 ? 10.512  -21.122 63.167 1.00 62.78  ?  350 ALA   B O      1 
ATOM   11514 C  CB     . ALA   B 1 325 ? 9.895   -22.588 65.882 1.00 63.03  ?  350 ALA   B CB     1 
ATOM   11515 H  HA     . ALA   B 1 325 ? 8.641   -22.442 64.263 1.00 75.32  ?  350 ALA   B HA     1 
ATOM   11516 H  HB1    . ALA   B 1 325 ? 9.997   -21.629 65.992 1.00 75.62  ?  350 ALA   B HB1    1 
ATOM   11517 H  HB2    . ALA   B 1 325 ? 9.204   -22.917 66.478 1.00 75.62  ?  350 ALA   B HB2    1 
ATOM   11518 H  HB3    . ALA   B 1 325 ? 10.735  -23.033 66.071 1.00 75.62  ?  350 ALA   B HB3    1 
ATOM   11519 N  N      . VAL   B 1 326 ? 11.416  -23.179 62.977 1.00 63.05  ?  351 VAL   B N      1 
ATOM   11520 C  CA     . VAL   B 1 326 ? 12.484  -22.787 62.065 1.00 62.87  ?  351 VAL   B CA     1 
ATOM   11521 C  C      . VAL   B 1 326 ? 11.979  -22.923 60.639 1.00 59.84  ?  351 VAL   B C      1 
ATOM   11522 O  O      . VAL   B 1 326 ? 11.289  -23.893 60.303 1.00 60.39  ?  351 VAL   B O      1 
ATOM   11523 C  CB     . VAL   B 1 326 ? 13.742  -23.648 62.286 1.00 65.25  ?  351 VAL   B CB     1 
ATOM   11524 C  CG1    . VAL   B 1 326 ? 14.898  -23.130 61.440 1.00 65.89  ?  351 VAL   B CG1    1 
ATOM   11525 C  CG2    . VAL   B 1 326 ? 14.112  -23.678 63.756 1.00 66.40  ?  351 VAL   B CG2    1 
ATOM   11526 H  H      . VAL   B 1 326 ? 11.422  -24.018 63.168 1.00 75.66  ?  351 VAL   B H      1 
ATOM   11527 H  HA     . VAL   B 1 326 ? 12.718  -21.860 62.229 1.00 75.44  ?  351 VAL   B HA     1 
ATOM   11528 H  HB     . VAL   B 1 326 ? 13.555  -24.558 62.008 1.00 78.30  ?  351 VAL   B HB     1 
ATOM   11529 H  HG11   . VAL   B 1 326 ? 15.707  -23.606 61.685 1.00 79.06  ?  351 VAL   B HG11   1 
ATOM   11530 H  HG12   . VAL   B 1 326 ? 14.696  -23.281 60.503 1.00 79.06  ?  351 VAL   B HG12   1 
ATOM   11531 H  HG13   . VAL   B 1 326 ? 15.010  -22.181 61.605 1.00 79.06  ?  351 VAL   B HG13   1 
ATOM   11532 H  HG21   . VAL   B 1 326 ? 14.992  -24.074 63.852 1.00 79.67  ?  351 VAL   B HG21   1 
ATOM   11533 H  HG22   . VAL   B 1 326 ? 14.118  -22.771 64.099 1.00 79.67  ?  351 VAL   B HG22   1 
ATOM   11534 H  HG23   . VAL   B 1 326 ? 13.456  -24.209 64.236 1.00 79.67  ?  351 VAL   B HG23   1 
ATOM   11535 N  N      . LYS   B 1 327 ? 12.329  -21.958 59.793 1.00 56.10  ?  352 LYS   B N      1 
ATOM   11536 C  CA     . LYS   B 1 327 ? 11.906  -21.950 58.403 1.00 53.43  ?  352 LYS   B CA     1 
ATOM   11537 C  C      . LYS   B 1 327 ? 13.098  -22.162 57.482 1.00 50.38  ?  352 LYS   B C      1 
ATOM   11538 O  O      . LYS   B 1 327 ? 14.225  -21.761 57.787 1.00 48.59  ?  352 LYS   B O      1 
ATOM   11539 C  CB     . LYS   B 1 327 ? 11.207  -20.637 58.047 1.00 53.94  ?  352 LYS   B CB     1 
ATOM   11540 C  CG     . LYS   B 1 327 ? 10.002  -20.348 58.919 1.00 55.68  ?  352 LYS   B CG     1 
ATOM   11541 C  CD     . LYS   B 1 327 ? 9.088   -19.313 58.287 1.00 57.38  ?  352 LYS   B CD     1 
ATOM   11542 C  CE     . LYS   B 1 327 ? 8.349   -18.522 59.354 1.00 58.55  ?  352 LYS   B CE     1 
ATOM   11543 N  NZ     . LYS   B 1 327 ? 9.294   -17.695 60.166 1.00 59.69  ?  352 LYS   B NZ     1 
ATOM   11544 H  H      . LYS   B 1 327 ? 12.821  -21.287 60.009 1.00 67.31  ?  352 LYS   B H      1 
ATOM   11545 H  HA     . LYS   B 1 327 ? 11.281  -22.677 58.258 1.00 64.11  ?  352 LYS   B HA     1 
ATOM   11546 H  HB2    . LYS   B 1 327 ? 11.836  -19.907 58.154 1.00 64.72  ?  352 LYS   B HB2    1 
ATOM   11547 H  HB3    . LYS   B 1 327 ? 10.905  -20.682 57.126 1.00 64.72  ?  352 LYS   B HB3    1 
ATOM   11548 H  HG2    . LYS   B 1 327 ? 9.495   -21.165 59.047 1.00 66.81  ?  352 LYS   B HG2    1 
ATOM   11549 H  HG3    . LYS   B 1 327 ? 10.301  -20.007 59.776 1.00 66.81  ?  352 LYS   B HG3    1 
ATOM   11550 H  HD2    . LYS   B 1 327 ? 9.615   -18.696 57.757 1.00 68.85  ?  352 LYS   B HD2    1 
ATOM   11551 H  HD3    . LYS   B 1 327 ? 8.434   -19.758 57.726 1.00 68.85  ?  352 LYS   B HD3    1 
ATOM   11552 H  HE2    . LYS   B 1 327 ? 7.709   -17.929 58.930 1.00 70.26  ?  352 LYS   B HE2    1 
ATOM   11553 H  HE3    . LYS   B 1 327 ? 7.889   -19.135 59.949 1.00 70.26  ?  352 LYS   B HE3    1 
ATOM   11554 H  HZ1    . LYS   B 1 327 ? 9.796   -18.222 60.679 1.00 71.62  ?  352 LYS   B HZ1    1 
ATOM   11555 H  HZ2    . LYS   B 1 327 ? 9.825   -17.224 59.629 1.00 71.62  ?  352 LYS   B HZ2    1 
ATOM   11556 H  HZ3    . LYS   B 1 327 ? 8.838   -17.135 60.686 1.00 71.62  ?  352 LYS   B HZ3    1 
ATOM   11557 N  N      . ALA   B 1 328 ? 12.823  -22.788 56.337 1.00 48.96  ?  353 ALA   B N      1 
ATOM   11558 C  CA     . ALA   B 1 328 ? 13.885  -23.160 55.411 1.00 46.62  ?  353 ALA   B CA     1 
ATOM   11559 C  C      . ALA   B 1 328 ? 14.731  -21.958 55.006 1.00 42.89  ?  353 ALA   B C      1 
ATOM   11560 O  O      . ALA   B 1 328 ? 15.964  -22.042 54.969 1.00 40.81  ?  353 ALA   B O      1 
ATOM   11561 C  CB     . ALA   B 1 328 ? 13.280  -23.825 54.173 1.00 47.68  ?  353 ALA   B CB     1 
ATOM   11562 H  H      . ALA   B 1 328 ? 12.033  -23.007 56.077 1.00 58.74  ?  353 ALA   B H      1 
ATOM   11563 H  HA     . ALA   B 1 328 ? 14.469  -23.795 55.854 1.00 55.93  ?  353 ALA   B HA     1 
ATOM   11564 H  HB1    . ALA   B 1 328 ? 13.993  -24.046 53.553 1.00 57.21  ?  353 ALA   B HB1    1 
ATOM   11565 H  HB2    . ALA   B 1 328 ? 12.815  -24.632 54.444 1.00 57.21  ?  353 ALA   B HB2    1 
ATOM   11566 H  HB3    . ALA   B 1 328 ? 12.658  -23.209 53.756 1.00 57.21  ?  353 ALA   B HB3    1 
ATOM   11567 N  N      . HIS   B 1 329 ? 14.086  -20.831 54.679 1.00 40.99  ?  354 HIS   B N      1 
ATOM   11568 C  CA     . HIS   B 1 329 ? 14.836  -19.697 54.138 1.00 39.44  ?  354 HIS   B CA     1 
ATOM   11569 C  C      . HIS   B 1 329 ? 15.880  -19.209 55.138 1.00 37.77  ?  354 HIS   B C      1 
ATOM   11570 O  O      . HIS   B 1 329 ? 16.904  -18.635 54.747 1.00 37.80  ?  354 HIS   B O      1 
ATOM   11571 C  CB     . HIS   B 1 329 ? 13.894  -18.557 53.716 1.00 39.34  ?  354 HIS   B CB     1 
ATOM   11572 C  CG     . HIS   B 1 329 ? 13.399  -17.696 54.840 1.00 41.22  ?  354 HIS   B CG     1 
ATOM   11573 N  ND1    . HIS   B 1 329 ? 12.223  -17.954 55.511 1.00 43.35  ?  354 HIS   B ND1    1 
ATOM   11574 C  CD2    . HIS   B 1 329 ? 13.899  -16.560 55.382 1.00 42.11  ?  354 HIS   B CD2    1 
ATOM   11575 C  CE1    . HIS   B 1 329 ? 12.033  -17.029 56.436 1.00 43.75  ?  354 HIS   B CE1    1 
ATOM   11576 N  NE2    . HIS   B 1 329 ? 13.039  -16.175 56.383 1.00 43.63  ?  354 HIS   B NE2    1 
ATOM   11577 H  H      . HIS   B 1 329 ? 13.239  -20.702 54.759 1.00 49.18  ?  354 HIS   B H      1 
ATOM   11578 H  HA     . HIS   B 1 329 ? 15.296  -19.983 53.333 1.00 47.32  ?  354 HIS   B HA     1 
ATOM   11579 H  HB2    . HIS   B 1 329 ? 14.368  -17.982 53.096 1.00 47.21  ?  354 HIS   B HB2    1 
ATOM   11580 H  HB3    . HIS   B 1 329 ? 13.118  -18.945 53.283 1.00 47.21  ?  354 HIS   B HB3    1 
ATOM   11581 H  HD2    . HIS   B 1 329 ? 14.678  -16.123 55.125 1.00 50.52  ?  354 HIS   B HD2    1 
ATOM   11582 H  HE1    . HIS   B 1 329 ? 11.314  -16.987 57.024 1.00 52.49  ?  354 HIS   B HE1    1 
ATOM   11583 H  HE2    . HIS   B 1 329 ? 13.140  -15.489 56.892 1.00 52.35  ?  354 HIS   B HE2    1 
ATOM   11584 N  N      . GLN   B 1 330 ? 15.645  -19.446 56.435 1.00 37.09  ?  355 GLN   B N      1 
ATOM   11585 C  CA     . GLN   B 1 330 ? 16.604  -19.051 57.463 1.00 38.58  ?  355 GLN   B CA     1 
ATOM   11586 C  C      . GLN   B 1 330 ? 17.860  -19.916 57.425 1.00 35.70  ?  355 GLN   B C      1 
ATOM   11587 O  O      . GLN   B 1 330 ? 18.967  -19.416 57.650 1.00 34.53  ?  355 GLN   B O      1 
ATOM   11588 C  CB     . GLN   B 1 330 ? 15.955  -19.138 58.846 1.00 42.35  ?  355 GLN   B CB     1 
ATOM   11589 C  CG     . GLN   B 1 330 ? 14.758  -18.213 59.038 1.00 45.52  ?  355 GLN   B CG     1 
ATOM   11590 C  CD     . GLN   B 1 330 ? 14.024  -18.448 60.354 1.00 49.07  ?  355 GLN   B CD     1 
ATOM   11591 O  OE1    . GLN   B 1 330 ? 13.237  -19.387 60.482 1.00 50.55  ?  355 GLN   B OE1    1 
ATOM   11592 N  NE2    . GLN   B 1 330 ? 14.277  -17.589 61.334 1.00 50.47  ?  355 GLN   B NE2    1 
ATOM   11593 H  H      . GLN   B 1 330 ? 14.940  -19.832 56.742 1.00 44.50  ?  355 GLN   B H      1 
ATOM   11594 H  HA     . GLN   B 1 330 ? 16.866  -18.132 57.299 1.00 46.29  ?  355 GLN   B HA     1 
ATOM   11595 H  HB2    . GLN   B 1 330 ? 15.648  -20.047 58.988 1.00 50.81  ?  355 GLN   B HB2    1 
ATOM   11596 H  HB3    . GLN   B 1 330 ? 16.617  -18.903 59.514 1.00 50.81  ?  355 GLN   B HB3    1 
ATOM   11597 H  HG2    . GLN   B 1 330 ? 15.066  -17.293 59.028 1.00 54.62  ?  355 GLN   B HG2    1 
ATOM   11598 H  HG3    . GLN   B 1 330 ? 14.128  -18.359 58.315 1.00 54.62  ?  355 GLN   B HG3    1 
ATOM   11599 H  HE21   . GLN   B 1 330 ? 14.830  -16.942 61.207 1.00 60.55  ?  355 GLN   B HE21   1 
ATOM   11600 H  HE22   . GLN   B 1 330 ? 13.888  -17.679 62.096 1.00 60.55  ?  355 GLN   B HE22   1 
ATOM   11601 N  N      . VAL   B 1 331 ? 17.708  -21.219 57.174 1.00 35.51  ?  356 VAL   B N      1 
ATOM   11602 C  CA     . VAL   B 1 331 ? 18.875  -22.080 57.006 1.00 34.98  ?  356 VAL   B CA     1 
ATOM   11603 C  C      . VAL   B 1 331 ? 19.592  -21.728 55.711 1.00 33.89  ?  356 VAL   B C      1 
ATOM   11604 O  O      . VAL   B 1 331 ? 20.825  -21.624 55.658 1.00 33.33  ?  356 VAL   B O      1 
ATOM   11605 C  CB     . VAL   B 1 331 ? 18.456  -23.563 57.014 1.00 36.67  ?  356 VAL   B CB     1 
ATOM   11606 C  CG1    . VAL   B 1 331 ? 19.647  -24.439 56.652 1.00 35.95  ?  356 VAL   B CG1    1 
ATOM   11607 C  CG2    . VAL   B 1 331 ? 17.863  -23.962 58.358 1.00 39.27  ?  356 VAL   B CG2    1 
ATOM   11608 H  H      . VAL   B 1 331 ? 16.951  -21.621 57.097 1.00 42.61  ?  356 VAL   B H      1 
ATOM   11609 H  HA     . VAL   B 1 331 ? 19.478  -21.932 57.752 1.00 41.97  ?  356 VAL   B HA     1 
ATOM   11610 H  HB     . VAL   B 1 331 ? 17.763  -23.700 56.348 1.00 44.00  ?  356 VAL   B HB     1 
ATOM   11611 H  HG11   . VAL   B 1 331 ? 19.466  -25.350 56.933 1.00 43.14  ?  356 VAL   B HG11   1 
ATOM   11612 H  HG12   . VAL   B 1 331 ? 19.781  -24.409 55.692 1.00 43.14  ?  356 VAL   B HG12   1 
ATOM   11613 H  HG13   . VAL   B 1 331 ? 20.435  -24.104 57.107 1.00 43.14  ?  356 VAL   B HG13   1 
ATOM   11614 H  HG21   . VAL   B 1 331 ? 17.436  -24.828 58.270 1.00 47.12  ?  356 VAL   B HG21   1 
ATOM   11615 H  HG22   . VAL   B 1 331 ? 18.575  -24.009 59.015 1.00 47.12  ?  356 VAL   B HG22   1 
ATOM   11616 H  HG23   . VAL   B 1 331 ? 17.210  -23.297 58.625 1.00 47.12  ?  356 VAL   B HG23   1 
ATOM   11617 N  N      . LYS   B 1 332 ? 18.826  -21.539 54.643 1.00 33.75  ?  357 LYS   B N      1 
ATOM   11618 C  CA     . LYS   B 1 332 ? 19.431  -21.319 53.342 1.00 34.27  ?  357 LYS   B CA     1 
ATOM   11619 C  C      . LYS   B 1 332 ? 20.255  -20.046 53.309 1.00 33.13  ?  357 LYS   B C      1 
ATOM   11620 O  O      . LYS   B 1 332 ? 21.274  -19.986 52.611 1.00 32.35  ?  357 LYS   B O      1 
ATOM   11621 C  CB     . LYS   B 1 332 ? 18.332  -21.303 52.288 1.00 36.35  ?  357 LYS   B CB     1 
ATOM   11622 C  CG     . LYS   B 1 332 ? 18.711  -22.061 51.060 1.00 37.67  ?  357 LYS   B CG     1 
ATOM   11623 C  CD     . LYS   B 1 332 ? 17.571  -22.136 50.071 1.00 38.17  ?  357 LYS   B CD     1 
ATOM   11624 C  CE     . LYS   B 1 332 ? 18.127  -22.183 48.661 1.00 38.48  ?  357 LYS   B CE     1 
ATOM   11625 N  NZ     . LYS   B 1 332 ? 17.076  -22.492 47.660 1.00 39.42  ?  357 LYS   B NZ     1 
ATOM   11626 H  H      . LYS   B 1 332 ? 17.966  -21.535 54.647 1.00 40.49  ?  357 LYS   B H      1 
ATOM   11627 H  HA     . LYS   B 1 332 ? 20.039  -22.045 53.134 1.00 41.12  ?  357 LYS   B HA     1 
ATOM   11628 H  HB2    . LYS   B 1 332 ? 17.532  -21.708 52.658 1.00 43.62  ?  357 LYS   B HB2    1 
ATOM   11629 H  HB3    . LYS   B 1 332 ? 18.151  -20.385 52.032 1.00 43.62  ?  357 LYS   B HB3    1 
ATOM   11630 H  HG2    . LYS   B 1 332 ? 19.458  -21.619 50.628 1.00 45.20  ?  357 LYS   B HG2    1 
ATOM   11631 H  HG3    . LYS   B 1 332 ? 18.959  -22.966 51.306 1.00 45.20  ?  357 LYS   B HG3    1 
ATOM   11632 H  HD2    . LYS   B 1 332 ? 17.051  -22.939 50.229 1.00 45.79  ?  357 LYS   B HD2    1 
ATOM   11633 H  HD3    . LYS   B 1 332 ? 17.007  -21.352 50.159 1.00 45.79  ?  357 LYS   B HD3    1 
ATOM   11634 H  HE2    . LYS   B 1 332 ? 18.511  -21.320 48.441 1.00 46.17  ?  357 LYS   B HE2    1 
ATOM   11635 H  HE3    . LYS   B 1 332 ? 18.807  -22.873 48.609 1.00 46.17  ?  357 LYS   B HE3    1 
ATOM   11636 H  HZ1    . LYS   B 1 332 ? 17.423  -22.480 46.841 1.00 47.30  ?  357 LYS   B HZ1    1 
ATOM   11637 H  HZ2    . LYS   B 1 332 ? 16.733  -23.298 47.817 1.00 47.30  ?  357 LYS   B HZ2    1 
ATOM   11638 H  HZ3    . LYS   B 1 332 ? 16.425  -21.887 47.707 1.00 47.30  ?  357 LYS   B HZ3    1 
ATOM   11639 N  N      . ASN   B 1 333 ? 19.873  -19.032 54.061 1.00 32.14  ?  358 ASN   B N      1 
ATOM   11640 C  CA     . ASN   B 1 333 ? 20.606  -17.788 53.889 1.00 34.54  ?  358 ASN   B CA     1 
ATOM   11641 C  C      . ASN   B 1 333 ? 21.965  -17.808 54.567 1.00 32.34  ?  358 ASN   B C      1 
ATOM   11642 O  O      . ASN   B 1 333 ? 22.735  -16.863 54.373 1.00 32.24  ?  358 ASN   B O      1 
ATOM   11643 C  CB     . ASN   B 1 333 ? 19.745  -16.616 54.324 1.00 39.97  ?  358 ASN   B CB     1 
ATOM   11644 C  CG     . ASN   B 1 333 ? 18.916  -16.077 53.156 1.00 43.34  ?  358 ASN   B CG     1 
ATOM   11645 O  OD1    . ASN   B 1 333 ? 19.385  -15.251 52.355 1.00 44.06  ?  358 ASN   B OD1    1 
ATOM   11646 N  ND2    . ASN   B 1 333 ? 17.703  -16.598 53.014 1.00 45.32  ?  358 ASN   B ND2    1 
ATOM   11647 H  H      . ASN   B 1 333 ? 19.237  -19.037 54.640 1.00 38.56  ?  358 ASN   B H      1 
ATOM   11648 H  HA     . ASN   B 1 333 ? 20.789  -17.640 52.948 1.00 41.44  ?  358 ASN   B HA     1 
ATOM   11649 H  HB2    . ASN   B 1 333 ? 19.139  -16.904 55.024 1.00 47.95  ?  358 ASN   B HB2    1 
ATOM   11650 H  HB3    . ASN   B 1 333 ? 20.315  -15.902 54.652 1.00 47.95  ?  358 ASN   B HB3    1 
ATOM   11651 H  HD21   . ASN   B 1 333 ? 17.193  -16.332 52.374 1.00 54.38  ?  358 ASN   B HD21   1 
ATOM   11652 H  HD22   . ASN   B 1 333 ? 17.427  -17.201 53.561 1.00 54.38  ?  358 ASN   B HD22   1 
ATOM   11653 N  N      . HIS   B 1 334 ? 22.320  -18.896 55.250 1.00 30.11  ?  359 HIS   B N      1 
ATOM   11654 C  CA     . HIS   B 1 334 ? 23.677  -19.077 55.742 1.00 31.08  ?  359 HIS   B CA     1 
ATOM   11655 C  C      . HIS   B 1 334 ? 24.576  -19.844 54.776 1.00 29.88  ?  359 HIS   B C      1 
ATOM   11656 O  O      . HIS   B 1 334 ? 25.757  -20.048 55.085 1.00 31.99  ?  359 HIS   B O      1 
ATOM   11657 C  CB     . HIS   B 1 334 ? 23.667  -19.825 57.079 1.00 35.20  ?  359 HIS   B CB     1 
ATOM   11658 C  CG     . HIS   B 1 334 ? 23.148  -19.020 58.223 1.00 39.52  ?  359 HIS   B CG     1 
ATOM   11659 N  ND1    . HIS   B 1 334 ? 23.924  -18.106 58.900 1.00 41.85  ?  359 HIS   B ND1    1 
ATOM   11660 C  CD2    . HIS   B 1 334 ? 21.939  -19.014 58.832 1.00 40.98  ?  359 HIS   B CD2    1 
ATOM   11661 C  CE1    . HIS   B 1 334 ? 23.213  -17.561 59.871 1.00 42.84  ?  359 HIS   B CE1    1 
ATOM   11662 N  NE2    . HIS   B 1 334 ? 22.005  -18.096 59.853 1.00 42.81  ?  359 HIS   B NE2    1 
ATOM   11663 H  H      . HIS   B 1 334 ? 21.787  -19.544 55.441 1.00 36.13  ?  359 HIS   B H      1 
ATOM   11664 H  HA     . HIS   B 1 334 ? 24.056  -18.195 55.881 1.00 37.29  ?  359 HIS   B HA     1 
ATOM   11665 H  HB2    . HIS   B 1 334 ? 23.105  -20.610 56.991 1.00 42.23  ?  359 HIS   B HB2    1 
ATOM   11666 H  HB3    . HIS   B 1 334 ? 24.576  -20.090 57.293 1.00 42.23  ?  359 HIS   B HB3    1 
ATOM   11667 H  HD2    . HIS   B 1 334 ? 21.202  -19.533 58.604 1.00 49.17  ?  359 HIS   B HD2    1 
ATOM   11668 H  HE1    . HIS   B 1 334 ? 23.511  -16.911 60.466 1.00 51.40  ?  359 HIS   B HE1    1 
ATOM   11669 H  HE2    . HIS   B 1 334 ? 21.364  -17.901 60.392 1.00 51.37  ?  359 HIS   B HE2    1 
ATOM   11670 N  N      . MET   B 1 335 ? 24.055  -20.279 53.631 1.00 27.54  ?  360 MET   B N      1 
ATOM   11671 C  CA     . MET   B 1 335 ? 24.750  -21.227 52.773 1.00 26.04  ?  360 MET   B CA     1 
ATOM   11672 C  C      . MET   B 1 335 ? 25.392  -20.565 51.562 1.00 24.63  ?  360 MET   B C      1 
ATOM   11673 O  O      . MET   B 1 335 ? 24.793  -19.699 50.919 1.00 24.43  ?  360 MET   B O      1 
ATOM   11674 C  CB     . MET   B 1 335 ? 23.782  -22.312 52.283 1.00 27.66  ?  360 MET   B CB     1 
ATOM   11675 C  CG     . MET   B 1 335 ? 23.271  -23.227 53.385 1.00 30.20  ?  360 MET   B CG     1 
ATOM   11676 S  SD     . MET   B 1 335 ? 21.888  -24.281 52.886 1.00 32.41  ?  360 MET   B SD     1 
ATOM   11677 C  CE     . MET   B 1 335 ? 22.579  -25.153 51.487 1.00 31.84  ?  360 MET   B CE     1 
ATOM   11678 H  H      . MET   B 1 335 ? 23.288  -20.035 53.328 1.00 33.04  ?  360 MET   B H      1 
ATOM   11679 H  HA     . MET   B 1 335 ? 25.459  -21.625 53.303 1.00 31.24  ?  360 MET   B HA     1 
ATOM   11680 H  HB2    . MET   B 1 335 ? 23.013  -21.883 51.876 1.00 33.18  ?  360 MET   B HB2    1 
ATOM   11681 H  HB3    . MET   B 1 335 ? 24.239  -22.865 51.629 1.00 33.18  ?  360 MET   B HB3    1 
ATOM   11682 H  HG2    . MET   B 1 335 ? 23.995  -23.806 53.669 1.00 36.23  ?  360 MET   B HG2    1 
ATOM   11683 H  HG3    . MET   B 1 335 ? 22.972  -22.681 54.129 1.00 36.23  ?  360 MET   B HG3    1 
ATOM   11684 H  HE1    . MET   B 1 335 ? 21.922  -25.783 51.151 1.00 38.20  ?  360 MET   B HE1    1 
ATOM   11685 H  HE2    . MET   B 1 335 ? 22.806  -24.512 50.796 1.00 38.20  ?  360 MET   B HE2    1 
ATOM   11686 H  HE3    . MET   B 1 335 ? 23.375  -25.627 51.773 1.00 38.20  ?  360 MET   B HE3    1 
ATOM   11687 N  N      . TRP   B 1 336 ? 26.611  -21.005 51.246 1.00 25.34  ?  361 TRP   B N      1 
ATOM   11688 C  CA     . TRP   B 1 336 ? 27.295  -20.700 49.990 1.00 24.57  ?  361 TRP   B CA     1 
ATOM   11689 C  C      . TRP   B 1 336 ? 27.597  -22.048 49.347 1.00 24.41  ?  361 TRP   B C      1 
ATOM   11690 O  O      . TRP   B 1 336 ? 28.445  -22.795 49.846 1.00 25.50  ?  361 TRP   B O      1 
ATOM   11691 C  CB     . TRP   B 1 336 ? 28.577  -19.909 50.227 1.00 25.40  ?  361 TRP   B CB     1 
ATOM   11692 C  CG     . TRP   B 1 336 ? 29.253  -19.368 48.986 1.00 25.75  ?  361 TRP   B CG     1 
ATOM   11693 C  CD1    . TRP   B 1 336 ? 28.885  -19.553 47.679 1.00 25.59  ?  361 TRP   B CD1    1 
ATOM   11694 C  CD2    . TRP   B 1 336 ? 30.432  -18.555 48.957 1.00 27.10  ?  361 TRP   B CD2    1 
ATOM   11695 N  NE1    . TRP   B 1 336 ? 29.768  -18.898 46.844 1.00 26.44  ?  361 TRP   B NE1    1 
ATOM   11696 C  CE2    . TRP   B 1 336 ? 30.724  -18.279 47.606 1.00 27.04  ?  361 TRP   B CE2    1 
ATOM   11697 C  CE3    . TRP   B 1 336 ? 31.268  -18.028 49.948 1.00 27.82  ?  361 TRP   B CE3    1 
ATOM   11698 C  CZ2    . TRP   B 1 336 ? 31.825  -17.501 47.225 1.00 27.45  ?  361 TRP   B CZ2    1 
ATOM   11699 C  CZ3    . TRP   B 1 336 ? 32.357  -17.262 49.568 1.00 28.33  ?  361 TRP   B CZ3    1 
ATOM   11700 C  CH2    . TRP   B 1 336 ? 32.623  -17.004 48.223 1.00 28.67  ?  361 TRP   B CH2    1 
ATOM   11701 H  H      . TRP   B 1 336 ? 27.081  -21.503 51.767 1.00 30.40  ?  361 TRP   B H      1 
ATOM   11702 H  HA     . TRP   B 1 336 ? 26.730  -20.166 49.410 1.00 29.48  ?  361 TRP   B HA     1 
ATOM   11703 H  HB2    . TRP   B 1 336 ? 28.366  -19.150 50.794 1.00 30.47  ?  361 TRP   B HB2    1 
ATOM   11704 H  HB3    . TRP   B 1 336 ? 29.215  -20.488 50.673 1.00 30.47  ?  361 TRP   B HB3    1 
ATOM   11705 H  HD1    . TRP   B 1 336 ? 28.149  -20.046 47.396 1.00 30.71  ?  361 TRP   B HD1    1 
ATOM   11706 H  HE1    . TRP   B 1 336 ? 29.725  -18.882 45.985 1.00 31.72  ?  361 TRP   B HE1    1 
ATOM   11707 H  HE3    . TRP   B 1 336 ? 31.095  -18.191 50.847 1.00 33.38  ?  361 TRP   B HE3    1 
ATOM   11708 H  HZ2    . TRP   B 1 336 ? 32.008  -17.329 46.330 1.00 32.94  ?  361 TRP   B HZ2    1 
ATOM   11709 H  HZ3    . TRP   B 1 336 ? 32.920  -16.913 50.221 1.00 33.99  ?  361 TRP   B HZ3    1 
ATOM   11710 H  HH2    . TRP   B 1 336 ? 33.359  -16.482 47.998 1.00 34.40  ?  361 TRP   B HH2    1 
ATOM   11711 N  N      . ILE   B 1 337 ? 26.896  -22.382 48.270 1.00 22.56  ?  362 ILE   B N      1 
ATOM   11712 C  CA     . ILE   B 1 337 ? 27.002  -23.700 47.658 1.00 22.86  ?  362 ILE   B CA     1 
ATOM   11713 C  C      . ILE   B 1 337 ? 27.617  -23.585 46.271 1.00 21.39  ?  362 ILE   B C      1 
ATOM   11714 O  O      . ILE   B 1 337 ? 27.375  -22.619 45.537 1.00 22.50  ?  362 ILE   B O      1 
ATOM   11715 C  CB     . ILE   B 1 337 ? 25.622  -24.394 47.634 1.00 23.59  ?  362 ILE   B CB     1 
ATOM   11716 C  CG1    . ILE   B 1 337 ? 25.763  -25.880 47.309 1.00 27.68  ?  362 ILE   B CG1    1 
ATOM   11717 C  CG2    . ILE   B 1 337 ? 24.658  -23.719 46.657 1.00 22.77  ?  362 ILE   B CG2    1 
ATOM   11718 C  CD1    . ILE   B 1 337 ? 24.536  -26.683 47.703 1.00 30.50  ?  362 ILE   B CD1    1 
ATOM   11719 H  H      . ILE   B 1 337 ? 26.345  -21.854 47.872 1.00 27.07  ?  362 ILE   B H      1 
ATOM   11720 H  HA     . ILE   B 1 337 ? 27.613  -24.249 48.174 1.00 27.43  ?  362 ILE   B HA     1 
ATOM   11721 H  HB     . ILE   B 1 337 ? 25.248  -24.305 48.524 1.00 28.30  ?  362 ILE   B HB     1 
ATOM   11722 H  HG12   . ILE   B 1 337 ? 25.895  -25.984 46.353 1.00 33.21  ?  362 ILE   B HG12   1 
ATOM   11723 H  HG13   . ILE   B 1 337 ? 26.524  -26.239 47.790 1.00 33.21  ?  362 ILE   B HG13   1 
ATOM   11724 H  HG21   . ILE   B 1 337 ? 23.769  -24.085 46.788 1.00 27.32  ?  362 ILE   B HG21   1 
ATOM   11725 H  HG22   . ILE   B 1 337 ? 24.652  -22.765 46.828 1.00 27.32  ?  362 ILE   B HG22   1 
ATOM   11726 H  HG23   . ILE   B 1 337 ? 24.957  -23.891 45.750 1.00 27.32  ?  362 ILE   B HG23   1 
ATOM   11727 H  HD11   . ILE   B 1 337 ? 24.764  -27.626 47.708 1.00 36.59  ?  362 ILE   B HD11   1 
ATOM   11728 H  HD12   . ILE   B 1 337 ? 24.250  -26.407 48.587 1.00 36.59  ?  362 ILE   B HD12   1 
ATOM   11729 H  HD13   . ILE   B 1 337 ? 23.830  -26.517 47.059 1.00 36.59  ?  362 ILE   B HD13   1 
ATOM   11730 N  N      . PHE   B 1 338 ? 28.463  -24.561 45.942 1.00 21.45  ?  363 PHE   B N      1 
ATOM   11731 C  CA     . PHE   B 1 338 ? 29.082  -24.701 44.633 1.00 20.86  ?  363 PHE   B CA     1 
ATOM   11732 C  C      . PHE   B 1 338 ? 28.664  -26.047 44.048 1.00 20.83  ?  363 PHE   B C      1 
ATOM   11733 O  O      . PHE   B 1 338 ? 28.817  -27.079 44.711 1.00 21.94  ?  363 PHE   B O      1 
ATOM   11734 C  CB     . PHE   B 1 338 ? 30.616  -24.663 44.725 1.00 23.10  ?  363 PHE   B CB     1 
ATOM   11735 C  CG     . PHE   B 1 338 ? 31.186  -23.388 45.280 1.00 25.01  ?  363 PHE   B CG     1 
ATOM   11736 C  CD1    . PHE   B 1 338 ? 31.098  -23.087 46.635 1.00 26.74  ?  363 PHE   B CD1    1 
ATOM   11737 C  CD2    . PHE   B 1 338 ? 31.877  -22.514 44.450 1.00 25.95  ?  363 PHE   B CD2    1 
ATOM   11738 C  CE1    . PHE   B 1 338 ? 31.656  -21.919 47.140 1.00 28.80  ?  363 PHE   B CE1    1 
ATOM   11739 C  CE2    . PHE   B 1 338 ? 32.440  -21.347 44.953 1.00 26.44  ?  363 PHE   B CE2    1 
ATOM   11740 C  CZ     . PHE   B 1 338 ? 32.328  -21.051 46.295 1.00 27.83  ?  363 PHE   B CZ     1 
ATOM   11741 H  H      . PHE   B 1 338 ? 28.702  -25.180 46.489 1.00 25.73  ?  363 PHE   B H      1 
ATOM   11742 H  HA     . PHE   B 1 338 ? 28.785  -23.977 44.059 1.00 25.03  ?  363 PHE   B HA     1 
ATOM   11743 H  HB2    . PHE   B 1 338 ? 30.907  -25.387 45.301 1.00 27.71  ?  363 PHE   B HB2    1 
ATOM   11744 H  HB3    . PHE   B 1 338 ? 30.980  -24.781 43.834 1.00 27.71  ?  363 PHE   B HB3    1 
ATOM   11745 H  HD1    . PHE   B 1 338 ? 30.661  -23.674 47.210 1.00 32.08  ?  363 PHE   B HD1    1 
ATOM   11746 H  HD2    . PHE   B 1 338 ? 31.965  -22.713 43.546 1.00 31.13  ?  363 PHE   B HD2    1 
ATOM   11747 H  HE1    . PHE   B 1 338 ? 31.579  -21.720 48.045 1.00 34.55  ?  363 PHE   B HE1    1 
ATOM   11748 H  HE2    . PHE   B 1 338 ? 32.891  -20.765 44.385 1.00 31.72  ?  363 PHE   B HE2    1 
ATOM   11749 H  HZ     . PHE   B 1 338 ? 32.702  -20.269 46.633 1.00 33.39  ?  363 PHE   B HZ     1 
ATOM   11750 N  N      . VAL   B 1 339 ? 28.158  -26.045 42.815 1.00 19.71  ?  364 VAL   B N      1 
ATOM   11751 C  CA     . VAL   B 1 339 ? 27.630  -27.251 42.184 1.00 19.10  ?  364 VAL   B CA     1 
ATOM   11752 C  C      . VAL   B 1 339 ? 28.134  -27.323 40.751 1.00 18.95  ?  364 VAL   B C      1 
ATOM   11753 O  O      . VAL   B 1 339 ? 27.947  -26.378 39.981 1.00 20.76  ?  364 VAL   B O      1 
ATOM   11754 C  CB     . VAL   B 1 339 ? 26.087  -27.283 42.179 1.00 18.63  ?  364 VAL   B CB     1 
ATOM   11755 C  CG1    . VAL   B 1 339 ? 25.580  -28.540 41.475 1.00 19.93  ?  364 VAL   B CG1    1 
ATOM   11756 C  CG2    . VAL   B 1 339 ? 25.525  -27.191 43.582 1.00 20.54  ?  364 VAL   B CG2    1 
ATOM   11757 H  H      . VAL   B 1 339 ? 28.110  -25.345 42.317 1.00 23.65  ?  364 VAL   B H      1 
ATOM   11758 H  HA     . VAL   B 1 339 ? 27.963  -28.019 42.675 1.00 22.92  ?  364 VAL   B HA     1 
ATOM   11759 H  HB     . VAL   B 1 339 ? 25.770  -26.507 41.690 1.00 22.35  ?  364 VAL   B HB     1 
ATOM   11760 H  HG11   . VAL   B 1 339 ? 24.639  -28.658 41.678 1.00 23.91  ?  364 VAL   B HG11   1 
ATOM   11761 H  HG12   . VAL   B 1 339 ? 25.702  -28.437 40.518 1.00 23.91  ?  364 VAL   B HG12   1 
ATOM   11762 H  HG13   . VAL   B 1 339 ? 26.085  -29.305 41.792 1.00 23.91  ?  364 VAL   B HG13   1 
ATOM   11763 H  HG21   . VAL   B 1 339 ? 24.557  -27.243 43.538 1.00 24.65  ?  364 VAL   B HG21   1 
ATOM   11764 H  HG22   . VAL   B 1 339 ? 25.872  -27.926 44.110 1.00 24.65  ?  364 VAL   B HG22   1 
ATOM   11765 H  HG23   . VAL   B 1 339 ? 25.793  -26.346 43.975 1.00 24.65  ?  364 VAL   B HG23   1 
ATOM   11766 N  N      . ASN   B 1 340 ? 28.751  -28.445 40.382 1.00 19.83  ?  365 ASN   B N      1 
ATOM   11767 C  CA     . ASN   B 1 340 ? 29.120  -28.732 38.999 1.00 18.77  ?  365 ASN   B CA     1 
ATOM   11768 C  C      . ASN   B 1 340 ? 28.353  -29.969 38.555 1.00 20.44  ?  365 ASN   B C      1 
ATOM   11769 O  O      . ASN   B 1 340 ? 28.545  -31.050 39.120 1.00 21.78  ?  365 ASN   B O      1 
ATOM   11770 C  CB     . ASN   B 1 340 ? 30.625  -28.966 38.859 1.00 19.35  ?  365 ASN   B CB     1 
ATOM   11771 C  CG     . ASN   B 1 340 ? 31.081  -28.913 37.418 1.00 20.15  ?  365 ASN   B CG     1 
ATOM   11772 O  OD1    . ASN   B 1 340 ? 30.515  -28.183 36.602 1.00 21.26  ?  365 ASN   B OD1    1 
ATOM   11773 N  ND2    . ASN   B 1 340 ? 32.116  -29.683 37.096 1.00 22.83  ?  365 ASN   B ND2    1 
ATOM   11774 H  H      . ASN   B 1 340 ? 28.970  -29.070 40.930 1.00 23.79  ?  365 ASN   B H      1 
ATOM   11775 H  HA     . ASN   B 1 340 ? 28.876  -27.982 38.435 1.00 22.52  ?  365 ASN   B HA     1 
ATOM   11776 H  HB2    . ASN   B 1 340 ? 31.100  -28.279 39.352 1.00 23.21  ?  365 ASN   B HB2    1 
ATOM   11777 H  HB3    . ASN   B 1 340 ? 30.845  -29.841 39.214 1.00 23.21  ?  365 ASN   B HB3    1 
ATOM   11778 H  HD21   . ASN   B 1 340 ? 32.414  -29.688 36.290 1.00 27.40  ?  365 ASN   B HD21   1 
ATOM   11779 H  HD22   . ASN   B 1 340 ? 32.488  -30.175 37.695 1.00 27.40  ?  365 ASN   B HD22   1 
ATOM   11780 N  N      . ALA   B 1 341 ? 27.486  -29.814 37.552 1.00 19.75  ?  366 ALA   B N      1 
ATOM   11781 C  CA     . ALA   B 1 341 ? 26.605  -30.893 37.144 1.00 19.31  ?  366 ALA   B CA     1 
ATOM   11782 C  C      . ALA   B 1 341 ? 26.615  -31.130 35.641 1.00 18.34  ?  366 ALA   B C      1 
ATOM   11783 O  O      . ALA   B 1 341 ? 26.767  -30.203 34.839 1.00 19.18  ?  366 ALA   B O      1 
ATOM   11784 C  CB     . ALA   B 1 341 ? 25.147  -30.620 37.569 1.00 18.35  ?  366 ALA   B CB     1 
ATOM   11785 H  H      . ALA   B 1 341 ? 27.394  -29.090 37.096 1.00 23.69  ?  366 ALA   B H      1 
ATOM   11786 H  HA     . ALA   B 1 341 ? 26.941  -31.701 37.563 1.00 23.17  ?  366 ALA   B HA     1 
ATOM   11787 H  HB1    . ALA   B 1 341 ? 24.591  -31.364 37.287 1.00 22.02  ?  366 ALA   B HB1    1 
ATOM   11788 H  HB2    . ALA   B 1 341 ? 25.111  -30.528 38.534 1.00 22.02  ?  366 ALA   B HB2    1 
ATOM   11789 H  HB3    . ALA   B 1 341 ? 24.843  -29.802 37.147 1.00 22.02  ?  366 ALA   B HB3    1 
ATOM   11790 N  N      . LEU   B 1 342 ? 26.395  -32.397 35.276 1.00 19.99  ?  367 LEU   B N      1 
ATOM   11791 C  CA     . LEU   B 1 342 ? 26.096  -32.811 33.908 1.00 19.36  ?  367 LEU   B CA     1 
ATOM   11792 C  C      . LEU   B 1 342 ? 24.653  -33.312 33.865 1.00 19.57  ?  367 LEU   B C      1 
ATOM   11793 O  O      . LEU   B 1 342 ? 24.302  -34.279 34.559 1.00 20.21  ?  367 LEU   B O      1 
ATOM   11794 C  CB     . LEU   B 1 342 ? 27.067  -33.890 33.428 1.00 21.15  ?  367 LEU   B CB     1 
ATOM   11795 C  CG     . LEU   B 1 342 ? 28.533  -33.494 33.220 1.00 21.37  ?  367 LEU   B CG     1 
ATOM   11796 C  CD1    . LEU   B 1 342 ? 29.391  -34.716 32.915 1.00 23.89  ?  367 LEU   B CD1    1 
ATOM   11797 C  CD2    . LEU   B 1 342 ? 28.682  -32.446 32.098 1.00 23.09  ?  367 LEU   B CD2    1 
ATOM   11798 H  H      . LEU   B 1 342 ? 26.416  -33.058 35.827 1.00 23.99  ?  367 LEU   B H      1 
ATOM   11799 H  HA     . LEU   B 1 342 ? 26.180  -32.052 33.310 1.00 23.22  ?  367 LEU   B HA     1 
ATOM   11800 H  HB2    . LEU   B 1 342 ? 27.061  -34.605 34.083 1.00 25.37  ?  367 LEU   B HB2    1 
ATOM   11801 H  HB3    . LEU   B 1 342 ? 26.744  -34.219 32.575 1.00 25.37  ?  367 LEU   B HB3    1 
ATOM   11802 H  HG     . LEU   B 1 342 ? 28.853  -33.095 34.045 1.00 25.64  ?  367 LEU   B HG     1 
ATOM   11803 H  HD11   . LEU   B 1 342 ? 30.309  -34.433 32.780 1.00 28.66  ?  367 LEU   B HD11   1 
ATOM   11804 H  HD12   . LEU   B 1 342 ? 29.342  -35.332 33.663 1.00 28.66  ?  367 LEU   B HD12   1 
ATOM   11805 H  HD13   . LEU   B 1 342 ? 29.056  -35.145 32.111 1.00 28.66  ?  367 LEU   B HD13   1 
ATOM   11806 H  HD21   . LEU   B 1 342 ? 29.624  -32.259 31.963 1.00 27.71  ?  367 LEU   B HD21   1 
ATOM   11807 H  HD22   . LEU   B 1 342 ? 28.295  -32.800 31.282 1.00 27.71  ?  367 LEU   B HD22   1 
ATOM   11808 H  HD23   . LEU   B 1 342 ? 28.218  -31.635 32.359 1.00 27.71  ?  367 LEU   B HD23   1 
ATOM   11809 N  N      . ILE   B 1 343 ? 23.830  -32.638 33.053 1.00 18.35  ?  368 ILE   B N      1 
ATOM   11810 C  CA     . ILE   B 1 343 ? 22.388  -32.834 32.962 1.00 16.87  ?  368 ILE   B CA     1 
ATOM   11811 C  C      . ILE   B 1 343 ? 22.030  -33.200 31.529 1.00 17.15  ?  368 ILE   B C      1 
ATOM   11812 O  O      . ILE   B 1 343 ? 22.484  -32.541 30.590 1.00 18.28  ?  368 ILE   B O      1 
ATOM   11813 C  CB     . ILE   B 1 343 ? 21.636  -31.550 33.384 1.00 16.83  ?  368 ILE   B CB     1 
ATOM   11814 C  CG1    . ILE   B 1 343 ? 22.047  -31.102 34.787 1.00 18.94  ?  368 ILE   B CG1    1 
ATOM   11815 C  CG2    . ILE   B 1 343 ? 20.131  -31.731 33.240 1.00 16.97  ?  368 ILE   B CG2    1 
ATOM   11816 C  CD1    . ILE   B 1 343 ? 21.620  -31.985 35.889 1.00 19.56  ?  368 ILE   B CD1    1 
ATOM   11817 H  H      . ILE   B 1 343 ? 24.106  -32.026 32.515 1.00 22.01  ?  368 ILE   B H      1 
ATOM   11818 H  HA     . ILE   B 1 343 ? 22.124  -33.568 33.539 1.00 20.24  ?  368 ILE   B HA     1 
ATOM   11819 H  HB     . ILE   B 1 343 ? 21.895  -30.834 32.782 1.00 20.19  ?  368 ILE   B HB     1 
ATOM   11820 H  HG12   . ILE   B 1 343 ? 23.015  -31.049 34.819 1.00 22.72  ?  368 ILE   B HG12   1 
ATOM   11821 H  HG13   . ILE   B 1 343 ? 21.662  -30.227 34.953 1.00 22.72  ?  368 ILE   B HG13   1 
ATOM   11822 H  HG21   . ILE   B 1 343 ? 19.680  -31.009 33.705 1.00 20.36  ?  368 ILE   B HG21   1 
ATOM   11823 H  HG22   . ILE   B 1 343 ? 19.900  -31.715 32.299 1.00 20.36  ?  368 ILE   B HG22   1 
ATOM   11824 H  HG23   . ILE   B 1 343 ? 19.878  -32.583 33.628 1.00 20.36  ?  368 ILE   B HG23   1 
ATOM   11825 H  HD11   . ILE   B 1 343 ? 21.974  -31.641 36.724 1.00 23.46  ?  368 ILE   B HD11   1 
ATOM   11826 H  HD12   . ILE   B 1 343 ? 20.651  -32.002 35.922 1.00 23.46  ?  368 ILE   B HD12   1 
ATOM   11827 H  HD13   . ILE   B 1 343 ? 21.962  -32.878 35.728 1.00 23.46  ?  368 ILE   B HD13   1 
ATOM   11828 N  N      . GLU   B 1 344 ? 21.174  -34.204 31.356 1.00 17.82  ?  369 GLU   B N      1 
ATOM   11829 C  CA     . GLU   B 1 344 ? 20.748  -34.586 30.011 1.00 18.39  ?  369 GLU   B CA     1 
ATOM   11830 C  C      . GLU   B 1 344 ? 19.713  -33.597 29.480 1.00 17.74  ?  369 GLU   B C      1 
ATOM   11831 O  O      . GLU   B 1 344 ? 18.740  -33.267 30.165 1.00 18.51  ?  369 GLU   B O      1 
ATOM   11832 C  CB     . GLU   B 1 344 ? 20.188  -36.015 30.000 1.00 20.76  ?  369 GLU   B CB     1 
ATOM   11833 C  CG     . GLU   B 1 344 ? 21.267  -37.071 30.286 1.00 21.64  ?  369 GLU   B CG     1 
ATOM   11834 C  CD     . GLU   B 1 344 ? 20.740  -38.500 30.414 1.00 24.19  ?  369 GLU   B CD     1 
ATOM   11835 O  OE1    . GLU   B 1 344 ? 19.523  -38.712 30.243 1.00 25.70  ?  369 GLU   B OE1    1 
ATOM   11836 O  OE2    . GLU   B 1 344 ? 21.558  -39.417 30.662 1.00 26.08  ?  369 GLU   B OE2    1 
ATOM   11837 H  H      . GLU   B 1 344 ? 20.831  -34.672 31.990 1.00 21.38  ?  369 GLU   B H      1 
ATOM   11838 H  HA     . GLU   B 1 344 ? 21.515  -34.565 29.418 1.00 22.07  ?  369 GLU   B HA     1 
ATOM   11839 H  HB2    . GLU   B 1 344 ? 19.502  -36.092 30.681 1.00 24.90  ?  369 GLU   B HB2    1 
ATOM   11840 H  HB3    . GLU   B 1 344 ? 19.810  -36.200 29.126 1.00 24.90  ?  369 GLU   B HB3    1 
ATOM   11841 H  HG2    . GLU   B 1 344 ? 21.910  -37.060 29.560 1.00 25.96  ?  369 GLU   B HG2    1 
ATOM   11842 H  HG3    . GLU   B 1 344 ? 21.706  -36.845 31.121 1.00 25.96  ?  369 GLU   B HG3    1 
ATOM   11843 N  N      . ASN   B 1 345 ? 19.941  -33.114 28.260 1.00 18.00  ?  370 ASN   B N      1 
ATOM   11844 C  CA     . ASN   B 1 345 ? 18.997  -32.305 27.494 1.00 18.91  ?  370 ASN   B CA     1 
ATOM   11845 C  C      . ASN   B 1 345 ? 18.320  -31.240 28.371 1.00 17.83  ?  370 ASN   B C      1 
ATOM   11846 O  O      . ASN   B 1 345 ? 17.092  -31.188 28.463 1.00 18.49  ?  370 ASN   B O      1 
ATOM   11847 C  CB     . ASN   B 1 345 ? 17.964  -33.193 26.809 1.00 20.01  ?  370 ASN   B CB     1 
ATOM   11848 C  CG     . ASN   B 1 345 ? 18.604  -34.169 25.833 1.00 21.82  ?  370 ASN   B CG     1 
ATOM   11849 O  OD1    . ASN   B 1 345 ? 19.776  -34.021 25.468 1.00 22.12  ?  370 ASN   B OD1    1 
ATOM   11850 N  ND2    . ASN   B 1 345 ? 17.854  -35.183 25.423 1.00 23.75  ?  370 ASN   B ND2    1 
ATOM   11851 H  H      . ASN   B 1 345 ? 20.675  -33.251 27.834 1.00 21.59  ?  370 ASN   B H      1 
ATOM   11852 H  HA     . ASN   B 1 345 ? 19.485  -31.827 26.805 1.00 22.69  ?  370 ASN   B HA     1 
ATOM   11853 H  HB2    . ASN   B 1 345 ? 17.489  -33.706 27.481 1.00 24.01  ?  370 ASN   B HB2    1 
ATOM   11854 H  HB3    . ASN   B 1 345 ? 17.342  -32.636 26.316 1.00 24.01  ?  370 ASN   B HB3    1 
ATOM   11855 H  HD21   . ASN   B 1 345 ? 18.175  -35.759 24.871 1.00 28.50  ?  370 ASN   B HD21   1 
ATOM   11856 H  HD22   . ASN   B 1 345 ? 17.047  -35.264 25.709 1.00 28.50  ?  370 ASN   B HD22   1 
ATOM   11857 N  N      . PRO   B 1 346 ? 19.102  -30.366 28.992 1.00 16.86  ?  371 PRO   B N      1 
ATOM   11858 C  CA     . PRO   B 1 346 ? 18.520  -29.365 29.889 1.00 16.29  ?  371 PRO   B CA     1 
ATOM   11859 C  C      . PRO   B 1 346 ? 17.645  -28.351 29.166 1.00 17.25  ?  371 PRO   B C      1 
ATOM   11860 O  O      . PRO   B 1 346 ? 17.774  -28.101 27.964 1.00 18.92  ?  371 PRO   B O      1 
ATOM   11861 C  CB     . PRO   B 1 346 ? 19.752  -28.680 30.500 1.00 16.03  ?  371 PRO   B CB     1 
ATOM   11862 C  CG     . PRO   B 1 346 ? 20.830  -28.874 29.473 1.00 17.06  ?  371 PRO   B CG     1 
ATOM   11863 C  CD     . PRO   B 1 346 ? 20.571  -30.266 28.929 1.00 17.05  ?  371 PRO   B CD     1 
ATOM   11864 H  HA     . PRO   B 1 346 ? 17.994  -29.804 30.576 1.00 19.54  ?  371 PRO   B HA     1 
ATOM   11865 H  HB2    . PRO   B 1 346 ? 19.572  -27.738 30.644 1.00 19.23  ?  371 PRO   B HB2    1 
ATOM   11866 H  HB3    . PRO   B 1 346 ? 19.988  -29.105 31.339 1.00 19.23  ?  371 PRO   B HB3    1 
ATOM   11867 H  HG2    . PRO   B 1 346 ? 20.751  -28.205 28.775 1.00 20.47  ?  371 PRO   B HG2    1 
ATOM   11868 H  HG3    . PRO   B 1 346 ? 21.703  -28.817 29.890 1.00 20.47  ?  371 PRO   B HG3    1 
ATOM   11869 H  HD2    . PRO   B 1 346 ? 20.887  -30.347 28.015 1.00 20.45  ?  371 PRO   B HD2    1 
ATOM   11870 H  HD3    . PRO   B 1 346 ? 20.990  -30.941 29.486 1.00 20.45  ?  371 PRO   B HD3    1 
ATOM   11871 N  N      . THR   B 1 347 ? 16.752  -27.749 29.954 1.00 16.89  ?  372 THR   B N      1 
ATOM   11872 C  CA     . THR   B 1 347 ? 15.927  -26.630 29.543 1.00 16.13  ?  372 THR   B CA     1 
ATOM   11873 C  C      . THR   B 1 347 ? 16.262  -25.430 30.414 1.00 15.01  ?  372 THR   B C      1 
ATOM   11874 O  O      . THR   B 1 347 ? 16.708  -25.578 31.557 1.00 15.47  ?  372 THR   B O      1 
ATOM   11875 C  CB     . THR   B 1 347 ? 14.423  -26.932 29.667 1.00 16.54  ?  372 THR   B CB     1 
ATOM   11876 O  OG1    . THR   B 1 347 ? 14.092  -27.345 30.998 1.00 17.62  ?  372 THR   B OG1    1 
ATOM   11877 C  CG2    . THR   B 1 347 ? 14.030  -28.033 28.728 1.00 17.49  ?  372 THR   B CG2    1 
ATOM   11878 H  H      . THR   B 1 347 ? 16.606  -27.988 30.767 1.00 20.27  ?  372 THR   B H      1 
ATOM   11879 H  HA     . THR   B 1 347 ? 16.108  -26.425 28.612 1.00 19.35  ?  372 THR   B HA     1 
ATOM   11880 H  HB     . THR   B 1 347 ? 13.933  -26.124 29.448 1.00 19.85  ?  372 THR   B HB     1 
ATOM   11881 H  HG1    . THR   B 1 347 ? 14.264  -26.729 31.542 1.00 21.13  ?  372 THR   B HG1    1 
ATOM   11882 H  HG21   . THR   B 1 347 ? 13.081  -28.215 28.809 1.00 20.98  ?  372 THR   B HG21   1 
ATOM   11883 H  HG22   . THR   B 1 347 ? 14.224  -27.775 27.814 1.00 20.98  ?  372 THR   B HG22   1 
ATOM   11884 H  HG23   . THR   B 1 347 ? 14.524  -28.841 28.939 1.00 20.98  ?  372 THR   B HG23   1 
ATOM   11885 N  N      . PHE   B 1 348 ? 16.014  -24.236 29.865 1.00 15.61  ?  373 PHE   B N      1 
ATOM   11886 C  CA     . PHE   B 1 348 ? 16.293  -22.966 30.518 1.00 14.97  ?  373 PHE   B CA     1 
ATOM   11887 C  C      . PHE   B 1 348 ? 15.191  -21.970 30.155 1.00 16.72  ?  373 PHE   B C      1 
ATOM   11888 O  O      . PHE   B 1 348 ? 14.437  -22.177 29.200 1.00 17.88  ?  373 PHE   B O      1 
ATOM   11889 C  CB     . PHE   B 1 348 ? 17.651  -22.397 30.093 1.00 14.56  ?  373 PHE   B CB     1 
ATOM   11890 C  CG     . PHE   B 1 348 ? 18.828  -23.352 30.247 1.00 14.82  ?  373 PHE   B CG     1 
ATOM   11891 C  CD1    . PHE   B 1 348 ? 19.137  -24.285 29.262 1.00 16.35  ?  373 PHE   B CD1    1 
ATOM   11892 C  CD2    . PHE   B 1 348 ? 19.668  -23.254 31.340 1.00 16.33  ?  373 PHE   B CD2    1 
ATOM   11893 C  CE1    . PHE   B 1 348 ? 20.238  -25.112 29.398 1.00 16.94  ?  373 PHE   B CE1    1 
ATOM   11894 C  CE2    . PHE   B 1 348 ? 20.769  -24.073 31.457 1.00 15.99  ?  373 PHE   B CE2    1 
ATOM   11895 C  CZ     . PHE   B 1 348 ? 21.038  -25.016 30.498 1.00 16.14  ?  373 PHE   B CZ     1 
ATOM   11896 H  H      . PHE   B 1 348 ? 15.671  -24.138 29.083 1.00 18.73  ?  373 PHE   B H      1 
ATOM   11897 H  HA     . PHE   B 1 348 ? 16.297  -23.105 31.478 1.00 17.96  ?  373 PHE   B HA     1 
ATOM   11898 H  HB2    . PHE   B 1 348 ? 17.599  -22.147 29.157 1.00 17.46  ?  373 PHE   B HB2    1 
ATOM   11899 H  HB3    . PHE   B 1 348 ? 17.839  -21.615 30.635 1.00 17.46  ?  373 PHE   B HB3    1 
ATOM   11900 H  HD1    . PHE   B 1 348 ? 18.599  -24.354 28.507 1.00 19.62  ?  373 PHE   B HD1    1 
ATOM   11901 H  HD2    . PHE   B 1 348 ? 19.488  -22.628 32.004 1.00 19.59  ?  373 PHE   B HD2    1 
ATOM   11902 H  HE1    . PHE   B 1 348 ? 20.433  -25.735 28.736 1.00 20.32  ?  373 PHE   B HE1    1 
ATOM   11903 H  HE2    . PHE   B 1 348 ? 21.333  -23.986 32.192 1.00 19.18  ?  373 PHE   B HE2    1 
ATOM   11904 H  HZ     . PHE   B 1 348 ? 21.764  -25.588 30.598 1.00 19.37  ?  373 PHE   B HZ     1 
ATOM   11905 N  N      . ASP   B 1 349 ? 15.136  -20.854 30.904 1.00 15.93  ?  374 ASP   B N      1 
ATOM   11906 C  CA     . ASP   B 1 349 ? 14.156  -19.803 30.629 1.00 17.66  ?  374 ASP   B CA     1 
ATOM   11907 C  C      . ASP   B 1 349 ? 14.450  -19.041 29.339 1.00 18.46  ?  374 ASP   B C      1 
ATOM   11908 O  O      . ASP   B 1 349 ? 13.535  -18.464 28.734 1.00 20.87  ?  374 ASP   B O      1 
ATOM   11909 C  CB     . ASP   B 1 349 ? 14.108  -18.758 31.752 1.00 20.64  ?  374 ASP   B CB     1 
ATOM   11910 C  CG     . ASP   B 1 349 ? 13.476  -19.260 33.022 1.00 23.25  ?  374 ASP   B CG     1 
ATOM   11911 O  OD1    . ASP   B 1 349 ? 12.468  -19.992 32.959 1.00 23.91  ?  374 ASP   B OD1    1 
ATOM   11912 O  OD2    . ASP   B 1 349 ? 13.984  -18.879 34.096 1.00 24.00  ?  374 ASP   B OD2    1 
ATOM   11913 H  H      . ASP   B 1 349 ? 15.653  -20.687 31.570 1.00 19.11  ?  374 ASP   B H      1 
ATOM   11914 H  HA     . ASP   B 1 349 ? 13.301  -20.257 30.565 1.00 21.19  ?  374 ASP   B HA     1 
ATOM   11915 H  HB2    . ASP   B 1 349 ? 15.015  -18.484 31.961 1.00 24.76  ?  374 ASP   B HB2    1 
ATOM   11916 H  HB3    . ASP   B 1 349 ? 13.593  -17.995 31.446 1.00 24.76  ?  374 ASP   B HB3    1 
ATOM   11917 N  N      . SER   B 1 350 ? 15.714  -18.978 28.932 1.00 17.06  ?  375 SER   B N      1 
ATOM   11918 C  CA     . SER   B 1 350 ? 16.120  -18.093 27.851 1.00 17.24  ?  375 SER   B CA     1 
ATOM   11919 C  C      . SER   B 1 350 ? 17.344  -18.667 27.155 1.00 16.02  ?  375 SER   B C      1 
ATOM   11920 O  O      . SER   B 1 350 ? 17.999  -19.582 27.660 1.00 15.58  ?  375 SER   B O      1 
ATOM   11921 C  CB     . SER   B 1 350 ? 16.447  -16.693 28.371 1.00 22.30  ?  375 SER   B CB     1 
ATOM   11922 O  OG     . SER   B 1 350 ? 17.654  -16.748 29.104 1.00 25.32  ?  375 SER   B OG     1 
ATOM   11923 H  H      . SER   B 1 350 ? 16.357  -19.440 29.269 1.00 20.46  ?  375 SER   B H      1 
ATOM   11924 H  HA     . SER   B 1 350 ? 15.391  -18.042 27.213 1.00 20.68  ?  375 SER   B HA     1 
ATOM   11925 H  HB2    . SER   B 1 350 ? 16.551  -16.085 27.622 1.00 26.75  ?  375 SER   B HB2    1 
ATOM   11926 H  HB3    . SER   B 1 350 ? 15.731  -16.387 28.950 1.00 26.75  ?  375 SER   B HB3    1 
ATOM   11927 H  HG     . SER   B 1 350 ? 17.566  -17.259 29.765 1.00 30.37  ?  375 SER   B HG     1 
ATOM   11928 N  N      . GLN   B 1 351 ? 17.663  -18.089 25.993 1.00 16.72  ?  376 GLN   B N      1 
ATOM   11929 C  CA     . GLN   B 1 351 ? 18.874  -18.456 25.272 1.00 17.01  ?  376 GLN   B CA     1 
ATOM   11930 C  C      . GLN   B 1 351 ? 20.128  -18.246 26.108 1.00 16.30  ?  376 GLN   B C      1 
ATOM   11931 O  O      . GLN   B 1 351 ? 21.118  -18.950 25.900 1.00 18.17  ?  376 GLN   B O      1 
ATOM   11932 C  CB     . GLN   B 1 351 ? 18.962  -17.651 23.968 1.00 17.80  ?  376 GLN   B CB     1 
ATOM   11933 C  CG     . GLN   B 1 351 ? 20.241  -17.853 23.152 1.00 19.67  ?  376 GLN   B CG     1 
ATOM   11934 C  CD     . GLN   B 1 351 ? 20.407  -19.270 22.625 1.00 21.07  ?  376 GLN   B CD     1 
ATOM   11935 O  OE1    . GLN   B 1 351 ? 19.420  -19.961 22.336 1.00 22.82  ?  376 GLN   B OE1    1 
ATOM   11936 N  NE2    . GLN   B 1 351 ? 21.658  -19.712 22.490 1.00 20.72  ?  376 GLN   B NE2    1 
ATOM   11937 H  H      . GLN   B 1 351 ? 17.194  -17.482 25.604 1.00 20.06  ?  376 GLN   B H      1 
ATOM   11938 H  HA     . GLN   B 1 351 ? 18.829  -19.399 25.050 1.00 20.41  ?  376 GLN   B HA     1 
ATOM   11939 H  HB2    . GLN   B 1 351 ? 18.216  -17.905 23.402 1.00 21.35  ?  376 GLN   B HB2    1 
ATOM   11940 H  HB3    . GLN   B 1 351 ? 18.906  -16.708 24.187 1.00 21.35  ?  376 GLN   B HB3    1 
ATOM   11941 H  HG2    . GLN   B 1 351 ? 20.225  -17.253 22.391 1.00 23.60  ?  376 GLN   B HG2    1 
ATOM   11942 H  HG3    . GLN   B 1 351 ? 21.006  -17.655 23.715 1.00 23.60  ?  376 GLN   B HG3    1 
ATOM   11943 H  HE21   . GLN   B 1 351 ? 22.319  -19.202 22.698 1.00 24.85  ?  376 GLN   B HE21   1 
ATOM   11944 H  HE22   . GLN   B 1 351 ? 21.804  -20.507 22.196 1.00 24.85  ?  376 GLN   B HE22   1 
ATOM   11945 N  N      . THR   B 1 352 ? 20.122  -17.290 27.047 1.00 16.38  ?  377 THR   B N      1 
ATOM   11946 C  CA     . THR   B 1 352 ? 21.340  -17.028 27.815 1.00 16.60  ?  377 THR   B CA     1 
ATOM   11947 C  C      . THR   B 1 352 ? 21.644  -18.111 28.852 1.00 16.36  ?  377 THR   B C      1 
ATOM   11948 O  O      . THR   B 1 352 ? 22.765  -18.124 29.381 1.00 18.00  ?  377 THR   B O      1 
ATOM   11949 C  CB     . THR   B 1 352 ? 21.290  -15.671 28.534 1.00 18.34  ?  377 THR   B CB     1 
ATOM   11950 O  OG1    . THR   B 1 352 ? 20.157  -15.619 29.417 1.00 19.96  ?  377 THR   B OG1    1 
ATOM   11951 C  CG2    . THR   B 1 352 ? 21.227  -14.528 27.530 1.00 20.40  ?  377 THR   B CG2    1 
ATOM   11952 H  H      . THR   B 1 352 ? 19.447  -16.798 27.250 1.00 19.65  ?  377 THR   B H      1 
ATOM   11953 H  HA     . THR   B 1 352 ? 22.065  -16.992 27.171 1.00 19.92  ?  377 THR   B HA     1 
ATOM   11954 H  HB     . THR   B 1 352 ? 22.097  -15.559 29.061 1.00 22.00  ?  377 THR   B HB     1 
ATOM   11955 H  HG1    . THR   B 1 352 ? 19.446  -15.698 28.976 1.00 23.94  ?  377 THR   B HG1    1 
ATOM   11956 H  HG21   . THR   B 1 352 ? 21.185  -13.678 27.996 1.00 24.48  ?  377 THR   B HG21   1 
ATOM   11957 H  HG22   . THR   B 1 352 ? 22.017  -14.538 26.966 1.00 24.48  ?  377 THR   B HG22   1 
ATOM   11958 H  HG23   . THR   B 1 352 ? 20.440  -14.620 26.971 1.00 24.48  ?  377 THR   B HG23   1 
ATOM   11959 N  N      . LYS   B 1 353 ? 20.666  -18.970 29.168 1.00 15.82  ?  378 LYS   B N      1 
ATOM   11960 C  CA     A LYS   B 1 353 ? 20.860  -20.188 29.968 0.24 15.41  ?  378 LYS   B CA     1 
ATOM   11961 C  CA     B LYS   B 1 353 ? 20.879  -20.185 29.962 0.76 14.93  ?  378 LYS   B CA     1 
ATOM   11962 C  C      . LYS   B 1 353 ? 21.403  -19.893 31.364 1.00 15.67  ?  378 LYS   B C      1 
ATOM   11963 O  O      . LYS   B 1 353 ? 22.226  -20.634 31.904 1.00 17.44  ?  378 LYS   B O      1 
ATOM   11964 C  CB     A LYS   B 1 353 ? 21.743  -21.190 29.212 0.24 15.17  ?  378 LYS   B CB     1 
ATOM   11965 C  CB     B LYS   B 1 353 ? 21.802  -21.158 29.227 0.76 15.69  ?  378 LYS   B CB     1 
ATOM   11966 C  CG     A LYS   B 1 353 ? 21.106  -21.636 27.894 0.24 15.25  ?  378 LYS   B CG     1 
ATOM   11967 C  CG     B LYS   B 1 353 ? 21.230  -21.612 27.889 0.76 16.72  ?  378 LYS   B CG     1 
ATOM   11968 C  CD     A LYS   B 1 353 ? 21.895  -22.738 27.206 0.24 16.58  ?  378 LYS   B CD     1 
ATOM   11969 C  CD     B LYS   B 1 353 ? 22.230  -22.492 27.175 0.76 21.53  ?  378 LYS   B CD     1 
ATOM   11970 C  CE     A LYS   B 1 353 ? 22.602  -22.229 25.961 0.24 18.37  ?  378 LYS   B CE     1 
ATOM   11971 C  CE     B LYS   B 1 353 ? 21.876  -22.775 25.743 0.76 23.47  ?  378 LYS   B CE     1 
ATOM   11972 N  NZ     A LYS   B 1 353 ? 21.634  -21.910 24.873 0.24 18.57  ?  378 LYS   B NZ     1 
ATOM   11973 N  NZ     B LYS   B 1 353 ? 23.089  -23.319 24.995 0.76 24.85  ?  378 LYS   B NZ     1 
ATOM   11974 H  H      A LYS   B 1 353 ? 19.849  -18.865 28.922 0.24 18.97  ?  378 LYS   B H      1 
ATOM   11975 H  H      B LYS   B 1 353 ? 19.847  -18.867 28.927 0.76 18.97  ?  378 LYS   B H      1 
ATOM   11976 H  HA     A LYS   B 1 353 ? 19.992  -20.598 30.111 0.24 18.48  ?  378 LYS   B HA     1 
ATOM   11977 H  HA     B LYS   B 1 353 ? 20.014  -20.608 30.083 0.76 17.91  ?  378 LYS   B HA     1 
ATOM   11978 H  HB2    A LYS   B 1 353 ? 22.596  -20.774 29.012 0.24 18.20  ?  378 LYS   B HB2    1 
ATOM   11979 H  HB2    B LYS   B 1 353 ? 22.652  -20.722 29.058 0.76 18.82  ?  378 LYS   B HB2    1 
ATOM   11980 H  HB3    A LYS   B 1 353 ? 21.879  -21.976 29.765 0.24 18.20  ?  378 LYS   B HB3    1 
ATOM   11981 H  HB3    B LYS   B 1 353 ? 21.936  -21.945 29.779 0.76 18.82  ?  378 LYS   B HB3    1 
ATOM   11982 H  HG2    A LYS   B 1 353 ? 20.213  -21.972 28.071 0.24 18.29  ?  378 LYS   B HG2    1 
ATOM   11983 H  HG2    B LYS   B 1 353 ? 20.417  -22.120 28.036 0.76 20.05  ?  378 LYS   B HG2    1 
ATOM   11984 H  HG3    A LYS   B 1 353 ? 21.061  -20.878 27.291 0.24 18.29  ?  378 LYS   B HG3    1 
ATOM   11985 H  HG3    B LYS   B 1 353 ? 21.043  -20.839 27.334 0.76 20.05  ?  378 LYS   B HG3    1 
ATOM   11986 H  HD2    A LYS   B 1 353 ? 22.565  -23.082 27.817 0.24 19.89  ?  378 LYS   B HD2    1 
ATOM   11987 H  HD2    B LYS   B 1 353 ? 23.094  -22.052 27.184 0.76 25.83  ?  378 LYS   B HD2    1 
ATOM   11988 H  HD3    A LYS   B 1 353 ? 21.290  -23.450 26.943 0.24 19.89  ?  378 LYS   B HD3    1 
ATOM   11989 H  HD3    B LYS   B 1 353 ? 22.285  -23.342 27.639 0.76 25.83  ?  378 LYS   B HD3    1 
ATOM   11990 H  HE2    A LYS   B 1 353 ? 23.094  -21.422 26.179 0.24 22.03  ?  378 LYS   B HE2    1 
ATOM   11991 H  HE2    B LYS   B 1 353 ? 21.167  -23.436 25.707 0.76 28.16  ?  378 LYS   B HE2    1 
ATOM   11992 H  HE3    A LYS   B 1 353 ? 23.211  -22.911 25.637 0.24 22.03  ?  378 LYS   B HE3    1 
ATOM   11993 H  HE3    B LYS   B 1 353 ? 21.587  -21.956 25.310 0.76 28.16  ?  378 LYS   B HE3    1 
ATOM   11994 H  HZ1    A LYS   B 1 353 ? 21.069  -21.279 25.144 0.24 22.27  ?  378 LYS   B HZ1    1 
ATOM   11995 H  HZ1    B LYS   B 1 353 ? 23.390  -24.055 25.397 0.76 29.82  ?  378 LYS   B HZ1    1 
ATOM   11996 H  HZ2    A LYS   B 1 353 ? 22.070  -21.617 24.154 0.24 22.27  ?  378 LYS   B HZ2    1 
ATOM   11997 H  HZ2    B LYS   B 1 353 ? 22.866  -23.519 24.157 0.76 29.82  ?  378 LYS   B HZ2    1 
ATOM   11998 H  HZ3    A LYS   B 1 353 ? 21.172  -22.638 24.654 0.24 22.27  ?  378 LYS   B HZ3    1 
ATOM   11999 H  HZ3    B LYS   B 1 353 ? 23.738  -22.711 24.984 0.76 29.82  ?  378 LYS   B HZ3    1 
ATOM   12000 N  N      . GLU   B 1 354 ? 20.869  -18.839 31.987 1.00 15.82  ?  379 GLU   B N      1 
ATOM   12001 C  CA     . GLU   B 1 354 ? 21.228  -18.506 33.365 1.00 15.76  ?  379 GLU   B CA     1 
ATOM   12002 C  C      . GLU   B 1 354 ? 20.424  -19.294 34.402 1.00 15.66  ?  379 GLU   B C      1 
ATOM   12003 O  O      . GLU   B 1 354 ? 20.888  -19.428 35.538 1.00 15.98  ?  379 GLU   B O      1 
ATOM   12004 C  CB     . GLU   B 1 354 ? 21.070  -16.994 33.589 1.00 17.79  ?  379 GLU   B CB     1 
ATOM   12005 C  CG     . GLU   B 1 354 ? 22.087  -16.217 32.751 1.00 20.75  ?  379 GLU   B CG     1 
ATOM   12006 C  CD     . GLU   B 1 354 ? 21.956  -14.705 32.722 1.00 27.94  ?  379 GLU   B CD     1 
ATOM   12007 O  OE1    . GLU   B 1 354 ? 21.039  -14.129 33.317 1.00 31.35  ?  379 GLU   B OE1    1 
ATOM   12008 O  OE2    . GLU   B 1 354 ? 22.810  -14.074 32.067 1.00 31.21  ?  379 GLU   B OE2    1 
ATOM   12009 H  H      . GLU   B 1 354 ? 20.298  -18.302 31.633 1.00 18.98  ?  379 GLU   B H      1 
ATOM   12010 H  HA     . GLU   B 1 354 ? 22.161  -18.727 33.512 1.00 18.90  ?  379 GLU   B HA     1 
ATOM   12011 H  HB2    . GLU   B 1 354 ? 20.178  -16.720 33.327 1.00 21.34  ?  379 GLU   B HB2    1 
ATOM   12012 H  HB3    . GLU   B 1 354 ? 21.219  -16.788 34.526 1.00 21.34  ?  379 GLU   B HB3    1 
ATOM   12013 H  HG2    . GLU   B 1 354 ? 22.972  -16.416 33.095 1.00 24.89  ?  379 GLU   B HG2    1 
ATOM   12014 H  HG3    . GLU   B 1 354 ? 22.012  -16.522 31.833 1.00 24.89  ?  379 GLU   B HG3    1 
ATOM   12015 N  N      . ASN   B 1 355 ? 19.246  -19.815 34.048 1.00 15.38  ?  380 ASN   B N      1 
ATOM   12016 C  CA     . ASN   B 1 355 ? 18.379  -20.522 34.992 1.00 14.03  ?  380 ASN   B CA     1 
ATOM   12017 C  C      . ASN   B 1 355 ? 17.933  -21.833 34.367 1.00 15.03  ?  380 ASN   B C      1 
ATOM   12018 O  O      . ASN   B 1 355 ? 17.252  -21.825 33.339 1.00 15.66  ?  380 ASN   B O      1 
ATOM   12019 C  CB     . ASN   B 1 355 ? 17.157  -19.681 35.379 1.00 15.40  ?  380 ASN   B CB     1 
ATOM   12020 C  CG     . ASN   B 1 355 ? 16.303  -20.343 36.441 1.00 20.08  ?  380 ASN   B CG     1 
ATOM   12021 O  OD1    . ASN   B 1 355 ? 16.804  -20.869 37.425 1.00 23.95  ?  380 ASN   B OD1    1 
ATOM   12022 N  ND2    . ASN   B 1 355 ? 15.000  -20.283 36.259 1.00 22.65  ?  380 ASN   B ND2    1 
ATOM   12023 H  H      . ASN   B 1 355 ? 18.922  -19.769 33.253 1.00 18.44  ?  380 ASN   B H      1 
ATOM   12024 H  HA     . ASN   B 1 355 ? 18.887  -20.717 35.795 1.00 16.83  ?  380 ASN   B HA     1 
ATOM   12025 H  HB2    . ASN   B 1 355 ? 17.459  -18.827 35.726 1.00 18.48  ?  380 ASN   B HB2    1 
ATOM   12026 H  HB3    . ASN   B 1 355 ? 16.606  -19.544 34.593 1.00 18.48  ?  380 ASN   B HB3    1 
ATOM   12027 H  HD21   . ASN   B 1 355 ? 14.469  -20.643 36.832 1.00 27.17  ?  380 ASN   B HD21   1 
ATOM   12028 H  HD22   . ASN   B 1 355 ? 14.680  -19.885 35.567 1.00 27.17  ?  380 ASN   B HD22   1 
ATOM   12029 N  N      . MET   B 1 356 ? 18.321  -22.947 34.980 1.00 14.96  ?  381 MET   B N      1 
ATOM   12030 C  CA     . MET   B 1 356 ? 18.067  -24.283 34.435 1.00 14.67  ?  381 MET   B CA     1 
ATOM   12031 C  C      . MET   B 1 356 ? 16.787  -24.841 35.058 1.00 14.92  ?  381 MET   B C      1 
ATOM   12032 O  O      . MET   B 1 356 ? 16.716  -25.036 36.278 1.00 16.31  ?  381 MET   B O      1 
ATOM   12033 C  CB     . MET   B 1 356 ? 19.281  -25.177 34.703 1.00 15.68  ?  381 MET   B CB     1 
ATOM   12034 C  CG     . MET   B 1 356 ? 19.448  -26.353 33.756 1.00 16.24  ?  381 MET   B CG     1 
ATOM   12035 S  SD     . MET   B 1 356 ? 18.284  -27.706 34.026 1.00 17.46  ?  381 MET   B SD     1 
ATOM   12036 C  CE     . MET   B 1 356 ? 18.575  -28.147 35.733 1.00 18.50  ?  381 MET   B CE     1 
ATOM   12037 H  H      . MET   B 1 356 ? 18.742  -22.959 35.730 1.00 17.94  ?  381 MET   B H      1 
ATOM   12038 H  HA     . MET   B 1 356 ? 17.935  -24.244 33.475 1.00 17.60  ?  381 MET   B HA     1 
ATOM   12039 H  HB2    . MET   B 1 356 ? 20.081  -24.634 34.633 1.00 18.81  ?  381 MET   B HB2    1 
ATOM   12040 H  HB3    . MET   B 1 356 ? 19.202  -25.538 35.600 1.00 18.81  ?  381 MET   B HB3    1 
ATOM   12041 H  HG2    . MET   B 1 356 ? 19.324  -26.038 32.847 1.00 19.48  ?  381 MET   B HG2    1 
ATOM   12042 H  HG3    . MET   B 1 356 ? 20.343  -26.712 33.864 1.00 19.48  ?  381 MET   B HG3    1 
ATOM   12043 H  HE1    . MET   B 1 356 ? 18.126  -28.985 35.924 1.00 22.19  ?  381 MET   B HE1    1 
ATOM   12044 H  HE2    . MET   B 1 356 ? 19.530  -28.243 35.876 1.00 22.19  ?  381 MET   B HE2    1 
ATOM   12045 H  HE3    . MET   B 1 356 ? 18.224  -27.446 36.304 1.00 22.19  ?  381 MET   B HE3    1 
ATOM   12046 N  N      . THR   B 1 357 ? 15.776  -25.090 34.215 1.00 14.57  ?  382 THR   B N      1 
ATOM   12047 C  CA     . THR   B 1 357 ? 14.406  -25.348 34.656 1.00 15.29  ?  382 THR   B CA     1 
ATOM   12048 C  C      . THR   B 1 357 ? 13.975  -26.813 34.599 1.00 15.74  ?  382 THR   B C      1 
ATOM   12049 O  O      . THR   B 1 357 ? 12.834  -27.118 34.963 1.00 17.15  ?  382 THR   B O      1 
ATOM   12050 C  CB     . THR   B 1 357 ? 13.428  -24.540 33.792 1.00 16.27  ?  382 THR   B CB     1 
ATOM   12051 O  OG1    . THR   B 1 357 ? 13.628  -24.926 32.420 1.00 17.15  ?  382 THR   B OG1    1 
ATOM   12052 C  CG2    . THR   B 1 357 ? 13.657  -23.041 33.934 1.00 16.71  ?  382 THR   B CG2    1 
ATOM   12053 H  H      . THR   B 1 357 ? 15.865  -25.115 33.360 1.00 17.48  ?  382 THR   B H      1 
ATOM   12054 H  HA     . THR   B 1 357 ? 14.352  -25.066 35.582 1.00 18.35  ?  382 THR   B HA     1 
ATOM   12055 H  HB     . THR   B 1 357 ? 12.516  -24.717 34.073 1.00 19.52  ?  382 THR   B HB     1 
ATOM   12056 H  HG1    . THR   B 1 357 ? 13.095  -24.508 31.923 1.00 20.58  ?  382 THR   B HG1    1 
ATOM   12057 H  HG21   . THR   B 1 357 ? 13.019  -22.555 33.389 1.00 20.05  ?  382 THR   B HG21   1 
ATOM   12058 H  HG22   . THR   B 1 357 ? 13.549  -22.775 34.860 1.00 20.05  ?  382 THR   B HG22   1 
ATOM   12059 H  HG23   . THR   B 1 357 ? 14.555  -22.815 33.644 1.00 20.05  ?  382 THR   B HG23   1 
ATOM   12060 N  N      . LEU   B 1 358 ? 14.833  -27.715 34.130 1.00 15.92  ?  383 LEU   B N      1 
ATOM   12061 C  CA     . LEU   B 1 358 ? 14.461  -29.115 33.972 1.00 16.63  ?  383 LEU   B CA     1 
ATOM   12062 C  C      . LEU   B 1 358 ? 14.223  -29.762 35.330 1.00 18.27  ?  383 LEU   B C      1 
ATOM   12063 O  O      . LEU   B 1 358 ? 15.006  -29.571 36.257 1.00 18.54  ?  383 LEU   B O      1 
ATOM   12064 C  CB     . LEU   B 1 358 ? 15.567  -29.861 33.228 1.00 17.10  ?  383 LEU   B CB     1 
ATOM   12065 C  CG     . LEU   B 1 358 ? 15.302  -31.307 32.806 1.00 17.37  ?  383 LEU   B CG     1 
ATOM   12066 C  CD1    . LEU   B 1 358 ? 14.251  -31.323 31.708 1.00 20.46  ?  383 LEU   B CD1    1 
ATOM   12067 C  CD2    . LEU   B 1 358 ? 16.582  -32.015 32.353 1.00 18.94  ?  383 LEU   B CD2    1 
ATOM   12068 H  H      . LEU   B 1 358 ? 15.641  -27.540 33.895 1.00 19.10  ?  383 LEU   B H      1 
ATOM   12069 H  HA     . LEU   B 1 358 ? 13.641  -29.180 33.458 1.00 19.94  ?  383 LEU   B HA     1 
ATOM   12070 H  HB2    . LEU   B 1 358 ? 15.761  -29.366 32.417 1.00 20.52  ?  383 LEU   B HB2    1 
ATOM   12071 H  HB3    . LEU   B 1 358 ? 16.349  -29.877 33.802 1.00 20.52  ?  383 LEU   B HB3    1 
ATOM   12072 H  HG     . LEU   B 1 358 ? 14.973  -31.804 33.571 1.00 20.84  ?  383 LEU   B HG     1 
ATOM   12073 H  HD11   . LEU   B 1 358 ? 14.116  -32.238 31.413 1.00 24.55  ?  383 LEU   B HD11   1 
ATOM   12074 H  HD12   . LEU   B 1 358 ? 13.421  -30.964 32.059 1.00 24.55  ?  383 LEU   B HD12   1 
ATOM   12075 H  HD13   . LEU   B 1 358 ? 14.559  -30.779 30.966 1.00 24.55  ?  383 LEU   B HD13   1 
ATOM   12076 H  HD21   . LEU   B 1 358 ? 16.374  -32.938 32.143 1.00 22.73  ?  383 LEU   B HD21   1 
ATOM   12077 H  HD22   . LEU   B 1 358 ? 16.929  -31.566 31.566 1.00 22.73  ?  383 LEU   B HD22   1 
ATOM   12078 H  HD23   . LEU   B 1 358 ? 17.234  -31.977 33.070 1.00 22.73  ?  383 LEU   B HD23   1 
ATOM   12079 N  N      . GLN   B 1 359 ? 13.145  -30.547 35.438 1.00 18.38  ?  384 GLN   B N      1 
ATOM   12080 C  CA     . GLN   B 1 359 ? 12.829  -31.239 36.685 1.00 18.94  ?  384 GLN   B CA     1 
ATOM   12081 C  C      . GLN   B 1 359 ? 13.781  -32.410 36.944 1.00 19.75  ?  384 GLN   B C      1 
ATOM   12082 O  O      . GLN   B 1 359 ? 14.230  -33.077 36.009 1.00 19.36  ?  384 GLN   B O      1 
ATOM   12083 C  CB     . GLN   B 1 359 ? 11.394  -31.767 36.651 1.00 20.65  ?  384 GLN   B CB     1 
ATOM   12084 C  CG     . GLN   B 1 359 ? 10.334  -30.688 36.599 1.00 24.37  ?  384 GLN   B CG     1 
ATOM   12085 C  CD     . GLN   B 1 359 ? 10.096  -30.083 37.956 1.00 28.11  ?  384 GLN   B CD     1 
ATOM   12086 O  OE1    . GLN   B 1 359 ? 10.896  -30.260 38.879 1.00 29.24  ?  384 GLN   B OE1    1 
ATOM   12087 N  NE2    . GLN   B 1 359 ? 8.990   -29.366 38.099 1.00 30.10  ?  384 GLN   B NE2    1 
ATOM   12088 H  H      . GLN   B 1 359 ? 12.583  -30.693 34.804 1.00 22.05  ?  384 GLN   B H      1 
ATOM   12089 H  HA     . GLN   B 1 359 ? 12.926  -30.608 37.415 1.00 22.72  ?  384 GLN   B HA     1 
ATOM   12090 H  HB2    . GLN   B 1 359 ? 11.287  -32.322 35.863 1.00 24.78  ?  384 GLN   B HB2    1 
ATOM   12091 H  HB3    . GLN   B 1 359 ? 11.239  -32.292 37.451 1.00 24.78  ?  384 GLN   B HB3    1 
ATOM   12092 H  HG2    . GLN   B 1 359 ? 10.621  -29.985 35.996 1.00 29.24  ?  384 GLN   B HG2    1 
ATOM   12093 H  HG3    . GLN   B 1 359 ? 9.500   -31.073 36.286 1.00 29.24  ?  384 GLN   B HG3    1 
ATOM   12094 H  HE21   . GLN   B 1 359 ? 8.453   -29.268 37.435 1.00 36.12  ?  384 GLN   B HE21   1 
ATOM   12095 H  HE22   . GLN   B 1 359 ? 8.810   -28.999 38.855 1.00 36.12  ?  384 GLN   B HE22   1 
ATOM   12096 N  N      . PRO   B 1 360 ? 14.068  -32.704 38.218 1.00 21.22  ?  385 PRO   B N      1 
ATOM   12097 C  CA     . PRO   B 1 360 ? 15.036  -33.778 38.525 1.00 23.87  ?  385 PRO   B CA     1 
ATOM   12098 C  C      . PRO   B 1 360 ? 14.678  -35.129 37.935 1.00 23.57  ?  385 PRO   B C      1 
ATOM   12099 O  O      . PRO   B 1 360 ? 15.583  -35.918 37.632 1.00 24.99  ?  385 PRO   B O      1 
ATOM   12100 C  CB     . PRO   B 1 360 ? 15.033  -33.824 40.062 1.00 26.35  ?  385 PRO   B CB     1 
ATOM   12101 C  CG     . PRO   B 1 360 ? 14.745  -32.399 40.451 1.00 25.53  ?  385 PRO   B CG     1 
ATOM   12102 C  CD     . PRO   B 1 360 ? 13.739  -31.899 39.410 1.00 23.31  ?  385 PRO   B CD     1 
ATOM   12103 H  HA     . PRO   B 1 360 ? 15.913  -33.517 38.203 1.00 28.64  ?  385 PRO   B HA     1 
ATOM   12104 H  HB2    . PRO   B 1 360 ? 14.341  -34.424 40.380 1.00 31.61  ?  385 PRO   B HB2    1 
ATOM   12105 H  HB3    . PRO   B 1 360 ? 15.899  -34.112 40.391 1.00 31.61  ?  385 PRO   B HB3    1 
ATOM   12106 H  HG2    . PRO   B 1 360 ? 14.364  -32.371 41.343 1.00 30.63  ?  385 PRO   B HG2    1 
ATOM   12107 H  HG3    . PRO   B 1 360 ? 15.561  -31.877 40.423 1.00 30.63  ?  385 PRO   B HG3    1 
ATOM   12108 H  HD2    . PRO   B 1 360 ? 12.828  -32.066 39.700 1.00 27.96  ?  385 PRO   B HD2    1 
ATOM   12109 H  HD3    . PRO   B 1 360 ? 13.863  -30.953 39.235 1.00 27.96  ?  385 PRO   B HD3    1 
ATOM   12110 N  N      . LYS   B 1 361 ? 13.392  -35.433 37.767 1.00 24.92  ?  386 LYS   B N      1 
ATOM   12111 C  CA     . LYS   B 1 361 ? 13.025  -36.718 37.189 1.00 27.38  ?  386 LYS   B CA     1 
ATOM   12112 C  C      . LYS   B 1 361 ? 13.620  -36.908 35.800 1.00 27.39  ?  386 LYS   B C      1 
ATOM   12113 O  O      . LYS   B 1 361 ? 13.744  -38.051 35.346 1.00 29.19  ?  386 LYS   B O      1 
ATOM   12114 C  CB     . LYS   B 1 361 ? 11.504  -36.868 37.124 1.00 30.29  ?  386 LYS   B CB     1 
ATOM   12115 C  CG     . LYS   B 1 361 ? 10.798  -35.918 36.173 1.00 31.94  ?  386 LYS   B CG     1 
ATOM   12116 C  CD     . LYS   B 1 361 ? 9.286   -36.116 36.234 1.00 36.93  ?  386 LYS   B CD     1 
ATOM   12117 C  CE     . LYS   B 1 361 ? 8.602   -35.480 35.046 1.00 43.74  ?  386 LYS   B CE     1 
ATOM   12118 N  NZ     . LYS   B 1 361 ? 8.759   -36.296 33.797 1.00 47.74  ?  386 LYS   B NZ     1 
ATOM   12119 H  H      . LYS   B 1 361 ? 12.731  -34.924 37.976 1.00 29.89  ?  386 LYS   B H      1 
ATOM   12120 H  HA     . LYS   B 1 361 ? 13.364  -37.420 37.767 1.00 32.85  ?  386 LYS   B HA     1 
ATOM   12121 H  HB2    . LYS   B 1 361 ? 11.299  -37.772 36.836 1.00 36.34  ?  386 LYS   B HB2    1 
ATOM   12122 H  HB3    . LYS   B 1 361 ? 11.143  -36.712 38.010 1.00 36.34  ?  386 LYS   B HB3    1 
ATOM   12123 H  HG2    . LYS   B 1 361 ? 10.999  -35.002 36.421 1.00 38.32  ?  386 LYS   B HG2    1 
ATOM   12124 H  HG3    . LYS   B 1 361 ? 11.094  -36.088 35.265 1.00 38.32  ?  386 LYS   B HG3    1 
ATOM   12125 H  HD2    . LYS   B 1 361 ? 9.084   -37.065 36.231 1.00 44.31  ?  386 LYS   B HD2    1 
ATOM   12126 H  HD3    . LYS   B 1 361 ? 8.939   -35.707 37.043 1.00 44.31  ?  386 LYS   B HD3    1 
ATOM   12127 H  HE2    . LYS   B 1 361 ? 7.655   -35.392 35.233 1.00 52.48  ?  386 LYS   B HE2    1 
ATOM   12128 H  HE3    . LYS   B 1 361 ? 8.991   -34.605 34.887 1.00 52.48  ?  386 LYS   B HE3    1 
ATOM   12129 H  HZ1    . LYS   B 1 361 ? 8.353   -35.891 33.116 1.00 57.28  ?  386 LYS   B HZ1    1 
ATOM   12130 H  HZ2    . LYS   B 1 361 ? 9.622   -36.392 33.602 1.00 57.28  ?  386 LYS   B HZ2    1 
ATOM   12131 H  HZ3    . LYS   B 1 361 ? 8.397   -37.101 33.912 1.00 57.28  ?  386 LYS   B HZ3    1 
ATOM   12132 N  N      . SER   B 1 362 ? 14.011  -35.822 35.131 1.00 24.25  ?  387 SER   B N      1 
ATOM   12133 C  CA     . SER   B 1 362 ? 14.554  -35.885 33.782 1.00 24.13  ?  387 SER   B CA     1 
ATOM   12134 C  C      . SER   B 1 362 ? 16.071  -35.696 33.708 1.00 22.47  ?  387 SER   B C      1 
ATOM   12135 O  O      . SER   B 1 362 ? 16.617  -35.693 32.602 1.00 23.10  ?  387 SER   B O      1 
ATOM   12136 C  CB     . SER   B 1 362 ? 13.864  -34.833 32.896 1.00 23.71  ?  387 SER   B CB     1 
ATOM   12137 O  OG     . SER   B 1 362 ? 12.466  -35.083 32.780 1.00 27.27  ?  387 SER   B OG     1 
ATOM   12138 H  H      . SER   B 1 362 ? 13.969  -35.023 35.447 1.00 29.09  ?  387 SER   B H      1 
ATOM   12139 H  HA     . SER   B 1 362 ? 14.363  -36.767 33.425 1.00 28.95  ?  387 SER   B HA     1 
ATOM   12140 H  HB2    . SER   B 1 362 ? 13.994  -33.957 33.292 1.00 28.44  ?  387 SER   B HB2    1 
ATOM   12141 H  HB3    . SER   B 1 362 ? 14.262  -34.859 32.011 1.00 28.44  ?  387 SER   B HB3    1 
ATOM   12142 H  HG     . SER   B 1 362 ? 12.107  -34.494 32.302 1.00 32.72  ?  387 SER   B HG     1 
ATOM   12143 N  N      . PHE   B 1 363 ? 16.768  -35.557 34.844 1.00 21.56  ?  388 PHE   B N      1 
ATOM   12144 C  CA     . PHE   B 1 363 ? 18.196  -35.234 34.807 1.00 20.20  ?  388 PHE   B CA     1 
ATOM   12145 C  C      . PHE   B 1 363 ? 19.027  -36.309 34.099 1.00 20.42  ?  388 PHE   B C      1 
ATOM   12146 O  O      . PHE   B 1 363 ? 20.066  -36.007 33.498 1.00 20.25  ?  388 PHE   B O      1 
ATOM   12147 C  CB     . PHE   B 1 363 ? 18.763  -35.082 36.218 1.00 20.28  ?  388 PHE   B CB     1 
ATOM   12148 C  CG     . PHE   B 1 363 ? 18.390  -33.814 36.925 1.00 19.83  ?  388 PHE   B CG     1 
ATOM   12149 C  CD1    . PHE   B 1 363 ? 17.740  -32.782 36.275 1.00 19.44  ?  388 PHE   B CD1    1 
ATOM   12150 C  CD2    . PHE   B 1 363 ? 18.715  -33.658 38.258 1.00 21.29  ?  388 PHE   B CD2    1 
ATOM   12151 C  CE1    . PHE   B 1 363 ? 17.412  -31.612 36.952 1.00 21.26  ?  388 PHE   B CE1    1 
ATOM   12152 C  CE2    . PHE   B 1 363 ? 18.396  -32.501 38.934 1.00 21.21  ?  388 PHE   B CE2    1 
ATOM   12153 C  CZ     . PHE   B 1 363 ? 17.746  -31.467 38.271 1.00 20.93  ?  388 PHE   B CZ     1 
ATOM   12154 H  H      . PHE   B 1 363 ? 16.441  -35.644 35.635 1.00 25.87  ?  388 PHE   B H      1 
ATOM   12155 H  HA     . PHE   B 1 363 ? 18.267  -34.395 34.325 1.00 24.23  ?  388 PHE   B HA     1 
ATOM   12156 H  HB2    . PHE   B 1 363 ? 18.441  -35.820 36.759 1.00 24.33  ?  388 PHE   B HB2    1 
ATOM   12157 H  HB3    . PHE   B 1 363 ? 19.731  -35.109 36.163 1.00 24.33  ?  388 PHE   B HB3    1 
ATOM   12158 H  HD1    . PHE   B 1 363 ? 17.519  -32.870 35.376 1.00 23.32  ?  388 PHE   B HD1    1 
ATOM   12159 H  HD2    . PHE   B 1 363 ? 19.156  -34.344 38.705 1.00 25.54  ?  388 PHE   B HD2    1 
ATOM   12160 H  HE1    . PHE   B 1 363 ? 16.966  -30.928 36.508 1.00 25.51  ?  388 PHE   B HE1    1 
ATOM   12161 H  HE2    . PHE   B 1 363 ? 18.615  -32.412 39.833 1.00 25.45  ?  388 PHE   B HE2    1 
ATOM   12162 H  HZ     . PHE   B 1 363 ? 17.538  -30.681 38.722 1.00 25.11  ?  388 PHE   B HZ     1 
ATOM   12163 N  N      . GLY   B 1 364 ? 18.645  -37.579 34.246 1.00 21.71  ?  389 GLY   B N      1 
ATOM   12164 C  CA     . GLY   B 1 364 ? 19.453  -38.682 33.758 1.00 22.72  ?  389 GLY   B CA     1 
ATOM   12165 C  C      . GLY   B 1 364 ? 20.435  -39.230 34.768 1.00 23.45  ?  389 GLY   B C      1 
ATOM   12166 O  O      . GLY   B 1 364 ? 21.211  -40.139 34.438 1.00 25.42  ?  389 GLY   B O      1 
ATOM   12167 H  H      . GLY   B 1 364 ? 17.916  -37.824 34.630 1.00 26.05  ?  389 GLY   B H      1 
ATOM   12168 H  HA2    . GLY   B 1 364 ? 18.866  -39.405 33.490 1.00 27.25  ?  389 GLY   B HA2    1 
ATOM   12169 H  HA3    . GLY   B 1 364 ? 19.957  -38.381 32.985 1.00 27.25  ?  389 GLY   B HA3    1 
ATOM   12170 N  N      . SER   B 1 365 ? 20.429  -38.691 35.981 1.00 22.31  ?  390 SER   B N      1 
ATOM   12171 C  CA     . SER   B 1 365 ? 21.304  -39.114 37.065 1.00 24.48  ?  390 SER   B CA     1 
ATOM   12172 C  C      . SER   B 1 365 ? 20.653  -38.612 38.344 1.00 25.18  ?  390 SER   B C      1 
ATOM   12173 O  O      . SER   B 1 365 ? 19.711  -37.811 38.306 1.00 24.18  ?  390 SER   B O      1 
ATOM   12174 C  CB     . SER   B 1 365 ? 22.725  -38.570 36.904 1.00 24.06  ?  390 SER   B CB     1 
ATOM   12175 O  OG     . SER   B 1 365 ? 22.758  -37.154 36.848 1.00 24.30  ?  390 SER   B OG     1 
ATOM   12176 H  H      . SER   B 1 365 ? 19.904  -38.051 36.211 1.00 26.76  ?  390 SER   B H      1 
ATOM   12177 H  HA     . SER   B 1 365 ? 21.380  -40.081 37.088 1.00 29.37  ?  390 SER   B HA     1 
ATOM   12178 H  HB2    . SER   B 1 365 ? 23.257  -38.862 37.661 1.00 28.86  ?  390 SER   B HB2    1 
ATOM   12179 H  HB3    . SER   B 1 365 ? 23.100  -38.920 36.080 1.00 28.86  ?  390 SER   B HB3    1 
ATOM   12180 H  HG     . SER   B 1 365 ? 22.313  -36.882 36.190 1.00 29.16  ?  390 SER   B HG     1 
ATOM   12181 N  N      . THR   B 1 366 ? 21.159  -39.086 39.475 1.00 26.99  ?  391 THR   B N      1 
ATOM   12182 C  CA     . THR   B 1 366 ? 20.757  -38.597 40.786 1.00 28.21  ?  391 THR   B CA     1 
ATOM   12183 C  C      . THR   B 1 366 ? 21.970  -38.014 41.495 1.00 27.18  ?  391 THR   B C      1 
ATOM   12184 O  O      . THR   B 1 366 ? 23.117  -38.221 41.092 1.00 28.53  ?  391 THR   B O      1 
ATOM   12185 C  CB     . THR   B 1 366 ? 20.133  -39.713 41.633 1.00 30.90  ?  391 THR   B CB     1 
ATOM   12186 O  OG1    . THR   B 1 366 ? 21.136  -40.685 41.936 1.00 32.40  ?  391 THR   B OG1    1 
ATOM   12187 C  CG2    . THR   B 1 366 ? 18.985  -40.359 40.886 1.00 32.49  ?  391 THR   B CG2    1 
ATOM   12188 H  H      . THR   B 1 366 ? 21.753  -39.708 39.509 1.00 32.38  ?  391 THR   B H      1 
ATOM   12189 H  HA     . THR   B 1 366 ? 20.091  -37.899 40.679 1.00 33.85  ?  391 THR   B HA     1 
ATOM   12190 H  HB     . THR   B 1 366 ? 19.781  -39.350 42.461 1.00 37.08  ?  391 THR   B HB     1 
ATOM   12191 H  HG1    . THR   B 1 366 ? 21.701  -40.360 42.466 1.00 38.88  ?  391 THR   B HG1    1 
ATOM   12192 H  HG21   . THR   B 1 366 ? 18.549  -41.016 41.452 1.00 38.99  ?  391 THR   B HG21   1 
ATOM   12193 H  HG22   . THR   B 1 366 ? 18.336  -39.686 40.628 1.00 38.99  ?  391 THR   B HG22   1 
ATOM   12194 H  HG23   . THR   B 1 366 ? 19.315  -40.801 40.088 1.00 38.99  ?  391 THR   B HG23   1 
ATOM   12195 N  N      . CYS   B 1 367 ? 21.703  -37.260 42.570 1.00 25.84  ?  392 CYS   B N      1 
ATOM   12196 C  CA     . CYS   B 1 367 ? 22.754  -36.650 43.385 1.00 27.68  ?  392 CYS   B CA     1 
ATOM   12197 C  C      . CYS   B 1 367 ? 22.284  -36.708 44.840 1.00 30.70  ?  392 CYS   B C      1 
ATOM   12198 O  O      . CYS   B 1 367 ? 21.838  -35.706 45.406 1.00 32.19  ?  392 CYS   B O      1 
ATOM   12199 C  CB     . CYS   B 1 367 ? 23.075  -35.217 42.958 1.00 27.30  ?  392 CYS   B CB     1 
ATOM   12200 S  SG     . CYS   B 1 367 ? 24.496  -34.524 43.865 1.00 27.68  ?  392 CYS   B SG     1 
ATOM   12201 H  H      . CYS   B 1 367 ? 20.907  -37.087 42.847 1.00 31.00  ?  392 CYS   B H      1 
ATOM   12202 H  HA     . CYS   B 1 367 ? 23.564  -37.174 43.287 1.00 33.21  ?  392 CYS   B HA     1 
ATOM   12203 H  HB2    . CYS   B 1 367 ? 23.288  -35.208 42.012 1.00 32.75  ?  392 CYS   B HB2    1 
ATOM   12204 H  HB3    . CYS   B 1 367 ? 22.304  -34.655 43.130 1.00 32.75  ?  392 CYS   B HB3    1 
ATOM   12205 H  HG     . CYS   B 1 367 ? 24.690  -33.401 43.488 1.00 33.20  ?  392 CYS   B HG     1 
ATOM   12206 N  N      . GLN   B 1 368 ? 22.375  -37.901 45.427 1.00 31.41  ?  393 GLN   B N      1 
ATOM   12207 C  CA     . GLN   B 1 368 ? 22.029  -38.133 46.827 1.00 32.42  ?  393 GLN   B CA     1 
ATOM   12208 C  C      . GLN   B 1 368 ? 23.299  -37.917 47.643 1.00 30.65  ?  393 GLN   B C      1 
ATOM   12209 O  O      . GLN   B 1 368 ? 24.228  -38.727 47.579 1.00 31.91  ?  393 GLN   B O      1 
ATOM   12210 C  CB     . GLN   B 1 368 ? 21.468  -39.543 47.016 1.00 37.31  ?  393 GLN   B CB     1 
ATOM   12211 C  CG     . GLN   B 1 368 ? 20.377  -39.935 45.994 1.00 44.96  ?  393 GLN   B CG     1 
ATOM   12212 C  CD     . GLN   B 1 368 ? 19.920  -41.398 46.103 1.00 51.67  ?  393 GLN   B CD     1 
ATOM   12213 O  OE1    . GLN   B 1 368 ? 18.724  -41.696 46.008 1.00 54.17  ?  393 GLN   B OE1    1 
ATOM   12214 N  NE2    . GLN   B 1 368 ? 20.873  -42.311 46.283 1.00 53.68  ?  393 GLN   B NE2    1 
ATOM   12215 H  H      . GLN   B 1 368 ? 22.642  -38.612 45.023 1.00 37.69  ?  393 GLN   B H      1 
ATOM   12216 H  HA     . GLN   B 1 368 ? 21.350  -37.506 47.121 1.00 38.90  ?  393 GLN   B HA     1 
ATOM   12217 H  HB2    . GLN   B 1 368 ? 22.194  -40.180 46.929 1.00 44.77  ?  393 GLN   B HB2    1 
ATOM   12218 H  HB3    . GLN   B 1 368 ? 21.077  -39.604 47.902 1.00 44.77  ?  393 GLN   B HB3    1 
ATOM   12219 H  HG2    . GLN   B 1 368 ? 19.601  -39.372 46.136 1.00 53.94  ?  393 GLN   B HG2    1 
ATOM   12220 H  HG3    . GLN   B 1 368 ? 20.726  -39.800 45.099 1.00 53.94  ?  393 GLN   B HG3    1 
ATOM   12221 H  HE21   . GLN   B 1 368 ? 21.697  -42.069 46.333 1.00 64.41  ?  393 GLN   B HE21   1 
ATOM   12222 H  HE22   . GLN   B 1 368 ? 20.664  -43.143 46.349 1.00 64.41  ?  393 GLN   B HE22   1 
ATOM   12223 N  N      . LEU   B 1 369 ? 23.360  -36.809 48.373 1.00 28.91  ?  394 LEU   B N      1 
ATOM   12224 C  CA     . LEU   B 1 369 ? 24.544  -36.517 49.172 1.00 29.59  ?  394 LEU   B CA     1 
ATOM   12225 C  C      . LEU   B 1 369 ? 24.732  -37.595 50.233 1.00 30.27  ?  394 LEU   B C      1 
ATOM   12226 O  O      . LEU   B 1 369 ? 23.766  -38.097 50.809 1.00 31.66  ?  394 LEU   B O      1 
ATOM   12227 C  CB     . LEU   B 1 369 ? 24.418  -35.140 49.819 1.00 29.44  ?  394 LEU   B CB     1 
ATOM   12228 C  CG     . LEU   B 1 369 ? 24.433  -33.970 48.831 1.00 30.42  ?  394 LEU   B CG     1 
ATOM   12229 C  CD1    . LEU   B 1 369 ? 23.922  -32.723 49.516 1.00 30.43  ?  394 LEU   B CD1    1 
ATOM   12230 C  CD2    . LEU   B 1 369 ? 25.825  -33.708 48.249 1.00 31.88  ?  394 LEU   B CD2    1 
ATOM   12231 H  H      . LEU   B 1 369 ? 22.738  -36.217 48.423 1.00 34.69  ?  394 LEU   B H      1 
ATOM   12232 H  HA     . LEU   B 1 369 ? 25.330  -36.504 48.605 1.00 35.50  ?  394 LEU   B HA     1 
ATOM   12233 H  HB2    . LEU   B 1 369 ? 23.580  -35.104 50.305 1.00 35.32  ?  394 LEU   B HB2    1 
ATOM   12234 H  HB3    . LEU   B 1 369 ? 25.162  -35.018 50.430 1.00 35.32  ?  394 LEU   B HB3    1 
ATOM   12235 H  HG     . LEU   B 1 369 ? 23.855  -34.201 48.087 1.00 36.49  ?  394 LEU   B HG     1 
ATOM   12236 H  HD11   . LEU   B 1 369 ? 23.985  -31.976 48.900 1.00 36.50  ?  394 LEU   B HD11   1 
ATOM   12237 H  HD12   . LEU   B 1 369 ? 22.997  -32.861 49.774 1.00 36.50  ?  394 LEU   B HD12   1 
ATOM   12238 H  HD13   . LEU   B 1 369 ? 24.463  -32.550 50.302 1.00 36.50  ?  394 LEU   B HD13   1 
ATOM   12239 H  HD21   . LEU   B 1 369 ? 25.778  -32.947 47.650 1.00 38.25  ?  394 LEU   B HD21   1 
ATOM   12240 H  HD22   . LEU   B 1 369 ? 26.440  -33.521 48.975 1.00 38.25  ?  394 LEU   B HD22   1 
ATOM   12241 H  HD23   . LEU   B 1 369 ? 26.117  -34.495 47.763 1.00 38.25  ?  394 LEU   B HD23   1 
ATOM   12242 N  N      . SER   B 1 370 ? 25.985  -37.947 50.492 1.00 30.74  ?  395 SER   B N      1 
ATOM   12243 C  CA     . SER   B 1 370 ? 26.280  -39.027 51.420 1.00 32.88  ?  395 SER   B CA     1 
ATOM   12244 C  C      . SER   B 1 370 ? 25.929  -38.638 52.855 1.00 33.95  ?  395 SER   B C      1 
ATOM   12245 O  O      . SER   B 1 370 ? 25.892  -37.462 53.219 1.00 32.99  ?  395 SER   B O      1 
ATOM   12246 C  CB     . SER   B 1 370 ? 27.760  -39.390 51.357 1.00 32.97  ?  395 SER   B CB     1 
ATOM   12247 O  OG     . SER   B 1 370 ? 28.524  -38.388 52.014 1.00 33.02  ?  395 SER   B OG     1 
ATOM   12248 H  H      . SER   B 1 370 ? 26.679  -37.577 50.144 1.00 36.88  ?  395 SER   B H      1 
ATOM   12249 H  HA     . SER   B 1 370 ? 25.748  -39.800 51.172 1.00 39.45  ?  395 SER   B HA     1 
ATOM   12250 H  HB2    . SER   B 1 370 ? 27.901  -40.241 51.799 1.00 39.55  ?  395 SER   B HB2    1 
ATOM   12251 H  HB3    . SER   B 1 370 ? 28.038  -39.448 50.430 1.00 39.55  ?  395 SER   B HB3    1 
ATOM   12252 H  HG     . SER   B 1 370 ? 29.341  -38.581 51.979 1.00 39.61  ?  395 SER   B HG     1 
ATOM   12253 N  N      . GLU   B 1 371 ? 25.709  -39.655 53.692 1.00 35.03  ?  396 GLU   B N      1 
ATOM   12254 C  CA     . GLU   B 1 371 ? 25.488  -39.386 55.107 1.00 37.86  ?  396 GLU   B CA     1 
ATOM   12255 C  C      . GLU   B 1 371 ? 26.701  -38.704 55.731 1.00 37.85  ?  396 GLU   B C      1 
ATOM   12256 O  O      . GLU   B 1 371 ? 26.547  -37.901 56.657 1.00 38.30  ?  396 GLU   B O      1 
ATOM   12257 C  CB     . GLU   B 1 371 ? 25.151  -40.678 55.850 1.00 43.17  ?  396 GLU   B CB     1 
ATOM   12258 C  CG     . GLU   B 1 371 ? 23.723  -41.167 55.602 1.00 48.12  ?  396 GLU   B CG     1 
ATOM   12259 C  CD     . GLU   B 1 371 ? 22.654  -40.153 56.017 1.00 53.77  ?  396 GLU   B CD     1 
ATOM   12260 O  OE1    . GLU   B 1 371 ? 22.261  -39.293 55.190 1.00 55.94  ?  396 GLU   B OE1    1 
ATOM   12261 O  OE2    . GLU   B 1 371 ? 22.206  -40.217 57.181 1.00 56.07  ?  396 GLU   B OE2    1 
ATOM   12262 H  H      . GLU   B 1 371 ? 25.684  -40.485 53.469 1.00 42.03  ?  396 GLU   B H      1 
ATOM   12263 H  HA     . GLU   B 1 371 ? 24.725  -38.794 55.201 1.00 45.43  ?  396 GLU   B HA     1 
ATOM   12264 H  HB2    . GLU   B 1 371 ? 25.759  -41.375 55.558 1.00 51.80  ?  396 GLU   B HB2    1 
ATOM   12265 H  HB3    . GLU   B 1 371 ? 25.252  -40.527 56.803 1.00 51.80  ?  396 GLU   B HB3    1 
ATOM   12266 H  HG2    . GLU   B 1 371 ? 23.612  -41.346 54.655 1.00 57.73  ?  396 GLU   B HG2    1 
ATOM   12267 H  HG3    . GLU   B 1 371 ? 23.577  -41.979 56.112 1.00 57.73  ?  396 GLU   B HG3    1 
ATOM   12268 N  N      . LYS   B 1 372 ? 27.906  -38.987 55.226 1.00 37.42  ?  397 LYS   B N      1 
ATOM   12269 C  CA     . LYS   B 1 372 ? 29.097  -38.298 55.714 1.00 38.48  ?  397 LYS   B CA     1 
ATOM   12270 C  C      . LYS   B 1 372 ? 29.042  -36.809 55.394 1.00 35.45  ?  397 LYS   B C      1 
ATOM   12271 O  O      . LYS   B 1 372 ? 29.357  -35.962 56.238 1.00 36.67  ?  397 LYS   B O      1 
ATOM   12272 C  CB     . LYS   B 1 372 ? 30.361  -38.903 55.098 1.00 41.94  ?  397 LYS   B CB     1 
ATOM   12273 C  CG     . LYS   B 1 372 ? 31.638  -38.259 55.621 1.00 47.25  ?  397 LYS   B CG     1 
ATOM   12274 C  CD     . LYS   B 1 372 ? 32.727  -38.166 54.557 1.00 51.56  ?  397 LYS   B CD     1 
ATOM   12275 C  CE     . LYS   B 1 372 ? 33.719  -39.316 54.658 1.00 54.66  ?  397 LYS   B CE     1 
ATOM   12276 N  NZ     . LYS   B 1 372 ? 34.842  -39.156 53.688 1.00 56.75  ?  397 LYS   B NZ     1 
ATOM   12277 H  H      . LYS   B 1 372 ? 28.056  -39.567 54.609 1.00 44.90  ?  397 LYS   B H      1 
ATOM   12278 H  HA     . LYS   B 1 372 ? 29.134  -38.414 56.676 1.00 46.17  ?  397 LYS   B HA     1 
ATOM   12279 H  HB2    . LYS   B 1 372 ? 30.393  -39.849 55.309 1.00 50.33  ?  397 LYS   B HB2    1 
ATOM   12280 H  HB3    . LYS   B 1 372 ? 30.334  -38.778 54.136 1.00 50.33  ?  397 LYS   B HB3    1 
ATOM   12281 H  HG2    . LYS   B 1 372 ? 31.438  -37.360 55.925 1.00 56.70  ?  397 LYS   B HG2    1 
ATOM   12282 H  HG3    . LYS   B 1 372 ? 31.981  -38.790 56.356 1.00 56.70  ?  397 LYS   B HG3    1 
ATOM   12283 H  HD2    . LYS   B 1 372 ? 32.318  -38.194 53.678 1.00 61.87  ?  397 LYS   B HD2    1 
ATOM   12284 H  HD3    . LYS   B 1 372 ? 33.214  -37.334 54.670 1.00 61.87  ?  397 LYS   B HD3    1 
ATOM   12285 H  HE2    . LYS   B 1 372 ? 34.090  -39.341 55.554 1.00 65.59  ?  397 LYS   B HE2    1 
ATOM   12286 H  HE3    . LYS   B 1 372 ? 33.264  -40.150 54.464 1.00 65.59  ?  397 LYS   B HE3    1 
ATOM   12287 H  HZ1    . LYS   B 1 372 ? 35.412  -39.835 53.768 1.00 68.09  ?  397 LYS   B HZ1    1 
ATOM   12288 H  HZ2    . LYS   B 1 372 ? 34.526  -39.141 52.856 1.00 68.09  ?  397 LYS   B HZ2    1 
ATOM   12289 H  HZ3    . LYS   B 1 372 ? 35.276  -38.395 53.847 1.00 68.09  ?  397 LYS   B HZ3    1 
ATOM   12290 N  N      . PHE   B 1 373 ? 28.709  -36.473 54.148 1.00 32.39  ?  398 PHE   B N      1 
ATOM   12291 C  CA     . PHE   B 1 373 ? 28.578  -35.069 53.780 1.00 31.47  ?  398 PHE   B CA     1 
ATOM   12292 C  C      . PHE   B 1 373 ? 27.530  -34.397 54.653 1.00 31.39  ?  398 PHE   B C      1 
ATOM   12293 O  O      . PHE   B 1 373 ? 27.756  -33.315 55.199 1.00 31.37  ?  398 PHE   B O      1 
ATOM   12294 C  CB     . PHE   B 1 373 ? 28.213  -34.948 52.297 1.00 30.55  ?  398 PHE   B CB     1 
ATOM   12295 C  CG     . PHE   B 1 373 ? 28.107  -33.525 51.803 1.00 30.39  ?  398 PHE   B CG     1 
ATOM   12296 C  CD1    . PHE   B 1 373 ? 27.006  -32.743 52.113 1.00 30.43  ?  398 PHE   B CD1    1 
ATOM   12297 C  CD2    . PHE   B 1 373 ? 29.104  -32.980 51.010 1.00 30.66  ?  398 PHE   B CD2    1 
ATOM   12298 C  CE1    . PHE   B 1 373 ? 26.913  -31.443 51.657 1.00 30.15  ?  398 PHE   B CE1    1 
ATOM   12299 C  CE2    . PHE   B 1 373 ? 29.015  -31.679 50.552 1.00 31.50  ?  398 PHE   B CE2    1 
ATOM   12300 C  CZ     . PHE   B 1 373 ? 27.919  -30.912 50.874 1.00 31.40  ?  398 PHE   B CZ     1 
ATOM   12301 H  H      . PHE   B 1 373 ? 28.558  -37.030 53.510 1.00 38.86  ?  398 PHE   B H      1 
ATOM   12302 H  HA     . PHE   B 1 373 ? 29.427  -34.618 53.912 1.00 37.76  ?  398 PHE   B HA     1 
ATOM   12303 H  HB2    . PHE   B 1 373 ? 28.897  -35.393 51.771 1.00 36.66  ?  398 PHE   B HB2    1 
ATOM   12304 H  HB3    . PHE   B 1 373 ? 27.354  -35.375 52.152 1.00 36.66  ?  398 PHE   B HB3    1 
ATOM   12305 H  HD1    . PHE   B 1 373 ? 26.322  -33.097 52.634 1.00 36.50  ?  398 PHE   B HD1    1 
ATOM   12306 H  HD2    . PHE   B 1 373 ? 29.843  -33.497 50.782 1.00 36.79  ?  398 PHE   B HD2    1 
ATOM   12307 H  HE1    . PHE   B 1 373 ? 26.172  -30.925 51.877 1.00 36.18  ?  398 PHE   B HE1    1 
ATOM   12308 H  HE2    . PHE   B 1 373 ? 29.695  -31.322 50.028 1.00 37.79  ?  398 PHE   B HE2    1 
ATOM   12309 H  HZ     . PHE   B 1 373 ? 27.856  -30.037 50.565 1.00 37.67  ?  398 PHE   B HZ     1 
ATOM   12310 N  N      . ILE   B 1 374 ? 26.377  -35.045 54.814 1.00 32.57  ?  399 ILE   B N      1 
ATOM   12311 C  CA     . ILE   B 1 374 ? 25.284  -34.455 55.580 1.00 34.15  ?  399 ILE   B CA     1 
ATOM   12312 C  C      . ILE   B 1 374 ? 25.682  -34.253 57.040 1.00 35.39  ?  399 ILE   B C      1 
ATOM   12313 O  O      . ILE   B 1 374 ? 25.371  -33.217 57.643 1.00 34.26  ?  399 ILE   B O      1 
ATOM   12314 C  CB     . ILE   B 1 374 ? 24.023  -35.332 55.435 1.00 35.17  ?  399 ILE   B CB     1 
ATOM   12315 C  CG1    . ILE   B 1 374 ? 23.504  -35.255 53.991 1.00 34.33  ?  399 ILE   B CG1    1 
ATOM   12316 C  CG2    . ILE   B 1 374 ? 22.969  -34.940 56.461 1.00 36.48  ?  399 ILE   B CG2    1 
ATOM   12317 C  CD1    . ILE   B 1 374 ? 22.971  -33.898 53.575 1.00 34.41  ?  399 ILE   B CD1    1 
ATOM   12318 H  H      . ILE   B 1 374 ? 26.204  -35.823 54.491 1.00 39.08  ?  399 ILE   B H      1 
ATOM   12319 H  HA     . ILE   B 1 374 ? 25.087  -33.576 55.220 1.00 40.97  ?  399 ILE   B HA     1 
ATOM   12320 H  HB     . ILE   B 1 374 ? 24.251  -36.258 55.616 1.00 42.20  ?  399 ILE   B HB     1 
ATOM   12321 H  HG12   . ILE   B 1 374 ? 24.232  -35.479 53.390 1.00 41.19  ?  399 ILE   B HG12   1 
ATOM   12322 H  HG13   . ILE   B 1 374 ? 22.782  -35.895 53.889 1.00 41.19  ?  399 ILE   B HG13   1 
ATOM   12323 H  HG21   . ILE   B 1 374 ? 22.113  -35.308 56.191 1.00 43.77  ?  399 ILE   B HG21   1 
ATOM   12324 H  HG22   . ILE   B 1 374 ? 23.223  -35.296 57.327 1.00 43.77  ?  399 ILE   B HG22   1 
ATOM   12325 H  HG23   . ILE   B 1 374 ? 22.914  -33.973 56.504 1.00 43.77  ?  399 ILE   B HG23   1 
ATOM   12326 H  HD11   . ILE   B 1 374 ? 22.571  -33.972 52.694 1.00 41.29  ?  399 ILE   B HD11   1 
ATOM   12327 H  HD12   . ILE   B 1 374 ? 22.303  -33.610 54.217 1.00 41.29  ?  399 ILE   B HD12   1 
ATOM   12328 H  HD13   . ILE   B 1 374 ? 23.704  -33.263 53.553 1.00 41.29  ?  399 ILE   B HD13   1 
ATOM   12329 N  N      . LYS   B 1 375 ? 26.362  -35.237 57.636 1.00 35.96  ?  400 LYS   B N      1 
ATOM   12330 C  CA     . LYS   B 1 375 ? 26.785  -35.091 59.028 1.00 37.65  ?  400 LYS   B CA     1 
ATOM   12331 C  C      . LYS   B 1 375 ? 27.735  -33.912 59.195 1.00 37.35  ?  400 LYS   B C      1 
ATOM   12332 O  O      . LYS   B 1 375 ? 27.652  -33.164 60.177 1.00 38.54  ?  400 LYS   B O      1 
ATOM   12333 C  CB     . LYS   B 1 375 ? 27.456  -36.373 59.524 1.00 41.51  ?  400 LYS   B CB     1 
ATOM   12334 C  CG     . LYS   B 1 375 ? 26.507  -37.389 60.124 1.00 45.05  ?  400 LYS   B CG     1 
ATOM   12335 C  CD     . LYS   B 1 375 ? 27.254  -38.445 60.949 1.00 47.61  ?  400 LYS   B CD     1 
ATOM   12336 C  CE     . LYS   B 1 375 ? 27.965  -39.461 60.061 1.00 49.75  ?  400 LYS   B CE     1 
ATOM   12337 N  NZ     . LYS   B 1 375 ? 28.653  -40.529 60.853 1.00 50.53  ?  400 LYS   B NZ     1 
ATOM   12338 H  H      . LYS   B 1 375 ? 26.585  -35.980 57.266 1.00 43.15  ?  400 LYS   B H      1 
ATOM   12339 H  HA     . LYS   B 1 375 ? 25.996  -34.934 59.570 1.00 45.18  ?  400 LYS   B HA     1 
ATOM   12340 H  HB2    . LYS   B 1 375 ? 27.903  -36.796 58.774 1.00 49.81  ?  400 LYS   B HB2    1 
ATOM   12341 H  HB3    . LYS   B 1 375 ? 28.104  -36.138 60.207 1.00 49.81  ?  400 LYS   B HB3    1 
ATOM   12342 H  HG2    . LYS   B 1 375 ? 25.879  -36.936 60.707 1.00 54.05  ?  400 LYS   B HG2    1 
ATOM   12343 H  HG3    . LYS   B 1 375 ? 26.031  -37.843 59.411 1.00 54.05  ?  400 LYS   B HG3    1 
ATOM   12344 H  HD2    . LYS   B 1 375 ? 27.919  -38.006 61.502 1.00 57.13  ?  400 LYS   B HD2    1 
ATOM   12345 H  HD3    . LYS   B 1 375 ? 26.620  -38.921 61.508 1.00 57.13  ?  400 LYS   B HD3    1 
ATOM   12346 H  HE2    . LYS   B 1 375 ? 27.314  -39.888 59.482 1.00 59.69  ?  400 LYS   B HE2    1 
ATOM   12347 H  HE3    . LYS   B 1 375 ? 28.634  -39.004 59.528 1.00 59.69  ?  400 LYS   B HE3    1 
ATOM   12348 H  HZ1    . LYS   B 1 375 ? 28.836  -41.226 60.331 1.00 60.63  ?  400 LYS   B HZ1    1 
ATOM   12349 H  HZ2    . LYS   B 1 375 ? 29.414  -40.214 61.192 1.00 60.63  ?  400 LYS   B HZ2    1 
ATOM   12350 H  HZ3    . LYS   B 1 375 ? 28.129  -40.798 61.521 1.00 60.63  ?  400 LYS   B HZ3    1 
ATOM   12351 N  N      . ALA   B 1 376 ? 28.660  -33.737 58.252 1.00 34.79  ?  401 ALA   B N      1 
ATOM   12352 C  CA     . ALA   B 1 376 ? 29.576  -32.608 58.341 1.00 34.32  ?  401 ALA   B CA     1 
ATOM   12353 C  C      . ALA   B 1 376 ? 28.843  -31.288 58.153 1.00 35.84  ?  401 ALA   B C      1 
ATOM   12354 O  O      . ALA   B 1 376 ? 29.204  -30.287 58.781 1.00 37.24  ?  401 ALA   B O      1 
ATOM   12355 C  CB     . ALA   B 1 376 ? 30.690  -32.761 57.309 1.00 32.10  ?  401 ALA   B CB     1 
ATOM   12356 H  H      . ALA   B 1 376 ? 28.773  -34.246 57.568 1.00 41.74  ?  401 ALA   B H      1 
ATOM   12357 H  HA     . ALA   B 1 376 ? 29.987  -32.598 59.219 1.00 41.18  ?  401 ALA   B HA     1 
ATOM   12358 H  HB1    . ALA   B 1 376 ? 31.294  -32.006 57.383 1.00 38.51  ?  401 ALA   B HB1    1 
ATOM   12359 H  HB2    . ALA   B 1 376 ? 31.169  -33.587 57.482 1.00 38.51  ?  401 ALA   B HB2    1 
ATOM   12360 H  HB3    . ALA   B 1 376 ? 30.298  -32.785 56.422 1.00 38.51  ?  401 ALA   B HB3    1 
ATOM   12361 N  N      . ALA   B 1 377 ? 27.814  -31.268 57.299 1.00 35.33  ?  402 ALA   B N      1 
ATOM   12362 C  CA     . ALA   B 1 377 ? 27.015  -30.059 57.132 1.00 36.24  ?  402 ALA   B CA     1 
ATOM   12363 C  C      . ALA   B 1 377 ? 26.275  -29.720 58.419 1.00 39.56  ?  402 ALA   B C      1 
ATOM   12364 O  O      . ALA   B 1 377 ? 26.155  -28.544 58.784 1.00 40.25  ?  402 ALA   B O      1 
ATOM   12365 C  CB     . ALA   B 1 377 ? 26.028  -30.238 55.976 1.00 35.18  ?  402 ALA   B CB     1 
ATOM   12366 H  H      . ALA   B 1 377 ? 27.564  -31.932 56.814 1.00 42.38  ?  402 ALA   B H      1 
ATOM   12367 H  HA     . ALA   B 1 377 ? 27.600  -29.318 56.911 1.00 43.48  ?  402 ALA   B HA     1 
ATOM   12368 H  HB1    . ALA   B 1 377 ? 25.505  -29.428 55.879 1.00 42.21  ?  402 ALA   B HB1    1 
ATOM   12369 H  HB2    . ALA   B 1 377 ? 26.525  -30.411 55.161 1.00 42.21  ?  402 ALA   B HB2    1 
ATOM   12370 H  HB3    . ALA   B 1 377 ? 25.444  -30.988 56.173 1.00 42.21  ?  402 ALA   B HB3    1 
ATOM   12371 N  N      . ILE   B 1 378 ? 25.779  -30.744 59.121 1.00 41.44  ?  403 ILE   B N      1 
ATOM   12372 C  CA     . ILE   B 1 378 ? 25.103  -30.519 60.394 1.00 44.61  ?  403 ILE   B CA     1 
ATOM   12373 C  C      . ILE   B 1 378 ? 26.065  -29.902 61.396 1.00 46.30  ?  403 ILE   B C      1 
ATOM   12374 O  O      . ILE   B 1 378 ? 25.657  -29.104 62.250 1.00 47.73  ?  403 ILE   B O      1 
ATOM   12375 C  CB     . ILE   B 1 378 ? 24.490  -31.838 60.917 1.00 46.07  ?  403 ILE   B CB     1 
ATOM   12376 C  CG1    . ILE   B 1 378 ? 23.409  -32.317 59.940 1.00 47.49  ?  403 ILE   B CG1    1 
ATOM   12377 C  CG2    . ILE   B 1 378 ? 23.934  -31.660 62.335 1.00 45.92  ?  403 ILE   B CG2    1 
ATOM   12378 C  CD1    . ILE   B 1 378 ? 22.637  -33.535 60.393 1.00 48.35  ?  403 ILE   B CD1    1 
ATOM   12379 H  H      . ILE   B 1 378 ? 25.823  -31.569 58.883 1.00 49.72  ?  403 ILE   B H      1 
ATOM   12380 H  HA     . ILE   B 1 378 ? 24.373  -29.896 60.257 1.00 53.53  ?  403 ILE   B HA     1 
ATOM   12381 H  HB     . ILE   B 1 378 ? 25.183  -32.514 60.966 1.00 55.28  ?  403 ILE   B HB     1 
ATOM   12382 H  HG12   . ILE   B 1 378 ? 22.770  -31.599 59.811 1.00 56.99  ?  403 ILE   B HG12   1 
ATOM   12383 H  HG13   . ILE   B 1 378 ? 23.833  -32.539 59.096 1.00 56.99  ?  403 ILE   B HG13   1 
ATOM   12384 H  HG21   . ILE   B 1 378 ? 23.541  -32.498 62.627 1.00 55.10  ?  403 ILE   B HG21   1 
ATOM   12385 H  HG22   . ILE   B 1 378 ? 24.659  -31.411 62.929 1.00 55.10  ?  403 ILE   B HG22   1 
ATOM   12386 H  HG23   . ILE   B 1 378 ? 23.260  -30.963 62.325 1.00 55.10  ?  403 ILE   B HG23   1 
ATOM   12387 H  HD11   . ILE   B 1 378 ? 22.115  -33.874 59.648 1.00 58.02  ?  403 ILE   B HD11   1 
ATOM   12388 H  HD12   . ILE   B 1 378 ? 23.263  -34.213 60.693 1.00 58.02  ?  403 ILE   B HD12   1 
ATOM   12389 H  HD13   . ILE   B 1 378 ? 22.048  -33.283 61.121 1.00 58.02  ?  403 ILE   B HD13   1 
ATOM   12390 N  N      . GLY   B 1 379 ? 27.350  -30.225 61.291 1.00 46.91  ?  404 GLY   B N      1 
ATOM   12391 C  CA     . GLY   B 1 379 ? 28.356  -29.744 62.211 1.00 48.61  ?  404 GLY   B CA     1 
ATOM   12392 C  C      . GLY   B 1 379 ? 29.139  -28.533 61.759 1.00 50.79  ?  404 GLY   B C      1 
ATOM   12393 O  O      . GLY   B 1 379 ? 30.144  -28.195 62.397 1.00 51.52  ?  404 GLY   B O      1 
ATOM   12394 H  H      . GLY   B 1 379 ? 27.666  -30.736 60.676 1.00 56.29  ?  404 GLY   B H      1 
ATOM   12395 H  HA2    . GLY   B 1 379 ? 27.921  -29.514 63.047 1.00 58.32  ?  404 GLY   B HA2    1 
ATOM   12396 H  HA3    . GLY   B 1 379 ? 28.991  -30.459 62.371 1.00 58.32  ?  404 GLY   B HA3    1 
ATOM   12397 N  N      . CYS   B 1 380 ? 28.719  -27.857 60.699 1.00 52.68  ?  405 CYS   B N      1 
ATOM   12398 C  CA     . CYS   B 1 380 ? 29.462  -26.712 60.194 1.00 54.94  ?  405 CYS   B CA     1 
ATOM   12399 C  C      . CYS   B 1 380 ? 29.089  -25.407 60.889 1.00 56.22  ?  405 CYS   B C      1 
ATOM   12400 O  O      . CYS   B 1 380 ? 29.713  -24.378 60.610 1.00 57.60  ?  405 CYS   B O      1 
ATOM   12401 C  CB     . CYS   B 1 380 ? 29.258  -26.569 58.685 1.00 56.88  ?  405 CYS   B CB     1 
ATOM   12402 S  SG     . CYS   B 1 380 ? 27.644  -25.923 58.208 1.00 57.48  ?  405 CYS   B SG     1 
ATOM   12403 H  H      . CYS   B 1 380 ? 28.007  -28.043 60.254 1.00 63.21  ?  405 CYS   B H      1 
ATOM   12404 H  HA     . CYS   B 1 380 ? 30.407  -26.868 60.349 1.00 65.92  ?  405 CYS   B HA     1 
ATOM   12405 H  HB2    . CYS   B 1 380 ? 29.931  -25.962 58.338 1.00 68.25  ?  405 CYS   B HB2    1 
ATOM   12406 H  HB3    . CYS   B 1 380 ? 29.357  -27.442 58.275 1.00 68.25  ?  405 CYS   B HB3    1 
ATOM   12407 H  HG     . CYS   B 1 380 ? 27.592  -25.847 57.011 1.00 68.97  ?  405 CYS   B HG     1 
ATOM   12408 N  N      . GLY   B 1 381 ? 28.096  -25.420 61.780 1.00 55.79  ?  406 GLY   B N      1 
ATOM   12409 C  CA     . GLY   B 1 381 ? 27.750  -24.262 62.581 1.00 54.72  ?  406 GLY   B CA     1 
ATOM   12410 C  C      . GLY   B 1 381 ? 26.418  -23.621 62.256 1.00 53.61  ?  406 GLY   B C      1 
ATOM   12411 O  O      . GLY   B 1 381 ? 25.941  -22.795 63.048 1.00 53.84  ?  406 GLY   B O      1 
ATOM   12412 H  H      . GLY   B 1 381 ? 27.602  -26.106 61.936 1.00 66.94  ?  406 GLY   B H      1 
ATOM   12413 H  HA2    . GLY   B 1 381 ? 27.728  -24.527 63.514 1.00 65.66  ?  406 GLY   B HA2    1 
ATOM   12414 H  HA3    . GLY   B 1 381 ? 28.436  -23.587 62.461 1.00 65.66  ?  406 GLY   B HA3    1 
ATOM   12415 N  N      . ILE   B 1 382 ? 25.803  -23.962 61.122 1.00 50.90  ?  407 ILE   B N      1 
ATOM   12416 C  CA     . ILE   B 1 382 ? 24.506  -23.382 60.787 1.00 49.95  ?  407 ILE   B CA     1 
ATOM   12417 C  C      . ILE   B 1 382 ? 23.458  -23.799 61.812 1.00 50.71  ?  407 ILE   B C      1 
ATOM   12418 O  O      . ILE   B 1 382 ? 22.667  -22.974 62.285 1.00 50.78  ?  407 ILE   B O      1 
ATOM   12419 C  CB     . ILE   B 1 382 ? 24.091  -23.784 59.358 1.00 48.63  ?  407 ILE   B CB     1 
ATOM   12420 C  CG1    . ILE   B 1 382 ? 25.060  -23.184 58.338 1.00 47.80  ?  407 ILE   B CG1    1 
ATOM   12421 C  CG2    . ILE   B 1 382 ? 22.664  -23.338 59.082 1.00 47.96  ?  407 ILE   B CG2    1 
ATOM   12422 C  CD1    . ILE   B 1 382 ? 24.885  -23.723 56.934 1.00 47.49  ?  407 ILE   B CD1    1 
ATOM   12423 H  H      . ILE   B 1 382 ? 26.111  -24.516 60.541 1.00 61.07  ?  407 ILE   B H      1 
ATOM   12424 H  HA     . ILE   B 1 382 ? 24.585  -22.416 60.813 1.00 59.93  ?  407 ILE   B HA     1 
ATOM   12425 H  HB     . ILE   B 1 382 ? 24.128  -24.750 59.281 1.00 58.34  ?  407 ILE   B HB     1 
ATOM   12426 H  HG12   . ILE   B 1 382 ? 24.923  -22.225 58.306 1.00 57.36  ?  407 ILE   B HG12   1 
ATOM   12427 H  HG13   . ILE   B 1 382 ? 25.967  -23.380 58.619 1.00 57.36  ?  407 ILE   B HG13   1 
ATOM   12428 H  HG21   . ILE   B 1 382 ? 22.497  -23.389 58.128 1.00 57.55  ?  407 ILE   B HG21   1 
ATOM   12429 H  HG22   . ILE   B 1 382 ? 22.053  -23.922 59.557 1.00 57.55  ?  407 ILE   B HG22   1 
ATOM   12430 H  HG23   . ILE   B 1 382 ? 22.554  -22.424 59.388 1.00 57.55  ?  407 ILE   B HG23   1 
ATOM   12431 H  HD11   . ILE   B 1 382 ? 25.653  -23.467 56.399 1.00 56.98  ?  407 ILE   B HD11   1 
ATOM   12432 H  HD12   . ILE   B 1 382 ? 24.817  -24.690 56.973 1.00 56.98  ?  407 ILE   B HD12   1 
ATOM   12433 H  HD13   . ILE   B 1 382 ? 24.076  -23.349 56.551 1.00 56.98  ?  407 ILE   B HD13   1 
ATOM   12434 N  N      . VAL   B 1 383 ? 23.439  -25.082 62.177 1.00 51.39  ?  408 VAL   B N      1 
ATOM   12435 C  CA     . VAL   B 1 383 ? 22.471  -25.564 63.159 1.00 53.34  ?  408 VAL   B CA     1 
ATOM   12436 C  C      . VAL   B 1 383 ? 22.643  -24.826 64.480 1.00 55.84  ?  408 VAL   B C      1 
ATOM   12437 O  O      . VAL   B 1 383 ? 21.669  -24.378 65.095 1.00 55.26  ?  408 VAL   B O      1 
ATOM   12438 C  CB     . VAL   B 1 383 ? 22.609  -27.086 63.341 1.00 53.40  ?  408 VAL   B CB     1 
ATOM   12439 C  CG1    . VAL   B 1 383 ? 21.926  -27.544 64.624 1.00 53.83  ?  408 VAL   B CG1    1 
ATOM   12440 C  CG2    . VAL   B 1 383 ? 22.028  -27.810 62.137 1.00 52.90  ?  408 VAL   B CG2    1 
ATOM   12441 H  H      . VAL   B 1 383 ? 23.971  -25.687 61.874 1.00 61.67  ?  408 VAL   B H      1 
ATOM   12442 H  HA     . VAL   B 1 383 ? 21.578  -25.379 62.828 1.00 64.01  ?  408 VAL   B HA     1 
ATOM   12443 H  HB     . VAL   B 1 383 ? 23.550  -27.310 63.412 1.00 64.08  ?  408 VAL   B HB     1 
ATOM   12444 H  HG11   . VAL   B 1 383 ? 21.814  -28.507 64.596 1.00 64.59  ?  408 VAL   B HG11   1 
ATOM   12445 H  HG12   . VAL   B 1 383 ? 22.479  -27.297 65.381 1.00 64.59  ?  408 VAL   B HG12   1 
ATOM   12446 H  HG13   . VAL   B 1 383 ? 21.060  -27.112 64.692 1.00 64.59  ?  408 VAL   B HG13   1 
ATOM   12447 H  HG21   . VAL   B 1 383 ? 22.133  -28.766 62.263 1.00 63.47  ?  408 VAL   B HG21   1 
ATOM   12448 H  HG22   . VAL   B 1 383 ? 21.087  -27.588 62.059 1.00 63.47  ?  408 VAL   B HG22   1 
ATOM   12449 H  HG23   . VAL   B 1 383 ? 22.502  -27.527 61.340 1.00 63.47  ?  408 VAL   B HG23   1 
ATOM   12450 N  N      . GLU   B 1 384 ? 23.889  -24.692 64.936 1.00 58.31  ?  409 GLU   B N      1 
ATOM   12451 C  CA     . GLU   B 1 384 ? 24.144  -24.031 66.211 1.00 62.01  ?  409 GLU   B CA     1 
ATOM   12452 C  C      . GLU   B 1 384 ? 23.657  -22.588 66.189 1.00 64.05  ?  409 GLU   B C      1 
ATOM   12453 O  O      . GLU   B 1 384 ? 22.982  -22.133 67.120 1.00 64.93  ?  409 GLU   B O      1 
ATOM   12454 C  CB     . GLU   B 1 384 ? 25.636  -24.093 66.531 1.00 63.88  ?  409 GLU   B CB     1 
ATOM   12455 C  CG     . GLU   B 1 384 ? 25.963  -23.921 67.999 1.00 65.86  ?  409 GLU   B CG     1 
ATOM   12456 C  CD     . GLU   B 1 384 ? 27.441  -24.092 68.283 1.00 67.98  ?  409 GLU   B CD     1 
ATOM   12457 O  OE1    . GLU   B 1 384 ? 27.848  -25.197 68.706 1.00 69.15  ?  409 GLU   B OE1    1 
ATOM   12458 O  OE2    . GLU   B 1 384 ? 28.197  -23.120 68.069 1.00 68.82  ?  409 GLU   B OE2    1 
ATOM   12459 H  H      . GLU   B 1 384 ? 24.594  -24.971 64.530 1.00 69.96  ?  409 GLU   B H      1 
ATOM   12460 H  HA     . GLU   B 1 384 ? 23.662  -24.498 66.911 1.00 74.40  ?  409 GLU   B HA     1 
ATOM   12461 H  HB2    . GLU   B 1 384 ? 25.977  -24.958 66.253 1.00 76.65  ?  409 GLU   B HB2    1 
ATOM   12462 H  HB3    . GLU   B 1 384 ? 26.087  -23.386 66.044 1.00 76.65  ?  409 GLU   B HB3    1 
ATOM   12463 H  HG2    . GLU   B 1 384 ? 25.703  -23.029 68.280 1.00 79.03  ?  409 GLU   B HG2    1 
ATOM   12464 H  HG3    . GLU   B 1 384 ? 25.478  -24.585 68.513 1.00 79.03  ?  409 GLU   B HG3    1 
ATOM   12465 N  N      . SER   B 1 385 ? 23.988  -21.853 65.126 1.00 64.58  ?  410 SER   B N      1 
ATOM   12466 C  CA     . SER   B 1 385 ? 23.593  -20.452 65.037 1.00 65.03  ?  410 SER   B CA     1 
ATOM   12467 C  C      . SER   B 1 385 ? 22.078  -20.306 65.096 1.00 65.34  ?  410 SER   B C      1 
ATOM   12468 O  O      . SER   B 1 385 ? 21.545  -19.539 65.906 1.00 65.47  ?  410 SER   B O      1 
ATOM   12469 C  CB     . SER   B 1 385 ? 24.146  -19.841 63.750 1.00 66.02  ?  410 SER   B CB     1 
ATOM   12470 O  OG     . SER   B 1 385 ? 23.643  -18.532 63.558 1.00 67.56  ?  410 SER   B OG     1 
ATOM   12471 H  H      . SER   B 1 385 ? 24.437  -22.141 64.451 1.00 77.48  ?  410 SER   B H      1 
ATOM   12472 H  HA     . SER   B 1 385 ? 23.969  -19.968 65.789 1.00 78.03  ?  410 SER   B HA     1 
ATOM   12473 H  HB2    . SER   B 1 385 ? 25.113  -19.802 63.809 1.00 79.22  ?  410 SER   B HB2    1 
ATOM   12474 H  HB3    . SER   B 1 385 ? 23.881  -20.394 62.998 1.00 79.22  ?  410 SER   B HB3    1 
ATOM   12475 H  HG     . SER   B 1 385 ? 23.946  -18.209 62.844 1.00 81.06  ?  410 SER   B HG     1 
ATOM   12476 N  N      . ILE   B 1 386 ? 21.364  -21.050 64.249 1.00 64.82  ?  411 ILE   B N      1 
ATOM   12477 C  CA     . ILE   B 1 386 ? 19.908  -20.961 64.234 1.00 64.75  ?  411 ILE   B CA     1 
ATOM   12478 C  C      . ILE   B 1 386 ? 19.323  -21.420 65.563 1.00 65.42  ?  411 ILE   B C      1 
ATOM   12479 O  O      . ILE   B 1 386 ? 18.363  -20.828 66.072 1.00 65.52  ?  411 ILE   B O      1 
ATOM   12480 C  CB     . ILE   B 1 386 ? 19.336  -21.775 63.057 1.00 64.02  ?  411 ILE   B CB     1 
ATOM   12481 C  CG1    . ILE   B 1 386 ? 19.716  -21.105 61.738 1.00 63.22  ?  411 ILE   B CG1    1 
ATOM   12482 C  CG2    . ILE   B 1 386 ? 17.829  -21.923 63.204 1.00 64.46  ?  411 ILE   B CG2    1 
ATOM   12483 C  CD1    . ILE   B 1 386 ? 19.384  -21.927 60.533 1.00 62.93  ?  411 ILE   B CD1    1 
ATOM   12484 H  H      . ILE   B 1 386 ? 21.695  -21.605 63.682 1.00 77.78  ?  411 ILE   B H      1 
ATOM   12485 H  HA     . ILE   B 1 386 ? 19.662  -20.031 64.108 1.00 77.69  ?  411 ILE   B HA     1 
ATOM   12486 H  HB     . ILE   B 1 386 ? 19.718  -22.666 63.062 1.00 76.81  ?  411 ILE   B HB     1 
ATOM   12487 H  HG12   . ILE   B 1 386 ? 19.238  -20.265 61.665 1.00 75.86  ?  411 ILE   B HG12   1 
ATOM   12488 H  HG13   . ILE   B 1 386 ? 20.673  -20.944 61.734 1.00 75.86  ?  411 ILE   B HG13   1 
ATOM   12489 H  HG21   . ILE   B 1 386 ? 17.451  -22.175 62.347 1.00 77.34  ?  411 ILE   B HG21   1 
ATOM   12490 H  HG22   . ILE   B 1 386 ? 17.642  -22.609 63.864 1.00 77.34  ?  411 ILE   B HG22   1 
ATOM   12491 H  HG23   . ILE   B 1 386 ? 17.455  -21.076 63.493 1.00 77.34  ?  411 ILE   B HG23   1 
ATOM   12492 H  HD11   . ILE   B 1 386 ? 19.995  -21.697 59.816 1.00 75.50  ?  411 ILE   B HD11   1 
ATOM   12493 H  HD12   . ILE   B 1 386 ? 19.476  -22.867 60.757 1.00 75.50  ?  411 ILE   B HD12   1 
ATOM   12494 H  HD13   . ILE   B 1 386 ? 18.472  -21.739 60.264 1.00 75.50  ?  411 ILE   B HD13   1 
ATOM   12495 N  N      . LEU   B 1 387 ? 19.873  -22.492 66.137 1.00 65.62  ?  412 LEU   B N      1 
ATOM   12496 C  CA     . LEU   B 1 387 ? 19.351  -22.997 67.403 1.00 66.65  ?  412 LEU   B CA     1 
ATOM   12497 C  C      . LEU   B 1 387 ? 19.401  -21.921 68.479 1.00 68.27  ?  412 LEU   B C      1 
ATOM   12498 O  O      . LEU   B 1 387 ? 18.433  -21.720 69.221 1.00 68.57  ?  412 LEU   B O      1 
ATOM   12499 C  CB     . LEU   B 1 387 ? 20.138  -24.227 67.845 1.00 66.23  ?  412 LEU   B CB     1 
ATOM   12500 C  CG     . LEU   B 1 387 ? 19.413  -25.565 67.703 1.00 66.33  ?  412 LEU   B CG     1 
ATOM   12501 C  CD1    . LEU   B 1 387 ? 20.364  -26.693 68.080 1.00 66.47  ?  412 LEU   B CD1    1 
ATOM   12502 C  CD2    . LEU   B 1 387 ? 18.155  -25.614 68.554 1.00 66.48  ?  412 LEU   B CD2    1 
ATOM   12503 H  H      . LEU   B 1 387 ? 20.538  -22.936 65.819 1.00 78.73  ?  412 LEU   B H      1 
ATOM   12504 H  HA     . LEU   B 1 387 ? 18.426  -23.261 67.274 1.00 79.97  ?  412 LEU   B HA     1 
ATOM   12505 H  HB2    . LEU   B 1 387 ? 20.946  -24.278 67.311 1.00 79.47  ?  412 LEU   B HB2    1 
ATOM   12506 H  HB3    . LEU   B 1 387 ? 20.365  -24.120 68.782 1.00 79.47  ?  412 LEU   B HB3    1 
ATOM   12507 H  HG     . LEU   B 1 387 ? 19.132  -25.679 66.781 1.00 79.59  ?  412 LEU   B HG     1 
ATOM   12508 H  HD11   . LEU   B 1 387 ? 19.905  -27.541 67.976 1.00 79.76  ?  412 LEU   B HD11   1 
ATOM   12509 H  HD12   . LEU   B 1 387 ? 21.138  -26.662 67.496 1.00 79.76  ?  412 LEU   B HD12   1 
ATOM   12510 H  HD13   . LEU   B 1 387 ? 20.640  -26.578 69.003 1.00 79.76  ?  412 LEU   B HD13   1 
ATOM   12511 H  HD21   . LEU   B 1 387 ? 17.738  -26.484 68.451 1.00 79.77  ?  412 LEU   B HD21   1 
ATOM   12512 H  HD22   . LEU   B 1 387 ? 18.396  -25.470 69.482 1.00 79.77  ?  412 LEU   B HD22   1 
ATOM   12513 H  HD23   . LEU   B 1 387 ? 17.547  -24.919 68.258 1.00 79.77  ?  412 LEU   B HD23   1 
ATOM   12514 N  N      . ASN   B 1 388 ? 20.535  -21.222 68.585 1.00 69.35  ?  413 ASN   B N      1 
ATOM   12515 C  CA     . ASN   B 1 388 ? 20.646  -20.141 69.558 1.00 70.47  ?  413 ASN   B CA     1 
ATOM   12516 C  C      . ASN   B 1 388 ? 19.653  -19.026 69.261 1.00 71.77  ?  413 ASN   B C      1 
ATOM   12517 O  O      . ASN   B 1 388 ? 19.141  -18.384 70.186 1.00 71.96  ?  413 ASN   B O      1 
ATOM   12518 C  CB     . ASN   B 1 388 ? 22.078  -19.600 69.574 1.00 70.35  ?  413 ASN   B CB     1 
ATOM   12519 C  CG     . ASN   B 1 388 ? 23.080  -20.606 70.133 1.00 70.31  ?  413 ASN   B CG     1 
ATOM   12520 O  OD1    . ASN   B 1 388 ? 22.706  -21.550 70.829 1.00 70.16  ?  413 ASN   B OD1    1 
ATOM   12521 N  ND2    . ASN   B 1 388 ? 24.359  -20.401 69.834 1.00 70.31  ?  413 ASN   B ND2    1 
ATOM   12522 H  H      . ASN   B 1 388 ? 21.241  -21.353 68.112 1.00 83.21  ?  413 ASN   B H      1 
ATOM   12523 H  HA     . ASN   B 1 388 ? 20.450  -20.487 70.443 1.00 84.55  ?  413 ASN   B HA     1 
ATOM   12524 H  HB2    . ASN   B 1 388 ? 22.345  -19.383 68.667 1.00 84.41  ?  413 ASN   B HB2    1 
ATOM   12525 H  HB3    . ASN   B 1 388 ? 22.110  -18.805 70.128 1.00 84.41  ?  413 ASN   B HB3    1 
ATOM   12526 H  HD21   . ASN   B 1 388 ? 24.961  -20.941 70.126 1.00 84.37  ?  413 ASN   B HD21   1 
ATOM   12527 H  HD22   . ASN   B 1 388 ? 24.585  -19.728 69.348 1.00 84.37  ?  413 ASN   B HD22   1 
ATOM   12528 N  N      . TRP   B 1 389 ? 19.358  -18.794 67.981 1.00 72.52  ?  414 TRP   B N      1 
ATOM   12529 C  CA     . TRP   B 1 389 ? 18.428  -17.737 67.597 1.00 73.06  ?  414 TRP   B CA     1 
ATOM   12530 C  C      . TRP   B 1 389 ? 17.007  -18.050 68.049 1.00 73.41  ?  414 TRP   B C      1 
ATOM   12531 O  O      . TRP   B 1 389 ? 16.332  -17.190 68.628 1.00 73.67  ?  414 TRP   B O      1 
ATOM   12532 C  CB     . TRP   B 1 389 ? 18.501  -17.539 66.080 1.00 73.45  ?  414 TRP   B CB     1 
ATOM   12533 C  CG     . TRP   B 1 389 ? 17.419  -16.697 65.472 1.00 73.88  ?  414 TRP   B CG     1 
ATOM   12534 C  CD1    . TRP   B 1 389 ? 16.544  -17.073 64.492 1.00 73.84  ?  414 TRP   B CD1    1 
ATOM   12535 C  CD2    . TRP   B 1 389 ? 17.102  -15.336 65.791 1.00 74.24  ?  414 TRP   B CD2    1 
ATOM   12536 N  NE1    . TRP   B 1 389 ? 15.703  -16.032 64.182 1.00 73.87  ?  414 TRP   B NE1    1 
ATOM   12537 C  CE2    . TRP   B 1 389 ? 16.023  -14.955 64.966 1.00 74.12  ?  414 TRP   B CE2    1 
ATOM   12538 C  CE3    . TRP   B 1 389 ? 17.622  -14.404 66.695 1.00 74.58  ?  414 TRP   B CE3    1 
ATOM   12539 C  CZ2    . TRP   B 1 389 ? 15.455  -13.684 65.019 1.00 74.38  ?  414 TRP   B CZ2    1 
ATOM   12540 C  CZ3    . TRP   B 1 389 ? 17.054  -13.142 66.747 1.00 74.98  ?  414 TRP   B CZ3    1 
ATOM   12541 C  CH2    . TRP   B 1 389 ? 15.984  -12.794 65.912 1.00 74.77  ?  414 TRP   B CH2    1 
ATOM   12542 H  H      . TRP   B 1 389 ? 19.682  -19.235 67.318 1.00 87.02  ?  414 TRP   B H      1 
ATOM   12543 H  HA     . TRP   B 1 389 ? 18.685  -16.907 68.028 1.00 87.66  ?  414 TRP   B HA     1 
ATOM   12544 H  HB2    . TRP   B 1 389 ? 19.347  -17.113 65.870 1.00 88.13  ?  414 TRP   B HB2    1 
ATOM   12545 H  HB3    . TRP   B 1 389 ? 18.455  -18.411 65.659 1.00 88.13  ?  414 TRP   B HB3    1 
ATOM   12546 H  HD1    . TRP   B 1 389 ? 16.522  -17.912 64.092 1.00 88.60  ?  414 TRP   B HD1    1 
ATOM   12547 H  HE1    . TRP   B 1 389 ? 15.078  -16.053 63.592 1.00 88.64  ?  414 TRP   B HE1    1 
ATOM   12548 H  HE3    . TRP   B 1 389 ? 18.335  -14.627 67.249 1.00 89.49  ?  414 TRP   B HE3    1 
ATOM   12549 H  HZ2    . TRP   B 1 389 ? 14.742  -13.450 64.469 1.00 89.26  ?  414 TRP   B HZ2    1 
ATOM   12550 H  HZ3    . TRP   B 1 389 ? 17.389  -12.515 67.347 1.00 89.96  ?  414 TRP   B HZ3    1 
ATOM   12551 H  HH2    . TRP   B 1 389 ? 15.627  -11.937 65.966 1.00 89.72  ?  414 TRP   B HH2    1 
ATOM   12552 N  N      . VAL   B 1 390 ? 16.538  -19.280 67.815 1.00 73.52  ?  415 VAL   B N      1 
ATOM   12553 C  CA     . VAL   B 1 390 ? 15.138  -19.598 68.083 1.00 73.73  ?  415 VAL   B CA     1 
ATOM   12554 C  C      . VAL   B 1 390 ? 14.838  -19.509 69.577 1.00 74.04  ?  415 VAL   B C      1 
ATOM   12555 O  O      . VAL   B 1 390 ? 13.893  -18.829 69.996 1.00 74.05  ?  415 VAL   B O      1 
ATOM   12556 C  CB     . VAL   B 1 390 ? 14.767  -20.984 67.519 1.00 73.29  ?  415 VAL   B CB     1 
ATOM   12557 C  CG1    . VAL   B 1 390 ? 14.694  -20.936 65.996 1.00 73.32  ?  415 VAL   B CG1    1 
ATOM   12558 C  CG2    . VAL   B 1 390 ? 15.749  -22.061 67.975 1.00 72.85  ?  415 VAL   B CG2    1 
ATOM   12559 H  H      . VAL   B 1 390 ? 17.003  -19.935 67.507 1.00 88.22  ?  415 VAL   B H      1 
ATOM   12560 H  HA     . VAL   B 1 390 ? 14.593  -18.936 67.627 1.00 88.47  ?  415 VAL   B HA     1 
ATOM   12561 H  HB     . VAL   B 1 390 ? 13.894  -21.226 67.865 1.00 87.95  ?  415 VAL   B HB     1 
ATOM   12562 H  HG11   . VAL   B 1 390 ? 13.874  -21.367 65.705 1.00 87.98  ?  415 VAL   B HG11   1 
ATOM   12563 H  HG12   . VAL   B 1 390 ? 14.700  -20.010 65.708 1.00 87.98  ?  415 VAL   B HG12   1 
ATOM   12564 H  HG13   . VAL   B 1 390 ? 15.461  -21.402 65.628 1.00 87.98  ?  415 VAL   B HG13   1 
ATOM   12565 H  HG21   . VAL   B 1 390 ? 15.498  -22.907 67.573 1.00 87.41  ?  415 VAL   B HG21   1 
ATOM   12566 H  HG22   . VAL   B 1 390 ? 16.643  -21.813 67.694 1.00 87.41  ?  415 VAL   B HG22   1 
ATOM   12567 H  HG23   . VAL   B 1 390 ? 15.714  -22.131 68.942 1.00 87.41  ?  415 VAL   B HG23   1 
ATOM   12568 N  N      . LYS   B 1 391 ? 15.627  -20.199 70.404 1.00 73.99  ?  416 LYS   B N      1 
ATOM   12569 C  CA     . LYS   B 1 391 ? 15.396  -20.153 71.845 1.00 74.02  ?  416 LYS   B CA     1 
ATOM   12570 C  C      . LYS   B 1 391 ? 15.363  -18.716 72.348 1.00 75.00  ?  416 LYS   B C      1 
ATOM   12571 O  O      . LYS   B 1 391 ? 14.601  -18.392 73.266 1.00 74.84  ?  416 LYS   B O      1 
ATOM   12572 C  CB     . LYS   B 1 391 ? 16.472  -20.966 72.569 1.00 73.06  ?  416 LYS   B CB     1 
ATOM   12573 H  H      . LYS   B 1 391 ? 16.288  -20.691 70.160 1.00 88.78  ?  416 LYS   B H      1 
ATOM   12574 H  HA     . LYS   B 1 391 ? 14.539  -20.559 72.052 1.00 88.81  ?  416 LYS   B HA     1 
ATOM   12575 N  N      . PHE   B 1 392 ? 16.163  -17.843 71.747 1.00 76.03  ?  417 PHE   B N      1 
ATOM   12576 C  CA     . PHE   B 1 392 ? 16.161  -16.416 72.054 1.00 76.65  ?  417 PHE   B CA     1 
ATOM   12577 C  C      . PHE   B 1 392 ? 14.926  -15.750 71.455 1.00 77.60  ?  417 PHE   B C      1 
ATOM   12578 O  O      . PHE   B 1 392 ? 14.264  -14.942 72.108 1.00 78.21  ?  417 PHE   B O      1 
ATOM   12579 C  CB     . PHE   B 1 392 ? 17.446  -15.778 71.518 1.00 76.04  ?  417 PHE   B CB     1 
ATOM   12580 H  H      . PHE   B 1 392 ? 16.734  -18.057 71.141 1.00 91.23  ?  417 PHE   B H      1 
ATOM   12581 H  HA     . PHE   B 1 392 ? 16.135  -16.272 73.013 1.00 91.97  ?  417 PHE   B HA     1 
HETATM 12582 P  PG     . ANP   C 2 .   ? 4.578   -9.622  22.366 1.00 19.35  ?  501 ANP   A PG     1 
HETATM 12583 O  O1G    . ANP   C 2 .   ? 3.272   -10.007 22.976 1.00 20.12  ?  501 ANP   A O1G    1 
HETATM 12584 O  O2G    . ANP   C 2 .   ? 5.621   -9.065  23.403 1.00 19.81  ?  501 ANP   A O2G    1 
HETATM 12585 O  O3G    . ANP   C 2 .   ? 5.216   -10.806 21.562 1.00 21.21  ?  501 ANP   A O3G    1 
HETATM 12586 P  PB     . ANP   C 2 .   ? 2.906   -7.925  20.618 1.00 21.94  ?  501 ANP   A PB     1 
HETATM 12587 O  O1B    . ANP   C 2 .   ? 1.817   -7.818  21.628 1.00 20.21  ?  501 ANP   A O1B    1 
HETATM 12588 O  O2B    . ANP   C 2 .   ? 3.186   -6.614  19.804 1.00 22.90  ?  501 ANP   A O2B    1 
HETATM 12589 N  N3B    . ANP   C 2 .   ? 4.386   -8.331  21.295 1.00 19.42  ?  501 ANP   A N3B    1 
HETATM 12590 P  PA     . ANP   C 2 .   ? 1.330   -10.051 19.591 1.00 21.81  ?  501 ANP   A PA     1 
HETATM 12591 O  O1A    . ANP   C 2 .   ? 0.876   -10.393 20.964 1.00 20.65  ?  501 ANP   A O1A    1 
HETATM 12592 O  O2A    . ANP   C 2 .   ? 1.688   -11.249 18.709 1.00 22.35  ?  501 ANP   A O2A    1 
HETATM 12593 O  O3A    . ANP   C 2 .   ? 2.590   -9.071  19.607 1.00 22.04  ?  501 ANP   A O3A    1 
HETATM 12594 O  "O5'"  . ANP   C 2 .   ? 0.196   -9.163  18.904 1.00 23.21  ?  501 ANP   A "O5'"  1 
HETATM 12595 C  "C5'"  . ANP   C 2 .   ? 0.411   -8.729  17.551 1.00 25.38  ?  501 ANP   A "C5'"  1 
HETATM 12596 C  "C4'"  . ANP   C 2 .   ? -0.214  -7.383  17.332 1.00 26.53  ?  501 ANP   A "C4'"  1 
HETATM 12597 O  "O4'"  . ANP   C 2 .   ? -1.644  -7.532  17.264 1.00 25.65  ?  501 ANP   A "O4'"  1 
HETATM 12598 C  "C3'"  . ANP   C 2 .   ? 0.030   -6.376  18.444 1.00 26.01  ?  501 ANP   A "C3'"  1 
HETATM 12599 O  "O3'"  . ANP   C 2 .   ? 1.246   -5.667  18.224 1.00 27.65  ?  501 ANP   A "O3'"  1 
HETATM 12600 C  "C2'"  . ANP   C 2 .   ? -1.186  -5.458  18.341 1.00 26.61  ?  501 ANP   A "C2'"  1 
HETATM 12601 O  "O2'"  . ANP   C 2 .   ? -0.976  -4.432  17.372 1.00 28.48  ?  501 ANP   A "O2'"  1 
HETATM 12602 C  "C1'"  . ANP   C 2 .   ? -2.281  -6.391  17.805 1.00 26.46  ?  501 ANP   A "C1'"  1 
HETATM 12603 N  N9     . ANP   C 2 .   ? -3.267  -6.851  18.776 1.00 26.53  ?  501 ANP   A N9     1 
HETATM 12604 C  C8     . ANP   C 2 .   ? -3.266  -8.023  19.486 1.00 26.64  ?  501 ANP   A C8     1 
HETATM 12605 N  N7     . ANP   C 2 .   ? -4.308  -8.176  20.268 1.00 25.30  ?  501 ANP   A N7     1 
HETATM 12606 C  C5     . ANP   C 2 .   ? -5.056  -7.030  20.041 1.00 26.21  ?  501 ANP   A C5     1 
HETATM 12607 C  C6     . ANP   C 2 .   ? -6.289  -6.588  20.559 1.00 27.83  ?  501 ANP   A C6     1 
HETATM 12608 N  N6     . ANP   C 2 .   ? -7.002  -7.267  21.457 1.00 27.21  ?  501 ANP   A N6     1 
HETATM 12609 N  N1     . ANP   C 2 .   ? -6.758  -5.399  20.122 1.00 29.31  ?  501 ANP   A N1     1 
HETATM 12610 C  C2     . ANP   C 2 .   ? -6.045  -4.716  19.222 1.00 28.62  ?  501 ANP   A C2     1 
HETATM 12611 N  N3     . ANP   C 2 .   ? -4.875  -5.032  18.664 1.00 28.42  ?  501 ANP   A N3     1 
HETATM 12612 C  C4     . ANP   C 2 .   ? -4.430  -6.208  19.123 1.00 26.60  ?  501 ANP   A C4     1 
HETATM 12613 H  HNB1   . ANP   C 2 .   ? 4.902   -8.554  20.583 1.00 23.30  ?  501 ANP   A HNB1   1 
HETATM 12614 H  "H5'1" . ANP   C 2 .   ? 1.368   -8.672  17.382 1.00 30.45  ?  501 ANP   A "H5'1" 1 
HETATM 12615 H  "H5'2" . ANP   C 2 .   ? 0.012   -9.374  16.941 1.00 30.45  ?  501 ANP   A "H5'2" 1 
HETATM 12616 H  "H4'"  . ANP   C 2 .   ? 0.078   -6.995  16.482 1.00 31.83  ?  501 ANP   A "H4'"  1 
HETATM 12617 H  "H3'"  . ANP   C 2 .   ? 0.027   -6.831  19.290 1.00 31.20  ?  501 ANP   A "H3'"  1 
HETATM 12618 H  "H2'"  . ANP   C 2 .   ? -1.425  -5.138  19.220 1.00 31.93  ?  501 ANP   A "H2'"  1 
HETATM 12619 H  "HO2'" . ANP   C 2 .   ? -1.023  -3.647  17.772 1.00 34.17  ?  501 ANP   A "HO2'" 1 
HETATM 12620 H  "H1'"  . ANP   C 2 .   ? -2.725  -5.892  17.102 1.00 31.74  ?  501 ANP   A "H1'"  1 
HETATM 12621 H  H8     . ANP   C 2 .   ? -2.568  -8.673  19.416 1.00 31.96  ?  501 ANP   A H8     1 
HETATM 12622 H  HN61   . ANP   C 2 .   ? -7.803  -6.923  21.764 1.00 32.64  ?  501 ANP   A HN61   1 
HETATM 12623 H  HN62   . ANP   C 2 .   ? -6.696  -8.069  21.771 1.00 32.64  ?  501 ANP   A HN62   1 
HETATM 12624 H  H2     . ANP   C 2 .   ? -6.432  -3.873  18.935 1.00 34.34  ?  501 ANP   A H2     1 
HETATM 12625 MG MG     . MG    D 3 .   ? 1.265   -9.423  22.817 1.00 20.32  ?  502 MG    A MG     1 
HETATM 12626 C  C1     . A1ASC E 4 .   ? 8.899   -17.575 49.431 1.00 30.04  ?  503 A1ASC A C1     1 
HETATM 12627 C  C2     . A1ASC E 4 .   ? 7.323   -17.275 45.944 1.00 23.67  ?  503 A1ASC A C2     1 
HETATM 12628 C  C3     . A1ASC E 4 .   ? 5.034   -16.552 45.330 1.00 22.51  ?  503 A1ASC A C3     1 
HETATM 12629 C  C5     . A1ASC E 4 .   ? 3.087   -16.149 41.142 1.00 15.40  ?  503 A1ASC A C5     1 
HETATM 12630 C  C8     . A1ASC E 4 .   ? 2.750   -13.251 41.487 1.00 14.31  ?  503 A1ASC A C8     1 
HETATM 12631 C  C11    . A1ASC E 4 .   ? 5.079   -17.526 39.769 1.00 15.35  ?  503 A1ASC A C11    1 
HETATM 12632 C  C12    . A1ASC E 4 .   ? 3.086   -16.212 39.710 1.00 16.22  ?  503 A1ASC A C12    1 
HETATM 12633 C  C13    . A1ASC E 4 .   ? 4.098   -16.767 41.869 1.00 15.70  ?  503 A1ASC A C13    1 
HETATM 12634 C  C14    . A1ASC E 4 .   ? 4.071   -16.901 39.019 1.00 16.48  ?  503 A1ASC A C14    1 
HETATM 12635 C  C15    . A1ASC E 4 .   ? 2.415   -12.217 40.596 1.00 14.93  ?  503 A1ASC A C15    1 
HETATM 12636 C  C16    . A1ASC E 4 .   ? 1.941   -15.605 37.707 1.00 17.15  ?  503 A1ASC A C16    1 
HETATM 12637 C  C17    . A1ASC E 4 .   ? 4.021   -13.310 42.034 1.00 14.24  ?  503 A1ASC A C17    1 
HETATM 12638 C  C20    . A1ASC E 4 .   ? 5.040   -17.319 44.028 1.00 21.19  ?  503 A1ASC A C20    1 
HETATM 12639 N  N      . A1ASC E 4 .   ? 5.897   -17.147 46.382 1.00 22.52  ?  503 A1ASC A N      1 
HETATM 12640 C  C      . A1ASC E 4 .   ? 1.869   -15.564 41.832 1.00 16.57  ?  503 A1ASC A C      1 
HETATM 12641 O  O      . A1ASC E 4 .   ? 4.049   -16.665 43.218 1.00 18.64  ?  503 A1ASC A O      1 
HETATM 12642 C  C10    . A1ASC E 4 .   ? 2.929   -16.335 36.970 1.00 20.37  ?  503 A1ASC A C10    1 
HETATM 12643 C  C18    . A1ASC E 4 .   ? 3.364   -11.235 40.243 1.00 15.40  ?  503 A1ASC A C18    1 
HETATM 12644 C  C19    . A1ASC E 4 .   ? 4.947   -17.732 36.793 1.00 20.48  ?  503 A1ASC A C19    1 
HETATM 12645 C  C1A    . A1ASC E 4 .   ? 6.649   -16.810 48.732 1.00 24.23  ?  503 A1ASC A C1A    1 
HETATM 12646 C  C1B    . A1ASC E 4 .   ? 0.348   -13.674 42.165 1.00 15.93  ?  503 A1ASC A C1B    1 
HETATM 12647 C  C1C    . A1ASC E 4 .   ? 5.831   -16.277 47.637 1.00 23.31  ?  503 A1ASC A C1C    1 
HETATM 12648 C  C1E    . A1ASC E 4 .   ? 4.552   -19.240 36.749 1.00 21.80  ?  503 A1ASC A C1E    1 
HETATM 12649 C  C1F    . A1ASC E 4 .   ? 4.659   -11.322 40.771 1.00 15.64  ?  503 A1ASC A C1F    1 
HETATM 12650 C  C1G    . A1ASC E 4 .   ? 1.002   -12.183 40.120 1.00 15.41  ?  503 A1ASC A C1G    1 
HETATM 12651 C  C1H    . A1ASC E 4 .   ? 5.465   -20.031 35.827 1.00 23.36  ?  503 A1ASC A C1H    1 
HETATM 12652 C  C1I    . A1ASC E 4 .   ? 0.106   -12.325 41.400 1.00 15.88  ?  503 A1ASC A C1I    1 
HETATM 12653 C  C1J    . A1ASC E 4 .   ? 8.097   -17.891 47.073 1.00 25.30  ?  503 A1ASC A C1J    1 
HETATM 12654 C  C1K    . A1ASC E 4 .   ? 4.992   -12.336 41.690 1.00 14.67  ?  503 A1ASC A C1K    1 
HETATM 12655 C  C7     . A1ASC E 4 .   ? 5.107   -17.464 41.169 1.00 15.76  ?  503 A1ASC A C7     1 
HETATM 12656 C  C9     . A1ASC E 4 .   ? 3.955   -16.943 37.564 1.00 17.29  ?  503 A1ASC A C9     1 
HETATM 12657 N  N4     . A1ASC E 4 .   ? 1.714   -14.180 41.830 1.00 15.84  ?  503 A1ASC A N4     1 
HETATM 12658 N  N6     . A1ASC E 4 .   ? 8.068   -16.965 48.281 1.00 27.50  ?  503 A1ASC A N6     1 
HETATM 12659 O  O1     . A1ASC E 4 .   ? 2.014   -15.559 39.087 1.00 16.59  ?  503 A1ASC A O1     1 
HETATM 12660 O  O2     . A1ASC E 4 .   ? 1.038   -16.316 42.325 1.00 17.62  ?  503 A1ASC A O2     1 
HETATM 12661 O  O3     . A1ASC E 4 .   ? 0.974   -15.059 37.197 1.00 18.09  ?  503 A1ASC A O3     1 
HETATM 12662 H  H1C    . A1ASC E 4 .   ? 9.979   -17.414 49.265 1.00 36.05  ?  503 A1ASC A H1C    1 
HETATM 12663 H  H1A    . A1ASC E 4 .   ? 8.725   -18.663 49.509 1.00 36.05  ?  503 A1ASC A H1A    1 
HETATM 12664 H  H1B    . A1ASC E 4 .   ? 8.630   -17.117 50.398 1.00 36.05  ?  503 A1ASC A H1B    1 
HETATM 12665 H  H2B    . A1ASC E 4 .   ? 7.636   -16.243 45.676 1.00 28.40  ?  503 A1ASC A H2B    1 
HETATM 12666 H  H2A    . A1ASC E 4 .   ? 7.286   -17.891 45.019 1.00 28.40  ?  503 A1ASC A H2A    1 
HETATM 12667 H  H3A    . A1ASC E 4 .   ? 4.042   -16.505 45.835 1.00 27.01  ?  503 A1ASC A H3A    1 
HETATM 12668 H  H3B    . A1ASC E 4 .   ? 5.429   -15.513 45.257 1.00 27.01  ?  503 A1ASC A H3B    1 
HETATM 12669 H  H11    . A1ASC E 4 .   ? 5.898   -18.101 39.221 1.00 18.42  ?  503 A1ASC A H11    1 
HETATM 12670 H  H17    . A1ASC E 4 .   ? 4.337   -14.113 42.760 1.00 17.09  ?  503 A1ASC A H17    1 
HETATM 12671 H  H20B   . A1ASC E 4 .   ? 6.070   -17.310 43.579 1.00 25.43  ?  503 A1ASC A H20B   1 
HETATM 12672 H  H20A   . A1ASC E 4 .   ? 4.824   -18.406 44.218 1.00 25.43  ?  503 A1ASC A H20A   1 
HETATM 12673 H  H10    . A1ASC E 4 .   ? 2.828   -16.389 35.866 1.00 24.44  ?  503 A1ASC A H10    1 
HETATM 12674 H  H18    . A1ASC E 4 .   ? 3.159   -10.357 39.547 1.00 18.48  ?  503 A1ASC A H18    1 
HETATM 12675 H  H19A   . A1ASC E 4 .   ? 5.075   -17.344 35.740 1.00 24.58  ?  503 A1ASC A H19A   1 
HETATM 12676 H  H19B   . A1ASC E 4 .   ? 5.992   -17.626 37.207 1.00 24.58  ?  503 A1ASC A H19B   1 
HETATM 12677 H  H1AA   . A1ASC E 4 .   ? 6.337   -17.825 49.076 1.00 29.08  ?  503 A1ASC A H1AA   1 
HETATM 12678 H  H1AB   . A1ASC E 4 .   ? 6.695   -16.145 49.627 1.00 29.08  ?  503 A1ASC A H1AB   1 
HETATM 12679 H  H1BB   . A1ASC E 4 .   ? -0.471  -14.415 41.910 1.00 19.11  ?  503 A1ASC A H1BB   1 
HETATM 12680 H  H1BA   . A1ASC E 4 .   ? 0.196   -13.521 43.277 1.00 19.11  ?  503 A1ASC A H1BA   1 
HETATM 12681 H  H1CA   . A1ASC E 4 .   ? 4.750   -16.231 47.889 1.00 27.97  ?  503 A1ASC A H1CA   1 
HETATM 12682 H  H1CB   . A1ASC E 4 .   ? 6.165   -15.273 47.299 1.00 27.97  ?  503 A1ASC A H1CB   1 
HETATM 12683 H  H1EB   . A1ASC E 4 .   ? 4.582   -19.667 37.780 1.00 26.16  ?  503 A1ASC A H1EB   1 
HETATM 12684 H  H1EA   . A1ASC E 4 .   ? 3.490   -19.342 36.421 1.00 26.16  ?  503 A1ASC A H1EA   1 
HETATM 12685 H  H1F    . A1ASC E 4 .   ? 5.415   -10.545 40.426 1.00 18.76  ?  503 A1ASC A H1F    1 
HETATM 12686 H  H1GA   . A1ASC E 4 .   ? 0.794   -12.996 39.369 1.00 18.49  ?  503 A1ASC A H1GA   1 
HETATM 12687 H  H1GB   . A1ASC E 4 .   ? 0.775   -11.239 39.550 1.00 18.49  ?  503 A1ASC A H1GB   1 
HETATM 12688 H  H1HA   . A1ASC E 4 .   ? 6.534   -19.795 35.982 1.00 28.03  ?  503 A1ASC A H1HA   1 
HETATM 12689 H  H1HC   . A1ASC E 4 .   ? 5.259   -19.839 34.758 1.00 28.03  ?  503 A1ASC A H1HC   1 
HETATM 12690 H  H1HB   . A1ASC E 4 .   ? 5.368   -21.123 35.967 1.00 28.03  ?  503 A1ASC A H1HB   1 
HETATM 12691 H  H1IB   . A1ASC E 4 .   ? -0.997  -12.217 41.120 1.00 19.06  ?  503 A1ASC A H1IB   1 
HETATM 12692 H  H1IA   . A1ASC E 4 .   ? 0.275   -11.435 42.097 1.00 19.06  ?  503 A1ASC A H1IA   1 
HETATM 12693 H  H1JB   . A1ASC E 4 .   ? 9.167   -18.045 46.832 1.00 30.37  ?  503 A1ASC A H1JB   1 
HETATM 12694 H  H1JA   . A1ASC E 4 .   ? 7.673   -18.854 47.416 1.00 30.37  ?  503 A1ASC A H1JA   1 
HETATM 12695 H  H1K    . A1ASC E 4 .   ? 6.020   -12.408 42.173 1.00 17.61  ?  503 A1ASC A H1K    1 
HETATM 12696 H  H7     . A1ASC E 4 .   ? 5.926   -17.963 41.770 1.00 18.91  ?  503 A1ASC A H7     1 
HETATM 12697 H  H      . A1ASC E 4 .   ? 5.567   -18.141 46.622 1.00 27.03  ?  503 A1ASC A H      1 
HETATM 12698 H  H6     . A1ASC E 4 .   ? 8.506   -16.017 48.037 1.00 33.00  ?  503 A1ASC A H6     1 
HETATM 12699 CL CL     . CL    F 5 .   ? 11.921  -12.858 31.611 1.00 21.06  ?  504 CL    A CL     1 
HETATM 12700 P  PG     . ANP   G 2 .   ? 22.912  -23.227 21.433 1.00 19.86  ?  501 ANP   B PG     1 
HETATM 12701 O  O1G    . ANP   G 2 .   ? 24.331  -22.796 21.671 1.00 19.21  ?  501 ANP   B O1G    1 
HETATM 12702 O  O2G    . ANP   G 2 .   ? 22.109  -23.623 22.723 1.00 19.40  ?  501 ANP   B O2G    1 
HETATM 12703 O  O3G    . ANP   G 2 .   ? 22.103  -22.160 20.606 1.00 20.28  ?  501 ANP   B O3G    1 
HETATM 12704 P  PB     . ANP   G 2 .   ? 24.175  -25.234 19.659 1.00 21.64  ?  501 ANP   B PB     1 
HETATM 12705 O  O1B    . ANP   G 2 .   ? 25.480  -25.227 20.369 1.00 21.08  ?  501 ANP   B O1B    1 
HETATM 12706 O  O2B    . ANP   G 2 .   ? 23.807  -26.643 19.110 1.00 22.41  ?  501 ANP   B O2B    1 
HETATM 12707 N  N3B    . ANP   G 2 .   ? 22.871  -24.680 20.544 1.00 21.00  ?  501 ANP   B N3B    1 
HETATM 12708 P  PA     . ANP   G 2 .   ? 25.481  -23.315 18.035 1.00 22.43  ?  501 ANP   B PA     1 
HETATM 12709 O  O1A    . ANP   G 2 .   ? 26.181  -22.774 19.230 1.00 22.16  ?  501 ANP   B O1A    1 
HETATM 12710 O  O2A    . ANP   G 2 .   ? 24.924  -22.281 17.052 1.00 22.35  ?  501 ANP   B O2A    1 
HETATM 12711 O  O3A    . ANP   G 2 .   ? 24.238  -24.272 18.430 1.00 22.25  ?  501 ANP   B O3A    1 
HETATM 12712 O  "O5'"  . ANP   G 2 .   ? 26.453  -24.282 17.267 1.00 23.04  ?  501 ANP   B "O5'"  1 
HETATM 12713 C  "C5'"  . ANP   G 2 .   ? 25.940  -24.956 16.095 1.00 24.07  ?  501 ANP   B "C5'"  1 
HETATM 12714 C  "C4'"  . ANP   G 2 .   ? 26.552  -26.320 15.947 1.00 25.37  ?  501 ANP   B "C4'"  1 
HETATM 12715 O  "O4'"  . ANP   G 2 .   ? 27.935  -26.201 15.551 1.00 26.92  ?  501 ANP   B "O4'"  1 
HETATM 12716 C  "C3'"  . ANP   G 2 .   ? 26.575  -27.147 17.221 1.00 25.69  ?  501 ANP   B "C3'"  1 
HETATM 12717 O  "O3'"  . ANP   G 2 .   ? 25.369  -27.883 17.396 1.00 27.02  ?  501 ANP   B "O3'"  1 
HETATM 12718 C  "C2'"  . ANP   G 2 .   ? 27.763  -28.080 17.000 1.00 27.51  ?  501 ANP   B "C2'"  1 
HETATM 12719 O  "O2'"  . ANP   G 2 .   ? 27.383  -29.249 16.280 1.00 28.90  ?  501 ANP   B "O2'"  1 
HETATM 12720 C  "C1'"  . ANP   G 2 .   ? 28.688  -27.272 16.091 1.00 27.41  ?  501 ANP   B "C1'"  1 
HETATM 12721 N  N9     . ANP   G 2 .   ? 29.873  -26.710 16.737 1.00 28.20  ?  501 ANP   B N9     1 
HETATM 12722 C  C8     . ANP   G 2 .   ? 30.004  -25.454 17.262 1.00 28.87  ?  501 ANP   B C8     1 
HETATM 12723 N  N7     . ANP   G 2 .   ? 31.200  -25.193 17.743 1.00 28.65  ?  501 ANP   B N7     1 
HETATM 12724 C  C5     . ANP   G 2 .   ? 31.893  -26.374 17.533 1.00 28.59  ?  501 ANP   B C5     1 
HETATM 12725 C  C6     . ANP   G 2 .   ? 33.220  -26.758 17.830 1.00 29.73  ?  501 ANP   B C6     1 
HETATM 12726 N  N6     . ANP   G 2 .   ? 34.104  -25.966 18.442 1.00 29.71  ?  501 ANP   B N6     1 
HETATM 12727 N  N1     . ANP   G 2 .   ? 33.604  -28.004 17.480 1.00 30.21  ?  501 ANP   B N1     1 
HETATM 12728 C  C2     . ANP   G 2 .   ? 32.718  -28.806 16.884 1.00 30.63  ?  501 ANP   B C2     1 
HETATM 12729 N  N3     . ANP   G 2 .   ? 31.446  -28.559 16.561 1.00 29.89  ?  501 ANP   B N3     1 
HETATM 12730 C  C4     . ANP   G 2 .   ? 31.096  -27.320 16.914 1.00 28.14  ?  501 ANP   B C4     1 
HETATM 12731 H  HNB1   . ANP   G 2 .   ? 22.223  -24.542 19.923 1.00 25.19  ?  501 ANP   B HNB1   1 
HETATM 12732 H  "H5'1" . ANP   G 2 .   ? 24.975  -25.047 16.180 1.00 28.88  ?  501 ANP   B "H5'1" 1 
HETATM 12733 H  "H5'2" . ANP   G 2 .   ? 26.149  -24.425 15.308 1.00 28.88  ?  501 ANP   B "H5'2" 1 
HETATM 12734 H  "H4'"  . ANP   G 2 .   ? 26.102  -26.825 15.239 1.00 30.44  ?  501 ANP   B "H4'"  1 
HETATM 12735 H  "H3'"  . ANP   G 2 .   ? 26.739  -26.556 17.959 1.00 30.82  ?  501 ANP   B "H3'"  1 
HETATM 12736 H  "H2'"  . ANP   G 2 .   ? 28.190  -28.246 17.849 1.00 33.01  ?  501 ANP   B "H2'"  1 
HETATM 12737 H  "HO2'" . ANP   G 2 .   ? 27.561  -29.957 16.776 1.00 34.68  ?  501 ANP   B "HO2'" 1 
HETATM 12738 H  "H1'"  . ANP   G 2 .   ? 28.953  -27.874 15.379 1.00 32.88  ?  501 ANP   B "H1'"  1 
HETATM 12739 H  H8     . ANP   G 2 .   ? 29.288  -24.820 17.277 1.00 34.63  ?  501 ANP   B H8     1 
HETATM 12740 H  HN61   . ANP   G 2 .   ? 34.956  -26.279 18.619 1.00 35.65  ?  501 ANP   B HN61   1 
HETATM 12741 H  HN62   . ANP   G 2 .   ? 33.867  -25.120 18.695 1.00 35.65  ?  501 ANP   B HN62   1 
HETATM 12742 H  H2     . ANP   G 2 .   ? 33.043  -29.691 16.653 1.00 36.75  ?  501 ANP   B H2     1 
HETATM 12743 MG MG     . MG    H 3 .   ? 26.214  -23.417 21.210 1.00 21.34  ?  502 MG    B MG     1 
HETATM 12744 C  C1     . GOL   I 6 .   ? 45.550  -13.816 33.938 1.00 42.97  ?  503 GOL   B C1     1 
HETATM 12745 O  O1     . GOL   I 6 .   ? 45.782  -12.483 33.492 1.00 41.13  ?  503 GOL   B O1     1 
HETATM 12746 C  C2     . GOL   I 6 .   ? 45.476  -14.757 32.742 1.00 42.93  ?  503 GOL   B C2     1 
HETATM 12747 O  O2     . GOL   I 6 .   ? 46.530  -14.482 31.816 1.00 42.38  ?  503 GOL   B O2     1 
HETATM 12748 C  C3     . GOL   I 6 .   ? 45.539  -16.208 33.207 1.00 44.76  ?  503 GOL   B C3     1 
HETATM 12749 O  O3     . GOL   I 6 .   ? 46.152  -16.321 34.495 1.00 43.83  ?  503 GOL   B O3     1 
HETATM 12750 H  H11    . GOL   I 6 .   ? 44.614  -13.859 34.499 1.00 51.55  ?  503 GOL   B H11    1 
HETATM 12751 H  H12    . GOL   I 6 .   ? 46.359  -14.128 34.602 1.00 51.55  ?  503 GOL   B H12    1 
HETATM 12752 H  H2     . GOL   I 6 .   ? 44.508  -14.600 32.245 1.00 51.51  ?  503 GOL   B H2     1 
HETATM 12753 H  HO2    . GOL   I 6 .   ? 47.383  -14.634 32.244 1.00 50.85  ?  503 GOL   B HO2    1 
HETATM 12754 H  H31    . GOL   I 6 .   ? 44.528  -16.619 33.250 1.00 53.70  ?  503 GOL   B H31    1 
HETATM 12755 H  H32    . GOL   I 6 .   ? 46.107  -16.795 32.483 1.00 53.70  ?  503 GOL   B H32    1 
HETATM 12756 H  HO3    . GOL   I 6 .   ? 46.179  -17.251 34.759 1.00 52.59  ?  503 GOL   B HO3    1 
HETATM 12757 C  C1     . A1ASC J 4 .   ? 24.528  -11.376 47.322 1.00 32.41  ?  504 A1ASC B C1     1 
HETATM 12758 C  C2     . A1ASC J 4 .   ? 25.308  -12.183 43.619 1.00 25.45  ?  504 A1ASC B C2     1 
HETATM 12759 C  C3     . A1ASC J 4 .   ? 27.403  -13.127 42.612 1.00 22.07  ?  504 A1ASC B C3     1 
HETATM 12760 C  C5     . A1ASC J 4 .   ? 28.299  -14.103 38.189 1.00 18.49  ?  504 A1ASC B C5     1 
HETATM 12761 C  C8     . A1ASC J 4 .   ? 28.759  -16.883 38.902 1.00 18.07  ?  504 A1ASC B C8     1 
HETATM 12762 C  C11    . A1ASC J 4 .   ? 25.991  -12.835 37.155 1.00 18.35  ?  504 A1ASC B C11    1 
HETATM 12763 C  C12    . A1ASC J 4 .   ? 27.972  -14.202 36.807 1.00 17.89  ?  504 A1ASC B C12    1 
HETATM 12764 C  C13    . A1ASC J 4 .   ? 27.493  -13.373 39.030 1.00 17.59  ?  504 A1ASC B C13    1 
HETATM 12765 C  C14    . A1ASC J 4 .   ? 26.843  -13.563 36.250 1.00 18.97  ?  504 A1ASC B C14    1 
HETATM 12766 C  C15    . A1ASC J 4 .   ? 28.917  -18.036 38.168 1.00 17.54  ?  504 A1ASC B C15    1 
HETATM 12767 C  C16    . A1ASC J 4 .   ? 28.687  -15.063 34.737 1.00 20.34  ?  504 A1ASC B C16    1 
HETATM 12768 C  C17    . A1ASC J 4 .   ? 27.599  -16.728 39.719 1.00 18.54  ?  504 A1ASC B C17    1 
HETATM 12769 C  C20    . A1ASC J 4 .   ? 27.134  -12.527 41.217 1.00 22.05  ?  504 A1ASC B C20    1 
HETATM 12770 N  N      . A1ASC J 4 .   ? 26.805  -12.345 43.716 1.00 23.41  ?  504 A1ASC B N      1 
HETATM 12771 C  C      . A1ASC J 4 .   ? 29.628  -14.585 38.668 1.00 18.96  ?  504 A1ASC B C      1 
HETATM 12772 O  O      . A1ASC J 4 .   ? 27.852  -13.325 40.310 1.00 20.92  ?  504 A1ASC B O      1 
HETATM 12773 C  C10    . A1ASC J 4 .   ? 27.547  -14.416 34.153 1.00 21.91  ?  504 A1ASC B C10    1 
HETATM 12774 C  C18    . A1ASC J 4 .   ? 27.951  -19.078 38.190 1.00 18.05  ?  504 A1ASC B C18    1 
HETATM 12775 C  C19    . A1ASC J 4 .   ? 25.474  -13.019 34.163 1.00 24.46  ?  504 A1ASC B C19    1 
HETATM 12776 C  C1A    . A1ASC J 4 .   ? 26.596  -12.279 46.228 1.00 26.75  ?  504 A1ASC B C1A    1 
HETATM 12777 C  C1B    . A1ASC J 4 .   ? 31.239  -16.436 38.987 1.00 19.37  ?  504 A1ASC B C1B    1 
HETATM 12778 C  C1C    . A1ASC J 4 .   ? 27.079  -13.062 45.060 1.00 25.33  ?  504 A1ASC B C1C    1 
HETATM 12779 C  C1E    . A1ASC J 4 .   ? 25.929  -11.566 33.823 1.00 23.41  ?  504 A1ASC B C1E    1 
HETATM 12780 C  C1F    . A1ASC J 4 .   ? 26.813  -18.918 38.956 1.00 17.55  ?  504 A1ASC B C1F    1 
HETATM 12781 C  C1G    . A1ASC J 4 .   ? 30.238  -18.159 37.408 1.00 18.39  ?  504 A1ASC B C1G    1 
HETATM 12782 C  C1H    . A1ASC J 4 .   ? 24.823  -10.852 33.030 1.00 25.96  ?  504 A1ASC B C1H    1 
HETATM 12783 C  C1I    . A1ASC J 4 .   ? 31.370  -17.864 38.398 1.00 19.70  ?  504 A1ASC B C1I    1 
HETATM 12784 C  C1J    . A1ASC J 4 .   ? 24.736  -11.417 44.802 1.00 27.74  ?  504 A1ASC B C1J    1 
HETATM 12785 C  C1K    . A1ASC J 4 .   ? 26.642  -17.751 39.744 1.00 18.36  ?  504 A1ASC B C1K    1 
HETATM 12786 C  C7     . A1ASC J 4 .   ? 26.325  -12.724 38.521 1.00 17.21  ?  504 A1ASC B C7     1 
HETATM 12787 C  C9     . A1ASC J 4 .   ? 26.654  -13.715 34.828 1.00 20.26  ?  504 A1ASC B C9     1 
HETATM 12788 N  N4     . A1ASC J 4 .   ? 29.818  -15.938 38.852 1.00 18.24  ?  504 A1ASC B N4     1 
HETATM 12789 N  N6     . A1ASC J 4 .   ? 25.059  -12.152 46.126 1.00 29.20  ?  504 A1ASC B N6     1 
HETATM 12790 O  O1     . A1ASC J 4 .   ? 28.897  -14.940 36.108 1.00 19.70  ?  504 A1ASC B O1     1 
HETATM 12791 O  O2     . A1ASC J 4 .   ? 30.543  -13.775 38.856 1.00 20.20  ?  504 A1ASC B O2     1 
HETATM 12792 O  O3     . A1ASC J 4 .   ? 29.498  -15.714 34.109 1.00 21.01  ?  504 A1ASC B O3     1 
HETATM 12793 H  H1C    . A1ASC J 4 .   ? 23.496  -11.029 47.139 1.00 38.89  ?  504 A1ASC B H1C    1 
HETATM 12794 H  H1A    . A1ASC J 4 .   ? 25.154  -10.490 47.527 1.00 38.89  ?  504 A1ASC B H1A    1 
HETATM 12795 H  H1B    . A1ASC J 4 .   ? 24.521  -12.005 48.229 1.00 38.89  ?  504 A1ASC B H1B    1 
HETATM 12796 H  H2B    . A1ASC J 4 .   ? 24.940  -13.229 43.537 1.00 30.54  ?  504 A1ASC B H2B    1 
HETATM 12797 H  H2A    . A1ASC J 4 .   ? 25.166  -11.675 42.640 1.00 30.54  ?  504 A1ASC B H2A    1 
HETATM 12798 H  H3A    . A1ASC J 4 .   ? 28.478  -13.167 42.900 1.00 26.48  ?  504 A1ASC B H3A    1 
HETATM 12799 H  H3B    . A1ASC J 4 .   ? 26.969  -14.140 42.772 1.00 26.48  ?  504 A1ASC B H3B    1 
HETATM 12800 H  H11    . A1ASC J 4 .   ? 25.040  -12.346 36.761 1.00 22.02  ?  504 A1ASC B H11    1 
HETATM 12801 H  H17    . A1ASC J 4 .   ? 27.407  -15.816 40.355 1.00 22.24  ?  504 A1ASC B H17    1 
HETATM 12802 H  H20B   . A1ASC J 4 .   ? 26.028  -12.508 41.018 1.00 26.46  ?  504 A1ASC B H20B   1 
HETATM 12803 H  H20A   . A1ASC J 4 .   ? 27.442  -11.446 41.203 1.00 26.46  ?  504 A1ASC B H20A   1 
HETATM 12804 H  H10    . A1ASC J 4 .   ? 27.415  -14.519 33.056 1.00 26.29  ?  504 A1ASC B H10    1 
HETATM 12805 H  H18    . A1ASC J 4 .   ? 28.040  -20.056 37.614 1.00 21.66  ?  504 A1ASC B H18    1 
HETATM 12806 H  H19A   . A1ASC J 4 .   ? 25.109  -13.551 33.237 1.00 29.35  ?  504 A1ASC B H19A   1 
HETATM 12807 H  H19B   . A1ASC J 4 .   ? 24.546  -13.008 34.806 1.00 29.35  ?  504 A1ASC B H19B   1 
HETATM 12808 H  H1AA   . A1ASC J 4 .   ? 26.986  -11.235 46.272 1.00 32.10  ?  504 A1ASC B H1AA   1 
HETATM 12809 H  H1AB   . A1ASC J 4 .   ? 26.797  -12.760 47.215 1.00 32.10  ?  504 A1ASC B H1AB   1 
HETATM 12810 H  H1BB   . A1ASC J 4 .   ? 31.989  -15.750 38.485 1.00 23.24  ?  504 A1ASC B H1BB   1 
HETATM 12811 H  H1BA   . A1ASC J 4 .   ? 31.598  -16.436 40.062 1.00 23.24  ?  504 A1ASC B H1BA   1 
HETATM 12812 H  H1CA   . A1ASC J 4 .   ? 28.179  -13.221 45.073 1.00 30.40  ?  504 A1ASC B H1CA   1 
HETATM 12813 H  H1CB   . A1ASC J 4 .   ? 26.574  -14.046 44.961 1.00 30.40  ?  504 A1ASC B H1CB   1 
HETATM 12814 H  H1EB   . A1ASC J 4 .   ? 26.169  -11.006 34.758 1.00 28.09  ?  504 A1ASC B H1EB   1 
HETATM 12815 H  H1EA   . A1ASC J 4 .   ? 26.882  -11.584 33.242 1.00 28.09  ?  504 A1ASC B H1EA   1 
HETATM 12816 H  H1F    . A1ASC J 4 .   ? 26.038  -19.750 38.925 1.00 21.06  ?  504 A1ASC B H1F    1 
HETATM 12817 H  H1GA   . A1ASC J 4 .   ? 30.271  -17.463 36.523 1.00 22.06  ?  504 A1ASC B H1GA   1 
HETATM 12818 H  H1GB   . A1ASC J 4 .   ? 30.352  -19.178 36.942 1.00 22.06  ?  504 A1ASC B H1GB   1 
HETATM 12819 H  H1HA   . A1ASC J 4 .   ? 24.054  -11.550 32.650 1.00 31.16  ?  504 A1ASC B H1HA   1 
HETATM 12820 H  H1HC   . A1ASC J 4 .   ? 25.213  -10.313 32.146 1.00 31.16  ?  504 A1ASC B H1HC   1 
HETATM 12821 H  H1HB   . A1ASC J 4 .   ? 24.284  -10.100 33.635 1.00 31.16  ?  504 A1ASC B H1HB   1 
HETATM 12822 H  H1IB   . A1ASC J 4 .   ? 32.387  -18.007 37.898 1.00 23.63  ?  504 A1ASC B H1IB   1 
HETATM 12823 H  H1IA   . A1ASC J 4 .   ? 31.388  -18.648 39.230 1.00 23.63  ?  504 A1ASC B H1IA   1 
HETATM 12824 H  H1JB   . A1ASC J 4 .   ? 23.633  -11.328 44.767 1.00 33.29  ?  504 A1ASC B H1JB   1 
HETATM 12825 H  H1JA   . A1ASC J 4 .   ? 25.165  -10.402 44.908 1.00 33.29  ?  504 A1ASC B H1JA   1 
HETATM 12826 H  H1K    . A1ASC J 4 .   ? 25.734  -17.606 40.414 1.00 22.03  ?  504 A1ASC B H1K    1 
HETATM 12827 H  H7     . A1ASC J 4 .   ? 25.688  -12.127 39.242 1.00 20.65  ?  504 A1ASC B H7     1 
HETATM 12828 H  H      . A1ASC J 4 .   ? 27.230  -11.358 43.697 1.00 28.09  ?  504 A1ASC B H      1 
HETATM 12829 H  H6     . A1ASC J 4 .   ? 24.574  -13.108 46.157 1.00 35.04  ?  504 A1ASC B H6     1 
HETATM 12830 CL CL     . CL    K 5 .   ? 17.738  -18.646 31.430 1.00 22.92  ?  505 CL    B CL     1 
HETATM 12831 O  O      . HOH   L 7 .   ? 26.246  -35.192 3.597  1.00 42.64  ?  601 HOH   A O      1 
HETATM 12832 O  O      . HOH   L 7 .   ? -8.734  -0.932  38.488 1.00 50.38  ?  602 HOH   A O      1 
HETATM 12833 O  O      . HOH   L 7 .   ? 10.714  -17.073 15.178 1.00 42.61  ?  603 HOH   A O      1 
HETATM 12834 O  O      . HOH   L 7 .   ? -4.060  -9.576  67.098 1.00 42.38  ?  604 HOH   A O      1 
HETATM 12835 O  O      . HOH   L 7 .   ? -2.769  1.137   54.216 1.00 63.51  ?  605 HOH   A O      1 
HETATM 12836 O  O      . HOH   L 7 .   ? 22.686  2.760   35.038 1.00 56.41  ?  606 HOH   A O      1 
HETATM 12837 O  O      . HOH   L 7 .   ? -5.290  -29.992 15.673 1.00 51.34  ?  607 HOH   A O      1 
HETATM 12838 O  O      . HOH   L 7 .   ? -17.601 -3.100  21.184 1.00 40.65  ?  608 HOH   A O      1 
HETATM 12839 O  O      . HOH   L 7 .   ? -22.212 -1.470  17.951 1.00 42.99  ?  609 HOH   A O      1 
HETATM 12840 O  O      . HOH   L 7 .   ? 8.271   -33.785 32.889 1.00 50.81  ?  610 HOH   A O      1 
HETATM 12841 O  O      . HOH   L 7 .   ? 24.726  -39.006 16.946 1.00 58.24  ?  611 HOH   A O      1 
HETATM 12842 O  O      . HOH   L 7 .   ? 6.703   3.576   13.327 1.00 49.69  ?  612 HOH   A O      1 
HETATM 12843 O  O      . HOH   L 7 .   ? -22.596 -2.769  12.039 1.00 50.05  ?  613 HOH   A O      1 
HETATM 12844 O  O      . HOH   L 7 .   ? 19.594  -37.620 15.359 1.00 53.27  ?  614 HOH   A O      1 
HETATM 12845 O  O      . HOH   L 7 .   ? 20.428  -0.235  38.215 1.00 37.84  ?  615 HOH   A O      1 
HETATM 12846 O  O      . HOH   L 7 .   ? -18.703 0.743   28.688 1.00 57.79  ?  616 HOH   A O      1 
HETATM 12847 O  O      . HOH   L 7 .   ? 18.045  5.959   28.722 1.00 57.35  ?  617 HOH   A O      1 
HETATM 12848 O  O      . HOH   L 7 .   ? 9.381   -10.644 59.468 1.00 52.26  ?  618 HOH   A O      1 
HETATM 12849 O  O      . HOH   L 7 .   ? -3.225  -29.332 43.405 1.00 40.71  ?  619 HOH   A O      1 
HETATM 12850 O  O      . HOH   L 7 .   ? 13.252  -22.555 23.392 1.00 27.26  ?  620 HOH   A O      1 
HETATM 12851 O  O      . HOH   L 7 .   ? -5.542  2.068   44.544 1.00 36.30  ?  621 HOH   A O      1 
HETATM 12852 O  O      . HOH   L 7 .   ? -1.739  1.451   40.179 1.00 23.40  ?  622 HOH   A O      1 
HETATM 12853 O  O      . HOH   L 7 .   ? 10.201  -0.652  60.272 1.00 53.38  ?  623 HOH   A O      1 
HETATM 12854 O  O      . HOH   L 7 .   ? -1.102  -3.707  29.131 1.00 24.82  ?  624 HOH   A O      1 
HETATM 12855 O  O      . HOH   L 7 .   ? 0.755   -11.147 23.854 1.00 17.88  ?  625 HOH   A O      1 
HETATM 12856 O  O      . HOH   L 7 .   ? 14.783  8.278   40.926 1.00 50.95  ?  626 HOH   A O      1 
HETATM 12857 O  O      . HOH   L 7 .   ? -9.952  -34.630 27.443 1.00 42.48  ?  627 HOH   A O      1 
HETATM 12858 O  O      . HOH   L 7 .   ? -12.959 4.010   20.086 1.00 48.54  ?  628 HOH   A O      1 
HETATM 12859 O  O      . HOH   L 7 .   ? -15.521 0.026   21.129 1.00 39.38  ?  629 HOH   A O      1 
HETATM 12860 O  O      . HOH   L 7 .   ? 23.222  -1.945  36.692 1.00 39.52  ?  630 HOH   A O      1 
HETATM 12861 O  O      . HOH   L 7 .   ? 10.380  9.303   27.492 1.00 29.67  ?  631 HOH   A O      1 
HETATM 12862 O  O      A HOH   L 7 .   ? 5.381   -16.211 26.421 0.53 38.48  ?  632 HOH   A O      1 
HETATM 12863 O  O      B HOH   L 7 .   ? 4.598   -16.597 25.379 0.47 41.55  ?  632 HOH   A O      1 
HETATM 12864 O  O      . HOH   L 7 .   ? 21.361  7.112   68.001 1.00 52.32  ?  633 HOH   A O      1 
HETATM 12865 O  O      . HOH   L 7 .   ? -1.711  -12.827 0.923  1.00 53.74  ?  634 HOH   A O      1 
HETATM 12866 O  O      . HOH   L 7 .   ? 20.709  -35.045 15.309 1.00 51.56  ?  635 HOH   A O      1 
HETATM 12867 O  O      . HOH   L 7 .   ? -3.083  -27.598 47.219 1.00 44.21  ?  636 HOH   A O      1 
HETATM 12868 O  O      . HOH   L 7 .   ? -0.343  4.978   27.012 1.00 31.77  ?  637 HOH   A O      1 
HETATM 12869 O  O      . HOH   L 7 .   ? -10.097 0.299   13.578 1.00 46.35  ?  638 HOH   A O      1 
HETATM 12870 O  O      . HOH   L 7 .   ? 12.796  -15.820 25.036 1.00 24.42  ?  639 HOH   A O      1 
HETATM 12871 O  O      . HOH   L 7 .   ? 6.216   10.645  46.614 1.00 43.43  ?  640 HOH   A O      1 
HETATM 12872 O  O      . HOH   L 7 .   ? 5.622   -13.250 45.349 1.00 28.01  ?  641 HOH   A O      1 
HETATM 12873 O  O      . HOH   L 7 .   ? 12.021  -15.170 49.756 1.00 54.88  ?  642 HOH   A O      1 
HETATM 12874 O  O      . HOH   L 7 .   ? -10.161 -28.163 18.260 1.00 53.03  ?  643 HOH   A O      1 
HETATM 12875 O  O      . HOH   L 7 .   ? 13.324  -26.522 24.954 1.00 35.68  ?  644 HOH   A O      1 
HETATM 12876 O  O      . HOH   L 7 .   ? -10.604 -7.324  50.507 1.00 43.35  ?  645 HOH   A O      1 
HETATM 12877 O  O      . HOH   L 7 .   ? 7.725   -19.499 32.820 1.00 23.64  ?  646 HOH   A O      1 
HETATM 12878 O  O      . HOH   L 7 .   ? -0.198  -5.822  22.285 1.00 23.28  ?  647 HOH   A O      1 
HETATM 12879 O  O      . HOH   L 7 .   ? 5.275   7.524   27.299 1.00 34.22  ?  648 HOH   A O      1 
HETATM 12880 O  O      . HOH   L 7 .   ? 18.061  -12.948 27.926 1.00 24.50  ?  649 HOH   A O      1 
HETATM 12881 O  O      . HOH   L 7 .   ? 29.867  -34.769 13.742 1.00 52.51  ?  650 HOH   A O      1 
HETATM 12882 O  O      . HOH   L 7 .   ? -2.638  6.097   25.838 1.00 42.92  ?  651 HOH   A O      1 
HETATM 12883 O  O      . HOH   L 7 .   ? -18.338 -1.912  4.283  1.00 56.15  ?  652 HOH   A O      1 
HETATM 12884 O  O      . HOH   L 7 .   ? 10.882  9.813   20.718 1.00 53.20  ?  653 HOH   A O      1 
HETATM 12885 O  O      . HOH   L 7 .   ? -11.045 -23.711 42.776 1.00 36.77  ?  654 HOH   A O      1 
HETATM 12886 O  O      . HOH   L 7 .   ? 4.757   4.807   13.727 1.00 60.03  ?  655 HOH   A O      1 
HETATM 12887 O  O      . HOH   L 7 .   ? -1.673  -15.171 8.225  1.00 49.83  ?  656 HOH   A O      1 
HETATM 12888 O  O      . HOH   L 7 .   ? 9.658   -28.017 29.293 1.00 23.99  ?  657 HOH   A O      1 
HETATM 12889 O  O      . HOH   L 7 .   ? 13.690  6.634   36.496 1.00 45.06  ?  658 HOH   A O      1 
HETATM 12890 O  O      . HOH   L 7 .   ? -5.007  -0.061  38.877 1.00 32.49  ?  659 HOH   A O      1 
HETATM 12891 O  O      . HOH   L 7 .   ? -12.353 -19.429 9.239  1.00 40.53  ?  660 HOH   A O      1 
HETATM 12892 O  O      . HOH   L 7 .   ? -9.350  -4.296  19.846 1.00 34.92  ?  661 HOH   A O      1 
HETATM 12893 O  O      . HOH   L 7 .   ? 6.288   0.906   18.177 1.00 33.53  ?  662 HOH   A O      1 
HETATM 12894 O  O      . HOH   L 7 .   ? -15.854 1.678   25.552 1.00 54.66  ?  663 HOH   A O      1 
HETATM 12895 O  O      . HOH   L 7 .   ? 14.094  -6.463  44.540 1.00 28.98  ?  664 HOH   A O      1 
HETATM 12896 O  O      . HOH   L 7 .   ? -4.650  -21.685 51.032 1.00 45.01  ?  665 HOH   A O      1 
HETATM 12897 O  O      . HOH   L 7 .   ? -0.732  4.788   39.661 1.00 27.20  ?  666 HOH   A O      1 
HETATM 12898 O  O      . HOH   L 7 .   ? -19.609 -10.931 40.297 1.00 48.18  ?  667 HOH   A O      1 
HETATM 12899 O  O      . HOH   L 7 .   ? -10.666 -28.500 28.915 1.00 32.72  ?  668 HOH   A O      1 
HETATM 12900 O  O      . HOH   L 7 .   ? -11.223 -2.574  3.944  1.00 52.54  ?  669 HOH   A O      1 
HETATM 12901 O  O      . HOH   L 7 .   ? -8.489  -29.597 13.121 1.00 55.84  ?  670 HOH   A O      1 
HETATM 12902 O  O      . HOH   L 7 .   ? -11.568 -21.000 17.951 1.00 37.86  ?  671 HOH   A O      1 
HETATM 12903 O  O      . HOH   L 7 .   ? 1.190   -2.383  35.375 1.00 18.04  ?  672 HOH   A O      1 
HETATM 12904 O  O      . HOH   L 7 .   ? 7.389   5.165   32.845 1.00 18.45  ?  673 HOH   A O      1 
HETATM 12905 O  O      . HOH   L 7 .   ? 6.515   -20.999 44.276 1.00 44.64  ?  674 HOH   A O      1 
HETATM 12906 O  O      . HOH   L 7 .   ? -22.923 -11.871 39.118 1.00 46.70  ?  675 HOH   A O      1 
HETATM 12907 O  O      . HOH   L 7 .   ? -18.038 -14.362 26.512 1.00 44.98  ?  676 HOH   A O      1 
HETATM 12908 O  O      . HOH   L 7 .   ? -11.305 -20.905 40.498 1.00 33.59  ?  677 HOH   A O      1 
HETATM 12909 O  O      . HOH   L 7 .   ? -1.033  -0.875  34.498 1.00 33.93  ?  678 HOH   A O      1 
HETATM 12910 O  O      . HOH   L 7 .   ? 0.979   2.367   16.873 1.00 55.87  ?  679 HOH   A O      1 
HETATM 12911 O  O      . HOH   L 7 .   ? 4.817   -14.371 35.618 1.00 27.97  ?  680 HOH   A O      1 
HETATM 12912 O  O      . HOH   L 7 .   ? 16.945  -7.184  38.904 1.00 33.01  ?  681 HOH   A O      1 
HETATM 12913 O  O      . HOH   L 7 .   ? 8.272   9.922   29.820 1.00 41.75  ?  682 HOH   A O      1 
HETATM 12914 O  O      . HOH   L 7 .   ? 5.371   -28.906 21.173 1.00 28.04  ?  683 HOH   A O      1 
HETATM 12915 O  O      . HOH   L 7 .   ? 7.429   -25.352 9.092  1.00 45.27  ?  684 HOH   A O      1 
HETATM 12916 O  O      . HOH   L 7 .   ? -6.183  -32.688 37.019 1.00 44.80  ?  685 HOH   A O      1 
HETATM 12917 O  O      . HOH   L 7 .   ? -10.217 -17.328 3.111  1.00 53.47  ?  686 HOH   A O      1 
HETATM 12918 O  O      . HOH   L 7 .   ? 20.999  -2.769  30.971 1.00 30.25  ?  687 HOH   A O      1 
HETATM 12919 O  O      . HOH   L 7 .   ? -9.444  -1.215  35.795 1.00 30.30  ?  688 HOH   A O      1 
HETATM 12920 O  O      . HOH   L 7 .   ? 1.660   -0.724  19.865 1.00 34.46  ?  689 HOH   A O      1 
HETATM 12921 O  O      . HOH   L 7 .   ? 5.011   -29.945 23.730 1.00 37.65  ?  690 HOH   A O      1 
HETATM 12922 O  O      . HOH   L 7 .   ? 15.479  -9.538  39.209 1.00 39.67  ?  691 HOH   A O      1 
HETATM 12923 O  O      . HOH   L 7 .   ? 3.248   -31.555 31.011 1.00 34.07  ?  692 HOH   A O      1 
HETATM 12924 O  O      . HOH   L 7 .   ? 18.440  -10.062 29.578 1.00 32.93  ?  693 HOH   A O      1 
HETATM 12925 O  O      . HOH   L 7 .   ? 5.106   -12.801 32.951 1.00 16.44  ?  694 HOH   A O      1 
HETATM 12926 O  O      . HOH   L 7 .   ? 30.073  -30.835 15.629 1.00 40.04  ?  695 HOH   A O      1 
HETATM 12927 O  O      . HOH   L 7 .   ? -0.136  3.083   36.595 1.00 31.93  ?  696 HOH   A O      1 
HETATM 12928 O  O      . HOH   L 7 .   ? 11.573  -19.562 15.835 1.00 46.10  ?  697 HOH   A O      1 
HETATM 12929 O  O      . HOH   L 7 .   ? 3.521   1.616   15.851 1.00 38.78  ?  698 HOH   A O      1 
HETATM 12930 O  O      . HOH   L 7 .   ? -5.677  -14.111 51.110 1.00 50.52  ?  699 HOH   A O      1 
HETATM 12931 O  O      . HOH   L 7 .   ? 2.548   -10.248 26.572 1.00 26.81  ?  700 HOH   A O      1 
HETATM 12932 O  O      . HOH   L 7 .   ? -17.675 -25.626 31.430 1.00 46.66  ?  701 HOH   A O      1 
HETATM 12933 O  O      . HOH   L 7 .   ? 8.991   -23.153 38.686 1.00 41.51  ?  702 HOH   A O      1 
HETATM 12934 O  O      . HOH   L 7 .   ? 10.724  -13.076 56.575 1.00 33.74  ?  703 HOH   A O      1 
HETATM 12935 O  O      . HOH   L 7 .   ? -3.168  -27.444 36.066 1.00 24.46  ?  704 HOH   A O      1 
HETATM 12936 O  O      . HOH   L 7 .   ? -9.935  5.994   30.709 1.00 48.41  ?  705 HOH   A O      1 
HETATM 12937 O  O      . HOH   L 7 .   ? 3.785   2.291   60.468 1.00 53.86  ?  706 HOH   A O      1 
HETATM 12938 O  O      . HOH   L 7 .   ? -10.605 -5.721  48.483 1.00 40.30  ?  707 HOH   A O      1 
HETATM 12939 O  O      . HOH   L 7 .   ? -1.542  -1.395  18.034 1.00 41.95  ?  708 HOH   A O      1 
HETATM 12940 O  O      . HOH   L 7 .   ? -16.437 8.404   21.076 1.00 48.13  ?  709 HOH   A O      1 
HETATM 12941 O  O      . HOH   L 7 .   ? -19.291 -7.618  41.126 1.00 48.58  ?  710 HOH   A O      1 
HETATM 12942 O  O      . HOH   L 7 .   ? -14.201 -18.508 11.578 1.00 41.78  ?  711 HOH   A O      1 
HETATM 12943 O  O      . HOH   L 7 .   ? 11.059  -30.814 14.196 1.00 44.60  ?  712 HOH   A O      1 
HETATM 12944 O  O      . HOH   L 7 .   ? 9.546   -14.760 47.511 1.00 29.53  ?  713 HOH   A O      1 
HETATM 12945 O  O      . HOH   L 7 .   ? -13.386 -15.229 18.540 1.00 39.73  ?  714 HOH   A O      1 
HETATM 12946 O  O      . HOH   L 7 .   ? -14.250 -11.620 44.745 1.00 49.68  ?  715 HOH   A O      1 
HETATM 12947 O  O      . HOH   L 7 .   ? 21.576  2.479   29.038 1.00 32.54  ?  716 HOH   A O      1 
HETATM 12948 O  O      . HOH   L 7 .   ? 3.757   -13.334 47.608 1.00 26.94  ?  717 HOH   A O      1 
HETATM 12949 O  O      . HOH   L 7 .   ? -9.401  -11.884 50.384 1.00 39.76  ?  718 HOH   A O      1 
HETATM 12950 O  O      . HOH   L 7 .   ? 2.237   -12.288 33.186 1.00 17.46  ?  719 HOH   A O      1 
HETATM 12951 O  O      . HOH   L 7 .   ? 13.002  -8.211  23.542 1.00 36.35  ?  720 HOH   A O      1 
HETATM 12952 O  O      . HOH   L 7 .   ? -16.306 2.214   16.930 1.00 49.37  ?  721 HOH   A O      1 
HETATM 12953 O  O      . HOH   L 7 .   ? -0.564  -29.771 43.713 1.00 41.27  ?  722 HOH   A O      1 
HETATM 12954 O  O      . HOH   L 7 .   ? -2.893  -5.454  21.802 1.00 25.34  ?  723 HOH   A O      1 
HETATM 12955 O  O      . HOH   L 7 .   ? -8.196  -33.431 33.695 1.00 34.29  ?  724 HOH   A O      1 
HETATM 12956 O  O      . HOH   L 7 .   ? 18.912  -10.550 33.872 1.00 27.63  ?  725 HOH   A O      1 
HETATM 12957 O  O      . HOH   L 7 .   ? 8.754   -28.516 34.326 1.00 30.15  ?  726 HOH   A O      1 
HETATM 12958 O  O      . HOH   L 7 .   ? 12.114  5.892   27.679 1.00 37.15  ?  727 HOH   A O      1 
HETATM 12959 O  O      . HOH   L 7 .   ? 10.424  -10.059 26.113 1.00 19.26  ?  728 HOH   A O      1 
HETATM 12960 O  O      . HOH   L 7 .   ? -9.295  -9.587  23.138 1.00 29.30  ?  729 HOH   A O      1 
HETATM 12961 O  O      . HOH   L 7 .   ? -2.140  -7.743  35.471 1.00 18.83  ?  730 HOH   A O      1 
HETATM 12962 O  O      . HOH   L 7 .   ? -11.936 -27.219 36.037 1.00 38.87  ?  731 HOH   A O      1 
HETATM 12963 O  O      . HOH   L 7 .   ? -12.216 1.949   13.913 1.00 47.11  ?  732 HOH   A O      1 
HETATM 12964 O  O      . HOH   L 7 .   ? -7.311  5.608   32.336 1.00 45.96  ?  733 HOH   A O      1 
HETATM 12965 O  O      . HOH   L 7 .   ? 4.735   -13.002 27.980 1.00 22.53  ?  734 HOH   A O      1 
HETATM 12966 O  O      . HOH   L 7 .   ? 1.963   -26.485 12.726 1.00 45.73  ?  735 HOH   A O      1 
HETATM 12967 O  O      A HOH   L 7 .   ? 23.084  1.708   31.101 0.68 35.72  ?  736 HOH   A O      1 
HETATM 12968 O  O      . HOH   L 7 .   ? 14.094  -0.442  25.503 1.00 30.18  ?  737 HOH   A O      1 
HETATM 12969 O  O      . HOH   L 7 .   ? -1.261  -36.602 31.959 1.00 51.13  ?  738 HOH   A O      1 
HETATM 12970 O  O      . HOH   L 7 .   ? 2.352   -6.984  62.428 1.00 48.14  ?  739 HOH   A O      1 
HETATM 12971 O  O      . HOH   L 7 .   ? 20.023  -4.611  32.317 1.00 31.07  ?  740 HOH   A O      1 
HETATM 12972 O  O      . HOH   L 7 .   ? -10.752 -23.667 40.050 1.00 31.50  ?  741 HOH   A O      1 
HETATM 12973 O  O      . HOH   L 7 .   ? 18.581  -3.201  39.680 1.00 36.73  ?  742 HOH   A O      1 
HETATM 12974 O  O      . HOH   L 7 .   ? -0.992  -18.383 9.050  1.00 46.11  ?  743 HOH   A O      1 
HETATM 12975 O  O      . HOH   L 7 .   ? 6.094   -0.876  25.533 1.00 23.54  ?  744 HOH   A O      1 
HETATM 12976 O  O      . HOH   L 7 .   ? -17.476 -15.921 37.487 1.00 48.31  ?  745 HOH   A O      1 
HETATM 12977 O  O      . HOH   L 7 .   ? 13.757  7.730   31.845 1.00 35.53  ?  746 HOH   A O      1 
HETATM 12978 O  O      . HOH   L 7 .   ? -5.366  -11.672 3.901  1.00 47.41  ?  747 HOH   A O      1 
HETATM 12979 O  O      . HOH   L 7 .   ? 7.081   -32.620 35.550 1.00 35.32  ?  748 HOH   A O      1 
HETATM 12980 O  O      . HOH   L 7 .   ? -9.222  -3.797  1.959  1.00 54.45  ?  749 HOH   A O      1 
HETATM 12981 O  O      . HOH   L 7 .   ? 1.477   -8.312  24.638 1.00 19.36  ?  750 HOH   A O      1 
HETATM 12982 O  O      . HOH   L 7 .   ? 4.089   8.762   58.135 1.00 49.08  ?  751 HOH   A O      1 
HETATM 12983 O  O      . HOH   L 7 .   ? -5.612  4.558   28.667 1.00 38.21  ?  752 HOH   A O      1 
HETATM 12984 O  O      . HOH   L 7 .   ? -9.211  -27.916 14.789 1.00 54.38  ?  753 HOH   A O      1 
HETATM 12985 O  O      . HOH   L 7 .   ? 16.411  3.117   44.343 1.00 32.90  ?  754 HOH   A O      1 
HETATM 12986 O  O      . HOH   L 7 .   ? -1.683  -1.555  32.126 1.00 29.42  ?  755 HOH   A O      1 
HETATM 12987 O  O      . HOH   L 7 .   ? -21.515 -17.915 34.499 1.00 44.87  ?  756 HOH   A O      1 
HETATM 12988 O  O      . HOH   L 7 .   ? -4.002  -23.132 15.402 1.00 26.63  ?  757 HOH   A O      1 
HETATM 12989 O  O      . HOH   L 7 .   ? -1.521  5.327   30.609 1.00 48.56  ?  758 HOH   A O      1 
HETATM 12990 O  O      . HOH   L 7 .   ? 8.729   -25.575 41.203 1.00 30.09  ?  759 HOH   A O      1 
HETATM 12991 O  O      . HOH   L 7 .   ? 3.324   -16.141 50.501 1.00 41.22  ?  760 HOH   A O      1 
HETATM 12992 O  O      . HOH   L 7 .   ? 4.581   -31.534 27.208 1.00 27.27  ?  761 HOH   A O      1 
HETATM 12993 O  O      . HOH   L 7 .   ? 10.105  -18.419 31.780 1.00 31.72  ?  762 HOH   A O      1 
HETATM 12994 O  O      . HOH   L 7 .   ? 4.765   -15.950 33.421 1.00 24.81  ?  763 HOH   A O      1 
HETATM 12995 O  O      . HOH   L 7 .   ? -6.709  -29.005 43.018 1.00 57.09  ?  764 HOH   A O      1 
HETATM 12996 O  O      . HOH   L 7 .   ? 12.605  2.999   27.615 1.00 27.58  ?  765 HOH   A O      1 
HETATM 12997 O  O      . HOH   L 7 .   ? -17.034 -12.732 31.024 1.00 34.94  ?  766 HOH   A O      1 
HETATM 12998 O  O      . HOH   L 7 .   ? 10.778  -29.034 26.143 1.00 36.53  ?  767 HOH   A O      1 
HETATM 12999 O  O      . HOH   L 7 .   ? -0.730  2.764   56.818 1.00 57.76  ?  768 HOH   A O      1 
HETATM 13000 O  O      . HOH   L 7 .   ? 5.539   -19.492 31.423 1.00 21.37  ?  769 HOH   A O      1 
HETATM 13001 O  O      . HOH   L 7 .   ? -16.444 -17.119 21.308 1.00 49.93  ?  770 HOH   A O      1 
HETATM 13002 O  O      . HOH   L 7 .   ? 19.060  1.531   29.510 1.00 37.92  ?  771 HOH   A O      1 
HETATM 13003 O  O      . HOH   L 7 .   ? -14.821 0.980   32.501 1.00 42.99  ?  772 HOH   A O      1 
HETATM 13004 O  O      . HOH   L 7 .   ? 15.989  6.579   43.951 1.00 65.62  ?  773 HOH   A O      1 
HETATM 13005 O  O      . HOH   L 7 .   ? 8.849   -29.390 15.594 1.00 29.16  ?  774 HOH   A O      1 
HETATM 13006 O  O      . HOH   L 7 .   ? 9.009   10.473  41.759 1.00 41.05  ?  775 HOH   A O      1 
HETATM 13007 O  O      . HOH   L 7 .   ? -0.253  -1.244  29.951 1.00 26.81  ?  776 HOH   A O      1 
HETATM 13008 O  O      . HOH   L 7 .   ? -3.483  -30.055 38.794 1.00 32.12  ?  777 HOH   A O      1 
HETATM 13009 O  O      . HOH   L 7 .   ? -5.503  -32.489 32.796 1.00 26.66  ?  778 HOH   A O      1 
HETATM 13010 O  O      . HOH   L 7 .   ? 14.335  -14.333 34.271 1.00 49.13  ?  779 HOH   A O      1 
HETATM 13011 O  O      . HOH   L 7 .   ? 18.137  -9.605  36.320 1.00 42.40  ?  780 HOH   A O      1 
HETATM 13012 O  O      . HOH   L 7 .   ? 7.354   -14.868 42.738 1.00 26.56  ?  781 HOH   A O      1 
HETATM 13013 O  O      . HOH   L 7 .   ? -1.846  -26.743 33.717 1.00 22.02  ?  782 HOH   A O      1 
HETATM 13014 O  O      . HOH   L 7 .   ? 0.872   -33.417 20.175 1.00 54.31  ?  783 HOH   A O      1 
HETATM 13015 O  O      . HOH   L 7 .   ? 1.888   7.240   51.904 1.00 53.07  ?  784 HOH   A O      1 
HETATM 13016 O  O      . HOH   L 7 .   ? 10.940  -12.924 22.189 1.00 41.18  ?  785 HOH   A O      1 
HETATM 13017 O  O      . HOH   L 7 .   ? -0.327  4.017   54.102 1.00 46.11  ?  786 HOH   A O      1 
HETATM 13018 O  O      . HOH   L 7 .   ? 12.798  -8.478  26.216 1.00 23.08  ?  787 HOH   A O      1 
HETATM 13019 O  O      . HOH   L 7 .   ? 6.463   8.608   22.183 1.00 38.39  ?  788 HOH   A O      1 
HETATM 13020 O  O      . HOH   L 7 .   ? -16.246 5.220   9.007  1.00 61.69  ?  789 HOH   A O      1 
HETATM 13021 O  O      . HOH   L 7 .   ? 4.940   -31.788 39.084 1.00 46.82  ?  790 HOH   A O      1 
HETATM 13022 O  O      . HOH   L 7 .   ? 23.429  -7.747  52.122 1.00 50.46  ?  791 HOH   A O      1 
HETATM 13023 O  O      . HOH   L 7 .   ? -10.250 -12.986 47.994 1.00 39.84  ?  792 HOH   A O      1 
HETATM 13024 O  O      . HOH   L 7 .   ? -13.853 -20.174 39.407 1.00 45.94  ?  793 HOH   A O      1 
HETATM 13025 O  O      . HOH   L 7 .   ? 14.156  -8.082  41.278 1.00 24.41  ?  794 HOH   A O      1 
HETATM 13026 O  O      . HOH   L 7 .   ? -5.194  1.791   41.199 1.00 35.92  ?  795 HOH   A O      1 
HETATM 13027 O  O      . HOH   L 7 .   ? 5.038   -17.153 10.236 1.00 41.03  ?  796 HOH   A O      1 
HETATM 13028 O  O      . HOH   L 7 .   ? 8.485   -17.111 38.135 1.00 29.67  ?  797 HOH   A O      1 
HETATM 13029 O  O      . HOH   L 7 .   ? -2.266  -1.200  58.193 1.00 46.64  ?  798 HOH   A O      1 
HETATM 13030 O  O      . HOH   L 7 .   ? -13.046 -24.608 38.707 1.00 52.76  ?  799 HOH   A O      1 
HETATM 13031 O  O      . HOH   L 7 .   ? -14.955 -14.515 40.805 1.00 52.20  ?  800 HOH   A O      1 
HETATM 13032 O  O      . HOH   L 7 .   ? 0.558   2.350   38.995 1.00 24.64  ?  801 HOH   A O      1 
HETATM 13033 O  O      . HOH   L 7 .   ? 2.792   -11.303 29.020 1.00 23.99  ?  802 HOH   A O      1 
HETATM 13034 O  O      . HOH   L 7 .   ? -3.873  -1.049  30.254 1.00 26.48  ?  803 HOH   A O      1 
HETATM 13035 O  O      . HOH   L 7 .   ? 15.961  6.047   50.039 1.00 51.47  ?  804 HOH   A O      1 
HETATM 13036 O  O      . HOH   L 7 .   ? 13.739  -13.804 41.076 1.00 45.72  ?  805 HOH   A O      1 
HETATM 13037 O  O      . HOH   L 7 .   ? 12.059  -11.016 21.509 1.00 48.90  ?  806 HOH   A O      1 
HETATM 13038 O  O      . HOH   L 7 .   ? 6.203   -0.986  22.724 1.00 26.34  ?  807 HOH   A O      1 
HETATM 13039 O  O      . HOH   L 7 .   ? 1.186   -14.718 34.311 1.00 19.77  ?  808 HOH   A O      1 
HETATM 13040 O  O      . HOH   L 7 .   ? 12.271  -4.869  24.405 1.00 35.38  ?  809 HOH   A O      1 
HETATM 13041 O  O      . HOH   L 7 .   ? -4.572  -22.848 5.223  1.00 53.20  ?  810 HOH   A O      1 
HETATM 13042 O  O      . HOH   L 7 .   ? 17.639  -2.752  28.558 1.00 28.29  ?  811 HOH   A O      1 
HETATM 13043 O  O      . HOH   L 7 .   ? -0.770  -26.246 49.927 1.00 44.50  ?  812 HOH   A O      1 
HETATM 13044 O  O      . HOH   L 7 .   ? 4.486   -33.237 32.352 1.00 39.38  ?  813 HOH   A O      1 
HETATM 13045 O  O      . HOH   L 7 .   ? 0.786   6.810   31.588 1.00 30.66  ?  814 HOH   A O      1 
HETATM 13046 O  O      . HOH   L 7 .   ? -13.940 -5.035  37.269 1.00 38.42  ?  815 HOH   A O      1 
HETATM 13047 O  O      . HOH   L 7 .   ? 5.892   -1.856  14.718 1.00 31.73  ?  816 HOH   A O      1 
HETATM 13048 O  O      . HOH   L 7 .   ? -4.753  -10.917 21.177 1.00 22.69  ?  817 HOH   A O      1 
HETATM 13049 O  O      . HOH   L 7 .   ? -21.673 -17.884 37.342 1.00 51.18  ?  818 HOH   A O      1 
HETATM 13050 O  O      . HOH   L 7 .   ? -2.444  5.909   51.344 1.00 64.22  ?  819 HOH   A O      1 
HETATM 13051 O  O      . HOH   L 7 .   ? 6.765   -23.735 46.255 1.00 36.99  ?  820 HOH   A O      1 
HETATM 13052 O  O      . HOH   L 7 .   ? 11.239  -20.291 9.107  1.00 50.95  ?  821 HOH   A O      1 
HETATM 13053 O  O      . HOH   L 7 .   ? 0.494   -3.195  21.877 1.00 29.57  ?  822 HOH   A O      1 
HETATM 13054 O  O      . HOH   L 7 .   ? 18.687  -32.871 7.726  1.00 46.67  ?  823 HOH   A O      1 
HETATM 13055 O  O      . HOH   L 7 .   ? -5.171  0.763   32.050 1.00 25.90  ?  824 HOH   A O      1 
HETATM 13056 O  O      . HOH   L 7 .   ? 12.529  -0.686  18.500 1.00 57.80  ?  825 HOH   A O      1 
HETATM 13057 O  O      . HOH   L 7 .   ? -1.265  7.764   47.987 1.00 39.47  ?  826 HOH   A O      1 
HETATM 13058 O  O      . HOH   L 7 .   ? 10.191  -12.810 43.179 1.00 41.71  ?  827 HOH   A O      1 
HETATM 13059 O  O      . HOH   L 7 .   ? 1.485   3.570   25.401 1.00 26.89  ?  828 HOH   A O      1 
HETATM 13060 O  O      . HOH   L 7 .   ? -9.182  -29.049 21.821 1.00 59.88  ?  829 HOH   A O      1 
HETATM 13061 O  O      . HOH   L 7 .   ? -6.613  -9.944  23.052 1.00 24.83  ?  830 HOH   A O      1 
HETATM 13062 O  O      . HOH   L 7 .   ? 11.409  -0.904  13.408 1.00 48.36  ?  831 HOH   A O      1 
HETATM 13063 O  O      . HOH   L 7 .   ? -2.937  -14.899 59.124 1.00 53.08  ?  832 HOH   A O      1 
HETATM 13064 O  O      . HOH   L 7 .   ? 3.395   -12.018 56.283 1.00 52.54  ?  833 HOH   A O      1 
HETATM 13065 O  O      . HOH   L 7 .   ? 7.468   0.956   20.925 1.00 31.78  ?  834 HOH   A O      1 
HETATM 13066 O  O      . HOH   L 7 .   ? 6.373   11.188  41.360 1.00 40.79  ?  835 HOH   A O      1 
HETATM 13067 O  O      . HOH   L 7 .   ? -6.250  -29.377 39.504 1.00 31.29  ?  836 HOH   A O      1 
HETATM 13068 O  O      . HOH   L 7 .   ? 7.945   10.655  36.783 1.00 39.48  ?  837 HOH   A O      1 
HETATM 13069 O  O      . HOH   L 7 .   ? -10.494 -31.121 27.177 1.00 52.14  ?  838 HOH   A O      1 
HETATM 13070 O  O      . HOH   L 7 .   ? -3.722  -2.861  21.141 1.00 29.54  ?  839 HOH   A O      1 
HETATM 13071 O  O      . HOH   L 7 .   ? -10.003 -30.651 38.331 1.00 44.08  ?  840 HOH   A O      1 
HETATM 13072 O  O      . HOH   L 7 .   ? 14.985  -17.643 22.428 1.00 38.31  ?  841 HOH   A O      1 
HETATM 13073 O  O      . HOH   L 7 .   ? 3.437   -5.773  59.926 1.00 45.26  ?  842 HOH   A O      1 
HETATM 13074 O  O      . HOH   L 7 .   ? 8.642   -22.116 33.064 1.00 27.37  ?  843 HOH   A O      1 
HETATM 13075 O  O      . HOH   L 7 .   ? -1.957  1.304   35.467 1.00 50.86  ?  844 HOH   A O      1 
HETATM 13076 O  O      . HOH   L 7 .   ? -18.717 -2.004  23.914 1.00 50.50  ?  845 HOH   A O      1 
HETATM 13077 O  O      . HOH   L 7 .   ? 10.328  -19.159 52.128 1.00 58.26  ?  846 HOH   A O      1 
HETATM 13078 O  O      . HOH   L 7 .   ? 5.232   13.240  52.535 1.00 50.95  ?  847 HOH   A O      1 
HETATM 13079 O  O      . HOH   L 7 .   ? 18.773  -1.013  30.350 1.00 23.43  ?  848 HOH   A O      1 
HETATM 13080 O  O      . HOH   L 7 .   ? -3.608  -17.797 51.870 1.00 38.45  ?  849 HOH   A O      1 
HETATM 13081 O  O      . HOH   L 7 .   ? -11.731 -3.474  37.705 1.00 41.20  ?  850 HOH   A O      1 
HETATM 13082 O  O      . HOH   L 7 .   ? 9.068   -19.691 35.663 1.00 42.51  ?  851 HOH   A O      1 
HETATM 13083 O  O      . HOH   L 7 .   ? 8.142   -21.193 10.016 1.00 45.02  ?  852 HOH   A O      1 
HETATM 13084 O  O      . HOH   L 7 .   ? -8.601  0.585   45.404 1.00 32.17  ?  853 HOH   A O      1 
HETATM 13085 O  O      . HOH   L 7 .   ? -5.518  -34.203 25.460 1.00 49.19  ?  854 HOH   A O      1 
HETATM 13086 O  O      . HOH   L 7 .   ? -1.363  -20.994 8.640  1.00 57.91  ?  855 HOH   A O      1 
HETATM 13087 O  O      . HOH   L 7 .   ? 18.039  -12.794 56.319 1.00 52.33  ?  856 HOH   A O      1 
HETATM 13088 O  O      . HOH   L 7 .   ? 13.205  3.101   24.025 1.00 40.73  ?  857 HOH   A O      1 
HETATM 13089 O  O      . HOH   L 7 .   ? 7.864   13.796  50.224 1.00 50.87  ?  858 HOH   A O      1 
HETATM 13090 O  O      . HOH   L 7 .   ? 8.407   -13.174 45.632 1.00 26.10  ?  859 HOH   A O      1 
HETATM 13091 O  O      . HOH   L 7 .   ? -9.753  2.071   37.850 1.00 53.80  ?  860 HOH   A O      1 
HETATM 13092 O  O      . HOH   L 7 .   ? 16.975  -10.352 50.771 1.00 59.44  ?  861 HOH   A O      1 
HETATM 13093 O  O      . HOH   L 7 .   ? -5.200  -32.077 22.489 1.00 51.82  ?  862 HOH   A O      1 
HETATM 13094 O  O      . HOH   L 7 .   ? 19.824  3.622   36.121 1.00 26.90  ?  863 HOH   A O      1 
HETATM 13095 O  O      . HOH   L 7 .   ? 15.038  -15.469 51.489 1.00 52.08  ?  864 HOH   A O      1 
HETATM 13096 O  O      . HOH   L 7 .   ? 4.415   -13.947 54.863 1.00 36.16  ?  865 HOH   A O      1 
HETATM 13097 O  O      . HOH   L 7 .   ? 13.091  -15.951 14.113 1.00 52.96  ?  866 HOH   A O      1 
HETATM 13098 O  O      . HOH   L 7 .   ? 18.775  -3.726  49.129 1.00 46.67  ?  867 HOH   A O      1 
HETATM 13099 O  O      . HOH   L 7 .   ? 7.736   -19.927 38.930 1.00 25.04  ?  868 HOH   A O      1 
HETATM 13100 O  O      . HOH   L 7 .   ? 18.326  -5.084  45.019 1.00 57.74  ?  869 HOH   A O      1 
HETATM 13101 O  O      . HOH   L 7 .   ? -14.156 3.290   31.496 1.00 45.54  ?  870 HOH   A O      1 
HETATM 13102 O  O      . HOH   L 7 .   ? 3.303   -19.009 33.038 1.00 25.41  ?  871 HOH   A O      1 
HETATM 13103 O  O      . HOH   L 7 .   ? -6.842  -30.403 23.326 1.00 37.17  ?  872 HOH   A O      1 
HETATM 13104 O  O      . HOH   L 7 .   ? -15.662 -13.354 26.180 1.00 44.76  ?  873 HOH   A O      1 
HETATM 13105 O  O      . HOH   L 7 .   ? 9.228   -30.950 21.924 1.00 56.14  ?  874 HOH   A O      1 
HETATM 13106 O  O      . HOH   L 7 .   ? -4.756  -16.021 6.615  1.00 57.25  ?  875 HOH   A O      1 
HETATM 13107 O  O      . HOH   L 7 .   ? 17.185  -0.954  39.689 1.00 38.45  ?  876 HOH   A O      1 
HETATM 13108 O  O      . HOH   L 7 .   ? 9.969   -30.352 27.996 1.00 32.46  ?  877 HOH   A O      1 
HETATM 13109 O  O      . HOH   L 7 .   ? -12.496 -0.289  3.702  1.00 54.71  ?  878 HOH   A O      1 
HETATM 13110 O  O      . HOH   L 7 .   ? 12.058  -16.112 32.981 1.00 48.25  ?  879 HOH   A O      1 
HETATM 13111 O  O      . HOH   L 7 .   ? 0.587   7.270   28.949 1.00 48.85  ?  880 HOH   A O      1 
HETATM 13112 O  O      . HOH   L 7 .   ? -10.907 -3.054  49.512 1.00 55.51  ?  881 HOH   A O      1 
HETATM 13113 O  O      . HOH   L 7 .   ? -2.905  1.643   33.166 1.00 52.54  ?  882 HOH   A O      1 
HETATM 13114 O  O      . HOH   L 7 .   ? -0.370  0.940   21.085 1.00 34.70  ?  883 HOH   A O      1 
HETATM 13115 O  O      . HOH   L 7 .   ? -13.459 12.081  19.333 1.00 47.78  ?  884 HOH   A O      1 
HETATM 13116 O  O      . HOH   L 7 .   ? 15.545  -17.047 37.633 1.00 41.89  ?  885 HOH   A O      1 
HETATM 13117 O  O      . HOH   L 7 .   ? -4.860  1.777   4.601  1.00 55.23  ?  886 HOH   A O      1 
HETATM 13118 O  O      . HOH   L 7 .   ? 9.756   -16.953 40.560 1.00 51.11  ?  887 HOH   A O      1 
HETATM 13119 O  O      . HOH   L 7 .   ? 11.404  -14.979 42.045 1.00 46.76  ?  888 HOH   A O      1 
HETATM 13120 O  O      . HOH   L 7 .   ? -12.721 -0.322  37.071 1.00 53.46  ?  889 HOH   A O      1 
HETATM 13121 O  O      . HOH   L 7 .   ? 17.777  3.462   46.671 1.00 47.46  ?  890 HOH   A O      1 
HETATM 13122 O  O      . HOH   L 7 .   ? 15.320  -35.814 14.989 1.00 53.83  ?  891 HOH   A O      1 
HETATM 13123 O  O      . HOH   L 7 .   ? -3.358  1.538   37.943 1.00 49.38  ?  892 HOH   A O      1 
HETATM 13124 O  O      . HOH   L 7 .   ? 23.781  -13.136 57.511 1.00 57.03  ?  893 HOH   A O      1 
HETATM 13125 O  O      . HOH   L 7 .   ? 27.350  -4.005  66.628 1.00 61.22  ?  894 HOH   A O      1 
HETATM 13126 O  O      . HOH   L 7 .   ? 14.608  -2.823  23.372 1.00 46.76  ?  895 HOH   A O      1 
HETATM 13127 O  O      . HOH   L 7 .   ? 10.965  11.247  30.735 1.00 59.65  ?  896 HOH   A O      1 
HETATM 13128 O  O      . HOH   L 7 .   ? 1.353   -16.892 32.710 1.00 26.34  ?  897 HOH   A O      1 
HETATM 13129 O  O      . HOH   L 7 .   ? 17.685  1.739   26.988 1.00 36.53  ?  898 HOH   A O      1 
HETATM 13130 O  O      . HOH   L 7 .   ? 15.349  -13.667 36.921 1.00 42.84  ?  899 HOH   A O      1 
HETATM 13131 O  O      . HOH   L 7 .   ? -5.611  3.535   31.315 1.00 30.37  ?  900 HOH   A O      1 
HETATM 13132 O  O      . HOH   L 7 .   ? 20.823  -7.412  32.608 1.00 40.77  ?  901 HOH   A O      1 
HETATM 13133 O  O      . HOH   L 7 .   ? -19.012 -4.345  28.933 1.00 52.45  ?  902 HOH   A O      1 
HETATM 13134 O  O      . HOH   L 7 .   ? -2.901  4.139   32.372 1.00 45.94  ?  903 HOH   A O      1 
HETATM 13135 O  O      . HOH   L 7 .   ? 1.523   -16.115 52.397 1.00 48.39  ?  904 HOH   A O      1 
HETATM 13136 O  O      . HOH   L 7 .   ? 16.924  -7.308  36.325 1.00 35.96  ?  905 HOH   A O      1 
HETATM 13137 O  O      . HOH   L 7 .   ? 17.728  0.380   42.051 1.00 53.63  ?  906 HOH   A O      1 
HETATM 13138 O  O      . HOH   L 7 .   ? 11.674  10.765  33.672 1.00 49.41  ?  907 HOH   A O      1 
HETATM 13139 O  O      . HOH   L 7 .   ? 8.649   -30.113 42.680 1.00 46.23  ?  908 HOH   A O      1 
HETATM 13140 O  O      . HOH   L 7 .   ? 8.114   -30.938 17.825 1.00 43.76  ?  909 HOH   A O      1 
HETATM 13141 O  O      . HOH   L 7 .   ? 9.569   -30.170 24.316 1.00 56.28  ?  910 HOH   A O      1 
HETATM 13142 O  O      . HOH   L 7 .   ? -14.719 -19.931 37.162 1.00 48.84  ?  911 HOH   A O      1 
HETATM 13143 O  O      . HOH   L 7 .   ? 13.856  7.420   28.736 1.00 47.54  ?  912 HOH   A O      1 
HETATM 13144 O  O      . HOH   L 7 .   ? 7.853   -19.594 42.235 1.00 38.50  ?  913 HOH   A O      1 
HETATM 13145 O  O      . HOH   L 7 .   ? -3.542  6.442   28.434 1.00 53.52  ?  914 HOH   A O      1 
HETATM 13146 O  O      . HOH   L 7 .   ? -13.979 0.985   35.506 1.00 51.27  ?  915 HOH   A O      1 
HETATM 13147 O  O      . HOH   L 7 .   ? -1.166  10.105  41.235 1.00 50.52  ?  916 HOH   A O      1 
HETATM 13148 O  O      . HOH   L 7 .   ? -13.845 -25.064 36.710 1.00 52.95  ?  917 HOH   A O      1 
HETATM 13149 O  O      . HOH   L 7 .   ? 5.222   -30.862 19.249 1.00 33.55  ?  918 HOH   A O      1 
HETATM 13150 O  O      . HOH   L 7 .   ? 15.808  7.190   38.174 1.00 45.16  ?  919 HOH   A O      1 
HETATM 13151 O  O      . HOH   L 7 .   ? -17.000 -18.533 37.167 1.00 51.36  ?  920 HOH   A O      1 
HETATM 13152 O  O      . HOH   L 7 .   ? 6.788   -22.988 8.382  1.00 54.58  ?  921 HOH   A O      1 
HETATM 13153 O  O      . HOH   L 7 .   ? 16.918  -34.536 7.238  1.00 52.91  ?  922 HOH   A O      1 
HETATM 13154 O  O      . HOH   L 7 .   ? 12.661  -11.464 43.762 1.00 47.83  ?  923 HOH   A O      1 
HETATM 13155 O  O      . HOH   L 7 .   ? -14.711 2.344   19.413 1.00 58.22  ?  924 HOH   A O      1 
HETATM 13156 O  O      . HOH   L 7 .   ? 2.879   13.064  51.058 1.00 59.89  ?  925 HOH   A O      1 
HETATM 13157 O  O      . HOH   L 7 .   ? 0.218   2.696   23.102 1.00 41.47  ?  926 HOH   A O      1 
HETATM 13158 O  O      . HOH   L 7 .   ? -14.753 -22.244 35.457 1.00 51.08  ?  927 HOH   A O      1 
HETATM 13159 O  O      . HOH   L 7 .   ? -1.482  -1.672  21.066 1.00 44.74  ?  928 HOH   A O      1 
HETATM 13160 O  O      . HOH   L 7 .   ? -9.230  1.449   48.073 1.00 64.97  ?  929 HOH   A O      1 
HETATM 13161 O  O      . HOH   L 7 .   ? -8.883  -32.988 36.424 1.00 50.95  ?  930 HOH   A O      1 
HETATM 13162 O  O      . HOH   L 7 .   ? 8.685   -17.362 42.699 1.00 40.71  ?  931 HOH   A O      1 
HETATM 13163 O  O      . HOH   L 7 .   ? 12.850  -9.093  43.295 1.00 36.02  ?  932 HOH   A O      1 
HETATM 13164 O  O      . HOH   L 7 .   ? 19.409  -8.384  49.075 1.00 46.49  ?  933 HOH   A O      1 
HETATM 13165 O  O      . HOH   L 7 .   ? 11.344  -15.950 45.665 1.00 53.77  ?  934 HOH   A O      1 
HETATM 13166 O  O      . HOH   L 7 .   ? 7.473   -30.787 23.916 1.00 57.73  ?  935 HOH   A O      1 
HETATM 13167 O  O      . HOH   L 7 .   ? 6.489   13.167  47.916 1.00 61.30  ?  936 HOH   A O      1 
HETATM 13168 O  O      . HOH   L 7 .   ? 15.431  -15.276 39.363 1.00 44.58  ?  937 HOH   A O      1 
HETATM 13169 O  O      . HOH   L 7 .   ? 14.449  2.512   26.035 1.00 52.12  ?  938 HOH   A O      1 
HETATM 13170 O  O      . HOH   L 7 .   ? 6.790   -29.434 13.983 1.00 47.41  ?  939 HOH   A O      1 
HETATM 13171 O  O      . HOH   L 7 .   ? 12.051  -31.216 29.177 1.00 32.83  ?  940 HOH   A O      1 
HETATM 13172 O  O      . HOH   L 7 .   ? -11.234 -9.730  50.139 1.00 50.27  ?  941 HOH   A O      1 
HETATM 13173 O  O      . HOH   L 7 .   ? 16.798  -0.790  26.400 1.00 28.50  ?  942 HOH   A O      1 
HETATM 13174 O  O      . HOH   L 7 .   ? 5.447   -26.897 10.245 1.00 46.98  ?  943 HOH   A O      1 
HETATM 13175 O  O      . HOH   L 7 .   ? -13.578 -10.073 46.484 1.00 59.90  ?  944 HOH   A O      1 
HETATM 13176 O  O      . HOH   L 7 .   ? -0.212  -36.789 34.460 1.00 59.53  ?  945 HOH   A O      1 
HETATM 13177 O  O      . HOH   L 7 .   ? -18.074 -12.705 24.936 1.00 54.41  ?  946 HOH   A O      1 
HETATM 13178 O  O      . HOH   L 7 .   ? 17.634  6.147   39.355 1.00 57.37  ?  947 HOH   A O      1 
HETATM 13179 O  O      . HOH   L 7 .   ? 18.590  4.021   40.220 1.00 54.23  ?  948 HOH   A O      1 
HETATM 13180 O  O      . HOH   M 7 .   ? 37.765  -12.999 11.928 1.00 48.69  ?  601 HOH   B O      1 
HETATM 13181 O  O      . HOH   M 7 .   ? 30.341  -12.701 47.164 1.00 42.18  ?  602 HOH   B O      1 
HETATM 13182 O  O      . HOH   M 7 .   ? 29.902  -37.590 4.988  1.00 63.00  ?  603 HOH   B O      1 
HETATM 13183 O  O      . HOH   M 7 .   ? 28.739  -34.590 -1.377 1.00 45.19  ?  604 HOH   B O      1 
HETATM 13184 O  O      . HOH   M 7 .   ? 15.062  -16.856 14.676 1.00 43.39  ?  605 HOH   B O      1 
HETATM 13185 O  O      . HOH   M 7 .   ? 36.907  -30.261 52.171 1.00 56.74  ?  606 HOH   B O      1 
HETATM 13186 O  O      . HOH   M 7 .   ? 19.163  -13.222 51.014 1.00 52.91  ?  607 HOH   B O      1 
HETATM 13187 O  O      . HOH   M 7 .   ? 13.456  -17.334 18.182 1.00 50.16  ?  608 HOH   B O      1 
HETATM 13188 O  O      . HOH   M 7 .   ? 45.105  -7.333  30.333 1.00 46.83  ?  609 HOH   B O      1 
HETATM 13189 O  O      . HOH   M 7 .   ? 42.700  -16.990 14.237 1.00 56.98  ?  610 HOH   B O      1 
HETATM 13190 O  O      . HOH   M 7 .   ? 17.932  -33.184 -3.700 1.00 47.03  ?  611 HOH   B O      1 
HETATM 13191 O  O      . HOH   M 7 .   ? 14.600  -10.090 22.373 1.00 33.44  ?  612 HOH   B O      1 
HETATM 13192 O  O      . HOH   M 7 .   ? 11.173  -20.045 54.529 1.00 54.41  ?  613 HOH   B O      1 
HETATM 13193 O  O      . HOH   M 7 .   ? 3.770   -11.627 5.137  1.00 57.13  ?  614 HOH   B O      1 
HETATM 13194 O  O      . HOH   M 7 .   ? 34.832  -0.781  37.026 1.00 37.14  ?  615 HOH   B O      1 
HETATM 13195 O  O      . HOH   M 7 .   ? 18.306  -23.071 45.482 1.00 34.37  ?  616 HOH   B O      1 
HETATM 13196 O  O      . HOH   M 7 .   ? 15.482  -16.472 24.913 1.00 24.20  ?  617 HOH   B O      1 
HETATM 13197 O  O      . HOH   M 7 .   ? 29.562  -31.967 -5.168 1.00 51.08  ?  618 HOH   B O      1 
HETATM 13198 O  O      . HOH   M 7 .   ? 26.923  -21.596 21.865 1.00 22.12  ?  619 HOH   B O      1 
HETATM 13199 O  O      . HOH   M 7 .   ? 41.404  -18.964 11.134 1.00 52.94  ?  620 HOH   B O      1 
HETATM 13200 O  O      . HOH   M 7 .   ? 20.986  -14.176 48.403 1.00 53.62  ?  621 HOH   B O      1 
HETATM 13201 O  O      . HOH   M 7 .   ? 18.798  -41.201 30.301 1.00 51.29  ?  622 HOH   B O      1 
HETATM 13202 O  O      . HOH   M 7 .   ? -3.524  -0.317  3.894  1.00 49.86  ?  623 HOH   B O      1 
HETATM 13203 O  O      . HOH   M 7 .   ? 11.591  -24.173 30.979 1.00 26.30  ?  624 HOH   B O      1 
HETATM 13204 O  O      . HOH   M 7 .   ? 44.206  -10.834 32.231 1.00 42.00  ?  625 HOH   B O      1 
HETATM 13205 O  O      . HOH   M 7 .   ? 27.633  -27.091 20.929 1.00 26.75  ?  626 HOH   B O      1 
HETATM 13206 O  O      . HOH   M 7 .   ? 19.168  -16.971 58.560 1.00 49.13  ?  627 HOH   B O      1 
HETATM 13207 O  O      . HOH   M 7 .   ? 39.041  -3.646  21.616 1.00 49.51  ?  628 HOH   B O      1 
HETATM 13208 O  O      . HOH   M 7 .   ? 14.925  -38.450 28.643 1.00 50.09  ?  629 HOH   B O      1 
HETATM 13209 O  O      . HOH   M 7 .   ? 35.777  1.714   29.443 1.00 59.35  ?  630 HOH   B O      1 
HETATM 13210 O  O      . HOH   M 7 .   ? 29.987  -28.277 27.631 1.00 28.09  ?  631 HOH   B O      1 
HETATM 13211 O  O      . HOH   M 7 .   ? 11.022  -30.467 41.510 1.00 48.13  ?  632 HOH   B O      1 
HETATM 13212 O  O      . HOH   M 7 .   ? 43.117  -12.701 19.657 1.00 54.96  ?  633 HOH   B O      1 
HETATM 13213 O  O      . HOH   M 7 .   ? 10.954  -18.803 29.197 1.00 24.34  ?  634 HOH   B O      1 
HETATM 13214 O  O      . HOH   M 7 .   ? 47.705  -10.099 31.849 1.00 41.83  ?  635 HOH   B O      1 
HETATM 13215 O  O      . HOH   M 7 .   ? 37.707  -31.729 42.340 1.00 40.15  ?  636 HOH   B O      1 
HETATM 13216 O  O      . HOH   M 7 .   ? 39.744  -29.496 32.876 1.00 39.81  ?  637 HOH   B O      1 
HETATM 13217 O  O      . HOH   M 7 .   ? 28.981  -37.146 27.044 1.00 31.88  ?  638 HOH   B O      1 
HETATM 13218 O  O      . HOH   M 7 .   ? 26.250  1.153   34.192 1.00 38.57  ?  639 HOH   B O      1 
HETATM 13219 O  O      . HOH   M 7 .   ? 40.330  -37.272 18.178 1.00 57.27  ?  640 HOH   B O      1 
HETATM 13220 O  O      . HOH   M 7 .   ? 6.179   7.436   15.036 1.00 55.38  ?  641 HOH   B O      1 
HETATM 13221 O  O      . HOH   M 7 .   ? 26.837  -16.384 43.266 1.00 29.94  ?  642 HOH   B O      1 
HETATM 13222 O  O      . HOH   M 7 .   ? 31.211  -30.355 33.244 1.00 31.60  ?  643 HOH   B O      1 
HETATM 13223 O  O      . HOH   M 7 .   ? 38.248  -16.654 5.465  1.00 56.63  ?  644 HOH   B O      1 
HETATM 13224 O  O      . HOH   M 7 .   ? 46.054  -18.266 38.636 1.00 50.56  ?  645 HOH   B O      1 
HETATM 13225 O  O      . HOH   M 7 .   ? 26.613  -39.971 47.912 1.00 37.82  ?  646 HOH   B O      1 
HETATM 13226 O  O      . HOH   M 7 .   ? 22.697  -36.441 34.275 1.00 22.05  ?  647 HOH   B O      1 
HETATM 13227 O  O      . HOH   M 7 .   ? 19.149  -3.924  26.440 1.00 29.27  ?  648 HOH   B O      1 
HETATM 13228 O  O      . HOH   M 7 .   ? 43.185  -19.186 20.281 1.00 45.41  ?  649 HOH   B O      1 
HETATM 13229 O  O      . HOH   M 7 .   ? 22.881  -35.430 16.669 1.00 42.91  ?  650 HOH   B O      1 
HETATM 13230 O  O      . HOH   M 7 .   ? 42.527  -6.629  35.629 1.00 31.73  ?  651 HOH   B O      1 
HETATM 13231 O  O      . HOH   M 7 .   ? 29.175  -28.668 34.335 1.00 21.41  ?  652 HOH   B O      1 
HETATM 13232 O  O      . HOH   M 7 .   ? 17.785  -7.527  29.022 1.00 31.29  ?  653 HOH   B O      1 
HETATM 13233 O  O      . HOH   M 7 .   ? 33.037  -31.885 38.717 1.00 28.92  ?  654 HOH   B O      1 
HETATM 13234 O  O      . HOH   M 7 .   ? 22.655  -40.107 52.194 1.00 49.13  ?  655 HOH   B O      1 
HETATM 13235 O  O      . HOH   M 7 .   ? 17.029  -37.722 30.260 1.00 43.92  ?  656 HOH   B O      1 
HETATM 13236 O  O      . HOH   M 7 .   ? 42.114  -27.340 34.006 1.00 43.91  ?  657 HOH   B O      1 
HETATM 13237 O  O      . HOH   M 7 .   ? 33.258  -3.553  30.144 1.00 27.55  ?  658 HOH   B O      1 
HETATM 13238 O  O      . HOH   M 7 .   ? 35.426  -1.765  40.942 1.00 46.17  ?  659 HOH   B O      1 
HETATM 13239 O  O      . HOH   M 7 .   ? 32.024  -35.769 51.863 1.00 53.16  ?  660 HOH   B O      1 
HETATM 13240 O  O      . HOH   M 7 .   ? -2.079  2.568   3.361  1.00 55.05  ?  661 HOH   B O      1 
HETATM 13241 O  O      . HOH   M 7 .   ? 23.598  -39.655 28.661 1.00 40.31  ?  662 HOH   B O      1 
HETATM 13242 O  O      . HOH   M 7 .   ? 42.972  -33.094 17.618 1.00 45.17  ?  663 HOH   B O      1 
HETATM 13243 O  O      . HOH   M 7 .   ? 31.056  -36.943 30.136 1.00 42.79  ?  664 HOH   B O      1 
HETATM 13244 O  O      . HOH   M 7 .   ? 14.778  -5.925  23.197 1.00 47.36  ?  665 HOH   B O      1 
HETATM 13245 O  O      . HOH   M 7 .   ? 15.449  -16.739 34.855 1.00 36.53  ?  666 HOH   B O      1 
HETATM 13246 O  O      . HOH   M 7 .   ? 26.924  -33.999 62.647 1.00 55.85  ?  667 HOH   B O      1 
HETATM 13247 O  O      . HOH   M 7 .   ? 21.168  -36.737 50.992 1.00 50.90  ?  668 HOH   B O      1 
HETATM 13248 O  O      . HOH   M 7 .   ? 25.587  -8.783  41.276 1.00 39.08  ?  669 HOH   B O      1 
HETATM 13249 O  O      . HOH   M 7 .   ? -4.076  0.725   14.511 1.00 49.65  ?  670 HOH   B O      1 
HETATM 13250 O  O      . HOH   M 7 .   ? 37.751  -7.035  45.247 1.00 44.30  ?  671 HOH   B O      1 
HETATM 13251 O  O      . HOH   M 7 .   ? 14.273  -14.416 15.233 1.00 51.18  ?  672 HOH   B O      1 
HETATM 13252 O  O      . HOH   M 7 .   ? 5.181   -2.582  6.666  1.00 40.32  ?  673 HOH   B O      1 
HETATM 13253 O  O      . HOH   M 7 .   ? 36.151  -29.128 16.862 1.00 36.04  ?  674 HOH   B O      1 
HETATM 13254 O  O      A HOH   M 7 .   ? 22.774  -16.134 24.756 0.48 22.70  ?  675 HOH   B O      1 
HETATM 13255 O  O      B HOH   M 7 .   ? 23.646  -15.839 22.976 0.52 25.29  ?  675 HOH   B O      1 
HETATM 13256 O  O      . HOH   M 7 .   ? 25.663  -22.008 24.922 1.00 30.98  ?  676 HOH   B O      1 
HETATM 13257 O  O      . HOH   M 7 .   ? 16.218  -32.445 46.946 1.00 39.03  ?  677 HOH   B O      1 
HETATM 13258 O  O      . HOH   M 7 .   ? 20.809  -41.586 32.131 1.00 44.33  ?  678 HOH   B O      1 
HETATM 13259 O  O      . HOH   M 7 .   ? 24.774  1.629   27.408 1.00 34.71  ?  679 HOH   B O      1 
HETATM 13260 O  O      . HOH   M 7 .   ? 36.154  -30.512 36.727 1.00 45.89  ?  680 HOH   B O      1 
HETATM 13261 O  O      . HOH   M 7 .   ? 32.158  -0.260  37.743 1.00 39.84  ?  681 HOH   B O      1 
HETATM 13262 O  O      . HOH   M 7 .   ? 17.773  -30.358 8.112  1.00 43.82  ?  682 HOH   B O      1 
HETATM 13263 O  O      . HOH   M 7 .   ? 17.186  -37.393 39.274 1.00 36.44  ?  683 HOH   B O      1 
HETATM 13264 O  O      . HOH   M 7 .   ? 25.583  -16.625 33.527 1.00 28.85  ?  684 HOH   B O      1 
HETATM 13265 O  O      . HOH   M 7 .   ? 24.662  -18.606 31.283 1.00 18.62  ?  685 HOH   B O      1 
HETATM 13266 O  O      . HOH   M 7 .   ? -3.743  -2.908  17.083 1.00 31.35  ?  686 HOH   B O      1 
HETATM 13267 O  O      . HOH   M 7 .   ? 19.582  -13.092 30.275 1.00 31.44  ?  687 HOH   B O      1 
HETATM 13268 O  O      . HOH   M 7 .   ? 25.490  -32.507 19.750 1.00 29.89  ?  688 HOH   B O      1 
HETATM 13269 O  O      . HOH   M 7 .   ? 20.635  -34.293 19.372 1.00 27.30  ?  689 HOH   B O      1 
HETATM 13270 O  O      . HOH   M 7 .   ? 22.751  -4.746  38.048 1.00 34.80  ?  690 HOH   B O      1 
HETATM 13271 O  O      . HOH   M 7 .   ? 11.366  -20.473 35.423 1.00 29.09  ?  691 HOH   B O      1 
HETATM 13272 O  O      . HOH   M 7 .   ? 16.078  -20.549 40.055 1.00 44.45  ?  692 HOH   B O      1 
HETATM 13273 O  O      . HOH   M 7 .   ? 32.265  -23.394 32.871 1.00 22.90  ?  693 HOH   B O      1 
HETATM 13274 O  O      . HOH   M 7 .   ? 13.081  -26.864 41.971 1.00 33.22  ?  694 HOH   B O      1 
HETATM 13275 O  O      . HOH   M 7 .   ? 25.862  -0.257  25.847 1.00 39.82  ?  695 HOH   B O      1 
HETATM 13276 O  O      . HOH   M 7 .   ? 14.467  -31.728 27.831 1.00 29.13  ?  696 HOH   B O      1 
HETATM 13277 O  O      . HOH   M 7 .   ? 31.119  -38.394 25.724 1.00 42.14  ?  697 HOH   B O      1 
HETATM 13278 O  O      . HOH   M 7 .   ? 10.159  -26.465 35.029 1.00 30.63  ?  698 HOH   B O      1 
HETATM 13279 O  O      . HOH   M 7 .   ? 16.467  -34.813 29.939 1.00 28.59  ?  699 HOH   B O      1 
HETATM 13280 O  O      . HOH   M 7 .   ? 27.467  -19.164 30.903 1.00 20.31  ?  700 HOH   B O      1 
HETATM 13281 O  O      . HOH   M 7 .   ? 16.800  -4.740  12.870 1.00 36.77  ?  701 HOH   B O      1 
HETATM 13282 O  O      . HOH   M 7 .   ? 37.943  -1.096  35.747 1.00 49.75  ?  702 HOH   B O      1 
HETATM 13283 O  O      . HOH   M 7 .   ? 16.360  -38.966 35.295 1.00 39.91  ?  703 HOH   B O      1 
HETATM 13284 O  O      . HOH   M 7 .   ? 23.149  -8.096  9.039  1.00 49.76  ?  704 HOH   B O      1 
HETATM 13285 O  O      . HOH   M 7 .   ? 25.345  -26.693 60.684 1.00 51.74  ?  705 HOH   B O      1 
HETATM 13286 O  O      . HOH   M 7 .   ? 36.660  -32.094 39.478 1.00 39.57  ?  706 HOH   B O      1 
HETATM 13287 O  O      . HOH   M 7 .   ? 14.397  -23.095 40.325 1.00 38.22  ?  707 HOH   B O      1 
HETATM 13288 O  O      . HOH   M 7 .   ? 24.373  -14.804 55.264 1.00 38.83  ?  708 HOH   B O      1 
HETATM 13289 O  O      . HOH   M 7 .   ? 28.723  -24.256 1.432  1.00 50.62  ?  709 HOH   B O      1 
HETATM 13290 O  O      . HOH   M 7 .   ? 23.544  -14.480 45.974 1.00 29.04  ?  710 HOH   B O      1 
HETATM 13291 O  O      . HOH   M 7 .   ? 14.934  -24.241 24.551 1.00 31.85  ?  711 HOH   B O      1 
HETATM 13292 O  O      . HOH   M 7 .   ? 16.650  -19.801 22.048 1.00 38.05  ?  712 HOH   B O      1 
HETATM 13293 O  O      . HOH   M 7 .   ? 34.085  -0.735  32.246 1.00 35.31  ?  713 HOH   B O      1 
HETATM 13294 O  O      . HOH   M 7 .   ? 29.504  -10.981 10.864 1.00 38.35  ?  714 HOH   B O      1 
HETATM 13295 O  O      . HOH   M 7 .   ? 30.189  -27.582 19.888 1.00 27.11  ?  715 HOH   B O      1 
HETATM 13296 O  O      . HOH   M 7 .   ? 31.268  -29.929 30.693 1.00 30.34  ?  716 HOH   B O      1 
HETATM 13297 O  O      . HOH   M 7 .   ? 26.440  -24.287 23.168 1.00 19.88  ?  717 HOH   B O      1 
HETATM 13298 O  O      . HOH   M 7 .   ? 36.400  -16.258 3.672  1.00 49.24  ?  718 HOH   B O      1 
HETATM 13299 O  O      . HOH   M 7 .   ? 5.554   0.980   13.953 1.00 38.95  ?  719 HOH   B O      1 
HETATM 13300 O  O      . HOH   M 7 .   ? 25.082  -15.418 31.134 1.00 26.37  ?  720 HOH   B O      1 
HETATM 13301 O  O      . HOH   M 7 .   ? 22.232  -31.506 26.080 1.00 21.80  ?  721 HOH   B O      1 
HETATM 13302 O  O      . HOH   M 7 .   ? 44.037  -32.547 28.700 1.00 49.32  ?  722 HOH   B O      1 
HETATM 13303 O  O      . HOH   M 7 .   ? 42.405  -16.933 44.540 1.00 47.53  ?  723 HOH   B O      1 
HETATM 13304 O  O      . HOH   M 7 .   ? 21.937  -11.807 30.664 1.00 26.32  ?  724 HOH   B O      1 
HETATM 13305 O  O      . HOH   M 7 .   ? 10.957  -21.620 31.238 1.00 33.09  ?  725 HOH   B O      1 
HETATM 13306 O  O      . HOH   M 7 .   ? 27.480  3.062   18.909 1.00 54.41  ?  726 HOH   B O      1 
HETATM 13307 O  O      . HOH   M 7 .   ? 8.011   -28.355 40.535 1.00 31.19  ?  727 HOH   B O      1 
HETATM 13308 O  O      . HOH   M 7 .   ? 36.715  -23.447 19.259 1.00 34.58  ?  728 HOH   B O      1 
HETATM 13309 O  O      . HOH   M 7 .   ? 43.756  -25.642 32.802 1.00 40.06  ?  729 HOH   B O      1 
HETATM 13310 O  O      . HOH   M 7 .   ? 23.614  -0.804  22.688 1.00 43.22  ?  730 HOH   B O      1 
HETATM 13311 O  O      . HOH   M 7 .   ? 42.197  -9.540  33.607 1.00 31.08  ?  731 HOH   B O      1 
HETATM 13312 O  O      . HOH   M 7 .   ? 32.003  -1.438  15.951 1.00 50.27  ?  732 HOH   B O      1 
HETATM 13313 O  O      . HOH   M 7 .   ? 28.552  -3.679  10.884 1.00 52.74  ?  733 HOH   B O      1 
HETATM 13314 O  O      . HOH   M 7 .   ? 26.580  -8.240  46.046 1.00 46.76  ?  734 HOH   B O      1 
HETATM 13315 O  O      . HOH   M 7 .   ? 29.361  -30.567 28.957 1.00 26.60  ?  735 HOH   B O      1 
HETATM 13316 O  O      . HOH   M 7 .   ? 18.007  -22.125 26.267 1.00 21.05  ?  736 HOH   B O      1 
HETATM 13317 O  O      . HOH   M 7 .   ? 23.864  -12.000 28.839 1.00 23.03  ?  737 HOH   B O      1 
HETATM 13318 O  O      . HOH   M 7 .   ? 45.955  -19.274 24.652 1.00 39.79  ?  738 HOH   B O      1 
HETATM 13319 O  O      . HOH   M 7 .   ? 17.682  -21.971 41.955 1.00 25.46  ?  739 HOH   B O      1 
HETATM 13320 O  O      . HOH   M 7 .   ? 14.653  -3.486  11.669 1.00 47.26  ?  740 HOH   B O      1 
HETATM 13321 O  O      . HOH   M 7 .   ? 15.396  -35.643 26.764 1.00 45.46  ?  741 HOH   B O      1 
HETATM 13322 O  O      . HOH   M 7 .   ? 27.255  -41.459 45.492 1.00 55.98  ?  742 HOH   B O      1 
HETATM 13323 O  O      . HOH   M 7 .   ? 41.554  -6.978  32.935 1.00 31.45  ?  743 HOH   B O      1 
HETATM 13324 O  O      . HOH   M 7 .   ? 33.603  -41.011 6.216  1.00 56.39  ?  744 HOH   B O      1 
HETATM 13325 O  O      . HOH   M 7 .   ? 24.513  -15.039 40.879 1.00 30.67  ?  745 HOH   B O      1 
HETATM 13326 O  O      . HOH   M 7 .   ? 34.432  -36.470 27.605 1.00 43.55  ?  746 HOH   B O      1 
HETATM 13327 O  O      . HOH   M 7 .   ? 31.845  -29.758 59.710 1.00 47.23  ?  747 HOH   B O      1 
HETATM 13328 O  O      . HOH   M 7 .   ? 28.225  -32.239 17.084 1.00 40.88  ?  748 HOH   B O      1 
HETATM 13329 O  O      . HOH   M 7 .   ? 23.919  -19.097 26.425 1.00 25.65  ?  749 HOH   B O      1 
HETATM 13330 O  O      . HOH   M 7 .   ? 31.964  -35.295 39.093 1.00 33.18  ?  750 HOH   B O      1 
HETATM 13331 O  O      . HOH   M 7 .   ? 43.372  -23.535 44.042 1.00 52.30  ?  751 HOH   B O      1 
HETATM 13332 O  O      . HOH   M 7 .   ? 25.323  -36.545 17.466 1.00 44.42  ?  752 HOH   B O      1 
HETATM 13333 O  O      . HOH   M 7 .   ? 18.382  -14.728 32.436 1.00 49.01  ?  753 HOH   B O      1 
HETATM 13334 O  O      . HOH   M 7 .   ? 26.617  -17.437 58.122 1.00 51.42  ?  754 HOH   B O      1 
HETATM 13335 O  O      . HOH   M 7 .   ? 51.530  -21.601 25.356 1.00 47.97  ?  755 HOH   B O      1 
HETATM 13336 O  O      . HOH   M 7 .   ? 6.341   -5.141  7.261  1.00 38.34  ?  756 HOH   B O      1 
HETATM 13337 O  O      . HOH   M 7 .   ? 15.763  -23.674 27.061 1.00 21.82  ?  757 HOH   B O      1 
HETATM 13338 O  O      . HOH   M 7 .   ? 29.242  -15.963 44.852 1.00 28.04  ?  758 HOH   B O      1 
HETATM 13339 O  O      . HOH   M 7 .   ? 21.332  -11.322 33.847 1.00 39.38  ?  759 HOH   B O      1 
HETATM 13340 O  O      . HOH   M 7 .   ? 11.596  -28.730 31.315 1.00 32.63  ?  760 HOH   B O      1 
HETATM 13341 O  O      . HOH   M 7 .   ? 14.275  -32.522 20.943 1.00 54.54  ?  761 HOH   B O      1 
HETATM 13342 O  O      . HOH   M 7 .   ? 38.549  -28.537 53.157 1.00 57.59  ?  762 HOH   B O      1 
HETATM 13343 O  O      . HOH   M 7 .   ? 42.809  -4.585  39.796 1.00 46.52  ?  763 HOH   B O      1 
HETATM 13344 O  O      . HOH   M 7 .   ? 10.941  -7.606  6.980  1.00 49.50  ?  764 HOH   B O      1 
HETATM 13345 O  O      . HOH   M 7 .   ? 21.584  -31.853 23.414 1.00 22.82  ?  765 HOH   B O      1 
HETATM 13346 O  O      . HOH   M 7 .   ? 39.371  -18.649 12.850 1.00 41.31  ?  766 HOH   B O      1 
HETATM 13347 O  O      . HOH   M 7 .   ? 31.483  -4.570  28.270 1.00 24.52  ?  767 HOH   B O      1 
HETATM 13348 O  O      . HOH   M 7 .   ? 17.176  -3.398  23.330 1.00 47.23  ?  768 HOH   B O      1 
HETATM 13349 O  O      . HOH   M 7 .   ? 19.595  -17.772 8.724  1.00 42.64  ?  769 HOH   B O      1 
HETATM 13350 O  O      . HOH   M 7 .   ? 17.755  -16.356 40.751 1.00 48.44  ?  770 HOH   B O      1 
HETATM 13351 O  O      . HOH   M 7 .   ? 34.300  -37.037 47.333 1.00 38.51  ?  771 HOH   B O      1 
HETATM 13352 O  O      . HOH   M 7 .   ? 25.994  -20.616 27.331 1.00 26.36  ?  772 HOH   B O      1 
HETATM 13353 O  O      . HOH   M 7 .   ? 28.960  -1.824  12.859 1.00 57.27  ?  773 HOH   B O      1 
HETATM 13354 O  O      . HOH   M 7 .   ? 43.337  -15.855 42.220 1.00 37.16  ?  774 HOH   B O      1 
HETATM 13355 O  O      . HOH   M 7 .   ? 25.810  -20.031 5.529  1.00 54.58  ?  775 HOH   B O      1 
HETATM 13356 O  O      . HOH   M 7 .   ? 51.681  -21.553 30.353 1.00 51.07  ?  776 HOH   B O      1 
HETATM 13357 O  O      . HOH   M 7 .   ? 32.978  -30.759 28.507 1.00 34.13  ?  777 HOH   B O      1 
HETATM 13358 O  O      . HOH   M 7 .   ? 20.215  -32.147 15.582 1.00 28.33  ?  778 HOH   B O      1 
HETATM 13359 O  O      . HOH   M 7 .   ? 31.206  -37.871 51.021 1.00 54.32  ?  779 HOH   B O      1 
HETATM 13360 O  O      . HOH   M 7 .   ? 21.767  -4.358  17.601 1.00 34.65  ?  780 HOH   B O      1 
HETATM 13361 O  O      . HOH   M 7 .   ? 22.360  -13.580 36.223 1.00 37.59  ?  781 HOH   B O      1 
HETATM 13362 O  O      . HOH   M 7 .   ? 26.930  -29.771 21.099 1.00 28.99  ?  782 HOH   B O      1 
HETATM 13363 O  O      . HOH   M 7 .   ? 10.552  -32.888 32.929 1.00 49.63  ?  783 HOH   B O      1 
HETATM 13364 O  O      . HOH   M 7 .   ? 22.543  -2.846  19.531 1.00 48.46  ?  784 HOH   B O      1 
HETATM 13365 O  O      . HOH   M 7 .   ? 13.579  -14.694 8.451  1.00 50.07  ?  785 HOH   B O      1 
HETATM 13366 O  O      . HOH   M 7 .   ? 28.617  -16.542 31.450 1.00 23.47  ?  786 HOH   B O      1 
HETATM 13367 O  O      . HOH   M 7 .   ? 14.792  -22.097 44.933 1.00 56.39  ?  787 HOH   B O      1 
HETATM 13368 O  O      . HOH   M 7 .   ? 15.012  -25.349 51.089 1.00 44.03  ?  788 HOH   B O      1 
HETATM 13369 O  O      . HOH   M 7 .   ? 31.687  -22.332 18.080 1.00 27.95  ?  789 HOH   B O      1 
HETATM 13370 O  O      . HOH   M 7 .   ? 17.241  -9.744  6.955  1.00 42.86  ?  790 HOH   B O      1 
HETATM 13371 O  O      . HOH   M 7 .   ? 15.902  -27.634 25.755 1.00 41.49  ?  791 HOH   B O      1 
HETATM 13372 O  O      . HOH   M 7 .   ? 21.360  -41.366 24.177 1.00 42.22  ?  792 HOH   B O      1 
HETATM 13373 O  O      . HOH   M 7 .   ? 30.594  -32.962 38.247 1.00 29.06  ?  793 HOH   B O      1 
HETATM 13374 O  O      . HOH   M 7 .   ? 23.068  -41.283 39.093 1.00 39.29  ?  794 HOH   B O      1 
HETATM 13375 O  O      . HOH   M 7 .   ? 34.332  -32.614 53.144 1.00 42.37  ?  795 HOH   B O      1 
HETATM 13376 O  O      . HOH   M 7 .   ? -3.088  3.311   5.929  1.00 50.52  ?  796 HOH   B O      1 
HETATM 13377 O  O      . HOH   M 7 .   ? 33.980  -23.100 19.663 1.00 28.40  ?  797 HOH   B O      1 
HETATM 13378 O  O      . HOH   M 7 .   ? 23.353  -40.337 43.861 1.00 36.84  ?  798 HOH   B O      1 
HETATM 13379 O  O      . HOH   M 7 .   ? 30.754  -32.574 -0.504 1.00 43.35  ?  799 HOH   B O      1 
HETATM 13380 O  O      . HOH   M 7 .   ? 32.487  -32.520 33.860 1.00 59.12  ?  800 HOH   B O      1 
HETATM 13381 O  O      . HOH   M 7 .   ? 25.676  -5.814  42.679 1.00 36.73  ?  801 HOH   B O      1 
HETATM 13382 O  O      . HOH   M 7 .   ? 30.819  -33.957 35.917 1.00 37.42  ?  802 HOH   B O      1 
HETATM 13383 O  O      . HOH   M 7 .   ? 22.057  -16.942 42.251 1.00 40.51  ?  803 HOH   B O      1 
HETATM 13384 O  O      . HOH   M 7 .   ? 35.391  -4.254  14.943 1.00 54.01  ?  804 HOH   B O      1 
HETATM 13385 O  O      . HOH   M 7 .   ? 36.866  -1.340  32.608 1.00 33.39  ?  805 HOH   B O      1 
HETATM 13386 O  O      . HOH   M 7 .   ? 12.651  -21.230 37.816 1.00 42.84  ?  806 HOH   B O      1 
HETATM 13387 O  O      . HOH   M 7 .   ? 26.805  -36.007 25.598 1.00 27.10  ?  807 HOH   B O      1 
HETATM 13388 O  O      . HOH   M 7 .   ? 38.207  -32.474 49.700 1.00 63.25  ?  808 HOH   B O      1 
HETATM 13389 O  O      . HOH   M 7 .   ? 19.910  -34.018 22.219 1.00 30.66  ?  809 HOH   B O      1 
HETATM 13390 O  O      . HOH   M 7 .   ? 38.072  -32.369 -3.380 1.00 56.27  ?  810 HOH   B O      1 
HETATM 13391 O  O      . HOH   M 7 .   ? 33.675  -3.034  44.516 1.00 49.79  ?  811 HOH   B O      1 
HETATM 13392 O  O      . HOH   M 7 .   ? 40.413  -0.301  30.537 1.00 39.66  ?  812 HOH   B O      1 
HETATM 13393 O  O      . HOH   M 7 .   ? 28.817  -38.417 31.713 1.00 39.23  ?  813 HOH   B O      1 
HETATM 13394 O  O      . HOH   M 7 .   ? 37.106  -10.764 46.797 1.00 41.06  ?  814 HOH   B O      1 
HETATM 13395 O  O      . HOH   M 7 .   ? 10.971  -30.222 33.337 1.00 24.12  ?  815 HOH   B O      1 
HETATM 13396 O  O      . HOH   M 7 .   ? 12.674  -15.095 22.458 1.00 37.26  ?  816 HOH   B O      1 
HETATM 13397 O  O      . HOH   M 7 .   ? 33.881  -2.677  16.568 1.00 47.39  ?  817 HOH   B O      1 
HETATM 13398 O  O      . HOH   M 7 .   ? 30.963  -30.259 19.531 1.00 34.07  ?  818 HOH   B O      1 
HETATM 13399 O  O      . HOH   M 7 .   ? 21.203  -9.245  30.679 1.00 30.19  ?  819 HOH   B O      1 
HETATM 13400 O  O      . HOH   M 7 .   ? 40.778  -30.217 42.557 1.00 40.22  ?  820 HOH   B O      1 
HETATM 13401 O  O      . HOH   M 7 .   ? 27.893  -38.852 29.015 1.00 56.19  ?  821 HOH   B O      1 
HETATM 13402 O  O      . HOH   M 7 .   ? 34.597  -32.269 30.181 1.00 32.58  ?  822 HOH   B O      1 
HETATM 13403 O  O      . HOH   M 7 .   ? 16.502  -13.928 8.663  1.00 43.67  ?  823 HOH   B O      1 
HETATM 13404 O  O      . HOH   M 7 .   ? 25.927  -42.492 52.529 1.00 44.70  ?  824 HOH   B O      1 
HETATM 13405 O  O      . HOH   M 7 .   ? 25.447  -41.422 43.082 1.00 40.51  ?  825 HOH   B O      1 
HETATM 13406 O  O      . HOH   M 7 .   ? 24.278  -16.332 44.251 1.00 26.66  ?  826 HOH   B O      1 
HETATM 13407 O  O      . HOH   M 7 .   ? 11.035  -34.381 39.473 1.00 27.76  ?  827 HOH   B O      1 
HETATM 13408 O  O      . HOH   M 7 .   ? 41.883  -4.282  28.730 1.00 43.10  ?  828 HOH   B O      1 
HETATM 13409 O  O      . HOH   M 7 .   ? 14.490  -33.332 15.433 1.00 54.64  ?  829 HOH   B O      1 
HETATM 13410 O  O      . HOH   M 7 .   ? 34.917  1.090   26.314 1.00 52.02  ?  830 HOH   B O      1 
HETATM 13411 O  O      . HOH   M 7 .   ? 30.307  -14.383 52.216 1.00 36.24  ?  831 HOH   B O      1 
HETATM 13412 O  O      . HOH   M 7 .   ? 14.545  -29.299 41.993 1.00 41.03  ?  832 HOH   B O      1 
HETATM 13413 O  O      . HOH   M 7 .   ? 30.007  -42.491 39.043 1.00 40.04  ?  833 HOH   B O      1 
HETATM 13414 O  O      . HOH   M 7 .   ? 32.849  -34.119 31.659 1.00 55.72  ?  834 HOH   B O      1 
HETATM 13415 O  O      . HOH   M 7 .   ? 47.063  -19.544 21.846 1.00 53.96  ?  835 HOH   B O      1 
HETATM 13416 O  O      . HOH   M 7 .   ? 23.207  -10.587 36.424 1.00 29.14  ?  836 HOH   B O      1 
HETATM 13417 O  O      . HOH   M 7 .   ? 52.332  -15.991 25.099 1.00 45.36  ?  837 HOH   B O      1 
HETATM 13418 O  O      . HOH   M 7 .   ? 41.351  -24.021 4.293  1.00 57.05  ?  838 HOH   B O      1 
HETATM 13419 O  O      . HOH   M 7 .   ? 11.291  -33.383 30.334 1.00 49.94  ?  839 HOH   B O      1 
HETATM 13420 O  O      . HOH   M 7 .   ? 26.384  -12.347 30.021 1.00 29.10  ?  840 HOH   B O      1 
HETATM 13421 O  O      . HOH   M 7 .   ? 28.784  -41.782 53.890 1.00 48.04  ?  841 HOH   B O      1 
HETATM 13422 O  O      . HOH   M 7 .   ? 24.635  -6.151  6.604  1.00 62.64  ?  842 HOH   B O      1 
HETATM 13423 O  O      . HOH   M 7 .   ? 50.585  -12.452 29.062 1.00 25.49  ?  843 HOH   B O      1 
HETATM 13424 O  O      . HOH   M 7 .   ? 21.735  -13.356 38.962 1.00 49.70  ?  844 HOH   B O      1 
HETATM 13425 O  O      . HOH   M 7 .   ? 46.433  -11.842 29.886 1.00 46.82  ?  845 HOH   B O      1 
HETATM 13426 O  O      . HOH   M 7 .   ? 18.429  -1.696  24.820 1.00 36.60  ?  846 HOH   B O      1 
HETATM 13427 O  O      . HOH   M 7 .   ? 48.557  -14.505 23.290 1.00 52.86  ?  847 HOH   B O      1 
HETATM 13428 O  O      . HOH   M 7 .   ? 27.713  -34.034 20.658 1.00 33.10  ?  848 HOH   B O      1 
HETATM 13429 O  O      . HOH   M 7 .   ? 15.415  -32.797 49.662 1.00 46.31  ?  849 HOH   B O      1 
HETATM 13430 O  O      . HOH   M 7 .   ? 28.233  -14.563 29.553 1.00 29.98  ?  850 HOH   B O      1 
HETATM 13431 O  O      . HOH   M 7 .   ? 14.389  -30.131 44.448 1.00 47.08  ?  851 HOH   B O      1 
HETATM 13432 O  O      . HOH   M 7 .   ? 48.719  -17.314 22.258 1.00 52.89  ?  852 HOH   B O      1 
HETATM 13433 O  O      . HOH   M 7 .   ? 20.062  -14.938 40.992 1.00 51.69  ?  853 HOH   B O      1 
HETATM 13434 O  O      . HOH   M 7 .   ? 17.039  -40.214 37.925 1.00 50.75  ?  854 HOH   B O      1 
HETATM 13435 O  O      . HOH   M 7 .   ? 14.077  -12.999 57.761 1.00 57.43  ?  855 HOH   B O      1 
HETATM 13436 O  O      . HOH   M 7 .   ? 34.985  -35.114 29.931 1.00 52.38  ?  856 HOH   B O      1 
HETATM 13437 O  O      . HOH   M 7 .   ? 9.631   -23.558 34.965 1.00 37.96  ?  857 HOH   B O      1 
HETATM 13438 O  O      . HOH   M 7 .   ? 47.208  -13.435 41.318 1.00 51.05  ?  858 HOH   B O      1 
HETATM 13439 O  O      . HOH   M 7 .   ? 15.564  -8.490  4.627  1.00 61.31  ?  859 HOH   B O      1 
HETATM 13440 O  O      . HOH   M 7 .   ? 13.726  -23.307 37.919 1.00 42.25  ?  860 HOH   B O      1 
HETATM 13441 O  O      . HOH   M 7 .   ? 18.229  -2.820  14.436 1.00 41.98  ?  861 HOH   B O      1 
HETATM 13442 O  O      . HOH   M 7 .   ? 27.654  -35.720 23.030 1.00 40.69  ?  862 HOH   B O      1 
HETATM 13443 O  O      . HOH   M 7 .   ? 21.322  -2.787  15.355 1.00 53.01  ?  863 HOH   B O      1 
HETATM 13444 O  O      . HOH   M 7 .   ? 32.684  -34.737 53.982 1.00 56.87  ?  864 HOH   B O      1 
HETATM 13445 O  O      . HOH   M 7 .   ? 17.340  -12.304 6.461  1.00 44.92  ?  865 HOH   B O      1 
HETATM 13446 O  O      . HOH   M 7 .   ? 51.881  -18.812 23.152 1.00 48.20  ?  866 HOH   B O      1 
HETATM 13447 O  O      . HOH   M 7 .   ? 32.804  -38.346 28.227 1.00 52.54  ?  867 HOH   B O      1 
HETATM 13448 O  O      . HOH   M 7 .   ? 8.149   -33.097 39.014 1.00 54.57  ?  868 HOH   B O      1 
HETATM 13449 O  O      . HOH   M 7 .   ? 13.641  -23.983 46.366 1.00 56.09  ?  869 HOH   B O      1 
HETATM 13450 O  O      . HOH   M 7 .   ? 28.860  -31.454 20.042 1.00 42.63  ?  870 HOH   B O      1 
HETATM 13451 O  O      . HOH   M 7 .   ? 23.807  -10.335 39.975 1.00 47.46  ?  871 HOH   B O      1 
HETATM 13452 O  O      . HOH   M 7 .   ? 16.545  -35.704 47.177 1.00 55.18  ?  872 HOH   B O      1 
HETATM 13453 O  O      . HOH   M 7 .   ? 21.367  -10.046 48.481 1.00 46.32  ?  873 HOH   B O      1 
HETATM 13454 O  O      . HOH   M 7 .   ? 24.356  -42.424 28.499 1.00 55.96  ?  874 HOH   B O      1 
HETATM 13455 O  O      . HOH   M 7 .   ? 23.252  -12.637 40.764 1.00 37.05  ?  875 HOH   B O      1 
HETATM 13456 O  O      . HOH   M 7 .   ? 18.075  -15.479 48.357 1.00 52.79  ?  876 HOH   B O      1 
HETATM 13457 O  O      . HOH   M 7 .   ? 44.648  -10.449 29.897 1.00 58.03  ?  877 HOH   B O      1 
HETATM 13458 O  O      . HOH   M 7 .   ? 19.457  -20.586 43.449 1.00 37.89  ?  878 HOH   B O      1 
HETATM 13459 O  O      . HOH   M 7 .   ? 6.345   2.518   5.634  1.00 59.02  ?  879 HOH   B O      1 
HETATM 13460 O  O      . HOH   M 7 .   ? 43.033  -5.881  30.897 1.00 39.10  ?  880 HOH   B O      1 
HETATM 13461 O  O      . HOH   M 7 .   ? 11.440  -33.271 42.051 1.00 51.82  ?  881 HOH   B O      1 
HETATM 13462 O  O      . HOH   M 7 .   ? 44.270  -18.934 44.352 1.00 52.93  ?  882 HOH   B O      1 
HETATM 13463 O  O      . HOH   M 7 .   ? 15.930  -34.518 51.143 1.00 57.96  ?  883 HOH   B O      1 
HETATM 13464 O  O      . HOH   M 7 .   ? 33.746  1.715   32.954 1.00 46.63  ?  884 HOH   B O      1 
HETATM 13465 O  O      . HOH   M 7 .   ? 20.146  -1.945  20.297 1.00 60.92  ?  885 HOH   B O      1 
HETATM 13466 O  O      . HOH   M 7 .   ? 26.390  -42.254 49.493 1.00 47.69  ?  886 HOH   B O      1 
HETATM 13467 O  O      . HOH   M 7 .   ? 38.707  -8.218  47.503 1.00 54.11  ?  887 HOH   B O      1 
HETATM 13468 O  O      . HOH   M 7 .   ? 34.378  -29.770 58.132 1.00 58.65  ?  888 HOH   B O      1 
HETATM 13469 O  O      . HOH   M 7 .   ? 24.206  -7.554  42.790 1.00 64.76  ?  889 HOH   B O      1 
HETATM 13470 O  O      . HOH   M 7 .   ? 45.427  -20.471 18.863 1.00 58.25  ?  890 HOH   B O      1 
HETATM 13471 O  O      . HOH   M 7 .   ? 18.564  -4.969  10.658 1.00 51.02  ?  891 HOH   B O      1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1     N  N     . ALA   A 3   ? 1.0346 0.5317 0.6705 -0.0538 0.1515  -0.0793 28  ALA   A N     
2     C  CA    . ALA   A 3   ? 1.0269 0.5001 0.6596 -0.0334 0.1401  -0.0878 28  ALA   A CA    
3     C  C     . ALA   A 3   ? 1.0089 0.4326 0.6326 -0.0036 0.1556  -0.1241 28  ALA   A C     
4     O  O     . ALA   A 3   ? 1.0091 0.4158 0.6382 0.0248  0.1624  -0.1358 28  ALA   A O     
5     C  CB    . ALA   A 3   ? 1.0282 0.5267 0.6666 -0.0246 0.1236  -0.0735 28  ALA   A CB    
10    N  N     . SER   A 4   ? 0.9874 0.3707 0.5913 0.0092  0.1727  -0.1506 29  SER   A N     
11    C  CA    . SER   A 4   ? 0.9412 0.3487 0.5529 0.0068  0.1842  -0.1501 29  SER   A CA    
12    C  C     . SER   A 4   ? 0.9359 0.3373 0.5108 -0.0024 0.2013  -0.1269 29  SER   A C     
13    O  O     . SER   A 4   ? 0.9560 0.3344 0.4976 -0.0091 0.1913  -0.1218 29  SER   A O     
14    C  CB    . SER   A 4   ? 0.9504 0.3589 0.5628 0.0078  0.1909  -0.1561 29  SER   A CB    
15    O  OG    . SER   A 4   ? 0.9798 0.3516 0.5697 -0.0404 0.1778  -0.1571 29  SER   A OG    
21    N  N     . VAL   A 5   ? 0.9244 0.3183 0.4874 -0.0436 0.2150  -0.1117 30  VAL   A N     
22    C  CA    . VAL   A 5   ? 0.9386 0.3376 0.4647 -0.0317 0.2356  -0.0844 30  VAL   A CA    
23    C  C     . VAL   A 5   ? 0.9369 0.3244 0.4295 -0.0504 0.2083  -0.0956 30  VAL   A C     
24    O  O     . VAL   A 5   ? 0.8784 0.3230 0.4065 -0.0358 0.2080  -0.0990 30  VAL   A O     
25    C  CB    . VAL   A 5   ? 0.9576 0.3916 0.4814 -0.0266 0.2558  -0.0536 30  VAL   A CB    
26    C  CG1   . VAL   A 5   ? 0.9624 0.3658 0.4807 -0.0235 0.2601  -0.0596 30  VAL   A CG1   
27    C  CG2   . VAL   A 5   ? 0.9663 0.4253 0.4917 -0.0075 0.2515  -0.0415 30  VAL   A CG2   
37    N  N     . GLU   A 6   ? 0.9405 0.3228 0.4259 -0.0818 0.1572  -0.1110 31  GLU   A N     
38    C  CA    . GLU   A 6   ? 0.9456 0.3373 0.4194 -0.1157 0.1298  -0.1185 31  GLU   A CA    
39    C  C     . GLU   A 6   ? 0.9361 0.3310 0.4150 -0.0965 0.0800  -0.1212 31  GLU   A C     
40    O  O     . GLU   A 6   ? 0.9503 0.3479 0.4279 -0.0844 0.0552  -0.1225 31  GLU   A O     
41    C  CB    . GLU   A 6   ? 0.9909 0.3541 0.4205 -0.1582 0.1564  -0.1094 31  GLU   A CB    
42    C  CG    . GLU   A 6   ? 1.0213 0.3792 0.4328 -0.1621 0.1834  -0.1065 31  GLU   A CG    
43    C  CD    . GLU   A 6   ? 1.0345 0.3826 0.4344 -0.1304 0.2067  -0.1199 31  GLU   A CD    
44    O  OE1   . GLU   A 6   ? 1.0506 0.3785 0.4413 -0.0853 0.1910  -0.1201 31  GLU   A OE1   
45    O  OE2   . GLU   A 6   ? 1.0185 0.3956 0.4264 -0.1578 0.2386  -0.1179 31  GLU   A OE2   
52    N  N     . ARG   A 7   ? 0.9084 0.3047 0.4023 -0.1053 0.0695  -0.1021 32  ARG   A N     
53    C  CA    . ARG   A 7   ? 0.9041 0.3067 0.4189 -0.0813 0.0520  -0.0781 32  ARG   A CA    
54    C  C     . ARG   A 7   ? 0.8537 0.2868 0.3883 -0.0587 0.0581  -0.0799 32  ARG   A C     
55    O  O     . ARG   A 7   ? 0.8281 0.2922 0.3901 -0.0614 0.0606  -0.0954 32  ARG   A O     
56    C  CB    . ARG   A 7   ? 0.9350 0.3351 0.4577 -0.0779 0.0342  -0.0574 32  ARG   A CB    
57    C  CG    . ARG   A 7   ? 0.9700 0.4121 0.4998 -0.0791 0.0027  -0.0383 32  ARG   A CG    
58    C  CD    . ARG   A 7   ? 1.0085 0.4975 0.5406 -0.0707 -0.0197 -0.0278 32  ARG   A CD    
59    N  NE    . ARG   A 7   ? 1.0383 0.5714 0.5802 -0.0823 -0.0350 -0.0237 32  ARG   A NE    
60    C  CZ    . ARG   A 7   ? 1.0490 0.6337 0.6151 -0.0860 -0.0381 -0.0177 32  ARG   A CZ    
61    N  NH1   . ARG   A 7   ? 1.0565 0.6506 0.6282 -0.0843 -0.0290 -0.0243 32  ARG   A NH1   
62    N  NH2   . ARG   A 7   ? 1.0392 0.6507 0.6255 -0.0859 -0.0492 -0.0053 32  ARG   A NH2   
76    N  N     . ILE   A 8   ? 0.8153 0.2487 0.3639 -0.0484 0.0777  -0.0652 33  ILE   A N     
77    C  CA    . ILE   A 8   ? 0.7863 0.2257 0.3479 -0.0124 0.0850  -0.0582 33  ILE   A CA    
78    C  C     . ILE   A 8   ? 0.7338 0.2244 0.3209 0.0001  0.1035  -0.0612 33  ILE   A C     
79    O  O     . ILE   A 8   ? 0.7231 0.2453 0.3005 -0.0540 0.1100  -0.0662 33  ILE   A O     
80    C  CB    . ILE   A 8   ? 0.7840 0.2324 0.3696 0.0260  0.0671  -0.0686 33  ILE   A CB    
81    C  CG1   . ILE   A 8   ? 0.8584 0.2693 0.4020 0.0569  0.0462  -0.0742 33  ILE   A CG1   
82    C  CG2   . ILE   A 8   ? 0.7598 0.2455 0.3613 0.0444  0.0850  -0.0776 33  ILE   A CG2   
83    C  CD1   . ILE   A 8   ? 0.8914 0.2975 0.4199 0.0655  0.0562  -0.0789 33  ILE   A CD1   
95    N  N     . TYR   A 9   ? 0.6995 0.2134 0.3088 -0.0033 0.1117  -0.0559 34  TYR   A N     
96    C  CA    . TYR   A 9   ? 0.6802 0.2333 0.3025 -0.0123 0.1556  -0.0609 34  TYR   A CA    
97    C  C     . TYR   A 9   ? 0.6506 0.2525 0.2853 -0.0547 0.1633  -0.0733 34  TYR   A C     
98    O  O     . TYR   A 9   ? 0.6891 0.2993 0.2873 -0.0627 0.1460  -0.0934 34  TYR   A O     
99    C  CB    . TYR   A 9   ? 0.6559 0.2374 0.3124 -0.0173 0.1768  -0.0634 34  TYR   A CB    
100   C  CG    . TYR   A 9   ? 0.6749 0.2577 0.3293 -0.0059 0.1801  -0.0729 34  TYR   A CG    
101   C  CD1   . TYR   A 9   ? 0.6402 0.2607 0.3273 -0.0149 0.1953  -0.0723 34  TYR   A CD1   
102   C  CD2   . TYR   A 9   ? 0.6935 0.2842 0.3457 0.0133  0.1838  -0.0808 34  TYR   A CD2   
103   C  CE1   . TYR   A 9   ? 0.6141 0.2788 0.3435 -0.0137 0.1931  -0.0921 34  TYR   A CE1   
104   C  CE2   . TYR   A 9   ? 0.6735 0.3039 0.3570 0.0253  0.1772  -0.0987 34  TYR   A CE2   
105   C  CZ    . TYR   A 9   ? 0.6685 0.3169 0.3616 0.0106  0.1854  -0.1046 34  TYR   A CZ    
106   O  OH    . TYR   A 9   ? 0.6667 0.3407 0.3705 0.0116  0.1749  -0.1290 34  TYR   A OH    
116   N  N     . GLN   A 10  ? 0.6213 0.2247 0.2883 -0.0513 0.1291  -0.0774 35  GLN   A N     
117   C  CA    . GLN   A 10  ? 0.6485 0.1980 0.2886 -0.0541 0.1114  -0.0523 35  GLN   A CA    
118   C  C     . GLN   A 10  ? 0.6379 0.2096 0.2550 -0.0578 0.0873  -0.0442 35  GLN   A C     
119   O  O     . GLN   A 10  ? 0.6334 0.2060 0.2439 -0.0625 0.0488  -0.0573 35  GLN   A O     
120   C  CB    . GLN   A 10  ? 0.6632 0.1996 0.3379 -0.0491 0.0871  -0.0278 35  GLN   A CB    
121   C  CG    . GLN   A 10  ? 0.6607 0.2108 0.4054 -0.0636 0.0897  -0.0212 35  GLN   A CG    
122   C  CD    . GLN   A 10  ? 0.6790 0.2633 0.4779 -0.0394 0.1057  -0.0164 35  GLN   A CD    
123   O  OE1   . GLN   A 10  ? 0.6787 0.2974 0.5204 -0.0475 0.1278  -0.0023 35  GLN   A OE1   
124   N  NE2   . GLN   A 10  ? 0.6932 0.2476 0.4918 -0.0665 0.0917  -0.0310 35  GLN   A NE2   
133   N  N     . LYS   A 11  ? 0.6522 0.2306 0.2379 -0.0464 0.0701  -0.0286 36  LYS   A N     
134   C  CA    . LYS   A 11  ? 0.6853 0.2415 0.2387 -0.0255 0.0431  -0.0093 36  LYS   A CA    
135   C  C     . LYS   A 11  ? 0.6877 0.2564 0.2495 0.0029  0.0234  -0.0240 36  LYS   A C     
136   O  O     . LYS   A 11  ? 0.6741 0.3096 0.2831 0.0059  0.0258  -0.0303 36  LYS   A O     
137   C  CB    . LYS   A 11  ? 0.7393 0.2647 0.2481 -0.0215 0.0421  0.0247  36  LYS   A CB    
138   C  CG    . LYS   A 11  ? 0.7908 0.3055 0.2667 -0.0008 0.0479  0.0714  36  LYS   A CG    
139   C  CD    . LYS   A 11  ? 0.8425 0.3510 0.3183 -0.0087 0.0502  0.0777  36  LYS   A CD    
140   C  CE    . LYS   A 11  ? 0.8844 0.3930 0.3371 0.0143  0.0360  0.0798  36  LYS   A CE    
141   N  NZ    . LYS   A 11  ? 0.9068 0.4319 0.3355 0.0167  0.0304  0.0633  36  LYS   A NZ    
155   N  N     . LYS   A 12  ? 0.6817 0.2311 0.2221 0.0028  0.0182  -0.0280 37  LYS   A N     
156   C  CA    . LYS   A 12  ? 0.6961 0.2456 0.2215 -0.0194 0.0052  -0.0247 37  LYS   A CA    
157   C  C     . LYS   A 12  ? 0.6957 0.2633 0.2359 0.0079  0.0197  -0.0136 37  LYS   A C     
158   O  O     . LYS   A 12  ? 0.6929 0.2789 0.2638 0.0130  0.0096  -0.0020 37  LYS   A O     
159   C  CB    . LYS   A 12  ? 0.6949 0.2437 0.2233 -0.0327 -0.0058 -0.0278 37  LYS   A CB    
160   C  CG    . LYS   A 12  ? 0.6871 0.2470 0.2445 -0.0026 0.0052  -0.0253 37  LYS   A CG    
161   C  CD    . LYS   A 12  ? 0.7160 0.2662 0.2797 -0.0110 0.0107  -0.0058 37  LYS   A CD    
162   C  CE    . LYS   A 12  ? 0.7481 0.2864 0.3136 -0.0184 -0.0021 -0.0082 37  LYS   A CE    
163   N  NZ    . LYS   A 12  ? 0.7622 0.2967 0.3381 -0.0249 -0.0024 -0.0203 37  LYS   A NZ    
177   N  N     . THR   A 13  ? 0.6970 0.2671 0.2154 0.0057  0.0106  -0.0159 38  THR   A N     
178   C  CA    . THR   A 13  ? 0.7159 0.2758 0.2095 0.0152  -0.0079 -0.0213 38  THR   A CA    
179   C  C     . THR   A 13  ? 0.6925 0.2488 0.2113 0.0141  0.0031  -0.0268 38  THR   A C     
180   O  O     . THR   A 13  ? 0.6414 0.2515 0.2031 -0.0015 -0.0103 -0.0211 38  THR   A O     
181   C  CB    . THR   A 13  ? 0.7430 0.3223 0.2028 0.0030  -0.0457 -0.0317 38  THR   A CB    
182   O  OG1   . THR   A 13  ? 0.7415 0.3225 0.2229 -0.0051 -0.0974 -0.0155 38  THR   A OG1   
183   C  CG2   . THR   A 13  ? 0.8028 0.3764 0.2127 0.0179  -0.0299 -0.0406 38  THR   A CG2   
191   N  N     . GLN   A 14  ? 0.7162 0.2620 0.2431 0.0068  0.0087  -0.0035 39  GLN   A N     
192   C  CA    . GLN   A 14  ? 0.6998 0.2616 0.2567 0.0222  0.0111  0.0029  39  GLN   A CA    
193   C  C     . GLN   A 14  ? 0.6267 0.2652 0.2433 0.0208  -0.0416 0.0028  39  GLN   A C     
194   O  O     . GLN   A 14  ? 0.5738 0.2751 0.2421 -0.0103 -0.0743 -0.0200 39  GLN   A O     
195   C  CB    . GLN   A 14  ? 0.7608 0.2882 0.2917 0.0257  0.0279  0.0022  39  GLN   A CB    
196   C  CG    . GLN   A 14  ? 0.8292 0.3342 0.3343 0.0007  0.0265  -0.0087 39  GLN   A CG    
197   C  CD    . GLN   A 14  ? 0.9008 0.3771 0.3752 -0.0075 0.0364  -0.0228 39  GLN   A CD    
198   O  OE1   . GLN   A 14  ? 0.9419 0.4132 0.4281 -0.0137 0.0456  -0.0541 39  GLN   A OE1   
199   N  NE2   . GLN   A 14  ? 0.9177 0.3906 0.3501 0.0025  0.0439  0.0057  39  GLN   A NE2   
208   N  N     . LEU   A 15  ? 0.5911 0.2727 0.2277 0.0224  -0.0769 -0.0006 40  LEU   A N     
209   C  CA    . LEU   A 15  ? 0.5624 0.2925 0.2433 0.0421  -0.1219 -0.0120 40  LEU   A CA    
210   C  C     . LEU   A 15  ? 0.5376 0.2673 0.2546 0.0131  -0.1110 -0.0175 40  LEU   A C     
211   O  O     . LEU   A 15  ? 0.4924 0.2722 0.2482 0.0135  -0.1158 -0.0199 40  LEU   A O     
212   C  CB    . LEU   A 15  ? 0.6046 0.3669 0.2725 0.0401  -0.1506 -0.0333 40  LEU   A CB    
213   C  CG    . LEU   A 15  ? 0.6238 0.4307 0.3035 0.0240  -0.1719 -0.0621 40  LEU   A CG    
214   C  CD1   . LEU   A 15  ? 0.6321 0.4243 0.3258 0.0327  -0.1502 -0.0704 40  LEU   A CD1   
215   C  CD2   . LEU   A 15  ? 0.6690 0.4810 0.3189 0.0197  -0.1703 -0.0461 40  LEU   A CD2   
227   N  N     . GLU   A 16  ? 0.5531 0.2350 0.2492 0.0055  -0.1075 -0.0229 41  GLU   A N     
228   C  CA    . GLU   A 16  ? 0.5263 0.2309 0.2423 -0.0021 -0.0988 -0.0330 41  GLU   A CA    
229   C  C     . GLU   A 16  ? 0.4635 0.2346 0.2319 -0.0224 -0.0674 -0.0178 41  GLU   A C     
230   O  O     . GLU   A 16  ? 0.4351 0.2239 0.2449 -0.0277 -0.0683 -0.0041 41  GLU   A O     
231   C  CB    . GLU   A 16  ? 0.5935 0.2714 0.2449 0.0228  -0.0913 -0.0689 41  GLU   A CB    
232   C  CG    . GLU   A 16  ? 0.6660 0.3224 0.2630 0.0040  -0.0954 -0.0783 41  GLU   A CG    
233   C  CD    . GLU   A 16  ? 0.7296 0.3505 0.2870 -0.0101 -0.0874 -0.1007 41  GLU   A CD    
234   O  OE1   . GLU   A 16  ? 0.7437 0.3268 0.2705 0.0082  -0.0992 -0.0901 41  GLU   A OE1   
235   O  OE2   . GLU   A 16  ? 0.7822 0.4124 0.3243 -0.0438 -0.0624 -0.1156 41  GLU   A OE2   
242   N  N     . HIS   A 17  ? 0.4616 0.2510 0.2305 -0.0179 -0.0446 -0.0179 42  HIS   A N     
243   C  CA    . HIS   A 17  ? 0.4020 0.2396 0.2175 -0.0199 -0.0264 -0.0091 42  HIS   A CA    
244   C  C     . HIS   A 17  ? 0.3904 0.2145 0.2177 -0.0117 -0.0452 -0.0135 42  HIS   A C     
245   O  O     . HIS   A 17  ? 0.3528 0.2213 0.2153 -0.0053 -0.0583 0.0137  42  HIS   A O     
246   C  CB    . HIS   A 17  ? 0.3675 0.2514 0.2209 0.0009  0.0014  -0.0127 42  HIS   A CB    
247   C  CG    . HIS   A 17  ? 0.4028 0.2463 0.2275 -0.0260 0.0012  -0.0169 42  HIS   A CG    
248   N  ND1   . HIS   A 17  ? 0.3875 0.2522 0.2294 -0.0436 0.0135  -0.0055 42  HIS   A ND1   
249   C  CD2   . HIS   A 17  ? 0.4102 0.2446 0.2435 -0.0094 -0.0158 -0.0219 42  HIS   A CD2   
250   C  CE1   . HIS   A 17  ? 0.3979 0.2421 0.2623 -0.0044 0.0234  -0.0379 42  HIS   A CE1   
251   N  NE2   . HIS   A 17  ? 0.3904 0.2442 0.2652 0.0064  0.0041  -0.0359 42  HIS   A NE2   
259   N  N     . ILE   A 18  ? 0.3845 0.2172 0.2212 0.0134  -0.0449 -0.0088 43  ILE   A N     
260   C  CA    . ILE   A 18  ? 0.3782 0.1904 0.2343 0.0248  -0.0458 -0.0108 43  ILE   A CA    
261   C  C     . ILE   A 18  ? 0.3567 0.1924 0.2374 0.0178  -0.0386 -0.0095 43  ILE   A C     
262   O  O     . ILE   A 18  ? 0.3392 0.1961 0.2446 -0.0012 -0.0567 -0.0019 43  ILE   A O     
263   C  CB    . ILE   A 18  ? 0.4130 0.1957 0.2322 0.0052  -0.0549 0.0439  43  ILE   A CB    
264   C  CG1   . ILE   A 18  ? 0.4263 0.1932 0.2334 -0.0016 -0.0585 0.0596  43  ILE   A CG1   
265   C  CG2   . ILE   A 18  ? 0.4284 0.2217 0.2335 -0.0378 -0.0836 0.0461  43  ILE   A CG2   
266   C  CD1   . ILE   A 18  ? 0.4400 0.2081 0.2338 0.0175  -0.0396 0.0500  43  ILE   A CD1   
278   N  N     . LEU   A 19  ? 0.3843 0.1972 0.2410 -0.0154 -0.0716 0.0042  44  LEU   A N     
279   C  CA    . LEU   A 19  ? 0.3538 0.1836 0.2656 -0.0264 -0.0692 0.0023  44  LEU   A CA    
280   C  C     . LEU   A 19  ? 0.3104 0.2111 0.2698 -0.0151 -0.0565 0.0190  44  LEU   A C     
281   O  O     . LEU   A 19  ? 0.3319 0.2328 0.2938 -0.0026 -0.0466 0.0144  44  LEU   A O     
282   C  CB    . LEU   A 19  ? 0.4016 0.2268 0.2997 -0.0396 -0.0583 0.0018  44  LEU   A CB    
283   C  CG    . LEU   A 19  ? 0.4088 0.2681 0.3222 -0.0593 -0.0936 -0.0304 44  LEU   A CG    
284   C  CD1   . LEU   A 19  ? 0.4821 0.3817 0.3379 -0.0628 -0.0824 -0.0464 44  LEU   A CD1   
285   C  CD2   . LEU   A 19  ? 0.4042 0.2724 0.3515 -0.0274 -0.1285 -0.0288 44  LEU   A CD2   
297   N  N     . LEU   A 20  ? 0.2967 0.2025 0.2659 -0.0229 -0.0232 0.0010  45  LEU   A N     
298   C  CA    . LEU   A 20  ? 0.3090 0.2329 0.2683 -0.0150 -0.0180 -0.0092 45  LEU   A CA    
299   C  C     . LEU   A 20  ? 0.3224 0.2078 0.2490 0.0036  0.0015  0.0160  45  LEU   A C     
300   O  O     . LEU   A 20  ? 0.3782 0.2255 0.2579 0.0449  -0.0157 0.0229  45  LEU   A O     
301   C  CB    . LEU   A 20  ? 0.3300 0.2592 0.2857 -0.0067 -0.0224 -0.0126 45  LEU   A CB    
302   C  CG    . LEU   A 20  ? 0.3881 0.2831 0.3281 0.0405  -0.0118 -0.0190 45  LEU   A CG    
303   C  CD1   . LEU   A 20  ? 0.4129 0.2908 0.3670 0.0424  -0.0174 -0.0226 45  LEU   A CD1   
304   C  CD2   . LEU   A 20  ? 0.4147 0.3287 0.3267 0.0547  -0.0016 -0.0124 45  LEU   A CD2   
316   N  N     . ARG   A 21  ? 0.3040 0.1847 0.2455 0.0058  -0.0100 0.0183  46  ARG   A N     
317   C  CA    . ARG   A 21  ? 0.3050 0.2163 0.2438 0.0031  -0.0137 0.0146  46  ARG   A CA    
318   C  C     . ARG   A 21  ? 0.2762 0.2079 0.2458 0.0055  -0.0299 0.0278  46  ARG   A C     
319   O  O     . ARG   A 21  ? 0.3157 0.2312 0.2674 0.0141  -0.0102 0.0197  46  ARG   A O     
320   C  CB    . ARG   A 21  ? 0.2808 0.2525 0.2412 0.0307  -0.0207 -0.0047 46  ARG   A CB    
321   C  CG    . ARG   A 21  ? 0.2872 0.2850 0.2562 0.0339  -0.0169 0.0001  46  ARG   A CG    
322   C  CD    . ARG   A 21  ? 0.3336 0.2731 0.2674 0.0219  -0.0050 0.0120  46  ARG   A CD    
323   N  NE    . ARG   A 21  ? 0.3412 0.3017 0.2695 0.0284  0.0144  0.0093  46  ARG   A NE    
324   C  CZ    . ARG   A 21  ? 0.3521 0.2798 0.2402 0.0937  0.0057  0.0070  46  ARG   A CZ    
325   N  NH1   . ARG   A 21  ? 0.3870 0.2813 0.2616 0.0880  -0.0057 0.0256  46  ARG   A NH1   
326   N  NH2   . ARG   A 21  ? 0.3882 0.3201 0.2207 0.1157  0.0233  -0.0084 46  ARG   A NH2   
340   N  N     . PRO   A 22  ? 0.2412 0.1891 0.2652 0.0107  -0.0237 0.0332  47  PRO   A N     
341   C  CA    . PRO   A 22  ? 0.2091 0.2043 0.2678 0.0118  -0.0213 0.0368  47  PRO   A CA    
342   C  C     . PRO   A 22  ? 0.1982 0.2114 0.2581 0.0354  -0.0279 0.0086  47  PRO   A C     
343   O  O     . PRO   A 22  ? 0.1924 0.1930 0.2595 0.0150  -0.0206 0.0263  47  PRO   A O     
344   C  CB    . PRO   A 22  ? 0.2410 0.1893 0.3091 0.0036  -0.0209 0.0363  47  PRO   A CB    
345   C  CG    . PRO   A 22  ? 0.3123 0.2236 0.3356 0.0147  0.0265  0.0188  47  PRO   A CG    
346   C  CD    . PRO   A 22  ? 0.2537 0.2027 0.2909 -0.0022 0.0155  0.0424  47  PRO   A CD    
354   N  N     . ASP   A 23  ? 0.2449 0.2289 0.2546 0.0492  -0.0342 -0.0033 48  ASP   A N     
355   C  CA    . ASP   A 23  ? 0.2148 0.2170 0.2333 0.0230  -0.0403 0.0056  48  ASP   A CA    
356   C  C     . ASP   A 23  ? 0.1869 0.2253 0.2383 -0.0039 -0.0170 -0.0036 48  ASP   A C     
357   O  O     . ASP   A 23  ? 0.2013 0.2090 0.2339 -0.0146 -0.0217 -0.0101 48  ASP   A O     
358   C  CB    . ASP   A 23  ? 0.2173 0.2274 0.2624 -0.0057 -0.0540 0.0097  48  ASP   A CB    
359   C  CG    . ASP   A 23  ? 0.2687 0.2430 0.2900 -0.0199 -0.0632 0.0132  48  ASP   A CG    
360   O  OD1   . ASP   A 23  ? 0.3177 0.2532 0.3217 0.0109  -0.0901 -0.0037 48  ASP   A OD1   
361   O  OD2   . ASP   A 23  ? 0.2289 0.2584 0.2913 0.0153  -0.0489 0.0363  48  ASP   A OD2   
366   N  N     . THR   A 24  ? 0.1997 0.2310 0.2393 0.0165  -0.0056 0.0047  49  THR   A N     
367   C  CA    . THR   A 24  ? 0.1715 0.2341 0.2655 0.0124  -0.0058 0.0069  49  THR   A CA    
368   C  C     . THR   A 24  ? 0.2070 0.2112 0.2800 -0.0207 -0.0375 0.0183  49  THR   A C     
369   O  O     . THR   A 24  ? 0.2397 0.2379 0.3159 -0.0417 -0.0598 0.0258  49  THR   A O     
370   C  CB    . THR   A 24  ? 0.2119 0.2880 0.2705 -0.0102 -0.0154 0.0065  49  THR   A CB    
371   O  OG1   . THR   A 24  ? 0.2809 0.3299 0.2711 -0.0023 -0.0070 0.0403  49  THR   A OG1   
372   C  CG2   . THR   A 24  ? 0.2702 0.2981 0.2817 -0.0241 -0.0190 -0.0135 49  THR   A CG2   
380   N  N     . TYR   A 25  ? 0.2117 0.1874 0.2685 -0.0028 -0.0340 0.0126  50  TYR   A N     
381   C  CA    . TYR   A 25  ? 0.2217 0.1895 0.2509 -0.0007 -0.0429 0.0014  50  TYR   A CA    
382   C  C     . TYR   A 25  ? 0.2324 0.1710 0.2408 0.0175  -0.0316 0.0164  50  TYR   A C     
383   O  O     . TYR   A 25  ? 0.2448 0.1668 0.2409 0.0183  -0.0180 0.0187  50  TYR   A O     
384   C  CB    . TYR   A 25  ? 0.2621 0.1858 0.2240 0.0045  -0.0502 0.0042  50  TYR   A CB    
385   C  CG    . TYR   A 25  ? 0.3027 0.1874 0.1953 -0.0099 -0.0393 0.0104  50  TYR   A CG    
386   C  CD1   . TYR   A 25  ? 0.3246 0.2127 0.1767 0.0083  -0.0188 0.0130  50  TYR   A CD1   
387   C  CD2   . TYR   A 25  ? 0.2974 0.2134 0.1926 -0.0165 -0.0234 0.0114  50  TYR   A CD2   
388   C  CE1   . TYR   A 25  ? 0.3503 0.2079 0.1820 0.0292  0.0071  0.0141  50  TYR   A CE1   
389   C  CE2   . TYR   A 25  ? 0.3179 0.2258 0.1894 -0.0079 -0.0121 0.0019  50  TYR   A CE2   
390   C  CZ    . TYR   A 25  ? 0.3647 0.2430 0.2025 0.0013  -0.0001 0.0031  50  TYR   A CZ    
391   O  OH    . TYR   A 25  ? 0.3981 0.2755 0.2275 0.0120  -0.0103 0.0034  50  TYR   A OH    
401   N  N     . ILE   A 26  ? 0.2106 0.1714 0.2327 0.0130  -0.0473 0.0059  51  ILE   A N     
402   C  CA    . ILE   A 26  ? 0.1808 0.1690 0.2306 0.0002  -0.0236 0.0140  51  ILE   A CA    
403   C  C     . ILE   A 26  ? 0.1800 0.1724 0.2368 0.0014  -0.0355 0.0113  51  ILE   A C     
404   O  O     . ILE   A 26  ? 0.1964 0.1828 0.2407 0.0041  -0.0294 0.0115  51  ILE   A O     
405   C  CB    . ILE   A 26  ? 0.2161 0.1554 0.2248 0.0043  -0.0286 0.0175  51  ILE   A CB    
406   C  CG1   . ILE   A 26  ? 0.2340 0.1647 0.2321 -0.0190 -0.0390 0.0051  51  ILE   A CG1   
407   C  CG2   . ILE   A 26  ? 0.2361 0.2115 0.2356 0.0131  -0.0421 0.0193  51  ILE   A CG2   
408   C  CD1   . ILE   A 26  ? 0.2500 0.1630 0.2406 0.0128  -0.0472 0.0023  51  ILE   A CD1   
420   N  N     . GLY   A 27  ? 0.1878 0.1782 0.2459 0.0232  -0.0408 0.0326  52  GLY   A N     
421   C  CA    . GLY   A 27  ? 0.1635 0.1807 0.2609 0.0132  -0.0275 0.0387  52  GLY   A CA    
422   C  C     . GLY   A 27  ? 0.1849 0.1696 0.2506 -0.0088 -0.0564 0.0178  52  GLY   A C     
423   O  O     . GLY   A 27  ? 0.2415 0.1979 0.2462 0.0014  -0.0593 0.0210  52  GLY   A O     
427   N  N     . SER   A 28  ? 0.2128 0.1821 0.2537 -0.0108 -0.0401 0.0158  53  SER   A N     
428   C  CA    . SER   A 28  ? 0.1922 0.1761 0.2573 -0.0155 -0.0343 0.0275  53  SER   A CA    
429   C  C     . SER   A 28  ? 0.1831 0.1866 0.2641 0.0066  -0.0167 0.0162  53  SER   A C     
430   O  O     . SER   A 28  ? 0.2189 0.1928 0.2563 0.0050  -0.0260 0.0288  53  SER   A O     
431   C  CB    . SER   A 28  ? 0.2722 0.1937 0.2876 0.0227  -0.0435 0.0676  53  SER   A CB    
432   O  OG    . SER   A 28  ? 0.2950 0.2191 0.3355 0.0081  -0.0336 0.0634  53  SER   A OG    
438   N  N     . VAL   A 29  ? 0.1727 0.2105 0.3040 0.0225  -0.0021 0.0311  54  VAL   A N     
439   C  CA    . VAL   A 29  ? 0.1911 0.1814 0.3172 0.0053  -0.0148 0.0282  54  VAL   A CA    
440   C  C     . VAL   A 29  ? 0.2464 0.1841 0.3317 -0.0008 -0.0062 0.0232  54  VAL   A C     
441   O  O     . VAL   A 29  ? 0.3273 0.1909 0.3464 -0.0247 -0.0049 0.0055  54  VAL   A O     
442   C  CB    . VAL   A 29  ? 0.2244 0.1999 0.3082 0.0116  -0.0317 0.0208  54  VAL   A CB    
443   C  CG1   . VAL   A 29  ? 0.2351 0.2054 0.3098 0.0102  -0.0445 0.0335  54  VAL   A CG1   
444   C  CG2   . VAL   A 29  ? 0.2225 0.2313 0.2911 -0.0047 -0.0341 0.0126  54  VAL   A CG2   
454   N  N     . GLU   A 30  ? 0.3000 0.1881 0.3240 -0.0067 -0.0213 0.0352  55  GLU   A N     
455   C  CA    . GLU   A 30  ? 0.3329 0.1902 0.3467 0.0051  0.0251  0.0648  55  GLU   A CA    
456   C  C     . GLU   A 30  ? 0.3099 0.1922 0.3349 0.0198  0.0334  0.0593  55  GLU   A C     
457   O  O     . GLU   A 30  ? 0.3255 0.2000 0.3099 0.0157  0.0072  0.0340  55  GLU   A O     
458   C  CB    . GLU   A 30  ? 0.3946 0.2480 0.4000 0.0433  0.0290  0.1067  55  GLU   A CB    
459   C  CG    . GLU   A 30  ? 0.4667 0.3307 0.4626 0.0475  0.0222  0.0700  55  GLU   A CG    
460   C  CD    . GLU   A 30  ? 0.5382 0.4107 0.5182 0.0640  0.0285  0.0264  55  GLU   A CD    
461   O  OE1   . GLU   A 30  ? 0.5482 0.4111 0.5416 0.0405  0.0373  0.0061  55  GLU   A OE1   
462   O  OE2   . GLU   A 30  ? 0.5926 0.4793 0.5457 0.0804  0.0200  -0.0104 55  GLU   A OE2   
469   N  N     . LEU   A 31  ? 0.3371 0.2190 0.3623 0.0054  0.0435  0.0562  56  LEU   A N     
470   C  CA    . LEU   A 31  ? 0.3448 0.2639 0.3916 0.0191  0.0399  0.0799  56  LEU   A CA    
471   C  C     . LEU   A 31  ? 0.2906 0.3166 0.3674 0.0984  0.0113  0.0572  56  LEU   A C     
472   O  O     . LEU   A 31  ? 0.3548 0.3807 0.3911 0.1651  -0.0363 0.0235  56  LEU   A O     
473   C  CB    . LEU   A 31  ? 0.4218 0.2826 0.4444 0.0138  0.0703  0.1153  56  LEU   A CB    
474   C  CG    . LEU   A 31  ? 0.4656 0.2828 0.4981 -0.0325 0.0918  0.1256  56  LEU   A CG    
475   C  CD1   . LEU   A 31  ? 0.5262 0.3146 0.5381 -0.0550 0.0919  0.1052  56  LEU   A CD1   
476   C  CD2   . LEU   A 31  ? 0.4898 0.3238 0.5091 -0.0303 0.0718  0.1381  56  LEU   A CD2   
488   N  N     . VAL   A 32  ? 0.2087 0.2673 0.3173 0.0556  0.0038  0.0845  57  VAL   A N     
489   C  CA    A VAL   A 32  ? 0.2220 0.2932 0.3088 0.0264  0.0061  0.0845  57  VAL   A CA    
490   C  CA    B VAL   A 32  ? 0.2197 0.2744 0.3058 0.0542  0.0007  0.0875  57  VAL   A CA    
491   C  C     . VAL   A 32  ? 0.2079 0.2638 0.3096 0.0378  0.0034  0.0865  57  VAL   A C     
492   O  O     . VAL   A 32  ? 0.2268 0.2656 0.3187 0.0213  0.0046  0.0776  57  VAL   A O     
493   C  CB    A VAL   A 32  ? 0.2467 0.3336 0.3072 -0.0260 0.0138  0.0673  57  VAL   A CB    
494   C  CB    B VAL   A 32  ? 0.2444 0.2800 0.2987 0.0517  0.0008  0.0721  57  VAL   A CB    
495   C  CG1   A VAL   A 32  ? 0.2315 0.3594 0.3100 -0.0477 -0.0062 0.0547  57  VAL   A CG1   
496   C  CG1   B VAL   A 32  ? 0.2443 0.2825 0.2933 0.0816  -0.0056 0.0867  57  VAL   A CG1   
497   C  CG2   A VAL   A 32  ? 0.2813 0.3420 0.3070 -0.0328 0.0208  0.0781  57  VAL   A CG2   
498   C  CG2   B VAL   A 32  ? 0.2479 0.2755 0.2999 0.0516  -0.0196 0.0660  57  VAL   A CG2   
515   N  N     . THR   A 33  ? 0.2470 0.2459 0.3213 0.0418  0.0094  0.0809  58  THR   A N     
516   C  CA    . THR   A 33  ? 0.3020 0.2568 0.3303 0.0429  0.0120  0.0842  58  THR   A CA    
517   C  C     . THR   A 33  ? 0.2714 0.2806 0.3526 0.0373  0.0106  0.0705  58  THR   A C     
518   O  O     . THR   A 33  ? 0.2486 0.3057 0.3497 0.0549  -0.0100 0.0602  58  THR   A O     
519   C  CB    . THR   A 33  ? 0.3213 0.2732 0.3342 0.0398  0.0145  0.0810  58  THR   A CB    
520   O  OG1   . THR   A 33  ? 0.3070 0.2733 0.3487 0.0244  0.0046  0.0839  58  THR   A OG1   
521   C  CG2   . THR   A 33  ? 0.3657 0.3109 0.3462 0.0398  0.0084  0.0655  58  THR   A CG2   
529   N  N     . GLN   A 34  ? 0.2455 0.2517 0.3546 0.0268  0.0132  0.0681  59  GLN   A N     
530   C  CA    . GLN   A 34  ? 0.2750 0.2607 0.3683 0.0353  0.0154  0.0746  59  GLN   A CA    
531   C  C     . GLN   A 34  ? 0.2865 0.2537 0.3620 0.0389  0.0124  0.0839  59  GLN   A C     
532   O  O     . GLN   A 34  ? 0.2502 0.2983 0.3514 0.0152  0.0298  0.0814  59  GLN   A O     
533   C  CB    . GLN   A 34  ? 0.2582 0.2634 0.3836 0.0452  0.0224  0.0755  59  GLN   A CB    
534   C  CG    . GLN   A 34  ? 0.2386 0.2405 0.3921 0.0286  0.0258  0.0793  59  GLN   A CG    
535   C  CD    . GLN   A 34  ? 0.2298 0.2674 0.4155 0.0442  0.0285  0.0593  59  GLN   A CD    
536   O  OE1   . GLN   A 34  ? 0.2523 0.3439 0.4457 0.0296  0.0347  0.0695  59  GLN   A OE1   
537   N  NE2   . GLN   A 34  ? 0.1936 0.2501 0.4054 0.0347  0.0275  0.0571  59  GLN   A NE2   
546   N  N     . GLN   A 35  ? 0.3506 0.2447 0.3728 0.0349  -0.0035 0.1069  60  GLN   A N     
547   C  CA    . GLN   A 35  ? 0.3684 0.2709 0.3896 0.0425  0.0232  0.0951  60  GLN   A CA    
548   C  C     . GLN   A 35  ? 0.3055 0.2351 0.3883 0.0295  0.0351  0.0910  60  GLN   A C     
549   O  O     . GLN   A 35  ? 0.3066 0.2617 0.4030 0.0178  0.0529  0.0845  60  GLN   A O     
550   C  CB    . GLN   A 35  ? 0.4676 0.3290 0.4143 0.0894  0.0232  0.1064  60  GLN   A CB    
551   C  CG    . GLN   A 35  ? 0.5545 0.4081 0.4605 0.0845  0.0139  0.1072  60  GLN   A CG    
552   C  CD    . GLN   A 35  ? 0.6348 0.5210 0.5342 0.0590  0.0174  0.0786  60  GLN   A CD    
553   O  OE1   . GLN   A 35  ? 0.6870 0.5700 0.5807 0.0312  0.0356  0.0739  60  GLN   A OE1   
554   N  NE2   . GLN   A 35  ? 0.6510 0.5636 0.5459 0.0424  -0.0108 0.0531  60  GLN   A NE2   
563   N  N     . MET   A 36  ? 0.2908 0.2249 0.3676 0.0119  0.0624  0.0947  61  MET   A N     
564   C  CA    . MET   A 36  ? 0.2970 0.2178 0.3742 0.0366  0.0302  0.0704  61  MET   A CA    
565   C  C     . MET   A 36  ? 0.2729 0.2310 0.3317 0.0181  0.0529  0.0872  61  MET   A C     
566   O  O     . MET   A 36  ? 0.2776 0.2329 0.3367 0.0097  0.0973  0.0958  61  MET   A O     
567   C  CB    . MET   A 36  ? 0.2562 0.1960 0.4024 -0.0008 -0.0048 0.0343  61  MET   A CB    
568   C  CG    . MET   A 36  ? 0.1857 0.1962 0.4532 -0.0232 0.0063  0.0379  61  MET   A CG    
569   S  SD    . MET   A 36  ? 0.2786 0.3050 0.4158 0.0273  0.0379  0.0550  61  MET   A SD    
570   C  CE    . MET   A 36  ? 0.2470 0.2127 0.3876 0.0214  0.0085  0.1292  61  MET   A CE    
580   N  N     . TRP   A 37  ? 0.1981 0.2371 0.3042 -0.0038 0.0657  0.0606  62  TRP   A N     
581   C  CA    . TRP   A 37  ? 0.1985 0.2315 0.3046 -0.0042 0.0527  0.0478  62  TRP   A CA    
582   C  C     . TRP   A 37  ? 0.1618 0.2418 0.3258 -0.0214 0.0534  0.0655  62  TRP   A C     
583   O  O     . TRP   A 37  ? 0.1702 0.2373 0.3130 -0.0149 0.0398  0.0583  62  TRP   A O     
584   C  CB    . TRP   A 37  ? 0.1964 0.2267 0.3038 0.0116  0.0501  0.0298  62  TRP   A CB    
585   C  CG    . TRP   A 37  ? 0.1975 0.2605 0.3013 -0.0053 0.0360  0.0183  62  TRP   A CG    
586   C  CD1   . TRP   A 37  ? 0.1851 0.2511 0.2933 -0.0176 0.0240  0.0311  62  TRP   A CD1   
587   C  CD2   . TRP   A 37  ? 0.2240 0.2712 0.3003 -0.0069 0.0519  0.0252  62  TRP   A CD2   
588   N  NE1   . TRP   A 37  ? 0.2328 0.2823 0.3125 -0.0111 0.0265  0.0494  62  TRP   A NE1   
589   C  CE2   . TRP   A 37  ? 0.2307 0.2802 0.3037 -0.0047 0.0572  0.0400  62  TRP   A CE2   
590   C  CE3   . TRP   A 37  ? 0.2828 0.2866 0.3001 -0.0403 0.0559  0.0280  62  TRP   A CE3   
591   C  CZ2   . TRP   A 37  ? 0.2490 0.2989 0.3114 -0.0437 0.0655  0.0274  62  TRP   A CZ2   
592   C  CZ3   . TRP   A 37  ? 0.3290 0.2922 0.3039 -0.0598 0.0541  0.0156  62  TRP   A CZ3   
593   C  CH2   . TRP   A 37  ? 0.2985 0.3108 0.3143 -0.0590 0.0594  0.0242  62  TRP   A CH2   
604   N  N     . VAL   A 38  ? 0.1976 0.2521 0.3586 -0.0289 0.0692  0.0462  63  VAL   A N     
605   C  CA    . VAL   A 38  ? 0.2198 0.2487 0.4063 -0.0087 0.0589  0.0493  63  VAL   A CA    
606   C  C     . VAL   A 38  ? 0.2014 0.2850 0.4451 -0.0133 0.0779  0.0465  63  VAL   A C     
607   O  O     . VAL   A 38  ? 0.1942 0.3312 0.4547 0.0195  0.1040  0.0027  63  VAL   A O     
608   C  CB    . VAL   A 38  ? 0.2667 0.2540 0.4195 0.0057  0.0526  0.0508  63  VAL   A CB    
609   C  CG1   . VAL   A 38  ? 0.2588 0.2766 0.4256 -0.0043 0.0378  0.0202  63  VAL   A CG1   
610   C  CG2   . VAL   A 38  ? 0.3040 0.2991 0.4339 -0.0114 0.0717  0.0568  63  VAL   A CG2   
620   N  N     . TYR   A 39  ? 0.1655 0.2808 0.4740 0.0024  0.0663  0.0665  64  TYR   A N     
621   C  CA    . TYR   A 39  ? 0.1715 0.3302 0.5167 0.0081  0.0752  0.0506  64  TYR   A CA    
622   C  C     . TYR   A 39  ? 0.1842 0.3731 0.5458 -0.0190 0.1086  0.0297  64  TYR   A C     
623   O  O     . TYR   A 39  ? 0.1809 0.3901 0.5382 -0.0359 0.1110  0.0134  64  TYR   A O     
624   C  CB    . TYR   A 39  ? 0.1739 0.3726 0.5288 0.0341  0.0787  0.0416  64  TYR   A CB    
625   C  CG    . TYR   A 39  ? 0.2081 0.4040 0.5415 0.0603  0.1064  0.0195  64  TYR   A CG    
626   C  CD1   . TYR   A 39  ? 0.2121 0.4447 0.5487 0.0418  0.1462  -0.0035 64  TYR   A CD1   
627   C  CD2   . TYR   A 39  ? 0.2524 0.4243 0.5449 0.0876  0.1185  0.0050  64  TYR   A CD2   
628   C  CE1   . TYR   A 39  ? 0.2437 0.4845 0.5696 0.0627  0.1529  -0.0069 64  TYR   A CE1   
629   C  CE2   . TYR   A 39  ? 0.2749 0.4624 0.5609 0.1029  0.1152  0.0128  64  TYR   A CE2   
630   C  CZ    . TYR   A 39  ? 0.2625 0.5011 0.5790 0.1011  0.1596  0.0082  64  TYR   A CZ    
631   O  OH    . TYR   A 39  ? 0.3325 0.5613 0.6114 0.0988  0.1340  0.0306  64  TYR   A OH    
641   N  N     . ASP   A 40  ? 0.2401 0.3843 0.5613 -0.0892 0.1343  0.0287  65  ASP   A N     
642   C  CA    . ASP   A 40  ? 0.2669 0.4170 0.6093 -0.1053 0.1428  0.0349  65  ASP   A CA    
643   C  C     . ASP   A 40  ? 0.3144 0.5045 0.6683 -0.1148 0.1418  0.0328  65  ASP   A C     
644   O  O     . ASP   A 40  ? 0.3092 0.5003 0.6688 -0.0771 0.1535  0.0310  65  ASP   A O     
645   C  CB    . ASP   A 40  ? 0.2826 0.3967 0.5996 -0.0618 0.1411  0.0392  65  ASP   A CB    
646   C  CG    . ASP   A 40  ? 0.2654 0.3985 0.5945 -0.0602 0.1331  0.0423  65  ASP   A CG    
647   O  OD1   . ASP   A 40  ? 0.2715 0.3919 0.5932 -0.0399 0.1254  0.0571  65  ASP   A OD1   
648   O  OD2   . ASP   A 40  ? 0.2944 0.4084 0.5909 -0.0745 0.1025  0.0247  65  ASP   A OD2   
653   N  N     . GLU   A 41  ? 0.3653 0.5921 0.7194 -0.1861 0.1312  0.0351  66  GLU   A N     
654   C  CA    . GLU   A 41  ? 0.4488 0.6860 0.7630 -0.1963 0.1297  0.0402  66  GLU   A CA    
655   C  C     . GLU   A 41  ? 0.4508 0.7175 0.7827 -0.2141 0.1444  0.0461  66  GLU   A C     
656   O  O     . GLU   A 41  ? 0.4501 0.7211 0.7917 -0.2357 0.1562  0.0407  66  GLU   A O     
657   C  CB    . GLU   A 41  ? 0.5590 0.7452 0.7832 -0.1931 0.1225  0.0428  66  GLU   A CB    
658   C  CG    . GLU   A 41  ? 0.6257 0.7941 0.8014 -0.1996 0.1209  0.0478  66  GLU   A CG    
659   C  CD    . GLU   A 41  ? 0.6897 0.8440 0.8196 -0.2001 0.1099  0.0491  66  GLU   A CD    
660   O  OE1   . GLU   A 41  ? 0.7177 0.8666 0.8334 -0.1822 0.0930  0.0332  66  GLU   A OE1   
661   O  OE2   . GLU   A 41  ? 0.7110 0.8546 0.8215 -0.2162 0.1138  0.0655  66  GLU   A OE2   
668   N  N     . ASP   A 42  ? 0.4710 0.7401 0.7926 -0.1857 0.1411  0.0539  67  ASP   A N     
669   C  CA    . ASP   A 42  ? 0.5290 0.7631 0.7985 -0.1653 0.1439  0.0579  67  ASP   A CA    
670   C  C     . ASP   A 42  ? 0.4984 0.7461 0.7675 -0.1374 0.1905  0.0598  67  ASP   A C     
671   O  O     . ASP   A 42  ? 0.4941 0.7728 0.7713 -0.1297 0.2033  0.0518  67  ASP   A O     
672   C  CB    . ASP   A 42  ? 0.6199 0.7934 0.8322 -0.1711 0.1058  0.0644  67  ASP   A CB    
673   C  CG    . ASP   A 42  ? 0.6955 0.8193 0.8630 -0.1743 0.0791  0.0726  67  ASP   A CG    
674   O  OD1   . ASP   A 42  ? 0.7326 0.8313 0.8744 -0.1658 0.0712  0.0736  67  ASP   A OD1   
675   O  OD2   . ASP   A 42  ? 0.7033 0.8320 0.8738 -0.1906 0.0727  0.0791  67  ASP   A OD2   
680   N  N     . VAL   A 43  ? 0.4362 0.6885 0.7310 -0.1093 0.2279  0.0699  68  VAL   A N     
681   C  CA    . VAL   A 43  ? 0.4354 0.6290 0.6998 -0.0722 0.2048  0.0798  68  VAL   A CA    
682   C  C     . VAL   A 43  ? 0.4063 0.5769 0.6573 -0.0335 0.1832  0.0722  68  VAL   A C     
683   O  O     . VAL   A 43  ? 0.4342 0.5699 0.6539 -0.0110 0.1725  0.0770  68  VAL   A O     
684   C  CB    . VAL   A 43  ? 0.4706 0.6224 0.7112 -0.0803 0.1860  0.1052  68  VAL   A CB    
685   C  CG1   . VAL   A 43  ? 0.4483 0.6118 0.7098 -0.0862 0.1868  0.1163  68  VAL   A CG1   
686   C  CG2   . VAL   A 43  ? 0.5148 0.6436 0.7200 -0.0735 0.1803  0.1077  68  VAL   A CG2   
696   N  N     . GLY   A 44  ? 0.3700 0.5397 0.6256 -0.0249 0.1659  0.0525  69  GLY   A N     
697   C  CA    . GLY   A 44  ? 0.3376 0.5014 0.5833 -0.0472 0.1702  0.0271  69  GLY   A CA    
698   C  C     . GLY   A 44  ? 0.3064 0.4663 0.5367 -0.0390 0.1896  0.0061  69  GLY   A C     
699   O  O     . GLY   A 44  ? 0.2853 0.4644 0.5364 -0.0617 0.1757  -0.0029 69  GLY   A O     
703   N  N     . ILE   A 45  ? 0.3248 0.4430 0.5102 -0.0093 0.1838  -0.0025 70  ILE   A N     
704   C  CA    . ILE   A 45  ? 0.2799 0.4262 0.5069 -0.0171 0.1730  0.0111  70  ILE   A CA    
705   C  C     . ILE   A 45  ? 0.3049 0.4182 0.4749 0.0069  0.1630  0.0000  70  ILE   A C     
706   O  O     . ILE   A 45  ? 0.3480 0.4531 0.4821 0.0080  0.1476  -0.0076 70  ILE   A O     
707   C  CB    . ILE   A 45  ? 0.3330 0.4425 0.5541 -0.0371 0.1281  0.0313  70  ILE   A CB    
708   C  CG1   . ILE   A 45  ? 0.4386 0.4775 0.5893 -0.0519 0.0686  0.0531  70  ILE   A CG1   
709   C  CG2   . ILE   A 45  ? 0.2907 0.4218 0.5691 -0.0567 0.1352  0.0370  70  ILE   A CG2   
710   C  CD1   . ILE   A 45  ? 0.4941 0.5331 0.6073 -0.0498 0.0618  0.0548  70  ILE   A CD1   
722   N  N     . ASN   A 46  ? 0.2734 0.3599 0.4439 0.0019  0.1652  0.0054  71  ASN   A N     
723   C  CA    . ASN   A 46  ? 0.2761 0.3589 0.4236 -0.0110 0.1493  0.0305  71  ASN   A CA    
724   C  C     . ASN   A 46  ? 0.2679 0.3282 0.3786 0.0174  0.1103  0.0629  71  ASN   A C     
725   O  O     . ASN   A 46  ? 0.2680 0.3051 0.3756 -0.0157 0.1075  0.0494  71  ASN   A O     
726   C  CB    . ASN   A 46  ? 0.3261 0.3789 0.4591 -0.0350 0.1435  0.0274  71  ASN   A CB    
727   C  CG    . ASN   A 46  ? 0.3478 0.3793 0.4840 -0.0478 0.1518  0.0419  71  ASN   A CG    
728   O  OD1   . ASN   A 46  ? 0.3963 0.3852 0.4983 -0.0507 0.1393  0.0517  71  ASN   A OD1   
729   N  ND2   . ASN   A 46  ? 0.3048 0.3803 0.4937 -0.0538 0.1619  0.0440  71  ASN   A ND2   
736   N  N     . TYR   A 47  ? 0.3104 0.3218 0.3394 0.0028  0.0931  0.0929  72  TYR   A N     
737   C  CA    . TYR   A 47  ? 0.3319 0.3040 0.3296 -0.0200 0.0776  0.0808  72  TYR   A CA    
738   C  C     . TYR   A 47  ? 0.3529 0.2895 0.3184 -0.0300 0.0690  0.0869  72  TYR   A C     
739   O  O     . TYR   A 47  ? 0.4040 0.3098 0.2993 -0.0266 0.0923  0.0778  72  TYR   A O     
740   C  CB    . TYR   A 47  ? 0.3324 0.2975 0.3544 -0.0234 0.0639  0.0537  72  TYR   A CB    
741   C  CG    . TYR   A 47  ? 0.3310 0.2883 0.3754 -0.0125 0.0443  0.0427  72  TYR   A CG    
742   C  CD1   . TYR   A 47  ? 0.3243 0.2980 0.3902 -0.0349 0.0654  0.0567  72  TYR   A CD1   
743   C  CD2   . TYR   A 47  ? 0.3777 0.3337 0.3861 -0.0376 0.0332  0.0299  72  TYR   A CD2   
744   C  CE1   . TYR   A 47  ? 0.3417 0.3080 0.3997 -0.0109 0.0452  0.0637  72  TYR   A CE1   
745   C  CE2   . TYR   A 47  ? 0.3648 0.3465 0.3974 -0.0210 0.0361  0.0483  72  TYR   A CE2   
746   C  CZ    . TYR   A 47  ? 0.3496 0.3383 0.4150 -0.0146 0.0318  0.0600  72  TYR   A CZ    
747   O  OH    . TYR   A 47  ? 0.3612 0.3408 0.4331 0.0105  0.0319  0.0635  72  TYR   A OH    
757   N  N     . ARG   A 48  ? 0.3417 0.2738 0.3385 -0.0347 0.0559  0.0791  73  ARG   A N     
758   C  CA    . ARG   A 48  ? 0.3466 0.2875 0.3586 -0.0478 0.0729  0.0757  73  ARG   A CA    
759   C  C     . ARG   A 48  ? 0.3489 0.2673 0.3479 -0.0337 0.0915  0.0885  73  ARG   A C     
760   O  O     . ARG   A 48  ? 0.3451 0.2896 0.3482 -0.0276 0.1071  0.1015  73  ARG   A O     
761   C  CB    . ARG   A 48  ? 0.3585 0.3152 0.3929 -0.0579 0.0869  0.0706  73  ARG   A CB    
762   C  CG    . ARG   A 48  ? 0.3462 0.3406 0.4186 -0.0560 0.0860  0.0715  73  ARG   A CG    
763   C  CD    . ARG   A 48  ? 0.3393 0.3565 0.4436 -0.0538 0.0723  0.0891  73  ARG   A CD    
764   N  NE    . ARG   A 48  ? 0.3384 0.3567 0.4631 -0.0244 0.0822  0.0946  73  ARG   A NE    
765   C  CZ    . ARG   A 48  ? 0.3613 0.3430 0.4757 -0.0097 0.0717  0.1039  73  ARG   A CZ    
766   N  NH1   . ARG   A 48  ? 0.4161 0.3507 0.4837 -0.0056 0.0547  0.1052  73  ARG   A NH1   
767   N  NH2   . ARG   A 48  ? 0.3530 0.3213 0.4860 0.0017  0.0626  0.1016  73  ARG   A NH2   
781   N  N     . GLU   A 49  ? 0.3156 0.2737 0.3523 0.0112  0.0787  0.0754  74  GLU   A N     
782   C  CA    . GLU   A 49  ? 0.3149 0.2711 0.3511 0.0104  0.0728  0.0726  74  GLU   A CA    
783   C  C     . GLU   A 49  ? 0.2880 0.2907 0.3599 0.0005  0.0719  0.0750  74  GLU   A C     
784   O  O     . GLU   A 49  ? 0.2803 0.3311 0.3615 -0.0185 0.0807  0.0847  74  GLU   A O     
785   C  CB    . GLU   A 49  ? 0.3795 0.2962 0.3712 0.0002  0.0601  0.0882  74  GLU   A CB    
786   C  CG    . GLU   A 49  ? 0.4865 0.3186 0.3945 0.0070  0.0462  0.0932  74  GLU   A CG    
787   C  CD    . GLU   A 49  ? 0.5833 0.3648 0.4363 0.0186  0.0227  0.0828  74  GLU   A CD    
788   O  OE1   . GLU   A 49  ? 0.6475 0.3615 0.4625 -0.0046 0.0619  0.0912  74  GLU   A OE1   
789   O  OE2   . GLU   A 49  ? 0.6224 0.4204 0.4425 0.0544  -0.0294 0.0725  74  GLU   A OE2   
796   N  N     . VAL   A 50  ? 0.2764 0.2699 0.3742 0.0166  0.0752  0.0620  75  VAL   A N     
797   C  CA    . VAL   A 50  ? 0.3042 0.2960 0.3938 0.0180  0.0592  0.0688  75  VAL   A CA    
798   C  C     . VAL   A 50  ? 0.2521 0.3055 0.3757 0.0070  0.0344  0.0682  75  VAL   A C     
799   O  O     . VAL   A 50  ? 0.2395 0.3449 0.3712 0.0126  0.0003  0.0393  75  VAL   A O     
800   C  CB    . VAL   A 50  ? 0.3265 0.3370 0.4290 0.0774  0.0621  0.0682  75  VAL   A CB    
801   C  CG1   . VAL   A 50  ? 0.3672 0.3736 0.4437 0.1495  0.0679  0.0696  75  VAL   A CG1   
802   C  CG2   . VAL   A 50  ? 0.3774 0.3066 0.4435 0.0257  0.0303  0.0785  75  VAL   A CG2   
812   N  N     . THR   A 51  ? 0.2295 0.2568 0.3690 -0.0085 0.0515  0.0924  76  THR   A N     
813   C  CA    . THR   A 51  ? 0.2288 0.2245 0.3701 -0.0272 0.0380  0.0873  76  THR   A CA    
814   C  C     . THR   A 51  ? 0.2169 0.2162 0.3539 -0.0579 0.0366  0.0625  76  THR   A C     
815   O  O     . THR   A 51  ? 0.2047 0.2430 0.3547 -0.0238 0.0261  0.0515  76  THR   A O     
816   C  CB    . THR   A 51  ? 0.2485 0.2826 0.3939 -0.0413 0.0250  0.0865  76  THR   A CB    
817   O  OG1   . THR   A 51  ? 0.3177 0.2883 0.4043 -0.0198 0.0338  0.1012  76  THR   A OG1   
818   C  CG2   . THR   A 51  ? 0.2992 0.2852 0.4099 -0.0412 -0.0093 0.0620  76  THR   A CG2   
826   N  N     . PHE   A 52  ? 0.2074 0.1816 0.3400 -0.0165 0.0138  0.0629  77  PHE   A N     
827   C  CA    . PHE   A 52  ? 0.2040 0.2007 0.3246 -0.0200 -0.0062 0.0665  77  PHE   A CA    
828   C  C     . PHE   A 52  ? 0.1843 0.1971 0.3153 -0.0141 -0.0316 0.0544  77  PHE   A C     
829   O  O     . PHE   A 52  ? 0.1762 0.2197 0.3149 -0.0086 -0.0245 0.0638  77  PHE   A O     
830   C  CB    . PHE   A 52  ? 0.1851 0.2129 0.3160 -0.0111 0.0157  0.0510  77  PHE   A CB    
831   C  CG    . PHE   A 52  ? 0.1938 0.1994 0.3072 -0.0203 0.0085  0.0436  77  PHE   A CG    
832   C  CD1   . PHE   A 52  ? 0.2395 0.2090 0.3262 -0.0317 -0.0320 0.0451  77  PHE   A CD1   
833   C  CD2   . PHE   A 52  ? 0.2091 0.1942 0.3077 -0.0259 0.0207  0.0306  77  PHE   A CD2   
834   C  CE1   . PHE   A 52  ? 0.2577 0.2188 0.3388 -0.0608 -0.0379 0.0642  77  PHE   A CE1   
835   C  CE2   . PHE   A 52  ? 0.2535 0.2071 0.3144 -0.0282 0.0205  0.0312  77  PHE   A CE2   
836   C  CZ    . PHE   A 52  ? 0.2385 0.2179 0.3344 -0.0541 -0.0186 0.0528  77  PHE   A CZ    
846   N  N     . VAL   A 53  ? 0.1923 0.1852 0.3139 -0.0055 -0.0234 0.0287  78  VAL   A N     
847   C  CA    . VAL   A 53  ? 0.1702 0.1739 0.3090 -0.0315 -0.0258 0.0236  78  VAL   A CA    
848   C  C     . VAL   A 53  ? 0.1607 0.1882 0.2877 -0.0031 -0.0316 0.0275  78  VAL   A C     
849   O  O     . VAL   A 53  ? 0.1663 0.1959 0.3009 0.0054  -0.0370 0.0298  78  VAL   A O     
850   C  CB    . VAL   A 53  ? 0.2083 0.1881 0.3201 -0.0313 -0.0285 0.0089  78  VAL   A CB    
851   C  CG1   . VAL   A 53  ? 0.2046 0.2196 0.3240 -0.0321 -0.0110 -0.0108 78  VAL   A CG1   
852   C  CG2   . VAL   A 53  ? 0.2127 0.1844 0.3203 -0.0290 -0.0596 0.0143  78  VAL   A CG2   
862   N  N     . PRO   A 54  ? 0.1844 0.1772 0.2707 -0.0047 -0.0409 0.0396  79  PRO   A N     
863   C  CA    . PRO   A 54  ? 0.1461 0.1761 0.2534 0.0042  -0.0514 0.0325  79  PRO   A CA    
864   C  C     . PRO   A 54  ? 0.1645 0.1698 0.2627 0.0126  -0.0430 0.0214  79  PRO   A C     
865   O  O     . PRO   A 54  ? 0.1691 0.1754 0.2694 0.0067  -0.0093 0.0338  79  PRO   A O     
866   C  CB    . PRO   A 54  ? 0.1614 0.1908 0.2521 -0.0151 -0.0646 0.0407  79  PRO   A CB    
867   C  CG    . PRO   A 54  ? 0.1837 0.1883 0.2568 -0.0190 -0.0619 0.0379  79  PRO   A CG    
868   C  CD    . PRO   A 54  ? 0.2091 0.1654 0.2547 -0.0167 -0.0463 0.0428  79  PRO   A CD    
876   N  N     . GLY   A 55  ? 0.2007 0.1691 0.2563 -0.0066 -0.0355 0.0250  80  GLY   A N     
877   C  CA    . GLY   A 55  ? 0.1958 0.1627 0.2645 -0.0182 -0.0155 0.0219  80  GLY   A CA    
878   C  C     . GLY   A 55  ? 0.1911 0.1712 0.2890 -0.0103 -0.0268 -0.0006 80  GLY   A C     
879   O  O     . GLY   A 55  ? 0.1793 0.1965 0.2884 0.0004  -0.0234 0.0066  80  GLY   A O     
883   N  N     . LEU   A 56  ? 0.1617 0.1683 0.3052 -0.0010 -0.0440 -0.0123 81  LEU   A N     
884   C  CA    . LEU   A 56  ? 0.1370 0.1975 0.3123 -0.0050 -0.0337 0.0147  81  LEU   A CA    
885   C  C     . LEU   A 56  ? 0.1654 0.2060 0.2907 0.0017  -0.0560 0.0257  81  LEU   A C     
886   O  O     . LEU   A 56  ? 0.1752 0.2228 0.2982 0.0209  -0.0476 0.0264  81  LEU   A O     
887   C  CB    . LEU   A 56  ? 0.1564 0.2370 0.3568 -0.0288 -0.0564 0.0206  81  LEU   A CB    
888   C  CG    . LEU   A 56  ? 0.1670 0.2754 0.3782 -0.0794 -0.0880 0.0318  81  LEU   A CG    
889   C  CD1   . LEU   A 56  ? 0.2181 0.3126 0.4101 -0.0937 -0.1098 0.0343  81  LEU   A CD1   
890   C  CD2   . LEU   A 56  ? 0.2161 0.3111 0.4125 -0.0946 -0.0777 0.0345  81  LEU   A CD2   
902   N  N     . TYR   A 57  ? 0.1823 0.1977 0.2729 -0.0147 -0.0504 0.0172  82  TYR   A N     
903   C  CA    . TYR   A 57  ? 0.1633 0.1872 0.2814 -0.0209 -0.0287 0.0137  82  TYR   A CA    
904   C  C     . TYR   A 57  ? 0.1642 0.1857 0.2773 -0.0034 -0.0047 -0.0038 82  TYR   A C     
905   O  O     . TYR   A 57  ? 0.1609 0.2011 0.2870 0.0049  -0.0307 0.0099  82  TYR   A O     
906   C  CB    . TYR   A 57  ? 0.1607 0.2087 0.2827 -0.0155 -0.0274 0.0476  82  TYR   A CB    
907   C  CG    . TYR   A 57  ? 0.1650 0.2042 0.3009 -0.0004 -0.0357 0.0170  82  TYR   A CG    
908   C  CD1   . TYR   A 57  ? 0.1584 0.1996 0.3111 0.0011  -0.0122 -0.0075 82  TYR   A CD1   
909   C  CD2   . TYR   A 57  ? 0.1583 0.1884 0.3094 0.0143  -0.0338 -0.0089 82  TYR   A CD2   
910   C  CE1   . TYR   A 57  ? 0.1802 0.2194 0.3280 0.0039  -0.0222 -0.0213 82  TYR   A CE1   
911   C  CE2   . TYR   A 57  ? 0.1888 0.2075 0.3244 0.0144  -0.0291 -0.0267 82  TYR   A CE2   
912   C  CZ    . TYR   A 57  ? 0.2176 0.2018 0.3438 0.0087  -0.0079 -0.0301 82  TYR   A CZ    
913   O  OH    . TYR   A 57  ? 0.2339 0.2504 0.3704 0.0302  0.0087  -0.0357 82  TYR   A OH    
923   N  N     . LYS   A 58  ? 0.1793 0.1778 0.2670 0.0007  -0.0211 0.0138  83  LYS   A N     
924   C  CA    . LYS   A 58  ? 0.1829 0.1946 0.2604 -0.0319 -0.0473 0.0181  83  LYS   A CA    
925   C  C     . LYS   A 58  ? 0.1778 0.1759 0.2586 -0.0149 -0.0452 0.0111  83  LYS   A C     
926   O  O     . LYS   A 58  ? 0.2042 0.1662 0.2773 0.0065  -0.0433 0.0212  83  LYS   A O     
927   C  CB    . LYS   A 58  ? 0.2043 0.1965 0.2569 -0.0265 -0.0404 0.0111  83  LYS   A CB    
928   C  CG    . LYS   A 58  ? 0.2226 0.2010 0.2653 -0.0148 -0.0221 0.0135  83  LYS   A CG    
929   C  CD    . LYS   A 58  ? 0.2235 0.2150 0.3030 -0.0200 -0.0166 -0.0030 83  LYS   A CD    
930   C  CE    . LYS   A 58  ? 0.2358 0.2176 0.3514 -0.0255 -0.0044 -0.0253 83  LYS   A CE    
931   N  NZ    . LYS   A 58  ? 0.2172 0.2572 0.3863 -0.0379 -0.0106 -0.0725 83  LYS   A NZ    
945   N  N     . ILE   A 59  ? 0.1942 0.1924 0.2752 0.0080  -0.0519 0.0051  84  ILE   A N     
946   C  CA    . ILE   A 59  ? 0.2234 0.1859 0.2752 -0.0129 -0.0874 0.0099  84  ILE   A CA    
947   C  C     . ILE   A 59  ? 0.2195 0.2062 0.2914 0.0089  -0.0864 -0.0056 84  ILE   A C     
948   O  O     . ILE   A 59  ? 0.2252 0.2369 0.2912 0.0333  -0.0868 -0.0120 84  ILE   A O     
949   C  CB    . ILE   A 59  ? 0.2294 0.1973 0.2763 0.0069  -0.0962 0.0136  84  ILE   A CB    
950   C  CG1   . ILE   A 59  ? 0.2089 0.1984 0.3012 0.0087  -0.0823 -0.0250 84  ILE   A CG1   
951   C  CG2   . ILE   A 59  ? 0.2826 0.1897 0.2735 0.0259  -0.0939 -0.0078 84  ILE   A CG2   
952   C  CD1   . ILE   A 59  ? 0.2062 0.2317 0.3240 0.0050  -0.0483 -0.0085 84  ILE   A CD1   
964   N  N     . PHE   A 60  ? 0.1873 0.1983 0.3067 0.0279  -0.0622 0.0052  85  PHE   A N     
965   C  CA    . PHE   A 60  ? 0.1508 0.1920 0.3122 0.0101  -0.0542 0.0018  85  PHE   A CA    
966   C  C     . PHE   A 60  ? 0.1476 0.2127 0.3099 0.0048  -0.0604 0.0030  85  PHE   A C     
967   O  O     . PHE   A 60  ? 0.1486 0.2173 0.3298 0.0214  -0.0662 -0.0124 85  PHE   A O     
968   C  CB    . PHE   A 60  ? 0.1688 0.1777 0.3349 -0.0140 -0.0394 0.0077  85  PHE   A CB    
969   C  CG    . PHE   A 60  ? 0.1763 0.2324 0.3679 -0.0311 -0.0448 -0.0173 85  PHE   A CG    
970   C  CD1   . PHE   A 60  ? 0.1916 0.2664 0.3988 0.0031  -0.0341 -0.0280 85  PHE   A CD1   
971   C  CD2   . PHE   A 60  ? 0.2033 0.2550 0.3723 -0.0221 -0.0590 -0.0101 85  PHE   A CD2   
972   C  CE1   . PHE   A 60  ? 0.2053 0.2668 0.4089 0.0304  -0.0353 -0.0388 85  PHE   A CE1   
973   C  CE2   . PHE   A 60  ? 0.1965 0.2491 0.3757 0.0212  -0.0913 -0.0217 85  PHE   A CE2   
974   C  CZ    . PHE   A 60  ? 0.2013 0.2532 0.3959 0.0456  -0.0412 -0.0434 85  PHE   A CZ    
984   N  N     . ASP   A 61  ? 0.1381 0.2169 0.2900 -0.0381 -0.0583 0.0169  86  ASP   A N     
985   C  CA    . ASP   A 61  ? 0.1562 0.1927 0.2624 -0.0260 -0.0630 0.0000  86  ASP   A CA    
986   C  C     . ASP   A 61  ? 0.1929 0.1556 0.2693 0.0063  -0.0542 0.0064  86  ASP   A C     
987   O  O     . ASP   A 61  ? 0.1791 0.1752 0.2816 0.0197  -0.0604 0.0041  86  ASP   A O     
988   C  CB    . ASP   A 61  ? 0.1715 0.2031 0.2606 0.0006  -0.0771 -0.0104 86  ASP   A CB    
989   C  CG    . ASP   A 61  ? 0.2098 0.2151 0.2850 0.0125  -0.0397 0.0094  86  ASP   A CG    
990   O  OD1   . ASP   A 61  ? 0.2139 0.2179 0.2924 0.0180  -0.0420 0.0152  86  ASP   A OD1   
991   O  OD2   . ASP   A 61  ? 0.1903 0.2273 0.2897 -0.0033 -0.0322 0.0025  86  ASP   A OD2   
996   N  N     . GLU   A 62  ? 0.1811 0.1698 0.2709 0.0124  -0.0508 0.0244  87  GLU   A N     
997   C  CA    . GLU   A 62  ? 0.2283 0.1709 0.2621 0.0433  -0.0676 0.0145  87  GLU   A CA    
998   C  C     . GLU   A 62  ? 0.2182 0.1717 0.2822 0.0464  -0.0853 -0.0133 87  GLU   A C     
999   O  O     . GLU   A 62  ? 0.2631 0.1652 0.3095 0.0538  -0.0923 -0.0019 87  GLU   A O     
1000  C  CB    . GLU   A 62  ? 0.2409 0.1927 0.2520 0.0373  -0.0415 0.0288  87  GLU   A CB    
1001  C  CG    . GLU   A 62  ? 0.2354 0.2098 0.2552 0.0549  -0.0336 0.0105  87  GLU   A CG    
1002  C  CD    . GLU   A 62  ? 0.2530 0.2255 0.2745 0.0624  -0.0711 0.0332  87  GLU   A CD    
1003  O  OE1   . GLU   A 62  ? 0.2695 0.2801 0.3070 0.0522  -0.0578 0.0340  87  GLU   A OE1   
1004  O  OE2   . GLU   A 62  ? 0.2968 0.2398 0.2832 0.0597  -0.0671 0.0365  87  GLU   A OE2   
1011  N  N     . ILE   A 63  ? 0.2271 0.2110 0.2894 0.0431  -0.0796 0.0020  88  ILE   A N     
1012  C  CA    . ILE   A 63  ? 0.2160 0.2231 0.3035 0.0365  -0.1176 -0.0019 88  ILE   A CA    
1013  C  C     . ILE   A 63  ? 0.2287 0.2148 0.3056 0.0412  -0.1261 0.0157  88  ILE   A C     
1014  O  O     . ILE   A 63  ? 0.2845 0.2014 0.3236 0.0477  -0.1435 -0.0006 88  ILE   A O     
1015  C  CB    . ILE   A 63  ? 0.2457 0.2314 0.3282 0.0417  -0.1424 -0.0136 88  ILE   A CB    
1016  C  CG1   . ILE   A 63  ? 0.2922 0.2283 0.3232 0.0769  -0.1546 -0.0074 88  ILE   A CG1   
1017  C  CG2   . ILE   A 63  ? 0.2536 0.2281 0.3441 0.0314  -0.1702 -0.0167 88  ILE   A CG2   
1018  C  CD1   . ILE   A 63  ? 0.3058 0.2426 0.3284 0.0641  -0.1584 -0.0331 88  ILE   A CD1   
1030  N  N     . LEU   A 64  ? 0.1802 0.2475 0.2984 0.0442  -0.0964 -0.0037 89  LEU   A N     
1031  C  CA    . LEU   A 64  ? 0.1785 0.2408 0.2914 0.0465  -0.0886 -0.0063 89  LEU   A CA    
1032  C  C     . LEU   A 64  ? 0.1991 0.2294 0.2843 0.0484  -0.0883 -0.0195 89  LEU   A C     
1033  O  O     . LEU   A 64  ? 0.2199 0.2365 0.3019 0.0613  -0.0722 0.0050  89  LEU   A O     
1034  C  CB    . LEU   A 64  ? 0.1588 0.2646 0.3052 0.0397  -0.0847 0.0078  89  LEU   A CB    
1035  C  CG    . LEU   A 64  ? 0.1692 0.2948 0.3299 0.0520  -0.0668 0.0263  89  LEU   A CG    
1036  C  CD1   . LEU   A 64  ? 0.1928 0.3512 0.3567 0.0407  -0.0508 0.0202  89  LEU   A CD1   
1037  C  CD2   . LEU   A 64  ? 0.2282 0.2989 0.3355 0.0262  -0.0192 0.0254  89  LEU   A CD2   
1049  N  N     . VAL   A 65  ? 0.1951 0.2133 0.2737 0.0563  -0.0899 -0.0137 90  VAL   A N     
1050  C  CA    . VAL   A 65  ? 0.2173 0.2015 0.2639 0.0150  -0.0992 -0.0066 90  VAL   A CA    
1051  C  C     . VAL   A 65  ? 0.2271 0.2042 0.2579 0.0414  -0.0907 -0.0010 90  VAL   A C     
1052  O  O     . VAL   A 65  ? 0.2659 0.1989 0.2633 0.0494  -0.0880 -0.0098 90  VAL   A O     
1053  C  CB    . VAL   A 65  ? 0.2047 0.2079 0.2590 0.0265  -0.0808 0.0135  90  VAL   A CB    
1054  C  CG1   . VAL   A 65  ? 0.2348 0.2291 0.2653 0.0527  -0.0610 -0.0019 90  VAL   A CG1   
1055  C  CG2   . VAL   A 65  ? 0.2051 0.2162 0.2411 0.0238  -0.0927 0.0178  90  VAL   A CG2   
1065  N  N     . ASN   A 66  ? 0.2772 0.1993 0.2604 0.0635  -0.1053 0.0149  91  ASN   A N     
1066  C  CA    . ASN   A 66  ? 0.3155 0.2100 0.2738 0.0707  -0.1202 -0.0093 91  ASN   A CA    
1067  C  C     . ASN   A 66  ? 0.3199 0.2168 0.2993 0.0685  -0.1272 -0.0188 91  ASN   A C     
1068  O  O     . ASN   A 66  ? 0.3264 0.2286 0.3149 0.0705  -0.1410 0.0026  91  ASN   A O     
1069  C  CB    . ASN   A 66  ? 0.3545 0.2146 0.2604 0.0733  -0.1140 -0.0158 91  ASN   A CB    
1070  C  CG    . ASN   A 66  ? 0.3476 0.2055 0.2497 0.0605  -0.1033 -0.0115 91  ASN   A CG    
1071  O  OD1   . ASN   A 66  ? 0.3109 0.1950 0.2343 0.0710  -0.1145 -0.0065 91  ASN   A OD1   
1072  N  ND2   . ASN   A 66  ? 0.3631 0.1953 0.2533 0.0503  -0.1197 -0.0055 91  ASN   A ND2   
1079  N  N     . ALA   A 67  ? 0.2688 0.2155 0.3143 0.0691  -0.1303 -0.0124 92  ALA   A N     
1080  C  CA    . ALA   A 67  ? 0.2729 0.2549 0.3453 0.0603  -0.1314 -0.0153 92  ALA   A CA    
1081  C  C     . ALA   A 67  ? 0.2723 0.2290 0.3224 0.0808  -0.1346 -0.0276 92  ALA   A C     
1082  O  O     . ALA   A 67  ? 0.2994 0.2314 0.3387 0.0848  -0.1167 -0.0278 92  ALA   A O     
1083  C  CB    . ALA   A 67  ? 0.2350 0.2734 0.3743 0.0485  -0.1394 -0.0200 92  ALA   A CB    
1089  N  N     . ALA   A 68  ? 0.2542 0.2275 0.3046 0.0636  -0.1304 -0.0162 93  ALA   A N     
1090  C  CA    . ALA   A 68  ? 0.2591 0.2257 0.2984 0.0455  -0.1035 -0.0039 93  ALA   A CA    
1091  C  C     . ALA   A 68  ? 0.3112 0.2177 0.3032 0.0656  -0.1080 0.0045  93  ALA   A C     
1092  O  O     . ALA   A 68  ? 0.3320 0.2008 0.3118 0.0779  -0.1166 -0.0052 93  ALA   A O     
1093  C  CB    . ALA   A 68  ? 0.2486 0.2234 0.2897 0.0439  -0.0550 -0.0028 93  ALA   A CB    
1099  N  N     . ASP   A 69  ? 0.3249 0.2194 0.2999 0.0535  -0.0951 -0.0017 94  ASP   A N     
1100  C  CA    . ASP   A 69  ? 0.3364 0.2040 0.2909 0.0539  -0.1110 -0.0005 94  ASP   A CA    
1101  C  C     . ASP   A 69  ? 0.3676 0.1916 0.3040 0.0689  -0.1307 -0.0088 94  ASP   A C     
1102  O  O     . ASP   A 69  ? 0.3745 0.1902 0.3089 0.0464  -0.1241 -0.0018 94  ASP   A O     
1103  C  CB    . ASP   A 69  ? 0.3306 0.2265 0.2783 0.0473  -0.0846 -0.0088 94  ASP   A CB    
1104  C  CG    . ASP   A 69  ? 0.3378 0.2599 0.2797 0.0603  -0.0829 -0.0198 94  ASP   A CG    
1105  O  OD1   . ASP   A 69  ? 0.3314 0.2797 0.2924 0.0464  -0.0798 0.0028  94  ASP   A OD1   
1106  O  OD2   . ASP   A 69  ? 0.3202 0.3045 0.2888 0.0939  -0.0724 -0.0208 94  ASP   A OD2   
1111  N  N     . ASN   A 70  ? 0.3729 0.1908 0.3002 0.0863  -0.1481 -0.0181 95  ASN   A N     
1112  C  CA    . ASN   A 70  ? 0.4041 0.2289 0.3198 0.1132  -0.1647 -0.0173 95  ASN   A CA    
1113  C  C     . ASN   A 70  ? 0.4124 0.2203 0.3147 0.1197  -0.1494 -0.0144 95  ASN   A C     
1114  O  O     . ASN   A 70  ? 0.4236 0.2212 0.3280 0.1036  -0.1495 -0.0097 95  ASN   A O     
1115  C  CB    . ASN   A 70  ? 0.4215 0.2397 0.3441 0.1120  -0.1815 -0.0221 95  ASN   A CB    
1116  C  CG    . ASN   A 70  ? 0.4470 0.2571 0.3685 0.1198  -0.1800 -0.0164 95  ASN   A CG    
1117  O  OD1   . ASN   A 70  ? 0.4762 0.2384 0.3737 0.1102  -0.1862 -0.0242 95  ASN   A OD1   
1118  N  ND2   . ASN   A 70  ? 0.4250 0.2857 0.3724 0.1229  -0.1954 -0.0188 95  ASN   A ND2   
1125  N  N     . LYS   A 71  ? 0.3871 0.2368 0.3170 0.1350  -0.1374 -0.0284 96  LYS   A N     
1126  C  CA    . LYS   A 71  ? 0.3636 0.2467 0.3327 0.1052  -0.1230 -0.0312 96  LYS   A CA    
1127  C  C     . LYS   A 71  ? 0.3794 0.2147 0.3418 0.1178  -0.1259 -0.0207 96  LYS   A C     
1128  O  O     . LYS   A 71  ? 0.4293 0.2173 0.3544 0.1158  -0.1228 -0.0238 96  LYS   A O     
1129  C  CB    . LYS   A 71  ? 0.3398 0.2544 0.3456 0.1338  -0.1160 -0.0319 96  LYS   A CB    
1130  C  CG    . LYS   A 71  ? 0.3162 0.2456 0.3534 0.1372  -0.1226 -0.0478 96  LYS   A CG    
1131  C  CD    . LYS   A 71  ? 0.3397 0.2466 0.3717 0.1408  -0.1319 -0.0555 96  LYS   A CD    
1132  C  CE    . LYS   A 71  ? 0.3534 0.2733 0.3757 0.1348  -0.1402 -0.0502 96  LYS   A CE    
1133  N  NZ    . LYS   A 71  ? 0.4080 0.2782 0.3849 0.1335  -0.1504 -0.0377 96  LYS   A NZ    
1147  N  N     . GLN   A 72  ? 0.3620 0.2189 0.3474 0.1008  -0.1091 -0.0149 97  GLN   A N     
1148  C  CA    . GLN   A 72  ? 0.3831 0.2325 0.3415 0.0813  -0.1107 0.0122  97  GLN   A CA    
1149  C  C     . GLN   A 72  ? 0.4779 0.2352 0.3266 0.0713  -0.1162 0.0173  97  GLN   A C     
1150  O  O     . GLN   A 72  ? 0.5427 0.2697 0.3345 0.0816  -0.1027 0.0396  97  GLN   A O     
1151  C  CB    . GLN   A 72  ? 0.3666 0.2395 0.3523 0.0610  -0.0886 0.0246  97  GLN   A CB    
1152  C  CG    . GLN   A 72  ? 0.3370 0.2671 0.3545 0.0329  -0.0815 0.0274  97  GLN   A CG    
1153  C  CD    . GLN   A 72  ? 0.3809 0.2759 0.3664 0.0484  -0.0638 0.0344  97  GLN   A CD    
1154  O  OE1   . GLN   A 72  ? 0.3923 0.2899 0.3659 0.0537  -0.0711 0.0231  97  GLN   A OE1   
1155  N  NE2   . GLN   A 72  ? 0.4645 0.2841 0.3782 0.0196  -0.0351 0.0376  97  GLN   A NE2   
1164  N  N     . ARG   A 73  ? 0.4974 0.2321 0.3144 0.0968  -0.1479 0.0072  98  ARG   A N     
1165  C  CA    . ARG   A 73  ? 0.5301 0.2445 0.3276 0.1393  -0.1414 0.0053  98  ARG   A CA    
1166  C  C     . ARG   A 73  ? 0.5500 0.2601 0.3665 0.1450  -0.1533 0.0111  98  ARG   A C     
1167  O  O     . ARG   A 73  ? 0.5481 0.2983 0.3775 0.1507  -0.1450 0.0216  98  ARG   A O     
1168  C  CB    . ARG   A 73  ? 0.5558 0.2731 0.3035 0.1309  -0.1532 -0.0205 98  ARG   A CB    
1169  C  CG    . ARG   A 73  ? 0.6156 0.2935 0.3100 0.1274  -0.1570 -0.0276 98  ARG   A CG    
1170  C  CD    . ARG   A 73  ? 0.6252 0.2920 0.3173 0.1101  -0.1808 -0.0384 98  ARG   A CD    
1171  N  NE    . ARG   A 73  ? 0.6375 0.2901 0.3490 0.1269  -0.1959 -0.0219 98  ARG   A NE    
1172  C  CZ    . ARG   A 73  ? 0.6354 0.3001 0.3659 0.1402  -0.2330 -0.0323 98  ARG   A CZ    
1173  N  NH1   . ARG   A 73  ? 0.6012 0.2988 0.3839 0.1540  -0.2346 -0.0481 98  ARG   A NH1   
1174  N  NH2   . ARG   A 73  ? 0.6925 0.3020 0.3707 0.1426  -0.2346 -0.0317 98  ARG   A NH2   
1188  N  N     . ASP   A 74  ? 0.5264 0.2415 0.3838 0.1322  -0.1666 -0.0065 99  ASP   A N     
1189  C  CA    . ASP   A 74  ? 0.5381 0.2395 0.3943 0.1371  -0.1776 -0.0246 99  ASP   A CA    
1190  C  C     . ASP   A 74  ? 0.5191 0.2373 0.3965 0.1359  -0.1751 -0.0251 99  ASP   A C     
1191  O  O     . ASP   A 74  ? 0.4873 0.2247 0.3771 0.1195  -0.1695 -0.0259 99  ASP   A O     
1192  C  CB    . ASP   A 74  ? 0.5463 0.2644 0.4069 0.1395  -0.2131 -0.0398 99  ASP   A CB    
1193  C  CG    . ASP   A 74  ? 0.5884 0.2817 0.4400 0.1355  -0.2282 -0.0477 99  ASP   A CG    
1194  O  OD1   . ASP   A 74  ? 0.5991 0.3079 0.4370 0.1405  -0.2293 -0.0569 99  ASP   A OD1   
1195  O  OD2   . ASP   A 74  ? 0.6000 0.3082 0.4738 0.1185  -0.2320 -0.0682 99  ASP   A OD2   
1200  N  N     . PRO   A 75  ? 0.5186 0.2411 0.4261 0.1290  -0.1858 -0.0581 100 PRO   A N     
1201  C  CA    . PRO   A 75  ? 0.5290 0.2640 0.4438 0.1290  -0.2026 -0.0664 100 PRO   A CA    
1202  C  C     . PRO   A 75  ? 0.5088 0.2709 0.4467 0.1468  -0.2203 -0.0592 100 PRO   A C     
1203  O  O     . PRO   A 75  ? 0.5221 0.2705 0.4446 0.1476  -0.2099 -0.0414 100 PRO   A O     
1204  C  CB    . PRO   A 75  ? 0.5449 0.2991 0.4537 0.1215  -0.1964 -0.0732 100 PRO   A CB    
1205  C  CG    . PRO   A 75  ? 0.5792 0.3119 0.4548 0.0872  -0.2006 -0.0708 100 PRO   A CG    
1206  C  CD    . PRO   A 75  ? 0.5692 0.2876 0.4458 0.1154  -0.1861 -0.0658 100 PRO   A CD    
1214  N  N     . LYS   A 76  ? 0.5107 0.2911 0.4486 0.1556  -0.2100 -0.0373 101 LYS   A N     
1215  C  CA    . LYS   A 76  ? 0.5321 0.3147 0.4664 0.1620  -0.2323 -0.0470 101 LYS   A CA    
1216  C  C     . LYS   A 76  ? 0.4767 0.3340 0.4883 0.1604  -0.2330 -0.0613 101 LYS   A C     
1217  O  O     . LYS   A 76  ? 0.4946 0.3634 0.5166 0.1921  -0.2220 -0.0771 101 LYS   A O     
1218  C  CB    . LYS   A 76  ? 0.6339 0.3302 0.4485 0.1759  -0.2406 -0.0366 101 LYS   A CB    
1219  C  CG    . LYS   A 76  ? 0.6830 0.3600 0.4508 0.1697  -0.2577 -0.0482 101 LYS   A CG    
1220  C  CD    . LYS   A 76  ? 0.7275 0.4043 0.4687 0.1983  -0.2351 -0.0144 101 LYS   A CD    
1221  C  CE    . LYS   A 76  ? 0.7614 0.4613 0.4809 0.1963  -0.2122 -0.0112 101 LYS   A CE    
1222  N  NZ    . LYS   A 76  ? 0.7681 0.4906 0.4911 0.1729  -0.2000 -0.0183 101 LYS   A NZ    
1236  N  N     . MET   A 77  ? 0.4430 0.2847 0.4711 0.1405  -0.2118 -0.0508 102 MET   A N     
1237  C  CA    . MET   A 77  ? 0.3985 0.2813 0.4727 0.1250  -0.2089 -0.0486 102 MET   A CA    
1238  C  C     . MET   A 77  ? 0.3707 0.3002 0.5067 0.1198  -0.2024 -0.0690 102 MET   A C     
1239  O  O     . MET   A 77  ? 0.3450 0.2759 0.5059 0.0951  -0.1929 -0.0953 102 MET   A O     
1240  C  CB    . MET   A 77  ? 0.3749 0.2408 0.4340 0.1176  -0.1757 -0.0348 102 MET   A CB    
1241  C  CG    . MET   A 77  ? 0.3610 0.2643 0.4216 0.1243  -0.1840 -0.0539 102 MET   A CG    
1242  S  SD    . MET   A 77  ? 0.3832 0.2810 0.4295 0.1300  -0.1805 -0.0512 102 MET   A SD    
1243  C  CE    . MET   A 77  ? 0.4045 0.2675 0.4450 0.1085  -0.1632 -0.0224 102 MET   A CE    
1253  N  N     . SER   A 78  ? 0.3439 0.3199 0.5344 0.1259  -0.1993 -0.0752 103 SER   A N     
1254  C  CA    . SER   A 78  ? 0.3105 0.3481 0.5724 0.1279  -0.1779 -0.0984 103 SER   A CA    
1255  C  C     . SER   A 78  ? 0.2928 0.3403 0.5803 0.1055  -0.1787 -0.1061 103 SER   A C     
1256  O  O     . SER   A 78  ? 0.2794 0.3351 0.5920 0.1131  -0.1574 -0.1108 103 SER   A O     
1257  C  CB    . SER   A 78  ? 0.3050 0.3693 0.5883 0.1252  -0.1823 -0.1241 103 SER   A CB    
1258  O  OG    . SER   A 78  ? 0.3116 0.3937 0.6294 0.1296  -0.1848 -0.1557 103 SER   A OG    
1264  N  N     . CYS   A 79  ? 0.2919 0.3411 0.5683 0.1207  -0.1688 -0.1171 104 CYS   A N     
1265  C  CA    . CYS   A 79  ? 0.2576 0.3531 0.5816 0.1035  -0.1501 -0.1166 104 CYS   A CA    
1266  C  C     . CYS   A 79  ? 0.2381 0.3250 0.5482 0.0881  -0.1448 -0.0880 104 CYS   A C     
1267  O  O     . CYS   A 79  ? 0.2707 0.2969 0.5270 0.0960  -0.1673 -0.0748 104 CYS   A O     
1268  C  CB    . CYS   A 79  ? 0.2858 0.4215 0.6223 0.1505  -0.1149 -0.1120 104 CYS   A CB    
1269  S  SG    . CYS   A 79  ? 0.3565 0.4549 0.7259 0.1416  -0.1050 -0.1273 104 CYS   A SG    
1275  N  N     . ILE   A 80  ? 0.1925 0.2873 0.5263 0.0673  -0.1026 -0.0917 105 ILE   A N     
1276  C  CA    . ILE   A 80  ? 0.1812 0.2901 0.5005 0.0498  -0.1109 -0.0766 105 ILE   A CA    
1277  C  C     . ILE   A 80  ? 0.1833 0.2887 0.5305 0.0457  -0.1090 -0.0786 105 ILE   A C     
1278  O  O     . ILE   A 80  ? 0.1744 0.3077 0.5580 0.0253  -0.0904 -0.0984 105 ILE   A O     
1279  C  CB    . ILE   A 80  ? 0.1809 0.2750 0.4501 0.0716  -0.1007 -0.0562 105 ILE   A CB    
1280  C  CG1   . ILE   A 80  ? 0.1926 0.2898 0.4485 0.0624  -0.0841 -0.0434 105 ILE   A CG1   
1281  C  CG2   . ILE   A 80  ? 0.1817 0.2954 0.4437 0.0768  -0.1005 -0.0578 105 ILE   A CG2   
1282  C  CD1   . ILE   A 80  ? 0.1857 0.3019 0.4375 0.0515  -0.0764 -0.0280 105 ILE   A CD1   
1294  N  N     . ARG   A 81  ? 0.1954 0.2848 0.5497 0.0377  -0.1260 -0.0748 106 ARG   A N     
1295  C  CA    . ARG   A 81  ? 0.1762 0.2833 0.5658 0.0428  -0.0864 -0.0676 106 ARG   A CA    
1296  C  C     . ARG   A 81  ? 0.1806 0.2799 0.5944 0.0436  -0.0803 -0.0644 106 ARG   A C     
1297  O  O     . ARG   A 81  ? 0.1990 0.2651 0.6126 0.0457  -0.1061 -0.0691 106 ARG   A O     
1298  C  CB    . ARG   A 81  ? 0.1940 0.3128 0.5738 0.0697  -0.0878 -0.0665 106 ARG   A CB    
1299  C  CG    . ARG   A 81  ? 0.2062 0.3505 0.5918 0.0830  -0.0925 -0.0570 106 ARG   A CG    
1300  C  CD    . ARG   A 81  ? 0.2406 0.3954 0.6211 0.1215  -0.0899 -0.0367 106 ARG   A CD    
1301  N  NE    . ARG   A 81  ? 0.2434 0.4402 0.6665 0.1224  -0.0889 -0.0445 106 ARG   A NE    
1302  C  CZ    . ARG   A 81  ? 0.2525 0.4362 0.6924 0.1229  -0.0910 -0.0611 106 ARG   A CZ    
1303  N  NH1   . ARG   A 81  ? 0.2671 0.4508 0.7078 0.1310  -0.0806 -0.0470 106 ARG   A NH1   
1304  N  NH2   . ARG   A 81  ? 0.2886 0.4342 0.7011 0.0818  -0.1104 -0.0817 106 ARG   A NH2   
1318  N  N     . VAL   A 82  ? 0.1808 0.2650 0.5990 0.0497  -0.0598 -0.0315 107 VAL   A N     
1319  C  CA    . VAL   A 82  ? 0.1647 0.2747 0.6295 0.0080  -0.0457 -0.0318 107 VAL   A CA    
1320  C  C     . VAL   A 82  ? 0.1696 0.2979 0.6462 -0.0093 -0.0421 -0.0437 107 VAL   A C     
1321  O  O     . VAL   A 82  ? 0.1754 0.3035 0.6657 -0.0071 -0.0383 -0.0696 107 VAL   A O     
1322  C  CB    . VAL   A 82  ? 0.1625 0.2792 0.6169 0.0216  -0.0376 -0.0127 107 VAL   A CB    
1323  C  CG1   . VAL   A 82  ? 0.1650 0.2878 0.6230 0.0276  -0.0306 0.0020  107 VAL   A CG1   
1324  C  CG2   . VAL   A 82  ? 0.1563 0.2804 0.5996 -0.0080 -0.0425 -0.0012 107 VAL   A CG2   
1334  N  N     . THR   A 83  ? 0.1734 0.3081 0.6613 0.0043  -0.0471 -0.0478 108 THR   A N     
1335  C  CA    . THR   A 83  ? 0.1830 0.3045 0.6774 0.0117  -0.0656 -0.0534 108 THR   A CA    
1336  C  C     . THR   A 83  ? 0.1934 0.2891 0.6682 0.0299  -0.0773 -0.0580 108 THR   A C     
1337  O  O     . THR   A 83  ? 0.2212 0.2847 0.6642 0.0551  -0.0927 -0.0505 108 THR   A O     
1338  C  CB    . THR   A 83  ? 0.1952 0.3150 0.6974 0.0010  -0.0861 -0.0519 108 THR   A CB    
1339  O  OG1   . THR   A 83  ? 0.2081 0.3465 0.7198 0.0179  -0.1038 -0.0456 108 THR   A OG1   
1340  C  CG2   . THR   A 83  ? 0.2158 0.3393 0.7195 -0.0402 -0.0613 -0.0558 108 THR   A CG2   
1348  N  N     . ILE   A 84  ? 0.1763 0.2820 0.6548 0.0178  -0.0576 -0.0541 109 ILE   A N     
1349  C  CA    . ILE   A 84  ? 0.1696 0.2911 0.6531 0.0009  -0.0411 -0.0398 109 ILE   A CA    
1350  C  C     . ILE   A 84  ? 0.1709 0.3007 0.6645 -0.0005 -0.0258 -0.0566 109 ILE   A C     
1351  O  O     . ILE   A 84  ? 0.2246 0.3157 0.6830 -0.0180 -0.0191 -0.0736 109 ILE   A O     
1352  C  CB    . ILE   A 84  ? 0.1803 0.2944 0.6783 -0.0045 -0.0449 -0.0307 109 ILE   A CB    
1353  C  CG1   . ILE   A 84  ? 0.2115 0.2915 0.6899 0.0056  -0.0905 -0.0446 109 ILE   A CG1   
1354  C  CG2   . ILE   A 84  ? 0.1841 0.3129 0.6836 -0.0019 -0.0404 -0.0117 109 ILE   A CG2   
1355  C  CD1   . ILE   A 84  ? 0.2401 0.3061 0.7043 0.0452  -0.1227 -0.0357 109 ILE   A CD1   
1367  N  N     . ASP   A 85  ? 0.1792 0.3403 0.6823 0.0145  -0.0449 -0.0558 110 ASP   A N     
1368  C  CA    . ASP   A 85  ? 0.1897 0.3638 0.7044 -0.0103 -0.0583 -0.0424 110 ASP   A CA    
1369  C  C     . ASP   A 85  ? 0.2289 0.3496 0.7030 -0.0275 -0.0665 -0.0306 110 ASP   A C     
1370  O  O     . ASP   A 85  ? 0.2280 0.3523 0.6932 -0.0201 -0.0625 -0.0397 110 ASP   A O     
1371  C  CB    . ASP   A 85  ? 0.2201 0.4068 0.7279 -0.0055 -0.0742 -0.0521 110 ASP   A CB    
1372  C  CG    . ASP   A 85  ? 0.2367 0.4556 0.7496 0.0060  -0.0894 -0.0677 110 ASP   A CG    
1373  O  OD1   . ASP   A 85  ? 0.2614 0.4564 0.7608 -0.0011 -0.0954 -0.0698 110 ASP   A OD1   
1374  O  OD2   . ASP   A 85  ? 0.2876 0.4973 0.7563 0.0001  -0.0964 -0.0864 110 ASP   A OD2   
1379  N  N     . PRO   A 86  ? 0.2087 0.2996 0.7076 -0.0392 -0.0835 -0.0118 111 PRO   A N     
1380  C  CA    . PRO   A 86  ? 0.2201 0.2980 0.7242 -0.0331 -0.1000 -0.0342 111 PRO   A CA    
1381  C  C     . PRO   A 86  ? 0.2601 0.3198 0.7478 -0.0329 -0.1162 -0.0613 111 PRO   A C     
1382  O  O     . PRO   A 86  ? 0.3238 0.3137 0.7527 0.0020  -0.1289 -0.0759 111 PRO   A O     
1383  C  CB    . PRO   A 86  ? 0.2157 0.2925 0.7209 -0.0352 -0.0824 -0.0202 111 PRO   A CB    
1384  C  CG    . PRO   A 86  ? 0.2063 0.2856 0.7140 -0.0213 -0.0815 -0.0150 111 PRO   A CG    
1385  C  CD    . PRO   A 86  ? 0.2130 0.2853 0.7109 -0.0110 -0.0788 -0.0113 111 PRO   A CD    
1393  N  N     . GLU   A 87  ? 0.3060 0.3692 0.7601 -0.0711 -0.1284 -0.0562 112 GLU   A N     
1394  C  CA    . GLU   A 87  ? 0.3654 0.4337 0.7738 -0.1247 -0.1131 -0.0458 112 GLU   A CA    
1395  C  C     . GLU   A 87  ? 0.4085 0.4025 0.7686 -0.1107 -0.1026 -0.0348 112 GLU   A C     
1396  O  O     . GLU   A 87  ? 0.4660 0.3877 0.7702 -0.1101 -0.0975 -0.0340 112 GLU   A O     
1397  C  CB    . GLU   A 87  ? 0.4125 0.5582 0.7971 -0.1533 -0.0895 -0.0333 112 GLU   A CB    
1398  C  CG    . GLU   A 87  ? 0.4155 0.6720 0.8172 -0.1717 -0.0827 -0.0272 112 GLU   A CG    
1399  C  CD    . GLU   A 87  ? 0.4838 0.7977 0.8365 -0.1230 -0.0639 -0.0249 112 GLU   A CD    
1400  O  OE1   . GLU   A 87  ? 0.5069 0.8417 0.8475 -0.1236 -0.0650 -0.0207 112 GLU   A OE1   
1401  O  OE2   . GLU   A 87  ? 0.5095 0.8421 0.8412 -0.0822 -0.0435 -0.0329 112 GLU   A OE2   
1408  N  N     . ASN   A 88  ? 0.3546 0.3929 0.7601 -0.1186 -0.1063 -0.0381 113 ASN   A N     
1409  C  CA    . ASN   A 88  ? 0.3124 0.4007 0.7479 -0.0829 -0.1262 -0.0521 113 ASN   A CA    
1410  C  C     . ASN   A 88  ? 0.2919 0.3413 0.7326 -0.0470 -0.1076 -0.0468 113 ASN   A C     
1411  O  O     . ASN   A 88  ? 0.3094 0.3256 0.7403 -0.0282 -0.1237 -0.0592 113 ASN   A O     
1412  C  CB    . ASN   A 88  ? 0.2883 0.4812 0.7589 -0.0832 -0.1404 -0.0643 113 ASN   A CB    
1413  C  CG    . ASN   A 88  ? 0.3650 0.5478 0.7802 -0.0985 -0.1381 -0.0705 113 ASN   A CG    
1414  O  OD1   . ASN   A 88  ? 0.4208 0.5631 0.7906 -0.1426 -0.1362 -0.0759 113 ASN   A OD1   
1415  N  ND2   . ASN   A 88  ? 0.3516 0.5841 0.7901 -0.0671 -0.1366 -0.0635 113 ASN   A ND2   
1422  N  N     . ASN   A 89  ? 0.2675 0.3239 0.7079 -0.0272 -0.1139 -0.0337 114 ASN   A N     
1423  C  CA    . ASN   A 89  ? 0.2526 0.3137 0.7009 0.0125  -0.0989 -0.0417 114 ASN   A CA    
1424  C  C     . ASN   A 89  ? 0.2430 0.3050 0.6801 -0.0033 -0.0987 -0.0468 114 ASN   A C     
1425  O  O     . ASN   A 89  ? 0.2298 0.2798 0.6844 -0.0099 -0.1193 -0.0331 114 ASN   A O     
1426  C  CB    . ASN   A 89  ? 0.2508 0.3124 0.7094 -0.0029 -0.1356 -0.0620 114 ASN   A CB    
1427  C  CG    . ASN   A 89  ? 0.2914 0.3203 0.7114 -0.0021 -0.1895 -0.0596 114 ASN   A CG    
1428  O  OD1   . ASN   A 89  ? 0.3380 0.3500 0.7130 0.0395  -0.2304 -0.0654 114 ASN   A OD1   
1429  N  ND2   . ASN   A 89  ? 0.2996 0.2939 0.7109 0.0062  -0.1775 -0.0504 114 ASN   A ND2   
1436  N  N     . LEU   A 90  ? 0.2159 0.3049 0.6500 -0.0130 -0.1048 -0.0755 115 LEU   A N     
1437  C  CA    . LEU   A 90  ? 0.2416 0.3601 0.6331 -0.0259 -0.1333 -0.0757 115 LEU   A CA    
1438  C  C     . LEU   A 90  ? 0.2363 0.3038 0.6048 0.0113  -0.1113 -0.0709 115 LEU   A C     
1439  O  O     . LEU   A 90  ? 0.2641 0.3101 0.6148 -0.0177 -0.0805 -0.0676 115 LEU   A O     
1440  C  CB    . LEU   A 90  ? 0.3059 0.4582 0.6529 -0.0600 -0.1481 -0.0618 115 LEU   A CB    
1441  C  CG    . LEU   A 90  ? 0.4059 0.5574 0.6803 -0.0462 -0.1512 -0.0303 115 LEU   A CG    
1442  C  CD1   . LEU   A 90  ? 0.4396 0.5954 0.6834 -0.0270 -0.1736 -0.0348 115 LEU   A CD1   
1443  C  CD2   . LEU   A 90  ? 0.4620 0.5852 0.6953 -0.0468 -0.1503 0.0003  115 LEU   A CD2   
1455  N  N     . ILE   A 91  ? 0.2104 0.2589 0.5674 0.0337  -0.1430 -0.0707 116 ILE   A N     
1456  C  CA    . ILE   A 91  ? 0.1931 0.2445 0.5348 0.0142  -0.1275 -0.0761 116 ILE   A CA    
1457  C  C     . ILE   A 91  ? 0.2001 0.2549 0.5421 0.0288  -0.1301 -0.1049 116 ILE   A C     
1458  O  O     . ILE   A 91  ? 0.2253 0.2495 0.5359 0.0219  -0.0963 -0.1020 116 ILE   A O     
1459  C  CB    . ILE   A 91  ? 0.1829 0.2461 0.5329 -0.0176 -0.1019 -0.0637 116 ILE   A CB    
1460  C  CG1   . ILE   A 91  ? 0.1802 0.2812 0.5419 -0.0101 -0.0988 -0.0310 116 ILE   A CG1   
1461  C  CG2   . ILE   A 91  ? 0.1933 0.2559 0.5305 0.0015  -0.0991 -0.0706 116 ILE   A CG2   
1462  C  CD1   . ILE   A 91  ? 0.1835 0.3046 0.5491 -0.0339 -0.0798 -0.0219 116 ILE   A CD1   
1474  N  N     . SER   A 92  ? 0.2085 0.2863 0.5487 0.0403  -0.1277 -0.1107 117 SER   A N     
1475  C  CA    . SER   A 92  ? 0.2306 0.2843 0.5403 0.0679  -0.1517 -0.0843 117 SER   A CA    
1476  C  C     . SER   A 92  ? 0.2526 0.2623 0.5332 0.0515  -0.1720 -0.0926 117 SER   A C     
1477  O  O     . SER   A 92  ? 0.3117 0.2752 0.5429 0.0503  -0.1799 -0.0889 117 SER   A O     
1478  C  CB    . SER   A 92  ? 0.2564 0.3292 0.5784 0.0721  -0.1734 -0.0712 117 SER   A CB    
1479  O  OG    . SER   A 92  ? 0.2951 0.3640 0.6167 0.0610  -0.1746 -0.0689 117 SER   A OG    
1485  N  N     . ILE   A 93  ? 0.2320 0.2478 0.5149 0.0447  -0.1661 -0.0843 118 ILE   A N     
1486  C  CA    . ILE   A 93  ? 0.2495 0.2572 0.4971 0.0626  -0.1735 -0.0679 118 ILE   A CA    
1487  C  C     . ILE   A 93  ? 0.2912 0.2710 0.4983 0.0785  -0.1910 -0.0748 118 ILE   A C     
1488  O  O     . ILE   A 93  ? 0.3294 0.2664 0.4744 0.0783  -0.2165 -0.0614 118 ILE   A O     
1489  C  CB    . ILE   A 93  ? 0.2545 0.2717 0.5006 0.0589  -0.1754 -0.0333 118 ILE   A CB    
1490  C  CG1   . ILE   A 93  ? 0.2207 0.2635 0.4873 0.0588  -0.1450 -0.0240 118 ILE   A CG1   
1491  C  CG2   . ILE   A 93  ? 0.2727 0.2879 0.4998 0.0394  -0.1958 -0.0176 118 ILE   A CG2   
1492  C  CD1   . ILE   A 93  ? 0.2206 0.2746 0.5056 0.0427  -0.1335 0.0063  118 ILE   A CD1   
1504  N  N     . TRP   A 94  ? 0.2913 0.2546 0.5048 0.0739  -0.1977 -0.0702 119 TRP   A N     
1505  C  CA    . TRP   A 94  ? 0.3078 0.2660 0.4952 0.0888  -0.2012 -0.0796 119 TRP   A CA    
1506  C  C     . TRP   A 94  ? 0.3151 0.2688 0.4793 0.0943  -0.1999 -0.0725 119 TRP   A C     
1507  O  O     . TRP   A 94  ? 0.3117 0.3076 0.5044 0.0873  -0.2087 -0.0786 119 TRP   A O     
1508  C  CB    . TRP   A 94  ? 0.3134 0.2906 0.5229 0.1049  -0.1988 -0.0990 119 TRP   A CB    
1509  C  CG    . TRP   A 94  ? 0.3116 0.3363 0.5562 0.0991  -0.2095 -0.1211 119 TRP   A CG    
1510  C  CD1   . TRP   A 94  ? 0.3520 0.3877 0.5870 0.1296  -0.2243 -0.1279 119 TRP   A CD1   
1511  C  CD2   . TRP   A 94  ? 0.3433 0.3647 0.5911 0.1187  -0.2226 -0.1176 119 TRP   A CD2   
1512  N  NE1   . TRP   A 94  ? 0.3917 0.4064 0.6119 0.1451  -0.2387 -0.1209 119 TRP   A NE1   
1513  C  CE2   . TRP   A 94  ? 0.3650 0.3903 0.6073 0.1334  -0.2317 -0.1278 119 TRP   A CE2   
1514  C  CE3   . TRP   A 94  ? 0.3405 0.3653 0.6043 0.1306  -0.2069 -0.1118 119 TRP   A CE3   
1515  C  CZ2   . TRP   A 94  ? 0.3869 0.4155 0.6276 0.1509  -0.2328 -0.1143 119 TRP   A CZ2   
1516  C  CZ3   . TRP   A 94  ? 0.3617 0.3741 0.6209 0.1405  -0.2140 -0.1085 119 TRP   A CZ3   
1517  C  CH2   . TRP   A 94  ? 0.3636 0.3968 0.6306 0.1430  -0.2178 -0.1180 119 TRP   A CH2   
1528  N  N     . ASN   A 95  ? 0.3217 0.2646 0.4611 0.1078  -0.1909 -0.0784 120 ASN   A N     
1529  C  CA    . ASN   A 95  ? 0.3437 0.2642 0.4422 0.1087  -0.2042 -0.0809 120 ASN   A CA    
1530  C  C     . ASN   A 95  ? 0.4196 0.2901 0.4658 0.1239  -0.2404 -0.0888 120 ASN   A C     
1531  O  O     . ASN   A 95  ? 0.4782 0.3004 0.4877 0.1345  -0.2560 -0.1051 120 ASN   A O     
1532  C  CB    . ASN   A 95  ? 0.3760 0.2654 0.4462 0.0998  -0.2070 -0.0689 120 ASN   A CB    
1533  C  CG    . ASN   A 95  ? 0.3955 0.2590 0.4382 0.1090  -0.2085 -0.0534 120 ASN   A CG    
1534  O  OD1   . ASN   A 95  ? 0.3860 0.2488 0.4532 0.0967  -0.2159 -0.0536 120 ASN   A OD1   
1535  N  ND2   . ASN   A 95  ? 0.4343 0.2733 0.4018 0.1406  -0.1886 -0.0358 120 ASN   A ND2   
1542  N  N     . ASN   A 96  ? 0.4408 0.2952 0.4746 0.1342  -0.2329 -0.0664 121 ASN   A N     
1543  C  CA    . ASN   A 96  ? 0.4279 0.3022 0.4815 0.1334  -0.2391 -0.0857 121 ASN   A CA    
1544  C  C     . ASN   A 96  ? 0.4739 0.2713 0.4798 0.1241  -0.2559 -0.0803 121 ASN   A C     
1545  O  O     . ASN   A 96  ? 0.5028 0.2746 0.4823 0.1145  -0.2683 -0.0675 121 ASN   A O     
1546  C  CB    . ASN   A 96  ? 0.4377 0.3332 0.5167 0.1601  -0.2385 -0.1187 121 ASN   A CB    
1547  C  CG    . ASN   A 96  ? 0.4397 0.3457 0.5494 0.1701  -0.2316 -0.1272 121 ASN   A CG    
1548  O  OD1   . ASN   A 96  ? 0.4226 0.3412 0.5374 0.1627  -0.2269 -0.1169 121 ASN   A OD1   
1549  N  ND2   . ASN   A 96  ? 0.4464 0.3860 0.5715 0.1510  -0.2548 -0.1300 121 ASN   A ND2   
1556  N  N     . GLY   A 97  ? 0.5119 0.2465 0.4837 0.1200  -0.2376 -0.0575 122 GLY   A N     
1557  C  CA    . GLY   A 97  ? 0.5619 0.2627 0.4837 0.1400  -0.2382 -0.0655 122 GLY   A CA    
1558  C  C     . GLY   A 97  ? 0.5975 0.2796 0.4839 0.1473  -0.2649 -0.0766 122 GLY   A C     
1559  O  O     . GLY   A 97  ? 0.6007 0.2827 0.4985 0.1278  -0.2923 -0.0806 122 GLY   A O     
1563  N  N     . LYS   A 98  ? 0.6295 0.2929 0.4722 0.1611  -0.2566 -0.0676 123 LYS   A N     
1564  C  CA    . LYS   A 98  ? 0.6691 0.3159 0.4582 0.1544  -0.2752 -0.0485 123 LYS   A CA    
1565  C  C     . LYS   A 98  ? 0.6697 0.3215 0.4490 0.1609  -0.2864 -0.0724 123 LYS   A C     
1566  O  O     . LYS   A 98  ? 0.6608 0.3013 0.4385 0.1561  -0.2665 -0.0585 123 LYS   A O     
1567  C  CB    . LYS   A 98  ? 0.7555 0.3830 0.4665 0.1715  -0.2763 -0.0159 123 LYS   A CB    
1568  C  CG    . LYS   A 98  ? 0.8266 0.4429 0.4812 0.1467  -0.2608 -0.0002 123 LYS   A CG    
1569  C  CD    . LYS   A 98  ? 0.8820 0.4961 0.4977 0.1412  -0.2455 0.0178  123 LYS   A CD    
1570  C  CE    . LYS   A 98  ? 0.9188 0.5589 0.5216 0.1372  -0.2195 0.0226  123 LYS   A CE    
1571  N  NZ    . LYS   A 98  ? 0.9437 0.5987 0.5449 0.1260  -0.1838 0.0191  123 LYS   A NZ    
1585  N  N     . GLY   A 99  ? 0.6648 0.3298 0.4572 0.1759  -0.2854 -0.0859 124 GLY   A N     
1586  C  CA    . GLY   A 99  ? 0.6615 0.3231 0.4550 0.1656  -0.2921 -0.0872 124 GLY   A CA    
1587  C  C     . GLY   A 99  ? 0.6960 0.3182 0.4576 0.1554  -0.3007 -0.0767 124 GLY   A C     
1588  O  O     . GLY   A 99  ? 0.7512 0.3080 0.4792 0.1615  -0.2740 -0.0718 124 GLY   A O     
1592  N  N     . ILE   A 100 ? 0.6587 0.3198 0.4473 0.1486  -0.2949 -0.0770 125 ILE   A N     
1593  C  CA    . ILE   A 100 ? 0.6582 0.3254 0.4403 0.1355  -0.2943 -0.0646 125 ILE   A CA    
1594  C  C     . ILE   A 100 ? 0.6832 0.3405 0.4455 0.1377  -0.2969 -0.0539 125 ILE   A C     
1595  O  O     . ILE   A 100 ? 0.6874 0.3663 0.4498 0.1372  -0.3082 -0.0777 125 ILE   A O     
1596  C  CB    . ILE   A 100 ? 0.6705 0.3172 0.4319 0.1343  -0.2884 -0.0553 125 ILE   A CB    
1597  C  CG1   . ILE   A 100 ? 0.6561 0.3404 0.4317 0.1317  -0.2846 -0.0479 125 ILE   A CG1   
1598  C  CG2   . ILE   A 100 ? 0.6798 0.3024 0.4280 0.1303  -0.2905 -0.0599 125 ILE   A CG2   
1599  C  CD1   . ILE   A 100 ? 0.6374 0.3395 0.4361 0.1292  -0.2699 -0.0161 125 ILE   A CD1   
1611  N  N     . PRO   A 101 ? 0.6995 0.3447 0.4441 0.1309  -0.2982 -0.0437 126 PRO   A N     
1612  C  CA    . PRO   A 101 ? 0.7334 0.3508 0.4465 0.1231  -0.3106 -0.0499 126 PRO   A CA    
1613  C  C     . PRO   A 101 ? 0.7737 0.3354 0.4477 0.1422  -0.3137 -0.0658 126 PRO   A C     
1614  O  O     . PRO   A 101 ? 0.8202 0.3271 0.4396 0.1479  -0.3057 -0.0578 126 PRO   A O     
1615  C  CB    . PRO   A 101 ? 0.7595 0.3723 0.4506 0.1287  -0.3075 -0.0308 126 PRO   A CB    
1616  C  CG    . PRO   A 101 ? 0.7599 0.3841 0.4520 0.1133  -0.3106 -0.0291 126 PRO   A CG    
1617  C  CD    . PRO   A 101 ? 0.7399 0.3722 0.4474 0.1271  -0.2983 -0.0188 126 PRO   A CD    
1625  N  N     . VAL   A 102 ? 0.7322 0.3189 0.4604 0.1470  -0.3128 -0.0743 127 VAL   A N     
1626  C  CA    . VAL   A 102 ? 0.7542 0.3265 0.4605 0.1377  -0.3186 -0.0664 127 VAL   A CA    
1627  C  C     . VAL   A 102 ? 0.7678 0.3335 0.4637 0.1225  -0.3208 -0.0469 127 VAL   A C     
1628  O  O     . VAL   A 102 ? 0.7819 0.3430 0.4739 0.1210  -0.3259 -0.0403 127 VAL   A O     
1629  C  CB    . VAL   A 102 ? 0.7337 0.3276 0.4655 0.1447  -0.3158 -0.0700 127 VAL   A CB    
1630  C  CG1   . VAL   A 102 ? 0.7506 0.3118 0.4662 0.1551  -0.3087 -0.0749 127 VAL   A CG1   
1631  C  CG2   . VAL   A 102 ? 0.7337 0.3439 0.4766 0.1449  -0.3201 -0.0649 127 VAL   A CG2   
1641  N  N     . VAL   A 103 ? 0.7932 0.3452 0.4534 0.0950  -0.3228 -0.0292 128 VAL   A N     
1642  C  CA    . VAL   A 103 ? 0.8118 0.3526 0.4479 0.0831  -0.3231 -0.0231 128 VAL   A CA    
1643  C  C     . VAL   A 103 ? 0.8451 0.3549 0.4277 0.0814  -0.3094 -0.0134 128 VAL   A C     
1644  O  O     . VAL   A 103 ? 0.7918 0.3209 0.4186 0.0811  -0.2981 -0.0129 128 VAL   A O     
1645  C  CB    . VAL   A 103 ? 0.8037 0.3308 0.4605 0.0698  -0.3294 -0.0158 128 VAL   A CB    
1646  C  CG1   . VAL   A 103 ? 0.8196 0.3354 0.4645 0.0674  -0.3325 -0.0123 128 VAL   A CG1   
1647  C  CG2   . VAL   A 103 ? 0.8193 0.3425 0.4647 0.0572  -0.3318 -0.0179 128 VAL   A CG2   
1657  N  N     . GLU   A 104 ? 0.8971 0.3668 0.4015 0.0628  -0.2958 -0.0126 129 GLU   A N     
1658  C  CA    . GLU   A 104 ? 0.9294 0.3587 0.3781 0.0545  -0.2748 -0.0081 129 GLU   A CA    
1659  C  C     . GLU   A 104 ? 0.9564 0.3364 0.3650 0.0556  -0.2552 0.0000  129 GLU   A C     
1660  O  O     . GLU   A 104 ? 0.9624 0.3025 0.3762 0.0337  -0.2481 0.0173  129 GLU   A O     
1661  C  CB    . GLU   A 104 ? 0.9966 0.4289 0.3748 0.0689  -0.2604 0.0039  129 GLU   A CB    
1662  C  CG    . GLU   A 104 ? 1.0568 0.4952 0.3765 0.0736  -0.2575 -0.0078 129 GLU   A CG    
1663  C  CD    . GLU   A 104 ? 1.1353 0.5609 0.3937 0.0738  -0.2345 -0.0209 129 GLU   A CD    
1664  O  OE1   . GLU   A 104 ? 1.1692 0.6038 0.4092 0.0646  -0.2040 -0.0304 129 GLU   A OE1   
1665  O  OE2   . GLU   A 104 ? 1.1518 0.5878 0.3989 0.0729  -0.2338 -0.0218 129 GLU   A OE2   
1672  N  N     . HIS   A 105 ? 0.9097 0.3242 0.3572 0.0756  -0.2448 -0.0003 130 HIS   A N     
1673  C  CA    . HIS   A 105 ? 0.9115 0.3530 0.3479 0.0886  -0.2132 0.0244  130 HIS   A CA    
1674  C  C     . HIS   A 105 ? 0.9519 0.3824 0.3494 0.0856  -0.2101 0.0312  130 HIS   A C     
1675  O  O     . HIS   A 105 ? 1.0049 0.3929 0.3497 0.1036  -0.2096 0.0158  130 HIS   A O     
1676  C  CB    . HIS   A 105 ? 0.8651 0.3344 0.3373 0.0976  -0.1898 0.0320  130 HIS   A CB    
1677  C  CG    . HIS   A 105 ? 0.8882 0.3268 0.3197 0.1026  -0.1589 0.0322  130 HIS   A CG    
1678  N  ND1   . HIS   A 105 ? 0.9066 0.3357 0.3039 0.1099  -0.1480 0.0181  130 HIS   A ND1   
1679  C  CD2   . HIS   A 105 ? 0.8481 0.3061 0.3028 0.0938  -0.1480 0.0309  130 HIS   A CD2   
1680  C  CE1   . HIS   A 105 ? 0.9081 0.3337 0.3003 0.1231  -0.1372 0.0218  130 HIS   A CE1   
1681  N  NE2   . HIS   A 105 ? 0.8686 0.3196 0.3010 0.1141  -0.1304 0.0323  130 HIS   A NE2   
1689  N  N     . LYS   A 106 ? 0.9302 0.4027 0.3477 0.0632  -0.2000 0.0574  131 LYS   A N     
1690  C  CA    A LYS   A 106 ? 0.9439 0.4121 0.3553 0.0661  -0.1854 0.0686  131 LYS   A CA    
1691  C  CA    B LYS   A 106 ? 0.9175 0.3997 0.3453 0.0635  -0.1936 0.0559  131 LYS   A CA    
1692  C  C     . LYS   A 106 ? 0.9590 0.4183 0.3496 0.0520  -0.1758 0.0583  131 LYS   A C     
1693  O  O     . LYS   A 106 ? 1.0002 0.4339 0.3641 0.0346  -0.1586 0.0521  131 LYS   A O     
1694  C  CB    A LYS   A 106 ? 0.9310 0.4155 0.3725 0.0781  -0.1834 0.0878  131 LYS   A CB    
1695  C  CB    B LYS   A 106 ? 0.8524 0.3789 0.3429 0.0712  -0.2072 0.0501  131 LYS   A CB    
1696  C  CG    A LYS   A 106 ? 0.9176 0.4136 0.3887 0.0810  -0.1730 0.1039  131 LYS   A CG    
1697  C  CG    B LYS   A 106 ? 0.7925 0.3536 0.3403 0.0692  -0.2151 0.0413  131 LYS   A CG    
1698  C  CD    A LYS   A 106 ? 0.8953 0.4045 0.3961 0.0713  -0.1628 0.1198  131 LYS   A CD    
1699  C  CD    B LYS   A 106 ? 0.7360 0.3200 0.3369 0.0544  -0.2226 0.0350  131 LYS   A CD    
1700  C  CE    A LYS   A 106 ? 0.8929 0.3933 0.4011 0.0641  -0.1492 0.1274  131 LYS   A CE    
1701  C  CE    B LYS   A 106 ? 0.6913 0.3120 0.3362 0.0442  -0.2221 0.0413  131 LYS   A CE    
1702  N  NZ    A LYS   A 106 ? 0.8961 0.3849 0.4040 0.0571  -0.1403 0.1305  131 LYS   A NZ    
1703  N  NZ    B LYS   A 106 ? 0.6640 0.3007 0.3342 0.0337  -0.2135 0.0529  131 LYS   A NZ    
1728  N  N     . VAL   A 107 ? 0.9686 0.4240 0.3374 0.0541  -0.1493 0.0843  132 VAL   A N     
1729  C  CA    . VAL   A 107 ? 0.9859 0.4178 0.3248 0.0132  -0.1265 0.0695  132 VAL   A CA    
1730  C  C     . VAL   A 107 ? 0.9966 0.4209 0.3091 0.0225  -0.1071 0.0564  132 VAL   A C     
1731  O  O     . VAL   A 107 ? 1.0142 0.4374 0.2889 -0.0004 -0.0760 0.0509  132 VAL   A O     
1732  C  CB    . VAL   A 107 ? 0.9949 0.4013 0.3356 -0.0126 -0.1114 0.0710  132 VAL   A CB    
1733  C  CG1   . VAL   A 107 ? 0.9942 0.3717 0.3209 -0.0306 -0.1340 0.0666  132 VAL   A CG1   
1734  C  CG2   . VAL   A 107 ? 0.9897 0.4062 0.3489 -0.0301 -0.0802 0.0807  132 VAL   A CG2   
1744  N  N     . GLU   A 108 ? 0.9761 0.3903 0.3025 0.0284  -0.1233 0.0608  133 GLU   A N     
1745  C  CA    . GLU   A 108 ? 1.0119 0.3622 0.3039 0.0125  -0.0941 0.0586  133 GLU   A CA    
1746  C  C     . GLU   A 108 ? 1.0710 0.3623 0.3277 0.0078  -0.0704 0.0347  133 GLU   A C     
1747  O  O     . GLU   A 108 ? 1.0875 0.3336 0.3258 0.0290  -0.0177 0.0146  133 GLU   A O     
1748  C  CB    . GLU   A 108 ? 0.9940 0.3596 0.2784 -0.0311 -0.0706 0.0438  133 GLU   A CB    
1749  C  CG    . GLU   A 108 ? 1.0106 0.3674 0.2881 -0.0376 -0.0212 0.0479  133 GLU   A CG    
1750  C  CD    . GLU   A 108 ? 1.0408 0.4128 0.3129 -0.0072 -0.0111 0.0389  133 GLU   A CD    
1751  O  OE1   . GLU   A 108 ? 1.0718 0.4213 0.3262 0.0332  0.0174  0.0073  133 GLU   A OE1   
1752  O  OE2   . GLU   A 108 ? 1.0434 0.4603 0.3245 0.0149  -0.0187 0.0435  133 GLU   A OE2   
1759  N  N     . LYS   A 109 ? 1.1189 0.4011 0.3485 -0.0024 -0.0864 0.0294  134 LYS   A N     
1760  C  CA    . LYS   A 109 ? 1.1433 0.4286 0.3486 -0.0421 -0.0955 0.0035  134 LYS   A CA    
1761  C  C     . LYS   A 109 ? 1.1361 0.4479 0.3439 -0.0624 -0.1211 -0.0189 134 LYS   A C     
1762  O  O     . LYS   A 109 ? 1.1502 0.4618 0.3327 -0.0877 -0.1161 -0.0281 134 LYS   A O     
1763  C  CB    . LYS   A 109 ? 1.1763 0.4518 0.3638 -0.0442 -0.0667 0.0022  134 LYS   A CB    
1764  C  CG    . LYS   A 109 ? 1.2057 0.5039 0.3875 -0.0345 -0.0460 0.0071  134 LYS   A CG    
1765  C  CD    . LYS   A 109 ? 1.2332 0.5294 0.4066 -0.0203 -0.0243 0.0373  134 LYS   A CD    
1766  C  CE    . LYS   A 109 ? 1.2646 0.5745 0.4257 -0.0164 -0.0072 0.0491  134 LYS   A CE    
1767  N  NZ    . LYS   A 109 ? 1.2765 0.5987 0.4307 -0.0194 -0.0066 0.0699  134 LYS   A NZ    
1781  N  N     . MET   A 110 ? 1.0849 0.4389 0.3370 -0.0306 -0.1870 -0.0244 135 MET   A N     
1782  C  CA    . MET   A 110 ? 1.0681 0.4049 0.3640 0.0266  -0.2239 -0.0098 135 MET   A CA    
1783  C  C     . MET   A 110 ? 0.9673 0.3737 0.3513 0.0505  -0.2449 -0.0080 135 MET   A C     
1784  O  O     . MET   A 110 ? 0.9721 0.3507 0.3564 0.0394  -0.2487 0.0002  135 MET   A O     
1785  C  CB    . MET   A 110 ? 1.1087 0.4374 0.4019 0.0700  -0.2350 -0.0104 135 MET   A CB    
1786  C  CG    . MET   A 110 ? 1.1406 0.4433 0.4252 0.1163  -0.2541 -0.0022 135 MET   A CG    
1787  S  SD    . MET   A 110 ? 1.1689 0.4359 0.4470 0.1452  -0.2603 -0.0044 135 MET   A SD    
1788  C  CE    . MET   A 110 ? 1.1794 0.4706 0.4718 0.1296  -0.2511 -0.0075 135 MET   A CE    
1798  N  N     . TYR   A 111 ? 0.8837 0.3716 0.3537 0.1032  -0.2460 -0.0106 136 TYR   A N     
1799  C  CA    . TYR   A 111 ? 0.8020 0.3644 0.3649 0.1397  -0.2523 -0.0274 136 TYR   A CA    
1800  C  C     . TYR   A 111 ? 0.8265 0.3275 0.3435 0.1316  -0.2440 -0.0465 136 TYR   A C     
1801  O  O     . TYR   A 111 ? 0.8581 0.3147 0.3362 0.1212  -0.2361 -0.0519 136 TYR   A O     
1802  C  CB    . TYR   A 111 ? 0.7451 0.3981 0.3911 0.1495  -0.2640 -0.0238 136 TYR   A CB    
1803  C  CG    . TYR   A 111 ? 0.7868 0.4588 0.4093 0.1760  -0.2777 -0.0395 136 TYR   A CG    
1804  C  CD1   . TYR   A 111 ? 0.8120 0.5150 0.4242 0.1943  -0.2837 -0.0396 136 TYR   A CD1   
1805  C  CD2   . TYR   A 111 ? 0.7915 0.4537 0.4165 0.1875  -0.2816 -0.0504 136 TYR   A CD2   
1806  C  CE1   . TYR   A 111 ? 0.8190 0.5436 0.4348 0.1975  -0.2889 -0.0338 136 TYR   A CE1   
1807  C  CE2   . TYR   A 111 ? 0.8172 0.4839 0.4285 0.1881  -0.2903 -0.0456 136 TYR   A CE2   
1808  C  CZ    . TYR   A 111 ? 0.8374 0.5428 0.4416 0.2039  -0.2909 -0.0314 136 TYR   A CZ    
1809  O  OH    . TYR   A 111 ? 0.8866 0.5989 0.4604 0.1971  -0.2887 -0.0103 136 TYR   A OH    
1819  N  N     . VAL   A 112 ? 0.7959 0.2894 0.3345 0.1171  -0.2405 -0.0473 137 VAL   A N     
1820  C  CA    . VAL   A 112 ? 0.7678 0.2568 0.3285 0.1156  -0.2360 -0.0471 137 VAL   A CA    
1821  C  C     . VAL   A 112 ? 0.7446 0.2646 0.3356 0.1225  -0.2361 -0.0440 137 VAL   A C     
1822  O  O     . VAL   A 112 ? 0.7527 0.2801 0.3308 0.1289  -0.2281 -0.0375 137 VAL   A O     
1823  C  CB    . VAL   A 112 ? 0.8182 0.2779 0.3416 0.1053  -0.2471 -0.0457 137 VAL   A CB    
1824  C  CG1   . VAL   A 112 ? 0.8134 0.2628 0.3393 0.1221  -0.2436 -0.0517 137 VAL   A CG1   
1825  C  CG2   . VAL   A 112 ? 0.8377 0.2962 0.3587 0.1018  -0.2613 -0.0413 137 VAL   A CG2   
1835  N  N     . PRO   A 113 ? 0.7093 0.2744 0.3459 0.1237  -0.2389 -0.0386 138 PRO   A N     
1836  C  CA    . PRO   A 113 ? 0.7460 0.2916 0.3477 0.1430  -0.2424 -0.0506 138 PRO   A CA    
1837  C  C     . PRO   A 113 ? 0.7453 0.2889 0.3436 0.1444  -0.2435 -0.0584 138 PRO   A C     
1838  O  O     . PRO   A 113 ? 0.7189 0.2951 0.3514 0.1507  -0.2409 -0.0532 138 PRO   A O     
1839  C  CB    . PRO   A 113 ? 0.7225 0.3094 0.3516 0.1509  -0.2376 -0.0436 138 PRO   A CB    
1840  C  CG    . PRO   A 113 ? 0.7504 0.2995 0.3498 0.1332  -0.2406 -0.0367 138 PRO   A CG    
1841  C  CD    . PRO   A 113 ? 0.7160 0.2958 0.3467 0.1180  -0.2492 -0.0452 138 PRO   A CD    
1849  N  N     . ALA   A 114 ? 0.7661 0.2750 0.3374 0.1125  -0.2430 -0.0576 139 ALA   A N     
1850  C  CA    . ALA   A 114 ? 0.7935 0.2754 0.3182 0.1145  -0.2258 -0.0429 139 ALA   A CA    
1851  C  C     . ALA   A 114 ? 0.8001 0.2800 0.3042 0.1241  -0.1873 -0.0154 139 ALA   A C     
1852  O  O     . ALA   A 114 ? 0.7876 0.2958 0.3242 0.1354  -0.1624 0.0142  139 ALA   A O     
1853  C  CB    . ALA   A 114 ? 0.8245 0.2888 0.3202 0.1082  -0.2256 -0.0441 139 ALA   A CB    
1859  N  N     . LEU   A 115 ? 0.7834 0.2620 0.2807 0.0889  -0.1836 -0.0143 140 LEU   A N     
1860  C  CA    . LEU   A 115 ? 0.8081 0.2444 0.2733 0.0922  -0.1553 -0.0098 140 LEU   A CA    
1861  C  C     . LEU   A 115 ? 0.7498 0.2404 0.2706 0.0945  -0.1557 -0.0054 140 LEU   A C     
1862  O  O     . LEU   A 115 ? 0.7724 0.2603 0.2771 0.1186  -0.1513 -0.0066 140 LEU   A O     
1863  C  CB    . LEU   A 115 ? 0.8561 0.2602 0.2719 0.0981  -0.1258 0.0014  140 LEU   A CB    
1864  C  CG    . LEU   A 115 ? 0.8753 0.2615 0.2720 0.0853  -0.1134 0.0088  140 LEU   A CG    
1865  C  CD1   . LEU   A 115 ? 0.8720 0.2762 0.2770 0.0814  -0.1212 0.0171  140 LEU   A CD1   
1866  C  CD2   . LEU   A 115 ? 0.8900 0.2820 0.2830 0.0886  -0.0957 0.0270  140 LEU   A CD2   
1878  N  N     . ILE   A 116 ? 0.6970 0.2134 0.2575 0.0717  -0.1682 -0.0132 141 ILE   A N     
1879  C  CA    . ILE   A 116 ? 0.6571 0.2089 0.2505 0.0817  -0.1630 -0.0161 141 ILE   A CA    
1880  C  C     . ILE   A 116 ? 0.6212 0.2276 0.2552 0.1008  -0.1550 -0.0074 141 ILE   A C     
1881  O  O     . ILE   A 116 ? 0.5773 0.2262 0.2523 0.0767  -0.1569 -0.0136 141 ILE   A O     
1882  C  CB    . ILE   A 116 ? 0.6628 0.2201 0.2631 0.0881  -0.1649 -0.0104 141 ILE   A CB    
1883  C  CG1   . ILE   A 116 ? 0.6592 0.2416 0.2586 0.0968  -0.1755 -0.0211 141 ILE   A CG1   
1884  C  CG2   . ILE   A 116 ? 0.6646 0.2438 0.2791 0.0990  -0.1585 0.0068  141 ILE   A CG2   
1885  C  CD1   . ILE   A 116 ? 0.6542 0.2559 0.2657 0.0856  -0.1842 -0.0149 141 ILE   A CD1   
1897  N  N     . PHE   A 117 ? 0.6185 0.2348 0.2642 0.0999  -0.1497 0.0056  142 PHE   A N     
1898  C  CA    . PHE   A 117 ? 0.5944 0.2543 0.2859 0.1167  -0.1811 -0.0142 142 PHE   A CA    
1899  C  C     . PHE   A 117 ? 0.5863 0.2526 0.2865 0.1021  -0.1743 -0.0024 142 PHE   A C     
1900  O  O     . PHE   A 117 ? 0.5801 0.2523 0.2724 0.0754  -0.1709 0.0183  142 PHE   A O     
1901  C  CB    . PHE   A 117 ? 0.5868 0.2670 0.3037 0.1285  -0.2097 -0.0502 142 PHE   A CB    
1902  C  CG    . PHE   A 117 ? 0.5867 0.2587 0.3287 0.1269  -0.2159 -0.0403 142 PHE   A CG    
1903  C  CD1   . PHE   A 117 ? 0.5801 0.2777 0.3365 0.0928  -0.2380 -0.0383 142 PHE   A CD1   
1904  C  CD2   . PHE   A 117 ? 0.6053 0.2480 0.3443 0.1249  -0.2332 -0.0552 142 PHE   A CD2   
1905  C  CE1   . PHE   A 117 ? 0.5613 0.2635 0.3468 0.0862  -0.2363 -0.0412 142 PHE   A CE1   
1906  C  CE2   . PHE   A 117 ? 0.5815 0.2519 0.3504 0.1140  -0.2436 -0.0601 142 PHE   A CE2   
1907  C  CZ    . PHE   A 117 ? 0.5300 0.2519 0.3536 0.0941  -0.2429 -0.0575 142 PHE   A CZ    
1917  N  N     . GLY   A 118 ? 0.6154 0.2441 0.2914 0.0973  -0.1598 -0.0207 143 GLY   A N     
1918  C  CA    . GLY   A 118 ? 0.6556 0.2516 0.2965 0.1126  -0.1607 -0.0233 143 GLY   A CA    
1919  C  C     . GLY   A 118 ? 0.6867 0.2374 0.2907 0.1090  -0.1476 -0.0276 143 GLY   A C     
1920  O  O     . GLY   A 118 ? 0.6909 0.2363 0.3192 0.1359  -0.1376 -0.0354 143 GLY   A O     
1924  N  N     . GLN   A 119 ? 0.7023 0.2286 0.2545 0.1031  -0.1485 -0.0131 144 GLN   A N     
1925  C  CA    . GLN   A 119 ? 0.7051 0.2429 0.2303 0.0736  -0.1276 -0.0039 144 GLN   A CA    
1926  C  C     . GLN   A 119 ? 0.6583 0.2254 0.2132 0.0949  -0.0961 0.0059  144 GLN   A C     
1927  O  O     . GLN   A 119 ? 0.6422 0.2346 0.2212 0.0970  -0.0973 0.0157  144 GLN   A O     
1928  C  CB    . GLN   A 119 ? 0.7485 0.2770 0.2312 0.0980  -0.1199 -0.0031 144 GLN   A CB    
1929  C  CG    . GLN   A 119 ? 0.7915 0.3325 0.2720 0.1213  -0.1062 -0.0165 144 GLN   A CG    
1930  C  CD    . GLN   A 119 ? 0.8290 0.3739 0.2983 0.1356  -0.0789 -0.0252 144 GLN   A CD    
1931  O  OE1   . GLN   A 119 ? 0.8627 0.3972 0.3122 0.1397  -0.0399 -0.0499 144 GLN   A OE1   
1932  N  NE2   . GLN   A 119 ? 0.8273 0.3681 0.3108 0.1442  -0.0853 -0.0143 144 GLN   A NE2   
1941  N  N     . LEU   A 120 ? 0.6553 0.2068 0.2157 0.0768  -0.0736 0.0076  145 LEU   A N     
1942  C  CA    . LEU   A 120 ? 0.6370 0.2006 0.2339 0.0488  -0.0644 0.0178  145 LEU   A CA    
1943  C  C     . LEU   A 120 ? 0.6206 0.1924 0.2023 0.0528  -0.0549 0.0252  145 LEU   A C     
1944  O  O     . LEU   A 120 ? 0.6703 0.2340 0.1950 0.0509  -0.0312 0.0334  145 LEU   A O     
1945  C  CB    . LEU   A 120 ? 0.6288 0.1842 0.2835 0.0500  -0.0608 0.0085  145 LEU   A CB    
1946  C  CG    . LEU   A 120 ? 0.6087 0.1871 0.3299 0.0381  -0.0700 0.0003  145 LEU   A CG    
1947  C  CD1   . LEU   A 120 ? 0.6276 0.2044 0.3404 0.0478  -0.0782 -0.0082 145 LEU   A CD1   
1948  C  CD2   . LEU   A 120 ? 0.5876 0.2129 0.3526 0.0417  -0.0407 0.0408  145 LEU   A CD2   
1960  N  N     . LEU   A 121 ? 0.6177 0.1795 0.2173 0.0435  -0.0442 0.0275  146 LEU   A N     
1961  C  CA    . LEU   A 121 ? 0.6230 0.1888 0.2159 0.0550  -0.0322 0.0320  146 LEU   A CA    
1962  C  C     . LEU   A 121 ? 0.6281 0.2072 0.1997 0.0634  -0.0309 0.0333  146 LEU   A C     
1963  O  O     . LEU   A 121 ? 0.6772 0.2253 0.1918 0.0760  -0.0172 0.0243  146 LEU   A O     
1964  C  CB    . LEU   A 121 ? 0.6361 0.2043 0.2472 0.0524  -0.0120 0.0425  146 LEU   A CB    
1965  C  CG    . LEU   A 121 ? 0.6331 0.2424 0.2672 0.0575  -0.0001 0.0434  146 LEU   A CG    
1966  C  CD1   . LEU   A 121 ? 0.6713 0.2146 0.2887 0.0306  0.0009  0.0549  146 LEU   A CD1   
1967  C  CD2   . LEU   A 121 ? 0.6449 0.3066 0.2774 0.0408  0.0045  0.0361  146 LEU   A CD2   
1979  N  N     . THR   A 122 ? 0.6055 0.2134 0.2000 0.0791  -0.0397 0.0342  147 THR   A N     
1980  C  CA    . THR   A 122 ? 0.6084 0.2210 0.1981 0.0722  -0.0536 0.0336  147 THR   A CA    
1981  C  C     . THR   A 122 ? 0.5981 0.2198 0.2017 0.0785  -0.0772 0.0249  147 THR   A C     
1982  O  O     . THR   A 122 ? 0.6153 0.2009 0.2050 0.0747  -0.0829 0.0134  147 THR   A O     
1983  C  CB    . THR   A 122 ? 0.6391 0.2437 0.1929 0.0811  -0.0582 0.0254  147 THR   A CB    
1984  O  OG1   . THR   A 122 ? 0.6696 0.2440 0.1969 0.0915  -0.0693 0.0123  147 THR   A OG1   
1985  C  CG2   . THR   A 122 ? 0.6724 0.2431 0.1974 0.0660  -0.0671 0.0213  147 THR   A CG2   
1993  N  N     . SER   A 123 ? 0.6016 0.2140 0.1968 0.0991  -0.0653 0.0155  148 SER   A N     
1994  C  CA    . SER   A 123 ? 0.5820 0.2028 0.1903 0.0874  -0.0525 0.0213  148 SER   A CA    
1995  C  C     . SER   A 123 ? 0.6122 0.1991 0.1946 0.0760  -0.0674 0.0145  148 SER   A C     
1996  O  O     . SER   A 123 ? 0.6221 0.2118 0.1926 0.0764  -0.0664 0.0169  148 SER   A O     
1997  C  CB    . SER   A 123 ? 0.5518 0.2364 0.1934 0.0548  -0.0372 0.0328  148 SER   A CB    
1998  O  OG    . SER   A 123 ? 0.5012 0.1983 0.1952 0.0463  -0.0324 0.0228  148 SER   A OG    
2004  N  N     . SER   A 124 ? 0.6459 0.1843 0.1855 0.0733  -0.0826 -0.0117 149 SER   A N     
2005  C  CA    . SER   A 124 ? 0.6346 0.1953 0.2267 0.0658  -0.0628 -0.0089 149 SER   A CA    
2006  C  C     . SER   A 124 ? 0.6241 0.1882 0.2287 0.0856  -0.0527 0.0024  149 SER   A C     
2007  O  O     . SER   A 124 ? 0.6042 0.2024 0.2429 0.0643  -0.0677 0.0217  149 SER   A O     
2008  C  CB    . SER   A 124 ? 0.6014 0.2298 0.2383 0.0804  -0.0527 -0.0063 149 SER   A CB    
2009  O  OG    . SER   A 124 ? 0.6027 0.2405 0.2575 0.0892  -0.0348 -0.0015 149 SER   A OG    
2015  N  N     . ASN   A 125 ? 0.6235 0.1818 0.2233 0.0696  -0.0487 0.0159  150 ASN   A N     
2016  C  CA    . ASN   A 125 ? 0.6046 0.1951 0.2069 0.0541  -0.0539 0.0323  150 ASN   A CA    
2017  C  C     . ASN   A 125 ? 0.5804 0.2262 0.2118 0.0483  -0.0480 0.0401  150 ASN   A C     
2018  O  O     . ASN   A 125 ? 0.5719 0.2576 0.2388 0.0364  -0.0241 0.0436  150 ASN   A O     
2019  C  CB    . ASN   A 125 ? 0.5972 0.1888 0.2285 0.0473  -0.0461 0.0201  150 ASN   A CB    
2020  C  CG    . ASN   A 125 ? 0.5865 0.1996 0.2521 0.0589  -0.0519 0.0037  150 ASN   A CG    
2021  O  OD1   . ASN   A 125 ? 0.5376 0.1990 0.2967 0.0406  -0.0310 -0.0208 150 ASN   A OD1   
2022  N  ND2   . ASN   A 125 ? 0.5794 0.2069 0.2285 0.0887  -0.0810 -0.0059 150 ASN   A ND2   
2029  N  N     . TYR   A 126 ? 0.5766 0.2124 0.2222 0.0569  -0.0133 0.0504  151 TYR   A N     
2030  C  CA    . TYR   A 126 ? 0.6292 0.2228 0.2363 0.0569  0.0046  0.0303  151 TYR   A CA    
2031  C  C     . TYR   A 126 ? 0.6468 0.2120 0.2781 0.0561  0.0384  0.0483  151 TYR   A C     
2032  O  O     . TYR   A 126 ? 0.6549 0.2148 0.3084 0.0249  0.0340  0.0460  151 TYR   A O     
2033  C  CB    . TYR   A 126 ? 0.6314 0.2163 0.2109 0.0600  -0.0144 0.0314  151 TYR   A CB    
2034  C  CG    . TYR   A 126 ? 0.6297 0.2294 0.2095 0.0829  -0.0389 0.0254  151 TYR   A CG    
2035  C  CD1   . TYR   A 126 ? 0.6106 0.2090 0.2067 0.0601  -0.0543 0.0262  151 TYR   A CD1   
2036  C  CD2   . TYR   A 126 ? 0.6421 0.2444 0.2143 0.0751  -0.0402 0.0090  151 TYR   A CD2   
2037  C  CE1   . TYR   A 126 ? 0.5991 0.1900 0.2035 0.0365  -0.0461 0.0203  151 TYR   A CE1   
2038  C  CE2   . TYR   A 126 ? 0.6254 0.2363 0.2066 0.0514  -0.0395 0.0275  151 TYR   A CE2   
2039  C  CZ    . TYR   A 126 ? 0.5966 0.2137 0.2080 0.0446  -0.0449 0.0251  151 TYR   A CZ    
2040  O  OH    . TYR   A 126 ? 0.6014 0.2265 0.2201 0.0319  -0.0151 0.0284  151 TYR   A OH    
2050  N  N     . ASP   A 127 ? 0.6596 0.1908 0.2797 0.0573  0.0566  0.0449  152 ASP   A N     
2051  C  CA    . ASP   A 127 ? 0.6706 0.2062 0.2973 0.0335  0.0554  0.0661  152 ASP   A CA    
2052  C  C     . ASP   A 127 ? 0.6743 0.1978 0.3094 0.0343  0.0691  0.0545  152 ASP   A C     
2053  O  O     . ASP   A 127 ? 0.6644 0.1958 0.3206 0.0560  0.0828  0.0474  152 ASP   A O     
2054  C  CB    . ASP   A 127 ? 0.7497 0.2316 0.3260 0.0332  0.0378  0.0751  152 ASP   A CB    
2055  C  CG    . ASP   A 127 ? 0.8100 0.2659 0.3351 0.0200  0.0559  0.0775  152 ASP   A CG    
2056  O  OD1   . ASP   A 127 ? 0.8351 0.2842 0.3348 -0.0080 0.0929  0.0677  152 ASP   A OD1   
2057  O  OD2   . ASP   A 127 ? 0.8480 0.2690 0.3581 0.0385  0.0349  0.0883  152 ASP   A OD2   
2062  N  N     . ASP   A 128 ? 0.6874 0.2100 0.3074 0.0372  0.0582  0.0487  153 ASP   A N     
2063  C  CA    . ASP   A 128 ? 0.6852 0.2275 0.3244 0.0334  0.0262  0.0473  153 ASP   A CA    
2064  C  C     . ASP   A 128 ? 0.7026 0.2253 0.3310 0.0062  0.0291  0.0524  153 ASP   A C     
2065  O  O     . ASP   A 128 ? 0.6943 0.2262 0.3335 0.0133  0.0320  0.0452  153 ASP   A O     
2066  C  CB    . ASP   A 128 ? 0.6718 0.2418 0.3348 0.0336  0.0190  0.0554  153 ASP   A CB    
2067  C  CG    . ASP   A 128 ? 0.6774 0.2482 0.3403 0.0413  0.0232  0.0794  153 ASP   A CG    
2068  O  OD1   . ASP   A 128 ? 0.6793 0.2491 0.3165 0.0264  0.0437  0.0819  153 ASP   A OD1   
2069  O  OD2   . ASP   A 128 ? 0.6705 0.2696 0.3647 0.0414  0.0304  0.0872  153 ASP   A OD2   
2074  N  N     . ASP   A 129 ? 0.7225 0.2196 0.3433 0.0003  0.0502  0.0567  154 ASP   A N     
2075  C  CA    . ASP   A 129 ? 0.7463 0.2343 0.3481 -0.0025 0.0541  0.0711  154 ASP   A CA    
2076  C  C     . ASP   A 129 ? 0.7317 0.2334 0.3461 -0.0014 0.0408  0.0567  154 ASP   A C     
2077  O  O     . ASP   A 129 ? 0.7262 0.2276 0.3657 0.0151  0.0544  0.0332  154 ASP   A O     
2078  C  CB    . ASP   A 129 ? 0.7845 0.2807 0.3641 0.0008  0.0557  0.0904  154 ASP   A CB    
2079  C  CG    . ASP   A 129 ? 0.8451 0.3918 0.3953 0.0151  0.0465  0.1007  154 ASP   A CG    
2080  O  OD1   . ASP   A 129 ? 0.8650 0.4393 0.4275 0.0308  0.0337  0.1055  154 ASP   A OD1   
2081  O  OD2   . ASP   A 129 ? 0.8691 0.4494 0.3968 0.0068  0.0781  0.0787  154 ASP   A OD2   
2086  N  N     . GLU   A 130 ? 0.6918 0.2527 0.3185 -0.0138 0.0131  0.0797  155 GLU   A N     
2087  C  CA    . GLU   A 130 ? 0.6619 0.2421 0.3129 0.0262  -0.0250 0.0960  155 GLU   A CA    
2088  C  C     . GLU   A 130 ? 0.5764 0.2210 0.3013 0.0403  -0.0084 0.0776  155 GLU   A C     
2089  O  O     . GLU   A 130 ? 0.5816 0.2194 0.3078 0.0712  0.0076  0.0609  155 GLU   A O     
2090  C  CB    . GLU   A 130 ? 0.7070 0.2766 0.3288 0.0554  -0.0644 0.0957  155 GLU   A CB    
2091  C  CG    . GLU   A 130 ? 0.7518 0.3074 0.3566 0.0754  -0.0822 0.0917  155 GLU   A CG    
2092  C  CD    . GLU   A 130 ? 0.7802 0.3309 0.3950 0.0740  -0.1078 0.0833  155 GLU   A CD    
2093  O  OE1   . GLU   A 130 ? 0.7643 0.3077 0.3848 0.0787  -0.0994 0.0631  155 GLU   A OE1   
2094  O  OE2   . GLU   A 130 ? 0.8114 0.3694 0.4344 0.0930  -0.1272 0.0849  155 GLU   A OE2   
2101  N  N     . LYS   A 131 ? 0.5301 0.2328 0.3105 0.0042  0.0314  0.0611  156 LYS   A N     
2102  C  CA    . LYS   A 131 ? 0.4792 0.1899 0.3185 0.0020  0.0626  0.0300  156 LYS   A CA    
2103  C  C     . LYS   A 131 ? 0.4127 0.2099 0.3370 0.0210  0.0445  -0.0162 156 LYS   A C     
2104  O  O     . LYS   A 131 ? 0.4392 0.2563 0.4026 -0.0017 0.0537  -0.0490 156 LYS   A O     
2105  C  CB    . LYS   A 131 ? 0.5247 0.2082 0.3322 -0.0430 0.0983  0.0103  156 LYS   A CB    
2106  C  CG    . LYS   A 131 ? 0.5615 0.2806 0.3595 -0.0695 0.1095  0.0015  156 LYS   A CG    
2107  C  CD    . LYS   A 131 ? 0.5776 0.3428 0.3883 -0.0873 0.1215  -0.0042 156 LYS   A CD    
2108  C  CE    . LYS   A 131 ? 0.6243 0.3967 0.4207 -0.1103 0.1074  -0.0228 156 LYS   A CE    
2109  N  NZ    . LYS   A 131 ? 0.6349 0.4391 0.4302 -0.1391 0.1070  -0.0283 156 LYS   A NZ    
2123  N  N     . LYS   A 132 ? 0.4054 0.1879 0.2818 0.0365  0.0233  0.0258  157 LYS   A N     
2124  C  CA    . LYS   A 132 ? 0.3830 0.1992 0.2459 0.0262  -0.0151 0.0315  157 LYS   A CA    
2125  C  C     . LYS   A 132 ? 0.3449 0.1961 0.2388 0.0417  -0.0206 0.0411  157 LYS   A C     
2126  O  O     . LYS   A 132 ? 0.3064 0.2325 0.2521 0.0197  -0.0181 0.0282  157 LYS   A O     
2127  C  CB    . LYS   A 132 ? 0.4654 0.2153 0.2697 0.0071  -0.0403 0.0325  157 LYS   A CB    
2128  C  CG    . LYS   A 132 ? 0.5470 0.2510 0.2816 -0.0116 -0.0649 0.0285  157 LYS   A CG    
2129  C  CD    . LYS   A 132 ? 0.6266 0.3298 0.3173 -0.0462 -0.0786 0.0285  157 LYS   A CD    
2130  C  CE    . LYS   A 132 ? 0.6944 0.4229 0.3670 -0.0952 -0.0768 0.0472  157 LYS   A CE    
2131  N  NZ    . LYS   A 132 ? 0.7381 0.5070 0.4069 -0.0949 -0.0601 0.0804  157 LYS   A NZ    
2145  N  N     . VAL   A 133 ? 0.2752 0.1880 0.2472 0.0362  -0.0278 0.0390  158 VAL   A N     
2146  C  CA    . VAL   A 133 ? 0.2409 0.1832 0.2451 0.0477  -0.0230 0.0258  158 VAL   A CA    
2147  C  C     . VAL   A 133 ? 0.2481 0.1805 0.2441 0.0071  -0.0100 0.0048  158 VAL   A C     
2148  O  O     . VAL   A 133 ? 0.2537 0.2039 0.2533 0.0086  -0.0139 0.0042  158 VAL   A O     
2149  C  CB    . VAL   A 133 ? 0.2620 0.2063 0.2628 0.0198  -0.0091 0.0051  158 VAL   A CB    
2150  C  CG1   . VAL   A 133 ? 0.2752 0.1916 0.2570 0.0137  0.0080  0.0154  158 VAL   A CG1   
2151  C  CG2   . VAL   A 133 ? 0.2871 0.2130 0.2866 0.0362  0.0040  0.0030  158 VAL   A CG2   
2161  N  N     . THR   A 134 ? 0.2953 0.1725 0.2544 0.0151  -0.0353 -0.0069 159 THR   A N     
2162  C  CA    . THR   A 134 ? 0.3030 0.1887 0.2459 0.0295  -0.0478 0.0009  159 THR   A CA    
2163  C  C     . THR   A 134 ? 0.2688 0.1832 0.2337 -0.0014 -0.0436 0.0019  159 THR   A C     
2164  O  O     . THR   A 134 ? 0.2966 0.2165 0.2445 0.0048  -0.0479 0.0200  159 THR   A O     
2165  C  CB    . THR   A 134 ? 0.3721 0.2559 0.2678 0.0630  -0.0622 0.0175  159 THR   A CB    
2166  O  OG1   . THR   A 134 ? 0.4376 0.3033 0.2716 0.0269  -0.0591 0.0193  159 THR   A OG1   
2167  C  CG2   . THR   A 134 ? 0.4179 0.2328 0.2983 0.0239  -0.0723 0.0157  159 THR   A CG2   
2175  N  N     . GLY   A 135 ? 0.2970 0.1779 0.2461 -0.0111 -0.0213 0.0007  160 GLY   A N     
2176  C  CA    . GLY   A 135 ? 0.3347 0.1470 0.2354 -0.0047 -0.0179 0.0017  160 GLY   A CA    
2177  C  C     . GLY   A 135 ? 0.3400 0.1797 0.2282 0.0378  -0.0351 -0.0022 160 GLY   A C     
2178  O  O     . GLY   A 135 ? 0.3250 0.1935 0.2355 0.0182  -0.0336 0.0125  160 GLY   A O     
2182  N  N     . GLY   A 136 ? 0.3771 0.1995 0.2222 0.0242  -0.0683 -0.0078 161 GLY   A N     
2183  C  CA    . GLY   A 136 ? 0.3544 0.2056 0.2331 0.0290  -0.0512 -0.0063 161 GLY   A CA    
2184  C  C     . GLY   A 136 ? 0.3758 0.1925 0.2251 0.0130  -0.0165 0.0089  161 GLY   A C     
2185  O  O     . GLY   A 136 ? 0.3525 0.1796 0.2408 0.0173  -0.0317 0.0110  161 GLY   A O     
2189  N  N     . ARG   A 137 ? 0.3999 0.1798 0.1992 0.0014  -0.0320 0.0171  162 ARG   A N     
2190  C  CA    . ARG   A 137 ? 0.3993 0.1903 0.2117 0.0120  -0.0213 0.0109  162 ARG   A CA    
2191  C  C     . ARG   A 137 ? 0.4368 0.1926 0.1965 -0.0044 -0.0004 0.0211  162 ARG   A C     
2192  O  O     . ARG   A 137 ? 0.4881 0.2094 0.1986 -0.0472 0.0194  0.0104  162 ARG   A O     
2193  C  CB    . ARG   A 137 ? 0.3693 0.1799 0.2401 0.0122  -0.0182 0.0115  162 ARG   A CB    
2194  C  CG    . ARG   A 137 ? 0.3556 0.2057 0.2633 0.0088  -0.0266 -0.0071 162 ARG   A CG    
2195  C  CD    . ARG   A 137 ? 0.3525 0.2146 0.2757 0.0207  -0.0151 0.0089  162 ARG   A CD    
2196  N  NE    . ARG   A 137 ? 0.3751 0.2513 0.2803 0.0033  -0.0037 0.0013  162 ARG   A NE    
2197  C  CZ    . ARG   A 137 ? 0.4108 0.2376 0.2811 0.0273  -0.0039 -0.0220 162 ARG   A CZ    
2198  N  NH1   . ARG   A 137 ? 0.4895 0.2594 0.2506 0.0283  -0.0193 -0.0216 162 ARG   A NH1   
2199  N  NH2   . ARG   A 137 ? 0.4511 0.2708 0.2988 0.0192  -0.0035 -0.0387 162 ARG   A NH2   
2213  N  N     . ASN   A 138 ? 0.4124 0.1871 0.2059 -0.0112 -0.0043 0.0081  163 ASN   A N     
2214  C  CA    . ASN   A 138 ? 0.4177 0.2091 0.2009 0.0118  -0.0400 0.0119  163 ASN   A CA    
2215  C  C     . ASN   A 138 ? 0.4619 0.2069 0.2008 0.0153  -0.0511 0.0119  163 ASN   A C     
2216  O  O     . ASN   A 138 ? 0.4690 0.2088 0.2032 0.0446  -0.0466 0.0146  163 ASN   A O     
2217  C  CB    . ASN   A 138 ? 0.4475 0.2443 0.2150 0.0262  -0.0574 0.0332  163 ASN   A CB    
2218  C  CG    . ASN   A 138 ? 0.4729 0.2762 0.2304 -0.0208 -0.0535 0.0340  163 ASN   A CG    
2219  O  OD1   . ASN   A 138 ? 0.4490 0.3012 0.2449 -0.0285 -0.0235 0.0287  163 ASN   A OD1   
2220  N  ND2   . ASN   A 138 ? 0.5468 0.2781 0.2304 -0.0633 -0.1029 0.0611  163 ASN   A ND2   
2227  N  N     . GLY   A 139 ? 0.4628 0.1962 0.1963 0.0250  -0.0368 0.0231  164 GLY   A N     
2228  C  CA    . GLY   A 139 ? 0.4873 0.1833 0.2051 0.0234  -0.0545 0.0279  164 GLY   A CA    
2229  C  C     . GLY   A 139 ? 0.4585 0.1832 0.1926 0.0255  -0.0635 0.0153  164 GLY   A C     
2230  O  O     . GLY   A 139 ? 0.5085 0.1923 0.1824 0.0476  -0.0752 0.0083  164 GLY   A O     
2234  N  N     . TYR   A 140 ? 0.4070 0.1906 0.1964 0.0421  -0.0524 0.0130  165 TYR   A N     
2235  C  CA    . TYR   A 140 ? 0.3916 0.1860 0.1998 0.0165  -0.0694 0.0105  165 TYR   A CA    
2236  C  C     . TYR   A 140 ? 0.3767 0.1921 0.2006 0.0205  -0.0971 0.0006  165 TYR   A C     
2237  O  O     . TYR   A 140 ? 0.3925 0.2117 0.2038 0.0050  -0.1039 0.0094  165 TYR   A O     
2238  C  CB    . TYR   A 140 ? 0.3777 0.1701 0.2187 0.0369  -0.0523 0.0074  165 TYR   A CB    
2239  C  CG    . TYR   A 140 ? 0.4068 0.2025 0.2549 0.0592  -0.0305 -0.0117 165 TYR   A CG    
2240  C  CD1   . TYR   A 140 ? 0.4401 0.2435 0.2798 0.0604  -0.0242 -0.0143 165 TYR   A CD1   
2241  C  CD2   . TYR   A 140 ? 0.4463 0.2448 0.2778 0.0675  -0.0151 -0.0084 165 TYR   A CD2   
2242  C  CE1   . TYR   A 140 ? 0.4703 0.2833 0.3080 0.0593  -0.0123 -0.0047 165 TYR   A CE1   
2243  C  CE2   . TYR   A 140 ? 0.4728 0.2872 0.3046 0.0460  -0.0020 -0.0002 165 TYR   A CE2   
2244  C  CZ    . TYR   A 140 ? 0.4863 0.3005 0.3110 0.0578  0.0154  0.0216  165 TYR   A CZ    
2245  O  OH    . TYR   A 140 ? 0.5029 0.3246 0.3234 0.0521  0.0444  0.0551  165 TYR   A OH    
2255  N  N     . GLY   A 141 ? 0.3716 0.1649 0.2019 0.0257  -0.0961 0.0097  166 GLY   A N     
2256  C  CA    . GLY   A 141 ? 0.3743 0.1880 0.2199 0.0314  -0.0978 0.0070  166 GLY   A CA    
2257  C  C     . GLY   A 141 ? 0.3636 0.1974 0.2410 0.0373  -0.1069 0.0060  166 GLY   A C     
2258  O  O     . GLY   A 141 ? 0.3537 0.1945 0.2392 0.0266  -0.1001 0.0101  166 GLY   A O     
2262  N  N     . ALA   A 142 ? 0.3833 0.1959 0.2528 0.0222  -0.1114 0.0084  167 ALA   A N     
2263  C  CA    . ALA   A 142 ? 0.3684 0.1967 0.2719 0.0546  -0.1139 0.0092  167 ALA   A CA    
2264  C  C     . ALA   A 142 ? 0.3914 0.2091 0.2622 0.0671  -0.1019 0.0110  167 ALA   A C     
2265  O  O     . ALA   A 142 ? 0.3926 0.2175 0.2542 0.0732  -0.0913 0.0068  167 ALA   A O     
2266  C  CB    . ALA   A 142 ? 0.4011 0.2253 0.2996 0.0816  -0.1429 -0.0021 167 ALA   A CB    
2272  N  N     . LYS   A 143 ? 0.3855 0.1885 0.2515 0.0538  -0.0825 0.0293  168 LYS   A N     
2273  C  CA    . LYS   A 143 ? 0.4248 0.1905 0.2428 0.0702  -0.0920 0.0086  168 LYS   A CA    
2274  C  C     . LYS   A 143 ? 0.3883 0.1847 0.2523 0.0819  -0.1119 -0.0041 168 LYS   A C     
2275  O  O     . LYS   A 143 ? 0.4313 0.1901 0.2618 0.0715  -0.1217 -0.0241 168 LYS   A O     
2276  C  CB    . LYS   A 143 ? 0.4660 0.1844 0.2187 0.0641  -0.1030 -0.0063 168 LYS   A CB    
2277  C  CG    . LYS   A 143 ? 0.5236 0.1833 0.2124 0.0951  -0.1105 -0.0065 168 LYS   A CG    
2278  C  CD    . LYS   A 143 ? 0.5406 0.2249 0.2034 0.1234  -0.1079 -0.0196 168 LYS   A CD    
2279  C  CE    . LYS   A 143 ? 0.5410 0.2314 0.2026 0.1100  -0.1033 -0.0168 168 LYS   A CE    
2280  N  NZ    . LYS   A 143 ? 0.5194 0.2182 0.2010 0.0960  -0.0997 -0.0048 168 LYS   A NZ    
2294  N  N     . LEU   A 144 ? 0.3502 0.1834 0.2399 0.0373  -0.1245 0.0236  169 LEU   A N     
2295  C  CA    . LEU   A 144 ? 0.3169 0.2018 0.2470 0.0303  -0.1019 0.0166  169 LEU   A CA    
2296  C  C     . LEU   A 144 ? 0.2753 0.1835 0.2539 0.0319  -0.1003 0.0191  169 LEU   A C     
2297  O  O     . LEU   A 144 ? 0.2589 0.1806 0.2731 0.0304  -0.0807 0.0120  169 LEU   A O     
2298  C  CB    . LEU   A 144 ? 0.2687 0.2137 0.2416 0.0303  -0.0927 0.0054  169 LEU   A CB    
2299  C  CG    . LEU   A 144 ? 0.2879 0.1990 0.2386 0.0347  -0.0927 -0.0056 169 LEU   A CG    
2300  C  CD1   . LEU   A 144 ? 0.3087 0.1997 0.2360 -0.0071 -0.0983 0.0197  169 LEU   A CD1   
2301  C  CD2   . LEU   A 144 ? 0.3603 0.2171 0.2488 0.0232  -0.0667 -0.0287 169 LEU   A CD2   
2313  N  N     . CYS   A 145 ? 0.2856 0.2113 0.2630 0.0110  -0.1209 0.0187  170 CYS   A N     
2314  C  CA    . CYS   A 145 ? 0.2796 0.2106 0.2959 0.0332  -0.1273 0.0004  170 CYS   A CA    
2315  C  C     . CYS   A 145 ? 0.2951 0.2038 0.3035 0.0207  -0.1441 -0.0219 170 CYS   A C     
2316  O  O     . CYS   A 145 ? 0.3090 0.2192 0.3164 0.0146  -0.1489 -0.0235 170 CYS   A O     
2317  C  CB    . CYS   A 145 ? 0.2803 0.1980 0.3417 0.0329  -0.1104 -0.0158 170 CYS   A CB    
2318  S  SG    . CYS   A 145 ? 0.2786 0.2319 0.3862 0.0328  -0.1177 -0.0098 170 CYS   A SG    
2324  N  N     . ASN   A 146 ? 0.3141 0.2109 0.3049 0.0425  -0.1661 -0.0195 171 ASN   A N     
2325  C  CA    . ASN   A 146 ? 0.3657 0.2108 0.2937 0.0661  -0.1669 -0.0214 171 ASN   A CA    
2326  C  C     . ASN   A 146 ? 0.3818 0.2291 0.2926 0.0516  -0.1605 -0.0424 171 ASN   A C     
2327  O  O     . ASN   A 146 ? 0.3778 0.2351 0.2975 0.0476  -0.1565 -0.0374 171 ASN   A O     
2328  C  CB    . ASN   A 146 ? 0.3762 0.2247 0.2919 0.0640  -0.1884 -0.0266 171 ASN   A CB    
2329  C  CG    . ASN   A 146 ? 0.4520 0.2361 0.3047 0.0904  -0.2024 -0.0370 171 ASN   A CG    
2330  O  OD1   . ASN   A 146 ? 0.4810 0.2550 0.3109 0.0876  -0.2045 -0.0460 171 ASN   A OD1   
2331  N  ND2   . ASN   A 146 ? 0.4823 0.2368 0.3149 0.0963  -0.2066 -0.0322 171 ASN   A ND2   
2338  N  N     . ILE   A 147 ? 0.3466 0.2041 0.2928 0.0182  -0.1430 -0.0349 172 ILE   A N     
2339  C  CA    . ILE   A 147 ? 0.3580 0.1870 0.2866 0.0143  -0.1472 -0.0233 172 ILE   A CA    
2340  C  C     . ILE   A 147 ? 0.3226 0.1745 0.2878 0.0205  -0.1238 -0.0304 172 ILE   A C     
2341  O  O     . ILE   A 147 ? 0.3298 0.1888 0.2883 0.0189  -0.1069 -0.0238 172 ILE   A O     
2342  C  CB    . ILE   A 147 ? 0.4015 0.1671 0.2867 0.0297  -0.1209 -0.0090 172 ILE   A CB    
2343  C  CG1   . ILE   A 147 ? 0.4094 0.2002 0.2779 0.0342  -0.1037 -0.0094 172 ILE   A CG1   
2344  C  CG2   . ILE   A 147 ? 0.4246 0.1848 0.3046 0.0565  -0.1175 -0.0221 172 ILE   A CG2   
2345  C  CD1   . ILE   A 147 ? 0.4280 0.2187 0.2755 0.0355  -0.0778 -0.0113 172 ILE   A CD1   
2357  N  N     . PHE   A 148 ? 0.3058 0.1762 0.3043 0.0421  -0.1377 -0.0227 173 PHE   A N     
2358  C  CA    . PHE   A 148 ? 0.2717 0.1832 0.3113 0.0107  -0.1326 -0.0106 173 PHE   A CA    
2359  C  C     . PHE   A 148 ? 0.2853 0.2026 0.3343 -0.0035 -0.1197 -0.0234 173 PHE   A C     
2360  O  O     . PHE   A 148 ? 0.2571 0.2248 0.3345 -0.0010 -0.0900 -0.0093 173 PHE   A O     
2361  C  CB    . PHE   A 148 ? 0.2188 0.1848 0.3055 -0.0072 -0.1337 -0.0168 173 PHE   A CB    
2362  C  CG    . PHE   A 148 ? 0.2118 0.1819 0.3007 0.0138  -0.1121 -0.0027 173 PHE   A CG    
2363  C  CD1   . PHE   A 148 ? 0.2626 0.1965 0.3150 0.0059  -0.0936 -0.0029 173 PHE   A CD1   
2364  C  CD2   . PHE   A 148 ? 0.2640 0.2052 0.3005 0.0340  -0.1060 0.0092  173 PHE   A CD2   
2365  C  CE1   . PHE   A 148 ? 0.2833 0.1909 0.3187 0.0382  -0.0874 -0.0222 173 PHE   A CE1   
2366  C  CE2   . PHE   A 148 ? 0.2901 0.2147 0.3048 0.0401  -0.1139 0.0148  173 PHE   A CE2   
2367  C  CZ    . PHE   A 148 ? 0.3057 0.2045 0.3206 0.0358  -0.1043 -0.0090 173 PHE   A CZ    
2377  N  N     . SER   A 149 ? 0.2835 0.2150 0.3577 0.0247  -0.1498 -0.0222 174 SER   A N     
2378  C  CA    . SER   A 149 ? 0.2767 0.2230 0.3942 0.0289  -0.1652 -0.0581 174 SER   A CA    
2379  C  C     . SER   A 149 ? 0.3019 0.2452 0.4221 0.0365  -0.1719 -0.0573 174 SER   A C     
2380  O  O     . SER   A 149 ? 0.3549 0.2248 0.4131 0.0459  -0.1663 -0.0594 174 SER   A O     
2381  C  CB    . SER   A 149 ? 0.2990 0.2140 0.4082 0.0365  -0.1476 -0.0744 174 SER   A CB    
2382  O  OG    . SER   A 149 ? 0.2932 0.2190 0.4233 0.0090  -0.1605 -0.0583 174 SER   A OG    
2388  N  N     . THR   A 150 ? 0.3010 0.2360 0.4433 0.0006  -0.1853 -0.0817 175 THR   A N     
2389  C  CA    . THR   A 150 ? 0.3043 0.2483 0.4559 0.0386  -0.2089 -0.0751 175 THR   A CA    
2390  C  C     . THR   A 150 ? 0.3295 0.2510 0.4545 0.0592  -0.2170 -0.0993 175 THR   A C     
2391  O  O     . THR   A 150 ? 0.3802 0.2786 0.4560 0.0694  -0.2061 -0.1151 175 THR   A O     
2392  C  CB    . THR   A 150 ? 0.3464 0.2690 0.5028 0.0443  -0.1864 -0.0567 175 THR   A CB    
2393  O  OG1   . THR   A 150 ? 0.4236 0.2960 0.5340 -0.0251 -0.1408 -0.0568 175 THR   A OG1   
2394  C  CG2   . THR   A 150 ? 0.3428 0.2628 0.5108 0.0399  -0.2210 -0.0465 175 THR   A CG2   
2402  N  N     . LYS   A 151 ? 0.3720 0.2398 0.4606 0.0788  -0.2167 -0.0866 176 LYS   A N     
2403  C  CA    . LYS   A 151 ? 0.3857 0.2603 0.4647 0.0560  -0.2150 -0.0922 176 LYS   A CA    
2404  C  C     . LYS   A 151 ? 0.3874 0.2452 0.4458 0.0513  -0.2054 -0.0914 176 LYS   A C     
2405  O  O     . LYS   A 151 ? 0.3514 0.2436 0.4437 0.0679  -0.1824 -0.0948 176 LYS   A O     
2406  C  CB    . LYS   A 151 ? 0.4359 0.3210 0.4862 0.0516  -0.2227 -0.1071 176 LYS   A CB    
2407  C  CG    . LYS   A 151 ? 0.4929 0.4056 0.5162 0.0419  -0.1986 -0.0888 176 LYS   A CG    
2408  C  CD    . LYS   A 151 ? 0.5062 0.4845 0.5498 0.0407  -0.1941 -0.0560 176 LYS   A CD    
2409  C  CE    . LYS   A 151 ? 0.5584 0.5463 0.5858 0.0398  -0.1667 -0.0411 176 LYS   A CE    
2410  N  NZ    . LYS   A 151 ? 0.5982 0.5868 0.6095 0.0283  -0.1439 -0.0382 176 LYS   A NZ    
2424  N  N     . PHE   A 152 ? 0.3786 0.2704 0.4367 0.0590  -0.2118 -0.0741 177 PHE   A N     
2425  C  CA    . PHE   A 152 ? 0.3809 0.2655 0.4008 0.0869  -0.2237 -0.0614 177 PHE   A CA    
2426  C  C     . PHE   A 152 ? 0.4019 0.2904 0.4113 0.1144  -0.2243 -0.0705 177 PHE   A C     
2427  O  O     . PHE   A 152 ? 0.4251 0.3160 0.4205 0.1109  -0.2390 -0.0733 177 PHE   A O     
2428  C  CB    . PHE   A 152 ? 0.3955 0.2569 0.3786 0.0530  -0.2072 -0.0477 177 PHE   A CB    
2429  C  CG    . PHE   A 152 ? 0.4027 0.2502 0.3437 0.0589  -0.2083 -0.0418 177 PHE   A CG    
2430  C  CD1   . PHE   A 152 ? 0.4294 0.2663 0.3422 0.0415  -0.2079 -0.0263 177 PHE   A CD1   
2431  C  CD2   . PHE   A 152 ? 0.3909 0.2451 0.3258 0.0469  -0.1729 -0.0387 177 PHE   A CD2   
2432  C  CE1   . PHE   A 152 ? 0.4358 0.2643 0.3291 0.0531  -0.1993 -0.0275 177 PHE   A CE1   
2433  C  CE2   . PHE   A 152 ? 0.3773 0.2334 0.3083 0.0632  -0.1578 -0.0346 177 PHE   A CE2   
2434  C  CZ    . PHE   A 152 ? 0.3709 0.2444 0.3075 0.0664  -0.1818 -0.0214 177 PHE   A CZ    
2444  N  N     . THR   A 153 ? 0.4156 0.2801 0.4200 0.1078  -0.2363 -0.0781 178 THR   A N     
2445  C  CA    . THR   A 153 ? 0.4316 0.2909 0.4484 0.0920  -0.2553 -0.0800 178 THR   A CA    
2446  C  C     . THR   A 153 ? 0.4598 0.2621 0.4421 0.0963  -0.2615 -0.0788 178 THR   A C     
2447  O  O     . THR   A 153 ? 0.4742 0.2592 0.4424 0.0819  -0.2659 -0.0543 178 THR   A O     
2448  C  CB    . THR   A 153 ? 0.4171 0.3375 0.4893 0.1071  -0.2558 -0.0868 178 THR   A CB    
2449  O  OG1   . THR   A 153 ? 0.4157 0.3465 0.5100 0.1087  -0.2598 -0.0959 178 THR   A OG1   
2450  C  CG2   . THR   A 153 ? 0.4326 0.3580 0.5047 0.1258  -0.2570 -0.0820 178 THR   A CG2   
2458  N  N     . VAL   A 154 ? 0.4836 0.2765 0.4495 0.0978  -0.2697 -0.0712 179 VAL   A N     
2459  C  CA    . VAL   A 154 ? 0.4769 0.2756 0.4582 0.1119  -0.2608 -0.0682 179 VAL   A CA    
2460  C  C     . VAL   A 154 ? 0.5120 0.2988 0.4680 0.1124  -0.2798 -0.0747 179 VAL   A C     
2461  O  O     . VAL   A 154 ? 0.5451 0.2954 0.4696 0.1282  -0.2887 -0.0955 179 VAL   A O     
2462  C  CB    . VAL   A 154 ? 0.5137 0.2598 0.4707 0.0898  -0.2629 -0.0393 179 VAL   A CB    
2463  C  CG1   . VAL   A 154 ? 0.5814 0.2721 0.4727 0.0506  -0.2313 -0.0231 179 VAL   A CG1   
2464  C  CG2   . VAL   A 154 ? 0.4733 0.2740 0.4860 0.0848  -0.2662 -0.0289 179 VAL   A CG2   
2474  N  N     . GLU   A 155 ? 0.4876 0.2925 0.4699 0.1052  -0.2727 -0.0658 180 GLU   A N     
2475  C  CA    . GLU   A 155 ? 0.5245 0.2969 0.4910 0.1163  -0.2889 -0.0786 180 GLU   A CA    
2476  C  C     . GLU   A 155 ? 0.5961 0.2936 0.4743 0.1412  -0.2959 -0.0938 180 GLU   A C     
2477  O  O     . GLU   A 155 ? 0.6114 0.2938 0.4459 0.1500  -0.2885 -0.0986 180 GLU   A O     
2478  C  CB    . GLU   A 155 ? 0.5170 0.3413 0.5283 0.1433  -0.2745 -0.0610 180 GLU   A CB    
2479  C  CG    . GLU   A 155 ? 0.5308 0.3757 0.5905 0.1574  -0.2888 -0.0694 180 GLU   A CG    
2480  C  CD    . GLU   A 155 ? 0.5021 0.4176 0.6483 0.1461  -0.3025 -0.0767 180 GLU   A CD    
2481  O  OE1   . GLU   A 155 ? 0.4785 0.4518 0.6690 0.1337  -0.2963 -0.0445 180 GLU   A OE1   
2482  O  OE2   . GLU   A 155 ? 0.4963 0.4293 0.6644 0.1395  -0.3134 -0.1033 180 GLU   A OE2   
2489  N  N     . THR   A 156 ? 0.5980 0.3259 0.4701 0.1500  -0.2915 -0.0850 181 THR   A N     
2490  C  CA    . THR   A 156 ? 0.6110 0.3159 0.4720 0.1497  -0.2910 -0.0798 181 THR   A CA    
2491  C  C     . THR   A 156 ? 0.6474 0.3309 0.4796 0.1575  -0.3020 -0.0830 181 THR   A C     
2492  O  O     . THR   A 156 ? 0.6396 0.3463 0.4696 0.1893  -0.2792 -0.0935 181 THR   A O     
2493  C  CB    . THR   A 156 ? 0.6915 0.2998 0.4774 0.1323  -0.3219 -0.0831 181 THR   A CB    
2494  O  OG1   . THR   A 156 ? 0.6913 0.2965 0.4648 0.1450  -0.3126 -0.0907 181 THR   A OG1   
2495  C  CG2   . THR   A 156 ? 0.7468 0.3179 0.4884 0.1183  -0.3387 -0.0770 181 THR   A CG2   
2503  N  N     . ALA   A 157 ? 0.6234 0.3289 0.4909 0.1410  -0.3043 -0.0709 182 ALA   A N     
2504  C  CA    . ALA   A 157 ? 0.6282 0.3323 0.4887 0.1425  -0.3041 -0.0700 182 ALA   A CA    
2505  C  C     . ALA   A 157 ? 0.6539 0.3198 0.4901 0.1373  -0.3157 -0.0778 182 ALA   A C     
2506  O  O     . ALA   A 157 ? 0.6498 0.3145 0.4826 0.1223  -0.3132 -0.0627 182 ALA   A O     
2507  C  CB    . ALA   A 157 ? 0.6087 0.3617 0.4886 0.1511  -0.2988 -0.0717 182 ALA   A CB    
2513  N  N     . SER   A 158 ? 0.6475 0.3152 0.4863 0.1254  -0.3178 -0.0758 183 SER   A N     
2514  C  CA    . SER   A 158 ? 0.6580 0.3201 0.4870 0.1397  -0.3053 -0.0616 183 SER   A CA    
2515  C  C     . SER   A 158 ? 0.6720 0.3319 0.4947 0.1408  -0.3097 -0.0558 183 SER   A C     
2516  O  O     . SER   A 158 ? 0.7188 0.3374 0.4905 0.1582  -0.3046 -0.0555 183 SER   A O     
2517  C  CB    . SER   A 158 ? 0.7353 0.3196 0.4898 0.1218  -0.3232 -0.0448 183 SER   A CB    
2518  O  OG    . SER   A 158 ? 0.7910 0.3409 0.4965 0.1219  -0.3083 -0.0192 183 SER   A OG    
2524  N  N     . ARG   A 159 ? 0.6165 0.3338 0.4977 0.1338  -0.2992 -0.0487 184 ARG   A N     
2525  C  CA    . ARG   A 159 ? 0.6156 0.3574 0.5209 0.1489  -0.2726 -0.0049 184 ARG   A CA    
2526  C  C     . ARG   A 159 ? 0.6467 0.3328 0.5276 0.1227  -0.3033 -0.0173 184 ARG   A C     
2527  O  O     . ARG   A 159 ? 0.6813 0.3063 0.5215 0.1028  -0.3055 -0.0071 184 ARG   A O     
2528  C  CB    . ARG   A 159 ? 0.6369 0.4112 0.5596 0.1856  -0.2541 0.0228  184 ARG   A CB    
2529  C  CG    . ARG   A 159 ? 0.6695 0.4566 0.6013 0.2166  -0.2566 0.0259  184 ARG   A CG    
2530  C  CD    . ARG   A 159 ? 0.6999 0.4868 0.6295 0.2404  -0.2468 0.0416  184 ARG   A CD    
2531  N  NE    . ARG   A 159 ? 0.7656 0.5367 0.6538 0.1913  -0.2141 0.0451  184 ARG   A NE    
2532  C  CZ    . ARG   A 159 ? 0.8007 0.5771 0.6731 0.1201  -0.1775 0.0324  184 ARG   A CZ    
2533  N  NH1   . ARG   A 159 ? 0.8216 0.6037 0.6755 0.0651  -0.1678 0.0008  184 ARG   A NH1   
2534  N  NH2   . ARG   A 159 ? 0.8015 0.5938 0.6833 0.1084  -0.1702 0.0549  184 ARG   A NH2   
2548  N  N     . GLU   A 160 ? 0.6599 0.3296 0.5272 0.1127  -0.3041 -0.0047 185 GLU   A N     
2549  C  CA    . GLU   A 160 ? 0.7156 0.3628 0.5468 0.1246  -0.3181 0.0018  185 GLU   A CA    
2550  C  C     . GLU   A 160 ? 0.7725 0.3547 0.5391 0.1315  -0.3135 0.0014  185 GLU   A C     
2551  O  O     . GLU   A 160 ? 0.7912 0.3700 0.5304 0.1029  -0.3243 0.0147  185 GLU   A O     
2552  C  CB    . GLU   A 160 ? 0.7726 0.3955 0.5751 0.1302  -0.3134 0.0228  185 GLU   A CB    
2553  C  CG    . GLU   A 160 ? 0.8113 0.4349 0.5971 0.1287  -0.3237 0.0467  185 GLU   A CG    
2554  C  CD    . GLU   A 160 ? 0.8733 0.4980 0.6210 0.0978  -0.3229 0.0629  185 GLU   A CD    
2555  O  OE1   . GLU   A 160 ? 0.8955 0.5197 0.6234 0.1010  -0.3324 0.0741  185 GLU   A OE1   
2556  O  OE2   . GLU   A 160 ? 0.8933 0.5375 0.6363 0.0856  -0.3187 0.0657  185 GLU   A OE2   
2563  N  N     . TYR   A 161 ? 0.7784 0.3534 0.5395 0.1451  -0.3152 -0.0146 186 TYR   A N     
2564  C  CA    . TYR   A 161 ? 0.7867 0.3602 0.5524 0.1544  -0.3220 -0.0235 186 TYR   A CA    
2565  C  C     . TYR   A 161 ? 0.7972 0.3759 0.5365 0.1455  -0.3430 -0.0456 186 TYR   A C     
2566  O  O     . TYR   A 161 ? 0.8209 0.3871 0.5499 0.1352  -0.3491 -0.0513 186 TYR   A O     
2567  C  CB    . TYR   A 161 ? 0.7586 0.3657 0.5692 0.1564  -0.3220 -0.0225 186 TYR   A CB    
2568  C  CG    . TYR   A 161 ? 0.7662 0.3824 0.5909 0.1520  -0.3186 0.0039  186 TYR   A CG    
2569  C  CD1   . TYR   A 161 ? 0.7267 0.3910 0.5970 0.1537  -0.2950 0.0331  186 TYR   A CD1   
2570  C  CD2   . TYR   A 161 ? 0.7841 0.3997 0.6102 0.1406  -0.3282 0.0172  186 TYR   A CD2   
2571  C  CE1   . TYR   A 161 ? 0.7803 0.4087 0.6171 0.1570  -0.3032 0.0466  186 TYR   A CE1   
2572  C  CE2   . TYR   A 161 ? 0.8241 0.4256 0.6291 0.1220  -0.3117 0.0277  186 TYR   A CE2   
2573  C  CZ    . TYR   A 161 ? 0.8374 0.4393 0.6420 0.1152  -0.2935 0.0332  186 TYR   A CZ    
2574  O  OH    . TYR   A 161 ? 0.8965 0.4625 0.6657 0.0870  -0.2575 0.0300  186 TYR   A OH    
2584  N  N     . LYS   A 162 ? 0.7760 0.3972 0.5278 0.1683  -0.3339 -0.0492 187 LYS   A N     
2585  C  CA    . LYS   A 162 ? 0.7367 0.4160 0.5218 0.1820  -0.3190 -0.0496 187 LYS   A CA    
2586  C  C     . LYS   A 162 ? 0.7452 0.4200 0.5140 0.2088  -0.3181 -0.0840 187 LYS   A C     
2587  O  O     . LYS   A 162 ? 0.7599 0.4246 0.5153 0.2088  -0.3301 -0.0990 187 LYS   A O     
2588  C  CB    . LYS   A 162 ? 0.7691 0.4473 0.5367 0.1914  -0.3065 -0.0087 187 LYS   A CB    
2589  C  CG    . LYS   A 162 ? 0.7934 0.4877 0.5658 0.2236  -0.2864 0.0195  187 LYS   A CG    
2590  C  CD    . LYS   A 162 ? 0.8625 0.5416 0.6038 0.2368  -0.2671 0.0283  187 LYS   A CD    
2591  C  CE    . LYS   A 162 ? 0.9037 0.5823 0.6235 0.2229  -0.2618 0.0291  187 LYS   A CE    
2592  N  NZ    . LYS   A 162 ? 0.9471 0.6096 0.6401 0.2014  -0.2367 0.0052  187 LYS   A NZ    
2606  N  N     . LYS   A 163 ? 0.7023 0.4110 0.4978 0.2129  -0.2981 -0.0860 188 LYS   A N     
2607  C  CA    . LYS   A 163 ? 0.7267 0.4385 0.4994 0.1961  -0.3015 -0.0453 188 LYS   A CA    
2608  C  C     . LYS   A 163 ? 0.7537 0.4077 0.5082 0.1804  -0.3260 -0.0665 188 LYS   A C     
2609  O  O     . LYS   A 163 ? 0.7742 0.3591 0.5088 0.1776  -0.3387 -0.0961 188 LYS   A O     
2610  C  CB    . LYS   A 163 ? 0.8025 0.5092 0.4990 0.1970  -0.3017 0.0006  188 LYS   A CB    
2611  C  CG    . LYS   A 163 ? 0.9279 0.5941 0.5095 0.1962  -0.2718 0.0096  188 LYS   A CG    
2612  C  CD    . LYS   A 163 ? 0.9981 0.6604 0.5134 0.1793  -0.2430 -0.0020 188 LYS   A CD    
2613  C  CE    . LYS   A 163 ? 1.0261 0.7163 0.5135 0.1528  -0.2486 -0.0163 188 LYS   A CE    
2614  N  NZ    . LYS   A 163 ? 1.0584 0.7551 0.5172 0.1305  -0.2439 -0.0248 188 LYS   A NZ    
2628  N  N     . MET   A 164 ? 0.7384 0.4111 0.5177 0.1600  -0.3327 -0.0534 189 MET   A N     
2629  C  CA    . MET   A 164 ? 0.7313 0.4076 0.5301 0.1612  -0.3372 -0.0589 189 MET   A CA    
2630  C  C     . MET   A 164 ? 0.7251 0.3977 0.4917 0.1600  -0.3251 -0.0734 189 MET   A C     
2631  O  O     . MET   A 164 ? 0.7010 0.3928 0.4679 0.1721  -0.3032 -0.0674 189 MET   A O     
2632  C  CB    . MET   A 164 ? 0.7904 0.4461 0.5774 0.1721  -0.3659 -0.0589 189 MET   A CB    
2633  C  CG    . MET   A 164 ? 0.8807 0.5208 0.6351 0.1343  -0.3702 -0.0736 189 MET   A CG    
2634  S  SD    . MET   A 164 ? 0.9521 0.5857 0.6791 0.1074  -0.3813 -0.0803 189 MET   A SD    
2635  C  CE    . MET   A 164 ? 0.9646 0.6032 0.7061 0.0781  -0.3582 -0.0883 189 MET   A CE    
2645  N  N     . PHE   A 165 ? 0.6519 0.3681 0.4712 0.1448  -0.3040 -0.0627 190 PHE   A N     
2646  C  CA    . PHE   A 165 ? 0.6543 0.3426 0.4543 0.1322  -0.3052 -0.0756 190 PHE   A CA    
2647  C  C     . PHE   A 165 ? 0.6532 0.3269 0.4519 0.1475  -0.3024 -0.0929 190 PHE   A C     
2648  O  O     . PHE   A 165 ? 0.6316 0.3462 0.4470 0.1625  -0.2909 -0.0937 190 PHE   A O     
2649  C  CB    . PHE   A 165 ? 0.6669 0.3281 0.4467 0.1303  -0.2932 -0.0464 190 PHE   A CB    
2650  C  CG    . PHE   A 165 ? 0.6734 0.3233 0.4366 0.1431  -0.2865 -0.0554 190 PHE   A CG    
2651  C  CD1   . PHE   A 165 ? 0.6426 0.3070 0.4376 0.1383  -0.2842 -0.0615 190 PHE   A CD1   
2652  C  CD2   . PHE   A 165 ? 0.6780 0.3112 0.4417 0.1503  -0.2795 -0.0555 190 PHE   A CD2   
2653  C  CE1   . PHE   A 165 ? 0.6490 0.3115 0.4391 0.1393  -0.2808 -0.0522 190 PHE   A CE1   
2654  C  CE2   . PHE   A 165 ? 0.6718 0.3224 0.4473 0.1561  -0.2802 -0.0567 190 PHE   A CE2   
2655  C  CZ    . PHE   A 165 ? 0.6738 0.3091 0.4483 0.1472  -0.2739 -0.0504 190 PHE   A CZ    
2665  N  N     . LYS   A 166 ? 0.6437 0.3174 0.4604 0.1634  -0.2928 -0.0928 191 LYS   A N     
2666  C  CA    . LYS   A 166 ? 0.6481 0.3224 0.4801 0.1523  -0.3123 -0.1072 191 LYS   A CA    
2667  C  C     . LYS   A 166 ? 0.6288 0.3369 0.4809 0.1498  -0.3114 -0.1110 191 LYS   A C     
2668  O  O     . LYS   A 166 ? 0.6226 0.3533 0.4789 0.1331  -0.3115 -0.0970 191 LYS   A O     
2669  C  CB    . LYS   A 166 ? 0.6139 0.3437 0.4936 0.1530  -0.3124 -0.1161 191 LYS   A CB    
2670  C  CG    . LYS   A 166 ? 0.6587 0.4027 0.5182 0.1474  -0.2811 -0.1024 191 LYS   A CG    
2671  C  CD    . LYS   A 166 ? 0.6908 0.4628 0.5471 0.1532  -0.2432 -0.0807 191 LYS   A CD    
2672  C  CE    . LYS   A 166 ? 0.6991 0.5021 0.5761 0.1689  -0.2100 -0.0605 191 LYS   A CE    
2673  N  NZ    . LYS   A 166 ? 0.7064 0.5194 0.5923 0.1627  -0.1890 -0.0636 191 LYS   A NZ    
2687  N  N     . GLN   A 167 ? 0.6092 0.3039 0.4776 0.1563  -0.3043 -0.1207 192 GLN   A N     
2688  C  CA    . GLN   A 167 ? 0.6193 0.3264 0.4778 0.1614  -0.3047 -0.1156 192 GLN   A CA    
2689  C  C     . GLN   A 167 ? 0.6133 0.3170 0.4786 0.1577  -0.3026 -0.1104 192 GLN   A C     
2690  O  O     . GLN   A 167 ? 0.6297 0.2984 0.4909 0.1398  -0.3173 -0.1068 192 GLN   A O     
2691  C  CB    . GLN   A 167 ? 0.6512 0.3815 0.4861 0.1644  -0.3153 -0.1177 192 GLN   A CB    
2692  C  CG    . GLN   A 167 ? 0.6643 0.4260 0.4985 0.1831  -0.3146 -0.1267 192 GLN   A CG    
2693  C  CD    . GLN   A 167 ? 0.6857 0.4805 0.5122 0.1607  -0.2974 -0.1442 192 GLN   A CD    
2694  O  OE1   . GLN   A 167 ? 0.7152 0.5113 0.5139 0.1486  -0.2848 -0.1551 192 GLN   A OE1   
2695  N  NE2   . GLN   A 167 ? 0.6671 0.4983 0.5218 0.1704  -0.2916 -0.1592 192 GLN   A NE2   
2704  N  N     . THR   A 168 ? 0.5899 0.3225 0.4755 0.1644  -0.2889 -0.1063 193 THR   A N     
2705  C  CA    . THR   A 168 ? 0.6002 0.3257 0.4831 0.1709  -0.2897 -0.1083 193 THR   A CA    
2706  C  C     . THR   A 168 ? 0.5691 0.3210 0.4566 0.1516  -0.2867 -0.1116 193 THR   A C     
2707  O  O     . THR   A 168 ? 0.6475 0.3406 0.4719 0.1764  -0.2910 -0.1271 193 THR   A O     
2708  C  CB    . THR   A 168 ? 0.5819 0.3402 0.5156 0.1460  -0.3129 -0.1159 193 THR   A CB    
2709  O  OG1   . THR   A 168 ? 0.5924 0.3501 0.5450 0.1202  -0.3307 -0.1115 193 THR   A OG1   
2710  C  CG2   . THR   A 168 ? 0.5817 0.3407 0.5178 0.1436  -0.3139 -0.1128 193 THR   A CG2   
2718  N  N     . TRP   A 169 ? 0.5190 0.2948 0.4264 0.1242  -0.2664 -0.0843 194 TRP   A N     
2719  C  CA    . TRP   A 169 ? 0.5195 0.2839 0.4098 0.1187  -0.2625 -0.1004 194 TRP   A CA    
2720  C  C     . TRP   A 169 ? 0.5169 0.2844 0.4143 0.1316  -0.2621 -0.1014 194 TRP   A C     
2721  O  O     . TRP   A 169 ? 0.5100 0.3056 0.4106 0.1430  -0.2563 -0.1073 194 TRP   A O     
2722  C  CB    . TRP   A 169 ? 0.5344 0.2809 0.3993 0.0988  -0.2637 -0.0836 194 TRP   A CB    
2723  C  CG    . TRP   A 169 ? 0.5697 0.3097 0.3988 0.0866  -0.2720 -0.0622 194 TRP   A CG    
2724  C  CD1   . TRP   A 169 ? 0.6028 0.3009 0.3941 0.0981  -0.2704 -0.0425 194 TRP   A CD1   
2725  C  CD2   . TRP   A 169 ? 0.5668 0.2875 0.3960 0.0895  -0.2701 -0.0631 194 TRP   A CD2   
2726  N  NE1   . TRP   A 169 ? 0.6264 0.2884 0.3907 0.1054  -0.2690 -0.0434 194 TRP   A NE1   
2727  C  CE2   . TRP   A 169 ? 0.6075 0.2697 0.3978 0.1007  -0.2726 -0.0507 194 TRP   A CE2   
2728  C  CE3   . TRP   A 169 ? 0.5770 0.2968 0.4028 0.0884  -0.2731 -0.0438 194 TRP   A CE3   
2729  C  CZ2   . TRP   A 169 ? 0.6293 0.2708 0.4123 0.1182  -0.2666 -0.0469 194 TRP   A CZ2   
2730  C  CZ3   . TRP   A 169 ? 0.6130 0.2882 0.4093 0.1048  -0.2562 -0.0354 194 TRP   A CZ3   
2731  C  CH2   . TRP   A 169 ? 0.6318 0.2737 0.4133 0.1172  -0.2630 -0.0366 194 TRP   A CH2   
2742  N  N     . MET   A 170 ? 0.5000 0.2829 0.4401 0.1307  -0.2601 -0.0859 195 MET   A N     
2743  C  CA    . MET   A 170 ? 0.4842 0.2954 0.4603 0.1139  -0.2700 -0.0954 195 MET   A CA    
2744  C  C     . MET   A 170 ? 0.4859 0.2853 0.4494 0.0905  -0.2433 -0.0930 195 MET   A C     
2745  O  O     . MET   A 170 ? 0.5108 0.2767 0.4470 0.0809  -0.2301 -0.0813 195 MET   A O     
2746  C  CB    . MET   A 170 ? 0.5331 0.3391 0.4917 0.0801  -0.2874 -0.1225 195 MET   A CB    
2747  C  CG    . MET   A 170 ? 0.6001 0.3958 0.5258 0.0988  -0.3131 -0.1283 195 MET   A CG    
2748  S  SD    . MET   A 170 ? 0.6907 0.4573 0.5658 0.1323  -0.3202 -0.1208 195 MET   A SD    
2749  C  CE    . MET   A 170 ? 0.7024 0.4777 0.5791 0.1440  -0.3308 -0.1152 195 MET   A CE    
2759  N  N     . ASP   A 171 ? 0.4691 0.2574 0.4369 0.0772  -0.2560 -0.0993 196 ASP   A N     
2760  C  CA    . ASP   A 171 ? 0.5120 0.2738 0.4405 0.0763  -0.2351 -0.0987 196 ASP   A CA    
2761  C  C     . ASP   A 171 ? 0.5226 0.2438 0.3995 0.0658  -0.2005 -0.0814 196 ASP   A C     
2762  O  O     . ASP   A 171 ? 0.5455 0.2495 0.3966 0.0721  -0.1939 -0.0729 196 ASP   A O     
2763  C  CB    . ASP   A 171 ? 0.5202 0.3214 0.4719 0.0652  -0.2664 -0.1216 196 ASP   A CB    
2764  C  CG    . ASP   A 171 ? 0.5769 0.3735 0.5112 0.0762  -0.2432 -0.1519 196 ASP   A CG    
2765  O  OD1   . ASP   A 171 ? 0.6151 0.3691 0.5348 0.0790  -0.2333 -0.1534 196 ASP   A OD1   
2766  O  OD2   . ASP   A 171 ? 0.5842 0.4295 0.5244 0.0614  -0.2429 -0.1660 196 ASP   A OD2   
2771  N  N     . ASN   A 172 ? 0.4810 0.2196 0.3612 0.0685  -0.1761 -0.0786 197 ASN   A N     
2772  C  CA    . ASN   A 172 ? 0.4572 0.2015 0.3448 0.0737  -0.1452 -0.0684 197 ASN   A CA    
2773  C  C     . ASN   A 172 ? 0.4788 0.2275 0.3318 0.0650  -0.1369 -0.0567 197 ASN   A C     
2774  O  O     . ASN   A 172 ? 0.4811 0.2448 0.3311 0.0795  -0.1532 -0.0601 197 ASN   A O     
2775  C  CB    . ASN   A 172 ? 0.4421 0.2074 0.3610 0.0684  -0.1327 -0.0483 197 ASN   A CB    
2776  C  CG    . ASN   A 172 ? 0.4196 0.2005 0.3909 0.0497  -0.1237 -0.0627 197 ASN   A CG    
2777  O  OD1   . ASN   A 172 ? 0.4712 0.2187 0.4220 0.0432  -0.0999 -0.0696 197 ASN   A OD1   
2778  N  ND2   . ASN   A 172 ? 0.3768 0.1920 0.3903 0.0286  -0.1298 -0.0437 197 ASN   A ND2   
2785  N  N     . MET   A 173 ? 0.4627 0.2349 0.3108 0.0729  -0.1615 -0.0385 198 MET   A N     
2786  C  CA    . MET   A 173 ? 0.5336 0.2686 0.3018 0.0757  -0.1476 -0.0531 198 MET   A CA    
2787  C  C     . MET   A 173 ? 0.5713 0.3164 0.3117 0.1036  -0.1366 -0.0596 198 MET   A C     
2788  O  O     . MET   A 173 ? 0.6381 0.3346 0.3181 0.0528  -0.1158 -0.0539 198 MET   A O     
2789  C  CB    . MET   A 173 ? 0.5733 0.2398 0.2993 0.1016  -0.1316 -0.0412 198 MET   A CB    
2790  C  CG    . MET   A 173 ? 0.6099 0.2480 0.2942 0.1044  -0.1438 -0.0271 198 MET   A CG    
2791  S  SD    . MET   A 173 ? 0.6292 0.2515 0.2827 0.1008  -0.1367 -0.0185 198 MET   A SD    
2792  C  CE    . MET   A 173 ? 0.6375 0.2565 0.2856 0.0600  -0.1272 -0.0340 198 MET   A CE    
2802  N  N     . GLY   A 174 ? 0.5320 0.3491 0.3073 0.1305  -0.1789 -0.0861 199 GLY   A N     
2803  C  CA    . GLY   A 174 ? 0.5508 0.3843 0.3193 0.1428  -0.1807 -0.1064 199 GLY   A CA    
2804  C  C     . GLY   A 174 ? 0.6096 0.4319 0.3424 0.1555  -0.1786 -0.1141 199 GLY   A C     
2805  O  O     . GLY   A 174 ? 0.6397 0.4732 0.3538 0.1432  -0.1659 -0.0923 199 GLY   A O     
2809  N  N     . ARG   A 175 ? 0.6207 0.4317 0.3669 0.1865  -0.2060 -0.1185 200 ARG   A N     
2810  C  CA    . ARG   A 175 ? 0.6440 0.4334 0.3984 0.1604  -0.2336 -0.1442 200 ARG   A CA    
2811  C  C     . ARG   A 175 ? 0.6607 0.4193 0.4028 0.1860  -0.2507 -0.1229 200 ARG   A C     
2812  O  O     . ARG   A 175 ? 0.6323 0.3771 0.3997 0.1428  -0.2638 -0.1261 200 ARG   A O     
2813  C  CB    . ARG   A 175 ? 0.6500 0.4369 0.4338 0.1101  -0.2258 -0.1806 200 ARG   A CB    
2814  C  CG    . ARG   A 175 ? 0.6524 0.4636 0.4682 0.0662  -0.2105 -0.2097 200 ARG   A CG    
2815  C  CD    . ARG   A 175 ? 0.6656 0.5086 0.5093 0.0333  -0.1982 -0.2138 200 ARG   A CD    
2816  N  NE    . ARG   A 175 ? 0.6991 0.5612 0.5559 0.0036  -0.1900 -0.1986 200 ARG   A NE    
2817  C  CZ    . ARG   A 175 ? 0.7355 0.5909 0.5963 -0.0272 -0.1921 -0.1824 200 ARG   A CZ    
2818  N  NH1   . ARG   A 175 ? 0.7548 0.5982 0.6138 -0.0135 -0.1889 -0.1833 200 ARG   A NH1   
2819  N  NH2   . ARG   A 175 ? 0.7402 0.5968 0.6112 -0.0729 -0.1918 -0.1715 200 ARG   A NH2   
2833  N  N     . ALA   A 176 ? 0.6910 0.4516 0.4072 0.2045  -0.2467 -0.1043 201 ALA   A N     
2834  C  CA    . ALA   A 176 ? 0.6892 0.4420 0.4170 0.2281  -0.2551 -0.1137 201 ALA   A CA    
2835  C  C     . ALA   A 176 ? 0.6909 0.4588 0.4233 0.2117  -0.2775 -0.1446 201 ALA   A C     
2836  O  O     . ALA   A 176 ? 0.7224 0.4869 0.4233 0.2081  -0.2701 -0.1634 201 ALA   A O     
2837  C  CB    . ALA   A 176 ? 0.6930 0.4527 0.4177 0.2241  -0.2540 -0.0991 201 ALA   A CB    
2843  N  N     . GLY   A 177 ? 0.6791 0.4532 0.4498 0.1902  -0.2959 -0.1353 202 GLY   A N     
2844  C  CA    . GLY   A 177 ? 0.6806 0.4599 0.4845 0.1780  -0.3145 -0.1420 202 GLY   A CA    
2845  C  C     . GLY   A 177 ? 0.6891 0.4530 0.5140 0.1845  -0.3204 -0.1562 202 GLY   A C     
2846  O  O     . GLY   A 177 ? 0.7198 0.4380 0.5289 0.1773  -0.3241 -0.1607 202 GLY   A O     
2850  N  N     . GLU   A 178 ? 0.6571 0.4554 0.5148 0.1896  -0.3209 -0.1611 203 GLU   A N     
2851  C  CA    . GLU   A 178 ? 0.6747 0.4858 0.5266 0.1883  -0.3276 -0.1619 203 GLU   A CA    
2852  C  C     . GLU   A 178 ? 0.7259 0.4945 0.5327 0.2257  -0.3366 -0.1564 203 GLU   A C     
2853  O  O     . GLU   A 178 ? 0.7846 0.5246 0.5310 0.2756  -0.3222 -0.1341 203 GLU   A O     
2854  C  CB    . GLU   A 178 ? 0.6758 0.5352 0.5362 0.1525  -0.3339 -0.1435 203 GLU   A CB    
2855  C  CG    . GLU   A 178 ? 0.6912 0.5738 0.5771 0.1088  -0.3095 -0.1338 203 GLU   A CG    
2856  C  CD    . GLU   A 178 ? 0.7345 0.6206 0.6196 0.0853  -0.2679 -0.1332 203 GLU   A CD    
2857  O  OE1   . GLU   A 178 ? 0.7455 0.6562 0.6461 0.0754  -0.2411 -0.1217 203 GLU   A OE1   
2858  O  OE2   . GLU   A 178 ? 0.7548 0.6398 0.6293 0.0607  -0.2674 -0.1361 203 GLU   A OE2   
2865  N  N     . MET   A 179 ? 0.7201 0.4701 0.5478 0.1868  -0.3421 -0.1795 204 MET   A N     
2866  C  CA    . MET   A 179 ? 0.7292 0.4783 0.5569 0.2036  -0.3508 -0.1757 204 MET   A CA    
2867  C  C     . MET   A 179 ? 0.7421 0.4817 0.5583 0.2152  -0.3552 -0.1522 204 MET   A C     
2868  O  O     . MET   A 179 ? 0.7870 0.5391 0.5523 0.2054  -0.3620 -0.1432 204 MET   A O     
2869  C  CB    . MET   A 179 ? 0.7591 0.5116 0.5679 0.1909  -0.3529 -0.1630 204 MET   A CB    
2870  C  CG    . MET   A 179 ? 0.8302 0.5663 0.5834 0.1597  -0.3314 -0.1134 204 MET   A CG    
2871  S  SD    . MET   A 179 ? 0.8944 0.6137 0.5885 0.1498  -0.3101 -0.0756 204 MET   A SD    
2872  C  CE    . MET   A 179 ? 0.9008 0.6063 0.5834 0.1564  -0.3079 -0.0985 204 MET   A CE    
2882  N  N     . GLU   A 180 ? 0.7355 0.4383 0.5592 0.1998  -0.3581 -0.1479 205 GLU   A N     
2883  C  CA    . GLU   A 180 ? 0.7478 0.4515 0.5678 0.1952  -0.3648 -0.1384 205 GLU   A CA    
2884  C  C     . GLU   A 180 ? 0.7660 0.4320 0.5480 0.2011  -0.3593 -0.1475 205 GLU   A C     
2885  O  O     . GLU   A 180 ? 0.7662 0.4023 0.5375 0.2130  -0.3531 -0.1525 205 GLU   A O     
2886  C  CB    . GLU   A 180 ? 0.7483 0.5102 0.5978 0.1729  -0.3687 -0.1164 205 GLU   A CB    
2887  C  CG    . GLU   A 180 ? 0.7759 0.5865 0.6350 0.1178  -0.3494 -0.1058 205 GLU   A CG    
2888  C  CD    . GLU   A 180 ? 0.8119 0.6589 0.6759 0.0820  -0.3184 -0.0980 205 GLU   A CD    
2889  O  OE1   . GLU   A 180 ? 0.8302 0.6962 0.6821 0.0629  -0.3094 -0.0949 205 GLU   A OE1   
2890  O  OE2   . GLU   A 180 ? 0.8260 0.6892 0.7010 0.0779  -0.3034 -0.0882 205 GLU   A OE2   
2897  N  N     . LEU   A 181 ? 0.7604 0.4498 0.5370 0.1747  -0.3556 -0.1385 206 LEU   A N     
2898  C  CA    . LEU   A 181 ? 0.7699 0.4745 0.5356 0.1608  -0.3581 -0.1291 206 LEU   A CA    
2899  C  C     . LEU   A 181 ? 0.7516 0.4817 0.5527 0.1626  -0.3640 -0.1141 206 LEU   A C     
2900  O  O     . LEU   A 181 ? 0.7453 0.5041 0.5603 0.1494  -0.3672 -0.1178 206 LEU   A O     
2901  C  CB    . LEU   A 181 ? 0.7945 0.4827 0.5281 0.1304  -0.3572 -0.1270 206 LEU   A CB    
2902  C  CG    . LEU   A 181 ? 0.8453 0.5057 0.5254 0.0814  -0.3472 -0.1263 206 LEU   A CG    
2903  C  CD1   . LEU   A 181 ? 0.8635 0.5214 0.5312 0.0473  -0.3469 -0.1368 206 LEU   A CD1   
2904  C  CD2   . LEU   A 181 ? 0.8677 0.5075 0.5209 0.0643  -0.3361 -0.1230 206 LEU   A CD2   
2916  N  N     . LYS   A 182 ? 0.7339 0.4455 0.5657 0.1604  -0.3658 -0.1018 207 LYS   A N     
2917  C  CA    . LYS   A 182 ? 0.7327 0.4825 0.5790 0.1524  -0.3659 -0.0908 207 LYS   A CA    
2918  C  C     . LYS   A 182 ? 0.6779 0.4588 0.5746 0.1787  -0.3434 -0.0836 207 LYS   A C     
2919  O  O     . LYS   A 182 ? 0.6320 0.4322 0.5585 0.1834  -0.3201 -0.0869 207 LYS   A O     
2920  C  CB    . LYS   A 182 ? 0.7982 0.5481 0.5975 0.1183  -0.3592 -0.0800 207 LYS   A CB    
2921  C  CG    . LYS   A 182 ? 0.8450 0.6091 0.6186 0.0860  -0.3375 -0.0703 207 LYS   A CG    
2922  C  CD    . LYS   A 182 ? 0.8820 0.6612 0.6429 0.0575  -0.3062 -0.0701 207 LYS   A CD    
2923  C  CE    . LYS   A 182 ? 0.9192 0.7003 0.6646 0.0190  -0.2721 -0.0795 207 LYS   A CE    
2924  N  NZ    . LYS   A 182 ? 0.9398 0.7225 0.6771 0.0009  -0.2521 -0.0888 207 LYS   A NZ    
2938  N  N     . PRO   A 183 ? 0.6643 0.4696 0.5734 0.1759  -0.3383 -0.0742 208 PRO   A N     
2939  C  CA    . PRO   A 183 ? 0.6484 0.4635 0.5723 0.1798  -0.3330 -0.0820 208 PRO   A CA    
2940  C  C     . PRO   A 183 ? 0.6730 0.4668 0.5869 0.1833  -0.3462 -0.0918 208 PRO   A C     
2941  O  O     . PRO   A 183 ? 0.6970 0.4686 0.5943 0.1765  -0.3586 -0.0900 208 PRO   A O     
2942  C  CB    . PRO   A 183 ? 0.6519 0.4776 0.5662 0.1672  -0.3370 -0.0735 208 PRO   A CB    
2943  C  CG    . PRO   A 183 ? 0.6670 0.4945 0.5748 0.1627  -0.3462 -0.0710 208 PRO   A CG    
2944  C  CD    . PRO   A 183 ? 0.6589 0.4925 0.5828 0.1707  -0.3441 -0.0765 208 PRO   A CD    
2952  N  N     . PHE   A 184 ? 0.6411 0.4345 0.5821 0.1966  -0.3281 -0.1082 209 PHE   A N     
2953  C  CA    . PHE   A 184 ? 0.6581 0.4406 0.5886 0.2179  -0.3196 -0.1093 209 PHE   A CA    
2954  C  C     . PHE   A 184 ? 0.7072 0.4402 0.5879 0.2158  -0.3343 -0.0996 209 PHE   A C     
2955  O  O     . PHE   A 184 ? 0.7626 0.4243 0.5921 0.2144  -0.3397 -0.0844 209 PHE   A O     
2956  C  CB    . PHE   A 184 ? 0.6434 0.4535 0.5875 0.2083  -0.3235 -0.1057 209 PHE   A CB    
2957  C  CG    . PHE   A 184 ? 0.6571 0.4635 0.5907 0.2070  -0.3330 -0.1092 209 PHE   A CG    
2958  C  CD1   . PHE   A 184 ? 0.6543 0.4702 0.5900 0.2149  -0.3253 -0.1043 209 PHE   A CD1   
2959  C  CD2   . PHE   A 184 ? 0.6749 0.4826 0.5930 0.2206  -0.3285 -0.0975 209 PHE   A CD2   
2960  C  CE1   . PHE   A 184 ? 0.6387 0.4888 0.5982 0.2187  -0.3148 -0.0875 209 PHE   A CE1   
2961  C  CE2   . PHE   A 184 ? 0.6613 0.4978 0.5983 0.2374  -0.3119 -0.0940 209 PHE   A CE2   
2962  C  CZ    . PHE   A 184 ? 0.6443 0.4857 0.5942 0.2339  -0.3003 -0.0841 209 PHE   A CZ    
2972  N  N     . ASN   A 185 ? 0.6897 0.4606 0.5842 0.2344  -0.3103 -0.0893 210 ASN   A N     
2973  C  CA    . ASN   A 185 ? 0.7111 0.4759 0.5934 0.2670  -0.2853 -0.0881 210 ASN   A CA    
2974  C  C     . ASN   A 185 ? 0.7281 0.5081 0.5975 0.2836  -0.2868 -0.0888 210 ASN   A C     
2975  O  O     . ASN   A 185 ? 0.7675 0.5410 0.6040 0.2921  -0.3067 -0.1155 210 ASN   A O     
2976  C  CB    . ASN   A 185 ? 0.7239 0.4664 0.6086 0.2809  -0.2623 -0.0900 210 ASN   A CB    
2977  C  CG    . ASN   A 185 ? 0.7664 0.4918 0.6208 0.2664  -0.2614 -0.1034 210 ASN   A CG    
2978  O  OD1   . ASN   A 185 ? 0.8189 0.5005 0.6396 0.2465  -0.2339 -0.1274 210 ASN   A OD1   
2979  N  ND2   . ASN   A 185 ? 0.7427 0.5052 0.6125 0.2698  -0.2980 -0.0704 210 ASN   A ND2   
2986  N  N     . GLY   A 186 ? 0.6972 0.5001 0.5871 0.2577  -0.2893 -0.0654 211 GLY   A N     
2987  C  CA    . GLY   A 186 ? 0.6679 0.4849 0.5880 0.2504  -0.2791 -0.0617 211 GLY   A CA    
2988  C  C     . GLY   A 186 ? 0.6612 0.4660 0.5875 0.2178  -0.3006 -0.0532 211 GLY   A C     
2989  O  O     . GLY   A 186 ? 0.6845 0.4519 0.5795 0.1863  -0.3233 -0.0409 211 GLY   A O     
2993  N  N     . GLU   A 187 ? 0.6251 0.4678 0.6061 0.2255  -0.2690 -0.0462 212 GLU   A N     
2994  C  CA    . GLU   A 187 ? 0.5859 0.4464 0.6105 0.2156  -0.2643 -0.0426 212 GLU   A CA    
2995  C  C     . GLU   A 187 ? 0.5672 0.3802 0.5863 0.1744  -0.2814 -0.0566 212 GLU   A C     
2996  O  O     . GLU   A 187 ? 0.5818 0.3522 0.5737 0.1331  -0.3011 -0.0297 212 GLU   A O     
2997  C  CB    . GLU   A 187 ? 0.6294 0.4683 0.6515 0.2580  -0.2331 -0.0346 212 GLU   A CB    
2998  C  CG    . GLU   A 187 ? 0.7094 0.4867 0.6918 0.2622  -0.2324 -0.0157 212 GLU   A CG    
2999  C  CD    . GLU   A 187 ? 0.8033 0.5466 0.7275 0.2201  -0.2122 -0.0149 212 GLU   A CD    
3000  O  OE1   . GLU   A 187 ? 0.8470 0.5901 0.7391 0.1907  -0.1916 -0.0254 212 GLU   A OE1   
3001  O  OE2   . GLU   A 187 ? 0.8651 0.5495 0.7434 0.1932  -0.2070 0.0020  212 GLU   A OE2   
3008  N  N     . ASP   A 188 ? 0.5499 0.3632 0.5739 0.1614  -0.2806 -0.0567 213 ASP   A N     
3009  C  CA    . ASP   A 188 ? 0.5087 0.3486 0.5370 0.1417  -0.2757 -0.0606 213 ASP   A CA    
3010  C  C     . ASP   A 188 ? 0.5157 0.3224 0.5237 0.1210  -0.2681 -0.0612 213 ASP   A C     
3011  O  O     . ASP   A 188 ? 0.5068 0.3084 0.5234 0.1095  -0.2649 -0.0417 213 ASP   A O     
3012  C  CB    . ASP   A 188 ? 0.5918 0.3785 0.5335 0.1743  -0.2789 -0.0546 213 ASP   A CB    
3013  C  CG    . ASP   A 188 ? 0.6124 0.4035 0.5202 0.1808  -0.2891 -0.0588 213 ASP   A CG    
3014  O  OD1   . ASP   A 188 ? 0.6196 0.4227 0.5180 0.1897  -0.2827 -0.0479 213 ASP   A OD1   
3015  O  OD2   . ASP   A 188 ? 0.6335 0.3950 0.5023 0.1599  -0.3016 -0.0543 213 ASP   A OD2   
3020  N  N     . TYR   A 189 ? 0.5096 0.3280 0.4904 0.1607  -0.2415 -0.0570 214 TYR   A N     
3021  C  CA    . TYR   A 189 ? 0.5293 0.3316 0.4866 0.1570  -0.2673 -0.0821 214 TYR   A CA    
3022  C  C     . TYR   A 189 ? 0.5333 0.3169 0.4622 0.1539  -0.2624 -0.0811 214 TYR   A C     
3023  O  O     . TYR   A 189 ? 0.5335 0.3072 0.4522 0.1476  -0.2597 -0.0739 214 TYR   A O     
3024  C  CB    . TYR   A 189 ? 0.5223 0.3242 0.5162 0.1485  -0.2784 -0.0974 214 TYR   A CB    
3025  C  CG    . TYR   A 189 ? 0.5355 0.3567 0.5452 0.1301  -0.2962 -0.0961 214 TYR   A CG    
3026  C  CD1   . TYR   A 189 ? 0.5284 0.3752 0.5569 0.1031  -0.3164 -0.0904 214 TYR   A CD1   
3027  C  CD2   . TYR   A 189 ? 0.5364 0.3630 0.5470 0.1472  -0.3034 -0.1056 214 TYR   A CD2   
3028  C  CE1   . TYR   A 189 ? 0.5445 0.3689 0.5606 0.1119  -0.3132 -0.1066 214 TYR   A CE1   
3029  C  CE2   . TYR   A 189 ? 0.5472 0.3894 0.5541 0.1274  -0.3113 -0.0961 214 TYR   A CE2   
3030  C  CZ    . TYR   A 189 ? 0.5270 0.3804 0.5613 0.1212  -0.3132 -0.0976 214 TYR   A CZ    
3031  O  OH    . TYR   A 189 ? 0.5315 0.4091 0.5743 0.1269  -0.3161 -0.0935 214 TYR   A OH    
3041  N  N     . THR   A 190 ? 0.5113 0.2956 0.4436 0.1553  -0.2445 -0.0865 215 THR   A N     
3042  C  CA    . THR   A 190 ? 0.5025 0.2932 0.4468 0.1397  -0.2575 -0.0862 215 THR   A CA    
3043  C  C     . THR   A 190 ? 0.4720 0.2901 0.4557 0.1334  -0.2584 -0.1011 215 THR   A C     
3044  O  O     . THR   A 190 ? 0.4682 0.3137 0.4445 0.1477  -0.2479 -0.1010 215 THR   A O     
3045  C  CB    . THR   A 190 ? 0.5438 0.2936 0.4516 0.1271  -0.2681 -0.0582 215 THR   A CB    
3046  O  OG1   . THR   A 190 ? 0.5840 0.3118 0.4509 0.1173  -0.2844 -0.0512 215 THR   A OG1   
3047  C  CG2   . THR   A 190 ? 0.5304 0.2940 0.4538 0.1234  -0.2656 -0.0540 215 THR   A CG2   
3055  N  N     . CYS   A 191 ? 0.4518 0.2747 0.4756 0.1081  -0.2593 -0.0734 216 CYS   A N     
3056  C  CA    . CYS   A 191 ? 0.4247 0.2894 0.4979 0.0936  -0.2508 -0.0796 216 CYS   A CA    
3057  C  C     . CYS   A 191 ? 0.3942 0.2902 0.4811 0.1007  -0.2439 -0.0805 216 CYS   A C     
3058  O  O     . CYS   A 191 ? 0.4326 0.2916 0.4904 0.1091  -0.2560 -0.0741 216 CYS   A O     
3059  C  CB    . CYS   A 191 ? 0.4208 0.3374 0.5265 0.1314  -0.2467 -0.0779 216 CYS   A CB    
3060  S  SG    . CYS   A 191 ? 0.4553 0.3712 0.5598 0.1202  -0.2112 -0.0853 216 CYS   A SG    
3066  N  N     . ILE   A 192 ? 0.3657 0.2645 0.4637 0.0942  -0.2294 -0.0816 217 ILE   A N     
3067  C  CA    . ILE   A 192 ? 0.3398 0.2740 0.4554 0.0763  -0.2213 -0.0663 217 ILE   A CA    
3068  C  C     . ILE   A 192 ? 0.2974 0.2652 0.4534 0.0634  -0.2039 -0.0762 217 ILE   A C     
3069  O  O     . ILE   A 192 ? 0.2703 0.2863 0.4608 0.0746  -0.1715 -0.0489 217 ILE   A O     
3070  C  CB    . ILE   A 192 ? 0.3249 0.2807 0.4472 0.0548  -0.2075 -0.0220 217 ILE   A CB    
3071  C  CG1   . ILE   A 192 ? 0.3651 0.3216 0.4286 0.0238  -0.2180 0.0094  217 ILE   A CG1   
3072  C  CG2   . ILE   A 192 ? 0.3079 0.3047 0.4429 0.0651  -0.2015 -0.0259 217 ILE   A CG2   
3073  C  CD1   . ILE   A 192 ? 0.3946 0.3351 0.4260 0.0043  -0.2246 0.0303  217 ILE   A CD1   
3085  N  N     . THR   A 193 ? 0.3300 0.2560 0.4617 0.0736  -0.2138 -0.0982 218 THR   A N     
3086  C  CA    . THR   A 193 ? 0.3123 0.2714 0.4787 0.0677  -0.2142 -0.0915 218 THR   A CA    
3087  C  C     . THR   A 193 ? 0.3255 0.2730 0.4803 0.0886  -0.1972 -0.0689 218 THR   A C     
3088  O  O     . THR   A 193 ? 0.3753 0.2772 0.4984 0.1060  -0.1887 -0.0465 218 THR   A O     
3089  C  CB    . THR   A 193 ? 0.3374 0.3176 0.5025 0.0483  -0.2274 -0.1013 218 THR   A CB    
3090  O  OG1   . THR   A 193 ? 0.3385 0.3226 0.5127 0.0393  -0.2319 -0.0891 218 THR   A OG1   
3091  C  CG2   . THR   A 193 ? 0.3448 0.3382 0.4997 0.0557  -0.2316 -0.1019 218 THR   A CG2   
3099  N  N     . PHE   A 194 ? 0.3043 0.2572 0.4694 0.0650  -0.1835 -0.0650 219 PHE   A N     
3100  C  CA    . PHE   A 194 ? 0.3025 0.2637 0.4552 0.0477  -0.1614 -0.0373 219 PHE   A CA    
3101  C  C     . PHE   A 194 ? 0.2785 0.2508 0.4509 0.0137  -0.1489 -0.0495 219 PHE   A C     
3102  O  O     . PHE   A 194 ? 0.2531 0.2705 0.4544 0.0427  -0.1466 -0.0370 219 PHE   A O     
3103  C  CB    . PHE   A 194 ? 0.3142 0.2692 0.4595 0.0214  -0.1356 -0.0340 219 PHE   A CB    
3104  C  CG    . PHE   A 194 ? 0.3000 0.2917 0.4627 0.0097  -0.1093 -0.0487 219 PHE   A CG    
3105  C  CD1   . PHE   A 194 ? 0.3022 0.2810 0.4615 -0.0093 -0.1084 -0.0624 219 PHE   A CD1   
3106  C  CD2   . PHE   A 194 ? 0.2884 0.3072 0.4572 -0.0362 -0.1066 -0.0358 219 PHE   A CD2   
3107  C  CE1   . PHE   A 194 ? 0.3135 0.3024 0.4633 -0.0371 -0.0850 -0.0641 219 PHE   A CE1   
3108  C  CE2   . PHE   A 194 ? 0.2802 0.3270 0.4620 -0.0570 -0.0823 -0.0340 219 PHE   A CE2   
3109  C  CZ    . PHE   A 194 ? 0.2852 0.3318 0.4567 -0.0572 -0.0883 -0.0597 219 PHE   A CZ    
3119  N  N     . GLN   A 195 ? 0.2738 0.2332 0.4476 0.0203  -0.1594 -0.0467 220 GLN   A N     
3120  C  CA    . GLN   A 195 ? 0.2861 0.2465 0.4542 0.0162  -0.1716 -0.0529 220 GLN   A CA    
3121  C  C     . GLN   A 195 ? 0.2721 0.2280 0.4426 0.0174  -0.1436 -0.0506 220 GLN   A C     
3122  O  O     . GLN   A 195 ? 0.2741 0.2413 0.4400 0.0147  -0.1542 -0.0739 220 GLN   A O     
3123  C  CB    . GLN   A 195 ? 0.2774 0.3217 0.4884 0.0427  -0.1994 -0.0391 220 GLN   A CB    
3124  C  CG    . GLN   A 195 ? 0.3449 0.3991 0.5266 0.0024  -0.2089 -0.0383 220 GLN   A CG    
3125  C  CD    . GLN   A 195 ? 0.4282 0.5095 0.5604 -0.0954 -0.2249 -0.0415 220 GLN   A CD    
3126  O  OE1   . GLN   A 195 ? 0.5270 0.5785 0.5771 -0.1252 -0.1964 -0.0561 220 GLN   A OE1   
3127  N  NE2   . GLN   A 195 ? 0.4772 0.5246 0.5838 -0.1342 -0.2132 -0.0400 220 GLN   A NE2   
3136  N  N     . PRO   A 196 ? 0.2511 0.2266 0.4272 0.0342  -0.1275 -0.0312 221 PRO   A N     
3137  C  CA    . PRO   A 196 ? 0.2449 0.2287 0.4135 0.0363  -0.1197 -0.0117 221 PRO   A CA    
3138  C  C     . PRO   A 196 ? 0.2630 0.2104 0.4160 0.0220  -0.1213 -0.0083 221 PRO   A C     
3139  O  O     . PRO   A 196 ? 0.2621 0.2161 0.4297 -0.0044 -0.1082 -0.0064 221 PRO   A O     
3140  C  CB    . PRO   A 196 ? 0.2195 0.2915 0.4116 0.0242  -0.0971 -0.0180 221 PRO   A CB    
3141  C  CG    . PRO   A 196 ? 0.2810 0.3349 0.4158 0.0060  -0.1157 -0.0128 221 PRO   A CG    
3142  C  CD    . PRO   A 196 ? 0.2738 0.2898 0.4200 -0.0038 -0.1265 -0.0249 221 PRO   A CD    
3150  N  N     . ASP   A 197 ? 0.2585 0.1962 0.4102 0.0078  -0.1228 -0.0002 222 ASP   A N     
3151  C  CA    . ASP   A 197 ? 0.2361 0.1963 0.4147 0.0101  -0.1114 -0.0091 222 ASP   A CA    
3152  C  C     . ASP   A 197 ? 0.2181 0.2117 0.4113 -0.0102 -0.0819 -0.0034 222 ASP   A C     
3153  O  O     . ASP   A 197 ? 0.2094 0.1937 0.4010 -0.0085 -0.0617 0.0050  222 ASP   A O     
3154  C  CB    . ASP   A 197 ? 0.3063 0.1932 0.4268 -0.0004 -0.1203 -0.0260 222 ASP   A CB    
3155  C  CG    . ASP   A 197 ? 0.3484 0.2334 0.4435 0.0016  -0.1192 -0.0216 222 ASP   A CG    
3156  O  OD1   . ASP   A 197 ? 0.3681 0.2325 0.4512 0.0065  -0.1131 -0.0200 222 ASP   A OD1   
3157  O  OD2   . ASP   A 197 ? 0.3324 0.2494 0.4550 -0.0092 -0.0881 -0.0272 222 ASP   A OD2   
3162  N  N     . LEU   A 198 ? 0.2244 0.2148 0.4318 -0.0228 -0.1090 0.0026  223 LEU   A N     
3163  C  CA    . LEU   A 198 ? 0.2228 0.2070 0.4457 -0.0147 -0.0785 0.0232  223 LEU   A CA    
3164  C  C     . LEU   A 198 ? 0.1919 0.2079 0.4612 -0.0247 -0.0662 0.0247  223 LEU   A C     
3165  O  O     . LEU   A 198 ? 0.1798 0.2380 0.4651 -0.0097 -0.0601 0.0537  223 LEU   A O     
3166  C  CB    . LEU   A 198 ? 0.2127 0.2331 0.4507 0.0017  -0.0638 0.0290  223 LEU   A CB    
3167  C  CG    . LEU   A 198 ? 0.2236 0.2692 0.4545 -0.0280 -0.0422 0.0425  223 LEU   A CG    
3168  C  CD1   . LEU   A 198 ? 0.2408 0.3203 0.4755 -0.0028 -0.0066 0.0574  223 LEU   A CD1   
3169  C  CD2   . LEU   A 198 ? 0.2469 0.2676 0.4342 0.0097  -0.0533 0.0164  223 LEU   A CD2   
3181  N  N     . SER   A 199 ? 0.2401 0.1932 0.4833 -0.0210 -0.0696 -0.0075 224 SER   A N     
3182  C  CA    . SER   A 199 ? 0.2789 0.2077 0.5010 -0.0208 -0.0785 -0.0055 224 SER   A CA    
3183  C  C     . SER   A 199 ? 0.2642 0.1954 0.4874 -0.0043 -0.0760 0.0099  224 SER   A C     
3184  O  O     . SER   A 199 ? 0.2805 0.1927 0.5062 -0.0006 -0.0936 0.0201  224 SER   A O     
3185  C  CB    . SER   A 199 ? 0.3294 0.2463 0.5205 -0.0790 -0.0597 -0.0067 224 SER   A CB    
3186  O  OG    . SER   A 199 ? 0.3341 0.2621 0.5274 -0.0345 -0.0537 -0.0151 224 SER   A OG    
3192  N  N     . LYS   A 200 ? 0.2454 0.1741 0.4423 -0.0273 -0.0838 -0.0059 225 LYS   A N     
3193  C  CA    . LYS   A 200 ? 0.2487 0.1854 0.4155 -0.0294 -0.0326 0.0030  225 LYS   A CA    
3194  C  C     . LYS   A 200 ? 0.2277 0.1895 0.3923 -0.0167 -0.0247 0.0049  225 LYS   A C     
3195  O  O     . LYS   A 200 ? 0.2424 0.2505 0.3716 -0.0264 -0.0345 0.0092  225 LYS   A O     
3196  C  CB    . LYS   A 200 ? 0.2393 0.2312 0.4072 -0.0142 -0.0291 0.0084  225 LYS   A CB    
3197  C  CG    . LYS   A 200 ? 0.2984 0.2928 0.4067 -0.0090 -0.0534 -0.0122 225 LYS   A CG    
3198  C  CD    . LYS   A 200 ? 0.3315 0.3428 0.4091 -0.0012 -0.0840 -0.0240 225 LYS   A CD    
3199  C  CE    . LYS   A 200 ? 0.3876 0.3692 0.4084 0.0121  -0.0892 -0.0138 225 LYS   A CE    
3200  N  NZ    . LYS   A 200 ? 0.4836 0.3874 0.4103 -0.0061 -0.0757 -0.0288 225 LYS   A NZ    
3214  N  N     . PHE   A 201 ? 0.1944 0.1924 0.3842 -0.0171 -0.0321 0.0073  226 PHE   A N     
3215  C  CA    . PHE   A 201 ? 0.1874 0.1844 0.3835 -0.0071 -0.0158 -0.0147 226 PHE   A CA    
3216  C  C     . PHE   A 201 ? 0.2149 0.1706 0.3591 -0.0244 -0.0189 -0.0042 226 PHE   A C     
3217  O  O     . PHE   A 201 ? 0.2636 0.2201 0.3585 -0.0303 -0.0352 0.0060  226 PHE   A O     
3218  C  CB    . PHE   A 201 ? 0.2056 0.1767 0.3948 0.0097  -0.0270 -0.0093 226 PHE   A CB    
3219  C  CG    . PHE   A 201 ? 0.1871 0.1680 0.3909 -0.0198 -0.0623 -0.0010 226 PHE   A CG    
3220  C  CD1   . PHE   A 201 ? 0.2085 0.1988 0.3670 -0.0511 -0.0658 -0.0033 226 PHE   A CD1   
3221  C  CD2   . PHE   A 201 ? 0.2315 0.1910 0.4185 -0.0170 -0.0614 0.0148  226 PHE   A CD2   
3222  C  CE1   . PHE   A 201 ? 0.2236 0.2156 0.3616 -0.0563 -0.0663 0.0026  226 PHE   A CE1   
3223  C  CE2   . PHE   A 201 ? 0.2515 0.2001 0.4021 -0.0259 -0.0750 0.0206  226 PHE   A CE2   
3224  C  CZ    . PHE   A 201 ? 0.2239 0.1937 0.3609 -0.0351 -0.0912 0.0182  226 PHE   A CZ    
3234  N  N     . LYS   A 202 ? 0.2296 0.1686 0.3591 -0.0283 -0.0225 -0.0077 227 LYS   A N     
3235  C  CA    . LYS   A 202 ? 0.2213 0.1966 0.3646 -0.0133 -0.0407 0.0126  227 LYS   A CA    
3236  C  C     . LYS   A 202 ? 0.2248 0.1890 0.3472 -0.0124 -0.0344 0.0045  227 LYS   A C     
3237  O  O     . LYS   A 202 ? 0.2700 0.2340 0.3416 -0.0222 -0.0520 0.0111  227 LYS   A O     
3238  C  CB    . LYS   A 202 ? 0.2420 0.2582 0.4122 -0.0455 -0.0315 0.0377  227 LYS   A CB    
3239  C  CG    . LYS   A 202 ? 0.3032 0.3120 0.4631 0.0066  -0.0226 0.0661  227 LYS   A CG    
3240  C  CD    . LYS   A 202 ? 0.3494 0.3817 0.5076 0.0335  -0.0125 0.0801  227 LYS   A CD    
3241  C  CE    . LYS   A 202 ? 0.4761 0.4673 0.5416 0.0390  -0.0091 0.0667  227 LYS   A CE    
3242  N  NZ    . LYS   A 202 ? 0.5470 0.5135 0.5694 0.0557  -0.0128 0.0477  227 LYS   A NZ    
3256  N  N     . MET   A 203 ? 0.1759 0.1923 0.3550 -0.0157 -0.0295 -0.0156 228 MET   A N     
3257  C  CA    A MET   A 203 ? 0.1820 0.1974 0.3644 -0.0220 -0.0211 -0.0366 228 MET   A CA    
3258  C  CA    B MET   A 203 ? 0.1886 0.1994 0.3625 -0.0289 -0.0281 -0.0246 228 MET   A CA    
3259  C  C     . MET   A 203 ? 0.1964 0.1993 0.3552 -0.0470 -0.0211 -0.0255 228 MET   A C     
3260  O  O     . MET   A 203 ? 0.2682 0.2103 0.3369 -0.0306 -0.0059 -0.0319 228 MET   A O     
3261  C  CB    A MET   A 203 ? 0.1939 0.2104 0.3928 -0.0413 -0.0293 -0.0789 228 MET   A CB    
3262  C  CB    B MET   A 203 ? 0.2018 0.2146 0.3855 -0.0470 -0.0444 -0.0414 228 MET   A CB    
3263  C  CG    A MET   A 203 ? 0.2217 0.2254 0.4166 -0.0362 -0.0227 -0.0964 228 MET   A CG    
3264  C  CG    B MET   A 203 ? 0.2281 0.2462 0.4062 -0.0387 -0.0299 -0.0463 228 MET   A CG    
3265  S  SD    A MET   A 203 ? 0.1826 0.2369 0.4288 -0.0563 -0.0225 -0.1003 228 MET   A SD    
3266  S  SD    B MET   A 203 ? 0.2246 0.2834 0.4156 -0.0490 -0.0122 -0.0555 228 MET   A SD    
3267  C  CE    A MET   A 203 ? 0.1831 0.2499 0.4098 -0.0747 -0.0336 -0.0897 228 MET   A CE    
3268  C  CE    B MET   A 203 ? 0.1953 0.2876 0.4184 -0.0190 -0.0158 -0.0656 228 MET   A CE    
3287  N  N     . GLN   A 204 ? 0.2552 0.1952 0.3689 -0.0691 -0.0323 0.0022  229 GLN   A N     
3288  C  CA    . GLN   A 204 ? 0.2811 0.1939 0.3996 -0.0739 -0.0435 -0.0011 229 GLN   A CA    
3289  C  C     . GLN   A 204 ? 0.3010 0.2304 0.4431 -0.0918 -0.0885 0.0140  229 GLN   A C     
3290  O  O     . GLN   A 204 ? 0.3267 0.2787 0.4594 -0.1103 -0.1214 0.0269  229 GLN   A O     
3291  C  CB    . GLN   A 204 ? 0.3324 0.1910 0.4049 -0.0395 0.0043  -0.0119 229 GLN   A CB    
3292  C  CG    . GLN   A 204 ? 0.3907 0.1923 0.3967 -0.0069 0.0513  -0.0237 229 GLN   A CG    
3293  C  CD    . GLN   A 204 ? 0.3974 0.1950 0.4129 0.0108  0.0590  -0.0073 229 GLN   A CD    
3294  O  OE1   . GLN   A 204 ? 0.5085 0.2277 0.4087 -0.0050 0.0204  -0.0305 229 GLN   A OE1   
3295  N  NE2   . GLN   A 204 ? 0.3690 0.1827 0.4241 0.0260  0.0595  0.0095  229 GLN   A NE2   
3304  N  N     . SER   A 205 ? 0.2579 0.2041 0.4695 -0.0605 -0.0806 0.0101  230 SER   A N     
3305  C  CA    . SER   A 205 ? 0.2554 0.2389 0.5213 -0.0567 -0.0639 0.0135  230 SER   A CA    
3306  C  C     . SER   A 205 ? 0.2157 0.2356 0.5549 -0.0640 -0.0738 0.0029  230 SER   A C     
3307  O  O     . SER   A 205 ? 0.2052 0.2531 0.5704 -0.0448 -0.0552 0.0039  230 SER   A O     
3308  C  CB    . SER   A 205 ? 0.3008 0.2934 0.5375 -0.0819 -0.0218 0.0222  230 SER   A CB    
3309  O  OG    . SER   A 205 ? 0.3263 0.3321 0.5553 -0.0930 0.0242  0.0289  230 SER   A OG    
3315  N  N     . LEU   A 206 ? 0.1898 0.2443 0.5712 -0.0470 -0.0724 -0.0051 231 LEU   A N     
3316  C  CA    . LEU   A 206 ? 0.1735 0.2484 0.5747 -0.0300 -0.0785 -0.0143 231 LEU   A CA    
3317  C  C     . LEU   A 206 ? 0.1896 0.2691 0.5788 -0.0417 -0.0639 -0.0083 231 LEU   A C     
3318  O  O     . LEU   A 206 ? 0.2274 0.3050 0.5891 -0.0220 -0.0677 -0.0069 231 LEU   A O     
3319  C  CB    . LEU   A 206 ? 0.1851 0.2776 0.5745 0.0027  -0.0653 -0.0172 231 LEU   A CB    
3320  C  CG    . LEU   A 206 ? 0.1584 0.2970 0.5619 0.0252  -0.0664 -0.0119 231 LEU   A CG    
3321  C  CD1   . LEU   A 206 ? 0.1677 0.3243 0.5787 0.0187  -0.0816 -0.0097 231 LEU   A CD1   
3322  C  CD2   . LEU   A 206 ? 0.1875 0.3201 0.5595 0.0046  -0.0604 -0.0087 231 LEU   A CD2   
3334  N  N     . ASP   A 207 ? 0.2070 0.2403 0.5763 -0.0584 -0.0483 0.0020  232 ASP   A N     
3335  C  CA    . ASP   A 207 ? 0.2236 0.2421 0.5774 -0.0434 -0.0158 0.0180  232 ASP   A CA    
3336  C  C     . ASP   A 207 ? 0.2105 0.2492 0.5793 -0.0789 0.0116  0.0333  232 ASP   A C     
3337  O  O     . ASP   A 207 ? 0.2180 0.2628 0.5759 -0.0807 0.0382  0.0530  232 ASP   A O     
3338  C  CB    . ASP   A 207 ? 0.2293 0.2392 0.5691 -0.0143 -0.0154 0.0337  232 ASP   A CB    
3339  C  CG    . ASP   A 207 ? 0.2810 0.2365 0.5664 -0.0247 -0.0284 0.0467  232 ASP   A CG    
3340  O  OD1   . ASP   A 207 ? 0.2870 0.2237 0.5405 -0.0354 -0.0316 0.0422  232 ASP   A OD1   
3341  O  OD2   . ASP   A 207 ? 0.2971 0.2656 0.5815 -0.0170 -0.0336 0.0604  232 ASP   A OD2   
3346  N  N     . LYS   A 208 ? 0.2377 0.2590 0.5711 -0.0658 0.0173  0.0258  233 LYS   A N     
3347  C  CA    . LYS   A 208 ? 0.2168 0.2624 0.5565 -0.0747 0.0743  0.0410  233 LYS   A CA    
3348  C  C     . LYS   A 208 ? 0.1851 0.2597 0.5320 -0.0679 0.0489  0.0334  233 LYS   A C     
3349  O  O     . LYS   A 208 ? 0.1871 0.2383 0.5400 -0.0570 0.0654  0.0230  233 LYS   A O     
3350  C  CB    . LYS   A 208 ? 0.2799 0.3093 0.5626 -0.0593 0.1229  0.0507  233 LYS   A CB    
3351  C  CG    . LYS   A 208 ? 0.4313 0.3685 0.5757 -0.0573 0.1061  0.0654  233 LYS   A CG    
3352  C  CD    . LYS   A 208 ? 0.5393 0.4281 0.5870 -0.0179 0.0899  0.0750  233 LYS   A CD    
3353  C  CE    . LYS   A 208 ? 0.6525 0.4925 0.6028 0.0069  0.0692  0.0963  233 LYS   A CE    
3354  N  NZ    . LYS   A 208 ? 0.7173 0.5415 0.6183 0.0207  0.0571  0.1009  233 LYS   A NZ    
3368  N  N     . ASP   A 209 ? 0.1929 0.2247 0.5160 -0.0355 0.0494  0.0475  234 ASP   A N     
3369  C  CA    . ASP   A 209 ? 0.1752 0.2296 0.4789 -0.0413 0.0245  0.0537  234 ASP   A CA    
3370  C  C     . ASP   A 209 ? 0.1691 0.2231 0.4682 -0.0277 0.0108  0.0499  234 ASP   A C     
3371  O  O     . ASP   A 209 ? 0.1724 0.2170 0.4676 -0.0470 0.0208  0.0504  234 ASP   A O     
3372  C  CB    . ASP   A 209 ? 0.1943 0.2458 0.4576 -0.0176 0.0269  0.0674  234 ASP   A CB    
3373  C  CG    . ASP   A 209 ? 0.2142 0.2843 0.4553 -0.0196 0.0583  0.0610  234 ASP   A CG    
3374  O  OD1   . ASP   A 209 ? 0.2641 0.3243 0.4668 -0.0318 0.0499  0.0682  234 ASP   A OD1   
3375  O  OD2   . ASP   A 209 ? 0.2160 0.3041 0.4514 -0.0230 0.0676  0.0544  234 ASP   A OD2   
3380  N  N     . ILE   A 210 ? 0.2230 0.2174 0.4611 -0.0382 0.0127  0.0551  235 ILE   A N     
3381  C  CA    . ILE   A 210 ? 0.2036 0.2080 0.4510 -0.0247 -0.0001 0.0545  235 ILE   A CA    
3382  C  C     . ILE   A 210 ? 0.1839 0.2087 0.4547 -0.0485 -0.0022 0.0542  235 ILE   A C     
3383  O  O     . ILE   A 210 ? 0.1926 0.2012 0.4445 -0.0270 -0.0082 0.0300  235 ILE   A O     
3384  C  CB    . ILE   A 210 ? 0.1902 0.2156 0.4375 -0.0442 -0.0173 0.0342  235 ILE   A CB    
3385  C  CG1   . ILE   A 210 ? 0.1917 0.2154 0.4273 -0.0641 0.0016  0.0287  235 ILE   A CG1   
3386  C  CG2   . ILE   A 210 ? 0.1727 0.2369 0.4404 -0.0418 -0.0316 0.0146  235 ILE   A CG2   
3387  C  CD1   . ILE   A 210 ? 0.1951 0.2461 0.4150 -0.0810 0.0119  0.0160  235 ILE   A CD1   
3399  N  N     . VAL   A 211 ? 0.1733 0.2158 0.4791 -0.0567 -0.0315 0.0341  236 VAL   A N     
3400  C  CA    . VAL   A 211 ? 0.1689 0.2386 0.4819 -0.0418 -0.0277 0.0366  236 VAL   A CA    
3401  C  C     . VAL   A 211 ? 0.1588 0.2342 0.4628 -0.0191 -0.0125 0.0246  236 VAL   A C     
3402  O  O     . VAL   A 211 ? 0.1645 0.2164 0.4516 -0.0090 -0.0046 0.0101  236 VAL   A O     
3403  C  CB    . VAL   A 211 ? 0.1558 0.2866 0.5119 -0.0170 -0.0252 0.0151  236 VAL   A CB    
3404  C  CG1   . VAL   A 211 ? 0.1502 0.2775 0.5115 -0.0463 -0.0462 0.0027  236 VAL   A CG1   
3405  C  CG2   . VAL   A 211 ? 0.1897 0.3102 0.5268 -0.0358 -0.0346 0.0099  236 VAL   A CG2   
3415  N  N     . ALA   A 212 ? 0.1568 0.2519 0.4631 -0.0206 0.0011  0.0128  237 ALA   A N     
3416  C  CA    . ALA   A 212 ? 0.1679 0.2497 0.4524 -0.0203 0.0261  0.0272  237 ALA   A CA    
3417  C  C     . ALA   A 212 ? 0.1737 0.2200 0.4247 -0.0243 0.0015  0.0235  237 ALA   A C     
3418  O  O     . ALA   A 212 ? 0.1492 0.2243 0.4213 -0.0243 0.0158  0.0106  237 ALA   A O     
3419  C  CB    . ALA   A 212 ? 0.2072 0.2370 0.4603 -0.0308 0.0564  0.0252  237 ALA   A CB    
3425  N  N     . LEU   A 213 ? 0.1515 0.2181 0.4034 -0.0223 0.0059  0.0226  238 LEU   A N     
3426  C  CA    . LEU   A 213 ? 0.1072 0.2184 0.3889 -0.0144 -0.0037 0.0260  238 LEU   A CA    
3427  C  C     . LEU   A 213 ? 0.1259 0.2127 0.3903 -0.0201 -0.0238 0.0143  238 LEU   A C     
3428  O  O     . LEU   A 213 ? 0.1268 0.1987 0.3751 -0.0040 -0.0025 0.0087  238 LEU   A O     
3429  C  CB    . LEU   A 213 ? 0.1173 0.2211 0.3713 -0.0137 0.0085  0.0061  238 LEU   A CB    
3430  C  CG    . LEU   A 213 ? 0.1506 0.2160 0.3672 0.0108  0.0113  0.0191  238 LEU   A CG    
3431  C  CD1   . LEU   A 213 ? 0.1513 0.2520 0.3683 0.0268  0.0191  0.0241  238 LEU   A CD1   
3432  C  CD2   . LEU   A 213 ? 0.1271 0.2466 0.3719 0.0001  -0.0228 0.0396  238 LEU   A CD2   
3444  N  N     . MET   A 214 ? 0.1310 0.2025 0.4068 -0.0088 -0.0498 0.0095  239 MET   A N     
3445  C  CA    . MET   A 214 ? 0.1598 0.2186 0.4439 0.0083  -0.0592 0.0014  239 MET   A CA    
3446  C  C     . MET   A 214 ? 0.1475 0.2218 0.4529 -0.0122 -0.0426 0.0138  239 MET   A C     
3447  O  O     . MET   A 214 ? 0.1561 0.2238 0.4604 -0.0177 -0.0515 0.0140  239 MET   A O     
3448  C  CB    . MET   A 214 ? 0.1892 0.2214 0.4780 -0.0071 -0.0586 -0.0037 239 MET   A CB    
3449  C  CG    . MET   A 214 ? 0.2262 0.2151 0.4955 -0.0210 -0.0651 -0.0251 239 MET   A CG    
3450  S  SD    . MET   A 214 ? 0.2774 0.3066 0.5266 0.0034  -0.0952 -0.0544 239 MET   A SD    
3451  C  CE    . MET   A 214 ? 0.3469 0.2855 0.5269 -0.0446 -0.0877 -0.0420 239 MET   A CE    
3461  N  N     . VAL   A 215 ? 0.1532 0.2407 0.4651 -0.0154 0.0016  0.0052  240 VAL   A N     
3462  C  CA    . VAL   A 215 ? 0.1412 0.2584 0.4738 -0.0144 0.0084  0.0169  240 VAL   A CA    
3463  C  C     . VAL   A 215 ? 0.1158 0.2401 0.4493 -0.0180 0.0036  0.0049  240 VAL   A C     
3464  O  O     . VAL   A 215 ? 0.1417 0.2127 0.4651 -0.0008 0.0107  0.0133  240 VAL   A O     
3465  C  CB    . VAL   A 215 ? 0.1354 0.3128 0.5008 -0.0309 0.0354  -0.0028 240 VAL   A CB    
3466  C  CG1   . VAL   A 215 ? 0.1602 0.3314 0.5190 -0.0323 0.0619  0.0034  240 VAL   A CG1   
3467  C  CG2   . VAL   A 215 ? 0.1245 0.3443 0.4930 -0.0080 -0.0038 0.0050  240 VAL   A CG2   
3477  N  N     . ARG   A 216 ? 0.1045 0.2550 0.3999 -0.0216 0.0098  0.0087  241 ARG   A N     
3478  C  CA    . ARG   A 216 ? 0.1302 0.2464 0.3728 -0.0138 -0.0049 0.0226  241 ARG   A CA    
3479  C  C     . ARG   A 216 ? 0.1226 0.2321 0.3546 -0.0058 -0.0070 0.0197  241 ARG   A C     
3480  O  O     . ARG   A 216 ? 0.1375 0.2256 0.3449 -0.0185 0.0133  0.0063  241 ARG   A O     
3481  C  CB    . ARG   A 216 ? 0.1373 0.2535 0.3494 -0.0291 0.0153  0.0292  241 ARG   A CB    
3482  C  CG    . ARG   A 216 ? 0.1383 0.2777 0.3233 0.0035  0.0216  0.0221  241 ARG   A CG    
3483  C  CD    . ARG   A 216 ? 0.1343 0.2446 0.3013 0.0091  0.0328  0.0309  241 ARG   A CD    
3484  N  NE    . ARG   A 216 ? 0.1342 0.2260 0.2849 -0.0009 0.0340  0.0114  241 ARG   A NE    
3485  C  CZ    . ARG   A 216 ? 0.1568 0.2105 0.2708 -0.0015 0.0586  0.0103  241 ARG   A CZ    
3486  N  NH1   . ARG   A 216 ? 0.2468 0.2174 0.2756 0.0265  0.0554  0.0419  241 ARG   A NH1   
3487  N  NH2   . ARG   A 216 ? 0.2031 0.2121 0.2666 0.0123  0.0425  0.0232  241 ARG   A NH2   
3501  N  N     . ARG   A 217 ? 0.1464 0.2123 0.3591 -0.0182 0.0017  0.0072  242 ARG   A N     
3502  C  CA    . ARG   A 217 ? 0.1554 0.2275 0.3600 -0.0057 -0.0097 0.0020  242 ARG   A CA    
3503  C  C     . ARG   A 217 ? 0.1468 0.2207 0.3770 -0.0041 -0.0204 0.0050  242 ARG   A C     
3504  O  O     . ARG   A 217 ? 0.1424 0.2135 0.3737 0.0111  0.0226  0.0165  242 ARG   A O     
3505  C  CB    . ARG   A 217 ? 0.1666 0.2337 0.3518 -0.0201 -0.0225 0.0128  242 ARG   A CB    
3506  C  CG    . ARG   A 217 ? 0.1608 0.2216 0.3450 0.0053  -0.0220 0.0245  242 ARG   A CG    
3507  C  CD    . ARG   A 217 ? 0.1605 0.1750 0.3142 -0.0018 -0.0235 0.0337  242 ARG   A CD    
3508  N  NE    . ARG   A 217 ? 0.1871 0.1498 0.2920 -0.0015 -0.0082 0.0279  242 ARG   A NE    
3509  C  CZ    . ARG   A 217 ? 0.1656 0.1677 0.2776 0.0070  0.0032  0.0138  242 ARG   A CZ    
3510  N  NH1   . ARG   A 217 ? 0.1592 0.2008 0.2788 -0.0137 0.0015  0.0166  242 ARG   A NH1   
3511  N  NH2   . ARG   A 217 ? 0.1833 0.1821 0.2661 -0.0255 0.0046  0.0156  242 ARG   A NH2   
3525  N  N     . ALA   A 218 ? 0.1412 0.2211 0.3830 0.0055  -0.0481 0.0036  243 ALA   A N     
3526  C  CA    . ALA   A 218 ? 0.1490 0.2426 0.3911 -0.0106 -0.0366 -0.0070 243 ALA   A CA    
3527  C  C     . ALA   A 218 ? 0.1290 0.2450 0.4049 0.0051  -0.0278 -0.0027 243 ALA   A C     
3528  O  O     . ALA   A 218 ? 0.1244 0.2398 0.4123 0.0061  -0.0173 -0.0163 243 ALA   A O     
3529  C  CB    . ALA   A 218 ? 0.1367 0.2489 0.3901 -0.0025 -0.0489 -0.0221 243 ALA   A CB    
3535  N  N     . TYR   A 219 ? 0.1276 0.2186 0.4038 0.0014  0.0265  0.0171  244 TYR   A N     
3536  C  CA    . TYR   A 219 ? 0.1287 0.2238 0.4040 0.0147  0.0411  0.0166  244 TYR   A CA    
3537  C  C     . TYR   A 219 ? 0.1182 0.2318 0.3817 0.0241  0.0212  0.0055  244 TYR   A C     
3538  O  O     . TYR   A 219 ? 0.1373 0.2282 0.3970 0.0281  0.0477  -0.0061 244 TYR   A O     
3539  C  CB    . TYR   A 219 ? 0.1589 0.2325 0.4248 0.0103  0.0698  0.0159  244 TYR   A CB    
3540  C  CG    . TYR   A 219 ? 0.1476 0.2666 0.4725 -0.0052 0.0735  0.0204  244 TYR   A CG    
3541  C  CD1   . TYR   A 219 ? 0.1603 0.3232 0.4987 -0.0352 0.0849  0.0311  244 TYR   A CD1   
3542  C  CD2   . TYR   A 219 ? 0.1508 0.3161 0.5045 0.0056  0.0727  0.0041  244 TYR   A CD2   
3543  C  CE1   . TYR   A 219 ? 0.1573 0.3654 0.5206 -0.0480 0.0663  0.0228  244 TYR   A CE1   
3544  C  CE2   . TYR   A 219 ? 0.1887 0.3514 0.5335 0.0050  0.0922  0.0016  244 TYR   A CE2   
3545  C  CZ    . TYR   A 219 ? 0.1647 0.4029 0.5494 -0.0321 0.0825  0.0217  244 TYR   A CZ    
3546  O  OH    . TYR   A 219 ? 0.1740 0.4703 0.5860 -0.0017 0.0903  0.0405  244 TYR   A OH    
3556  N  N     . ASP   A 220 ? 0.1124 0.2349 0.3507 0.0244  0.0158  0.0139  245 ASP   A N     
3557  C  CA    . ASP   A 220 ? 0.1047 0.2204 0.3203 0.0104  0.0114  0.0225  245 ASP   A CA    
3558  C  C     . ASP   A 220 ? 0.1039 0.2149 0.3187 0.0166  -0.0165 0.0165  245 ASP   A C     
3559  O  O     . ASP   A 220 ? 0.1409 0.2063 0.3089 0.0147  -0.0047 0.0199  245 ASP   A O     
3560  C  CB    . ASP   A 220 ? 0.1075 0.2149 0.3023 0.0321  0.0120  0.0291  245 ASP   A CB    
3561  C  CG    . ASP   A 220 ? 0.1104 0.2290 0.2837 -0.0010 0.0284  0.0287  245 ASP   A CG    
3562  O  OD1   . ASP   A 220 ? 0.1421 0.2382 0.2813 0.0025  0.0551  0.0333  245 ASP   A OD1   
3563  O  OD2   . ASP   A 220 ? 0.1294 0.2204 0.2828 -0.0093 0.0049  0.0280  245 ASP   A OD2   
3568  N  N     . ILE   A 221 ? 0.1131 0.1906 0.3235 0.0054  -0.0426 0.0199  246 ILE   A N     
3569  C  CA    . ILE   A 221 ? 0.1211 0.2009 0.3658 0.0240  -0.0352 0.0282  246 ILE   A CA    
3570  C  C     . ILE   A 221 ? 0.1335 0.2358 0.4085 0.0200  -0.0408 0.0175  246 ILE   A C     
3571  O  O     . ILE   A 221 ? 0.1637 0.2338 0.4205 0.0419  -0.0223 0.0166  246 ILE   A O     
3572  C  CB    . ILE   A 221 ? 0.1649 0.2423 0.3697 0.0358  -0.0449 0.0033  246 ILE   A CB    
3573  C  CG1   . ILE   A 221 ? 0.1759 0.2469 0.3579 -0.0149 -0.0345 -0.0131 246 ILE   A CG1   
3574  C  CG2   . ILE   A 221 ? 0.1835 0.2726 0.3719 0.0222  -0.0440 -0.0184 246 ILE   A CG2   
3575  C  CD1   . ILE   A 221 ? 0.2020 0.2553 0.3592 0.0105  -0.0190 0.0026  246 ILE   A CD1   
3587  N  N     . ALA   A 222 ? 0.1168 0.2436 0.4245 0.0215  -0.0271 0.0143  247 ALA   A N     
3588  C  CA    . ALA   A 222 ? 0.1350 0.2510 0.4413 0.0112  -0.0368 -0.0029 247 ALA   A CA    
3589  C  C     . ALA   A 222 ? 0.1588 0.2288 0.4333 0.0255  -0.0258 0.0007  247 ALA   A C     
3590  O  O     . ALA   A 222 ? 0.2231 0.2426 0.4460 0.0623  -0.0217 0.0079  247 ALA   A O     
3591  C  CB    . ALA   A 222 ? 0.1164 0.2570 0.4503 0.0149  -0.0160 -0.0220 247 ALA   A CB    
3597  N  N     . GLY   A 223 ? 0.1297 0.2122 0.4211 0.0156  -0.0138 -0.0142 248 GLY   A N     
3598  C  CA    . GLY   A 223 ? 0.1812 0.2366 0.3983 -0.0155 -0.0087 -0.0060 248 GLY   A CA    
3599  C  C     . GLY   A 223 ? 0.1690 0.2272 0.3747 -0.0099 -0.0048 -0.0041 248 GLY   A C     
3600  O  O     . GLY   A 223 ? 0.2384 0.2426 0.3819 -0.0030 0.0061  -0.0038 248 GLY   A O     
3604  N  N     . SER   A 224 ? 0.1601 0.2048 0.3306 -0.0036 -0.0014 -0.0020 249 SER   A N     
3605  C  CA    . SER   A 224 ? 0.1507 0.2159 0.3237 0.0132  -0.0005 0.0113  249 SER   A CA    
3606  C  C     . SER   A 224 ? 0.1886 0.2110 0.3234 0.0004  -0.0088 0.0214  249 SER   A C     
3607  O  O     . SER   A 224 ? 0.2274 0.2164 0.3172 0.0158  -0.0239 0.0231  249 SER   A O     
3608  C  CB    . SER   A 224 ? 0.1611 0.2155 0.3251 0.0159  -0.0073 0.0129  249 SER   A CB    
3609  O  OG    . SER   A 224 ? 0.1745 0.2341 0.3253 0.0079  0.0076  0.0035  249 SER   A OG    
3615  N  N     . THR   A 225 ? 0.2154 0.2332 0.3506 0.0094  -0.0155 0.0348  250 THR   A N     
3616  C  CA    . THR   A 225 ? 0.2330 0.2574 0.3891 -0.0158 -0.0065 0.0246  250 THR   A CA    
3617  C  C     . THR   A 225 ? 0.2769 0.2501 0.4072 0.0174  0.0187  0.0224  250 THR   A C     
3618  O  O     . THR   A 225 ? 0.3490 0.2725 0.4180 0.0707  0.0561  0.0220  250 THR   A O     
3619  C  CB    . THR   A 225 ? 0.2730 0.2899 0.4144 0.0093  -0.0158 0.0019  250 THR   A CB    
3620  O  OG1   . THR   A 225 ? 0.2499 0.2689 0.4301 0.0638  -0.0331 0.0047  250 THR   A OG1   
3621  C  CG2   . THR   A 225 ? 0.2554 0.3031 0.4166 0.0167  -0.0353 -0.0137 250 THR   A CG2   
3629  N  N     . LYS   A 226 ? 0.2798 0.2150 0.4106 0.0126  -0.0074 0.0005  251 LYS   A N     
3630  C  CA    . LYS   A 226 ? 0.3021 0.2240 0.4492 0.0453  -0.0407 -0.0064 251 LYS   A CA    
3631  C  C     . LYS   A 226 ? 0.2873 0.2321 0.4385 0.0674  -0.0546 -0.0269 251 LYS   A C     
3632  O  O     . LYS   A 226 ? 0.3085 0.2595 0.4337 0.0640  -0.0495 -0.0295 251 LYS   A O     
3633  C  CB    . LYS   A 226 ? 0.3751 0.2333 0.5079 0.0536  -0.0391 -0.0109 251 LYS   A CB    
3634  C  CG    . LYS   A 226 ? 0.4449 0.2795 0.5647 0.0416  -0.0461 -0.0200 251 LYS   A CG    
3635  C  CD    . LYS   A 226 ? 0.5057 0.3504 0.6000 0.0924  -0.0446 -0.0206 251 LYS   A CD    
3636  C  CE    . LYS   A 226 ? 0.4859 0.4081 0.6176 0.1265  -0.0603 -0.0259 251 LYS   A CE    
3637  N  NZ    . LYS   A 226 ? 0.5230 0.4756 0.6370 0.1283  -0.0453 -0.0214 251 LYS   A NZ    
3651  N  N     . ASP   A 227 ? 0.2750 0.2496 0.4440 0.0689  -0.0799 -0.0277 252 ASP   A N     
3652  C  CA    . ASP   A 227 ? 0.3394 0.2615 0.4791 0.0556  -0.0783 -0.0502 252 ASP   A CA    
3653  C  C     . ASP   A 227 ? 0.3336 0.2697 0.4975 0.0703  -0.1163 -0.0527 252 ASP   A C     
3654  O  O     . ASP   A 227 ? 0.3438 0.2910 0.5146 0.0690  -0.1406 -0.0545 252 ASP   A O     
3655  C  CB    . ASP   A 227 ? 0.3722 0.2772 0.5014 0.0535  -0.0443 -0.0751 252 ASP   A CB    
3656  C  CG    . ASP   A 227 ? 0.4346 0.3465 0.5366 0.0446  -0.0012 -0.0880 252 ASP   A CG    
3657  O  OD1   . ASP   A 227 ? 0.4569 0.3967 0.5413 0.0759  0.0239  -0.1039 252 ASP   A OD1   
3658  O  OD2   . ASP   A 227 ? 0.4532 0.3403 0.5607 0.0010  0.0106  -0.0924 252 ASP   A OD2   
3663  N  N     . VAL   A 228 ? 0.2806 0.2736 0.5057 0.0520  -0.1155 -0.0563 253 VAL   A N     
3664  C  CA    . VAL   A 228 ? 0.2514 0.2674 0.5179 0.0355  -0.1057 -0.0517 253 VAL   A CA    
3665  C  C     . VAL   A 228 ? 0.2126 0.2908 0.5337 0.0278  -0.0914 -0.0483 253 VAL   A C     
3666  O  O     . VAL   A 228 ? 0.2133 0.3070 0.5248 0.0198  -0.0889 -0.0153 253 VAL   A O     
3667  C  CB    . VAL   A 228 ? 0.2755 0.2327 0.5102 0.0248  -0.0765 -0.0616 253 VAL   A CB    
3668  C  CG1   . VAL   A 228 ? 0.3113 0.2338 0.5001 0.0136  -0.0672 -0.0549 253 VAL   A CG1   
3669  C  CG2   . VAL   A 228 ? 0.2992 0.2457 0.5170 0.0216  -0.0695 -0.0566 253 VAL   A CG2   
3679  N  N     . LYS   A 229 ? 0.2303 0.2861 0.5613 0.0565  -0.0790 -0.0704 254 LYS   A N     
3680  C  CA    . LYS   A 229 ? 0.2229 0.2985 0.5851 0.0735  -0.0695 -0.0763 254 LYS   A CA    
3681  C  C     . LYS   A 229 ? 0.2201 0.2868 0.5675 0.0572  -0.0717 -0.0636 254 LYS   A C     
3682  O  O     . LYS   A 229 ? 0.2826 0.2716 0.5579 0.0628  -0.0748 -0.0669 254 LYS   A O     
3683  C  CB    . LYS   A 229 ? 0.2597 0.3371 0.6285 0.0901  -0.0386 -0.0948 254 LYS   A CB    
3684  C  CG    . LYS   A 229 ? 0.3180 0.3822 0.6670 0.0852  -0.0154 -0.1012 254 LYS   A CG    
3685  C  CD    . LYS   A 229 ? 0.3908 0.4679 0.7031 0.0741  0.0239  -0.0974 254 LYS   A CD    
3686  C  CE    . LYS   A 229 ? 0.4537 0.5468 0.7346 0.0744  0.0295  -0.0836 254 LYS   A CE    
3687  N  NZ    . LYS   A 229 ? 0.4903 0.5837 0.7523 0.1118  0.0364  -0.0743 254 LYS   A NZ    
3701  N  N     . VAL   A 230 ? 0.1827 0.2934 0.5610 0.0557  -0.0879 -0.0428 255 VAL   A N     
3702  C  CA    . VAL   A 230 ? 0.1663 0.2684 0.5815 0.0309  -0.0554 -0.0353 255 VAL   A CA    
3703  C  C     . VAL   A 230 ? 0.1827 0.2835 0.6086 0.0201  -0.0286 -0.0395 255 VAL   A C     
3704  O  O     . VAL   A 230 ? 0.1702 0.2986 0.6116 0.0017  -0.0240 -0.0321 255 VAL   A O     
3705  C  CB    . VAL   A 230 ? 0.1758 0.2676 0.5725 0.0245  -0.0338 -0.0217 255 VAL   A CB    
3706  C  CG1   . VAL   A 230 ? 0.1865 0.2849 0.5747 0.0242  -0.0140 -0.0100 255 VAL   A CG1   
3707  C  CG2   . VAL   A 230 ? 0.1508 0.2813 0.5690 0.0167  -0.0386 -0.0152 255 VAL   A CG2   
3717  N  N     . PHE   A 231 ? 0.1787 0.2840 0.6290 0.0151  -0.0232 -0.0507 256 PHE   A N     
3718  C  CA    . PHE   A 231 ? 0.1655 0.3137 0.6339 0.0237  -0.0114 -0.0560 256 PHE   A CA    
3719  C  C     . PHE   A 231 ? 0.1710 0.3274 0.6335 0.0342  -0.0006 -0.0728 256 PHE   A C     
3720  O  O     . PHE   A 231 ? 0.1707 0.3652 0.6322 0.0240  0.0346  -0.0708 256 PHE   A O     
3721  C  CB    . PHE   A 231 ? 0.1900 0.3482 0.6725 0.0336  -0.0342 -0.0566 256 PHE   A CB    
3722  C  CG    . PHE   A 231 ? 0.1944 0.3665 0.6886 0.0520  -0.0280 -0.0649 256 PHE   A CG    
3723  C  CD1   . PHE   A 231 ? 0.1918 0.3850 0.6965 0.0354  -0.0472 -0.0692 256 PHE   A CD1   
3724  C  CD2   . PHE   A 231 ? 0.2014 0.3756 0.6789 0.0728  -0.0224 -0.0685 256 PHE   A CD2   
3725  C  CE1   . PHE   A 231 ? 0.1876 0.3797 0.6982 0.0351  -0.0372 -0.0720 256 PHE   A CE1   
3726  C  CE2   . PHE   A 231 ? 0.1962 0.3813 0.6948 0.0599  -0.0204 -0.0666 256 PHE   A CE2   
3727  C  CZ    . PHE   A 231 ? 0.2114 0.3836 0.7008 0.0608  -0.0245 -0.0755 256 PHE   A CZ    
3737  N  N     . LEU   A 232 ? 0.1756 0.2937 0.6238 0.0366  0.0051  -0.0929 257 LEU   A N     
3738  C  CA    . LEU   A 232 ? 0.1806 0.3073 0.6836 0.0151  0.0249  -0.0822 257 LEU   A CA    
3739  C  C     . LEU   A 232 ? 0.1848 0.3319 0.7070 0.0101  0.0325  -0.0714 257 LEU   A C     
3740  O  O     . LEU   A 232 ? 0.1825 0.3521 0.7080 0.0116  0.0253  -0.0537 257 LEU   A O     
3741  C  CB    . LEU   A 232 ? 0.1975 0.3186 0.7097 -0.0055 0.0458  -0.0803 257 LEU   A CB    
3742  C  CG    . LEU   A 232 ? 0.2346 0.3403 0.7266 0.0295  0.0509  -0.0685 257 LEU   A CG    
3743  C  CD1   . LEU   A 232 ? 0.2350 0.3628 0.7333 0.0363  0.0342  -0.0512 257 LEU   A CD1   
3744  C  CD2   . LEU   A 232 ? 0.3036 0.3473 0.7337 0.0745  0.0560  -0.0699 257 LEU   A CD2   
3756  N  N     . ASN   A 233 ? 0.1858 0.3175 0.7032 -0.0255 0.0188  -0.0810 258 ASN   A N     
3757  C  CA    . ASN   A 233 ? 0.1864 0.3269 0.7180 -0.0138 0.0250  -0.0774 258 ASN   A CA    
3758  C  C     . ASN   A 233 ? 0.1954 0.3580 0.7653 -0.0013 0.0049  -0.0730 258 ASN   A C     
3759  O  O     . ASN   A 233 ? 0.1952 0.3673 0.7562 -0.0097 0.0270  -0.0746 258 ASN   A O     
3760  C  CB    . ASN   A 233 ? 0.1966 0.3275 0.7391 -0.0244 0.0491  -0.0683 258 ASN   A CB    
3761  C  CG    . ASN   A 233 ? 0.2425 0.3229 0.7843 -0.0022 0.0786  -0.0535 258 ASN   A CG    
3762  O  OD1   . ASN   A 233 ? 0.2550 0.3399 0.8107 0.0351  0.0714  -0.0542 258 ASN   A OD1   
3763  N  ND2   . ASN   A 233 ? 0.3200 0.3302 0.7930 0.0581  0.0859  -0.0432 258 ASN   A ND2   
3770  N  N     . GLY   A 234 ? 0.1871 0.3494 0.7306 0.0054  0.0021  -0.0735 259 GLY   A N     
3771  C  CA    . GLY   A 234 ? 0.1939 0.3594 0.7382 0.0217  0.0205  -0.0778 259 GLY   A CA    
3772  C  C     . GLY   A 234 ? 0.1987 0.3748 0.7464 0.0256  0.0149  -0.0970 259 GLY   A C     
3773  O  O     . GLY   A 234 ? 0.2172 0.3952 0.7408 0.0587  0.0260  -0.1058 259 GLY   A O     
3777  N  N     . ASN   A 235 ? 0.1897 0.3497 0.7247 0.0039  0.0088  -0.1082 260 ASN   A N     
3778  C  CA    . ASN   A 235 ? 0.1904 0.3538 0.7296 -0.0061 -0.0025 -0.1046 260 ASN   A CA    
3779  C  C     . ASN   A 235 ? 0.1918 0.3283 0.7306 0.0066  0.0150  -0.1098 260 ASN   A C     
3780  O  O     . ASN   A 235 ? 0.1904 0.3481 0.7093 0.0253  0.0160  -0.0981 260 ASN   A O     
3781  C  CB    . ASN   A 235 ? 0.1902 0.3678 0.7391 -0.0006 -0.0003 -0.0846 260 ASN   A CB    
3782  C  CG    . ASN   A 235 ? 0.2041 0.3770 0.7918 0.0159  0.0104  -0.0755 260 ASN   A CG    
3783  O  OD1   . ASN   A 235 ? 0.2084 0.3921 0.8091 0.0227  -0.0070 -0.0645 260 ASN   A OD1   
3784  N  ND2   . ASN   A 235 ? 0.2144 0.3808 0.8048 -0.0063 0.0327  -0.0900 260 ASN   A ND2   
3791  N  N     . LYS   A 236 ? 0.1883 0.2947 0.7143 0.0119  0.0142  -0.1033 261 LYS   A N     
3792  C  CA    . LYS   A 236 ? 0.1909 0.3072 0.7247 0.0096  0.0220  -0.1015 261 LYS   A CA    
3793  C  C     . LYS   A 236 ? 0.1825 0.3619 0.6924 -0.0120 0.0375  -0.0826 261 LYS   A C     
3794  O  O     . LYS   A 236 ? 0.1807 0.4217 0.6876 -0.0126 0.0360  -0.0714 261 LYS   A O     
3795  C  CB    . LYS   A 236 ? 0.2090 0.3022 0.7597 0.0188  -0.0004 -0.0997 261 LYS   A CB    
3796  C  CG    . LYS   A 236 ? 0.2559 0.3438 0.7874 0.0362  -0.0143 -0.0993 261 LYS   A CG    
3797  C  CD    . LYS   A 236 ? 0.3736 0.3836 0.8098 0.0411  -0.0263 -0.0968 261 LYS   A CD    
3798  C  CE    . LYS   A 236 ? 0.4872 0.4471 0.8305 0.0291  -0.0362 -0.0947 261 LYS   A CE    
3799  N  NZ    . LYS   A 236 ? 0.5686 0.5011 0.8453 0.0195  -0.0361 -0.0850 261 LYS   A NZ    
3813  N  N     . LEU   A 237 ? 0.1772 0.3529 0.6546 -0.0373 0.0338  -0.0652 262 LEU   A N     
3814  C  CA    . LEU   A 237 ? 0.1682 0.3719 0.6378 -0.0189 0.0394  -0.0539 262 LEU   A CA    
3815  C  C     . LEU   A 237 ? 0.1702 0.3908 0.6468 -0.0113 0.0371  -0.0643 262 LEU   A C     
3816  O  O     . LEU   A 237 ? 0.2400 0.3895 0.6541 0.0198  0.0444  -0.0755 262 LEU   A O     
3817  C  CB    . LEU   A 237 ? 0.1657 0.3729 0.6378 -0.0200 0.0334  -0.0310 262 LEU   A CB    
3818  C  CG    . LEU   A 237 ? 0.1665 0.3494 0.6315 -0.0289 0.0359  -0.0142 262 LEU   A CG    
3819  C  CD1   . LEU   A 237 ? 0.1574 0.3531 0.6138 -0.0066 0.0321  -0.0101 262 LEU   A CD1   
3820  C  CD2   . LEU   A 237 ? 0.1803 0.3607 0.6540 -0.0238 0.0198  -0.0148 262 LEU   A CD2   
3832  N  N     . PRO   A 238 ? 0.1969 0.4326 0.6410 -0.0496 0.0250  -0.0746 263 PRO   A N     
3833  C  CA    . PRO   A 238 ? 0.2194 0.4894 0.6330 -0.0708 0.0400  -0.0753 263 PRO   A CA    
3834  C  C     . PRO   A 238 ? 0.2421 0.5255 0.6239 -0.0684 0.0591  -0.0643 263 PRO   A C     
3835  O  O     . PRO   A 238 ? 0.3145 0.5880 0.6336 -0.0789 0.0576  -0.0619 263 PRO   A O     
3836  C  CB    . PRO   A 238 ? 0.2440 0.4921 0.6313 -0.0616 0.0646  -0.0772 263 PRO   A CB    
3837  C  CG    . PRO   A 238 ? 0.2870 0.4870 0.6365 -0.0576 0.0534  -0.0784 263 PRO   A CG    
3838  C  CD    . PRO   A 238 ? 0.2764 0.4534 0.6416 -0.0645 0.0399  -0.0719 263 PRO   A CD    
3846  N  N     . VAL   A 239 ? 0.2244 0.4706 0.6119 -0.0391 0.0927  -0.0397 264 VAL   A N     
3847  C  CA    . VAL   A 239 ? 0.2163 0.4474 0.6105 0.0064  0.0583  -0.0149 264 VAL   A CA    
3848  C  C     . VAL   A 239 ? 0.2245 0.4662 0.6300 0.0051  0.0257  0.0001  264 VAL   A C     
3849  O  O     . VAL   A 239 ? 0.2694 0.4915 0.6333 -0.0006 0.0125  -0.0061 264 VAL   A O     
3850  C  CB    . VAL   A 239 ? 0.2028 0.4143 0.5871 0.0208  0.0828  0.0007  264 VAL   A CB    
3851  C  CG1   . VAL   A 239 ? 0.1714 0.3854 0.5780 0.0316  0.0761  -0.0170 264 VAL   A CG1   
3852  C  CG2   . VAL   A 239 ? 0.2505 0.4159 0.5809 0.0616  0.0667  0.0263  264 VAL   A CG2   
3862  N  N     . LYS   A 240 ? 0.1786 0.4689 0.6443 -0.0063 0.0148  0.0128  265 LYS   A N     
3863  C  CA    . LYS   A 240 ? 0.3388 0.5139 0.6558 -0.0144 0.0242  0.0256  265 LYS   A CA    
3864  C  C     . LYS   A 240 ? 0.3914 0.5138 0.6322 -0.0310 0.0217  0.0586  265 LYS   A C     
3865  O  O     . LYS   A 240 ? 0.4662 0.5563 0.6624 -0.0552 0.0592  0.0748  265 LYS   A O     
3866  C  CB    . LYS   A 240 ? 0.4568 0.5752 0.6884 0.0074  0.0187  0.0093  265 LYS   A CB    
3867  C  CG    . LYS   A 240 ? 0.5625 0.6253 0.7139 0.0013  0.0104  -0.0031 265 LYS   A CG    
3868  C  CD    . LYS   A 240 ? 0.6369 0.6702 0.7392 0.0149  0.0066  -0.0242 265 LYS   A CD    
3869  C  CE    . LYS   A 240 ? 0.6795 0.7005 0.7569 0.0380  0.0084  -0.0428 265 LYS   A CE    
3870  N  NZ    . LYS   A 240 ? 0.7111 0.7107 0.7649 0.0512  0.0131  -0.0587 265 LYS   A NZ    
3884  N  N     . GLY   A 241 ? 0.3779 0.4614 0.5737 -0.0021 -0.0030 0.0748  266 GLY   A N     
3885  C  CA    . GLY   A 241 ? 0.2450 0.3968 0.5132 0.0118  0.0303  0.0612  266 GLY   A CA    
3886  C  C     . GLY   A 241 ? 0.2311 0.3161 0.4586 0.0127  0.0540  0.0234  266 GLY   A C     
3887  O  O     . GLY   A 241 ? 0.2608 0.3387 0.4572 0.0140  0.0401  0.0281  266 GLY   A O     
3891  N  N     . PHE   A 242 ? 0.2104 0.2729 0.4123 0.0318  0.0504  -0.0016 267 PHE   A N     
3892  C  CA    . PHE   A 242 ? 0.1902 0.2632 0.3811 0.0311  0.0523  -0.0004 267 PHE   A CA    
3893  C  C     . PHE   A 242 ? 0.2234 0.2868 0.3895 0.0480  0.0702  -0.0043 267 PHE   A C     
3894  O  O     . PHE   A 242 ? 0.1872 0.2741 0.3934 0.0457  0.0732  0.0156  267 PHE   A O     
3895  C  CB    . PHE   A 242 ? 0.1821 0.2429 0.3611 0.0147  0.0449  -0.0050 267 PHE   A CB    
3896  C  CG    . PHE   A 242 ? 0.1764 0.2519 0.3400 0.0166  0.0422  0.0076  267 PHE   A CG    
3897  C  CD1   . PHE   A 242 ? 0.1769 0.2813 0.3335 0.0037  0.0438  0.0137  267 PHE   A CD1   
3898  C  CD2   . PHE   A 242 ? 0.1761 0.2481 0.3253 0.0108  0.0328  0.0175  267 PHE   A CD2   
3899  C  CE1   . PHE   A 242 ? 0.1620 0.2669 0.3154 0.0147  0.0739  0.0158  267 PHE   A CE1   
3900  C  CE2   . PHE   A 242 ? 0.2107 0.2629 0.3058 0.0206  0.0619  0.0194  267 PHE   A CE2   
3901  C  CZ    . PHE   A 242 ? 0.1947 0.2430 0.3099 0.0113  0.0697  0.0411  267 PHE   A CZ    
3911  N  N     . ARG   A 243 ? 0.2586 0.3056 0.4029 0.0626  0.0737  -0.0230 268 ARG   A N     
3912  C  CA    A ARG   A 243 ? 0.2826 0.3170 0.4085 0.0741  0.0862  -0.0361 268 ARG   A CA    
3913  C  CA    B ARG   A 243 ? 0.2742 0.3129 0.4017 0.0827  0.0710  -0.0358 268 ARG   A CA    
3914  C  C     . ARG   A 243 ? 0.2474 0.3260 0.4055 0.0811  0.0984  -0.0163 268 ARG   A C     
3915  O  O     . ARG   A 243 ? 0.2412 0.3437 0.4060 0.0637  0.1149  0.0086  268 ARG   A O     
3916  C  CB    A ARG   A 243 ? 0.3292 0.3365 0.4191 0.0837  0.1032  -0.0560 268 ARG   A CB    
3917  C  CB    B ARG   A 243 ? 0.3002 0.3326 0.4005 0.1131  0.0625  -0.0502 268 ARG   A CB    
3918  C  CG    A ARG   A 243 ? 0.3783 0.3657 0.4380 0.0687  0.1168  -0.0650 268 ARG   A CG    
3919  C  CG    B ARG   A 243 ? 0.3565 0.3715 0.4130 0.0935  0.0547  -0.0513 268 ARG   A CG    
3920  C  CD    A ARG   A 243 ? 0.3948 0.3991 0.4490 0.0539  0.1421  -0.0746 268 ARG   A CD    
3921  C  CD    B ARG   A 243 ? 0.3970 0.4190 0.4179 0.0761  0.0590  -0.0490 268 ARG   A CD    
3922  N  NE    A ARG   A 243 ? 0.4167 0.4223 0.4562 0.0368  0.1630  -0.0834 268 ARG   A NE    
3923  N  NE    B ARG   A 243 ? 0.4751 0.4434 0.4262 0.0410  0.0484  -0.0512 268 ARG   A NE    
3924  C  CZ    A ARG   A 243 ? 0.4642 0.4354 0.4622 0.0510  0.1668  -0.0933 268 ARG   A CZ    
3925  C  CZ    B ARG   A 243 ? 0.5035 0.4476 0.4261 0.0272  0.0309  -0.0526 268 ARG   A CZ    
3926  N  NH1   A ARG   A 243 ? 0.4744 0.4350 0.4623 0.0743  0.1622  -0.0998 268 ARG   A NH1   
3927  N  NH1   B ARG   A 243 ? 0.5003 0.4424 0.4246 0.0091  0.0197  -0.0644 268 ARG   A NH1   
3928  N  NH2   A ARG   A 243 ? 0.4916 0.4467 0.4682 0.0518  0.1722  -0.0952 268 ARG   A NH2   
3929  N  NH2   B ARG   A 243 ? 0.5201 0.4550 0.4297 0.0297  0.0370  -0.0421 268 ARG   A NH2   
3956  N  N     . SER   A 244 ? 0.2321 0.3230 0.4110 0.0657  0.0928  -0.0070 269 SER   A N     
3957  C  CA    . SER   A 244 ? 0.2473 0.3438 0.4256 0.0541  0.1000  -0.0076 269 SER   A CA    
3958  C  C     . SER   A 244 ? 0.2428 0.3334 0.4228 0.0265  0.1113  0.0086  269 SER   A C     
3959  O  O     . SER   A 244 ? 0.2397 0.3455 0.4489 0.0296  0.1455  0.0055  269 SER   A O     
3960  C  CB    . SER   A 244 ? 0.2809 0.3667 0.4478 0.0638  0.1032  -0.0147 269 SER   A CB    
3961  O  OG    . SER   A 244 ? 0.2771 0.3884 0.4708 0.0387  0.0773  -0.0204 269 SER   A OG    
3967  N  N     . TYR   A 245 ? 0.2191 0.2936 0.3902 0.0147  0.0930  0.0136  270 TYR   A N     
3968  C  CA    . TYR   A 245 ? 0.2035 0.2704 0.3592 0.0265  0.0813  0.0116  270 TYR   A CA    
3969  C  C     . TYR   A 245 ? 0.2215 0.2581 0.3406 0.0184  0.0963  0.0163  270 TYR   A C     
3970  O  O     . TYR   A 245 ? 0.2199 0.2555 0.3427 0.0002  0.0993  0.0119  270 TYR   A O     
3971  C  CB    . TYR   A 245 ? 0.1873 0.2760 0.3527 0.0438  0.0863  -0.0040 270 TYR   A CB    
3972  C  CG    . TYR   A 245 ? 0.2272 0.2613 0.3463 0.0280  0.0538  0.0003  270 TYR   A CG    
3973  C  CD1   . TYR   A 245 ? 0.2621 0.2843 0.3419 0.0319  0.0280  0.0173  270 TYR   A CD1   
3974  C  CD2   . TYR   A 245 ? 0.2525 0.2714 0.3506 0.0072  0.0793  -0.0113 270 TYR   A CD2   
3975  C  CE1   . TYR   A 245 ? 0.1961 0.2554 0.3295 0.0193  0.0423  -0.0092 270 TYR   A CE1   
3976  C  CE2   . TYR   A 245 ? 0.2460 0.2547 0.3468 -0.0096 0.0649  -0.0109 270 TYR   A CE2   
3977  C  CZ    . TYR   A 245 ? 0.2229 0.2713 0.3311 0.0138  0.0589  -0.0250 270 TYR   A CZ    
3978  O  OH    . TYR   A 245 ? 0.1991 0.2762 0.3316 -0.0075 0.0677  -0.0162 270 TYR   A OH    
3988  N  N     . VAL   A 246 ? 0.2080 0.2456 0.3343 0.0187  0.0727  0.0171  271 VAL   A N     
3989  C  CA    . VAL   A 246 ? 0.2021 0.2874 0.3441 0.0272  0.0724  0.0191  271 VAL   A CA    
3990  C  C     . VAL   A 246 ? 0.2435 0.3313 0.3468 0.0349  0.0884  0.0207  271 VAL   A C     
3991  O  O     . VAL   A 246 ? 0.2521 0.3280 0.3554 0.0386  0.0762  0.0380  271 VAL   A O     
3992  C  CB    . VAL   A 246 ? 0.2227 0.2692 0.3503 0.0256  0.0902  0.0270  271 VAL   A CB    
3993  C  CG1   . VAL   A 246 ? 0.2910 0.3054 0.3528 0.0359  0.0712  0.0195  271 VAL   A CG1   
3994  C  CG2   . VAL   A 246 ? 0.1866 0.2771 0.3528 0.0267  0.1136  0.0246  271 VAL   A CG2   
4004  N  N     . ASP   A 247 ? 0.2683 0.3782 0.3557 0.0549  0.1274  0.0052  272 ASP   A N     
4005  C  CA    A ASP   A 247 ? 0.3074 0.4066 0.3722 0.0623  0.1346  0.0148  272 ASP   A CA    
4006  C  CA    B ASP   A 247 ? 0.2843 0.4045 0.3690 0.0535  0.1346  0.0137  272 ASP   A CA    
4007  C  C     . ASP   A 247 ? 0.2971 0.4036 0.3682 0.0454  0.1334  0.0223  272 ASP   A C     
4008  O  O     . ASP   A 247 ? 0.3316 0.4327 0.3627 0.0285  0.1598  0.0254  272 ASP   A O     
4009  C  CB    A ASP   A 247 ? 0.3723 0.4431 0.3984 0.0810  0.1507  0.0064  272 ASP   A CB    
4010  C  CB    B ASP   A 247 ? 0.3039 0.4367 0.3893 0.0544  0.1534  0.0021  272 ASP   A CB    
4011  C  CG    A ASP   A 247 ? 0.4745 0.5032 0.4301 0.0750  0.1469  -0.0009 272 ASP   A CG    
4012  C  CG    B ASP   A 247 ? 0.3646 0.4941 0.4169 0.0335  0.1458  -0.0084 272 ASP   A CG    
4013  O  OD1   A ASP   A 247 ? 0.5268 0.5305 0.4421 0.0636  0.1272  0.0017  272 ASP   A OD1   
4014  O  OD1   B ASP   A 247 ? 0.3890 0.5123 0.4166 0.0238  0.1348  -0.0148 272 ASP   A OD1   
4015  O  OD2   A ASP   A 247 ? 0.5297 0.5234 0.4396 0.0686  0.1763  -0.0172 272 ASP   A OD2   
4016  O  OD2   B ASP   A 247 ? 0.4053 0.5163 0.4336 0.0271  0.1608  -0.0096 272 ASP   A OD2   
4023  N  N     . MET   A 248 ? 0.2571 0.3746 0.3614 0.0175  0.1170  0.0407  273 MET   A N     
4024  C  CA    . MET   A 248 ? 0.2522 0.3780 0.3941 0.0041  0.1047  0.0657  273 MET   A CA    
4025  C  C     . MET   A 248 ? 0.2824 0.3539 0.3763 0.0065  0.1186  0.0685  273 MET   A C     
4026  O  O     . MET   A 248 ? 0.3168 0.3733 0.3989 0.0086  0.1139  0.0746  273 MET   A O     
4027  C  CB    . MET   A 248 ? 0.2340 0.4121 0.4465 -0.0036 0.1001  0.0767  273 MET   A CB    
4028  C  CG    . MET   A 248 ? 0.2798 0.4815 0.4942 -0.0050 0.0790  0.0813  273 MET   A CG    
4029  S  SD    . MET   A 248 ? 0.3241 0.5451 0.5365 -0.0345 0.0574  0.0902  273 MET   A SD    
4030  C  CE    . MET   A 248 ? 0.4112 0.5695 0.5547 -0.0399 0.0539  0.0966  273 MET   A CE    
4040  N  N     . TYR   A 249 ? 0.2395 0.3203 0.3381 -0.0045 0.1265  0.0572  274 TYR   A N     
4041  C  CA    . TYR   A 249 ? 0.2387 0.2934 0.3223 -0.0089 0.0996  0.0433  274 TYR   A CA    
4042  C  C     . TYR   A 249 ? 0.3087 0.3320 0.3241 -0.0168 0.0975  0.0524  274 TYR   A C     
4043  O  O     . TYR   A 249 ? 0.3808 0.3566 0.3488 -0.0245 0.0635  0.0704  274 TYR   A O     
4044  C  CB    . TYR   A 249 ? 0.2072 0.2668 0.3095 -0.0140 0.0962  0.0387  274 TYR   A CB    
4045  C  CG    . TYR   A 249 ? 0.2192 0.2537 0.3031 -0.0151 0.0666  0.0137  274 TYR   A CG    
4046  C  CD1   . TYR   A 249 ? 0.2407 0.2665 0.2935 0.0108  0.0546  0.0005  274 TYR   A CD1   
4047  C  CD2   . TYR   A 249 ? 0.2476 0.2652 0.3027 0.0213  0.0868  0.0079  274 TYR   A CD2   
4048  C  CE1   . TYR   A 249 ? 0.2531 0.2725 0.2837 0.0053  0.0735  0.0045  274 TYR   A CE1   
4049  C  CE2   . TYR   A 249 ? 0.2587 0.2783 0.3003 0.0348  0.0858  0.0060  274 TYR   A CE2   
4050  C  CZ    . TYR   A 249 ? 0.2717 0.2681 0.2924 0.0260  0.0906  0.0111  274 TYR   A CZ    
4051  O  OH    . TYR   A 249 ? 0.3372 0.2688 0.3104 0.0247  0.0894  0.0072  274 TYR   A OH    
4061  N  N     . LEU   A 250 ? 0.3098 0.3723 0.3061 -0.0043 0.1138  0.0273  275 LEU   A N     
4062  C  CA    . LEU   A 250 ? 0.3207 0.4518 0.2817 0.0251  0.1281  0.0190  275 LEU   A CA    
4063  C  C     . LEU   A 250 ? 0.3428 0.5802 0.2897 0.0550  0.1445  0.0311  275 LEU   A C     
4064  O  O     . LEU   A 250 ? 0.3638 0.5994 0.2772 0.0715  0.1436  0.0443  275 LEU   A O     
4065  C  CB    . LEU   A 250 ? 0.3025 0.4276 0.2643 0.0196  0.1090  -0.0098 275 LEU   A CB    
4066  C  CG    . LEU   A 250 ? 0.3269 0.3986 0.2701 0.0030  0.0880  0.0133  275 LEU   A CG    
4067  C  CD1   . LEU   A 250 ? 0.3724 0.4079 0.2572 -0.0107 0.0342  0.0100  275 LEU   A CD1   
4068  C  CD2   . LEU   A 250 ? 0.3564 0.3819 0.2813 0.0092  0.0878  0.0115  275 LEU   A CD2   
4080  N  N     . LYS   A 251 ? 0.3840 0.6799 0.3330 0.0513  0.1633  0.0375  276 LYS   A N     
4081  C  CA    . LYS   A 251 ? 0.4388 0.7776 0.3937 -0.0063 0.1642  0.0612  276 LYS   A CA    
4082  C  C     . LYS   A 251 ? 0.4753 0.8133 0.4168 -0.0504 0.1583  0.0746  276 LYS   A C     
4083  O  O     . LYS   A 251 ? 0.4972 0.8233 0.4202 -0.0714 0.1421  0.0742  276 LYS   A O     
4084  C  CB    . LYS   A 251 ? 0.4243 0.8333 0.4354 -0.0378 0.1780  0.0650  276 LYS   A CB    
4085  C  CG    . LYS   A 251 ? 0.4700 0.8719 0.4824 -0.0669 0.1506  0.0671  276 LYS   A CG    
4086  C  CD    . LYS   A 251 ? 0.5382 0.8933 0.5201 -0.0842 0.1344  0.0643  276 LYS   A CD    
4087  C  CE    . LYS   A 251 ? 0.6015 0.9058 0.5462 -0.0862 0.1293  0.0578  276 LYS   A CE    
4088  N  NZ    . LYS   A 251 ? 0.6466 0.9226 0.5628 -0.0831 0.1334  0.0537  276 LYS   A NZ    
4102  N  N     . ASP   A 252 ? 0.5094 0.8406 0.4390 -0.0629 0.1617  0.0988  277 ASP   A N     
4103  C  CA    . ASP   A 252 ? 0.5676 0.8571 0.4609 -0.0848 0.1664  0.1084  277 ASP   A CA    
4104  C  C     . ASP   A 252 ? 0.5830 0.8188 0.4363 -0.0957 0.1737  0.1420  277 ASP   A C     
4105  O  O     . ASP   A 252 ? 0.6480 0.8293 0.4414 -0.0988 0.1573  0.1745  277 ASP   A O     
4106  C  CB    . ASP   A 252 ? 0.6299 0.9058 0.5002 -0.0745 0.1547  0.0779  277 ASP   A CB    
4107  C  CG    . ASP   A 252 ? 0.6741 0.9502 0.5296 -0.0691 0.1547  0.0471  277 ASP   A CG    
4108  O  OD1   . ASP   A 252 ? 0.6685 0.9644 0.5279 -0.0595 0.1885  0.0187  277 ASP   A OD1   
4109  O  OD2   . ASP   A 252 ? 0.6989 0.9656 0.5470 -0.0804 0.1289  0.0541  277 ASP   A OD2   
4114  N  N     . LYS   A 253 ? 0.5400 0.7765 0.4097 -0.0898 0.1769  0.1279  278 LYS   A N     
4115  C  CA    . LYS   A 253 ? 0.5565 0.7488 0.3955 -0.0675 0.1576  0.1121  278 LYS   A CA    
4116  C  C     . LYS   A 253 ? 0.5570 0.7164 0.3856 -0.0339 0.1492  0.1051  278 LYS   A C     
4117  O  O     . LYS   A 253 ? 0.5150 0.7017 0.3807 -0.0124 0.1257  0.0932  278 LYS   A O     
4118  C  CB    . LYS   A 253 ? 0.6063 0.7710 0.4065 -0.0306 0.1287  0.0957  278 LYS   A CB    
4119  C  CG    . LYS   A 253 ? 0.6502 0.8016 0.4287 -0.0031 0.1054  0.0767  278 LYS   A CG    
4120  C  CD    . LYS   A 253 ? 0.6735 0.8166 0.4527 0.0096  0.0788  0.0623  278 LYS   A CD    
4121  C  CE    . LYS   A 253 ? 0.6866 0.8125 0.4727 0.0193  0.0620  0.0615  278 LYS   A CE    
4122  N  NZ    . LYS   A 253 ? 0.6862 0.8048 0.4833 0.0195  0.0517  0.0717  278 LYS   A NZ    
4136  N  N     . LEU   A 254 ? 0.5703 0.6972 0.3740 -0.0235 0.1800  0.1142  279 LEU   A N     
4137  C  CA    . LEU   A 254 ? 0.5608 0.6967 0.3720 0.0017  0.2114  0.1115  279 LEU   A CA    
4138  C  C     . LEU   A 254 ? 0.5854 0.7137 0.3847 0.0397  0.2415  0.0837  279 LEU   A C     
4139  O  O     . LEU   A 254 ? 0.6111 0.7171 0.4065 0.0393  0.2378  0.0652  279 LEU   A O     
4140  C  CB    . LEU   A 254 ? 0.5463 0.6890 0.3673 -0.0033 0.2028  0.1312  279 LEU   A CB    
4141  C  CG    . LEU   A 254 ? 0.5470 0.6906 0.3692 0.0005  0.1874  0.1400  279 LEU   A CG    
4142  C  CD1   . LEU   A 254 ? 0.5370 0.6975 0.3640 0.0150  0.1859  0.1466  279 LEU   A CD1   
4143  C  CD2   . LEU   A 254 ? 0.5654 0.6998 0.3666 -0.0031 0.1924  0.1287  279 LEU   A CD2   
4155  N  N     . ASP   A 255 ? 0.5857 0.7259 0.3890 0.0851  0.2538  0.0737  280 ASP   A N     
4156  C  CA    . ASP   A 255 ? 0.6264 0.7574 0.4107 0.1243  0.2456  0.0829  280 ASP   A CA    
4157  C  C     . ASP   A 255 ? 0.6680 0.7814 0.4477 0.1733  0.2541  0.0877  280 ASP   A C     
4158  O  O     . ASP   A 255 ? 0.6416 0.7762 0.4501 0.1928  0.2674  0.0912  280 ASP   A O     
4159  C  CB    . ASP   A 255 ? 0.6302 0.7793 0.4042 0.1043  0.2163  0.0773  280 ASP   A CB    
4160  C  CG    . ASP   A 255 ? 0.6425 0.7910 0.4040 0.0645  0.1943  0.0841  280 ASP   A CG    
4161  O  OD1   . ASP   A 255 ? 0.6508 0.7949 0.3953 0.0565  0.2146  0.0814  280 ASP   A OD1   
4162  O  OD2   . ASP   A 255 ? 0.6443 0.7906 0.4076 0.0293  0.1665  0.0942  280 ASP   A OD2   
4167  N  N     . GLU   A 256 ? 0.7363 0.8053 0.4807 0.1919  0.2363  0.0958  281 GLU   A N     
4168  C  CA    . GLU   A 256 ? 0.7925 0.8344 0.5039 0.1725  0.2380  0.1040  281 GLU   A CA    
4169  C  C     . GLU   A 256 ? 0.8237 0.8291 0.5027 0.1529  0.2267  0.1214  281 GLU   A C     
4170  O  O     . GLU   A 256 ? 0.8425 0.8231 0.5179 0.1414  0.2090  0.1245  281 GLU   A O     
4171  C  CB    . GLU   A 256 ? 0.8389 0.8692 0.5347 0.1666  0.2256  0.0902  281 GLU   A CB    
4172  C  CG    . GLU   A 256 ? 0.8726 0.9006 0.5671 0.1599  0.2111  0.0695  281 GLU   A CG    
4173  C  CD    . GLU   A 256 ? 0.9065 0.9287 0.5928 0.1493  0.1958  0.0502  281 GLU   A CD    
4174  O  OE1   . GLU   A 256 ? 0.9301 0.9420 0.6128 0.1588  0.1801  0.0408  281 GLU   A OE1   
4175  O  OE2   . GLU   A 256 ? 0.9081 0.9328 0.5953 0.1421  0.2011  0.0452  281 GLU   A OE2   
4182  N  N     . THR   A 257 ? 0.8213 0.8272 0.4902 0.1393  0.2296  0.1294  282 THR   A N     
4183  C  CA    . THR   A 257 ? 0.7988 0.8261 0.4923 0.1091  0.2315  0.1202  282 THR   A CA    
4184  C  C     . THR   A 257 ? 0.7448 0.8193 0.4618 0.0987  0.2631  0.1088  282 THR   A C     
4185  O  O     . THR   A 257 ? 0.7634 0.8344 0.4537 0.1069  0.2751  0.0876  282 THR   A O     
4186  C  CB    . THR   A 257 ? 0.8469 0.8314 0.5297 0.0946  0.1884  0.1170  282 THR   A CB    
4187  O  OG1   . THR   A 257 ? 0.8797 0.8330 0.5471 0.0793  0.1682  0.1223  282 THR   A OG1   
4188  C  CG2   . THR   A 257 ? 0.8390 0.8332 0.5430 0.0903  0.1822  0.1121  282 THR   A CG2   
4196  N  N     . GLY   A 258 ? 0.6743 0.7925 0.4450 0.0739  0.2742  0.1151  283 GLY   A N     
4197  C  CA    . GLY   A 258 ? 0.6050 0.7688 0.4347 0.0365  0.2744  0.1136  283 GLY   A CA    
4198  C  C     . GLY   A 258 ? 0.5851 0.7615 0.4280 0.0185  0.2610  0.1118  283 GLY   A C     
4199  O  O     . GLY   A 258 ? 0.5873 0.7743 0.4346 -0.0216 0.2648  0.1239  283 GLY   A O     
4203  N  N     . ASN   A 259 ? 0.5924 0.7297 0.4188 0.0028  0.2221  0.1078  284 ASN   A N     
4204  C  CA    . ASN   A 259 ? 0.6222 0.7082 0.4183 0.0015  0.1865  0.1007  284 ASN   A CA    
4205  C  C     . ASN   A 259 ? 0.5712 0.6568 0.4089 0.0080  0.1858  0.1028  284 ASN   A C     
4206  O  O     . ASN   A 259 ? 0.5440 0.6381 0.4191 0.0721  0.1823  0.0980  284 ASN   A O     
4207  C  CB    . ASN   A 259 ? 0.6854 0.7348 0.4394 -0.0152 0.1586  0.0913  284 ASN   A CB    
4208  C  CG    . ASN   A 259 ? 0.7626 0.7631 0.4850 -0.0038 0.1221  0.0715  284 ASN   A CG    
4209  O  OD1   . ASN   A 259 ? 0.7918 0.7903 0.5280 -0.0093 0.0926  0.0787  284 ASN   A OD1   
4210  N  ND2   . ASN   A 259 ? 0.8018 0.7611 0.4712 0.0095  0.1161  0.0402  284 ASN   A ND2   
4217  N  N     . SER   A 260 ? 0.5388 0.6285 0.4019 -0.0317 0.1920  0.0996  285 SER   A N     
4218  C  CA    . SER   A 260 ? 0.5173 0.6207 0.3977 -0.0432 0.2141  0.0870  285 SER   A CA    
4219  C  C     . SER   A 260 ? 0.5236 0.5961 0.3797 -0.0469 0.2034  0.0603  285 SER   A C     
4220  O  O     . SER   A 260 ? 0.5577 0.6006 0.3570 -0.0424 0.1925  0.0255  285 SER   A O     
4221  C  CB    . SER   A 260 ? 0.5498 0.6459 0.4221 -0.0447 0.2042  0.0877  285 SER   A CB    
4222  O  OG    . SER   A 260 ? 0.5941 0.6711 0.4396 -0.0374 0.1937  0.0801  285 SER   A OG    
4228  N  N     . LEU   A 261 ? 0.5058 0.5623 0.3844 -0.0296 0.1929  0.0589  286 LEU   A N     
4229  C  CA    . LEU   A 261 ? 0.5208 0.5406 0.3970 -0.0098 0.1789  0.0585  286 LEU   A CA    
4230  C  C     . LEU   A 261 ? 0.5058 0.5265 0.4222 0.0182  0.1816  0.0520  286 LEU   A C     
4231  O  O     . LEU   A 261 ? 0.4814 0.5464 0.4650 0.0223  0.1544  0.0488  286 LEU   A O     
4232  C  CB    . LEU   A 261 ? 0.5380 0.5424 0.3812 -0.0066 0.1754  0.0585  286 LEU   A CB    
4233  C  CG    . LEU   A 261 ? 0.5418 0.5632 0.3682 -0.0091 0.1689  0.0456  286 LEU   A CG    
4234  C  CD1   . LEU   A 261 ? 0.5330 0.5663 0.3610 -0.0396 0.1640  0.0446  286 LEU   A CD1   
4235  C  CD2   . LEU   A 261 ? 0.5302 0.5687 0.3663 0.0081  0.1727  0.0456  286 LEU   A CD2   
4247  N  N     . LYS   A 262 ? 0.5296 0.4950 0.3936 0.0077  0.2225  0.0461  287 LYS   A N     
4248  C  CA    . LYS   A 262 ? 0.5860 0.4878 0.3777 0.0094  0.2318  0.0233  287 LYS   A CA    
4249  C  C     . LYS   A 262 ? 0.5548 0.4328 0.3574 0.0209  0.2363  0.0251  287 LYS   A C     
4250  O  O     . LYS   A 262 ? 0.5924 0.4272 0.3489 0.0601  0.2357  0.0312  287 LYS   A O     
4251  C  CB    . LYS   A 262 ? 0.6551 0.5429 0.4026 0.0050  0.2251  0.0005  287 LYS   A CB    
4252  C  CG    . LYS   A 262 ? 0.7082 0.6044 0.4359 -0.0041 0.1992  -0.0197 287 LYS   A CG    
4253  C  CD    . LYS   A 262 ? 0.7699 0.6603 0.4801 -0.0004 0.1612  -0.0360 287 LYS   A CD    
4254  C  CE    . LYS   A 262 ? 0.8127 0.7096 0.5089 0.0005  0.1349  -0.0455 287 LYS   A CE    
4255  N  NZ    . LYS   A 262 ? 0.8271 0.7452 0.5218 0.0027  0.1315  -0.0426 287 LYS   A NZ    
4269  N  N     . VAL   A 263 ? 0.4861 0.3913 0.3577 0.0284  0.2259  0.0044  288 VAL   A N     
4270  C  CA    . VAL   A 263 ? 0.4488 0.3693 0.3703 0.0320  0.2193  -0.0089 288 VAL   A CA    
4271  C  C     . VAL   A 263 ? 0.4444 0.3613 0.3678 0.0652  0.2076  -0.0230 288 VAL   A C     
4272  O  O     . VAL   A 263 ? 0.4629 0.3645 0.4001 0.0895  0.2099  -0.0454 288 VAL   A O     
4273  C  CB    . VAL   A 263 ? 0.4696 0.3843 0.3925 0.0308  0.1802  -0.0168 288 VAL   A CB    
4274  C  CG1   . VAL   A 263 ? 0.4312 0.3780 0.4011 0.0026  0.1602  -0.0157 288 VAL   A CG1   
4275  C  CG2   . VAL   A 263 ? 0.5117 0.4204 0.4093 0.0410  0.1701  -0.0306 288 VAL   A CG2   
4285  N  N     . ILE   A 264 ? 0.4251 0.3389 0.3220 0.0663  0.2020  -0.0201 289 ILE   A N     
4286  C  CA    . ILE   A 264 ? 0.4878 0.3550 0.3138 0.0485  0.1580  -0.0039 289 ILE   A CA    
4287  C  C     . ILE   A 264 ? 0.4682 0.3392 0.3025 0.0764  0.1441  -0.0231 289 ILE   A C     
4288  O  O     . ILE   A 264 ? 0.4441 0.3299 0.2877 0.0987  0.1220  -0.0208 289 ILE   A O     
4289  C  CB    . ILE   A 264 ? 0.5602 0.3990 0.3307 -0.0223 0.1404  0.0086  289 ILE   A CB    
4290  C  CG1   . ILE   A 264 ? 0.6059 0.4583 0.3565 -0.0312 0.1395  -0.0078 289 ILE   A CG1   
4291  C  CG2   . ILE   A 264 ? 0.5963 0.4019 0.3416 -0.0324 0.1402  0.0070  289 ILE   A CG2   
4292  C  CD1   . ILE   A 264 ? 0.6405 0.4953 0.3836 -0.0215 0.1183  -0.0269 289 ILE   A CD1   
4304  N  N     . HIS   A 265 ? 0.4719 0.3333 0.3236 0.0955  0.1535  -0.0339 290 HIS   A N     
4305  C  CA    . HIS   A 265 ? 0.4425 0.3341 0.3599 0.0976  0.1681  -0.0293 290 HIS   A CA    
4306  C  C     . HIS   A 265 ? 0.4373 0.3209 0.3531 0.0882  0.1991  -0.0298 290 HIS   A C     
4307  O  O     . HIS   A 265 ? 0.5036 0.3121 0.3713 0.0945  0.1986  -0.0497 290 HIS   A O     
4308  C  CB    . HIS   A 265 ? 0.4273 0.3639 0.3939 0.1112  0.1666  -0.0211 290 HIS   A CB    
4309  C  CG    . HIS   A 265 ? 0.4385 0.3803 0.4158 0.1345  0.1577  -0.0083 290 HIS   A CG    
4310  N  ND1   . HIS   A 265 ? 0.4924 0.4456 0.4295 0.1622  0.1471  -0.0166 290 HIS   A ND1   
4311  C  CD2   . HIS   A 265 ? 0.4381 0.3573 0.4185 0.1592  0.1504  -0.0156 290 HIS   A CD2   
4312  C  CE1   . HIS   A 265 ? 0.4925 0.4389 0.4238 0.1558  0.1317  -0.0206 290 HIS   A CE1   
4313  N  NE2   . HIS   A 265 ? 0.4425 0.3927 0.4263 0.1446  0.1414  -0.0076 290 HIS   A NE2   
4321  N  N     . GLU   A 266 ? 0.3913 0.3027 0.3447 0.0499  0.1962  -0.0053 291 GLU   A N     
4322  C  CA    . GLU   A 266 ? 0.4237 0.2928 0.3444 0.0506  0.1854  -0.0134 291 GLU   A CA    
4323  C  C     . GLU   A 266 ? 0.3865 0.2748 0.3422 0.0688  0.1470  -0.0274 291 GLU   A C     
4324  O  O     . GLU   A 266 ? 0.3602 0.2480 0.3344 0.0537  0.1456  -0.0250 291 GLU   A O     
4325  C  CB    . GLU   A 266 ? 0.4791 0.2898 0.3632 0.0481  0.1725  -0.0300 291 GLU   A CB    
4326  C  CG    . GLU   A 266 ? 0.5150 0.3067 0.3783 0.0215  0.1559  -0.0194 291 GLU   A CG    
4327  C  CD    . GLU   A 266 ? 0.5721 0.3281 0.3892 0.0124  0.1091  -0.0340 291 GLU   A CD    
4328  O  OE1   . GLU   A 266 ? 0.5969 0.3573 0.3991 -0.0014 0.0594  -0.0386 291 GLU   A OE1   
4329  O  OE2   . GLU   A 266 ? 0.5985 0.3658 0.3965 0.0009  0.1284  -0.0516 291 GLU   A OE2   
4336  N  N     . GLN   A 267 ? 0.3778 0.2710 0.3628 0.0680  0.1206  -0.0223 292 GLN   A N     
4337  C  CA    . GLN   A 267 ? 0.3506 0.2561 0.3953 0.0605  0.1069  -0.0127 292 GLN   A CA    
4338  C  C     . GLN   A 267 ? 0.3892 0.2354 0.4037 0.0527  0.1183  -0.0218 292 GLN   A C     
4339  O  O     . GLN   A 267 ? 0.3799 0.2507 0.4245 0.0884  0.1110  -0.0158 292 GLN   A O     
4340  C  CB    . GLN   A 267 ? 0.3362 0.2752 0.4271 0.0827  0.0728  -0.0239 292 GLN   A CB    
4341  C  CG    . GLN   A 267 ? 0.3729 0.3397 0.4678 0.1001  0.0324  -0.0295 292 GLN   A CG    
4342  C  CD    . GLN   A 267 ? 0.4331 0.4120 0.5084 0.1338  0.0029  -0.0394 292 GLN   A CD    
4343  O  OE1   . GLN   A 267 ? 0.4494 0.4427 0.5322 0.1217  -0.0271 -0.0149 292 GLN   A OE1   
4344  N  NE2   . GLN   A 267 ? 0.4570 0.4570 0.5234 0.1481  0.0127  -0.0610 292 GLN   A NE2   
4353  N  N     . VAL   A 268 ? 0.3901 0.2154 0.3890 0.0431  0.1568  -0.0372 293 VAL   A N     
4354  C  CA    . VAL   A 268 ? 0.4017 0.2461 0.3977 0.0158  0.1903  -0.0668 293 VAL   A CA    
4355  C  C     . VAL   A 268 ? 0.4395 0.2086 0.4126 0.0238  0.1785  -0.0684 293 VAL   A C     
4356  O  O     . VAL   A 268 ? 0.4743 0.2295 0.4267 -0.0240 0.1786  -0.1149 293 VAL   A O     
4357  C  CB    . VAL   A 268 ? 0.3992 0.2976 0.4057 -0.0279 0.1814  -0.0754 293 VAL   A CB    
4358  C  CG1   . VAL   A 268 ? 0.4094 0.3429 0.4072 -0.0742 0.1795  -0.1012 293 VAL   A CG1   
4359  C  CG2   . VAL   A 268 ? 0.4143 0.3067 0.4023 -0.0129 0.1807  -0.0812 293 VAL   A CG2   
4369  N  N     . ASN   A 269 ? 0.3952 0.2066 0.4095 0.0473  0.1663  -0.0258 294 ASN   A N     
4370  C  CA    . ASN   A 269 ? 0.3699 0.2232 0.4113 0.0484  0.1624  -0.0063 294 ASN   A CA    
4371  C  C     . ASN   A 269 ? 0.3384 0.2334 0.4124 0.0806  0.1617  0.0430  294 ASN   A C     
4372  O  O     . ASN   A 269 ? 0.3405 0.2453 0.4102 0.0803  0.1348  0.0771  294 ASN   A O     
4373  C  CB    . ASN   A 269 ? 0.3518 0.2030 0.4032 0.0221  0.1383  -0.0328 294 ASN   A CB    
4374  C  CG    . ASN   A 269 ? 0.3068 0.2037 0.3992 0.0248  0.0963  -0.0357 294 ASN   A CG    
4375  O  OD1   . ASN   A 269 ? 0.2815 0.2090 0.3891 0.0412  0.0727  -0.0238 294 ASN   A OD1   
4376  N  ND2   . ASN   A 269 ? 0.3300 0.2183 0.3939 -0.0055 0.1004  -0.0494 294 ASN   A ND2   
4383  N  N     . HIS   A 270 ? 0.3304 0.2170 0.4185 0.0906  0.1585  0.0610  295 HIS   A N     
4384  C  CA    . HIS   A 270 ? 0.3292 0.2069 0.4209 0.0811  0.1139  0.0808  295 HIS   A CA    
4385  C  C     . HIS   A 270 ? 0.2847 0.2027 0.3934 0.0588  0.0929  0.0680  295 HIS   A C     
4386  O  O     . HIS   A 270 ? 0.2723 0.2503 0.4251 0.0683  0.0631  0.0993  295 HIS   A O     
4387  C  CB    . HIS   A 270 ? 0.3626 0.2376 0.4455 0.0976  0.0920  0.0966  295 HIS   A CB    
4388  C  CG    . HIS   A 270 ? 0.3775 0.2678 0.4484 0.1009  0.0797  0.1097  295 HIS   A CG    
4389  N  ND1   . HIS   A 270 ? 0.3929 0.2994 0.4422 0.0971  0.0963  0.1287  295 HIS   A ND1   
4390  C  CD2   . HIS   A 270 ? 0.3777 0.2545 0.4520 0.0891  0.0728  0.0836  295 HIS   A CD2   
4391  C  CE1   . HIS   A 270 ? 0.3901 0.2906 0.4537 0.0591  0.0855  0.1444  295 HIS   A CE1   
4392  N  NE2   . HIS   A 270 ? 0.4208 0.2836 0.4535 0.1146  0.0822  0.1080  295 HIS   A NE2   
4400  N  N     . ARG   A 271 ? 0.2440 0.1655 0.3493 0.0474  0.0700  0.0530  296 ARG   A N     
4401  C  CA    . ARG   A 271 ? 0.2241 0.1726 0.3265 0.0397  0.0436  0.0358  296 ARG   A CA    
4402  C  C     . ARG   A 271 ? 0.2018 0.2020 0.3070 0.0348  0.0241  0.0263  296 ARG   A C     
4403  O  O     . ARG   A 271 ? 0.2195 0.1975 0.3122 0.0280  0.0488  0.0266  296 ARG   A O     
4404  C  CB    . ARG   A 271 ? 0.2030 0.1671 0.3230 0.0423  0.0443  0.0255  296 ARG   A CB    
4405  C  CG    . ARG   A 271 ? 0.2177 0.1777 0.3135 0.0450  0.0503  0.0350  296 ARG   A CG    
4406  C  CD    . ARG   A 271 ? 0.2240 0.1904 0.2916 0.0604  0.0395  0.0307  296 ARG   A CD    
4407  N  NE    . ARG   A 271 ? 0.2548 0.1916 0.3031 0.0483  0.0231  0.0416  296 ARG   A NE    
4408  C  CZ    . ARG   A 271 ? 0.2713 0.1939 0.3134 0.0290  0.0149  0.0286  296 ARG   A CZ    
4409  N  NH1   . ARG   A 271 ? 0.2800 0.1710 0.3171 0.0265  0.0051  0.0132  296 ARG   A NH1   
4410  N  NH2   . ARG   A 271 ? 0.2938 0.2084 0.3171 0.0249  0.0198  0.0273  296 ARG   A NH2   
4424  N  N     . TRP   A 272 ? 0.2224 0.2062 0.3108 0.0264  0.0409  -0.0036 297 TRP   A N     
4425  C  CA    . TRP   A 272 ? 0.2176 0.1787 0.3002 -0.0049 0.0631  -0.0082 297 TRP   A CA    
4426  C  C     . TRP   A 272 ? 0.1966 0.1802 0.3092 0.0046  0.0685  -0.0180 297 TRP   A C     
4427  O  O     . TRP   A 272 ? 0.2395 0.1972 0.3240 0.0322  0.0759  -0.0288 297 TRP   A O     
4428  C  CB    . TRP   A 272 ? 0.2217 0.1806 0.2995 0.0004  0.0653  -0.0173 297 TRP   A CB    
4429  C  CG    . TRP   A 272 ? 0.2242 0.1815 0.2844 0.0129  0.0616  -0.0115 297 TRP   A CG    
4430  C  CD1   . TRP   A 272 ? 0.2378 0.1815 0.2937 0.0137  0.0610  -0.0117 297 TRP   A CD1   
4431  C  CD2   . TRP   A 272 ? 0.1953 0.1598 0.2711 0.0167  0.0370  -0.0289 297 TRP   A CD2   
4432  N  NE1   . TRP   A 272 ? 0.2388 0.1950 0.2815 0.0149  0.0530  -0.0209 297 TRP   A NE1   
4433  C  CE2   . TRP   A 272 ? 0.1937 0.1713 0.2717 0.0048  0.0349  -0.0237 297 TRP   A CE2   
4434  C  CE3   . TRP   A 272 ? 0.2166 0.1792 0.2734 -0.0212 0.0388  -0.0335 297 TRP   A CE3   
4435  C  CZ2   . TRP   A 272 ? 0.2064 0.1639 0.2727 -0.0114 0.0371  -0.0389 297 TRP   A CZ2   
4436  C  CZ3   . TRP   A 272 ? 0.1850 0.1821 0.2786 -0.0229 0.0474  -0.0257 297 TRP   A CZ3   
4437  C  CH2   . TRP   A 272 ? 0.1509 0.1920 0.2906 -0.0262 0.0457  -0.0209 297 TRP   A CH2   
4448  N  N     . GLU   A 273 ? 0.1847 0.1977 0.3007 0.0055  0.0769  0.0073  298 GLU   A N     
4449  C  CA    . GLU   A 273 ? 0.2055 0.2155 0.3024 -0.0107 0.0898  0.0118  298 GLU   A CA    
4450  C  C     . GLU   A 273 ? 0.2142 0.2220 0.2745 0.0101  0.0823  -0.0078 298 GLU   A C     
4451  O  O     . GLU   A 273 ? 0.2641 0.2186 0.2607 0.0265  0.0479  -0.0174 298 GLU   A O     
4452  C  CB    . GLU   A 273 ? 0.2386 0.2608 0.3495 -0.0030 0.1203  -0.0067 298 GLU   A CB    
4453  C  CG    . GLU   A 273 ? 0.2023 0.3021 0.4117 0.0332  0.1210  -0.0145 298 GLU   A CG    
4454  C  CD    . GLU   A 273 ? 0.2483 0.3227 0.4503 0.0559  0.1386  -0.0223 298 GLU   A CD    
4455  O  OE1   . GLU   A 273 ? 0.2977 0.2734 0.4619 0.0212  0.1111  -0.0375 298 GLU   A OE1   
4456  O  OE2   . GLU   A 273 ? 0.3212 0.3632 0.4641 0.0745  0.1611  0.0058  298 GLU   A OE2   
4463  N  N     . VAL   A 274 ? 0.2525 0.2202 0.2630 0.0334  0.0652  -0.0214 299 VAL   A N     
4464  C  CA    . VAL   A 274 ? 0.2728 0.2275 0.2674 0.0138  0.0670  -0.0190 299 VAL   A CA    
4465  C  C     . VAL   A 274 ? 0.2867 0.2479 0.2566 0.0170  0.0725  -0.0312 299 VAL   A C     
4466  O  O     . VAL   A 274 ? 0.2994 0.2751 0.2711 0.0384  0.1021  -0.0262 299 VAL   A O     
4467  C  CB    . VAL   A 274 ? 0.2746 0.2390 0.2763 0.0073  0.0643  -0.0243 299 VAL   A CB    
4468  C  CG1   . VAL   A 274 ? 0.2680 0.2581 0.2807 -0.0199 0.0638  -0.0256 299 VAL   A CG1   
4469  C  CG2   . VAL   A 274 ? 0.2871 0.2461 0.2914 0.0090  0.0756  -0.0282 299 VAL   A CG2   
4479  N  N     . CYS   A 275 ? 0.2332 0.2427 0.2367 0.0156  0.0775  -0.0131 300 CYS   A N     
4480  C  CA    A CYS   A 275 ? 0.2652 0.2666 0.2528 0.0069  0.0722  -0.0035 300 CYS   A CA    
4481  C  CA    B CYS   A 275 ? 0.2467 0.2844 0.2401 0.0066  0.0721  -0.0137 300 CYS   A CA    
4482  C  C     . CYS   A 275 ? 0.2814 0.2902 0.2301 0.0181  0.0685  -0.0170 300 CYS   A C     
4483  O  O     . CYS   A 275 ? 0.3273 0.3033 0.2067 0.0279  0.0745  -0.0386 300 CYS   A O     
4484  C  CB    A CYS   A 275 ? 0.2554 0.2856 0.2987 0.0313  0.0747  0.0119  300 CYS   A CB    
4485  C  CB    B CYS   A 275 ? 0.2130 0.3263 0.2577 0.0045  0.0754  -0.0138 300 CYS   A CB    
4486  S  SG    A CYS   A 275 ? 0.2901 0.3039 0.3579 0.0356  0.0716  0.0254  300 CYS   A SG    
4487  S  SG    B CYS   A 275 ? 0.2004 0.3599 0.2805 0.0001  0.0789  -0.0090 300 CYS   A SG    
4498  N  N     . LEU   A 276 ? 0.2966 0.3062 0.2217 0.0533  0.0639  -0.0191 301 LEU   A N     
4499  C  CA    . LEU   A 276 ? 0.3345 0.3001 0.2305 0.0334  0.0835  -0.0325 301 LEU   A CA    
4500  C  C     . LEU   A 276 ? 0.3282 0.3011 0.2313 0.0397  0.0938  -0.0271 301 LEU   A C     
4501  O  O     . LEU   A 276 ? 0.3078 0.2919 0.2402 0.0336  0.0969  -0.0071 301 LEU   A O     
4502  C  CB    . LEU   A 276 ? 0.3625 0.3243 0.2600 0.0088  0.0871  -0.0394 301 LEU   A CB    
4503  C  CG    . LEU   A 276 ? 0.3958 0.3470 0.2992 -0.0282 0.0799  -0.0428 301 LEU   A CG    
4504  C  CD1   . LEU   A 276 ? 0.4227 0.3474 0.3226 -0.0175 0.0622  -0.0223 301 LEU   A CD1   
4505  C  CD2   . LEU   A 276 ? 0.4127 0.3957 0.3255 -0.0563 0.0634  -0.0392 301 LEU   A CD2   
4517  N  N     . THR   A 277 ? 0.3529 0.2948 0.2246 0.0308  0.0890  -0.0366 302 THR   A N     
4518  C  CA    . THR   A 277 ? 0.3464 0.3342 0.2263 0.0315  0.0810  -0.0290 302 THR   A CA    
4519  C  C     . THR   A 277 ? 0.3673 0.3372 0.2235 0.0210  0.0672  -0.0141 302 THR   A C     
4520  O  O     . THR   A 277 ? 0.3521 0.3476 0.2232 0.0207  0.0575  -0.0209 302 THR   A O     
4521  C  CB    . THR   A 277 ? 0.3677 0.3867 0.2430 0.0335  0.0959  -0.0185 302 THR   A CB    
4522  O  OG1   . THR   A 277 ? 0.3980 0.4136 0.2730 0.0493  0.1099  0.0050  302 THR   A OG1   
4523  C  CG2   . THR   A 277 ? 0.3684 0.4096 0.2622 0.0159  0.0731  -0.0253 302 THR   A CG2   
4531  N  N     . MET   A 278 ? 0.4186 0.3516 0.2306 0.0506  0.0755  0.0150  303 MET   A N     
4532  C  CA    . MET   A 278 ? 0.4537 0.4201 0.2498 0.0525  0.0769  -0.0029 303 MET   A CA    
4533  C  C     . MET   A 278 ? 0.4344 0.3951 0.2610 0.0579  0.0738  0.0198  303 MET   A C     
4534  O  O     . MET   A 278 ? 0.4419 0.3864 0.2796 0.0373  0.0919  0.0175  303 MET   A O     
4535  C  CB    . MET   A 278 ? 0.5603 0.5128 0.2800 0.0273  0.0831  -0.0496 303 MET   A CB    
4536  C  CG    . MET   A 278 ? 0.7222 0.6363 0.3494 0.0089  0.0601  -0.0785 303 MET   A CG    
4537  S  SD    . MET   A 278 ? 0.8689 0.7351 0.4186 0.0028  0.0217  -0.0886 303 MET   A SD    
4538  C  CE    . MET   A 278 ? 0.9006 0.7210 0.4201 0.0159  0.0039  -0.0977 303 MET   A CE    
4548  N  N     . SER   A 279 ? 0.4143 0.3831 0.2480 0.0616  0.0727  0.0353  304 SER   A N     
4549  C  CA    . SER   A 279 ? 0.4497 0.3776 0.2534 0.0762  0.0773  0.0337  304 SER   A CA    
4550  C  C     . SER   A 279 ? 0.5002 0.4091 0.2638 0.1152  0.0663  0.0429  304 SER   A C     
4551  O  O     . SER   A 279 ? 0.5236 0.4327 0.2729 0.1088  0.0540  0.0439  304 SER   A O     
4552  C  CB    . SER   A 279 ? 0.4418 0.3479 0.2514 0.0745  0.0673  0.0097  304 SER   A CB    
4553  O  OG    . SER   A 279 ? 0.4070 0.3375 0.2613 0.0437  0.0374  0.0184  304 SER   A OG    
4559  N  N     . GLU   A 280 ? 0.5649 0.4372 0.2886 0.1223  0.0775  0.0595  305 GLU   A N     
4560  C  CA    . GLU   A 280 ? 0.6140 0.4530 0.3252 0.1101  0.1207  0.0702  305 GLU   A CA    
4561  C  C     . GLU   A 280 ? 0.5906 0.4197 0.3306 0.0980  0.1051  0.0573  305 GLU   A C     
4562  O  O     . GLU   A 280 ? 0.6252 0.4344 0.3366 0.1224  0.1068  0.0701  305 GLU   A O     
4563  C  CB    . GLU   A 280 ? 0.6820 0.5116 0.3694 0.1110  0.1567  0.0742  305 GLU   A CB    
4564  C  CG    . GLU   A 280 ? 0.7152 0.5826 0.4205 0.0978  0.1962  0.0658  305 GLU   A CG    
4565  C  CD    . GLU   A 280 ? 0.7446 0.6453 0.4698 0.0859  0.2065  0.0465  305 GLU   A CD    
4566  O  OE1   . GLU   A 280 ? 0.7913 0.6801 0.5055 0.0758  0.1931  0.0485  305 GLU   A OE1   
4567  O  OE2   . GLU   A 280 ? 0.7271 0.6606 0.4802 0.1068  0.2096  0.0138  305 GLU   A OE2   
4574  N  N     . LYS   A 281 ? 0.5468 0.4021 0.3181 0.0544  0.0777  0.0370  306 LYS   A N     
4575  C  CA    . LYS   A 281 ? 0.5056 0.4216 0.3311 0.0359  0.0459  0.0073  306 LYS   A CA    
4576  C  C     . LYS   A 281 ? 0.4101 0.3773 0.2820 0.0505  0.0202  0.0074  306 LYS   A C     
4577  O  O     . LYS   A 281 ? 0.3807 0.3815 0.3080 0.0374  -0.0028 0.0003  306 LYS   A O     
4578  C  CB    . LYS   A 281 ? 0.5738 0.4958 0.3912 0.0018  0.0427  -0.0186 306 LYS   A CB    
4579  C  CG    . LYS   A 281 ? 0.6389 0.5658 0.4435 -0.0105 0.0093  -0.0378 306 LYS   A CG    
4580  C  CD    . LYS   A 281 ? 0.6915 0.6097 0.4867 -0.0393 -0.0063 -0.0340 306 LYS   A CD    
4581  C  CE    . LYS   A 281 ? 0.7312 0.6374 0.5125 -0.0585 -0.0198 -0.0303 306 LYS   A CE    
4582  N  NZ    . LYS   A 281 ? 0.7521 0.6630 0.5293 -0.0487 -0.0203 -0.0264 306 LYS   A NZ    
4596  N  N     . GLY   A 282 ? 0.3695 0.3506 0.2343 0.0454  0.0189  0.0032  307 GLY   A N     
4597  C  CA    . GLY   A 282 ? 0.3584 0.3514 0.2135 0.0350  0.0160  0.0050  307 GLY   A CA    
4598  C  C     . GLY   A 282 ? 0.3208 0.3450 0.2109 0.0234  -0.0127 0.0045  307 GLY   A C     
4599  O  O     . GLY   A 282 ? 0.3225 0.3176 0.2306 0.0422  0.0120  0.0071  307 GLY   A O     
4603  N  N     . PHE   A 283 ? 0.2772 0.3529 0.2040 0.0273  -0.0188 0.0134  308 PHE   A N     
4604  C  CA    . PHE   A 283 ? 0.2612 0.3297 0.1862 0.0269  -0.0152 0.0357  308 PHE   A CA    
4605  C  C     . PHE   A 283 ? 0.2158 0.3218 0.1982 0.0465  -0.0081 0.0108  308 PHE   A C     
4606  O  O     . PHE   A 283 ? 0.2936 0.3251 0.2341 0.0734  -0.0100 -0.0080 308 PHE   A O     
4607  C  CB    . PHE   A 283 ? 0.2570 0.3352 0.1943 0.0225  -0.0111 0.0027  308 PHE   A CB    
4608  C  CG    . PHE   A 283 ? 0.2263 0.3376 0.1929 0.0133  0.0027  0.0012  308 PHE   A CG    
4609  C  CD1   . PHE   A 283 ? 0.2262 0.3412 0.1898 0.0002  0.0034  0.0041  308 PHE   A CD1   
4610  C  CD2   . PHE   A 283 ? 0.2395 0.3459 0.2010 0.0083  0.0059  0.0098  308 PHE   A CD2   
4611  C  CE1   . PHE   A 283 ? 0.2312 0.3335 0.1880 -0.0090 -0.0205 0.0116  308 PHE   A CE1   
4612  C  CE2   . PHE   A 283 ? 0.2289 0.3536 0.2002 -0.0072 -0.0192 0.0082  308 PHE   A CE2   
4613  C  CZ    . PHE   A 283 ? 0.2276 0.3424 0.1963 -0.0171 -0.0368 0.0038  308 PHE   A CZ    
4623  N  N     . GLN   A 284 ? 0.2301 0.3135 0.1930 0.0391  0.0188  -0.0012 309 GLN   A N     
4624  C  CA    . GLN   A 284 ? 0.2530 0.2798 0.1961 0.0130  0.0128  0.0179  309 GLN   A CA    
4625  C  C     . GLN   A 284 ? 0.2285 0.2654 0.1831 0.0465  -0.0133 0.0208  309 GLN   A C     
4626  O  O     . GLN   A 284 ? 0.2315 0.2717 0.1786 0.0273  0.0020  0.0024  309 GLN   A O     
4627  C  CB    . GLN   A 284 ? 0.3039 0.2967 0.2213 -0.0144 0.0281  0.0449  309 GLN   A CB    
4628  C  CG    . GLN   A 284 ? 0.2991 0.3498 0.2399 -0.0145 0.0365  0.0365  309 GLN   A CG    
4629  C  CD    . GLN   A 284 ? 0.3223 0.3751 0.2613 -0.0027 0.0456  0.0365  309 GLN   A CD    
4630  O  OE1   . GLN   A 284 ? 0.3138 0.3750 0.3032 -0.0055 0.0514  0.0384  309 GLN   A OE1   
4631  N  NE2   . GLN   A 284 ? 0.3497 0.3776 0.2513 0.0438  0.0543  0.0217  309 GLN   A NE2   
4640  N  N     . GLN   A 285 ? 0.2023 0.2381 0.1871 0.0189  0.0162  0.0247  310 GLN   A N     
4641  C  CA    . GLN   A 285 ? 0.1596 0.2310 0.1863 0.0284  0.0255  0.0135  310 GLN   A CA    
4642  C  C     . GLN   A 285 ? 0.1893 0.2337 0.1935 0.0077  0.0235  0.0155  310 GLN   A C     
4643  O  O     . GLN   A 285 ? 0.1841 0.2266 0.2125 0.0157  0.0361  0.0101  310 GLN   A O     
4644  C  CB    . GLN   A 285 ? 0.1754 0.2528 0.1986 0.0012  0.0206  0.0021  310 GLN   A CB    
4645  C  CG    . GLN   A 285 ? 0.1721 0.2554 0.1935 -0.0020 0.0324  0.0085  310 GLN   A CG    
4646  C  CD    . GLN   A 285 ? 0.1871 0.2434 0.1896 0.0291  0.0284  0.0135  310 GLN   A CD    
4647  O  OE1   . GLN   A 285 ? 0.2158 0.2486 0.2075 0.0467  -0.0014 0.0222  310 GLN   A OE1   
4648  N  NE2   . GLN   A 285 ? 0.1721 0.2515 0.1909 0.0063  0.0143  0.0022  310 GLN   A NE2   
4657  N  N     . ILE   A 286 ? 0.1844 0.2337 0.2003 0.0080  0.0379  0.0003  311 ILE   A N     
4658  C  CA    . ILE   A 286 ? 0.1409 0.2174 0.2087 0.0124  0.0397  0.0179  311 ILE   A CA    
4659  C  C     . ILE   A 286 ? 0.1681 0.1999 0.1942 0.0097  0.0389  0.0059  311 ILE   A C     
4660  O  O     . ILE   A 286 ? 0.2341 0.2031 0.2061 0.0129  0.0219  -0.0006 311 ILE   A O     
4661  C  CB    . ILE   A 286 ? 0.1778 0.2545 0.2482 0.0266  0.0411  0.0513  311 ILE   A CB    
4662  C  CG1   . ILE   A 286 ? 0.1740 0.3151 0.2916 0.0312  0.0552  0.1005  311 ILE   A CG1   
4663  C  CG2   . ILE   A 286 ? 0.2070 0.2644 0.2553 -0.0115 0.0441  0.0427  311 ILE   A CG2   
4664  C  CD1   . ILE   A 286 ? 0.2686 0.3405 0.3364 0.0563  0.0403  0.0921  311 ILE   A CD1   
4676  N  N     . SER   A 287 ? 0.1400 0.1866 0.1919 -0.0095 0.0438  0.0048  312 SER   A N     
4677  C  CA    . SER   A 287 ? 0.1386 0.1923 0.2074 0.0118  0.0139  0.0173  312 SER   A CA    
4678  C  C     . SER   A 287 ? 0.1421 0.1773 0.2102 -0.0019 0.0227  0.0189  312 SER   A C     
4679  O  O     . SER   A 287 ? 0.1370 0.1769 0.2230 0.0198  0.0051  0.0072  312 SER   A O     
4680  C  CB    . SER   A 287 ? 0.1363 0.2123 0.2008 0.0286  0.0106  -0.0013 312 SER   A CB    
4681  O  OG    . SER   A 287 ? 0.1549 0.2196 0.1964 -0.0051 0.0218  0.0115  312 SER   A OG    
4687  N  N     . PHE   A 288 ? 0.1513 0.1626 0.2148 0.0050  0.0091  0.0029  313 PHE   A N     
4688  C  CA    . PHE   A 288 ? 0.1595 0.1637 0.2086 0.0119  0.0026  0.0058  313 PHE   A CA    
4689  C  C     . PHE   A 288 ? 0.1713 0.1703 0.1904 0.0121  0.0014  0.0036  313 PHE   A C     
4690  O  O     . PHE   A 288 ? 0.2010 0.1790 0.2043 0.0099  -0.0002 0.0056  313 PHE   A O     
4691  C  CB    . PHE   A 288 ? 0.1557 0.1830 0.2369 0.0207  0.0268  0.0061  313 PHE   A CB    
4692  C  CG    . PHE   A 288 ? 0.1439 0.1803 0.2475 0.0055  0.0111  0.0159  313 PHE   A CG    
4693  C  CD1   . PHE   A 288 ? 0.1235 0.1899 0.2592 0.0044  0.0064  0.0071  313 PHE   A CD1   
4694  C  CD2   . PHE   A 288 ? 0.1772 0.1887 0.2581 0.0201  0.0169  0.0145  313 PHE   A CD2   
4695  C  CE1   . PHE   A 288 ? 0.1430 0.1851 0.2719 0.0072  -0.0024 0.0098  313 PHE   A CE1   
4696  C  CE2   . PHE   A 288 ? 0.1642 0.2129 0.2630 0.0070  0.0114  0.0090  313 PHE   A CE2   
4697  C  CZ    . PHE   A 288 ? 0.1350 0.2090 0.2725 -0.0019 0.0052  0.0281  313 PHE   A CZ    
4707  N  N     . VAL   A 289 ? 0.1751 0.1633 0.1803 0.0226  0.0114  0.0003  314 VAL   A N     
4708  C  CA    . VAL   A 289 ? 0.1669 0.1656 0.1833 0.0087  0.0069  0.0142  314 VAL   A CA    
4709  C  C     . VAL   A 289 ? 0.1629 0.1679 0.2078 0.0241  0.0093  0.0186  314 VAL   A C     
4710  O  O     . VAL   A 289 ? 0.1864 0.1797 0.2128 0.0281  -0.0091 0.0059  314 VAL   A O     
4711  C  CB    . VAL   A 289 ? 0.1749 0.1924 0.1950 0.0426  0.0128  0.0209  314 VAL   A CB    
4712  C  CG1   . VAL   A 289 ? 0.1930 0.2065 0.2043 0.0231  0.0078  0.0363  314 VAL   A CG1   
4713  C  CG2   . VAL   A 289 ? 0.2048 0.2233 0.2026 0.0227  0.0216  0.0223  314 VAL   A CG2   
4723  N  N     . ASN   A 290 ? 0.1708 0.1554 0.2200 0.0324  -0.0012 0.0353  315 ASN   A N     
4724  C  CA    . ASN   A 290 ? 0.1670 0.1616 0.2372 0.0250  -0.0142 0.0475  315 ASN   A CA    
4725  C  C     . ASN   A 290 ? 0.1708 0.1639 0.2468 0.0339  -0.0209 0.0405  315 ASN   A C     
4726  O  O     . ASN   A 290 ? 0.2182 0.1759 0.2460 0.0224  -0.0356 0.0138  315 ASN   A O     
4727  C  CB    . ASN   A 290 ? 0.1815 0.1762 0.2424 0.0176  0.0013  0.0204  315 ASN   A CB    
4728  C  CG    . ASN   A 290 ? 0.1664 0.1723 0.2377 0.0142  0.0115  0.0227  315 ASN   A CG    
4729  O  OD1   . ASN   A 290 ? 0.2102 0.1856 0.2439 0.0119  0.0051  0.0216  315 ASN   A OD1   
4730  N  ND2   . ASN   A 290 ? 0.1743 0.1663 0.2354 0.0048  0.0104  -0.0016 315 ASN   A ND2   
4737  N  N     . SER   A 291 ? 0.1888 0.1816 0.2677 0.0303  -0.0090 0.0393  316 SER   A N     
4738  C  CA    . SER   A 291 ? 0.1805 0.2011 0.2968 0.0134  -0.0311 0.0327  316 SER   A CA    
4739  C  C     . SER   A 291 ? 0.1605 0.1812 0.2625 0.0038  -0.0297 0.0046  316 SER   A C     
4740  O  O     . SER   A 291 ? 0.1601 0.1827 0.2922 0.0081  -0.0119 -0.0015 316 SER   A O     
4741  C  CB    . SER   A 291 ? 0.2101 0.2363 0.3496 0.0413  -0.0070 0.0249  316 SER   A CB    
4742  O  OG    . SER   A 291 ? 0.2492 0.2692 0.3814 0.0268  -0.0244 0.0329  316 SER   A OG    
4748  N  N     . ILE   A 292 ? 0.1535 0.1874 0.2335 0.0176  -0.0222 0.0162  317 ILE   A N     
4749  C  CA    . ILE   A 292 ? 0.1679 0.1699 0.2125 0.0210  -0.0259 0.0076  317 ILE   A CA    
4750  C  C     . ILE   A 292 ? 0.1470 0.1642 0.2040 0.0139  -0.0158 0.0130  317 ILE   A C     
4751  O  O     . ILE   A 292 ? 0.1647 0.1837 0.2043 -0.0055 -0.0173 0.0180  317 ILE   A O     
4752  C  CB    . ILE   A 292 ? 0.1859 0.1905 0.2065 0.0338  -0.0155 0.0261  317 ILE   A CB    
4753  C  CG1   . ILE   A 292 ? 0.1889 0.2193 0.2066 0.0258  -0.0079 0.0140  317 ILE   A CG1   
4754  C  CG2   . ILE   A 292 ? 0.2032 0.1788 0.2100 0.0419  -0.0020 0.0339  317 ILE   A CG2   
4755  C  CD1   . ILE   A 292 ? 0.1832 0.2300 0.2107 0.0244  0.0169  0.0252  317 ILE   A CD1   
4767  N  N     . ALA   A 293 ? 0.1372 0.1666 0.2110 0.0063  -0.0232 0.0016  318 ALA   A N     
4768  C  CA    . ALA   A 293 ? 0.1475 0.1765 0.2168 -0.0062 0.0068  0.0173  318 ALA   A CA    
4769  C  C     . ALA   A 293 ? 0.1448 0.1787 0.2075 -0.0024 0.0013  -0.0002 318 ALA   A C     
4770  O  O     . ALA   A 293 ? 0.1654 0.1915 0.2130 0.0055  -0.0157 -0.0114 318 ALA   A O     
4771  C  CB    . ALA   A 293 ? 0.1713 0.1975 0.2240 0.0247  0.0015  0.0102  318 ALA   A CB    
4777  N  N     . THR   A 294 ? 0.1238 0.1830 0.1945 0.0121  0.0168  0.0037  319 THR   A N     
4778  C  CA    . THR   A 294 ? 0.1206 0.1859 0.1981 0.0024  0.0193  0.0243  319 THR   A CA    
4779  C  C     . THR   A 294 ? 0.1332 0.1937 0.2006 0.0082  0.0101  0.0208  319 THR   A C     
4780  O  O     . THR   A 294 ? 0.1631 0.2046 0.1854 0.0066  -0.0003 0.0184  319 THR   A O     
4781  C  CB    . THR   A 294 ? 0.1487 0.1922 0.2023 -0.0037 0.0110  0.0185  319 THR   A CB    
4782  O  OG1   . THR   A 294 ? 0.1577 0.1846 0.1972 -0.0049 0.0050  0.0225  319 THR   A OG1   
4783  C  CG2   . THR   A 294 ? 0.1553 0.1810 0.2053 0.0071  0.0043  0.0091  319 THR   A CG2   
4791  N  N     . SER   A 295 ? 0.1617 0.1736 0.2017 -0.0037 0.0059  0.0428  320 SER   A N     
4792  C  CA    . SER   A 295 ? 0.1464 0.1917 0.2084 0.0132  0.0149  0.0297  320 SER   A CA    
4793  C  C     . SER   A 295 ? 0.1530 0.1946 0.2177 0.0027  0.0058  0.0357  320 SER   A C     
4794  O  O     . SER   A 295 ? 0.2134 0.2344 0.2319 0.0159  -0.0042 0.0525  320 SER   A O     
4795  C  CB    . SER   A 295 ? 0.2004 0.2182 0.2440 -0.0289 0.0159  0.0197  320 SER   A CB    
4796  O  OG    . SER   A 295 ? 0.2649 0.2210 0.2591 -0.0542 0.0164  0.0224  320 SER   A OG    
4802  N  N     . LYS   A 296 ? 0.1316 0.1948 0.2139 0.0054  0.0117  0.0167  321 LYS   A N     
4803  C  CA    . LYS   A 296 ? 0.1358 0.2169 0.2340 0.0148  0.0106  0.0095  321 LYS   A CA    
4804  C  C     . LYS   A 296 ? 0.1442 0.2308 0.2581 -0.0073 -0.0207 -0.0025 321 LYS   A C     
4805  O  O     . LYS   A 296 ? 0.2182 0.2712 0.3476 0.0016  -0.0579 -0.0420 321 LYS   A O     
4806  C  CB    . LYS   A 296 ? 0.1507 0.2511 0.2671 0.0095  -0.0002 -0.0226 321 LYS   A CB    
4807  C  CG    . LYS   A 296 ? 0.2038 0.2779 0.3116 0.0024  -0.0154 -0.0322 321 LYS   A CG    
4808  C  CD    . LYS   A 296 ? 0.3233 0.3130 0.3542 0.0501  -0.0047 -0.0456 321 LYS   A CD    
4809  C  CE    . LYS   A 296 ? 0.4419 0.3568 0.4004 0.0629  -0.0291 -0.0464 321 LYS   A CE    
4810  N  NZ    . LYS   A 296 ? 0.5108 0.4033 0.4463 -0.0062 -0.0158 -0.0506 321 LYS   A NZ    
4824  N  N     . GLY   A 297 ? 0.1715 0.2016 0.2135 -0.0016 -0.0185 0.0063  322 GLY   A N     
4825  C  CA    . GLY   A 297 ? 0.2010 0.1915 0.1844 -0.0094 0.0077  -0.0085 322 GLY   A CA    
4826  C  C     . GLY   A 297 ? 0.1898 0.1864 0.1891 0.0025  0.0140  -0.0150 322 GLY   A C     
4827  O  O     . GLY   A 297 ? 0.1754 0.2181 0.1997 0.0046  0.0033  -0.0193 322 GLY   A O     
4831  N  N     . GLY   A 298 ? 0.1482 0.2161 0.2017 -0.0232 0.0201  -0.0131 323 GLY   A N     
4832  C  CA    . GLY   A 298 ? 0.1629 0.2291 0.2149 -0.0425 0.0270  -0.0082 323 GLY   A CA    
4833  C  C     . GLY   A 298 ? 0.1674 0.2206 0.2146 -0.0265 0.0344  -0.0187 323 GLY   A C     
4834  O  O     . GLY   A 298 ? 0.2055 0.2051 0.2045 0.0088  0.0362  -0.0090 323 GLY   A O     
4838  N  N     . ARG   A 299 ? 0.1637 0.2118 0.2267 -0.0191 0.0143  -0.0187 324 ARG   A N     
4839  C  CA    . ARG   A 299 ? 0.1486 0.2061 0.2404 -0.0272 0.0196  -0.0167 324 ARG   A CA    
4840  C  C     . ARG   A 299 ? 0.1903 0.1989 0.2238 -0.0382 0.0354  -0.0276 324 ARG   A C     
4841  O  O     . ARG   A 299 ? 0.2243 0.2201 0.2353 -0.0559 0.0306  -0.0320 324 ARG   A O     
4842  C  CB    . ARG   A 299 ? 0.1761 0.2205 0.2575 -0.0161 0.0687  -0.0204 324 ARG   A CB    
4843  C  CG    . ARG   A 299 ? 0.2223 0.2454 0.2819 -0.0308 0.0839  -0.0061 324 ARG   A CG    
4844  C  CD    . ARG   A 299 ? 0.3002 0.3273 0.3140 -0.0162 0.0669  -0.0209 324 ARG   A CD    
4845  N  NE    . ARG   A 299 ? 0.3035 0.3767 0.3493 -0.0272 0.0539  -0.0415 324 ARG   A NE    
4846  C  CZ    . ARG   A 299 ? 0.2593 0.4220 0.3777 0.0156  0.0572  -0.0451 324 ARG   A CZ    
4847  N  NH1   . ARG   A 299 ? 0.3009 0.4246 0.3968 0.0117  0.0300  -0.0311 324 ARG   A NH1   
4848  N  NH2   . ARG   A 299 ? 0.2185 0.4705 0.3936 0.0018  0.0801  -0.0484 324 ARG   A NH2   
4862  N  N     . HIS   A 300 ? 0.1839 0.2028 0.2152 -0.0296 0.0382  -0.0181 325 HIS   A N     
4863  C  CA    . HIS   A 300 ? 0.1682 0.2124 0.2176 -0.0292 0.0177  -0.0284 325 HIS   A CA    
4864  C  C     . HIS   A 300 ? 0.2016 0.2257 0.1996 -0.0236 0.0297  -0.0419 325 HIS   A C     
4865  O  O     . HIS   A 300 ? 0.2546 0.2445 0.2054 -0.0104 0.0350  -0.0372 325 HIS   A O     
4866  C  CB    . HIS   A 300 ? 0.1734 0.2040 0.2332 -0.0297 0.0197  -0.0197 325 HIS   A CB    
4867  C  CG    . HIS   A 300 ? 0.1790 0.1788 0.2366 -0.0112 0.0211  -0.0004 325 HIS   A CG    
4868  N  ND1   . HIS   A 300 ? 0.1786 0.1716 0.2317 -0.0026 0.0056  -0.0170 325 HIS   A ND1   
4869  C  CD2   . HIS   A 300 ? 0.2063 0.1648 0.2321 0.0157  0.0176  0.0011  325 HIS   A CD2   
4870  C  CE1   . HIS   A 300 ? 0.1554 0.1772 0.2319 -0.0037 0.0186  -0.0133 325 HIS   A CE1   
4871  N  NE2   . HIS   A 300 ? 0.1641 0.1678 0.2366 -0.0112 0.0209  0.0091  325 HIS   A NE2   
4879  N  N     . VAL   A 301 ? 0.1847 0.2256 0.1881 -0.0135 0.0172  -0.0364 326 VAL   A N     
4880  C  CA    . VAL   A 301 ? 0.1898 0.2279 0.1926 -0.0117 0.0089  -0.0461 326 VAL   A CA    
4881  C  C     . VAL   A 301 ? 0.1824 0.2602 0.2014 -0.0345 0.0342  -0.0428 326 VAL   A C     
4882  O  O     . VAL   A 301 ? 0.2389 0.3012 0.2113 -0.0343 0.0385  -0.0484 326 VAL   A O     
4883  C  CB    . VAL   A 301 ? 0.1774 0.2500 0.1899 -0.0252 -0.0159 -0.0230 326 VAL   A CB    
4884  C  CG1   . VAL   A 301 ? 0.2503 0.2777 0.2035 -0.0488 0.0122  0.0023  326 VAL   A CG1   
4885  C  CG2   . VAL   A 301 ? 0.2078 0.2734 0.2024 -0.0253 -0.0282 -0.0025 326 VAL   A CG2   
4895  N  N     . ASP   A 302 ? 0.2041 0.2709 0.2221 -0.0478 0.0243  -0.0335 327 ASP   A N     
4896  C  CA    . ASP   A 302 ? 0.2280 0.2955 0.2390 -0.0451 0.0024  -0.0523 327 ASP   A CA    
4897  C  C     . ASP   A 302 ? 0.2176 0.2938 0.2574 -0.0473 0.0176  -0.0692 327 ASP   A C     
4898  O  O     . ASP   A 302 ? 0.2592 0.3292 0.2761 -0.0509 0.0090  -0.0620 327 ASP   A O     
4899  C  CB    . ASP   A 302 ? 0.2015 0.3025 0.2522 -0.0586 0.0078  -0.0504 327 ASP   A CB    
4900  C  CG    . ASP   A 302 ? 0.2454 0.3206 0.2838 -0.0400 0.0096  -0.0417 327 ASP   A CG    
4901  O  OD1   . ASP   A 302 ? 0.2697 0.3143 0.2991 -0.0143 -0.0215 -0.0230 327 ASP   A OD1   
4902  O  OD2   . ASP   A 302 ? 0.2501 0.3478 0.3014 -0.0131 0.0276  -0.0536 327 ASP   A OD2   
4907  N  N     . TYR   A 303 ? 0.2132 0.2420 0.2656 -0.0594 0.0255  -0.0714 328 TYR   A N     
4908  C  CA    . TYR   A 303 ? 0.2623 0.2540 0.2904 -0.0402 0.0396  -0.0743 328 TYR   A CA    
4909  C  C     . TYR   A 303 ? 0.2467 0.2851 0.2839 -0.0480 0.0393  -0.0849 328 TYR   A C     
4910  O  O     . TYR   A 303 ? 0.2867 0.3301 0.2939 -0.0520 0.0350  -0.0937 328 TYR   A O     
4911  C  CB    . TYR   A 303 ? 0.2771 0.2393 0.3265 -0.0302 0.0455  -0.0541 328 TYR   A CB    
4912  C  CG    . TYR   A 303 ? 0.2666 0.2385 0.3719 -0.0307 0.0649  -0.0534 328 TYR   A CG    
4913  C  CD1   . TYR   A 303 ? 0.3064 0.2497 0.4104 -0.0125 0.0538  -0.0183 328 TYR   A CD1   
4914  C  CD2   . TYR   A 303 ? 0.2698 0.2448 0.3975 -0.0196 0.1067  -0.0539 328 TYR   A CD2   
4915  C  CE1   . TYR   A 303 ? 0.2725 0.2429 0.4381 -0.0218 0.0290  -0.0473 328 TYR   A CE1   
4916  C  CE2   . TYR   A 303 ? 0.2715 0.2539 0.4288 -0.0398 0.0866  -0.0660 328 TYR   A CE2   
4917  C  CZ    . TYR   A 303 ? 0.2846 0.2428 0.4518 -0.0497 0.0544  -0.0574 328 TYR   A CZ    
4918  O  OH    . TYR   A 303 ? 0.3464 0.2716 0.4844 -0.0230 0.0465  -0.0587 328 TYR   A OH    
4928  N  N     . VAL   A 304 ? 0.2300 0.2954 0.2678 -0.0318 0.0458  -0.0700 329 VAL   A N     
4929  C  CA    . VAL   A 304 ? 0.2754 0.3171 0.2556 -0.0224 0.0579  -0.0618 329 VAL   A CA    
4930  C  C     . VAL   A 304 ? 0.2820 0.3357 0.2517 -0.0191 0.0345  -0.0843 329 VAL   A C     
4931  O  O     . VAL   A 304 ? 0.2983 0.3233 0.2460 -0.0226 0.0360  -0.0879 329 VAL   A O     
4932  C  CB    . VAL   A 304 ? 0.2611 0.3509 0.2455 0.0234  0.0753  -0.0559 329 VAL   A CB    
4933  C  CG1   . VAL   A 304 ? 0.3242 0.3836 0.2581 0.0687  0.0822  -0.0953 329 VAL   A CG1   
4934  C  CG2   . VAL   A 304 ? 0.3306 0.3329 0.2728 0.0067  0.0460  -0.0596 329 VAL   A CG2   
4944  N  N     . ALA   A 305 ? 0.2670 0.3433 0.2468 -0.0166 0.0380  -0.1020 330 ALA   A N     
4945  C  CA    . ALA   A 305 ? 0.2775 0.3654 0.2440 -0.0273 0.0122  -0.0836 330 ALA   A CA    
4946  C  C     . ALA   A 305 ? 0.2738 0.4224 0.2657 -0.0261 0.0105  -0.0751 330 ALA   A C     
4947  O  O     . ALA   A 305 ? 0.3151 0.4266 0.2514 -0.0234 0.0178  -0.0898 330 ALA   A O     
4948  C  CB    . ALA   A 305 ? 0.3039 0.3494 0.2402 -0.0242 0.0063  -0.0546 330 ALA   A CB    
4954  N  N     . ASP   A 306 ? 0.2303 0.4686 0.3008 -0.0433 -0.0014 -0.0861 331 ASP   A N     
4955  C  CA    . ASP   A 306 ? 0.2545 0.5188 0.3362 -0.0382 0.0022  -0.0990 331 ASP   A CA    
4956  C  C     . ASP   A 306 ? 0.2845 0.4880 0.3366 -0.0486 0.0214  -0.0836 331 ASP   A C     
4957  O  O     . ASP   A 306 ? 0.3243 0.4994 0.3378 -0.0310 0.0217  -0.1075 331 ASP   A O     
4958  C  CB    . ASP   A 306 ? 0.2864 0.6033 0.3857 0.0031  -0.0079 -0.1272 331 ASP   A CB    
4959  C  CG    . ASP   A 306 ? 0.3671 0.6852 0.4269 0.0493  0.0014  -0.1391 331 ASP   A CG    
4960  O  OD1   . ASP   A 306 ? 0.3957 0.7115 0.4361 0.0651  -0.0021 -0.1389 331 ASP   A OD1   
4961  O  OD2   . ASP   A 306 ? 0.3943 0.7315 0.4530 0.0842  0.0253  -0.1347 331 ASP   A OD2   
4966  N  N     . GLN   A 307 ? 0.2777 0.4485 0.3404 -0.0497 0.0269  -0.0701 332 GLN   A N     
4967  C  CA    . GLN   A 307 ? 0.3708 0.4435 0.3561 -0.0662 0.0332  -0.0883 332 GLN   A CA    
4968  C  C     . GLN   A 307 ? 0.4089 0.4400 0.3491 -0.0908 0.0238  -0.0990 332 GLN   A C     
4969  O  O     . GLN   A 307 ? 0.4580 0.4396 0.3609 -0.0936 0.0047  -0.0905 332 GLN   A O     
4970  C  CB    . GLN   A 307 ? 0.4036 0.4208 0.3675 -0.0646 0.0368  -0.0985 332 GLN   A CB    
4971  C  CG    . GLN   A 307 ? 0.4329 0.3981 0.3872 -0.0843 0.0285  -0.1075 332 GLN   A CG    
4972  C  CD    . GLN   A 307 ? 0.4342 0.3619 0.3868 -0.0547 0.0309  -0.1148 332 GLN   A CD    
4973  O  OE1   . GLN   A 307 ? 0.4732 0.3660 0.3899 -0.0533 0.0379  -0.1296 332 GLN   A OE1   
4974  N  NE2   . GLN   A 307 ? 0.4051 0.3343 0.3827 -0.0696 0.0284  -0.0978 332 GLN   A NE2   
4983  N  N     . ILE   A 308 ? 0.3975 0.4331 0.3323 -0.1071 0.0273  -0.1034 333 ILE   A N     
4984  C  CA    . ILE   A 308 ? 0.3786 0.4342 0.2999 -0.0901 0.0383  -0.1260 333 ILE   A CA    
4985  C  C     . ILE   A 308 ? 0.3652 0.4592 0.2848 -0.0987 0.0277  -0.1235 333 ILE   A C     
4986  O  O     . ILE   A 308 ? 0.4032 0.4703 0.2913 -0.0885 0.0231  -0.1431 333 ILE   A O     
4987  C  CB    . ILE   A 308 ? 0.3822 0.4424 0.2969 -0.0721 0.0307  -0.1297 333 ILE   A CB    
4988  C  CG1   . ILE   A 308 ? 0.3597 0.4242 0.2948 -0.0490 0.0482  -0.1483 333 ILE   A CG1   
4989  C  CG2   . ILE   A 308 ? 0.3895 0.4663 0.2946 -0.1043 0.0232  -0.1397 333 ILE   A CG2   
4990  C  CD1   . ILE   A 308 ? 0.3432 0.4259 0.2801 -0.0426 0.0595  -0.1559 333 ILE   A CD1   
5002  N  N     . VAL   A 309 ? 0.3769 0.4662 0.2762 -0.0887 -0.0052 -0.1144 334 VAL   A N     
5003  C  CA    . VAL   A 309 ? 0.3893 0.4906 0.2925 -0.0742 -0.0182 -0.1213 334 VAL   A CA    
5004  C  C     . VAL   A 309 ? 0.3884 0.5241 0.2954 -0.0885 -0.0220 -0.1276 334 VAL   A C     
5005  O  O     . VAL   A 309 ? 0.3934 0.5332 0.2757 -0.0512 -0.0347 -0.1379 334 VAL   A O     
5006  C  CB    . VAL   A 309 ? 0.3682 0.4891 0.2979 -0.0437 -0.0279 -0.1198 334 VAL   A CB    
5007  C  CG1   . VAL   A 309 ? 0.4005 0.5070 0.3047 -0.0284 -0.0413 -0.1267 334 VAL   A CG1   
5008  C  CG2   . VAL   A 309 ? 0.3548 0.4775 0.3053 -0.0648 -0.0362 -0.1097 334 VAL   A CG2   
5018  N  N     . THR   A 310 ? 0.3844 0.5365 0.3119 -0.1616 -0.0126 -0.1311 335 THR   A N     
5019  C  CA    . THR   A 310 ? 0.4083 0.5762 0.3409 -0.1781 -0.0065 -0.1254 335 THR   A CA    
5020  C  C     . THR   A 310 ? 0.4706 0.5706 0.3428 -0.1393 -0.0004 -0.1581 335 THR   A C     
5021  O  O     . THR   A 310 ? 0.4853 0.5669 0.3403 -0.1463 -0.0136 -0.1702 335 THR   A O     
5022  C  CB    . THR   A 310 ? 0.4670 0.6390 0.3871 -0.1679 -0.0078 -0.0810 335 THR   A CB    
5023  O  OG1   . THR   A 310 ? 0.5486 0.6849 0.4361 -0.1467 -0.0253 -0.0499 335 THR   A OG1   
5024  C  CG2   . THR   A 310 ? 0.4470 0.6378 0.3698 -0.2044 0.0021  -0.0893 335 THR   A CG2   
5032  N  N     . LYS   A 311 ? 0.4938 0.5524 0.3383 -0.1274 0.0039  -0.1810 336 LYS   A N     
5033  C  CA    . LYS   A 311 ? 0.5793 0.5524 0.3410 -0.1256 0.0078  -0.1832 336 LYS   A CA    
5034  C  C     . LYS   A 311 ? 0.6278 0.5681 0.3110 -0.0957 0.0102  -0.1876 336 LYS   A C     
5035  O  O     . LYS   A 311 ? 0.6734 0.5850 0.3175 -0.0993 0.0058  -0.1905 336 LYS   A O     
5036  C  CB    . LYS   A 311 ? 0.6329 0.5428 0.3761 -0.1417 0.0232  -0.1920 336 LYS   A CB    
5037  C  CG    . LYS   A 311 ? 0.6665 0.5636 0.4039 -0.1567 0.0230  -0.1803 336 LYS   A CG    
5038  C  CD    . LYS   A 311 ? 0.6952 0.6120 0.4404 -0.1326 0.0130  -0.1528 336 LYS   A CD    
5039  C  CE    . LYS   A 311 ? 0.7405 0.6786 0.4757 -0.0938 -0.0032 -0.1280 336 LYS   A CE    
5040  N  NZ    . LYS   A 311 ? 0.7920 0.7231 0.5032 -0.0720 0.0023  -0.1085 336 LYS   A NZ    
5054  N  N     . LEU   A 312 ? 0.6167 0.5623 0.2929 -0.0599 0.0113  -0.1719 337 LEU   A N     
5055  C  CA    . LEU   A 312 ? 0.6106 0.5762 0.3082 -0.0301 0.0010  -0.1593 337 LEU   A CA    
5056  C  C     . LEU   A 312 ? 0.5937 0.6103 0.3000 -0.0390 -0.0426 -0.1574 337 LEU   A C     
5057  O  O     . LEU   A 312 ? 0.6122 0.6227 0.2866 -0.0531 -0.0528 -0.1584 337 LEU   A O     
5058  C  CB    . LEU   A 312 ? 0.6024 0.5370 0.3401 -0.0154 0.0078  -0.1624 337 LEU   A CB    
5059  C  CG    . LEU   A 312 ? 0.6355 0.5444 0.3872 -0.0012 0.0176  -0.1518 337 LEU   A CG    
5060  C  CD1   . LEU   A 312 ? 0.6254 0.5510 0.4058 -0.0166 0.0074  -0.1235 337 LEU   A CD1   
5061  C  CD2   . LEU   A 312 ? 0.6448 0.5351 0.4042 0.0313  0.0334  -0.1644 337 LEU   A CD2   
5073  N  N     . VAL   A 313 ? 0.5838 0.6246 0.3146 -0.0330 -0.0770 -0.1602 338 VAL   A N     
5074  C  CA    . VAL   A 313 ? 0.5715 0.6368 0.3478 -0.0569 -0.1038 -0.1694 338 VAL   A CA    
5075  C  C     . VAL   A 313 ? 0.6540 0.6573 0.3807 -0.0828 -0.1403 -0.1613 338 VAL   A C     
5076  O  O     . VAL   A 313 ? 0.6780 0.6694 0.3892 -0.0664 -0.1610 -0.1451 338 VAL   A O     
5077  C  CB    . VAL   A 313 ? 0.5019 0.6397 0.3597 -0.0454 -0.1003 -0.1750 338 VAL   A CB    
5078  C  CG1   . VAL   A 313 ? 0.5208 0.6519 0.3586 -0.0338 -0.0846 -0.1653 338 VAL   A CG1   
5079  C  CG2   . VAL   A 313 ? 0.4776 0.6402 0.3725 -0.0223 -0.0907 -0.1749 338 VAL   A CG2   
5089  N  N     . ASP   A 314 ? 0.7236 0.6634 0.4027 -0.1002 -0.1421 -0.1725 339 ASP   A N     
5090  C  CA    . ASP   A 314 ? 0.7942 0.6681 0.4154 -0.1001 -0.1539 -0.1880 339 ASP   A CA    
5091  C  C     . ASP   A 314 ? 0.8477 0.6769 0.4054 -0.0642 -0.1384 -0.2225 339 ASP   A C     
5092  O  O     . ASP   A 314 ? 0.8610 0.6864 0.4079 -0.0768 -0.1407 -0.2434 339 ASP   A O     
5093  C  CB    . ASP   A 314 ? 0.8375 0.6871 0.4480 -0.1074 -0.1707 -0.1471 339 ASP   A CB    
5094  C  CG    . ASP   A 314 ? 0.8817 0.7105 0.4854 -0.0967 -0.1820 -0.0877 339 ASP   A CG    
5095  O  OD1   . ASP   A 314 ? 0.8934 0.7317 0.5050 -0.0902 -0.1813 -0.0551 339 ASP   A OD1   
5096  O  OD2   . ASP   A 314 ? 0.9001 0.7000 0.4894 -0.0953 -0.1933 -0.0688 339 ASP   A OD2   
5101  N  N     . VAL   A 315 ? 0.8793 0.6801 0.3875 0.0056  -0.1153 -0.2382 340 VAL   A N     
5102  C  CA    . VAL   A 315 ? 0.8950 0.6964 0.3791 0.0781  -0.0882 -0.2306 340 VAL   A CA    
5103  C  C     . VAL   A 315 ? 0.8938 0.6914 0.3771 0.1016  -0.0971 -0.2339 340 VAL   A C     
5104  O  O     . VAL   A 315 ? 0.8939 0.6908 0.3685 0.0997  -0.0988 -0.2261 340 VAL   A O     
5105  C  CB    . VAL   A 315 ? 0.9132 0.7266 0.3772 0.0958  -0.0713 -0.2057 340 VAL   A CB    
5106  C  CG1   . VAL   A 315 ? 0.9282 0.7456 0.3790 0.0998  -0.0661 -0.1887 340 VAL   A CG1   
5107  C  CG2   . VAL   A 315 ? 0.9130 0.7350 0.3806 0.0998  -0.0644 -0.1991 340 VAL   A CG2   
5117  N  N     . VAL   A 316 ? 0.8972 0.6887 0.3946 0.1137  -0.1033 -0.2438 341 VAL   A N     
5118  C  CA    . VAL   A 316 ? 0.9322 0.6989 0.4212 0.1079  -0.1144 -0.2548 341 VAL   A CA    
5119  C  C     . VAL   A 316 ? 0.9640 0.7419 0.4531 0.0606  -0.1478 -0.2468 341 VAL   A C     
5120  O  O     . VAL   A 316 ? 0.9873 0.7585 0.4550 0.0546  -0.1609 -0.2196 341 VAL   A O     
5121  C  CB    . VAL   A 316 ? 0.9153 0.6689 0.4293 0.1285  -0.0966 -0.2563 341 VAL   A CB    
5122  C  CG1   . VAL   A 316 ? 0.9127 0.6785 0.4340 0.1367  -0.0964 -0.2506 341 VAL   A CG1   
5123  C  CG2   . VAL   A 316 ? 0.9008 0.6413 0.4362 0.1358  -0.0742 -0.2632 341 VAL   A CG2   
5133  N  N     . LYS   A 317 ? 0.9764 0.7707 0.4809 0.0297  -0.1611 -0.2726 342 LYS   A N     
5134  C  CA    . LYS   A 317 ? 0.9902 0.7973 0.5159 0.0058  -0.1618 -0.2903 342 LYS   A CA    
5135  C  C     . LYS   A 317 ? 1.0050 0.8080 0.5309 -0.0107 -0.1752 -0.3288 342 LYS   A C     
5136  O  O     . LYS   A 317 ? 1.0166 0.8261 0.5370 0.0047  -0.1838 -0.3189 342 LYS   A O     
5137  C  CB    . LYS   A 317 ? 0.9789 0.8059 0.5323 -0.0020 -0.1429 -0.2761 342 LYS   A CB    
5138  C  CG    . LYS   A 317 ? 0.9665 0.8165 0.5509 -0.0039 -0.1310 -0.2542 342 LYS   A CG    
5139  C  CD    . LYS   A 317 ? 0.9666 0.8115 0.5592 -0.0043 -0.1150 -0.2563 342 LYS   A CD    
5140  C  CE    . LYS   A 317 ? 0.9627 0.7950 0.5504 -0.0103 -0.1216 -0.2769 342 LYS   A CE    
5141  N  NZ    . LYS   A 317 ? 0.9603 0.7876 0.5368 -0.0090 -0.1272 -0.2842 342 LYS   A NZ    
5155  N  N     . LYS   A 318 ? 1.0205 0.8216 0.5506 -0.0207 -0.1691 -0.3454 343 LYS   A N     
5156  C  CA    . LYS   A 318 ? 1.0707 0.8529 0.5723 -0.0067 -0.1665 -0.3629 343 LYS   A CA    
5157  C  C     . LYS   A 318 ? 1.0918 0.8823 0.5801 0.0137  -0.1617 -0.3585 343 LYS   A C     
5158  O  O     . LYS   A 318 ? 1.0987 0.8943 0.5711 0.0319  -0.1836 -0.3603 343 LYS   A O     
5159  C  CB    . LYS   A 318 ? 1.1031 0.8760 0.6003 -0.0108 -0.1548 -0.3479 343 LYS   A CB    
5160  C  CG    . LYS   A 318 ? 1.1243 0.9000 0.6319 -0.0147 -0.1411 -0.3127 343 LYS   A CG    
5161  C  CD    . LYS   A 318 ? 1.1426 0.9219 0.6603 -0.0116 -0.1266 -0.2764 343 LYS   A CD    
5162  C  CE    . LYS   A 318 ? 1.1586 0.9382 0.6832 -0.0102 -0.1153 -0.2483 343 LYS   A CE    
5163  N  NZ    . LYS   A 318 ? 1.1693 0.9451 0.6948 -0.0099 -0.1093 -0.2350 343 LYS   A NZ    
5177  N  N     . LYS   A 319 ? 1.0956 0.9203 0.6041 0.0101  -0.1243 -0.3294 344 LYS   A N     
5178  C  CA    . LYS   A 319 ? 1.0983 0.9700 0.6488 -0.0006 -0.0764 -0.2803 344 LYS   A CA    
5179  C  C     . LYS   A 319 ? 1.1156 0.9861 0.6729 -0.0170 -0.0470 -0.2510 344 LYS   A C     
5180  O  O     . LYS   A 319 ? 1.1168 0.9913 0.6848 -0.0299 -0.0501 -0.2333 344 LYS   A O     
5181  C  CB    . LYS   A 319 ? 1.0858 0.9967 0.6653 -0.0019 -0.0741 -0.2591 344 LYS   A CB    
5182  C  CG    . LYS   A 319 ? 1.0806 1.0223 0.6816 -0.0039 -0.0750 -0.2286 344 LYS   A CG    
5183  C  CD    . LYS   A 319 ? 1.0748 1.0497 0.6973 -0.0049 -0.0715 -0.2005 344 LYS   A CD    
5184  C  CE    . LYS   A 319 ? 1.0717 1.0722 0.7126 -0.0108 -0.0715 -0.1796 344 LYS   A CE    
5185  N  NZ    . LYS   A 319 ? 1.0724 1.0866 0.7226 -0.0116 -0.0683 -0.1683 344 LYS   A NZ    
5199  N  N     . ASN   A 320 ? 1.1282 0.9854 0.6743 -0.0141 -0.0160 -0.2531 345 ASN   A N     
5200  C  CA    . ASN   A 320 ? 1.1379 0.9730 0.6639 -0.0092 0.0016  -0.2639 345 ASN   A CA    
5201  C  C     . ASN   A 320 ? 1.1449 0.9408 0.6421 -0.0203 0.0057  -0.2976 345 ASN   A C     
5202  O  O     . ASN   A 320 ? 1.1611 0.8942 0.6190 -0.0228 0.0202  -0.3521 345 ASN   A O     
5203  C  CB    . ASN   A 320 ? 1.1435 0.9910 0.6742 0.0181  0.0208  -0.2446 345 ASN   A CB    
5204  C  CG    . ASN   A 320 ? 1.1467 1.0020 0.6772 0.0283  0.0262  -0.2356 345 ASN   A CG    
5205  O  OD1   . ASN   A 320 ? 1.1469 0.9978 0.6773 0.0339  0.0288  -0.2390 345 ASN   A OD1   
5206  N  ND2   . ASN   A 320 ? 1.1430 1.0083 0.6734 0.0333  0.0236  -0.2295 345 ASN   A ND2   
5213  N  N     . ALA   A 325 ? 0.7759 0.7164 0.7399 -0.1373 -0.0920 -0.3090 350 ALA   A N     
5214  C  CA    . ALA   A 325 ? 0.7754 0.7261 0.7289 -0.1032 -0.1110 -0.2993 350 ALA   A CA    
5215  C  C     . ALA   A 325 ? 0.7575 0.7424 0.7201 -0.0917 -0.1253 -0.2737 350 ALA   A C     
5216  O  O     . ALA   A 325 ? 0.7708 0.7696 0.7357 -0.0796 -0.1215 -0.2632 350 ALA   A O     
5217  C  CB    . ALA   A 325 ? 0.7719 0.7104 0.7204 -0.0930 -0.1324 -0.3172 350 ALA   A CB    
5222  N  N     . VAL   A 326 ? 0.7328 0.7340 0.6917 -0.0777 -0.1340 -0.2527 351 VAL   A N     
5223  C  CA    . VAL   A 326 ? 0.6916 0.7163 0.6606 -0.0541 -0.1333 -0.2282 351 VAL   A CA    
5224  C  C     . VAL   A 326 ? 0.6485 0.6942 0.6192 -0.0567 -0.1495 -0.2246 351 VAL   A C     
5225  O  O     . VAL   A 326 ? 0.6884 0.7088 0.6108 -0.0495 -0.1664 -0.2191 351 VAL   A O     
5226  C  CB    . VAL   A 326 ? 0.7126 0.7281 0.6754 -0.0066 -0.1057 -0.1968 351 VAL   A CB    
5227  C  CG1   . VAL   A 326 ? 0.7304 0.7401 0.6825 0.0134  -0.0956 -0.1778 351 VAL   A CG1   
5228  C  CG2   . VAL   A 326 ? 0.7031 0.7271 0.6775 0.0169  -0.0939 -0.1902 351 VAL   A CG2   
5238  N  N     . LYS   A 327 ? 0.5711 0.6611 0.5894 -0.0251 -0.1369 -0.2258 352 LYS   A N     
5239  C  CA    . LYS   A 327 ? 0.5144 0.6403 0.5750 0.0165  -0.1022 -0.2040 352 LYS   A CA    
5240  C  C     . LYS   A 327 ? 0.4508 0.5911 0.5313 0.0275  -0.0723 -0.2056 352 LYS   A C     
5241  O  O     . LYS   A 327 ? 0.4570 0.5576 0.5218 0.0343  -0.0816 -0.2280 352 LYS   A O     
5242  C  CB    . LYS   A 327 ? 0.5190 0.6731 0.6039 0.0486  -0.0964 -0.1820 352 LYS   A CB    
5243  C  CG    . LYS   A 327 ? 0.5390 0.7068 0.6295 0.0642  -0.0935 -0.1585 352 LYS   A CG    
5244  C  CD    . LYS   A 327 ? 0.5764 0.7382 0.6480 0.0661  -0.0904 -0.1282 352 LYS   A CD    
5245  C  CE    . LYS   A 327 ? 0.5730 0.7552 0.6577 0.0736  -0.0874 -0.1037 352 LYS   A CE    
5246  N  NZ    . LYS   A 327 ? 0.5741 0.7722 0.6630 0.0593  -0.0789 -0.0921 352 LYS   A NZ    
5260  N  N     . ALA   A 328 ? 0.3914 0.5893 0.5038 0.0223  -0.0275 -0.1619 353 ALA   A N     
5261  C  CA    . ALA   A 328 ? 0.4111 0.5977 0.4698 0.0129  0.0130  -0.1256 353 ALA   A CA    
5262  C  C     . ALA   A 328 ? 0.3593 0.5627 0.4411 0.0319  0.0035  -0.1241 353 ALA   A C     
5263  O  O     . ALA   A 328 ? 0.3137 0.5399 0.4397 0.0378  0.0151  -0.1232 353 ALA   A O     
5264  C  CB    . ALA   A 328 ? 0.4295 0.6190 0.4653 -0.0021 0.0784  -0.1096 353 ALA   A CB    
5270  N  N     . HIS   A 329 ? 0.3276 0.5563 0.4127 0.0566  -0.0075 -0.1365 354 HIS   A N     
5271  C  CA    . HIS   A 329 ? 0.3457 0.5535 0.3890 0.0482  -0.0379 -0.1475 354 HIS   A CA    
5272  C  C     . HIS   A 329 ? 0.3217 0.5469 0.3663 0.0376  -0.0406 -0.1355 354 HIS   A C     
5273  O  O     . HIS   A 329 ? 0.3234 0.5498 0.3635 0.0280  -0.0290 -0.1226 354 HIS   A O     
5274  C  CB    . HIS   A 329 ? 0.3971 0.5607 0.3901 0.0752  -0.0465 -0.1714 354 HIS   A CB    
5275  C  CG    . HIS   A 329 ? 0.4304 0.5751 0.4019 0.0905  -0.0561 -0.1791 354 HIS   A CG    
5276  N  ND1   . HIS   A 329 ? 0.4274 0.5903 0.4077 0.0945  -0.0365 -0.1768 354 HIS   A ND1   
5277  C  CD2   . HIS   A 329 ? 0.4569 0.5776 0.4187 0.0896  -0.0834 -0.1776 354 HIS   A CD2   
5278  C  CE1   . HIS   A 329 ? 0.4270 0.5887 0.4157 0.0969  -0.0524 -0.1775 354 HIS   A CE1   
5279  N  NE2   . HIS   A 329 ? 0.4693 0.5922 0.4238 0.1007  -0.0719 -0.1717 354 HIS   A NE2   
5287  N  N     . GLN   A 330 ? 0.3332 0.5537 0.3645 0.0502  -0.0408 -0.1181 355 GLN   A N     
5288  C  CA    . GLN   A 330 ? 0.2999 0.5679 0.3709 0.0312  -0.0639 -0.1010 355 GLN   A CA    
5289  C  C     . GLN   A 330 ? 0.2823 0.5295 0.3663 0.0209  -0.0428 -0.0727 355 GLN   A C     
5290  O  O     . GLN   A 330 ? 0.3250 0.5345 0.3664 0.0124  -0.0320 -0.0666 355 GLN   A O     
5291  C  CB    . GLN   A 330 ? 0.3258 0.6192 0.3953 0.0310  -0.1091 -0.1055 355 GLN   A CB    
5292  C  CG    . GLN   A 330 ? 0.4145 0.6541 0.4248 0.0212  -0.1306 -0.0981 355 GLN   A CG    
5293  C  CD    . GLN   A 330 ? 0.5016 0.7021 0.4523 0.0117  -0.1215 -0.0777 355 GLN   A CD    
5294  O  OE1   . GLN   A 330 ? 0.5287 0.7143 0.4660 -0.0021 -0.1141 -0.0824 355 GLN   A OE1   
5295  N  NE2   . GLN   A 330 ? 0.5487 0.7242 0.4585 0.0175  -0.1158 -0.0568 355 GLN   A NE2   
5304  N  N     . VAL   A 331 ? 0.2685 0.4987 0.3629 0.0159  -0.0280 -0.0654 356 VAL   A N     
5305  C  CA    . VAL   A 331 ? 0.3074 0.4816 0.3569 0.0312  -0.0067 -0.0455 356 VAL   A CA    
5306  C  C     . VAL   A 331 ? 0.3037 0.4807 0.3246 0.0337  0.0232  -0.0337 356 VAL   A C     
5307  O  O     . VAL   A 331 ? 0.3102 0.4636 0.3242 0.0058  0.0161  -0.0291 356 VAL   A O     
5308  C  CB    . VAL   A 331 ? 0.3652 0.4957 0.3967 0.0024  -0.0043 -0.0273 356 VAL   A CB    
5309  C  CG1   . VAL   A 331 ? 0.3681 0.5064 0.4116 -0.0005 0.0199  -0.0250 356 VAL   A CG1   
5310  C  CG2   . VAL   A 331 ? 0.4318 0.5092 0.4206 -0.0135 0.0016  -0.0210 356 VAL   A CG2   
5320  N  N     . LYS   A 332 ? 0.2714 0.4896 0.2838 0.0384  0.0242  -0.0380 357 LYS   A N     
5321  C  CA    . LYS   A 332 ? 0.2914 0.5144 0.2643 0.0451  -0.0046 -0.0603 357 LYS   A CA    
5322  C  C     . LYS   A 332 ? 0.2775 0.5230 0.2369 0.0478  -0.0375 -0.0494 357 LYS   A C     
5323  O  O     . LYS   A 332 ? 0.2975 0.5500 0.2118 0.0429  -0.0182 -0.0413 357 LYS   A O     
5324  C  CB    . LYS   A 332 ? 0.3228 0.5540 0.2725 0.0453  -0.0172 -0.0929 357 LYS   A CB    
5325  C  CG    . LYS   A 332 ? 0.3373 0.5678 0.2593 0.0402  -0.0013 -0.1224 357 LYS   A CG    
5326  C  CD    . LYS   A 332 ? 0.3500 0.5747 0.2712 0.0186  0.0135  -0.1161 357 LYS   A CD    
5327  C  CE    . LYS   A 332 ? 0.3478 0.5687 0.2895 0.0118  0.0187  -0.1251 357 LYS   A CE    
5328  N  NZ    . LYS   A 332 ? 0.3845 0.5824 0.3218 0.0070  0.0557  -0.1245 357 LYS   A NZ    
5342  N  N     . ASN   A 333 ? 0.2944 0.5091 0.2389 0.0393  -0.0628 -0.0434 358 ASN   A N     
5343  C  CA    . ASN   A 333 ? 0.3454 0.4898 0.2789 0.0363  -0.0546 -0.0415 358 ASN   A CA    
5344  C  C     . ASN   A 333 ? 0.3773 0.4279 0.2475 0.0207  -0.0386 -0.0244 358 ASN   A C     
5345  O  O     . ASN   A 333 ? 0.4045 0.4110 0.2604 -0.0008 -0.0291 -0.0251 358 ASN   A O     
5346  C  CB    . ASN   A 333 ? 0.4175 0.5648 0.3477 0.0437  -0.0439 -0.0625 358 ASN   A CB    
5347  C  CG    . ASN   A 333 ? 0.4793 0.6399 0.3976 0.0847  -0.0709 -0.0715 358 ASN   A CG    
5348  O  OD1   . ASN   A 333 ? 0.4730 0.6988 0.3995 0.1536  -0.0849 -0.0366 358 ASN   A OD1   
5349  N  ND2   . ASN   A 333 ? 0.5184 0.6380 0.4318 0.0732  -0.0648 -0.0933 358 ASN   A ND2   
5356  N  N     . HIS   A 334 ? 0.3857 0.4167 0.2209 0.0134  -0.0222 -0.0171 359 HIS   A N     
5357  C  CA    . HIS   A 334 ? 0.3853 0.4235 0.2042 0.0187  -0.0215 -0.0234 359 HIS   A CA    
5358  C  C     . HIS   A 334 ? 0.3748 0.3899 0.2012 0.0299  -0.0056 -0.0391 359 HIS   A C     
5359  O  O     . HIS   A 334 ? 0.4010 0.3933 0.2143 0.0318  0.0056  -0.0461 359 HIS   A O     
5360  C  CB    . HIS   A 334 ? 0.4372 0.4985 0.2150 0.0186  -0.0167 -0.0027 359 HIS   A CB    
5361  C  CG    . HIS   A 334 ? 0.4582 0.5924 0.2340 0.0161  -0.0333 0.0409  359 HIS   A CG    
5362  N  ND1   . HIS   A 334 ? 0.5015 0.6251 0.2685 0.0196  -0.0517 0.0770  359 HIS   A ND1   
5363  C  CD2   . HIS   A 334 ? 0.5098 0.6323 0.2481 -0.0069 -0.0270 0.0521  359 HIS   A CD2   
5364  C  CE1   . HIS   A 334 ? 0.5246 0.6574 0.2709 0.0052  -0.0452 0.0787  359 HIS   A CE1   
5365  N  NE2   . HIS   A 334 ? 0.5295 0.6638 0.2669 -0.0076 -0.0330 0.0629  359 HIS   A NE2   
5373  N  N     . MET   A 335 ? 0.3442 0.3617 0.1982 0.0289  -0.0047 -0.0511 360 MET   A N     
5374  C  CA    . MET   A 335 ? 0.3033 0.3156 0.2140 0.0272  0.0141  -0.0307 360 MET   A CA    
5375  C  C     . MET   A 335 ? 0.2801 0.2997 0.2091 0.0289  0.0268  -0.0107 360 MET   A C     
5376  O  O     . MET   A 335 ? 0.2809 0.2892 0.2338 0.0415  0.0112  0.0132  360 MET   A O     
5377  C  CB    . MET   A 335 ? 0.3176 0.3166 0.2508 -0.0055 0.0254  -0.0234 360 MET   A CB    
5378  C  CG    . MET   A 335 ? 0.3770 0.3496 0.2902 -0.0378 0.0072  -0.0074 360 MET   A CG    
5379  S  SD    . MET   A 335 ? 0.4117 0.3854 0.3479 -0.0446 -0.0020 -0.0179 360 MET   A SD    
5380  C  CE    . MET   A 335 ? 0.3625 0.3895 0.3508 -0.0175 0.0137  0.0225  360 MET   A CE    
5390  N  N     . TRP   A 336 ? 0.2391 0.3049 0.1844 0.0457  0.0213  -0.0079 361 TRP   A N     
5391  C  CA    . TRP   A 336 ? 0.2511 0.2903 0.2056 0.0190  0.0319  0.0050  361 TRP   A CA    
5392  C  C     . TRP   A 336 ? 0.2826 0.2747 0.2001 0.0415  0.0483  0.0032  361 TRP   A C     
5393  O  O     . TRP   A 336 ? 0.2891 0.2847 0.2166 0.0377  0.0669  -0.0016 361 TRP   A O     
5394  C  CB    . TRP   A 336 ? 0.2494 0.2985 0.2256 0.0174  0.0307  0.0153  361 TRP   A CB    
5395  C  CG    . TRP   A 336 ? 0.2326 0.2913 0.2529 0.0272  0.0375  0.0147  361 TRP   A CG    
5396  C  CD1   . TRP   A 336 ? 0.2176 0.2949 0.2675 0.0374  0.0342  0.0127  361 TRP   A CD1   
5397  C  CD2   . TRP   A 336 ? 0.2302 0.2908 0.2781 0.0052  0.0347  0.0095  361 TRP   A CD2   
5398  N  NE1   . TRP   A 336 ? 0.2660 0.2977 0.2667 0.0158  0.0506  0.0079  361 TRP   A NE1   
5399  C  CE2   . TRP   A 336 ? 0.2738 0.2819 0.2839 0.0090  0.0445  0.0065  361 TRP   A CE2   
5400  C  CE3   . TRP   A 336 ? 0.2867 0.3083 0.2881 -0.0157 0.0375  0.0073  361 TRP   A CE3   
5401  C  CZ2   . TRP   A 336 ? 0.3145 0.2901 0.2891 -0.0042 0.0681  0.0353  361 TRP   A CZ2   
5402  C  CZ3   . TRP   A 336 ? 0.3280 0.3186 0.2882 -0.0446 0.0559  0.0155  361 TRP   A CZ3   
5403  C  CH2   . TRP   A 336 ? 0.3351 0.3177 0.2967 -0.0362 0.0621  0.0178  361 TRP   A CH2   
5414  N  N     . ILE   A 337 ? 0.2387 0.2592 0.1879 0.0364  0.0404  0.0000  362 ILE   A N     
5415  C  CA    . ILE   A 337 ? 0.2093 0.2431 0.2051 0.0223  0.0416  -0.0031 362 ILE   A CA    
5416  C  C     . ILE   A 337 ? 0.2133 0.2312 0.1974 0.0198  0.0354  0.0048  362 ILE   A C     
5417  O  O     . ILE   A 337 ? 0.1965 0.2283 0.2099 0.0095  0.0266  -0.0014 362 ILE   A O     
5418  C  CB    . ILE   A 337 ? 0.2194 0.2635 0.2362 0.0249  0.0514  0.0100  362 ILE   A CB    
5419  C  CG1   . ILE   A 337 ? 0.2773 0.3133 0.2707 0.0180  0.0737  0.0499  362 ILE   A CG1   
5420  C  CG2   . ILE   A 337 ? 0.1880 0.3000 0.2357 -0.0083 0.0215  0.0254  362 ILE   A CG2   
5421  C  CD1   . ILE   A 337 ? 0.3232 0.3720 0.2991 0.0432  0.0984  0.0331  362 ILE   A CD1   
5433  N  N     . PHE   A 338 ? 0.2185 0.2249 0.1994 0.0211  0.0534  -0.0102 363 PHE   A N     
5434  C  CA    . PHE   A 338 ? 0.2008 0.2095 0.2096 0.0114  0.0508  -0.0050 363 PHE   A CA    
5435  C  C     . PHE   A 338 ? 0.2238 0.2100 0.2107 0.0258  0.0432  -0.0062 363 PHE   A C     
5436  O  O     . PHE   A 338 ? 0.2695 0.2180 0.2169 0.0277  0.0383  -0.0111 363 PHE   A O     
5437  C  CB    . PHE   A 338 ? 0.1585 0.2483 0.2248 0.0202  0.0448  0.0030  363 PHE   A CB    
5438  C  CG    . PHE   A 338 ? 0.1786 0.2596 0.2484 0.0292  0.0451  0.0138  363 PHE   A CG    
5439  C  CD1   . PHE   A 338 ? 0.2469 0.2702 0.2617 0.0397  0.0577  0.0052  363 PHE   A CD1   
5440  C  CD2   . PHE   A 338 ? 0.2090 0.2611 0.2655 0.0131  0.0736  0.0251  363 PHE   A CD2   
5441  C  CE1   . PHE   A 338 ? 0.2432 0.2953 0.2709 0.0340  0.0530  0.0116  363 PHE   A CE1   
5442  C  CE2   . PHE   A 338 ? 0.2151 0.2836 0.2850 0.0186  0.0700  0.0131  363 PHE   A CE2   
5443  C  CZ    . PHE   A 338 ? 0.2350 0.2753 0.2782 0.0319  0.0646  0.0264  363 PHE   A CZ    
5453  N  N     . VAL   A 339 ? 0.2003 0.1929 0.2084 0.0166  0.0300  0.0073  364 VAL   A N     
5454  C  CA    . VAL   A 339 ? 0.1838 0.1853 0.2226 0.0067  0.0249  0.0072  364 VAL   A CA    
5455  C  C     . VAL   A 339 ? 0.1750 0.1730 0.2311 0.0217  0.0119  0.0011  364 VAL   A C     
5456  O  O     . VAL   A 339 ? 0.2171 0.1924 0.2461 0.0084  -0.0017 -0.0052 364 VAL   A O     
5457  C  CB    . VAL   A 339 ? 0.1681 0.2054 0.2325 0.0036  0.0166  0.0124  364 VAL   A CB    
5458  C  CG1   . VAL   A 339 ? 0.2164 0.2268 0.2466 -0.0122 0.0094  0.0059  364 VAL   A CG1   
5459  C  CG2   . VAL   A 339 ? 0.2227 0.2366 0.2375 -0.0211 0.0176  0.0065  364 VAL   A CG2   
5469  N  N     . ASN   A 340 ? 0.1781 0.1849 0.2428 0.0108  0.0119  -0.0034 365 ASN   A N     
5470  C  CA    . ASN   A 340 ? 0.1607 0.1791 0.2531 0.0412  0.0117  -0.0075 365 ASN   A CA    
5471  C  C     . ASN   A 340 ? 0.1791 0.1753 0.2555 0.0499  0.0212  0.0091  365 ASN   A C     
5472  O  O     . ASN   A 340 ? 0.1848 0.1916 0.2691 0.0399  0.0279  -0.0057 365 ASN   A O     
5473  C  CB    . ASN   A 340 ? 0.1957 0.1884 0.2588 0.0307  0.0366  0.0038  365 ASN   A CB    
5474  C  CG    . ASN   A 340 ? 0.1765 0.1988 0.2608 0.0195  0.0286  0.0079  365 ASN   A CG    
5475  O  OD1   . ASN   A 340 ? 0.1681 0.2084 0.2576 0.0190  0.0026  -0.0095 365 ASN   A OD1   
5476  N  ND2   . ASN   A 340 ? 0.1919 0.2035 0.2577 0.0134  -0.0031 -0.0081 365 ASN   A ND2   
5483  N  N     . ALA   A 341 ? 0.2137 0.1701 0.2386 0.0022  0.0406  -0.0001 366 ALA   A N     
5484  C  CA    . ALA   A 341 ? 0.1899 0.1465 0.2250 0.0084  0.0294  0.0068  366 ALA   A CA    
5485  C  C     . ALA   A 341 ? 0.1912 0.1441 0.2238 0.0127  0.0247  0.0103  366 ALA   A C     
5486  O  O     . ALA   A 341 ? 0.2276 0.1666 0.2249 0.0174  0.0180  0.0193  366 ALA   A O     
5487  C  CB    . ALA   A 341 ? 0.2109 0.2018 0.2427 0.0239  0.0390  0.0138  366 ALA   A CB    
5493  N  N     . LEU   A 342 ? 0.2111 0.1627 0.2307 0.0047  0.0237  0.0089  367 LEU   A N     
5494  C  CA    . LEU   A 342 ? 0.2093 0.1701 0.2530 0.0093  0.0159  0.0141  367 LEU   A CA    
5495  C  C     . LEU   A 342 ? 0.2236 0.1675 0.2532 0.0122  0.0233  0.0123  367 LEU   A C     
5496  O  O     . LEU   A 342 ? 0.2161 0.1689 0.2727 0.0065  0.0103  -0.0058 367 LEU   A O     
5497  C  CB    . LEU   A 342 ? 0.2167 0.1905 0.2786 0.0200  0.0049  0.0208  367 LEU   A CB    
5498  C  CG    . LEU   A 342 ? 0.2145 0.1920 0.3254 0.0359  0.0168  -0.0044 367 LEU   A CG    
5499  C  CD1   . LEU   A 342 ? 0.2081 0.2264 0.3432 0.0681  -0.0067 -0.0054 367 LEU   A CD1   
5500  C  CD2   . LEU   A 342 ? 0.2389 0.2136 0.3619 0.0263  0.0430  -0.0219 367 LEU   A CD2   
5512  N  N     . ILE   A 343 ? 0.2236 0.1671 0.2358 0.0232  0.0131  0.0152  368 ILE   A N     
5513  C  CA    . ILE   A 343 ? 0.1887 0.1751 0.2310 0.0157  0.0369  0.0005  368 ILE   A CA    
5514  C  C     . ILE   A 343 ? 0.2292 0.1694 0.2299 0.0278  0.0330  0.0128  368 ILE   A C     
5515  O  O     . ILE   A 343 ? 0.2305 0.1812 0.2384 0.0028  0.0059  0.0157  368 ILE   A O     
5516  C  CB    . ILE   A 343 ? 0.1525 0.2064 0.2404 0.0334  0.0595  0.0069  368 ILE   A CB    
5517  C  CG1   . ILE   A 343 ? 0.2095 0.2095 0.2656 0.0132  0.0368  0.0123  368 ILE   A CG1   
5518  C  CG2   . ILE   A 343 ? 0.2009 0.2153 0.2300 0.0443  0.0732  0.0094  368 ILE   A CG2   
5519  C  CD1   . ILE   A 343 ? 0.2595 0.2038 0.2653 -0.0103 0.0319  -0.0001 368 ILE   A CD1   
5531  N  N     . GLU   A 344 ? 0.2595 0.1687 0.2240 0.0072  0.0349  0.0371  369 GLU   A N     
5532  C  CA    . GLU   A 344 ? 0.2590 0.1641 0.2372 0.0305  0.0094  0.0328  369 GLU   A CA    
5533  C  C     . GLU   A 344 ? 0.2643 0.1815 0.2336 -0.0070 0.0168  0.0219  369 GLU   A C     
5534  O  O     . GLU   A 344 ? 0.2440 0.2174 0.2413 0.0005  0.0160  0.0005  369 GLU   A O     
5535  C  CB    . GLU   A 344 ? 0.2923 0.1585 0.2601 0.0088  0.0038  0.0402  369 GLU   A CB    
5536  C  CG    . GLU   A 344 ? 0.3184 0.1625 0.2997 0.0266  0.0109  0.0393  369 GLU   A CG    
5537  C  CD    . GLU   A 344 ? 0.3524 0.1892 0.3278 0.0108  0.0455  0.0476  369 GLU   A CD    
5538  O  OE1   . GLU   A 344 ? 0.3718 0.2048 0.3314 -0.0092 0.0519  0.0228  369 GLU   A OE1   
5539  O  OE2   . GLU   A 344 ? 0.3508 0.2041 0.3407 0.0283  0.0585  0.0331  369 GLU   A OE2   
5546  N  N     . ASN   A 345 ? 0.2894 0.1787 0.2259 0.0153  0.0348  0.0270  370 ASN   A N     
5547  C  CA    . ASN   A 345 ? 0.3383 0.1800 0.2151 0.0375  0.0560  0.0370  370 ASN   A CA    
5548  C  C     . ASN   A 345 ? 0.2558 0.1859 0.2320 -0.0112 0.0457  0.0123  370 ASN   A C     
5549  O  O     . ASN   A 345 ? 0.2643 0.2073 0.2421 -0.0080 0.0376  0.0063  370 ASN   A O     
5550  C  CB    . ASN   A 345 ? 0.3761 0.1946 0.2370 0.0323  0.0661  0.0491  370 ASN   A CB    
5551  C  CG    . ASN   A 345 ? 0.4541 0.2149 0.2443 0.0232  0.0633  0.0523  370 ASN   A CG    
5552  O  OD1   . ASN   A 345 ? 0.4642 0.2232 0.2488 -0.0148 0.0237  0.0869  370 ASN   A OD1   
5553  N  ND2   . ASN   A 345 ? 0.5119 0.2140 0.2518 0.0647  0.0648  0.0371  370 ASN   A ND2   
5560  N  N     . PRO   A 346 ? 0.2425 0.1848 0.2160 0.0063  0.0468  0.0093  371 PRO   A N     
5561  C  CA    . PRO   A 346 ? 0.2154 0.1818 0.2228 0.0244  0.0166  0.0150  371 PRO   A CA    
5562  C  C     . PRO   A 346 ? 0.2319 0.1868 0.2184 0.0360  0.0086  0.0048  371 PRO   A C     
5563  O  O     . PRO   A 346 ? 0.2677 0.1959 0.2272 0.0360  0.0003  -0.0013 371 PRO   A O     
5564  C  CB    . PRO   A 346 ? 0.1981 0.1958 0.2390 0.0066  -0.0029 0.0216  371 PRO   A CB    
5565  C  CG    . PRO   A 346 ? 0.1976 0.1628 0.2549 0.0160  -0.0028 0.0167  371 PRO   A CG    
5566  C  CD    . PRO   A 346 ? 0.2328 0.1480 0.2484 -0.0097 0.0247  0.0089  371 PRO   A CD    
5574  N  N     . THR   A 347 ? 0.2422 0.1884 0.2150 0.0262  0.0232  0.0136  372 THR   A N     
5575  C  CA    . THR   A 347 ? 0.2362 0.1779 0.2193 -0.0026 0.0260  0.0125  372 THR   A CA    
5576  C  C     . THR   A 347 ? 0.1900 0.1819 0.2095 0.0062  0.0325  0.0012  372 THR   A C     
5577  O  O     . THR   A 347 ? 0.2115 0.1902 0.1987 0.0031  0.0263  -0.0064 372 THR   A O     
5578  C  CB    . THR   A 347 ? 0.2416 0.1928 0.2251 -0.0157 0.0277  0.0067  372 THR   A CB    
5579  O  OG1   . THR   A 347 ? 0.2323 0.1999 0.2263 -0.0155 0.0283  0.0016  372 THR   A OG1   
5580  C  CG2   . THR   A 347 ? 0.2748 0.1920 0.2284 -0.0227 0.0191  0.0108  372 THR   A CG2   
5588  N  N     . PHE   A 348 ? 0.2066 0.1768 0.2113 -0.0045 0.0145  0.0000  373 PHE   A N     
5589  C  CA    . PHE   A 348 ? 0.1597 0.1906 0.2205 0.0106  0.0229  0.0135  373 PHE   A CA    
5590  C  C     . PHE   A 348 ? 0.1828 0.1967 0.2403 0.0116  0.0302  0.0020  373 PHE   A C     
5591  O  O     . PHE   A 348 ? 0.2243 0.1951 0.2538 0.0103  0.0761  0.0098  373 PHE   A O     
5592  C  CB    . PHE   A 348 ? 0.1721 0.2137 0.2206 0.0030  0.0109  0.0104  373 PHE   A CB    
5593  C  CG    . PHE   A 348 ? 0.1708 0.2017 0.2217 0.0290  0.0053  0.0119  373 PHE   A CG    
5594  C  CD1   . PHE   A 348 ? 0.1793 0.1910 0.2217 0.0108  -0.0064 0.0070  373 PHE   A CD1   
5595  C  CD2   . PHE   A 348 ? 0.1337 0.1920 0.2512 -0.0100 0.0107  0.0014  373 PHE   A CD2   
5596  C  CE1   . PHE   A 348 ? 0.2126 0.1834 0.2343 0.0048  -0.0066 0.0162  373 PHE   A CE1   
5597  C  CE2   . PHE   A 348 ? 0.1483 0.2032 0.2634 0.0025  0.0055  0.0058  373 PHE   A CE2   
5598  C  CZ    . PHE   A 348 ? 0.2031 0.1894 0.2574 0.0058  0.0062  -0.0008 373 PHE   A CZ    
5608  N  N     . ASP   A 349 ? 0.1852 0.1913 0.2307 0.0108  -0.0044 0.0024  374 ASP   A N     
5609  C  CA    . ASP   A 349 ? 0.1897 0.2031 0.2536 0.0535  0.0016  0.0049  374 ASP   A CA    
5610  C  C     . ASP   A 349 ? 0.1644 0.1978 0.2482 0.0114  0.0274  -0.0128 374 ASP   A C     
5611  O  O     . ASP   A 349 ? 0.2035 0.2199 0.2744 0.0179  0.0360  -0.0077 374 ASP   A O     
5612  C  CB    . ASP   A 349 ? 0.2581 0.2271 0.2895 0.0430  -0.0021 0.0105  374 ASP   A CB    
5613  C  CG    . ASP   A 349 ? 0.3054 0.2591 0.3218 0.0009  0.0187  0.0081  374 ASP   A CG    
5614  O  OD1   . ASP   A 349 ? 0.2927 0.2547 0.3376 -0.0149 0.0100  0.0074  374 ASP   A OD1   
5615  O  OD2   . ASP   A 349 ? 0.2889 0.3016 0.3311 -0.0025 0.0384  0.0095  374 ASP   A OD2   
5620  N  N     . SER   A 350 ? 0.1788 0.1938 0.2362 -0.0108 0.0274  -0.0195 375 SER   A N     
5621  C  CA    . SER   A 350 ? 0.2016 0.1919 0.2256 0.0101  0.0170  0.0153  375 SER   A CA    
5622  C  C     . SER   A 350 ? 0.1892 0.1652 0.2172 0.0361  -0.0118 -0.0019 375 SER   A C     
5623  O  O     . SER   A 350 ? 0.2034 0.1682 0.2039 0.0017  -0.0082 0.0071  375 SER   A O     
5624  C  CB    . SER   A 350 ? 0.2581 0.2443 0.2552 0.0027  0.0430  0.0350  375 SER   A CB    
5625  O  OG    . SER   A 350 ? 0.2726 0.2783 0.3096 0.0037  0.0231  0.0579  375 SER   A OG    
5631  N  N     . GLN   A 351 ? 0.2481 0.1750 0.2221 0.0073  -0.0235 -0.0148 376 GLN   A N     
5632  C  CA    . GLN   A 351 ? 0.2580 0.1755 0.2114 0.0157  -0.0302 -0.0049 376 GLN   A CA    
5633  C  C     . GLN   A 351 ? 0.2162 0.1792 0.2142 0.0142  -0.0341 -0.0025 376 GLN   A C     
5634  O  O     . GLN   A 351 ? 0.2048 0.2258 0.2192 0.0175  -0.0382 -0.0165 376 GLN   A O     
5635  C  CB    . GLN   A 351 ? 0.3192 0.1831 0.2097 0.0055  -0.0146 -0.0043 376 GLN   A CB    
5636  C  CG    . GLN   A 351 ? 0.3357 0.1858 0.2251 0.0141  -0.0260 0.0030  376 GLN   A CG    
5637  C  CD    . GLN   A 351 ? 0.3334 0.2076 0.2351 -0.0031 -0.0369 0.0004  376 GLN   A CD    
5638  O  OE1   . GLN   A 351 ? 0.3531 0.2488 0.2340 -0.0191 -0.0336 0.0248  376 GLN   A OE1   
5639  N  NE2   . GLN   A 351 ? 0.3313 0.1988 0.2556 0.0098  -0.0783 -0.0019 376 GLN   A NE2   
5648  N  N     . THR   A 352 ? 0.2086 0.1727 0.2198 -0.0128 -0.0385 -0.0085 377 THR   A N     
5649  C  CA    . THR   A 352 ? 0.1748 0.1803 0.2291 -0.0054 -0.0172 0.0087  377 THR   A CA    
5650  C  C     . THR   A 352 ? 0.1987 0.1865 0.2102 -0.0141 -0.0034 -0.0117 377 THR   A C     
5651  O  O     . THR   A 352 ? 0.2035 0.2129 0.2166 -0.0119 0.0153  -0.0257 377 THR   A O     
5652  C  CB    . THR   A 352 ? 0.1689 0.2026 0.2546 -0.0197 -0.0321 -0.0016 377 THR   A CB    
5653  O  OG1   . THR   A 352 ? 0.1875 0.2333 0.2829 -0.0107 -0.0128 0.0266  377 THR   A OG1   
5654  C  CG2   . THR   A 352 ? 0.1929 0.2096 0.2732 -0.0161 -0.0379 -0.0020 377 THR   A CG2   
5662  N  N     . LYS   A 353 ? 0.1866 0.1870 0.2012 -0.0083 -0.0102 -0.0101 378 LYS   A N     
5663  C  CA    . LYS   A 353 ? 0.1545 0.1931 0.1981 0.0084  -0.0115 -0.0120 378 LYS   A CA    
5664  C  C     . LYS   A 353 ? 0.1364 0.1881 0.2150 -0.0003 0.0091  -0.0130 378 LYS   A C     
5665  O  O     . LYS   A 353 ? 0.1634 0.2193 0.2288 0.0201  0.0201  -0.0062 378 LYS   A O     
5666  C  CB    . LYS   A 353 ? 0.1713 0.2083 0.2090 0.0143  -0.0428 0.0028  378 LYS   A CB    
5667  C  CG    . LYS   A 353 ? 0.2490 0.1949 0.2062 0.0440  -0.0549 0.0408  378 LYS   A CG    
5668  C  CD    . LYS   A 353 ? 0.3437 0.2182 0.2205 0.0889  -0.0558 0.0389  378 LYS   A CD    
5669  C  CE    . LYS   A 353 ? 0.4602 0.2524 0.2437 0.0933  -0.0835 0.0733  378 LYS   A CE    
5670  N  NZ    . LYS   A 353 ? 0.4949 0.2357 0.2594 0.0446  -0.0902 0.0507  378 LYS   A NZ    
5684  N  N     . GLU   A 354 ? 0.1541 0.1952 0.2163 -0.0078 -0.0149 -0.0250 379 GLU   A N     
5685  C  CA    . GLU   A 354 ? 0.1307 0.2120 0.2214 0.0150  -0.0002 0.0027  379 GLU   A CA    
5686  C  C     . GLU   A 354 ? 0.1180 0.1939 0.2038 0.0053  0.0195  0.0129  379 GLU   A C     
5687  O  O     . GLU   A 354 ? 0.1489 0.2078 0.1974 -0.0067 0.0136  0.0120  379 GLU   A O     
5688  C  CB    . GLU   A 354 ? 0.1908 0.2188 0.2573 0.0149  -0.0243 -0.0085 379 GLU   A CB    
5689  C  CG    . GLU   A 354 ? 0.2357 0.2045 0.3357 -0.0360 -0.0516 -0.0050 379 GLU   A CG    
5690  C  CD    . GLU   A 354 ? 0.3320 0.2699 0.4277 -0.0271 -0.0895 -0.0183 379 GLU   A CD    
5691  O  OE1   . GLU   A 354 ? 0.3792 0.3019 0.4881 0.0272  -0.1678 -0.0071 379 GLU   A OE1   
5692  O  OE2   . GLU   A 354 ? 0.3661 0.2830 0.4422 -0.0651 -0.0470 -0.0253 379 GLU   A OE2   
5699  N  N     . ASN   A 355 ? 0.1315 0.1828 0.2118 -0.0187 0.0007  0.0101  380 ASN   A N     
5700  C  CA    . ASN   A 355 ? 0.1498 0.1698 0.1955 0.0149  -0.0022 0.0078  380 ASN   A CA    
5701  C  C     . ASN   A 355 ? 0.1548 0.1829 0.1874 0.0110  0.0140  0.0012  380 ASN   A C     
5702  O  O     . ASN   A 355 ? 0.1664 0.1833 0.1965 -0.0117 0.0255  -0.0045 380 ASN   A O     
5703  C  CB    . ASN   A 355 ? 0.1600 0.1941 0.2086 0.0046  -0.0031 0.0066  380 ASN   A CB    
5704  C  CG    . ASN   A 355 ? 0.1706 0.2823 0.2565 -0.0072 -0.0145 -0.0357 380 ASN   A CG    
5705  O  OD1   . ASN   A 355 ? 0.1999 0.3164 0.3048 0.0229  -0.0379 -0.0598 380 ASN   A OD1   
5706  N  ND2   . ASN   A 355 ? 0.2303 0.3141 0.2679 -0.0620 -0.0147 -0.0185 380 ASN   A ND2   
5713  N  N     . MET   A 356 ? 0.1431 0.1771 0.1817 -0.0081 0.0359  0.0042  381 MET   A N     
5714  C  CA    . MET   A 356 ? 0.1665 0.1821 0.2017 0.0184  0.0215  0.0170  381 MET   A CA    
5715  C  C     . MET   A 356 ? 0.1793 0.1903 0.2004 -0.0137 0.0218  0.0122  381 MET   A C     
5716  O  O     . MET   A 356 ? 0.1889 0.2205 0.1964 -0.0449 0.0188  -0.0069 381 MET   A O     
5717  C  CB    . MET   A 356 ? 0.1851 0.1888 0.2066 0.0065  0.0296  0.0186  381 MET   A CB    
5718  C  CG    . MET   A 356 ? 0.2233 0.1927 0.2216 -0.0190 0.0172  0.0056  381 MET   A CG    
5719  S  SD    . MET   A 356 ? 0.2150 0.1958 0.2305 -0.0089 0.0246  0.0109  381 MET   A SD    
5720  C  CE    . MET   A 356 ? 0.2264 0.2185 0.2480 -0.0194 -0.0125 -0.0006 381 MET   A CE    
5730  N  N     . THR   A 357 ? 0.1392 0.1909 0.2063 0.0106  0.0088  0.0224  382 THR   A N     
5731  C  CA    . THR   A 357 ? 0.1581 0.2047 0.2156 0.0068  0.0256  -0.0048 382 THR   A CA    
5732  C  C     . THR   A 357 ? 0.1560 0.2019 0.2293 0.0002  0.0475  -0.0097 382 THR   A C     
5733  O  O     . THR   A 357 ? 0.1856 0.2118 0.2493 -0.0252 0.0457  -0.0091 382 THR   A O     
5734  C  CB    . THR   A 357 ? 0.1807 0.2092 0.2077 -0.0152 0.0367  -0.0109 382 THR   A CB    
5735  O  OG1   . THR   A 357 ? 0.2073 0.2407 0.2190 0.0089  0.0483  -0.0259 382 THR   A OG1   
5736  C  CG2   . THR   A 357 ? 0.2163 0.1968 0.1865 0.0215  0.0360  0.0080  382 THR   A CG2   
5744  N  N     . LEU   A 358 ? 0.1612 0.1905 0.2497 0.0040  0.0459  0.0126  383 LEU   A N     
5745  C  CA    . LEU   A 358 ? 0.1830 0.1890 0.2578 0.0001  0.0331  0.0134  383 LEU   A CA    
5746  C  C     . LEU   A 358 ? 0.1849 0.2068 0.2679 -0.0088 0.0296  0.0040  383 LEU   A C     
5747  O  O     . LEU   A 358 ? 0.2072 0.2120 0.2587 -0.0149 0.0324  0.0080  383 LEU   A O     
5748  C  CB    . LEU   A 358 ? 0.2143 0.2048 0.2408 0.0082  0.0167  0.0205  383 LEU   A CB    
5749  C  CG    . LEU   A 358 ? 0.2181 0.2140 0.2532 0.0069  0.0116  0.0360  383 LEU   A CG    
5750  C  CD1   . LEU   A 358 ? 0.2662 0.2743 0.2591 0.0151  0.0570  0.0586  383 LEU   A CD1   
5751  C  CD2   . LEU   A 358 ? 0.1970 0.2017 0.2677 0.0103  -0.0213 0.0458  383 LEU   A CD2   
5763  N  N     . GLN   A 359 ? 0.1768 0.2046 0.2808 -0.0206 0.0490  -0.0038 384 GLN   A N     
5764  C  CA    A GLN   A 359 ? 0.1753 0.2162 0.3037 -0.0236 0.0352  -0.0278 384 GLN   A CA    
5765  C  CA    B GLN   A 359 ? 0.1643 0.2205 0.2995 -0.0282 0.0237  -0.0305 384 GLN   A CA    
5766  C  C     . GLN   A 359 ? 0.1662 0.2139 0.3014 -0.0237 0.0218  -0.0270 384 GLN   A C     
5767  O  O     . GLN   A 359 ? 0.2190 0.1936 0.2934 -0.0288 0.0360  -0.0213 384 GLN   A O     
5768  C  CB    A GLN   A 359 ? 0.1953 0.2632 0.3408 0.0024  0.0381  -0.0467 384 GLN   A CB    
5769  C  CB    B GLN   A 359 ? 0.1612 0.2692 0.3249 -0.0192 0.0045  -0.0569 384 GLN   A CB    
5770  C  CG    A GLN   A 359 ? 0.2199 0.2953 0.3658 0.0156  0.0673  -0.0719 384 GLN   A CG    
5771  C  CG    B GLN   A 359 ? 0.1721 0.3024 0.3401 -0.0185 0.0134  -0.0826 384 GLN   A CG    
5772  C  CD    A GLN   A 359 ? 0.2205 0.3251 0.3897 0.0067  0.0627  -0.0823 384 GLN   A CD    
5773  C  CD    B GLN   A 359 ? 0.1509 0.3333 0.3483 -0.0389 0.0214  -0.0936 384 GLN   A CD    
5774  O  OE1   A GLN   A 359 ? 0.1979 0.3308 0.4013 -0.0198 0.0552  -0.0909 384 GLN   A OE1   
5775  O  OE1   B GLN   A 359 ? 0.1912 0.3428 0.3546 -0.0325 0.0200  -0.0967 384 GLN   A OE1   
5776  N  NE2   A GLN   A 359 ? 0.2271 0.3372 0.3977 -0.0106 0.0903  -0.0751 384 GLN   A NE2   
5777  N  NE2   B GLN   A 359 ? 0.1527 0.3541 0.3519 -0.0260 0.0384  -0.0888 384 GLN   A NE2   
5792  N  N     . PRO   A 360 ? 0.1841 0.2130 0.3167 -0.0069 0.0044  -0.0229 385 PRO   A N     
5793  C  CA    . PRO   A 360 ? 0.2221 0.2288 0.3323 -0.0021 0.0090  -0.0375 385 PRO   A CA    
5794  C  C     . PRO   A 360 ? 0.1937 0.1877 0.3606 -0.0232 0.0172  -0.0432 385 PRO   A C     
5795  O  O     . PRO   A 360 ? 0.2235 0.2044 0.3605 -0.0045 0.0087  -0.0365 385 PRO   A O     
5796  C  CB    . PRO   A 360 ? 0.2666 0.2548 0.3265 0.0237  0.0088  -0.0573 385 PRO   A CB    
5797  C  CG    . PRO   A 360 ? 0.2431 0.2520 0.3230 0.0221  -0.0060 -0.0533 385 PRO   A CG    
5798  C  CD    . PRO   A 360 ? 0.2197 0.2326 0.3227 -0.0086 0.0051  -0.0253 385 PRO   A CD    
5806  N  N     . LYS   A 361 ? 0.2249 0.2024 0.4006 -0.0619 0.0162  -0.0213 386 LYS   A N     
5807  C  CA    . LYS   A 361 ? 0.2450 0.2541 0.4450 -0.0587 0.0525  0.0180  386 LYS   A CA    
5808  C  C     . LYS   A 361 ? 0.2231 0.2215 0.4259 -0.0720 0.0461  0.0229  386 LYS   A C     
5809  O  O     . LYS   A 361 ? 0.2673 0.2377 0.4588 -0.0514 0.0373  0.0223  386 LYS   A O     
5810  C  CB    . LYS   A 361 ? 0.2462 0.3141 0.4953 -0.0676 0.0662  0.0405  386 LYS   A CB    
5811  C  CG    . LYS   A 361 ? 0.1890 0.3989 0.5309 -0.0409 0.0807  0.0675  386 LYS   A CG    
5812  C  CD    . LYS   A 361 ? 0.2539 0.4882 0.5690 -0.0378 0.0525  0.0844  386 LYS   A CD    
5813  C  CE    . LYS   A 361 ? 0.3801 0.5833 0.5982 -0.0487 0.0716  0.0971  386 LYS   A CE    
5814  N  NZ    . LYS   A 361 ? 0.4687 0.6441 0.6213 -0.0349 0.0743  0.0974  386 LYS   A NZ    
5828  N  N     . SER   A 362 ? 0.2150 0.2063 0.3865 -0.0206 0.0525  0.0087  387 SER   A N     
5829  C  CA    . SER   A 362 ? 0.2706 0.2152 0.3574 -0.0086 0.0683  0.0075  387 SER   A CA    
5830  C  C     . SER   A 362 ? 0.2749 0.2059 0.3219 -0.0024 0.0653  0.0106  387 SER   A C     
5831  O  O     . SER   A 362 ? 0.2992 0.2260 0.3025 -0.0120 0.0574  -0.0117 387 SER   A O     
5832  C  CB    . SER   A 362 ? 0.2608 0.2416 0.3709 -0.0341 0.0979  0.0060  387 SER   A CB    
5833  O  OG    . SER   A 362 ? 0.2875 0.2908 0.4003 -0.0226 0.0983  -0.0038 387 SER   A OG    
5839  N  N     . PHE   A 363 ? 0.2287 0.2110 0.3009 -0.0225 0.0736  0.0121  388 PHE   A N     
5840  C  CA    . PHE   A 363 ? 0.1962 0.2069 0.3002 0.0241  0.0297  -0.0013 388 PHE   A CA    
5841  C  C     . PHE   A 363 ? 0.2474 0.1944 0.3002 0.0151  0.0272  0.0104  388 PHE   A C     
5842  O  O     . PHE   A 363 ? 0.2742 0.2010 0.2974 0.0008  0.0171  0.0030  388 PHE   A O     
5843  C  CB    . PHE   A 363 ? 0.1961 0.2156 0.2911 -0.0011 0.0304  -0.0209 388 PHE   A CB    
5844  C  CG    . PHE   A 363 ? 0.1714 0.2130 0.2880 -0.0029 0.0267  -0.0132 388 PHE   A CG    
5845  C  CD1   . PHE   A 363 ? 0.1713 0.2049 0.2960 0.0008  0.0368  0.0045  388 PHE   A CD1   
5846  C  CD2   . PHE   A 363 ? 0.1704 0.2158 0.2946 0.0100  0.0246  -0.0191 388 PHE   A CD2   
5847  C  CE1   . PHE   A 363 ? 0.1525 0.2433 0.2918 -0.0024 0.0404  0.0037  388 PHE   A CE1   
5848  C  CE2   . PHE   A 363 ? 0.1807 0.2531 0.2905 0.0356  0.0504  0.0074  388 PHE   A CE2   
5849  C  CZ    . PHE   A 363 ? 0.1282 0.2397 0.2895 0.0359  0.0682  0.0193  388 PHE   A CZ    
5859  N  N     . GLY   A 364 ? 0.2358 0.1869 0.3169 -0.0055 0.0216  0.0269  389 GLY   A N     
5860  C  CA    . GLY   A 364 ? 0.2589 0.1839 0.3337 0.0372  0.0194  0.0307  389 GLY   A CA    
5861  C  C     . GLY   A 364 ? 0.2529 0.1758 0.3532 0.0298  0.0240  0.0138  389 GLY   A C     
5862  O  O     . GLY   A 364 ? 0.2888 0.2152 0.3728 0.0342  0.0271  0.0235  389 GLY   A O     
5866  N  N     . SER   A 365 ? 0.2544 0.1669 0.3591 0.0086  0.0193  -0.0046 390 SER   A N     
5867  C  CA    . SER   A 365 ? 0.2644 0.1945 0.3671 0.0221  0.0202  -0.0156 390 SER   A CA    
5868  C  C     . SER   A 365 ? 0.2663 0.2134 0.3609 0.0067  0.0280  -0.0454 390 SER   A C     
5869  O  O     . SER   A 365 ? 0.2508 0.2440 0.3518 0.0021  -0.0027 -0.0433 390 SER   A O     
5870  C  CB    . SER   A 365 ? 0.2903 0.1839 0.3788 -0.0019 0.0414  -0.0182 390 SER   A CB    
5871  O  OG    . SER   A 365 ? 0.2922 0.2011 0.3793 -0.0456 0.0496  -0.0073 390 SER   A OG    
5877  N  N     . THR   A 366 ? 0.2756 0.2353 0.3773 0.0288  0.0694  -0.0514 391 THR   A N     
5878  C  CA    . THR   A 366 ? 0.2844 0.2371 0.3844 -0.0196 0.0790  -0.0745 391 THR   A CA    
5879  C  C     . THR   A 366 ? 0.2908 0.2726 0.3706 -0.0104 0.0856  -0.0846 391 THR   A C     
5880  O  O     . THR   A 366 ? 0.3028 0.3047 0.3755 0.0036  0.0999  -0.0758 391 THR   A O     
5881  C  CB    . THR   A 366 ? 0.3458 0.2604 0.4176 -0.0248 0.0568  -0.0730 391 THR   A CB    
5882  O  OG1   . THR   A 366 ? 0.3864 0.2807 0.4446 -0.0170 0.0436  -0.0817 391 THR   A OG1   
5883  C  CG2   . THR   A 366 ? 0.3822 0.2868 0.4211 -0.0413 0.0615  -0.0428 391 THR   A CG2   
5891  N  N     . CYS   A 367 ? 0.2903 0.2967 0.3574 -0.0227 0.0920  -0.0924 392 CYS   A N     
5892  C  CA    . CYS   A 367 ? 0.3285 0.2934 0.3432 -0.0434 0.0863  -0.1097 392 CYS   A CA    
5893  C  C     . CYS   A 367 ? 0.4147 0.3117 0.3654 -0.0669 0.0577  -0.1230 392 CYS   A C     
5894  O  O     . CYS   A 367 ? 0.4246 0.3321 0.3921 -0.0403 0.0295  -0.1227 392 CYS   A O     
5895  C  CB    . CYS   A 367 ? 0.3136 0.3083 0.3315 -0.0407 0.0814  -0.0788 392 CYS   A CB    
5896  S  SG    . CYS   A 367 ? 0.3162 0.3248 0.3299 -0.0224 0.0580  -0.0701 392 CYS   A SG    
5902  N  N     . GLN   A 368 ? 0.4936 0.3439 0.3808 -0.1120 0.0732  -0.1216 393 GLN   A N     
5903  C  CA    A GLN   A 368 ? 0.5330 0.3414 0.3865 -0.1275 0.0750  -0.1324 393 GLN   A CA    
5904  C  CA    B GLN   A 368 ? 0.5274 0.3419 0.3902 -0.1166 0.0742  -0.1363 393 GLN   A CA    
5905  C  C     . GLN   A 368 ? 0.5345 0.3250 0.3908 -0.1019 0.0920  -0.1322 393 GLN   A C     
5906  O  O     . GLN   A 368 ? 0.5946 0.3170 0.4014 -0.1127 0.0982  -0.1003 393 GLN   A O     
5907  C  CB    A GLN   A 368 ? 0.5721 0.3769 0.4001 -0.1542 0.0554  -0.1214 393 GLN   A CB    
5908  C  CB    B GLN   A 368 ? 0.5541 0.3752 0.4108 -0.1221 0.0541  -0.1344 393 GLN   A CB    
5909  C  CG    A GLN   A 368 ? 0.6092 0.4253 0.4245 -0.1696 0.0283  -0.1153 393 GLN   A CG    
5910  C  CG    B GLN   A 368 ? 0.5748 0.4142 0.4420 -0.1220 0.0316  -0.1347 393 GLN   A CG    
5911  C  CD    A GLN   A 368 ? 0.6607 0.5058 0.4478 -0.1557 0.0092  -0.1112 393 GLN   A CD    
5912  C  CD    B GLN   A 368 ? 0.6068 0.4519 0.4748 -0.1401 0.0227  -0.1353 393 GLN   A CD    
5913  O  OE1   A GLN   A 368 ? 0.6921 0.5587 0.4677 -0.1497 0.0051  -0.1121 393 GLN   A OE1   
5914  O  OE1   B GLN   A 368 ? 0.6056 0.4355 0.4881 -0.1430 0.0299  -0.1282 393 GLN   A OE1   
5915  N  NE2   A GLN   A 368 ? 0.6785 0.5202 0.4499 -0.1422 -0.0052 -0.1051 393 GLN   A NE2   
5916  N  NE2   B GLN   A 368 ? 0.6163 0.4856 0.4888 -0.1481 0.0268  -0.1307 393 GLN   A NE2   
5932  N  N     . LEU   A 369 ? 0.5070 0.3011 0.3798 -0.0854 0.1130  -0.1466 394 LEU   A N     
5933  C  CA    . LEU   A 369 ? 0.4868 0.3194 0.3924 -0.0832 0.1202  -0.1319 394 LEU   A CA    
5934  C  C     . LEU   A 369 ? 0.5293 0.3507 0.4000 -0.1053 0.1083  -0.1646 394 LEU   A C     
5935  O  O     . LEU   A 369 ? 0.5362 0.3711 0.4173 -0.1235 0.0758  -0.1806 394 LEU   A O     
5936  C  CB    . LEU   A 369 ? 0.4822 0.3073 0.3885 -0.0906 0.1195  -0.1154 394 LEU   A CB    
5937  C  CG    . LEU   A 369 ? 0.4928 0.3089 0.3797 -0.1017 0.1093  -0.0939 394 LEU   A CG    
5938  C  CD1   . LEU   A 369 ? 0.4816 0.3370 0.3871 -0.0862 0.1091  -0.0908 394 LEU   A CD1   
5939  C  CD2   . LEU   A 369 ? 0.5344 0.3186 0.3776 -0.0929 0.0775  -0.0915 394 LEU   A CD2   
5951  N  N     . SER   A 370 ? 0.5883 0.3480 0.3953 -0.0789 0.1398  -0.1768 395 SER   A N     
5952  C  CA    . SER   A 370 ? 0.6598 0.3629 0.4083 -0.0679 0.1379  -0.1557 395 SER   A CA    
5953  C  C     . SER   A 370 ? 0.7105 0.3732 0.4213 -0.0788 0.1338  -0.1841 395 SER   A C     
5954  O  O     . SER   A 370 ? 0.6996 0.3686 0.4052 -0.0608 0.1330  -0.1759 395 SER   A O     
5955  C  CB    . SER   A 370 ? 0.6655 0.3619 0.4030 -0.0386 0.1359  -0.1181 395 SER   A CB    
5956  O  OG    . SER   A 370 ? 0.6719 0.3790 0.3946 -0.0135 0.1213  -0.0820 395 SER   A OG    
5962  N  N     . GLU   A 371 ? 0.7532 0.4015 0.4507 -0.0926 0.1417  -0.2046 396 GLU   A N     
5963  C  CA    . GLU   A 371 ? 0.7732 0.4276 0.4778 -0.1225 0.1271  -0.2233 396 GLU   A CA    
5964  C  C     . GLU   A 371 ? 0.7473 0.4403 0.4636 -0.0814 0.1286  -0.2317 396 GLU   A C     
5965  O  O     . GLU   A 371 ? 0.7669 0.4802 0.4576 -0.0725 0.1074  -0.2311 396 GLU   A O     
5966  C  CB    . GLU   A 371 ? 0.8254 0.4830 0.5236 -0.1450 0.1336  -0.2090 396 GLU   A CB    
5967  C  CG    . GLU   A 371 ? 0.8758 0.5356 0.5750 -0.1578 0.1219  -0.1859 396 GLU   A CG    
5968  C  CD    . GLU   A 371 ? 0.9167 0.5855 0.6208 -0.1491 0.1160  -0.1525 396 GLU   A CD    
5969  O  OE1   . GLU   A 371 ? 0.9479 0.6024 0.6376 -0.1385 0.1001  -0.1412 396 GLU   A OE1   
5970  O  OE2   . GLU   A 371 ? 0.9266 0.6078 0.6434 -0.1471 0.1181  -0.1370 396 GLU   A OE2   
5977  N  N     . LYS   A 372 ? 0.7214 0.4276 0.4687 -0.0534 0.1529  -0.2245 397 LYS   A N     
5978  C  CA    . LYS   A 372 ? 0.7105 0.4313 0.4835 -0.0162 0.1714  -0.1934 397 LYS   A CA    
5979  C  C     . LYS   A 372 ? 0.6881 0.4025 0.4421 -0.0066 0.1639  -0.1859 397 LYS   A C     
5980  O  O     . LYS   A 372 ? 0.7114 0.4338 0.4402 0.0048  0.1607  -0.1888 397 LYS   A O     
5981  C  CB    . LYS   A 372 ? 0.6979 0.4706 0.5333 0.0371  0.1899  -0.1694 397 LYS   A CB    
5982  C  CG    . LYS   A 372 ? 0.6891 0.5332 0.5776 0.0835  0.1923  -0.1372 397 LYS   A CG    
5983  C  CD    . LYS   A 372 ? 0.7019 0.5982 0.6180 0.0985  0.1719  -0.1039 397 LYS   A CD    
5984  C  CE    . LYS   A 372 ? 0.7193 0.6394 0.6529 0.1111  0.1452  -0.0811 397 LYS   A CE    
5985  N  NZ    . LYS   A 372 ? 0.7301 0.6594 0.6736 0.1227  0.1347  -0.0786 397 LYS   A NZ    
5999  N  N     . PHE   A 373 ? 0.6471 0.3533 0.4098 -0.0056 0.1480  -0.1742 398 PHE   A N     
6000  C  CA    . PHE   A 373 ? 0.5815 0.3321 0.3738 -0.0299 0.1312  -0.1573 398 PHE   A CA    
6001  C  C     . PHE   A 373 ? 0.5847 0.3670 0.3566 -0.0392 0.1245  -0.1584 398 PHE   A C     
6002  O  O     . PHE   A 373 ? 0.5693 0.3906 0.3580 -0.0186 0.1219  -0.1348 398 PHE   A O     
6003  C  CB    . PHE   A 373 ? 0.5306 0.3209 0.3554 -0.0382 0.1123  -0.1218 398 PHE   A CB    
6004  C  CG    . PHE   A 373 ? 0.4571 0.3148 0.3284 -0.0448 0.0904  -0.1113 398 PHE   A CG    
6005  C  CD1   . PHE   A 373 ? 0.4249 0.3308 0.3175 -0.0692 0.1168  -0.1049 398 PHE   A CD1   
6006  C  CD2   . PHE   A 373 ? 0.4199 0.3104 0.3172 -0.0396 0.0847  -0.1012 398 PHE   A CD2   
6007  C  CE1   . PHE   A 373 ? 0.4068 0.3086 0.3031 -0.0716 0.1048  -0.1031 398 PHE   A CE1   
6008  C  CE2   . PHE   A 373 ? 0.3960 0.3081 0.3031 -0.0662 0.0843  -0.0926 398 PHE   A CE2   
6009  C  CZ    . PHE   A 373 ? 0.4044 0.3093 0.3022 -0.0796 0.0967  -0.0872 398 PHE   A CZ    
6019  N  N     . ILE   A 374 ? 0.6054 0.4015 0.3542 -0.0767 0.0994  -0.1689 399 ILE   A N     
6020  C  CA    . ILE   A 374 ? 0.6317 0.4530 0.3631 -0.0722 0.0785  -0.1707 399 ILE   A CA    
6021  C  C     . ILE   A 374 ? 0.6539 0.4896 0.3790 -0.0521 0.0772  -0.1941 399 ILE   A C     
6022  O  O     . ILE   A 374 ? 0.6506 0.5008 0.3843 -0.0161 0.0669  -0.1998 399 ILE   A O     
6023  C  CB    . ILE   A 374 ? 0.6247 0.4744 0.3586 -0.0855 0.0729  -0.1426 399 ILE   A CB    
6024  C  CG1   . ILE   A 374 ? 0.5936 0.4838 0.3438 -0.0827 0.0829  -0.1577 399 ILE   A CG1   
6025  C  CG2   . ILE   A 374 ? 0.6491 0.4719 0.3659 -0.0591 0.0616  -0.1189 399 ILE   A CG2   
6026  C  CD1   . ILE   A 374 ? 0.5861 0.5055 0.3391 -0.0548 0.0840  -0.1616 399 ILE   A CD1   
6038  N  N     . LYS   A 375 ? 0.6831 0.5260 0.3923 -0.0560 0.0960  -0.2045 400 LYS   A N     
6039  C  CA    . LYS   A 375 ? 0.7298 0.5602 0.4082 -0.0404 0.1015  -0.2070 400 LYS   A CA    
6040  C  C     . LYS   A 375 ? 0.7306 0.5558 0.3836 -0.0141 0.1100  -0.2057 400 LYS   A C     
6041  O  O     . LYS   A 375 ? 0.7571 0.5711 0.3861 -0.0304 0.0883  -0.2043 400 LYS   A O     
6042  C  CB    . LYS   A 375 ? 0.7982 0.5989 0.4500 -0.0303 0.0850  -0.2070 400 LYS   A CB    
6043  C  CG    . LYS   A 375 ? 0.8651 0.6480 0.4868 -0.0126 0.0526  -0.2021 400 LYS   A CG    
6044  C  CD    . LYS   A 375 ? 0.9151 0.6832 0.5166 -0.0053 0.0199  -0.1988 400 LYS   A CD    
6045  C  CE    . LYS   A 375 ? 0.9458 0.7289 0.5446 -0.0151 -0.0137 -0.1724 400 LYS   A CE    
6046  N  NZ    . LYS   A 375 ? 0.9671 0.7524 0.5623 -0.0170 -0.0305 -0.1540 400 LYS   A NZ    
6060  N  N     . ALA   A 376 ? 0.6964 0.5409 0.3657 0.0180  0.1345  -0.1888 401 ALA   A N     
6061  C  CA    . ALA   A 376 ? 0.6839 0.5115 0.3602 0.0433  0.1316  -0.1556 401 ALA   A CA    
6062  C  C     . ALA   A 376 ? 0.6648 0.5035 0.3469 0.0665  0.1317  -0.1291 401 ALA   A C     
6063  O  O     . ALA   A 376 ? 0.6769 0.5114 0.3537 0.0724  0.1275  -0.1046 401 ALA   A O     
6064  C  CB    . ALA   A 376 ? 0.6834 0.4977 0.3617 0.0517  0.1242  -0.1462 401 ALA   A CB    
6070  N  N     . ALA   A 377 ? 0.6342 0.4910 0.3292 0.0827  0.1302  -0.1316 402 ALA   A N     
6071  C  CA    . ALA   A 377 ? 0.6354 0.5075 0.3253 0.0935  0.1151  -0.1214 402 ALA   A CA    
6072  C  C     . ALA   A 377 ? 0.6866 0.5712 0.3381 0.1100  0.0822  -0.1060 402 ALA   A C     
6073  O  O     . ALA   A 377 ? 0.7094 0.5895 0.3527 0.1025  0.0618  -0.0816 402 ALA   A O     
6074  C  CB    . ALA   A 377 ? 0.6141 0.4713 0.3135 0.0894  0.1368  -0.1418 402 ALA   A CB    
6080  N  N     . ILE   A 378 ? 0.7168 0.6212 0.3401 0.1324  0.0724  -0.1247 403 ILE   A N     
6081  C  CA    . ILE   A 378 ? 0.7555 0.6964 0.3647 0.1424  0.0570  -0.1021 403 ILE   A CA    
6082  C  C     . ILE   A 378 ? 0.7945 0.7525 0.3781 0.1833  0.0838  -0.0691 403 ILE   A C     
6083  O  O     . ILE   A 378 ? 0.8131 0.7784 0.3772 0.2065  0.0606  -0.0727 403 ILE   A O     
6084  C  CB    . ILE   A 378 ? 0.7669 0.7158 0.3813 0.1081  0.0058  -0.1108 403 ILE   A CB    
6085  C  CG1   . ILE   A 378 ? 0.7430 0.7138 0.3969 0.1097  -0.0037 -0.1165 403 ILE   A CG1   
6086  C  CG2   . ILE   A 378 ? 0.7845 0.7268 0.3961 0.1035  -0.0240 -0.1120 403 ILE   A CG2   
6087  C  CD1   . ILE   A 378 ? 0.7329 0.7173 0.4050 0.1141  -0.0109 -0.1149 403 ILE   A CD1   
6099  N  N     . GLY   A 379 ? 0.8063 0.7783 0.4052 0.2042  0.1372  -0.0396 404 GLY   A N     
6100  C  CA    . GLY   A 379 ? 0.8441 0.8029 0.4396 0.1793  0.1754  -0.0057 404 GLY   A CA    
6101  C  C     . GLY   A 379 ? 0.8886 0.8280 0.4770 0.1594  0.2041  0.0149  404 GLY   A C     
6102  O  O     . GLY   A 379 ? 0.8943 0.8450 0.4839 0.1701  0.2141  0.0154  404 GLY   A O     
6106  N  N     . CYS   A 380 ? 0.9285 0.8319 0.5082 0.1361  0.2118  0.0330  405 CYS   A N     
6107  C  CA    . CYS   A 380 ? 0.9683 0.8344 0.5395 0.1033  0.2121  0.0589  405 CYS   A CA    
6108  C  C     . CYS   A 380 ? 0.9695 0.8373 0.5513 0.1078  0.2350  0.0920  405 CYS   A C     
6109  O  O     . CYS   A 380 ? 0.9850 0.8285 0.5605 0.1006  0.2365  0.1093  405 CYS   A O     
6110  C  CB    . CYS   A 380 ? 1.0008 0.8380 0.5544 0.0704  0.1881  0.0391  405 CYS   A CB    
6111  S  SG    . CYS   A 380 ? 1.0170 0.8485 0.5696 0.0535  0.1662  0.0168  405 CYS   A SG    
6117  N  N     . GLY   A 381 ? 0.9425 0.8334 0.5441 0.1287  0.2519  0.1028  406 GLY   A N     
6118  C  CA    . GLY   A 381 ? 0.9278 0.8203 0.5303 0.1473  0.2604  0.1049  406 GLY   A CA    
6119  C  C     . GLY   A 381 ? 0.9315 0.7954 0.5147 0.1519  0.2490  0.0994  406 GLY   A C     
6120  O  O     . GLY   A 381 ? 0.9404 0.7992 0.5214 0.1490  0.2355  0.1167  406 GLY   A O     
6124  N  N     . ILE   A 382 ? 0.9196 0.7636 0.4879 0.1494  0.2489  0.0776  407 ILE   A N     
6125  C  CA    . ILE   A 382 ? 0.9287 0.7405 0.4611 0.1313  0.2345  0.0502  407 ILE   A CA    
6126  C  C     . ILE   A 382 ? 0.9633 0.7415 0.4478 0.1470  0.2016  0.0386  407 ILE   A C     
6127  O  O     . ILE   A 382 ? 0.9735 0.7266 0.4239 0.1681  0.2020  0.0413  407 ILE   A O     
6128  C  CB    . ILE   A 382 ? 0.8918 0.7133 0.4472 0.0954  0.2596  0.0353  407 ILE   A CB    
6129  C  CG1   . ILE   A 382 ? 0.8745 0.7024 0.4331 0.0816  0.2714  0.0201  407 ILE   A CG1   
6130  C  CG2   . ILE   A 382 ? 0.8749 0.6915 0.4419 0.0827  0.2713  0.0386  407 ILE   A CG2   
6131  C  CD1   . ILE   A 382 ? 0.8684 0.7004 0.4297 0.0646  0.2719  0.0181  407 ILE   A CD1   
6143  N  N     . VAL   A 383 ? 0.9806 0.7531 0.4600 0.1354  0.1700  0.0279  408 VAL   A N     
6144  C  CA    . VAL   A 383 ? 0.9899 0.7829 0.4727 0.1243  0.1450  0.0088  408 VAL   A CA    
6145  C  C     . VAL   A 383 ? 1.0109 0.8299 0.4925 0.1145  0.1444  -0.0002 408 VAL   A C     
6146  O  O     . VAL   A 383 ? 1.0051 0.8419 0.4843 0.1290  0.1447  -0.0148 408 VAL   A O     
6147  C  CB    . VAL   A 383 ? 0.9779 0.7749 0.4676 0.1202  0.1266  -0.0107 408 VAL   A CB    
6148  C  CG1   . VAL   A 383 ? 0.9635 0.7674 0.4658 0.1237  0.1166  -0.0331 408 VAL   A CG1   
6149  C  CG2   . VAL   A 383 ? 0.9734 0.7727 0.4611 0.1159  0.1232  -0.0063 408 VAL   A CG2   
6159  N  N     . GLU   A 384 ? 1.0316 0.8625 0.5281 0.0888  0.1412  0.0041  409 GLU   A N     
6160  C  CA    . GLU   A 384 ? 1.0459 0.8860 0.5671 0.0539  0.1285  0.0044  409 GLU   A CA    
6161  C  C     . GLU   A 384 ? 1.0414 0.8730 0.5823 0.0572  0.0989  0.0086  409 GLU   A C     
6162  O  O     . GLU   A 384 ? 1.0598 0.8835 0.5872 0.0693  0.0844  0.0080  409 GLU   A O     
6163  C  CB    . GLU   A 384 ? 1.0621 0.9224 0.5890 0.0127  0.1424  -0.0068 409 GLU   A CB    
6164  C  CG    . GLU   A 384 ? 1.0803 0.9623 0.6149 -0.0225 0.1527  -0.0195 409 GLU   A CG    
6165  C  CD    . GLU   A 384 ? 1.1020 0.9971 0.6430 -0.0562 0.1506  -0.0312 409 GLU   A CD    
6166  O  OE1   . GLU   A 384 ? 1.1094 1.0073 0.6558 -0.0691 0.1497  -0.0363 409 GLU   A OE1   
6167  O  OE2   . GLU   A 384 ? 1.1118 1.0119 0.6503 -0.0677 0.1459  -0.0354 409 GLU   A OE2   
6174  N  N     . SER   A 385 ? 1.0156 0.8463 0.5872 0.0465  0.0911  0.0134  410 SER   A N     
6175  C  CA    . SER   A 385 ? 0.9917 0.8138 0.5941 0.0443  0.0812  0.0146  410 SER   A CA    
6176  C  C     . SER   A 385 ? 0.9772 0.7873 0.6006 0.0463  0.0656  0.0074  410 SER   A C     
6177  O  O     . SER   A 385 ? 0.9840 0.7851 0.6044 0.0406  0.0695  0.0048  410 SER   A O     
6178  C  CB    . SER   A 385 ? 0.9913 0.8143 0.5976 0.0376  0.0838  0.0237  410 SER   A CB    
6179  O  OG    . SER   A 385 ? 0.9957 0.8171 0.6016 0.0287  0.0847  0.0290  410 SER   A OG    
6185  N  N     . ILE   A 386 ? 0.9675 0.7720 0.6030 0.0490  0.0406  0.0007  411 ILE   A N     
6186  C  CA    . ILE   A 386 ? 0.9743 0.7681 0.6080 0.0457  0.0181  -0.0054 411 ILE   A CA    
6187  C  C     . ILE   A 386 ? 1.0018 0.7856 0.6174 0.0498  0.0002  -0.0099 411 ILE   A C     
6188  O  O     . ILE   A 386 ? 1.0111 0.7943 0.6218 0.0520  0.0038  -0.0149 411 ILE   A O     
6189  C  CB    . ILE   A 386 ? 0.9534 0.7543 0.6043 0.0369  0.0107  -0.0039 411 ILE   A CB    
6190  C  CG1   . ILE   A 386 ? 0.9486 0.7525 0.6054 0.0346  0.0001  -0.0013 411 ILE   A CG1   
6191  C  CG2   . ILE   A 386 ? 0.9451 0.7469 0.6016 0.0294  0.0135  -0.0061 411 ILE   A CG2   
6192  C  CD1   . ILE   A 386 ? 0.9578 0.7606 0.6083 0.0351  -0.0022 -0.0045 411 ILE   A CD1   
6204  N  N     . LEU   A 387 ? 1.0238 0.7965 0.6228 0.0526  -0.0170 -0.0107 412 LEU   A N     
6205  C  CA    . LEU   A 387 ? 1.0400 0.8121 0.6326 0.0511  -0.0365 -0.0109 412 LEU   A CA    
6206  C  C     . LEU   A 387 ? 1.0456 0.8497 0.6574 0.0439  -0.0511 -0.0039 412 LEU   A C     
6207  O  O     . LEU   A 387 ? 1.0471 0.8535 0.6522 0.0323  -0.0575 -0.0026 412 LEU   A O     
6208  C  CB    . LEU   A 387 ? 1.0413 0.7960 0.6190 0.0610  -0.0336 -0.0204 412 LEU   A CB    
6209  C  CG    . LEU   A 387 ? 1.0324 0.7816 0.6098 0.0673  -0.0334 -0.0236 412 LEU   A CG    
6210  C  CD1   . LEU   A 387 ? 1.0260 0.7816 0.6093 0.0713  -0.0295 -0.0249 412 LEU   A CD1   
6211  C  CD2   . LEU   A 387 ? 1.0202 0.7710 0.6038 0.0685  -0.0366 -0.0244 412 LEU   A CD2   
6223  N  N     . ASN   A 388 ? 1.0472 0.8842 0.6889 0.0528  -0.0588 0.0036  413 ASN   A N     
6224  C  CA    . ASN   A 388 ? 1.0565 0.9229 0.7243 0.0632  -0.0707 0.0126  413 ASN   A CA    
6225  C  C     . ASN   A 388 ? 1.0505 0.9424 0.7413 0.0713  -0.0848 0.0143  413 ASN   A C     
6226  O  O     . ASN   A 388 ? 1.0486 0.9506 0.7444 0.0952  -0.0914 0.0311  413 ASN   A O     
6227  C  CB    . ASN   A 388 ? 1.0768 0.9417 0.7413 0.0620  -0.0720 0.0190  413 ASN   A CB    
6228  C  CG    . ASN   A 388 ? 1.0950 0.9587 0.7546 0.0562  -0.0762 0.0242  413 ASN   A CG    
6229  O  OD1   . ASN   A 388 ? 1.1050 0.9613 0.7573 0.0577  -0.0786 0.0215  413 ASN   A OD1   
6230  N  ND2   . ASN   A 388 ? 1.0994 0.9664 0.7609 0.0516  -0.0754 0.0316  413 ASN   A ND2   
6237  N  N     . TRP   A 389 ? 1.0393 0.9452 0.7530 0.0497  -0.0933 -0.0065 414 TRP   A N     
6238  C  CA    . TRP   A 389 ? 1.0214 0.9410 0.7602 0.0189  -0.1054 -0.0247 414 TRP   A CA    
6239  C  C     . TRP   A 389 ? 1.0279 0.9376 0.7640 0.0112  -0.0981 -0.0356 414 TRP   A C     
6240  O  O     . TRP   A 389 ? 1.0363 0.9431 0.7622 0.0098  -0.1044 -0.0429 414 TRP   A O     
6241  C  CB    . TRP   A 389 ? 0.9985 0.9379 0.7627 -0.0053 -0.1285 -0.0316 414 TRP   A CB    
6242  C  CG    . TRP   A 389 ? 0.9830 0.9319 0.7601 -0.0229 -0.1495 -0.0372 414 TRP   A CG    
6243  C  CD1   . TRP   A 389 ? 0.9747 0.9280 0.7585 -0.0297 -0.1611 -0.0414 414 TRP   A CD1   
6244  C  CD2   . TRP   A 389 ? 0.9795 0.9316 0.7583 -0.0265 -0.1607 -0.0337 414 TRP   A CD2   
6245  N  NE1   . TRP   A 389 ? 0.9708 0.9263 0.7577 -0.0290 -0.1722 -0.0393 414 TRP   A NE1   
6246  C  CE2   . TRP   A 389 ? 0.9752 0.9283 0.7567 -0.0303 -0.1696 -0.0359 414 TRP   A CE2   
6247  C  CE3   . TRP   A 389 ? 0.9792 0.9331 0.7575 -0.0261 -0.1642 -0.0268 414 TRP   A CE3   
6248  C  CZ2   . TRP   A 389 ? 0.9804 0.9299 0.7546 -0.0300 -0.1706 -0.0332 414 TRP   A CZ2   
6249  C  CZ3   . TRP   A 389 ? 0.9809 0.9337 0.7554 -0.0274 -0.1684 -0.0266 414 TRP   A CZ3   
6250  C  CH2   . TRP   A 389 ? 0.9803 0.9318 0.7536 -0.0315 -0.1697 -0.0311 414 TRP   A CH2   
6261  N  N     . VAL   A 390 ? 1.0243 0.9277 0.7714 0.0081  -0.0845 -0.0364 415 VAL   A N     
6262  C  CA    . VAL   A 390 ? 1.0234 0.9284 0.7832 0.0138  -0.0704 -0.0326 415 VAL   A CA    
6263  C  C     . VAL   A 390 ? 1.0404 0.9341 0.7983 0.0145  -0.0698 -0.0417 415 VAL   A C     
6264  O  O     . VAL   A 390 ? 1.0355 0.9422 0.7980 0.0004  -0.0740 -0.0506 415 VAL   A O     
6265  C  CB    . VAL   A 390 ? 1.0023 0.9256 0.7817 0.0172  -0.0611 -0.0210 415 VAL   A CB    
6266  C  CG1   . VAL   A 390 ? 0.9897 0.9242 0.7795 0.0193  -0.0569 -0.0143 415 VAL   A CG1   
6267  C  CG2   . VAL   A 390 ? 0.9978 0.9232 0.7828 0.0144  -0.0625 -0.0188 415 VAL   A CG2   
6277  N  N     . LYS   A 391 ? 1.0608 0.9286 0.8152 0.0289  -0.0622 -0.0408 416 LYS   A N     
6278  C  CA    . LYS   A 391 ? 1.0676 0.9226 0.8380 0.0391  -0.0560 -0.0413 416 LYS   A CA    
6279  C  C     . LYS   A 391 ? 1.1140 0.9273 0.8514 0.0442  -0.0698 -0.0413 416 LYS   A C     
6280  O  O     . LYS   A 391 ? 1.1239 0.9215 0.8491 0.0359  -0.0725 -0.0427 416 LYS   A O     
6281  C  CB    . LYS   A 391 ? 1.0201 0.9112 0.8473 0.0468  -0.0418 -0.0441 416 LYS   A CB    
6284  N  N     . PHE   A 392 ? 1.1466 0.9423 0.8680 0.0587  -0.0759 -0.0390 417 PHE   A N     
6285  C  CA    . PHE   A 392 ? 1.1703 0.9640 0.8841 0.0687  -0.0757 -0.0376 417 PHE   A CA    
6286  C  C     . PHE   A 392 ? 1.1601 0.9674 0.8927 0.0712  -0.0781 -0.0391 417 PHE   A C     
6287  O  O     . PHE   A 392 ? 1.1534 0.9713 0.8987 0.0722  -0.0797 -0.0406 417 PHE   A O     
6288  C  CB    . PHE   A 392 ? 1.1901 0.9826 0.8884 0.0751  -0.0712 -0.0326 417 PHE   A CB    
6291  N  N     . ALA   B 3   ? 1.0153 0.6031 0.4997 0.0674  -0.0569 0.0123  28  ALA   B N     
6292  C  CA    . ALA   B 3   ? 0.9977 0.5670 0.4932 0.0885  -0.0698 0.0295  28  ALA   B CA    
6293  C  C     . ALA   B 3   ? 0.9609 0.4640 0.4640 0.1530  -0.0913 0.0751  28  ALA   B C     
6294  O  O     . ALA   B 3   ? 0.9507 0.4386 0.4723 0.2139  -0.0804 0.0835  28  ALA   B O     
6295  C  CB    . ALA   B 3   ? 1.0083 0.6042 0.5004 0.0648  -0.0720 0.0145  28  ALA   B CB    
6300  N  N     . SER   B 4   ? 0.9480 0.4170 0.4314 0.1422  -0.1337 0.1037  29  SER   B N     
6301  C  CA    . SER   B 4   ? 0.9110 0.3726 0.4016 0.1233  -0.1389 0.0937  29  SER   B CA    
6302  C  C     . SER   B 4   ? 0.9089 0.3289 0.3596 0.1029  -0.1473 0.0568  29  SER   B C     
6303  O  O     . SER   B 4   ? 0.8833 0.2894 0.3433 0.0857  -0.1698 0.0288  29  SER   B O     
6304  C  CB    . SER   B 4   ? 0.8912 0.3866 0.4111 0.1343  -0.1399 0.0971  29  SER   B CB    
6305  O  OG    . SER   B 4   ? 0.8611 0.3941 0.4147 0.1273  -0.1343 0.1203  29  SER   B OG    
6311  N  N     . VAL   B 5   ? 0.9458 0.3423 0.3407 0.0903  -0.1450 0.0427  30  VAL   B N     
6312  C  CA    . VAL   B 5   ? 0.9520 0.3677 0.3533 0.0928  -0.1316 0.0310  30  VAL   B CA    
6313  C  C     . VAL   B 5   ? 0.9203 0.3461 0.3159 0.0906  -0.1437 0.0445  30  VAL   B C     
6314  O  O     . VAL   B 5   ? 0.8812 0.3285 0.3117 0.0836  -0.1559 0.0386  30  VAL   B O     
6315  C  CB    . VAL   B 5   ? 0.9842 0.4126 0.4192 0.0833  -0.0943 -0.0054 30  VAL   B CB    
6316  C  CG1   . VAL   B 5   ? 0.9826 0.4008 0.4498 0.0987  -0.0876 0.0175  30  VAL   B CG1   
6317  C  CG2   . VAL   B 5   ? 1.0054 0.4323 0.4312 0.0809  -0.0840 -0.0451 30  VAL   B CG2   
6327  N  N     . GLU   B 6   ? 0.9150 0.3460 0.3109 0.0878  -0.1331 0.0488  31  GLU   B N     
6328  C  CA    . GLU   B 6   ? 0.9023 0.3469 0.2942 0.0710  -0.1236 0.0495  31  GLU   B CA    
6329  C  C     . GLU   B 6   ? 0.8732 0.3335 0.3024 0.0807  -0.1183 0.0557  31  GLU   B C     
6330  O  O     . GLU   B 6   ? 0.8695 0.3177 0.3181 0.0961  -0.1034 0.0610  31  GLU   B O     
6331  C  CB    . GLU   B 6   ? 0.9262 0.3670 0.2955 0.0462  -0.1170 0.0607  31  GLU   B CB    
6332  C  CG    . GLU   B 6   ? 0.9482 0.3657 0.3067 0.0372  -0.1353 0.0533  31  GLU   B CG    
6333  C  CD    . GLU   B 6   ? 0.9668 0.3656 0.3231 0.0337  -0.1622 0.0539  31  GLU   B CD    
6334  O  OE1   . GLU   B 6   ? 0.9626 0.3765 0.3189 0.0287  -0.1599 0.0565  31  GLU   B OE1   
6335  O  OE2   . GLU   B 6   ? 0.9868 0.3478 0.3437 0.0468  -0.1771 0.0479  31  GLU   B OE2   
6342  N  N     . ARG   B 7   ? 0.8194 0.3017 0.2944 0.0631  -0.1305 0.0510  32  ARG   B N     
6343  C  CA    . ARG   B 7   ? 0.8167 0.3060 0.2983 0.0662  -0.1086 0.0644  32  ARG   B CA    
6344  C  C     . ARG   B 7   ? 0.7727 0.2953 0.2769 0.0774  -0.0814 0.0639  32  ARG   B C     
6345  O  O     . ARG   B 7   ? 0.7526 0.3112 0.2833 0.0871  -0.0584 0.0836  32  ARG   B O     
6346  C  CB    . ARG   B 7   ? 0.8680 0.3307 0.3269 0.0675  -0.1228 0.0744  32  ARG   B CB    
6347  C  CG    . ARG   B 7   ? 0.9631 0.3804 0.3845 0.0507  -0.1118 0.0635  32  ARG   B CG    
6348  C  CD    . ARG   B 7   ? 1.0404 0.4557 0.4358 0.0293  -0.1217 0.0637  32  ARG   B CD    
6349  N  NE    . ARG   B 7   ? 1.1290 0.5364 0.4866 0.0198  -0.1059 0.0562  32  ARG   B NE    
6350  C  CZ    . ARG   B 7   ? 1.1826 0.6042 0.5205 0.0258  -0.1183 0.0639  32  ARG   B CZ    
6351  N  NH1   . ARG   B 7   ? 1.2005 0.6391 0.5304 0.0268  -0.1202 0.0703  32  ARG   B NH1   
6352  N  NH2   . ARG   B 7   ? 1.1970 0.6315 0.5316 0.0334  -0.1299 0.0578  32  ARG   B NH2   
6366  N  N     . ILE   B 8   ? 0.7330 0.2526 0.2698 0.0799  -0.0605 0.0534  33  ILE   B N     
6367  C  CA    . ILE   B 8   ? 0.7449 0.2311 0.2625 0.0659  -0.0652 0.0376  33  ILE   B CA    
6368  C  C     . ILE   B 8   ? 0.7487 0.2343 0.2488 0.0774  -0.0824 0.0241  33  ILE   B C     
6369  O  O     . ILE   B 8   ? 0.7312 0.2279 0.2315 0.0512  -0.0875 0.0234  33  ILE   B O     
6370  C  CB    . ILE   B 8   ? 0.7454 0.2424 0.2910 0.0953  -0.0658 0.0428  33  ILE   B CB    
6371  C  CG1   . ILE   B 8   ? 0.7655 0.2626 0.3220 0.1251  -0.0586 0.0498  33  ILE   B CG1   
6372  C  CG2   . ILE   B 8   ? 0.7627 0.2796 0.2943 0.1133  -0.0828 0.0315  33  ILE   B CG2   
6373  C  CD1   . ILE   B 8   ? 0.7919 0.2756 0.3454 0.1428  -0.0580 0.0499  33  ILE   B CD1   
6385  N  N     . TYR   B 9   ? 0.7295 0.2279 0.2518 0.0737  -0.1052 0.0185  34  TYR   B N     
6386  C  CA    . TYR   B 9   ? 0.7318 0.2456 0.2536 0.0901  -0.1128 0.0179  34  TYR   B CA    
6387  C  C     . TYR   B 9   ? 0.7574 0.2654 0.2306 0.0940  -0.0823 0.0196  34  TYR   B C     
6388  O  O     . TYR   B 9   ? 0.7951 0.3095 0.2216 0.1151  -0.0513 0.0184  34  TYR   B O     
6389  C  CB    . TYR   B 9   ? 0.6520 0.2437 0.2763 0.0749  -0.1533 0.0252  34  TYR   B CB    
6390  C  CG    . TYR   B 9   ? 0.6500 0.2628 0.2851 0.0785  -0.1651 0.0281  34  TYR   B CG    
6391  C  CD1   . TYR   B 9   ? 0.6396 0.2563 0.2830 0.0792  -0.1596 0.0291  34  TYR   B CD1   
6392  C  CD2   . TYR   B 9   ? 0.6559 0.2768 0.2982 0.0941  -0.1693 0.0280  34  TYR   B CD2   
6393  C  CE1   . TYR   B 9   ? 0.6427 0.2556 0.2798 0.0894  -0.1565 0.0229  34  TYR   B CE1   
6394  C  CE2   . TYR   B 9   ? 0.6658 0.2829 0.2963 0.1121  -0.1598 0.0247  34  TYR   B CE2   
6395  C  CZ    . TYR   B 9   ? 0.6628 0.2908 0.2908 0.1136  -0.1653 0.0193  34  TYR   B CZ    
6396  O  OH    . TYR   B 9   ? 0.6606 0.3357 0.3127 0.1450  -0.1594 0.0333  34  TYR   B OH    
6406  N  N     . GLN   B 10  ? 0.7441 0.2424 0.2372 0.0772  -0.0741 0.0269  35  GLN   B N     
6407  C  CA    . GLN   B 10  ? 0.7294 0.2316 0.2736 0.0831  -0.0770 0.0348  35  GLN   B CA    
6408  C  C     . GLN   B 10  ? 0.6953 0.2350 0.2381 0.0776  -0.0599 0.0387  35  GLN   B C     
6409  O  O     . GLN   B 10  ? 0.6727 0.2426 0.2345 0.0712  -0.0547 0.0496  35  GLN   B O     
6410  C  CB    . GLN   B 10  ? 0.7825 0.2381 0.3527 0.0881  -0.0528 0.0509  35  GLN   B CB    
6411  C  CG    . GLN   B 10  ? 0.8119 0.2388 0.4298 0.0962  -0.0504 0.0482  35  GLN   B CG    
6412  C  CD    . GLN   B 10  ? 0.8452 0.2769 0.5034 0.1034  -0.0383 0.0412  35  GLN   B CD    
6413  O  OE1   . GLN   B 10  ? 0.8820 0.2998 0.5579 0.0985  -0.0276 0.0263  35  GLN   B OE1   
6414  N  NE2   . GLN   B 10  ? 0.8348 0.2687 0.5117 0.0757  -0.0315 0.0304  35  GLN   B NE2   
6423  N  N     . LYS   B 11  ? 0.7375 0.2446 0.2275 0.0941  -0.0405 0.0293  36  LYS   B N     
6424  C  CA    . LYS   B 11  ? 0.7772 0.2517 0.2152 0.0737  -0.0085 0.0268  36  LYS   B CA    
6425  C  C     . LYS   B 11  ? 0.7557 0.2659 0.2239 0.0643  0.0193  0.0476  36  LYS   B C     
6426  O  O     . LYS   B 11  ? 0.7626 0.3076 0.2456 0.0547  0.0294  0.0767  36  LYS   B O     
6427  C  CB    . LYS   B 11  ? 0.8383 0.2804 0.2577 0.0757  -0.0334 -0.0049 36  LYS   B CB    
6428  C  CG    . LYS   B 11  ? 0.8698 0.3167 0.3074 0.1054  -0.0434 -0.0294 36  LYS   B CG    
6429  C  CD    . LYS   B 11  ? 0.9194 0.3672 0.3735 0.0795  -0.0393 -0.0426 36  LYS   B CD    
6430  C  CE    . LYS   B 11  ? 0.9715 0.4609 0.4052 0.0371  -0.0170 -0.0663 36  LYS   B CE    
6431  N  NZ    . LYS   B 11  ? 1.0059 0.4875 0.4158 0.0382  -0.0089 -0.0951 36  LYS   B NZ    
6445  N  N     . LYS   B 12  ? 0.7451 0.2498 0.2205 0.0629  0.0466  0.0423  37  LYS   B N     
6446  C  CA    . LYS   B 12  ? 0.7645 0.2530 0.2201 0.0505  0.0154  0.0394  37  LYS   B CA    
6447  C  C     . LYS   B 12  ? 0.7585 0.2775 0.2079 0.0600  -0.0088 0.0195  37  LYS   B C     
6448  O  O     . LYS   B 12  ? 0.7677 0.2466 0.2264 0.0495  0.0085  0.0084  37  LYS   B O     
6449  C  CB    . LYS   B 12  ? 0.7866 0.2479 0.2361 0.0445  0.0415  0.0413  37  LYS   B CB    
6450  C  CG    . LYS   B 12  ? 0.8101 0.2431 0.2757 0.0351  0.0514  0.0467  37  LYS   B CG    
6451  C  CD    . LYS   B 12  ? 0.8377 0.2459 0.2987 0.0276  0.0698  0.0527  37  LYS   B CD    
6452  C  CE    . LYS   B 12  ? 0.8898 0.2706 0.3264 0.0333  0.0618  0.0672  37  LYS   B CE    
6453  N  NZ    . LYS   B 12  ? 0.9482 0.3117 0.3390 0.0259  0.0591  0.0664  37  LYS   B NZ    
6467  N  N     . THR   B 13  ? 0.7234 0.2970 0.1970 0.0824  -0.0212 0.0290  38  THR   B N     
6468  C  CA    . THR   B 13  ? 0.7218 0.2722 0.2038 0.0440  -0.0080 0.0115  38  THR   B CA    
6469  C  C     . THR   B 13  ? 0.7257 0.2309 0.2206 0.0453  0.0064  0.0226  38  THR   B C     
6470  O  O     . THR   B 13  ? 0.7297 0.2240 0.2207 0.0020  0.0192  0.0162  38  THR   B O     
6471  C  CB    . THR   B 13  ? 0.7317 0.3054 0.1953 0.0212  0.0177  0.0221  38  THR   B CB    
6472  O  OG1   . THR   B 13  ? 0.7517 0.3034 0.1970 0.0099  0.0477  0.0065  38  THR   B OG1   
6473  C  CG2   . THR   B 13  ? 0.7520 0.3551 0.1995 0.0186  0.0292  0.0164  38  THR   B CG2   
6481  N  N     . GLN   B 14  ? 0.7266 0.2377 0.2429 0.0592  0.0047  0.0088  39  GLN   B N     
6482  C  CA    . GLN   B 14  ? 0.7233 0.2470 0.2689 0.0484  0.0265  0.0202  39  GLN   B CA    
6483  C  C     . GLN   B 14  ? 0.6770 0.2496 0.2422 0.0596  0.0503  0.0138  39  GLN   B C     
6484  O  O     . GLN   B 14  ? 0.6461 0.2505 0.2359 0.0495  0.0721  0.0175  39  GLN   B O     
6485  C  CB    . GLN   B 14  ? 0.7808 0.2821 0.3199 0.0504  0.0166  0.0216  39  GLN   B CB    
6486  C  CG    . GLN   B 14  ? 0.8357 0.3375 0.3665 0.0379  0.0282  0.0498  39  GLN   B CG    
6487  C  CD    . GLN   B 14  ? 0.8908 0.3886 0.4053 0.0378  0.0421  0.0620  39  GLN   B CD    
6488  O  OE1   . GLN   B 14  ? 0.9127 0.4211 0.4500 0.0204  0.0499  0.0850  39  GLN   B OE1   
6489  N  NE2   . GLN   B 14  ? 0.9072 0.4115 0.3989 0.0489  0.0471  0.0299  39  GLN   B NE2   
6498  N  N     . LEU   B 15  ? 0.6677 0.2706 0.2382 0.0295  0.0678  0.0141  40  LEU   B N     
6499  C  CA    . LEU   B 15  ? 0.6795 0.2831 0.2321 0.0181  0.1084  0.0174  40  LEU   B CA    
6500  C  C     . LEU   B 15  ? 0.6735 0.2712 0.2092 0.0254  0.1081  0.0056  40  LEU   B C     
6501  O  O     . LEU   B 15  ? 0.6614 0.2724 0.2014 -0.0054 0.1088  0.0208  40  LEU   B O     
6502  C  CB    . LEU   B 15  ? 0.7072 0.3421 0.2469 -0.0016 0.1519  0.0081  40  LEU   B CB    
6503  C  CG    . LEU   B 15  ? 0.7444 0.4056 0.2656 -0.0303 0.1634  0.0133  40  LEU   B CG    
6504  C  CD1   . LEU   B 15  ? 0.7540 0.4357 0.2838 -0.0558 0.1517  0.0153  40  LEU   B CD1   
6505  C  CD2   . LEU   B 15  ? 0.7916 0.4390 0.2782 -0.0228 0.1862  0.0021  40  LEU   B CD2   
6517  N  N     . GLU   B 16  ? 0.6816 0.2708 0.1972 0.0339  0.0997  0.0141  41  GLU   B N     
6518  C  CA    . GLU   B 16  ? 0.7103 0.2800 0.2030 0.0359  0.0786  0.0284  41  GLU   B CA    
6519  C  C     . GLU   B 16  ? 0.6624 0.2595 0.2099 -0.0127 0.0810  0.0466  41  GLU   B C     
6520  O  O     . GLU   B 16  ? 0.6645 0.2531 0.2146 -0.0250 0.0735  0.0487  41  GLU   B O     
6521  C  CB    . GLU   B 16  ? 0.7572 0.3256 0.2152 0.0448  0.0862  0.0367  41  GLU   B CB    
6522  C  CG    . GLU   B 16  ? 0.7688 0.3697 0.2338 0.0378  0.1038  0.0581  41  GLU   B CG    
6523  C  CD    . GLU   B 16  ? 0.7814 0.4031 0.2599 0.0333  0.0929  0.0981  41  GLU   B CD    
6524  O  OE1   . GLU   B 16  ? 0.7457 0.3666 0.2643 0.0500  0.1149  0.0952  41  GLU   B OE1   
6525  O  OE2   . GLU   B 16  ? 0.7936 0.4708 0.2875 0.0137  0.0749  0.1200  41  GLU   B OE2   
6532  N  N     . HIS   B 17  ? 0.6167 0.2492 0.2050 -0.0057 0.1057  0.0395  42  HIS   B N     
6533  C  CA    . HIS   B 17  ? 0.5862 0.2217 0.1959 0.0240  0.0855  0.0471  42  HIS   B CA    
6534  C  C     . HIS   B 17  ? 0.5718 0.2150 0.2008 -0.0062 0.0869  0.0133  42  HIS   B C     
6535  O  O     . HIS   B 17  ? 0.5798 0.2834 0.1959 0.0083  0.0579  0.0145  42  HIS   B O     
6536  C  CB    . HIS   B 17  ? 0.5723 0.2537 0.2124 0.0317  0.0593  0.0373  42  HIS   B CB    
6537  C  CG    . HIS   B 17  ? 0.5386 0.2621 0.2168 0.0269  0.0562  0.0407  42  HIS   B CG    
6538  N  ND1   . HIS   B 17  ? 0.5030 0.2668 0.2238 0.0169  0.0334  0.0358  42  HIS   B ND1   
6539  C  CD2   . HIS   B 17  ? 0.5419 0.2618 0.2255 0.0301  0.0452  0.0352  42  HIS   B CD2   
6540  C  CE1   . HIS   B 17  ? 0.4897 0.2548 0.2184 0.0420  0.0224  0.0533  42  HIS   B CE1   
6541  N  NE2   . HIS   B 17  ? 0.5148 0.2592 0.2215 0.0368  0.0395  0.0521  42  HIS   B NE2   
6549  N  N     . ILE   B 18  ? 0.5495 0.2003 0.2026 -0.0022 0.1083  0.0032  43  ILE   B N     
6550  C  CA    . ILE   B 18  ? 0.5504 0.1821 0.2249 0.0084  0.0876  -0.0027 43  ILE   B CA    
6551  C  C     . ILE   B 18  ? 0.5507 0.1759 0.2208 -0.0056 0.0915  0.0073  43  ILE   B C     
6552  O  O     . ILE   B 18  ? 0.5504 0.2018 0.2172 -0.0195 0.0757  0.0092  43  ILE   B O     
6553  C  CB    . ILE   B 18  ? 0.5445 0.1892 0.2404 0.0123  0.0965  -0.0037 43  ILE   B CB    
6554  C  CG1   . ILE   B 18  ? 0.5708 0.1673 0.2417 0.0048  0.0751  -0.0144 43  ILE   B CG1   
6555  C  CG2   . ILE   B 18  ? 0.5171 0.2366 0.2638 0.0104  0.1250  -0.0238 43  ILE   B CG2   
6556  C  CD1   . ILE   B 18  ? 0.5460 0.1930 0.2459 0.0090  0.0947  -0.0241 43  ILE   B CD1   
6568  N  N     . LEU   B 19  ? 0.5833 0.2062 0.2355 -0.0134 0.1241  0.0098  44  LEU   B N     
6569  C  CA    . LEU   B 19  ? 0.6275 0.2088 0.2420 0.0038  0.1469  0.0188  44  LEU   B CA    
6570  C  C     . LEU   B 19  ? 0.6476 0.2244 0.2638 0.0211  0.1079  0.0138  44  LEU   B C     
6571  O  O     . LEU   B 19  ? 0.6476 0.2571 0.2669 -0.0053 0.1058  -0.0141 44  LEU   B O     
6572  C  CB    . LEU   B 19  ? 0.6422 0.2505 0.2713 0.0168  0.1964  0.0243  44  LEU   B CB    
6573  C  CG    . LEU   B 19  ? 0.6557 0.2986 0.3004 0.0137  0.2173  0.0355  44  LEU   B CG    
6574  C  CD1   . LEU   B 19  ? 0.6738 0.3721 0.3100 -0.0067 0.2278  0.0248  44  LEU   B CD1   
6575  C  CD2   . LEU   B 19  ? 0.6439 0.2740 0.3162 0.0370  0.2140  0.0414  44  LEU   B CD2   
6587  N  N     . LEU   B 20  ? 0.6602 0.2123 0.2627 0.0628  0.0648  0.0400  45  LEU   B N     
6588  C  CA    . LEU   B 20  ? 0.6678 0.2296 0.2661 0.0730  0.0607  0.0184  45  LEU   B CA    
6589  C  C     . LEU   B 20  ? 0.6284 0.2198 0.2536 0.0436  0.0526  -0.0064 45  LEU   B C     
6590  O  O     . LEU   B 20  ? 0.6822 0.2394 0.2631 0.0534  0.0409  -0.0186 45  LEU   B O     
6591  C  CB    . LEU   B 20  ? 0.6967 0.2389 0.2817 0.0679  0.0556  0.0149  45  LEU   B CB    
6592  C  CG    . LEU   B 20  ? 0.7531 0.2861 0.3186 0.0921  0.0403  0.0323  45  LEU   B CG    
6593  C  CD1   . LEU   B 20  ? 0.7753 0.2944 0.3405 0.1174  0.0389  0.0545  45  LEU   B CD1   
6594  C  CD2   . LEU   B 20  ? 0.7724 0.3090 0.3286 0.0692  0.0328  0.0132  45  LEU   B CD2   
6606  N  N     . ARG   B 21  ? 0.5418 0.2112 0.2468 0.0535  0.0515  0.0204  46  ARG   B N     
6607  C  CA    . ARG   B 21  ? 0.4763 0.2276 0.2336 0.0288  0.0552  0.0231  46  ARG   B CA    
6608  C  C     . ARG   B 21  ? 0.4504 0.2167 0.2417 0.0427  0.0580  0.0154  46  ARG   B C     
6609  O  O     . ARG   B 21  ? 0.4424 0.2284 0.2662 0.0587  0.0509  0.0085  46  ARG   B O     
6610  C  CB    . ARG   B 21  ? 0.4984 0.2886 0.2295 0.0425  0.0343  0.0077  46  ARG   B CB    
6611  C  CG    . ARG   B 21  ? 0.4862 0.3209 0.2382 0.0375  0.0261  0.0110  46  ARG   B CG    
6612  C  CD    . ARG   B 21  ? 0.4729 0.3233 0.2411 0.0188  0.0194  0.0132  46  ARG   B CD    
6613  N  NE    . ARG   B 21  ? 0.5126 0.2999 0.2508 -0.0025 0.0151  -0.0190 46  ARG   B NE    
6614  C  CZ    . ARG   B 21  ? 0.5498 0.3052 0.2424 0.0716  -0.0045 -0.0241 46  ARG   B CZ    
6615  N  NH1   . ARG   B 21  ? 0.5358 0.2859 0.2658 0.0823  -0.0136 -0.0300 46  ARG   B NH1   
6616  N  NH2   . ARG   B 21  ? 0.6076 0.3449 0.2435 0.0982  -0.0332 -0.0309 46  ARG   B NH2   
6630  N  N     . PRO   B 22  ? 0.4396 0.2051 0.2452 0.0195  0.0731  0.0025  47  PRO   B N     
6631  C  CA    . PRO   B 22  ? 0.3988 0.2285 0.2541 0.0017  0.0675  -0.0116 47  PRO   B CA    
6632  C  C     . PRO   B 22  ? 0.3285 0.2127 0.2439 0.0248  0.0721  -0.0017 47  PRO   B C     
6633  O  O     . PRO   B 22  ? 0.3235 0.2046 0.2577 0.0161  0.0711  -0.0040 47  PRO   B O     
6634  C  CB    . PRO   B 22  ? 0.4434 0.2292 0.2802 0.0089  0.0783  -0.0056 47  PRO   B CB    
6635  C  CG    . PRO   B 22  ? 0.4806 0.2537 0.3124 -0.0180 0.0464  0.0094  47  PRO   B CG    
6636  C  CD    . PRO   B 22  ? 0.4769 0.2322 0.2768 -0.0130 0.0571  0.0062  47  PRO   B CD    
6644  N  N     . ASP   B 23  ? 0.3394 0.2222 0.2245 0.0278  0.0460  0.0009  48  ASP   B N     
6645  C  CA    . ASP   B 23  ? 0.3378 0.2034 0.2255 0.0346  0.0388  -0.0001 48  ASP   B CA    
6646  C  C     . ASP   B 23  ? 0.3125 0.2215 0.2326 0.0373  0.0485  0.0005  48  ASP   B C     
6647  O  O     . ASP   B 23  ? 0.2923 0.2263 0.2506 -0.0102 0.0289  0.0102  48  ASP   B O     
6648  C  CB    . ASP   B 23  ? 0.3554 0.2236 0.2488 0.0317  0.0403  0.0003  48  ASP   B CB    
6649  C  CG    . ASP   B 23  ? 0.3808 0.2516 0.2903 0.0339  0.0690  0.0104  48  ASP   B CG    
6650  O  OD1   . ASP   B 23  ? 0.5012 0.2788 0.3119 0.0401  0.0843  0.0165  48  ASP   B OD1   
6651  O  OD2   . ASP   B 23  ? 0.3402 0.2658 0.3212 0.0337  0.0795  -0.0108 48  ASP   B OD2   
6656  N  N     . THR   B 24  ? 0.3141 0.2450 0.2337 0.0537  0.0487  -0.0171 49  THR   B N     
6657  C  CA    . THR   B 24  ? 0.3098 0.2509 0.2492 0.0152  0.0467  -0.0224 49  THR   B CA    
6658  C  C     . THR   B 24  ? 0.3259 0.2350 0.2614 -0.0078 0.0688  -0.0175 49  THR   B C     
6659  O  O     . THR   B 24  ? 0.3210 0.2626 0.2926 -0.0193 0.1022  -0.0045 49  THR   B O     
6660  C  CB    . THR   B 24  ? 0.2968 0.2609 0.2490 0.0163  0.0455  -0.0065 49  THR   B CB    
6661  O  OG1   . THR   B 24  ? 0.3685 0.3157 0.2485 0.0148  0.0179  -0.0023 49  THR   B OG1   
6662  C  CG2   . THR   B 24  ? 0.2589 0.2403 0.2660 0.0070  0.0292  0.0162  49  THR   B CG2   
6670  N  N     . TYR   B 25  ? 0.3257 0.2060 0.2302 0.0093  0.0857  -0.0093 50  TYR   B N     
6671  C  CA    . TYR   B 25  ? 0.3095 0.2037 0.2207 0.0099  0.0586  -0.0123 50  TYR   B CA    
6672  C  C     . TYR   B 25  ? 0.3019 0.1989 0.2276 0.0032  0.0579  -0.0054 50  TYR   B C     
6673  O  O     . TYR   B 25  ? 0.2830 0.1927 0.2390 -0.0063 0.0594  -0.0016 50  TYR   B O     
6674  C  CB    . TYR   B 25  ? 0.3679 0.1960 0.2127 0.0114  0.0521  0.0056  50  TYR   B CB    
6675  C  CG    . TYR   B 25  ? 0.4125 0.1929 0.2027 0.0051  0.0562  -0.0015 50  TYR   B CG    
6676  C  CD1   . TYR   B 25  ? 0.4617 0.2129 0.2003 0.0318  0.0487  0.0017  50  TYR   B CD1   
6677  C  CD2   . TYR   B 25  ? 0.4331 0.2039 0.1922 -0.0167 0.0746  -0.0041 50  TYR   B CD2   
6678  C  CE1   . TYR   B 25  ? 0.4652 0.2215 0.2024 0.0450  0.0309  0.0150  50  TYR   B CE1   
6679  C  CE2   . TYR   B 25  ? 0.4507 0.2144 0.1861 0.0118  0.0373  -0.0008 50  TYR   B CE2   
6680  C  CZ    . TYR   B 25  ? 0.4820 0.2404 0.2050 0.0340  0.0363  0.0094  50  TYR   B CZ    
6681  O  OH    . TYR   B 25  ? 0.5585 0.2619 0.2309 0.0411  0.0310  0.0101  50  TYR   B OH    
6691  N  N     . ILE   B 26  ? 0.2876 0.1772 0.2234 0.0162  0.0451  -0.0208 51  ILE   B N     
6692  C  CA    . ILE   B 26  ? 0.2642 0.2017 0.2386 -0.0181 0.0772  -0.0209 51  ILE   B CA    
6693  C  C     . ILE   B 26  ? 0.2292 0.1891 0.2300 0.0114  0.0839  -0.0256 51  ILE   B C     
6694  O  O     . ILE   B 26  ? 0.2536 0.2261 0.2373 -0.0093 0.0543  -0.0232 51  ILE   B O     
6695  C  CB    . ILE   B 26  ? 0.3011 0.1930 0.2549 -0.0110 0.1042  -0.0270 51  ILE   B CB    
6696  C  CG1   . ILE   B 26  ? 0.3209 0.2085 0.2685 -0.0251 0.0943  -0.0143 51  ILE   B CG1   
6697  C  CG2   . ILE   B 26  ? 0.3123 0.2179 0.2447 0.0110  0.1256  -0.0453 51  ILE   B CG2   
6698  C  CD1   . ILE   B 26  ? 0.3436 0.1989 0.2721 -0.0810 0.1070  -0.0165 51  ILE   B CD1   
6710  N  N     . GLY   B 27  ? 0.2501 0.1959 0.2427 0.0000  0.0784  -0.0373 52  GLY   B N     
6711  C  CA    . GLY   B 27  ? 0.2559 0.2112 0.2523 -0.0137 0.0752  -0.0417 52  GLY   B CA    
6712  C  C     . GLY   B 27  ? 0.2882 0.2085 0.2702 -0.0209 0.0626  -0.0429 52  GLY   B C     
6713  O  O     . GLY   B 27  ? 0.3486 0.2034 0.2706 0.0060  0.0389  -0.0267 52  GLY   B O     
6717  N  N     . SER   B 28  ? 0.2950 0.2047 0.2835 -0.0091 0.0592  -0.0455 53  SER   B N     
6718  C  CA    . SER   B 28  ? 0.3065 0.1823 0.3010 0.0001  0.0441  -0.0474 53  SER   B CA    
6719  C  C     . SER   B 28  ? 0.3203 0.2006 0.3091 0.0016  0.0404  -0.0259 53  SER   B C     
6720  O  O     . SER   B 28  ? 0.3072 0.2039 0.3108 0.0044  0.0558  -0.0095 53  SER   B O     
6721  C  CB    . SER   B 28  ? 0.3580 0.1978 0.3365 0.0451  0.0458  -0.0560 53  SER   B CB    
6722  O  OG    . SER   B 28  ? 0.3833 0.2509 0.3636 0.0081  0.0410  -0.0490 53  SER   B OG    
6728  N  N     . VAL   B 29  ? 0.3119 0.2025 0.3271 -0.0194 0.0315  -0.0260 54  VAL   B N     
6729  C  CA    . VAL   B 29  ? 0.3448 0.2128 0.3536 -0.0228 0.0402  -0.0278 54  VAL   B CA    
6730  C  C     . VAL   B 29  ? 0.3558 0.2360 0.3784 -0.0127 0.0423  -0.0345 54  VAL   B C     
6731  O  O     . VAL   B 29  ? 0.3781 0.2373 0.3813 -0.0317 0.0359  -0.0229 54  VAL   B O     
6732  C  CB    . VAL   B 29  ? 0.4075 0.2215 0.3608 -0.0024 0.0622  -0.0318 54  VAL   B CB    
6733  C  CG1   . VAL   B 29  ? 0.4252 0.2222 0.3654 -0.0378 0.0701  -0.0568 54  VAL   B CG1   
6734  C  CG2   . VAL   B 29  ? 0.4398 0.2439 0.3627 0.0227  0.0565  -0.0087 54  VAL   B CG2   
6744  N  N     . GLU   B 30  ? 0.3216 0.2103 0.3859 -0.0088 0.0506  -0.0502 55  GLU   B N     
6745  C  CA    . GLU   B 30  ? 0.3190 0.2143 0.4217 -0.0280 0.0168  -0.0450 55  GLU   B CA    
6746  C  C     . GLU   B 30  ? 0.3428 0.2088 0.4277 -0.0296 -0.0090 -0.0642 55  GLU   B C     
6747  O  O     . GLU   B 30  ? 0.3627 0.2127 0.4120 -0.0051 -0.0109 -0.0508 55  GLU   B O     
6748  C  CB    . GLU   B 30  ? 0.3469 0.2283 0.4567 -0.0086 -0.0039 -0.0619 55  GLU   B CB    
6749  C  CG    . GLU   B 30  ? 0.3607 0.2873 0.4931 -0.0319 -0.0139 -0.0445 55  GLU   B CG    
6750  C  CD    . GLU   B 30  ? 0.4404 0.3891 0.5191 0.0115  -0.0089 -0.0228 55  GLU   B CD    
6751  O  OE1   . GLU   B 30  ? 0.3952 0.3884 0.5309 0.0065  0.0238  0.0052  55  GLU   B OE1   
6752  O  OE2   . GLU   B 30  ? 0.5345 0.4598 0.5337 0.0343  -0.0231 -0.0153 55  GLU   B OE2   
6759  N  N     . LEU   B 31  ? 0.3515 0.2392 0.4558 -0.0220 -0.0237 -0.0704 56  LEU   B N     
6760  C  CA    . LEU   B 31  ? 0.3289 0.2681 0.4838 0.0057  -0.0245 -0.0909 56  LEU   B CA    
6761  C  C     . LEU   B 31  ? 0.3179 0.3266 0.4660 0.0757  -0.0089 -0.1080 56  LEU   B C     
6762  O  O     . LEU   B 31  ? 0.4073 0.3990 0.4699 0.1409  0.0060  -0.0968 56  LEU   B O     
6763  C  CB    . LEU   B 31  ? 0.3884 0.2880 0.5300 -0.0328 -0.0484 -0.0716 56  LEU   B CB    
6764  C  CG    . LEU   B 31  ? 0.4361 0.3123 0.5723 -0.0705 -0.0412 -0.0443 56  LEU   B CG    
6765  C  CD1   . LEU   B 31  ? 0.4867 0.3220 0.5921 -0.0704 -0.0540 -0.0489 56  LEU   B CD1   
6766  C  CD2   . LEU   B 31  ? 0.3850 0.3260 0.5843 -0.1238 -0.0368 -0.0151 56  LEU   B CD2   
6778  N  N     . VAL   B 32  ? 0.2271 0.2721 0.4368 0.0203  0.0197  -0.1395 57  VAL   B N     
6779  C  CA    A VAL   B 32  ? 0.2125 0.2980 0.4232 0.0030  0.0247  -0.1342 57  VAL   B CA    
6780  C  CA    B VAL   B 32  ? 0.2051 0.2901 0.4304 0.0037  0.0376  -0.1431 57  VAL   B CA    
6781  C  C     . VAL   B 32  ? 0.2142 0.3044 0.4129 -0.0057 0.0392  -0.1219 57  VAL   B C     
6782  O  O     . VAL   B 32  ? 0.1739 0.3286 0.3952 -0.0134 0.0518  -0.1066 57  VAL   B O     
6783  C  CB    A VAL   B 32  ? 0.2184 0.3323 0.4235 -0.0081 0.0205  -0.1321 57  VAL   B CB    
6784  C  CB    B VAL   B 32  ? 0.2067 0.3161 0.4444 -0.0104 0.0572  -0.1507 57  VAL   B CB    
6785  C  CG1   A VAL   B 32  ? 0.2397 0.3478 0.4218 -0.0004 0.0246  -0.1365 57  VAL   B CG1   
6786  C  CG1   B VAL   B 32  ? 0.2273 0.3295 0.4424 -0.0157 0.0533  -0.1684 57  VAL   B CG1   
6787  C  CG2   A VAL   B 32  ? 0.2091 0.3428 0.4199 -0.0295 0.0161  -0.1404 57  VAL   B CG2   
6788  C  CG2   B VAL   B 32  ? 0.1882 0.3120 0.4505 -0.0129 0.0879  -0.1652 57  VAL   B CG2   
6805  N  N     . THR   B 33  ? 0.2366 0.2999 0.4085 -0.0208 0.0453  -0.1358 58  THR   B N     
6806  C  CA    . THR   B 33  ? 0.2184 0.3209 0.4126 -0.0317 0.0364  -0.1330 58  THR   B CA    
6807  C  C     . THR   B 33  ? 0.2137 0.3566 0.4151 -0.0081 0.0557  -0.1251 58  THR   B C     
6808  O  O     . THR   B 33  ? 0.2276 0.3966 0.4177 -0.0119 0.0682  -0.1261 58  THR   B O     
6809  C  CB    . THR   B 33  ? 0.3016 0.3364 0.4239 -0.0175 0.0282  -0.1349 58  THR   B CB    
6810  O  OG1   . THR   B 33  ? 0.3360 0.3380 0.4385 -0.0357 0.0274  -0.1307 58  THR   B OG1   
6811  C  CG2   . THR   B 33  ? 0.3240 0.3632 0.4305 -0.0165 0.0252  -0.1213 58  THR   B CG2   
6819  N  N     . GLN   B 34  ? 0.2022 0.3527 0.4193 -0.0171 0.0677  -0.1242 59  GLN   B N     
6820  C  CA    . GLN   B 34  ? 0.1868 0.3446 0.4352 -0.0217 0.0339  -0.1204 59  GLN   B CA    
6821  C  C     . GLN   B 34  ? 0.1837 0.3347 0.4430 -0.0117 0.0396  -0.1100 59  GLN   B C     
6822  O  O     . GLN   B 34  ? 0.1555 0.3635 0.4354 -0.0144 0.0308  -0.0922 59  GLN   B O     
6823  C  CB    . GLN   B 34  ? 0.1864 0.3474 0.4438 -0.0158 0.0262  -0.1308 59  GLN   B CB    
6824  C  CG    . GLN   B 34  ? 0.1960 0.3346 0.4696 -0.0219 0.0207  -0.1380 59  GLN   B CG    
6825  C  CD    . GLN   B 34  ? 0.2024 0.3685 0.5062 -0.0015 0.0117  -0.1286 59  GLN   B CD    
6826  O  OE1   . GLN   B 34  ? 0.2186 0.3982 0.5442 -0.0098 0.0146  -0.1134 59  GLN   B OE1   
6827  N  NE2   . GLN   B 34  ? 0.2162 0.3524 0.5041 -0.0065 0.0195  -0.1416 59  GLN   B NE2   
6836  N  N     . GLN   B 35  ? 0.2193 0.3046 0.4665 0.0164  0.0251  -0.1052 60  GLN   B N     
6837  C  CA    . GLN   B 35  ? 0.2465 0.3157 0.4865 0.0195  0.0199  -0.1069 60  GLN   B CA    
6838  C  C     . GLN   B 35  ? 0.2462 0.3144 0.4804 -0.0035 0.0096  -0.0849 60  GLN   B C     
6839  O  O     . GLN   B 35  ? 0.2291 0.3046 0.5011 -0.0254 0.0053  -0.0706 60  GLN   B O     
6840  C  CB    . GLN   B 35  ? 0.2843 0.3500 0.5255 0.0137  0.0127  -0.1177 60  GLN   B CB    
6841  C  CG    . GLN   B 35  ? 0.4429 0.4414 0.5652 0.0140  0.0205  -0.1131 60  GLN   B CG    
6842  C  CD    . GLN   B 35  ? 0.5517 0.5197 0.6079 -0.0036 0.0536  -0.1044 60  GLN   B CD    
6843  O  OE1   . GLN   B 35  ? 0.6071 0.5481 0.6129 0.0028  0.1048  -0.1034 60  GLN   B OE1   
6844  N  NE2   . GLN   B 35  ? 0.5663 0.5597 0.6332 -0.0298 0.0462  -0.0882 60  GLN   B NE2   
6853  N  N     . MET   B 36  ? 0.1994 0.3031 0.4547 0.0176  0.0035  -0.0784 61  MET   B N     
6854  C  CA    . MET   B 36  ? 0.1982 0.2920 0.4431 0.0234  0.0239  -0.0535 61  MET   B CA    
6855  C  C     . MET   B 36  ? 0.1804 0.2901 0.4176 -0.0070 -0.0145 -0.0529 61  MET   B C     
6856  O  O     . MET   B 36  ? 0.1870 0.2903 0.4240 -0.0351 -0.0466 -0.0600 61  MET   B O     
6857  C  CB    . MET   B 36  ? 0.1650 0.2928 0.4613 0.0132  0.0384  -0.0169 61  MET   B CB    
6858  C  CG    . MET   B 36  ? 0.1528 0.2522 0.4968 -0.0038 0.0726  0.0040  61  MET   B CG    
6859  S  SD    . MET   B 36  ? 0.2540 0.3350 0.4907 0.0034  0.0149  -0.0679 61  MET   B SD    
6860  C  CE    . MET   B 36  ? 0.2234 0.2575 0.4691 -0.0289 0.0696  -0.1165 61  MET   B CE    
6870  N  N     . TRP   B 37  ? 0.1548 0.3071 0.4036 -0.0126 0.0001  -0.0459 62  TRP   B N     
6871  C  CA    . TRP   B 37  ? 0.1652 0.3002 0.4083 -0.0092 0.0121  -0.0537 62  TRP   B CA    
6872  C  C     . TRP   B 37  ? 0.1247 0.3111 0.4347 -0.0267 -0.0001 -0.0638 62  TRP   B C     
6873  O  O     . TRP   B 37  ? 0.1504 0.2933 0.4264 -0.0279 0.0054  -0.0605 62  TRP   B O     
6874  C  CB    . TRP   B 37  ? 0.1804 0.2967 0.4039 0.0172  0.0055  -0.0503 62  TRP   B CB    
6875  C  CG    . TRP   B 37  ? 0.1824 0.3163 0.4018 -0.0051 -0.0063 -0.0549 62  TRP   B CG    
6876  C  CD1   . TRP   B 37  ? 0.1633 0.3117 0.4000 -0.0278 0.0078  -0.0500 62  TRP   B CD1   
6877  C  CD2   . TRP   B 37  ? 0.1894 0.3501 0.4029 0.0058  -0.0239 -0.0509 62  TRP   B CD2   
6878  N  NE1   . TRP   B 37  ? 0.1842 0.3175 0.4107 -0.0209 -0.0095 -0.0426 62  TRP   B NE1   
6879  C  CE2   . TRP   B 37  ? 0.2276 0.3455 0.4023 -0.0235 -0.0338 -0.0483 62  TRP   B CE2   
6880  C  CE3   . TRP   B 37  ? 0.2248 0.3582 0.4036 0.0000  -0.0540 -0.0532 62  TRP   B CE3   
6881  C  CZ2   . TRP   B 37  ? 0.2541 0.3767 0.3965 -0.0315 -0.0649 -0.0502 62  TRP   B CZ2   
6882  C  CZ3   . TRP   B 37  ? 0.2353 0.3715 0.3993 0.0054  -0.0796 -0.0581 62  TRP   B CZ3   
6883  C  CH2   . TRP   B 37  ? 0.2539 0.3729 0.4001 -0.0338 -0.0652 -0.0546 62  TRP   B CH2   
6894  N  N     . VAL   B 38  ? 0.1371 0.3183 0.4726 -0.0341 -0.0173 -0.0599 63  VAL   B N     
6895  C  CA    . VAL   B 38  ? 0.1362 0.3085 0.5085 -0.0198 -0.0219 -0.0553 63  VAL   B CA    
6896  C  C     . VAL   B 38  ? 0.1425 0.3108 0.5479 -0.0027 -0.0135 -0.0632 63  VAL   B C     
6897  O  O     . VAL   B 38  ? 0.1595 0.3280 0.5687 -0.0141 -0.0155 -0.0679 63  VAL   B O     
6898  C  CB    . VAL   B 38  ? 0.1450 0.3013 0.5317 -0.0337 -0.0161 -0.0490 63  VAL   B CB    
6899  C  CG1   . VAL   B 38  ? 0.1901 0.2811 0.5478 -0.0177 0.0036  -0.0314 63  VAL   B CG1   
6900  C  CG2   . VAL   B 38  ? 0.1565 0.3312 0.5428 -0.0063 -0.0432 -0.0520 63  VAL   B CG2   
6910  N  N     . TYR   B 39  ? 0.1446 0.2882 0.5583 -0.0066 0.0040  -0.0665 64  TYR   B N     
6911  C  CA    . TYR   B 39  ? 0.1555 0.2912 0.5877 -0.0211 0.0110  -0.0740 64  TYR   B CA    
6912  C  C     . TYR   B 39  ? 0.1634 0.3221 0.6124 -0.0290 0.0147  -0.0704 64  TYR   B C     
6913  O  O     . TYR   B 39  ? 0.1726 0.3258 0.6166 -0.0419 0.0156  -0.0706 64  TYR   B O     
6914  C  CB    . TYR   B 39  ? 0.1611 0.3107 0.6191 -0.0148 -0.0027 -0.0700 64  TYR   B CB    
6915  C  CG    . TYR   B 39  ? 0.1654 0.3250 0.6371 -0.0208 0.0214  -0.0473 64  TYR   B CG    
6916  C  CD1   . TYR   B 39  ? 0.1770 0.3498 0.6830 -0.0114 0.0113  -0.0381 64  TYR   B CD1   
6917  C  CD2   . TYR   B 39  ? 0.1723 0.3217 0.6711 0.0180  0.0103  -0.0381 64  TYR   B CD2   
6918  C  CE1   . TYR   B 39  ? 0.1814 0.3428 0.7106 0.0168  0.0148  -0.0277 64  TYR   B CE1   
6919  C  CE2   . TYR   B 39  ? 0.1814 0.3309 0.7109 0.0183  0.0034  -0.0273 64  TYR   B CE2   
6920  C  CZ    . TYR   B 39  ? 0.1910 0.3308 0.7300 0.0324  0.0107  -0.0126 64  TYR   B CZ    
6921  O  OH    . TYR   B 39  ? 0.1918 0.3409 0.7606 0.0092  0.0100  0.0032  64  TYR   B OH    
6931  N  N     . ASP   B 40  ? 0.1629 0.3437 0.6223 -0.0122 0.0142  -0.0796 65  ASP   B N     
6932  C  CA    . ASP   B 40  ? 0.1728 0.3443 0.6363 -0.0278 0.0322  -0.0945 65  ASP   B CA    
6933  C  C     . ASP   B 40  ? 0.1741 0.3740 0.6581 -0.0169 0.0255  -0.0873 65  ASP   B C     
6934  O  O     . ASP   B 40  ? 0.1713 0.3957 0.6470 -0.0278 0.0263  -0.0664 65  ASP   B O     
6935  C  CB    . ASP   B 40  ? 0.1711 0.3568 0.6411 -0.0146 0.0268  -0.0972 65  ASP   B CB    
6936  C  CG    . ASP   B 40  ? 0.1716 0.3725 0.6436 -0.0011 -0.0061 -0.1097 65  ASP   B CG    
6937  O  OD1   . ASP   B 40  ? 0.1751 0.3786 0.6424 -0.0006 -0.0130 -0.1289 65  ASP   B OD1   
6938  O  OD2   . ASP   B 40  ? 0.1756 0.3832 0.6491 0.0305  -0.0166 -0.0957 65  ASP   B OD2   
6943  N  N     . GLU   B 41  ? 0.1736 0.4084 0.6360 -0.0016 0.0530  -0.0791 66  GLU   B N     
6944  C  CA    . GLU   B 41  ? 0.1836 0.4826 0.6785 -0.0382 0.0351  -0.0725 66  GLU   B CA    
6945  C  C     . GLU   B 41  ? 0.1849 0.4695 0.7024 -0.0267 0.0097  -0.0772 66  GLU   B C     
6946  O  O     . GLU   B 41  ? 0.1830 0.4558 0.6948 -0.0171 0.0356  -0.0697 66  GLU   B O     
6947  C  CB    . GLU   B 41  ? 0.1984 0.6095 0.7121 -0.0356 0.0504  -0.0720 66  GLU   B CB    
6948  C  CG    . GLU   B 41  ? 0.2608 0.6673 0.7459 -0.0191 0.0255  -0.0767 66  GLU   B CG    
6949  C  CD    . GLU   B 41  ? 0.2473 0.6783 0.7646 0.0107  0.0189  -0.0843 66  GLU   B CD    
6950  O  OE1   . GLU   B 41  ? 0.2371 0.6894 0.7697 0.0326  0.0009  -0.0990 66  GLU   B OE1   
6951  O  OE2   . GLU   B 41  ? 0.2650 0.6762 0.7736 0.0585  0.0297  -0.0841 66  GLU   B OE2   
6958  N  N     . ASP   B 42  ? 0.1901 0.4884 0.7153 -0.0194 -0.0202 -0.0894 67  ASP   B N     
6959  C  CA    . ASP   B 42  ? 0.2040 0.4980 0.7411 -0.0283 -0.0460 -0.0990 67  ASP   B CA    
6960  C  C     . ASP   B 42  ? 0.2201 0.5448 0.7396 -0.0057 -0.0664 -0.0838 67  ASP   B C     
6961  O  O     . ASP   B 42  ? 0.2327 0.6025 0.7505 0.0390  -0.0895 -0.0781 67  ASP   B O     
6962  C  CB    . ASP   B 42  ? 0.2300 0.4874 0.7738 -0.0445 -0.0621 -0.1178 67  ASP   B CB    
6963  C  CG    . ASP   B 42  ? 0.3013 0.4688 0.8063 -0.0426 -0.0688 -0.1302 67  ASP   B CG    
6964  O  OD1   . ASP   B 42  ? 0.2830 0.4471 0.8233 -0.0425 -0.0555 -0.1292 67  ASP   B OD1   
6965  O  OD2   . ASP   B 42  ? 0.3805 0.4940 0.8208 -0.0087 -0.0695 -0.1201 67  ASP   B OD2   
6970  N  N     . VAL   B 43  ? 0.2076 0.5147 0.7317 -0.0508 -0.0628 -0.0664 68  VAL   B N     
6971  C  CA    A VAL   B 43  ? 0.2291 0.5045 0.7256 -0.0437 -0.0507 -0.0539 68  VAL   B CA    
6972  C  CA    B VAL   B 43  ? 0.2301 0.5124 0.7287 -0.0489 -0.0579 -0.0784 68  VAL   B CA    
6973  C  C     . VAL   B 43  ? 0.2274 0.4912 0.7175 -0.0310 -0.0431 -0.0461 68  VAL   B C     
6974  O  O     . VAL   B 43  ? 0.3075 0.5119 0.7363 -0.0452 -0.0355 -0.0177 68  VAL   B O     
6975  C  CB    A VAL   B 43  ? 0.2505 0.5076 0.7231 -0.0449 -0.0473 -0.0524 68  VAL   B CB    
6976  C  CB    B VAL   B 43  ? 0.2398 0.5213 0.7268 -0.0439 -0.0679 -0.1152 68  VAL   B CB    
6977  C  CG1   A VAL   B 43  ? 0.2574 0.5088 0.7221 -0.0443 -0.0461 -0.0518 68  VAL   B CG1   
6978  C  CG1   B VAL   B 43  ? 0.2570 0.5166 0.7270 -0.0375 -0.0753 -0.1336 68  VAL   B CG1   
6979  C  CG2   A VAL   B 43  ? 0.2600 0.5083 0.7218 -0.0458 -0.0467 -0.0526 68  VAL   B CG2   
6980  C  CG2   B VAL   B 43  ? 0.2226 0.5162 0.7201 -0.0373 -0.0821 -0.1292 68  VAL   B CG2   
6999  N  N     . GLY   B 44  ? 0.1762 0.4289 0.6770 -0.0135 -0.0327 -0.0503 69  GLY   B N     
7000  C  CA    . GLY   B 44  ? 0.1757 0.4160 0.6463 -0.0240 -0.0498 -0.0582 69  GLY   B CA    
7001  C  C     . GLY   B 44  ? 0.1650 0.3709 0.6291 0.0042  -0.0352 -0.0620 69  GLY   B C     
7002  O  O     . GLY   B 44  ? 0.1710 0.2997 0.6420 -0.0101 -0.0195 -0.0959 69  GLY   B O     
7006  N  N     . ILE   B 45  ? 0.1642 0.4086 0.6125 -0.0117 -0.0510 -0.0427 70  ILE   B N     
7007  C  CA    . ILE   B 45  ? 0.1609 0.4101 0.6053 -0.0175 -0.0432 -0.0391 70  ILE   B CA    
7008  C  C     . ILE   B 45  ? 0.1728 0.4104 0.5904 -0.0092 -0.0652 -0.0469 70  ILE   B C     
7009  O  O     . ILE   B 45  ? 0.1981 0.4252 0.6062 0.0118  -0.0666 -0.0519 70  ILE   B O     
7010  C  CB    . ILE   B 45  ? 0.1884 0.4126 0.6135 0.0029  -0.0149 -0.0240 70  ILE   B CB    
7011  C  CG1   . ILE   B 45  ? 0.2135 0.4226 0.6098 0.0047  -0.0233 -0.0128 70  ILE   B CG1   
7012  C  CG2   . ILE   B 45  ? 0.1802 0.4187 0.6212 0.0246  0.0179  -0.0160 70  ILE   B CG2   
7013  C  CD1   . ILE   B 45  ? 0.2273 0.4366 0.6056 -0.0351 -0.0174 -0.0109 70  ILE   B CD1   
7025  N  N     . ASN   B 46  ? 0.1521 0.3945 0.5522 -0.0065 -0.0555 -0.0480 71  ASN   B N     
7026  C  CA    . ASN   B 46  ? 0.1748 0.3767 0.5332 -0.0220 -0.0651 -0.0515 71  ASN   B CA    
7027  C  C     . ASN   B 46  ? 0.1691 0.3687 0.4896 -0.0273 -0.0486 -0.0636 71  ASN   B C     
7028  O  O     . ASN   B 46  ? 0.1650 0.3680 0.4897 -0.0066 -0.0514 -0.0612 71  ASN   B O     
7029  C  CB    . ASN   B 46  ? 0.1768 0.3803 0.5542 -0.0365 -0.0826 -0.0514 71  ASN   B CB    
7030  C  CG    . ASN   B 46  ? 0.2152 0.3718 0.5703 -0.0412 -0.0662 -0.0657 71  ASN   B CG    
7031  O  OD1   . ASN   B 46  ? 0.2542 0.3781 0.5808 -0.0384 -0.0307 -0.0736 71  ASN   B OD1   
7032  N  ND2   . ASN   B 46  ? 0.1891 0.3514 0.5715 -0.0005 -0.0792 -0.0739 71  ASN   B ND2   
7039  N  N     . TYR   B 47  ? 0.1727 0.3698 0.4603 -0.0248 -0.0503 -0.0687 72  TYR   B N     
7040  C  CA    . TYR   B 47  ? 0.1853 0.3496 0.4431 -0.0407 -0.0408 -0.0658 72  TYR   B CA    
7041  C  C     . TYR   B 47  ? 0.2227 0.3204 0.4398 -0.0246 -0.0371 -0.0939 72  TYR   B C     
7042  O  O     . TYR   B 47  ? 0.2573 0.3571 0.4414 -0.0293 -0.0431 -0.0925 72  TYR   B O     
7043  C  CB    . TYR   B 47  ? 0.2035 0.3732 0.4493 -0.0259 -0.0163 -0.0538 72  TYR   B CB    
7044  C  CG    . TYR   B 47  ? 0.1925 0.3874 0.4573 -0.0234 -0.0008 -0.0551 72  TYR   B CG    
7045  C  CD1   . TYR   B 47  ? 0.1914 0.4012 0.4552 -0.0318 -0.0222 -0.0505 72  TYR   B CD1   
7046  C  CD2   . TYR   B 47  ? 0.2537 0.4033 0.4704 -0.0156 0.0048  -0.0489 72  TYR   B CD2   
7047  C  CE1   . TYR   B 47  ? 0.2133 0.3881 0.4708 -0.0061 0.0139  -0.0512 72  TYR   B CE1   
7048  C  CE2   . TYR   B 47  ? 0.2091 0.3789 0.4775 -0.0305 0.0186  -0.0523 72  TYR   B CE2   
7049  C  CZ    . TYR   B 47  ? 0.2180 0.3949 0.4856 -0.0138 0.0273  -0.0474 72  TYR   B CZ    
7050  O  OH    . TYR   B 47  ? 0.2247 0.4091 0.4957 -0.0106 0.0440  -0.0646 72  TYR   B OH    
7060  N  N     . ARG   B 48  ? 0.2080 0.3203 0.4530 -0.0150 -0.0264 -0.1023 73  ARG   B N     
7061  C  CA    . ARG   B 48  ? 0.1936 0.3079 0.4703 -0.0165 -0.0116 -0.1065 73  ARG   B CA    
7062  C  C     . ARG   B 48  ? 0.2018 0.2937 0.4614 -0.0057 -0.0026 -0.1030 73  ARG   B C     
7063  O  O     . ARG   B 48  ? 0.2181 0.2794 0.4614 -0.0071 -0.0079 -0.1112 73  ARG   B O     
7064  C  CB    . ARG   B 48  ? 0.1889 0.3210 0.4936 -0.0245 -0.0016 -0.1049 73  ARG   B CB    
7065  C  CG    . ARG   B 48  ? 0.1864 0.3293 0.5124 -0.0385 0.0114  -0.1098 73  ARG   B CG    
7066  C  CD    . ARG   B 48  ? 0.2001 0.3382 0.5340 -0.0610 0.0051  -0.1003 73  ARG   B CD    
7067  N  NE    . ARG   B 48  ? 0.2127 0.3582 0.5448 -0.0348 0.0008  -0.0977 73  ARG   B NE    
7068  C  CZ    . ARG   B 48  ? 0.2092 0.3744 0.5483 0.0108  0.0018  -0.1031 73  ARG   B CZ    
7069  N  NH1   . ARG   B 48  ? 0.2257 0.3729 0.5471 0.0430  -0.0177 -0.0945 73  ARG   B NH1   
7070  N  NH2   . ARG   B 48  ? 0.1794 0.3805 0.5547 0.0343  0.0253  -0.1122 73  ARG   B NH2   
7084  N  N     . GLU   B 49  ? 0.2174 0.3062 0.4625 -0.0097 -0.0023 -0.0954 74  GLU   B N     
7085  C  CA    . GLU   B 49  ? 0.2148 0.3228 0.4794 -0.0057 -0.0075 -0.0956 74  GLU   B CA    
7086  C  C     . GLU   B 49  ? 0.2124 0.3182 0.4645 -0.0161 -0.0075 -0.0839 74  GLU   B C     
7087  O  O     . GLU   B 49  ? 0.2406 0.3328 0.4557 -0.0319 -0.0257 -0.0959 74  GLU   B O     
7088  C  CB    . GLU   B 49  ? 0.2369 0.3222 0.5091 -0.0096 -0.0196 -0.1073 74  GLU   B CB    
7089  C  CG    . GLU   B 49  ? 0.3383 0.3540 0.5412 0.0394  -0.0366 -0.1292 74  GLU   B CG    
7090  C  CD    . GLU   B 49  ? 0.4744 0.4139 0.5732 0.0747  -0.0619 -0.1434 74  GLU   B CD    
7091  O  OE1   . GLU   B 49  ? 0.5388 0.4091 0.5973 0.0586  -0.1147 -0.1462 74  GLU   B OE1   
7092  O  OE2   . GLU   B 49  ? 0.5384 0.4644 0.5747 0.1335  -0.0256 -0.1592 74  GLU   B OE2   
7099  N  N     . VAL   B 50  ? 0.2236 0.3202 0.4612 -0.0201 -0.0013 -0.0751 75  VAL   B N     
7100  C  CA    A VAL   B 50  ? 0.2103 0.3193 0.4602 -0.0147 0.0022  -0.0620 75  VAL   B CA    
7101  C  CA    B VAL   B 50  ? 0.2112 0.3410 0.4640 -0.0059 0.0019  -0.0687 75  VAL   B CA    
7102  C  C     . VAL   B 50  ? 0.1959 0.3321 0.4554 -0.0145 0.0139  -0.0565 75  VAL   B C     
7103  O  O     . VAL   B 50  ? 0.1701 0.3869 0.4514 -0.0168 0.0138  -0.0401 75  VAL   B O     
7104  C  CB    A VAL   B 50  ? 0.2673 0.3298 0.4624 -0.0122 0.0053  -0.0632 75  VAL   B CB    
7105  C  CB    B VAL   B 50  ? 0.2405 0.3818 0.4754 0.0160  -0.0016 -0.0783 75  VAL   B CB    
7106  C  CG1   A VAL   B 50  ? 0.3206 0.3818 0.4782 0.0352  0.0027  -0.0519 75  VAL   B CG1   
7107  C  CG1   B VAL   B 50  ? 0.2481 0.3867 0.4776 0.0120  0.0020  -0.0861 75  VAL   B CG1   
7108  C  CG2   A VAL   B 50  ? 0.2843 0.2594 0.4475 -0.0801 0.0269  -0.0819 75  VAL   B CG2   
7109  C  CG2   B VAL   B 50  ? 0.2794 0.4059 0.4841 0.0394  -0.0039 -0.0787 75  VAL   B CG2   
7128  N  N     . THR   B 51  ? 0.1896 0.3001 0.4585 -0.0265 0.0339  -0.0763 76  THR   B N     
7129  C  CA    . THR   B 51  ? 0.2366 0.2741 0.4526 -0.0797 0.0495  -0.0947 76  THR   B CA    
7130  C  C     . THR   B 51  ? 0.2316 0.2649 0.4267 -0.0855 0.0883  -0.1000 76  THR   B C     
7131  O  O     . THR   B 51  ? 0.2346 0.3180 0.4408 -0.0686 0.0954  -0.1056 76  THR   B O     
7132  C  CB    . THR   B 51  ? 0.2825 0.2936 0.4737 -0.0729 0.0429  -0.1212 76  THR   B CB    
7133  O  OG1   . THR   B 51  ? 0.2832 0.3233 0.4842 -0.0281 0.0319  -0.1569 76  THR   B OG1   
7134  C  CG2   . THR   B 51  ? 0.2892 0.2997 0.4846 -0.0527 0.0565  -0.0990 76  THR   B CG2   
7142  N  N     . PHE   B 52  ? 0.2215 0.2282 0.3875 -0.0584 0.0950  -0.0951 77  PHE   B N     
7143  C  CA    . PHE   B 52  ? 0.2433 0.2169 0.3709 -0.0208 0.0742  -0.0766 77  PHE   B CA    
7144  C  C     . PHE   B 52  ? 0.2213 0.2357 0.3509 -0.0131 0.0915  -0.0567 77  PHE   B C     
7145  O  O     . PHE   B 52  ? 0.2039 0.2552 0.3475 -0.0173 0.0730  -0.0417 77  PHE   B O     
7146  C  CB    . PHE   B 52  ? 0.2428 0.2301 0.3682 -0.0158 0.0702  -0.0593 77  PHE   B CB    
7147  C  CG    . PHE   B 52  ? 0.2310 0.2307 0.3540 -0.0269 0.0597  -0.0378 77  PHE   B CG    
7148  C  CD1   . PHE   B 52  ? 0.2198 0.2560 0.3640 -0.0170 0.0442  -0.0401 77  PHE   B CD1   
7149  C  CD2   . PHE   B 52  ? 0.2154 0.2191 0.3367 -0.0270 0.0442  -0.0146 77  PHE   B CD2   
7150  C  CE1   . PHE   B 52  ? 0.2623 0.2721 0.3731 -0.0240 0.0459  -0.0519 77  PHE   B CE1   
7151  C  CE2   . PHE   B 52  ? 0.2401 0.2334 0.3489 -0.0028 0.0513  -0.0293 77  PHE   B CE2   
7152  C  CZ    . PHE   B 52  ? 0.2564 0.2555 0.3689 -0.0198 0.0413  -0.0431 77  PHE   B CZ    
7162  N  N     . VAL   B 53  ? 0.2616 0.2220 0.3468 -0.0157 0.0920  -0.0536 78  VAL   B N     
7163  C  CA    . VAL   B 53  ? 0.2592 0.2066 0.3321 -0.0222 0.0700  -0.0409 78  VAL   B CA    
7164  C  C     . VAL   B 53  ? 0.2509 0.2065 0.3087 -0.0180 0.0845  -0.0426 78  VAL   B C     
7165  O  O     . VAL   B 53  ? 0.2749 0.1998 0.3041 -0.0287 0.0930  -0.0279 78  VAL   B O     
7166  C  CB    . VAL   B 53  ? 0.2770 0.2112 0.3611 -0.0265 0.0534  -0.0254 78  VAL   B CB    
7167  C  CG1   . VAL   B 53  ? 0.2895 0.2350 0.3753 -0.0377 0.0490  -0.0238 78  VAL   B CG1   
7168  C  CG2   . VAL   B 53  ? 0.3081 0.2233 0.3774 -0.0289 0.0388  -0.0197 78  VAL   B CG2   
7178  N  N     . PRO   B 54  ? 0.2308 0.2159 0.3005 -0.0166 0.0864  -0.0376 79  PRO   B N     
7179  C  CA    . PRO   B 54  ? 0.2256 0.1996 0.2886 -0.0262 0.0985  -0.0396 79  PRO   B CA    
7180  C  C     . PRO   B 54  ? 0.2647 0.1846 0.2793 -0.0201 0.0848  -0.0321 79  PRO   B C     
7181  O  O     . PRO   B 54  ? 0.2542 0.2027 0.2768 0.0097  0.0725  -0.0285 79  PRO   B O     
7182  C  CB    . PRO   B 54  ? 0.2043 0.2218 0.2905 -0.0277 0.0874  -0.0434 79  PRO   B CB    
7183  C  CG    . PRO   B 54  ? 0.2166 0.2374 0.2904 -0.0194 0.0897  -0.0354 79  PRO   B CG    
7184  C  CD    . PRO   B 54  ? 0.2070 0.2314 0.2847 -0.0221 0.1003  -0.0451 79  PRO   B CD    
7192  N  N     . GLY   B 55  ? 0.2882 0.1860 0.2765 -0.0155 0.0833  -0.0244 80  GLY   B N     
7193  C  CA    . GLY   B 55  ? 0.2880 0.1982 0.2758 -0.0146 0.0882  -0.0193 80  GLY   B CA    
7194  C  C     . GLY   B 55  ? 0.2849 0.1997 0.2913 -0.0122 0.0915  -0.0281 80  GLY   B C     
7195  O  O     . GLY   B 55  ? 0.2755 0.2059 0.2871 -0.0213 0.0978  -0.0200 80  GLY   B O     
7199  N  N     . LEU   B 56  ? 0.2873 0.2036 0.3173 -0.0282 0.0910  -0.0197 81  LEU   B N     
7200  C  CA    . LEU   B 56  ? 0.2695 0.2206 0.3439 -0.0669 0.1189  -0.0246 81  LEU   B CA    
7201  C  C     . LEU   B 56  ? 0.2564 0.2094 0.3405 -0.0076 0.1452  -0.0374 81  LEU   B C     
7202  O  O     . LEU   B 56  ? 0.2775 0.2271 0.3639 0.0094  0.1427  -0.0255 81  LEU   B O     
7203  C  CB    . LEU   B 56  ? 0.2801 0.2345 0.3799 -0.0796 0.1250  -0.0214 81  LEU   B CB    
7204  C  CG    . LEU   B 56  ? 0.3209 0.2574 0.4018 -0.1003 0.1519  -0.0347 81  LEU   B CG    
7205  C  CD1   . LEU   B 56  ? 0.3600 0.2929 0.4030 -0.0763 0.1694  -0.0282 81  LEU   B CD1   
7206  C  CD2   . LEU   B 56  ? 0.3733 0.2787 0.4269 -0.1044 0.1495  -0.0387 81  LEU   B CD2   
7218  N  N     . TYR   B 57  ? 0.2699 0.2149 0.3297 -0.0027 0.1284  -0.0376 82  TYR   B N     
7219  C  CA    . TYR   B 57  ? 0.2306 0.2041 0.3235 -0.0077 0.1102  -0.0286 82  TYR   B CA    
7220  C  C     . TYR   B 57  ? 0.2346 0.2087 0.3110 -0.0183 0.0952  -0.0210 82  TYR   B C     
7221  O  O     . TYR   B 57  ? 0.2447 0.2111 0.3337 -0.0018 0.0814  -0.0378 82  TYR   B O     
7222  C  CB    . TYR   B 57  ? 0.1925 0.2091 0.3373 -0.0045 0.0898  -0.0286 82  TYR   B CB    
7223  C  CG    . TYR   B 57  ? 0.1470 0.2107 0.3686 -0.0045 0.0754  -0.0191 82  TYR   B CG    
7224  C  CD1   . TYR   B 57  ? 0.1463 0.2436 0.3828 -0.0065 0.0747  -0.0107 82  TYR   B CD1   
7225  C  CD2   . TYR   B 57  ? 0.1661 0.2390 0.3829 -0.0038 0.0919  -0.0174 82  TYR   B CD2   
7226  C  CE1   . TYR   B 57  ? 0.1724 0.2569 0.3947 0.0068  0.0869  -0.0125 82  TYR   B CE1   
7227  C  CE2   . TYR   B 57  ? 0.1940 0.2634 0.3924 0.0105  0.0915  -0.0059 82  TYR   B CE2   
7228  C  CZ    . TYR   B 57  ? 0.1981 0.2464 0.4049 0.0168  0.0772  0.0024  82  TYR   B CZ    
7229  O  OH    . TYR   B 57  ? 0.2395 0.2865 0.4192 0.0455  0.0693  -0.0027 82  TYR   B OH    
7239  N  N     . LYS   B 58  ? 0.2362 0.2088 0.2747 -0.0129 0.0860  -0.0249 83  LYS   B N     
7240  C  CA    . LYS   B 58  ? 0.2374 0.2033 0.2627 -0.0218 0.1029  -0.0307 83  LYS   B CA    
7241  C  C     . LYS   B 58  ? 0.2926 0.1964 0.2706 -0.0199 0.1097  -0.0110 83  LYS   B C     
7242  O  O     . LYS   B 58  ? 0.2874 0.1924 0.2996 -0.0269 0.1346  -0.0241 83  LYS   B O     
7243  C  CB    . LYS   B 58  ? 0.2256 0.2017 0.2691 -0.0185 0.0977  -0.0247 83  LYS   B CB    
7244  C  CG    . LYS   B 58  ? 0.2452 0.2154 0.2926 -0.0217 0.0791  -0.0112 83  LYS   B CG    
7245  C  CD    . LYS   B 58  ? 0.2781 0.2340 0.3258 -0.0120 0.0814  -0.0045 83  LYS   B CD    
7246  C  CE    . LYS   B 58  ? 0.2469 0.2507 0.3538 -0.0176 0.0836  0.0303  83  LYS   B CE    
7247  N  NZ    . LYS   B 58  ? 0.2269 0.2899 0.3757 -0.0172 0.0698  0.0719  83  LYS   B NZ    
7261  N  N     . ILE   B 59  ? 0.2943 0.2044 0.2760 -0.0203 0.1308  -0.0061 84  ILE   B N     
7262  C  CA    . ILE   B 59  ? 0.3138 0.2428 0.2845 0.0057  0.1388  -0.0020 84  ILE   B CA    
7263  C  C     . ILE   B 59  ? 0.3388 0.2400 0.3087 0.0092  0.1543  -0.0144 84  ILE   B C     
7264  O  O     . ILE   B 59  ? 0.3589 0.2335 0.3182 0.0174  0.1654  -0.0369 84  ILE   B O     
7265  C  CB    . ILE   B 59  ? 0.3410 0.2525 0.3066 -0.0370 0.1291  -0.0089 84  ILE   B CB    
7266  C  CG1   . ILE   B 59  ? 0.3734 0.2663 0.3148 -0.0630 0.1490  0.0168  84  ILE   B CG1   
7267  C  CG2   . ILE   B 59  ? 0.3712 0.2248 0.3070 -0.0078 0.1211  -0.0167 84  ILE   B CG2   
7268  C  CD1   . ILE   B 59  ? 0.4338 0.2746 0.3258 -0.0835 0.1376  0.0012  84  ILE   B CD1   
7280  N  N     . PHE   B 60  ? 0.2969 0.2254 0.3356 -0.0158 0.1464  -0.0131 85  PHE   B N     
7281  C  CA    . PHE   B 60  ? 0.3157 0.2232 0.3475 -0.0222 0.1391  -0.0385 85  PHE   B CA    
7282  C  C     . PHE   B 60  ? 0.2933 0.2139 0.3498 -0.0164 0.1561  -0.0303 85  PHE   B C     
7283  O  O     . PHE   B 60  ? 0.3009 0.2247 0.3682 -0.0103 0.1467  -0.0275 85  PHE   B O     
7284  C  CB    . PHE   B 60  ? 0.2877 0.2153 0.3676 -0.0191 0.1157  -0.0441 85  PHE   B CB    
7285  C  CG    . PHE   B 60  ? 0.2794 0.2479 0.3764 -0.0202 0.1376  -0.0416 85  PHE   B CG    
7286  C  CD1   . PHE   B 60  ? 0.2721 0.2848 0.4007 -0.0221 0.1176  -0.0389 85  PHE   B CD1   
7287  C  CD2   . PHE   B 60  ? 0.2819 0.2733 0.3841 -0.0168 0.1551  -0.0524 85  PHE   B CD2   
7288  C  CE1   . PHE   B 60  ? 0.2875 0.2905 0.4022 -0.0294 0.1277  -0.0304 85  PHE   B CE1   
7289  C  CE2   . PHE   B 60  ? 0.2690 0.2898 0.3909 -0.0087 0.1472  -0.0431 85  PHE   B CE2   
7290  C  CZ    . PHE   B 60  ? 0.2896 0.2954 0.3989 -0.0168 0.1420  -0.0369 85  PHE   B CZ    
7300  N  N     . ASP   B 61  ? 0.2621 0.2060 0.3389 -0.0170 0.1601  -0.0200 86  ASP   B N     
7301  C  CA    . ASP   B 61  ? 0.2593 0.2144 0.3374 -0.0057 0.1254  -0.0134 86  ASP   B CA    
7302  C  C     . ASP   B 61  ? 0.2608 0.2120 0.3352 -0.0065 0.1184  -0.0191 86  ASP   B C     
7303  O  O     . ASP   B 61  ? 0.2521 0.2122 0.3421 -0.0031 0.1165  -0.0198 86  ASP   B O     
7304  C  CB    . ASP   B 61  ? 0.2413 0.2085 0.3400 -0.0013 0.1075  -0.0142 86  ASP   B CB    
7305  C  CG    . ASP   B 61  ? 0.2586 0.2415 0.3506 0.0039  0.0732  -0.0204 86  ASP   B CG    
7306  O  OD1   . ASP   B 61  ? 0.2912 0.2415 0.3518 0.0205  0.0710  -0.0314 86  ASP   B OD1   
7307  O  OD2   . ASP   B 61  ? 0.2548 0.2540 0.3633 -0.0005 0.0730  -0.0129 86  ASP   B OD2   
7312  N  N     . GLU   B 62  ? 0.2550 0.1961 0.3287 -0.0064 0.1291  -0.0251 87  GLU   B N     
7313  C  CA    . GLU   B 62  ? 0.2824 0.1952 0.3227 -0.0017 0.1086  -0.0384 87  GLU   B CA    
7314  C  C     . GLU   B 62  ? 0.2691 0.2081 0.3352 -0.0140 0.1304  -0.0476 87  GLU   B C     
7315  O  O     . GLU   B 62  ? 0.2960 0.2092 0.3362 -0.0306 0.1342  -0.0571 87  GLU   B O     
7316  C  CB    . GLU   B 62  ? 0.2859 0.1956 0.3093 -0.0009 0.1063  -0.0282 87  GLU   B CB    
7317  C  CG    . GLU   B 62  ? 0.2612 0.2075 0.3096 -0.0001 0.1187  -0.0305 87  GLU   B CG    
7318  C  CD    . GLU   B 62  ? 0.3076 0.2254 0.3375 0.0287  0.0988  -0.0478 87  GLU   B CD    
7319  O  OE1   . GLU   B 62  ? 0.3490 0.2570 0.3851 0.0396  0.0789  -0.0438 87  GLU   B OE1   
7320  O  OE2   . GLU   B 62  ? 0.3065 0.2660 0.3237 0.0210  0.0918  -0.0633 87  GLU   B OE2   
7327  N  N     . ILE   B 63  ? 0.2521 0.2207 0.3538 -0.0271 0.1579  -0.0485 88  ILE   B N     
7328  C  CA    . ILE   B 63  ? 0.2971 0.2460 0.3882 -0.0191 0.1808  -0.0501 88  ILE   B CA    
7329  C  C     . ILE   B 63  ? 0.2971 0.2507 0.3970 -0.0225 0.1744  -0.0591 88  ILE   B C     
7330  O  O     . ILE   B 63  ? 0.3004 0.2643 0.4138 -0.0125 0.1841  -0.0664 88  ILE   B O     
7331  C  CB    . ILE   B 63  ? 0.3349 0.2506 0.3985 -0.0061 0.2052  -0.0556 88  ILE   B CB    
7332  C  CG1   . ILE   B 63  ? 0.3506 0.2362 0.3940 -0.0075 0.1928  -0.0532 88  ILE   B CG1   
7333  C  CG2   . ILE   B 63  ? 0.3258 0.2601 0.4093 -0.0004 0.2001  -0.0683 88  ILE   B CG2   
7334  C  CD1   . ILE   B 63  ? 0.3941 0.2206 0.3953 0.0009  0.1773  -0.0367 88  ILE   B CD1   
7346  N  N     . LEU   B 64  ? 0.2783 0.2507 0.3860 -0.0258 0.1512  -0.0572 89  LEU   B N     
7347  C  CA    . LEU   B 64  ? 0.2520 0.2672 0.3978 -0.0046 0.1399  -0.0528 89  LEU   B CA    
7348  C  C     . LEU   B 64  ? 0.2202 0.2629 0.3908 0.0062  0.1469  -0.0477 89  LEU   B C     
7349  O  O     . LEU   B 64  ? 0.2738 0.2599 0.4165 0.0130  0.1424  -0.0505 89  LEU   B O     
7350  C  CB    . LEU   B 64  ? 0.2754 0.3031 0.4212 0.0067  0.1455  -0.0629 89  LEU   B CB    
7351  C  CG    . LEU   B 64  ? 0.2378 0.3311 0.4489 0.0114  0.1294  -0.0616 89  LEU   B CG    
7352  C  CD1   . LEU   B 64  ? 0.2069 0.3627 0.4719 0.0185  0.1102  -0.0398 89  LEU   B CD1   
7353  C  CD2   . LEU   B 64  ? 0.2954 0.3593 0.4600 -0.0274 0.1041  -0.0664 89  LEU   B CD2   
7365  N  N     . VAL   B 65  ? 0.2163 0.2532 0.3607 -0.0090 0.1255  -0.0410 90  VAL   B N     
7366  C  CA    . VAL   B 65  ? 0.2354 0.2386 0.3271 0.0161  0.1297  -0.0300 90  VAL   B CA    
7367  C  C     . VAL   B 65  ? 0.2557 0.2111 0.3351 0.0002  0.1339  -0.0410 90  VAL   B C     
7368  O  O     . VAL   B 65  ? 0.2768 0.2055 0.3504 0.0274  0.1170  -0.0460 90  VAL   B O     
7369  C  CB    . VAL   B 65  ? 0.2271 0.2460 0.2938 -0.0050 0.1314  -0.0225 90  VAL   B CB    
7370  C  CG1   . VAL   B 65  ? 0.2398 0.2582 0.3017 0.0203  0.0956  -0.0162 90  VAL   B CG1   
7371  C  CG2   . VAL   B 65  ? 0.2416 0.2370 0.2884 -0.0045 0.1056  -0.0276 90  VAL   B CG2   
7381  N  N     . ASN   B 66  ? 0.2692 0.1991 0.3268 -0.0043 0.1351  -0.0476 91  ASN   B N     
7382  C  CA    . ASN   B 66  ? 0.2872 0.2290 0.3422 0.0122  0.1540  -0.0323 91  ASN   B CA    
7383  C  C     . ASN   B 66  ? 0.3063 0.2494 0.3834 0.0241  0.1488  -0.0364 91  ASN   B C     
7384  O  O     . ASN   B 66  ? 0.3359 0.2444 0.3775 0.0152  0.1580  -0.0371 91  ASN   B O     
7385  C  CB    . ASN   B 66  ? 0.3339 0.2294 0.3193 0.0285  0.1509  -0.0211 91  ASN   B CB    
7386  C  CG    . ASN   B 66  ? 0.3478 0.2093 0.2934 0.0070  0.1651  -0.0316 91  ASN   B CG    
7387  O  OD1   . ASN   B 66  ? 0.3060 0.2114 0.2890 -0.0253 0.1600  -0.0293 91  ASN   B OD1   
7388  N  ND2   . ASN   B 66  ? 0.4021 0.1976 0.2908 -0.0091 0.1618  -0.0449 91  ASN   B ND2   
7395  N  N     . ALA   B 67  ? 0.3084 0.2364 0.4213 0.0200  0.1572  -0.0485 92  ALA   B N     
7396  C  CA    . ALA   B 67  ? 0.3242 0.2431 0.4569 0.0229  0.1593  -0.0601 92  ALA   B CA    
7397  C  C     . ALA   B 67  ? 0.2972 0.2560 0.4826 0.0119  0.1367  -0.0758 92  ALA   B C     
7398  O  O     . ALA   B 67  ? 0.2730 0.2647 0.5145 0.0146  0.1462  -0.0725 92  ALA   B O     
7399  C  CB    . ALA   B 67  ? 0.3393 0.2570 0.4683 0.0268  0.1475  -0.0775 92  ALA   B CB    
7405  N  N     . ALA   B 68  ? 0.2660 0.2559 0.4724 0.0074  0.1133  -0.0673 93  ALA   B N     
7406  C  CA    . ALA   B 68  ? 0.2559 0.2396 0.4454 0.0293  0.1207  -0.0692 93  ALA   B CA    
7407  C  C     . ALA   B 68  ? 0.2544 0.2323 0.4519 0.0258  0.1148  -0.0591 93  ALA   B C     
7408  O  O     . ALA   B 68  ? 0.2533 0.2342 0.4492 0.0371  0.1113  -0.0395 93  ALA   B O     
7409  C  CB    . ALA   B 68  ? 0.2522 0.2464 0.4264 0.0423  0.1439  -0.0564 93  ALA   B CB    
7415  N  N     . ASP   B 69  ? 0.2645 0.2126 0.4524 0.0386  0.1103  -0.0542 94  ASP   B N     
7416  C  CA    . ASP   B 69  ? 0.2876 0.2048 0.4495 0.0108  0.1446  -0.0518 94  ASP   B CA    
7417  C  C     . ASP   B 69  ? 0.3222 0.2007 0.4667 -0.0048 0.1597  -0.0617 94  ASP   B C     
7418  O  O     . ASP   B 69  ? 0.3393 0.2095 0.4721 -0.0099 0.1554  -0.0709 94  ASP   B O     
7419  C  CB    . ASP   B 69  ? 0.2723 0.2424 0.4248 0.0184  0.1571  -0.0426 94  ASP   B CB    
7420  C  CG    . ASP   B 69  ? 0.3217 0.2817 0.4086 0.0192  0.1244  -0.0452 94  ASP   B CG    
7421  O  OD1   . ASP   B 69  ? 0.3028 0.3006 0.4052 0.0075  0.1145  -0.0230 94  ASP   B OD1   
7422  O  OD2   . ASP   B 69  ? 0.3417 0.3056 0.3913 0.0509  0.1097  -0.0530 94  ASP   B OD2   
7427  N  N     . ASN   B 70  ? 0.3252 0.2213 0.4827 0.0283  0.1579  -0.0580 95  ASN   B N     
7428  C  CA    . ASN   B 70  ? 0.3512 0.2392 0.5011 0.0352  0.1831  -0.0568 95  ASN   B CA    
7429  C  C     . ASN   B 70  ? 0.3808 0.2451 0.5297 0.0467  0.1859  -0.0580 95  ASN   B C     
7430  O  O     . ASN   B 70  ? 0.4060 0.2594 0.5426 0.0282  0.2012  -0.0684 95  ASN   B O     
7431  C  CB    . ASN   B 70  ? 0.3735 0.2539 0.5067 0.0363  0.1873  -0.0817 95  ASN   B CB    
7432  C  CG    . ASN   B 70  ? 0.4144 0.2957 0.5167 0.0431  0.2022  -0.0928 95  ASN   B CG    
7433  O  OD1   . ASN   B 70  ? 0.4139 0.3003 0.5105 0.0345  0.1980  -0.1205 95  ASN   B OD1   
7434  N  ND2   . ASN   B 70  ? 0.4338 0.3072 0.5267 0.0643  0.2021  -0.0884 95  ASN   B ND2   
7441  N  N     . LYS   B 71  ? 0.3852 0.2605 0.5447 0.0639  0.1705  -0.0328 96  LYS   B N     
7442  C  CA    . LYS   B 71  ? 0.3533 0.2797 0.5612 0.0760  0.1637  -0.0408 96  LYS   B CA    
7443  C  C     . LYS   B 71  ? 0.3561 0.2667 0.5642 0.0826  0.1484  -0.0499 96  LYS   B C     
7444  O  O     . LYS   B 71  ? 0.4041 0.2618 0.5793 0.0876  0.1341  -0.0658 96  LYS   B O     
7445  C  CB    . LYS   B 71  ? 0.3236 0.2872 0.5864 0.0759  0.1477  -0.0139 96  LYS   B CB    
7446  C  CG    . LYS   B 71  ? 0.2839 0.3101 0.6047 0.0988  0.1424  -0.0080 96  LYS   B CG    
7447  C  CD    . LYS   B 71  ? 0.3001 0.3251 0.6437 0.1075  0.1404  -0.0092 96  LYS   B CD    
7448  C  CE    . LYS   B 71  ? 0.3178 0.3544 0.6739 0.1070  0.1305  -0.0033 96  LYS   B CE    
7449  N  NZ    . LYS   B 71  ? 0.3384 0.3830 0.6970 0.0981  0.1089  0.0056  96  LYS   B NZ    
7463  N  N     . GLN   B 72  ? 0.2965 0.2732 0.5542 0.0708  0.1519  -0.0361 97  GLN   B N     
7464  C  CA    . GLN   B 72  ? 0.2915 0.2746 0.5416 0.0681  0.1518  -0.0202 97  GLN   B CA    
7465  C  C     . GLN   B 72  ? 0.3481 0.2592 0.5548 0.0554  0.1554  -0.0210 97  GLN   B C     
7466  O  O     . GLN   B 72  ? 0.4260 0.2674 0.5643 0.0509  0.1352  -0.0132 97  GLN   B O     
7467  C  CB    . GLN   B 72  ? 0.2787 0.2878 0.5287 0.0624  0.1451  -0.0126 97  GLN   B CB    
7468  C  CG    . GLN   B 72  ? 0.2697 0.3126 0.5246 0.0593  0.1299  -0.0110 97  GLN   B CG    
7469  C  CD    . GLN   B 72  ? 0.3218 0.3366 0.5287 0.0248  0.1020  -0.0105 97  GLN   B CD    
7470  O  OE1   . GLN   B 72  ? 0.3010 0.3222 0.5263 0.0348  0.1141  -0.0147 97  GLN   B OE1   
7471  N  NE2   . GLN   B 72  ? 0.3834 0.3635 0.5307 -0.0067 0.0706  0.0000  97  GLN   B NE2   
7480  N  N     . ARG   B 73  ? 0.3532 0.2589 0.5541 0.0388  0.1902  -0.0270 98  ARG   B N     
7481  C  CA    . ARG   B 73  ? 0.3884 0.2762 0.5692 0.0252  0.1998  -0.0554 98  ARG   B CA    
7482  C  C     . ARG   B 73  ? 0.4320 0.2621 0.6012 0.0375  0.2112  -0.0695 98  ARG   B C     
7483  O  O     . ARG   B 73  ? 0.4746 0.2465 0.6201 0.0185  0.1836  -0.0806 98  ARG   B O     
7484  C  CB    . ARG   B 73  ? 0.3833 0.2805 0.5487 0.0097  0.2051  -0.0791 98  ARG   B CB    
7485  C  CG    . ARG   B 73  ? 0.4394 0.2874 0.5371 -0.0086 0.1883  -0.1124 98  ARG   B CG    
7486  C  CD    . ARG   B 73  ? 0.4563 0.3065 0.5214 -0.0097 0.2007  -0.1281 98  ARG   B CD    
7487  N  NE    . ARG   B 73  ? 0.5165 0.2963 0.5061 -0.0220 0.2115  -0.1513 98  ARG   B NE    
7488  C  CZ    . ARG   B 73  ? 0.5542 0.3063 0.4928 -0.0127 0.2355  -0.1329 98  ARG   B CZ    
7489  N  NH1   . ARG   B 73  ? 0.5690 0.3276 0.4834 0.0148  0.2358  -0.1263 98  ARG   B NH1   
7490  N  NH2   . ARG   B 73  ? 0.5886 0.3119 0.4869 -0.0304 0.2612  -0.1227 98  ARG   B NH2   
7504  N  N     . ASP   B 74  ? 0.3992 0.2603 0.6252 0.0403  0.2266  -0.0607 99  ASP   B N     
7505  C  CA    . ASP   B 74  ? 0.4093 0.2764 0.6662 0.0585  0.2209  -0.0577 99  ASP   B CA    
7506  C  C     . ASP   B 74  ? 0.3997 0.2854 0.6948 0.0682  0.2045  -0.0538 99  ASP   B C     
7507  O  O     . ASP   B 74  ? 0.3780 0.2737 0.6893 0.0595  0.1980  -0.0591 99  ASP   B O     
7508  C  CB    . ASP   B 74  ? 0.4208 0.3209 0.6783 0.0736  0.2322  -0.0636 99  ASP   B CB    
7509  C  CG    . ASP   B 74  ? 0.4574 0.3616 0.6981 0.0818  0.2575  -0.0683 99  ASP   B CG    
7510  O  OD1   . ASP   B 74  ? 0.4604 0.3800 0.7026 0.0752  0.2694  -0.0721 99  ASP   B OD1   
7511  O  OD2   . ASP   B 74  ? 0.5083 0.3839 0.7042 0.1040  0.2612  -0.0787 99  ASP   B OD2   
7516  N  N     . PRO   B 75  ? 0.4365 0.3267 0.7215 0.0674  0.1795  -0.0494 100 PRO   B N     
7517  C  CA    . PRO   B 75  ? 0.4462 0.3402 0.7401 0.0755  0.1745  -0.0519 100 PRO   B CA    
7518  C  C     . PRO   B 75  ? 0.4233 0.3349 0.7555 0.0991  0.1649  -0.0761 100 PRO   B C     
7519  O  O     . PRO   B 75  ? 0.3884 0.3393 0.7704 0.1084  0.1447  -0.0827 100 PRO   B O     
7520  C  CB    . PRO   B 75  ? 0.4720 0.3710 0.7379 0.0421  0.1699  -0.0437 100 PRO   B CB    
7521  C  CG    . PRO   B 75  ? 0.4703 0.3771 0.7339 0.0511  0.1692  -0.0379 100 PRO   B CG    
7522  C  CD    . PRO   B 75  ? 0.4663 0.3585 0.7292 0.0701  0.1725  -0.0367 100 PRO   B CD    
7530  N  N     . LYS   B 76  ? 0.4525 0.3360 0.7504 0.1156  0.1682  -0.0967 101 LYS   B N     
7531  C  CA    . LYS   B 76  ? 0.4552 0.3634 0.7637 0.1168  0.1821  -0.1069 101 LYS   B CA    
7532  C  C     . LYS   B 76  ? 0.4213 0.3709 0.7623 0.1218  0.1755  -0.0893 101 LYS   B C     
7533  O  O     . LYS   B 76  ? 0.4129 0.4002 0.7628 0.1398  0.1665  -0.0862 101 LYS   B O     
7534  C  CB    . LYS   B 76  ? 0.5318 0.4223 0.7780 0.0983  0.1914  -0.1184 101 LYS   B CB    
7535  C  CG    . LYS   B 76  ? 0.5704 0.4818 0.7929 0.0922  0.1843  -0.1235 101 LYS   B CG    
7536  C  CD    . LYS   B 76  ? 0.5989 0.5426 0.8097 0.0775  0.1611  -0.1202 101 LYS   B CD    
7537  C  CE    . LYS   B 76  ? 0.6327 0.5986 0.8254 0.0644  0.1488  -0.1193 101 LYS   B CE    
7538  N  NZ    . LYS   B 76  ? 0.6506 0.6223 0.8345 0.0526  0.1396  -0.1192 101 LYS   B NZ    
7552  N  N     . MET   B 77  ? 0.4140 0.3391 0.7434 0.1043  0.1793  -0.0836 102 MET   B N     
7553  C  CA    . MET   B 77  ? 0.3669 0.3316 0.7387 0.0762  0.1854  -0.0816 102 MET   B CA    
7554  C  C     . MET   B 77  ? 0.3811 0.3625 0.7669 0.0889  0.1933  -0.0808 102 MET   B C     
7555  O  O     . MET   B 77  ? 0.3878 0.3850 0.7787 0.0904  0.1788  -0.0798 102 MET   B O     
7556  C  CB    . MET   B 77  ? 0.3597 0.3110 0.7292 0.0629  0.1857  -0.0826 102 MET   B CB    
7557  C  CG    . MET   B 77  ? 0.3553 0.3050 0.7210 0.0494  0.2011  -0.0784 102 MET   B CG    
7558  S  SD    . MET   B 77  ? 0.3651 0.3183 0.7221 0.0304  0.2233  -0.0920 102 MET   B SD    
7559  C  CE    . MET   B 77  ? 0.3854 0.3251 0.7034 0.0395  0.2266  -0.0978 102 MET   B CE    
7569  N  N     . SER   B 78  ? 0.3823 0.3748 0.7703 0.0953  0.1955  -0.0758 103 SER   B N     
7570  C  CA    . SER   B 78  ? 0.3536 0.3977 0.7636 0.0903  0.1985  -0.0603 103 SER   B CA    
7571  C  C     . SER   B 78  ? 0.3547 0.3807 0.7773 0.0745  0.2039  -0.0696 103 SER   B C     
7572  O  O     . SER   B 78  ? 0.3681 0.3638 0.7895 0.0515  0.1923  -0.0758 103 SER   B O     
7573  C  CB    . SER   B 78  ? 0.3545 0.4293 0.7632 0.0872  0.2171  -0.0473 103 SER   B CB    
7574  O  OG    . SER   B 78  ? 0.3638 0.4508 0.7815 0.0848  0.2270  -0.0537 103 SER   B OG    
7580  N  N     . CYS   B 79  ? 0.3641 0.3689 0.7596 0.0766  0.2061  -0.0708 104 CYS   B N     
7581  C  CA    . CYS   B 79  ? 0.3820 0.3964 0.7511 0.0956  0.2074  -0.0755 104 CYS   B CA    
7582  C  C     . CYS   B 79  ? 0.3396 0.3458 0.7083 0.0527  0.2001  -0.0870 104 CYS   B C     
7583  O  O     . CYS   B 79  ? 0.3403 0.3154 0.6965 0.0280  0.2057  -0.1012 104 CYS   B O     
7584  C  CB    . CYS   B 79  ? 0.4162 0.4772 0.7719 0.1371  0.2242  -0.0593 104 CYS   B CB    
7585  S  SG    . CYS   B 79  ? 0.4799 0.5404 0.8300 0.1159  0.2729  -0.0386 104 CYS   B SG    
7591  N  N     . ILE   B 80  ? 0.3118 0.3249 0.6781 0.0228  0.1998  -0.0927 105 ILE   B N     
7592  C  CA    . ILE   B 80  ? 0.2920 0.3398 0.6648 0.0135  0.2001  -0.0781 105 ILE   B CA    
7593  C  C     . ILE   B 80  ? 0.2951 0.3540 0.6856 0.0067  0.2021  -0.0905 105 ILE   B C     
7594  O  O     . ILE   B 80  ? 0.3058 0.3819 0.7022 0.0030  0.2056  -0.1010 105 ILE   B O     
7595  C  CB    . ILE   B 80  ? 0.2692 0.3226 0.6195 0.0078  0.1861  -0.0751 105 ILE   B CB    
7596  C  CG1   . ILE   B 80  ? 0.2496 0.3281 0.6066 -0.0048 0.1771  -0.0672 105 ILE   B CG1   
7597  C  CG2   . ILE   B 80  ? 0.2634 0.3179 0.6406 0.0061  0.1805  -0.0754 105 ILE   B CG2   
7598  C  CD1   . ILE   B 80  ? 0.2266 0.3324 0.6105 0.0173  0.1468  -0.0643 105 ILE   B CD1   
7610  N  N     . ARG   B 81  ? 0.2937 0.3263 0.6882 -0.0081 0.2086  -0.0815 106 ARG   B N     
7611  C  CA    . ARG   B 81  ? 0.2931 0.3482 0.6985 -0.0111 0.2037  -0.1021 106 ARG   B CA    
7612  C  C     . ARG   B 81  ? 0.3231 0.3562 0.6900 -0.0077 0.2215  -0.1018 106 ARG   B C     
7613  O  O     . ARG   B 81  ? 0.3433 0.3603 0.6772 -0.0066 0.2440  -0.0882 106 ARG   B O     
7614  C  CB    . ARG   B 81  ? 0.3143 0.3878 0.7333 -0.0051 0.2130  -0.1184 106 ARG   B CB    
7615  C  CG    . ARG   B 81  ? 0.3260 0.4026 0.7550 0.0129  0.2144  -0.1182 106 ARG   B CG    
7616  C  CD    . ARG   B 81  ? 0.3469 0.4340 0.7828 0.0163  0.2333  -0.1129 106 ARG   B CD    
7617  N  NE    . ARG   B 81  ? 0.3644 0.4890 0.8198 0.0347  0.2321  -0.0925 106 ARG   B NE    
7618  C  CZ    . ARG   B 81  ? 0.3633 0.5253 0.8465 0.0781  0.2306  -0.0724 106 ARG   B CZ    
7619  N  NH1   . ARG   B 81  ? 0.3684 0.5351 0.8506 0.1033  0.2266  -0.0459 106 ARG   B NH1   
7620  N  NH2   . ARG   B 81  ? 0.3687 0.5432 0.8638 0.0934  0.2195  -0.0866 106 ARG   B NH2   
7634  N  N     . VAL   B 82  ? 0.2904 0.3237 0.6636 -0.0204 0.2016  -0.1127 107 VAL   B N     
7635  C  CA    . VAL   B 82  ? 0.2777 0.3372 0.6624 -0.0497 0.1949  -0.1031 107 VAL   B CA    
7636  C  C     . VAL   B 82  ? 0.2877 0.3439 0.6760 -0.0531 0.2028  -0.1213 107 VAL   B C     
7637  O  O     . VAL   B 82  ? 0.2938 0.3677 0.6922 -0.0420 0.2002  -0.1193 107 VAL   B O     
7638  C  CB    . VAL   B 82  ? 0.2540 0.3256 0.6403 -0.0336 0.1709  -0.1069 107 VAL   B CB    
7639  C  CG1   . VAL   B 82  ? 0.2632 0.3210 0.6196 0.0096  0.1644  -0.1127 107 VAL   B CG1   
7640  C  CG2   . VAL   B 82  ? 0.2519 0.3306 0.6338 -0.0696 0.1605  -0.0850 107 VAL   B CG2   
7650  N  N     . THR   B 83  ? 0.3110 0.3385 0.6734 -0.0686 0.2212  -0.1156 108 THR   B N     
7651  C  CA    . THR   B 83  ? 0.3354 0.3386 0.6833 -0.0708 0.2405  -0.1107 108 THR   B CA    
7652  C  C     . THR   B 83  ? 0.3461 0.3202 0.6981 -0.0868 0.2398  -0.1116 108 THR   B C     
7653  O  O     . THR   B 83  ? 0.3407 0.3254 0.7088 -0.0532 0.2328  -0.1262 108 THR   B O     
7654  C  CB    . THR   B 83  ? 0.4079 0.3915 0.6936 -0.0410 0.2648  -0.1060 108 THR   B CB    
7655  O  OG1   . THR   B 83  ? 0.4232 0.4355 0.7081 -0.0668 0.2764  -0.0925 108 THR   B OG1   
7656  C  CG2   . THR   B 83  ? 0.4263 0.3695 0.6878 -0.0273 0.2941  -0.1054 108 THR   B CG2   
7664  N  N     . ILE   B 84  ? 0.3855 0.3161 0.7061 -0.0960 0.2594  -0.1143 109 ILE   B N     
7665  C  CA    . ILE   B 84  ? 0.3747 0.3298 0.7049 -0.0950 0.2573  -0.1082 109 ILE   B CA    
7666  C  C     . ILE   B 84  ? 0.4124 0.3527 0.7440 -0.1181 0.2686  -0.1165 109 ILE   B C     
7667  O  O     . ILE   B 84  ? 0.3961 0.3729 0.7523 -0.1275 0.2497  -0.1248 109 ILE   B O     
7668  C  CB    . ILE   B 84  ? 0.3420 0.3228 0.6908 -0.0755 0.2432  -0.1032 109 ILE   B CB    
7669  C  CG1   . ILE   B 84  ? 0.3289 0.3201 0.6721 -0.0461 0.2410  -0.0841 109 ILE   B CG1   
7670  C  CG2   . ILE   B 84  ? 0.3653 0.3305 0.6938 -0.0805 0.2271  -0.1124 109 ILE   B CG2   
7671  C  CD1   . ILE   B 84  ? 0.3281 0.3296 0.6830 -0.0394 0.2395  -0.0887 109 ILE   B CD1   
7683  N  N     . ASP   B 85  ? 0.4521 0.3500 0.7564 -0.1222 0.2876  -0.1019 110 ASP   B N     
7684  C  CA    . ASP   B 85  ? 0.4583 0.3865 0.7956 -0.1147 0.3035  -0.0841 110 ASP   B CA    
7685  C  C     . ASP   B 85  ? 0.4539 0.3818 0.8163 -0.1194 0.2952  -0.0911 110 ASP   B C     
7686  O  O     . ASP   B 85  ? 0.4659 0.3764 0.8256 -0.0857 0.3006  -0.0958 110 ASP   B O     
7687  C  CB    . ASP   B 85  ? 0.4868 0.4316 0.8146 -0.1003 0.3325  -0.0560 110 ASP   B CB    
7688  C  CG    . ASP   B 85  ? 0.5269 0.4939 0.8424 -0.0965 0.3537  -0.0369 110 ASP   B CG    
7689  O  OD1   . ASP   B 85  ? 0.5538 0.5002 0.8650 -0.1230 0.3364  -0.0288 110 ASP   B OD1   
7690  O  OD2   . ASP   B 85  ? 0.5511 0.5338 0.8447 -0.0752 0.3807  -0.0159 110 ASP   B OD2   
7695  N  N     . PRO   B 86  ? 0.4441 0.4040 0.8220 -0.1271 0.2857  -0.0936 111 PRO   B N     
7696  C  CA    . PRO   B 86  ? 0.4615 0.4362 0.8386 -0.1242 0.2770  -0.0816 111 PRO   B CA    
7697  C  C     . PRO   B 86  ? 0.4791 0.4658 0.8516 -0.1396 0.2806  -0.0506 111 PRO   B C     
7698  O  O     . PRO   B 86  ? 0.5039 0.4684 0.8625 -0.1358 0.3033  -0.0556 111 PRO   B O     
7699  C  CB    . PRO   B 86  ? 0.4518 0.4211 0.8340 -0.1316 0.2541  -0.1062 111 PRO   B CB    
7700  C  CG    . PRO   B 86  ? 0.4299 0.4196 0.8282 -0.1406 0.2630  -0.1026 111 PRO   B CG    
7701  C  CD    . PRO   B 86  ? 0.4329 0.4056 0.8219 -0.1318 0.2713  -0.0943 111 PRO   B CD    
7709  N  N     . GLU   B 87  ? 0.4691 0.4897 0.8419 -0.1685 0.2565  -0.0128 112 GLU   B N     
7710  C  CA    . GLU   B 87  ? 0.5313 0.5371 0.8739 -0.1499 0.2594  -0.0060 112 GLU   B CA    
7711  C  C     . GLU   B 87  ? 0.5531 0.5010 0.8841 -0.1405 0.2869  -0.0159 112 GLU   B C     
7712  O  O     . GLU   B 87  ? 0.5672 0.4923 0.8950 -0.1344 0.3047  -0.0106 112 GLU   B O     
7713  C  CB    . GLU   B 87  ? 0.5874 0.5902 0.8909 -0.1507 0.2441  0.0138  112 GLU   B CB    
7714  C  CG    . GLU   B 87  ? 0.6936 0.6481 0.9051 -0.1065 0.2190  0.0270  112 GLU   B CG    
7715  C  CD    . GLU   B 87  ? 0.7962 0.7178 0.9159 -0.0639 0.2039  0.0394  112 GLU   B CD    
7716  O  OE1   . GLU   B 87  ? 0.8217 0.7165 0.9197 -0.0825 0.2043  0.0628  112 GLU   B OE1   
7717  O  OE2   . GLU   B 87  ? 0.8394 0.7619 0.9200 -0.0333 0.1980  0.0328  112 GLU   B OE2   
7724  N  N     . ASN   B 88  ? 0.5500 0.4541 0.8721 -0.1430 0.3003  -0.0209 113 ASN   B N     
7725  C  CA    . ASN   B 88  ? 0.5574 0.4561 0.8513 -0.1274 0.3110  -0.0264 113 ASN   B CA    
7726  C  C     . ASN   B 88  ? 0.5549 0.4218 0.8049 -0.1462 0.3230  -0.0351 113 ASN   B C     
7727  O  O     . ASN   B 88  ? 0.5476 0.4443 0.7884 -0.1473 0.3269  -0.0385 113 ASN   B O     
7728  C  CB    . ASN   B 88  ? 0.5501 0.5097 0.8698 -0.0981 0.3130  -0.0198 113 ASN   B CB    
7729  C  CG    . ASN   B 88  ? 0.5723 0.5514 0.8832 -0.0718 0.2991  -0.0178 113 ASN   B CG    
7730  O  OD1   . ASN   B 88  ? 0.6113 0.5854 0.8916 -0.0431 0.2951  -0.0258 113 ASN   B OD1   
7731  N  ND2   . ASN   B 88  ? 0.5652 0.5514 0.8849 -0.0619 0.2866  -0.0121 113 ASN   B ND2   
7738  N  N     . ASN   B 89  ? 0.5626 0.3722 0.7767 -0.1316 0.3282  -0.0482 114 ASN   B N     
7739  C  CA    . ASN   B 89  ? 0.5496 0.3459 0.7383 -0.1107 0.3356  -0.0623 114 ASN   B CA    
7740  C  C     . ASN   B 89  ? 0.5471 0.3387 0.7067 -0.1148 0.3340  -0.0677 114 ASN   B C     
7741  O  O     . ASN   B 89  ? 0.6097 0.3269 0.7023 -0.1064 0.3591  -0.0588 114 ASN   B O     
7742  C  CB    . ASN   B 89  ? 0.5604 0.3435 0.7225 -0.1043 0.3419  -0.0601 114 ASN   B CB    
7743  C  CG    . ASN   B 89  ? 0.5504 0.3484 0.6989 -0.0862 0.3529  -0.0528 114 ASN   B CG    
7744  O  OD1   . ASN   B 89  ? 0.5929 0.4002 0.7027 -0.0505 0.3259  -0.0660 114 ASN   B OD1   
7745  N  ND2   . ASN   B 89  ? 0.5547 0.3393 0.6844 -0.0833 0.3498  -0.0433 114 ASN   B ND2   
7752  N  N     . LEU   B 90  ? 0.5074 0.3470 0.6707 -0.1221 0.3133  -0.0792 115 LEU   B N     
7753  C  CA    . LEU   B 90  ? 0.4668 0.3445 0.6524 -0.1092 0.3056  -0.0975 115 LEU   B CA    
7754  C  C     . LEU   B 90  ? 0.4501 0.3148 0.6396 -0.1082 0.2945  -0.1058 115 LEU   B C     
7755  O  O     . LEU   B 90  ? 0.4915 0.3077 0.6526 -0.1126 0.2991  -0.1032 115 LEU   B O     
7756  C  CB    . LEU   B 90  ? 0.4946 0.3886 0.6802 -0.1024 0.3215  -0.1123 115 LEU   B CB    
7757  C  CG    . LEU   B 90  ? 0.5580 0.4874 0.6988 -0.0659 0.3217  -0.1078 115 LEU   B CG    
7758  C  CD1   . LEU   B 90  ? 0.6090 0.5105 0.7152 -0.0468 0.2987  -0.1022 115 LEU   B CD1   
7759  C  CD2   . LEU   B 90  ? 0.5936 0.5257 0.6995 -0.0569 0.3346  -0.1103 115 LEU   B CD2   
7771  N  N     . ILE   B 91  ? 0.4388 0.2969 0.6091 -0.0968 0.2863  -0.0878 116 ILE   B N     
7772  C  CA    . ILE   B 91  ? 0.4117 0.3058 0.5817 -0.0783 0.2770  -0.0764 116 ILE   B CA    
7773  C  C     . ILE   B 91  ? 0.4090 0.3024 0.5788 -0.0867 0.2699  -0.0745 116 ILE   B C     
7774  O  O     . ILE   B 91  ? 0.4709 0.3055 0.5692 -0.0567 0.2917  -0.0676 116 ILE   B O     
7775  C  CB    . ILE   B 91  ? 0.3975 0.3163 0.5635 -0.0880 0.2618  -0.0661 116 ILE   B CB    
7776  C  CG1   . ILE   B 91  ? 0.4003 0.3432 0.5578 -0.0979 0.2596  -0.0666 116 ILE   B CG1   
7777  C  CG2   . ILE   B 91  ? 0.3744 0.3403 0.5547 -0.0506 0.2597  -0.0595 116 ILE   B CG2   
7778  C  CD1   . ILE   B 91  ? 0.4044 0.3711 0.5722 -0.0983 0.2651  -0.0683 116 ILE   B CD1   
7790  N  N     . SER   B 92  ? 0.3614 0.3196 0.5781 -0.0661 0.2533  -0.0810 117 SER   B N     
7791  C  CA    . SER   B 92  ? 0.3319 0.3400 0.5799 -0.0499 0.2377  -0.0849 117 SER   B CA    
7792  C  C     . SER   B 92  ? 0.3342 0.3375 0.5755 -0.0817 0.2248  -0.1077 117 SER   B C     
7793  O  O     . SER   B 92  ? 0.3321 0.3577 0.5825 -0.0866 0.2038  -0.1069 117 SER   B O     
7794  C  CB    . SER   B 92  ? 0.3473 0.3920 0.6147 -0.0304 0.2317  -0.0780 117 SER   B CB    
7795  O  OG    . SER   B 92  ? 0.4127 0.4224 0.6317 -0.0268 0.2219  -0.0778 117 SER   B OG    
7801  N  N     . ILE   B 93  ? 0.3498 0.3184 0.5598 -0.0710 0.2436  -0.0960 118 ILE   B N     
7802  C  CA    . ILE   B 93  ? 0.3284 0.3038 0.5555 -0.0538 0.2301  -0.1080 118 ILE   B CA    
7803  C  C     . ILE   B 93  ? 0.3640 0.3054 0.5888 -0.0500 0.2392  -0.1084 118 ILE   B C     
7804  O  O     . ILE   B 93  ? 0.3597 0.3055 0.5957 -0.0362 0.2457  -0.1122 118 ILE   B O     
7805  C  CB    . ILE   B 93  ? 0.3119 0.2933 0.5320 -0.0601 0.2191  -0.1048 118 ILE   B CB    
7806  C  CG1   . ILE   B 93  ? 0.2856 0.3261 0.5397 -0.0585 0.2014  -0.1120 118 ILE   B CG1   
7807  C  CG2   . ILE   B 93  ? 0.3467 0.3001 0.5309 -0.0649 0.2208  -0.1022 118 ILE   B CG2   
7808  C  CD1   . ILE   B 93  ? 0.2972 0.3632 0.5539 -0.0735 0.1700  -0.1201 118 ILE   B CD1   
7820  N  N     . TRP   B 94  ? 0.3465 0.3308 0.5883 -0.0180 0.2332  -0.1112 119 TRP   B N     
7821  C  CA    . TRP   B 94  ? 0.3742 0.3569 0.6132 -0.0051 0.2470  -0.1108 119 TRP   B CA    
7822  C  C     . TRP   B 94  ? 0.3692 0.3512 0.6132 0.0076  0.2402  -0.1051 119 TRP   B C     
7823  O  O     . TRP   B 94  ? 0.3613 0.3504 0.6088 0.0440  0.2169  -0.0972 119 TRP   B O     
7824  C  CB    . TRP   B 94  ? 0.4010 0.3908 0.6535 0.0191  0.2539  -0.1164 119 TRP   B CB    
7825  C  CG    . TRP   B 94  ? 0.4284 0.4233 0.6730 0.0418  0.2626  -0.1145 119 TRP   B CG    
7826  C  CD1   . TRP   B 94  ? 0.4729 0.4368 0.6790 0.0618  0.2686  -0.1226 119 TRP   B CD1   
7827  C  CD2   . TRP   B 94  ? 0.4285 0.4467 0.6973 0.0486  0.2693  -0.1032 119 TRP   B CD2   
7828  N  NE1   . TRP   B 94  ? 0.4683 0.4473 0.7011 0.0439  0.2751  -0.1003 119 TRP   B NE1   
7829  C  CE2   . TRP   B 94  ? 0.4629 0.4537 0.7124 0.0570  0.2645  -0.0972 119 TRP   B CE2   
7830  C  CE3   . TRP   B 94  ? 0.4119 0.4596 0.7036 0.0581  0.2606  -0.0988 119 TRP   B CE3   
7831  C  CZ2   . TRP   B 94  ? 0.4539 0.4631 0.7211 0.0723  0.2752  -0.0970 119 TRP   B CZ2   
7832  C  CZ3   . TRP   B 94  ? 0.4221 0.4723 0.7159 0.0605  0.2668  -0.1004 119 TRP   B CZ3   
7833  C  CH2   . TRP   B 94  ? 0.4460 0.4746 0.7206 0.0684  0.2718  -0.0983 119 TRP   B CH2   
7844  N  N     . ASN   B 95  ? 0.3833 0.3412 0.6006 -0.0001 0.2459  -0.1095 120 ASN   B N     
7845  C  CA    . ASN   B 95  ? 0.3915 0.3415 0.6127 0.0070  0.2412  -0.1189 120 ASN   B CA    
7846  C  C     . ASN   B 95  ? 0.4160 0.3652 0.6310 0.0024  0.2565  -0.1278 120 ASN   B C     
7847  O  O     . ASN   B 95  ? 0.4144 0.3697 0.6272 -0.0092 0.2486  -0.1499 120 ASN   B O     
7848  C  CB    . ASN   B 95  ? 0.3951 0.3281 0.6348 0.0095  0.2414  -0.1169 120 ASN   B CB    
7849  C  CG    . ASN   B 95  ? 0.4005 0.3141 0.6277 0.0010  0.2483  -0.1120 120 ASN   B CG    
7850  O  OD1   . ASN   B 95  ? 0.4347 0.2944 0.6298 -0.0112 0.2545  -0.1215 120 ASN   B OD1   
7851  N  ND2   . ASN   B 95  ? 0.3908 0.3145 0.6130 0.0079  0.2458  -0.1001 120 ASN   B ND2   
7858  N  N     . ASN   B 96  ? 0.4331 0.3517 0.6365 0.0252  0.2574  -0.1104 121 ASN   B N     
7859  C  CA    . ASN   B 96  ? 0.4758 0.3524 0.6736 0.0633  0.2473  -0.1090 121 ASN   B CA    
7860  C  C     . ASN   B 96  ? 0.4759 0.3485 0.6799 0.0650  0.2522  -0.0992 121 ASN   B C     
7861  O  O     . ASN   B 96  ? 0.4880 0.3324 0.6814 0.0709  0.2497  -0.0894 121 ASN   B O     
7862  C  CB    . ASN   B 96  ? 0.5126 0.3733 0.7120 0.0622  0.2509  -0.0991 121 ASN   B CB    
7863  C  CG    . ASN   B 96  ? 0.4882 0.3816 0.7383 0.0950  0.2343  -0.0957 121 ASN   B CG    
7864  O  OD1   . ASN   B 96  ? 0.4564 0.3550 0.7232 0.0790  0.2464  -0.0834 121 ASN   B OD1   
7865  N  ND2   . ASN   B 96  ? 0.4605 0.4251 0.7514 0.1158  0.2282  -0.1053 121 ASN   B ND2   
7872  N  N     . GLY   B 97  ? 0.4769 0.3551 0.6758 0.0670  0.2520  -0.1015 122 GLY   B N     
7873  C  CA    . GLY   B 97  ? 0.5066 0.3706 0.6829 0.0827  0.2491  -0.1103 122 GLY   B CA    
7874  C  C     . GLY   B 97  ? 0.5524 0.3899 0.6876 0.0864  0.2711  -0.1104 122 GLY   B C     
7875  O  O     . GLY   B 97  ? 0.5652 0.4001 0.6923 0.0675  0.2880  -0.1206 122 GLY   B O     
7879  N  N     . LYS   B 98  ? 0.5696 0.4008 0.6824 0.1034  0.2671  -0.1089 123 LYS   B N     
7880  C  CA    . LYS   B 98  ? 0.6111 0.4121 0.7039 0.0949  0.2986  -0.1040 123 LYS   B CA    
7881  C  C     . LYS   B 98  ? 0.6102 0.3933 0.6697 0.0638  0.3125  -0.1002 123 LYS   B C     
7882  O  O     . LYS   B 98  ? 0.5684 0.3743 0.6467 0.0743  0.2839  -0.0969 123 LYS   B O     
7883  C  CB    . LYS   B 98  ? 0.6654 0.4541 0.7470 0.1030  0.3218  -0.0936 123 LYS   B CB    
7884  C  CG    . LYS   B 98  ? 0.7594 0.5015 0.7824 0.0642  0.3139  -0.0899 123 LYS   B CG    
7885  C  CD    . LYS   B 98  ? 0.8271 0.5270 0.8049 0.0371  0.2988  -0.0881 123 LYS   B CD    
7886  C  CE    . LYS   B 98  ? 0.8753 0.5423 0.8208 0.0291  0.2819  -0.0823 123 LYS   B CE    
7887  N  NZ    . LYS   B 98  ? 0.8967 0.5375 0.8283 0.0311  0.2711  -0.0774 123 LYS   B NZ    
7901  N  N     . GLY   B 99  ? 0.6235 0.3827 0.6389 0.0542  0.3101  -0.1023 124 GLY   B N     
7902  C  CA    . GLY   B 99  ? 0.6379 0.3573 0.6063 0.0503  0.2983  -0.0996 124 GLY   B CA    
7903  C  C     . GLY   B 99  ? 0.6792 0.3357 0.5730 0.0218  0.2971  -0.0997 124 GLY   B C     
7904  O  O     . GLY   B 99  ? 0.7091 0.3376 0.5888 0.0329  0.2927  -0.0636 124 GLY   B O     
7908  N  N     . ILE   B 100 ? 0.6535 0.3276 0.5213 -0.0044 0.2973  -0.0983 125 ILE   B N     
7909  C  CA    . ILE   B 100 ? 0.6535 0.3364 0.4961 -0.0118 0.2919  -0.1009 125 ILE   B CA    
7910  C  C     . ILE   B 100 ? 0.7057 0.3615 0.4983 -0.0197 0.3128  -0.0951 125 ILE   B C     
7911  O  O     . ILE   B 100 ? 0.7212 0.3797 0.5106 -0.0055 0.3299  -0.0785 125 ILE   B O     
7912  C  CB    . ILE   B 100 ? 0.6593 0.3348 0.4800 -0.0241 0.2742  -0.1166 125 ILE   B CB    
7913  C  CG1   . ILE   B 100 ? 0.6440 0.3346 0.4673 -0.0224 0.2540  -0.1274 125 ILE   B CG1   
7914  C  CG2   . ILE   B 100 ? 0.6422 0.3424 0.4736 -0.0019 0.2603  -0.1184 125 ILE   B CG2   
7915  C  CD1   . ILE   B 100 ? 0.6722 0.3360 0.4648 0.0092  0.2390  -0.1237 125 ILE   B CD1   
7927  N  N     . PRO   B 101 ? 0.7276 0.3611 0.4939 -0.0170 0.3086  -0.0972 126 PRO   B N     
7928  C  CA    . PRO   B 101 ? 0.7786 0.3579 0.4883 -0.0127 0.3030  -0.0971 126 PRO   B CA    
7929  C  C     . PRO   B 101 ? 0.8012 0.3693 0.4808 0.0125  0.3088  -0.0779 126 PRO   B C     
7930  O  O     . PRO   B 101 ? 0.8188 0.3770 0.4824 0.0232  0.3152  -0.0685 126 PRO   B O     
7931  C  CB    . PRO   B 101 ? 0.7985 0.3473 0.4939 -0.0339 0.3041  -0.1023 126 PRO   B CB    
7932  C  CG    . PRO   B 101 ? 0.7854 0.3518 0.5009 -0.0497 0.3060  -0.1059 126 PRO   B CG    
7933  C  CD    . PRO   B 101 ? 0.7801 0.3513 0.4991 -0.0364 0.3072  -0.1069 126 PRO   B CD    
7941  N  N     . VAL   B 102 ? 0.8100 0.3667 0.4733 0.0186  0.3029  -0.0754 127 VAL   B N     
7942  C  CA    . VAL   B 102 ? 0.8601 0.3866 0.4694 0.0232  0.2987  -0.0795 127 VAL   B CA    
7943  C  C     . VAL   B 102 ? 0.8970 0.3812 0.4582 0.0180  0.2904  -0.0793 127 VAL   B C     
7944  O  O     . VAL   B 102 ? 0.9483 0.4028 0.4731 0.0461  0.2961  -0.0736 127 VAL   B O     
7945  C  CB    . VAL   B 102 ? 0.8177 0.4255 0.4752 0.0364  0.3052  -0.0833 127 VAL   B CB    
7946  C  CG1   . VAL   B 102 ? 0.8480 0.4296 0.4734 0.0439  0.3119  -0.0705 127 VAL   B CG1   
7947  C  CG2   . VAL   B 102 ? 0.8047 0.4576 0.4787 0.0321  0.3186  -0.0772 127 VAL   B CG2   
7957  N  N     . VAL   B 103 ? 0.9314 0.3676 0.4448 -0.0197 0.2659  -0.0905 128 VAL   B N     
7958  C  CA    . VAL   B 103 ? 0.9558 0.3777 0.4364 -0.0237 0.2551  -0.0993 128 VAL   B CA    
7959  C  C     . VAL   B 103 ? 0.9933 0.3803 0.4302 -0.0308 0.2565  -0.0919 128 VAL   B C     
7960  O  O     . VAL   B 103 ? 0.9582 0.3435 0.4287 -0.0201 0.2649  -0.0735 128 VAL   B O     
7961  C  CB    . VAL   B 103 ? 0.9536 0.3816 0.4294 -0.0686 0.2540  -0.1050 128 VAL   B CB    
7962  C  CG1   . VAL   B 103 ? 0.9508 0.3766 0.4156 -0.0662 0.2493  -0.1016 128 VAL   B CG1   
7963  C  CG2   . VAL   B 103 ? 0.9519 0.3796 0.4377 -0.0718 0.2374  -0.1217 128 VAL   B CG2   
7973  N  N     . GLU   B 104 ? 1.0212 0.3967 0.4207 -0.0601 0.2244  -0.1107 129 GLU   B N     
7974  C  CA    . GLU   B 104 ? 1.0501 0.4045 0.4242 -0.0828 0.2350  -0.1090 129 GLU   B CA    
7975  C  C     . GLU   B 104 ? 1.0549 0.4081 0.4128 -0.0807 0.2326  -0.1029 129 GLU   B C     
7976  O  O     . GLU   B 104 ? 1.0714 0.4026 0.4123 -0.0856 0.2325  -0.0981 129 GLU   B O     
7977  C  CB    . GLU   B 104 ? 1.1159 0.4411 0.4519 -0.0879 0.2300  -0.0886 129 GLU   B CB    
7978  C  CG    . GLU   B 104 ? 1.1507 0.4771 0.4938 -0.0755 0.2117  -0.0640 129 GLU   B CG    
7979  C  CD    . GLU   B 104 ? 1.1728 0.5239 0.5401 -0.0632 0.1822  -0.0209 129 GLU   B CD    
7980  O  OE1   . GLU   B 104 ? 1.1882 0.5366 0.5474 -0.0622 0.1761  -0.0069 129 GLU   B OE1   
7981  O  OE2   . GLU   B 104 ? 1.1729 0.5526 0.5724 -0.0620 0.1677  -0.0020 129 GLU   B OE2   
7988  N  N     . HIS   B 105 ? 0.9996 0.4000 0.4080 -0.0682 0.2270  -0.1085 130 HIS   B N     
7989  C  CA    . HIS   B 105 ? 0.9994 0.3955 0.3943 -0.0588 0.1945  -0.1114 130 HIS   B CA    
7990  C  C     . HIS   B 105 ? 1.0355 0.4089 0.3883 -0.0585 0.1702  -0.1140 130 HIS   B C     
7991  O  O     . HIS   B 105 ? 1.0534 0.4103 0.3851 -0.0523 0.1905  -0.0999 130 HIS   B O     
7992  C  CB    . HIS   B 105 ? 0.9302 0.3722 0.3784 -0.0463 0.1955  -0.1047 130 HIS   B CB    
7993  C  CG    . HIS   B 105 ? 0.9218 0.3625 0.3496 -0.0731 0.1943  -0.0886 130 HIS   B CG    
7994  N  ND1   . HIS   B 105 ? 0.9244 0.3661 0.3351 -0.0872 0.2037  -0.0731 130 HIS   B ND1   
7995  C  CD2   . HIS   B 105 ? 0.8939 0.3571 0.3390 -0.0852 0.1972  -0.0848 130 HIS   B CD2   
7996  C  CE1   . HIS   B 105 ? 0.9156 0.3564 0.3309 -0.0900 0.1983  -0.0684 130 HIS   B CE1   
7997  N  NE2   . HIS   B 105 ? 0.8850 0.3428 0.3378 -0.0840 0.1910  -0.0846 130 HIS   B NE2   
8005  N  N     . LYS   B 106 ? 1.0626 0.4233 0.3893 -0.0841 0.1390  -0.1239 131 LYS   B N     
8006  C  CA    A LYS   B 106 ? 1.0576 0.4288 0.3924 -0.0808 0.1201  -0.1328 131 LYS   B CA    
8007  C  CA    B LYS   B 106 ? 1.0703 0.4449 0.3952 -0.0801 0.1294  -0.1273 131 LYS   B CA    
8008  C  C     . LYS   B 106 ? 1.0824 0.4530 0.3857 -0.0999 0.1200  -0.1272 131 LYS   B C     
8009  O  O     . LYS   B 106 ? 1.1056 0.4920 0.3886 -0.1045 0.1066  -0.1430 131 LYS   B O     
8010  C  CB    A LYS   B 106 ? 1.0289 0.4255 0.4021 -0.0658 0.1130  -0.1394 131 LYS   B CB    
8011  C  CB    B LYS   B 106 ? 1.0562 0.4716 0.4087 -0.0596 0.1368  -0.1238 131 LYS   B CB    
8012  C  CG    A LYS   B 106 ? 0.9739 0.4265 0.4018 -0.0441 0.1168  -0.1565 131 LYS   B CG    
8013  C  CG    B LYS   B 106 ? 1.0281 0.4988 0.4143 -0.0344 0.1559  -0.1257 131 LYS   B CG    
8014  C  CD    A LYS   B 106 ? 0.9181 0.4175 0.4069 -0.0404 0.1081  -0.1697 131 LYS   B CD    
8015  C  CD    B LYS   B 106 ? 0.9964 0.5161 0.4133 -0.0220 0.1755  -0.1232 131 LYS   B CD    
8016  C  CE    A LYS   B 106 ? 0.8936 0.4323 0.4071 -0.0315 0.1148  -0.1783 131 LYS   B CE    
8017  C  CE    B LYS   B 106 ? 0.9538 0.5083 0.4051 -0.0111 0.2003  -0.1328 131 LYS   B CE    
8018  N  NZ    A LYS   B 106 ? 0.8869 0.4325 0.4077 -0.0406 0.1034  -0.1847 131 LYS   B NZ    
8019  N  NZ    B LYS   B 106 ? 0.9009 0.4792 0.3993 -0.0186 0.2163  -0.1411 131 LYS   B NZ    
8044  N  N     . VAL   B 107 ? 1.0727 0.4385 0.3645 -0.1293 0.1114  -0.1142 132 VAL   B N     
8045  C  CA    . VAL   B 107 ? 1.0677 0.4431 0.3516 -0.1668 0.1362  -0.1003 132 VAL   B CA    
8046  C  C     . VAL   B 107 ? 1.0436 0.4343 0.3490 -0.1712 0.1430  -0.1001 132 VAL   B C     
8047  O  O     . VAL   B 107 ? 1.0471 0.4493 0.3556 -0.1966 0.1604  -0.1026 132 VAL   B O     
8048  C  CB    . VAL   B 107 ? 1.0926 0.4600 0.3579 -0.1803 0.1504  -0.0855 132 VAL   B CB    
8049  C  CG1   . VAL   B 107 ? 1.0952 0.4793 0.3578 -0.1834 0.1556  -0.0892 132 VAL   B CG1   
8050  C  CG2   . VAL   B 107 ? 1.1181 0.4743 0.3702 -0.1868 0.1398  -0.0732 132 VAL   B CG2   
8060  N  N     . GLU   B 108 ? 1.0358 0.4347 0.3459 -0.1582 0.1381  -0.0903 133 GLU   B N     
8061  C  CA    . GLU   B 108 ? 1.0090 0.4169 0.3355 -0.1308 0.1339  -0.0976 133 GLU   B CA    
8062  C  C     . GLU   B 108 ? 1.0322 0.4067 0.3409 -0.1318 0.1461  -0.0862 133 GLU   B C     
8063  O  O     . GLU   B 108 ? 1.0604 0.3998 0.3462 -0.1420 0.1473  -0.0787 133 GLU   B O     
8064  C  CB    . GLU   B 108 ? 0.9782 0.4336 0.3236 -0.1293 0.1353  -0.0988 133 GLU   B CB    
8065  C  CG    . GLU   B 108 ? 0.9814 0.4552 0.3236 -0.1167 0.1345  -0.1033 133 GLU   B CG    
8066  C  CD    . GLU   B 108 ? 1.0323 0.4856 0.3276 -0.1141 0.1354  -0.0984 133 GLU   B CD    
8067  O  OE1   . GLU   B 108 ? 1.0488 0.4999 0.3265 -0.1114 0.1462  -0.0886 133 GLU   B OE1   
8068  O  OE2   . GLU   B 108 ? 1.0711 0.4945 0.3381 -0.1060 0.1151  -0.1077 133 GLU   B OE2   
8075  N  N     . LYS   B 109 ? 1.0128 0.4077 0.3307 -0.1304 0.1431  -0.0877 134 LYS   B N     
8076  C  CA    . LYS   B 109 ? 1.0352 0.4543 0.3360 -0.1209 0.1472  -0.0786 134 LYS   B CA    
8077  C  C     . LYS   B 109 ? 1.0493 0.4608 0.3318 -0.1281 0.1615  -0.0693 134 LYS   B C     
8078  O  O     . LYS   B 109 ? 1.0795 0.4724 0.3339 -0.1207 0.1487  -0.0828 134 LYS   B O     
8079  C  CB    . LYS   B 109 ? 1.0419 0.5098 0.3486 -0.0974 0.1448  -0.0552 134 LYS   B CB    
8080  C  CG    . LYS   B 109 ? 1.0447 0.6020 0.3892 -0.0971 0.1293  -0.0230 134 LYS   B CG    
8081  C  CD    . LYS   B 109 ? 1.0464 0.6599 0.4142 -0.0820 0.1354  -0.0115 134 LYS   B CD    
8082  C  CE    . LYS   B 109 ? 1.0555 0.6821 0.4235 -0.0607 0.1413  -0.0237 134 LYS   B CE    
8083  N  NZ    . LYS   B 109 ? 1.0747 0.7097 0.4308 -0.0440 0.1609  -0.0344 134 LYS   B NZ    
8097  N  N     . MET   B 110 ? 1.0178 0.4543 0.3266 -0.1222 0.1717  -0.0763 135 MET   B N     
8098  C  CA    . MET   B 110 ? 1.0074 0.4305 0.3367 -0.0969 0.1889  -0.0766 135 MET   B CA    
8099  C  C     . MET   B 110 ? 0.9707 0.3900 0.3465 -0.0997 0.2117  -0.0746 135 MET   B C     
8100  O  O     . MET   B 110 ? 0.9965 0.3646 0.3443 -0.1228 0.2141  -0.0611 135 MET   B O     
8101  C  CB    . MET   B 110 ? 1.0451 0.4638 0.3536 -0.0769 0.1881  -0.0576 135 MET   B CB    
8102  C  CG    . MET   B 110 ? 1.0477 0.4703 0.3461 -0.0660 0.2082  -0.0611 135 MET   B CG    
8103  S  SD    . MET   B 110 ? 1.0854 0.4857 0.3480 -0.0335 0.2069  -0.0483 135 MET   B SD    
8104  C  CE    . MET   B 110 ? 1.0881 0.4946 0.3430 -0.0101 0.2093  -0.0210 135 MET   B CE    
8114  N  N     . TYR   B 111 ? 0.9077 0.3793 0.3581 -0.0645 0.2261  -0.0817 136 TYR   B N     
8115  C  CA    . TYR   B 111 ? 0.8782 0.3847 0.3667 -0.0453 0.2418  -0.0783 136 TYR   B CA    
8116  C  C     . TYR   B 111 ? 0.8906 0.3454 0.3511 -0.0546 0.2402  -0.0550 136 TYR   B C     
8117  O  O     . TYR   B 111 ? 0.8911 0.3222 0.3507 -0.0583 0.2396  -0.0517 136 TYR   B O     
8118  C  CB    . TYR   B 111 ? 0.8451 0.4400 0.3927 -0.0361 0.2672  -0.0898 136 TYR   B CB    
8119  C  CG    . TYR   B 111 ? 0.8786 0.4993 0.4171 -0.0536 0.2875  -0.1012 136 TYR   B CG    
8120  C  CD1   . TYR   B 111 ? 0.8735 0.5266 0.4247 -0.0562 0.2798  -0.1268 136 TYR   B CD1   
8121  C  CD2   . TYR   B 111 ? 0.8846 0.5266 0.4334 -0.0364 0.2966  -0.1064 136 TYR   B CD2   
8122  C  CE1   . TYR   B 111 ? 0.8504 0.5459 0.4394 -0.0520 0.2850  -0.1398 136 TYR   B CE1   
8123  C  CE2   . TYR   B 111 ? 0.9096 0.5493 0.4477 -0.0478 0.3002  -0.1173 136 TYR   B CE2   
8124  C  CZ    . TYR   B 111 ? 0.9019 0.5600 0.4516 -0.0555 0.2946  -0.1400 136 TYR   B CZ    
8125  O  OH    . TYR   B 111 ? 0.9341 0.5870 0.4701 -0.0851 0.3184  -0.1362 136 TYR   B OH    
8135  N  N     . VAL   B 112 ? 0.8650 0.3259 0.3407 -0.0566 0.2294  -0.0562 137 VAL   B N     
8136  C  CA    . VAL   B 112 ? 0.8203 0.3016 0.3358 -0.0737 0.2323  -0.0554 137 VAL   B CA    
8137  C  C     . VAL   B 112 ? 0.7731 0.3130 0.3461 -0.0645 0.2337  -0.0714 137 VAL   B C     
8138  O  O     . VAL   B 112 ? 0.7264 0.3073 0.3351 -0.0795 0.2214  -0.0814 137 VAL   B O     
8139  C  CB    . VAL   B 112 ? 0.8265 0.2955 0.3383 -0.1087 0.2263  -0.0667 137 VAL   B CB    
8140  C  CG1   . VAL   B 112 ? 0.7765 0.2676 0.3317 -0.1036 0.2352  -0.0554 137 VAL   B CG1   
8141  C  CG2   . VAL   B 112 ? 0.8731 0.3007 0.3537 -0.0970 0.2060  -0.0739 137 VAL   B CG2   
8151  N  N     . PRO   B 113 ? 0.7696 0.3143 0.3592 -0.0518 0.2500  -0.0640 138 PRO   B N     
8152  C  CA    . PRO   B 113 ? 0.7875 0.3093 0.3638 -0.0324 0.2489  -0.0594 138 PRO   B CA    
8153  C  C     . PRO   B 113 ? 0.7906 0.3069 0.3507 -0.0546 0.2441  -0.0504 138 PRO   B C     
8154  O  O     . PRO   B 113 ? 0.7659 0.3068 0.3493 -0.0215 0.2288  -0.0644 138 PRO   B O     
8155  C  CB    . PRO   B 113 ? 0.7741 0.3058 0.3714 0.0005  0.2411  -0.0595 138 PRO   B CB    
8156  C  CG    . PRO   B 113 ? 0.7881 0.3031 0.3712 -0.0202 0.2393  -0.0661 138 PRO   B CG    
8157  C  CD    . PRO   B 113 ? 0.8011 0.3217 0.3738 -0.0358 0.2475  -0.0625 138 PRO   B CD    
8165  N  N     . ALA   B 114 ? 0.8126 0.3212 0.3382 -0.0781 0.2433  -0.0482 139 ALA   B N     
8166  C  CA    . ALA   B 114 ? 0.8003 0.3206 0.3317 -0.0832 0.2404  -0.0412 139 ALA   B CA    
8167  C  C     . ALA   B 114 ? 0.7871 0.3011 0.3291 -0.1013 0.2358  -0.0520 139 ALA   B C     
8168  O  O     . ALA   B 114 ? 0.7737 0.2980 0.3404 -0.0750 0.2380  -0.0613 139 ALA   B O     
8169  C  CB    . ALA   B 114 ? 0.8157 0.3135 0.3268 -0.1137 0.2310  -0.0352 139 ALA   B CB    
8175  N  N     . LEU   B 115 ? 0.7708 0.2936 0.3072 -0.1164 0.2115  -0.0596 140 LEU   B N     
8176  C  CA    . LEU   B 115 ? 0.7787 0.2757 0.2862 -0.1128 0.1831  -0.0550 140 LEU   B CA    
8177  C  C     . LEU   B 115 ? 0.7350 0.2601 0.2783 -0.0782 0.1875  -0.0452 140 LEU   B C     
8178  O  O     . LEU   B 115 ? 0.7526 0.2571 0.2808 -0.0973 0.1817  -0.0503 140 LEU   B O     
8179  C  CB    . LEU   B 115 ? 0.7932 0.2668 0.2836 -0.1481 0.1841  -0.0466 140 LEU   B CB    
8180  C  CG    . LEU   B 115 ? 0.8317 0.2788 0.2890 -0.1433 0.1693  -0.0532 140 LEU   B CG    
8181  C  CD1   . LEU   B 115 ? 0.8521 0.2795 0.2913 -0.0968 0.1563  -0.0533 140 LEU   B CD1   
8182  C  CD2   . LEU   B 115 ? 0.8259 0.2789 0.2981 -0.1439 0.1667  -0.0487 140 LEU   B CD2   
8194  N  N     . ILE   B 116 ? 0.7293 0.2441 0.2832 -0.0784 0.1909  -0.0448 141 ILE   B N     
8195  C  CA    . ILE   B 116 ? 0.6900 0.2106 0.2711 -0.0670 0.1940  -0.0279 141 ILE   B CA    
8196  C  C     . ILE   B 116 ? 0.6753 0.2462 0.2806 -0.0603 0.1974  -0.0429 141 ILE   B C     
8197  O  O     . ILE   B 116 ? 0.6344 0.2498 0.2845 -0.0519 0.2032  -0.0446 141 ILE   B O     
8198  C  CB    . ILE   B 116 ? 0.7264 0.2307 0.2713 -0.0744 0.1845  -0.0354 141 ILE   B CB    
8199  C  CG1   . ILE   B 116 ? 0.7215 0.2461 0.2758 -0.0526 0.1840  -0.0402 141 ILE   B CG1   
8200  C  CG2   . ILE   B 116 ? 0.7451 0.2418 0.2701 -0.1059 0.1735  -0.0234 141 ILE   B CG2   
8201  C  CD1   . ILE   B 116 ? 0.6961 0.2773 0.2857 -0.0461 0.1768  -0.0651 141 ILE   B CD1   
8213  N  N     . PHE   B 117 ? 0.6438 0.2391 0.2936 -0.0733 0.1919  -0.0630 142 PHE   B N     
8214  C  CA    . PHE   B 117 ? 0.6225 0.2378 0.2876 -0.0857 0.2091  -0.0471 142 PHE   B CA    
8215  C  C     . PHE   B 117 ? 0.6469 0.2412 0.2771 -0.0619 0.1900  -0.0311 142 PHE   B C     
8216  O  O     . PHE   B 117 ? 0.6399 0.2447 0.2840 -0.0552 0.1905  -0.0282 142 PHE   B O     
8217  C  CB    . PHE   B 117 ? 0.5697 0.2500 0.3029 -0.0600 0.2186  -0.0494 142 PHE   B CB    
8218  C  CG    . PHE   B 117 ? 0.5858 0.2671 0.3266 -0.0537 0.2292  -0.0526 142 PHE   B CG    
8219  C  CD1   . PHE   B 117 ? 0.5713 0.2846 0.3413 -0.0537 0.2436  -0.0489 142 PHE   B CD1   
8220  C  CD2   . PHE   B 117 ? 0.6147 0.2760 0.3404 -0.0144 0.2350  -0.0512 142 PHE   B CD2   
8221  C  CE1   . PHE   B 117 ? 0.5769 0.2917 0.3572 -0.0289 0.2475  -0.0551 142 PHE   B CE1   
8222  C  CE2   . PHE   B 117 ? 0.6285 0.2949 0.3637 -0.0194 0.2518  -0.0503 142 PHE   B CE2   
8223  C  CZ    . PHE   B 117 ? 0.6069 0.2828 0.3654 -0.0244 0.2584  -0.0428 142 PHE   B CZ    
8233  N  N     . GLY   B 118 ? 0.6766 0.2419 0.2733 -0.0687 0.1762  -0.0213 143 GLY   B N     
8234  C  CA    . GLY   B 118 ? 0.6991 0.2337 0.2616 -0.0501 0.1636  -0.0134 143 GLY   B CA    
8235  C  C     . GLY   B 118 ? 0.7274 0.2438 0.2642 -0.0858 0.1480  0.0016  143 GLY   B C     
8236  O  O     . GLY   B 118 ? 0.7654 0.2714 0.2885 -0.0818 0.1292  0.0234  143 GLY   B O     
8240  N  N     . GLN   B 119 ? 0.6947 0.2528 0.2508 -0.0998 0.1639  -0.0196 144 GLN   B N     
8241  C  CA    . GLN   B 119 ? 0.7030 0.2679 0.2373 -0.0674 0.1541  -0.0237 144 GLN   B CA    
8242  C  C     . GLN   B 119 ? 0.6776 0.2582 0.2219 -0.0508 0.1329  -0.0256 144 GLN   B C     
8243  O  O     . GLN   B 119 ? 0.6368 0.2388 0.2290 -0.0717 0.1107  -0.0319 144 GLN   B O     
8244  C  CB    . GLN   B 119 ? 0.7242 0.3095 0.2447 -0.0254 0.1606  -0.0202 144 GLN   B CB    
8245  C  CG    . GLN   B 119 ? 0.7883 0.3579 0.2665 -0.0243 0.1768  0.0014  144 GLN   B CG    
8246  C  CD    . GLN   B 119 ? 0.8689 0.4037 0.3097 -0.0225 0.1541  -0.0023 144 GLN   B CD    
8247  O  OE1   . GLN   B 119 ? 0.9063 0.4339 0.3361 -0.0333 0.1293  0.0189  144 GLN   B OE1   
8248  N  NE2   . GLN   B 119 ? 0.9078 0.4109 0.3196 -0.0348 0.1589  -0.0023 144 GLN   B NE2   
8257  N  N     . LEU   B 120 ? 0.6680 0.2636 0.2256 -0.0496 0.1167  -0.0034 145 LEU   B N     
8258  C  CA    . LEU   B 120 ? 0.6391 0.2290 0.2258 -0.0323 0.0911  -0.0122 145 LEU   B CA    
8259  C  C     . LEU   B 120 ? 0.6424 0.2322 0.2191 -0.0235 0.0796  0.0001  145 LEU   B C     
8260  O  O     . LEU   B 120 ? 0.6209 0.2320 0.2164 -0.0296 0.0574  0.0078  145 LEU   B O     
8261  C  CB    . LEU   B 120 ? 0.6157 0.2109 0.2391 -0.0184 0.0769  -0.0062 145 LEU   B CB    
8262  C  CG    . LEU   B 120 ? 0.5935 0.2078 0.2621 -0.0244 0.0758  0.0078  145 LEU   B CG    
8263  C  CD1   . LEU   B 120 ? 0.6082 0.2344 0.2640 -0.0053 0.0852  0.0169  145 LEU   B CD1   
8264  C  CD2   . LEU   B 120 ? 0.5941 0.2429 0.2980 0.0123  0.0436  0.0044  145 LEU   B CD2   
8276  N  N     . LEU   B 121 ? 0.6343 0.2144 0.2131 -0.0357 0.0665  0.0075  146 LEU   B N     
8277  C  CA    . LEU   B 121 ? 0.6199 0.2010 0.2269 -0.0455 0.0746  -0.0100 146 LEU   B CA    
8278  C  C     . LEU   B 121 ? 0.6165 0.2097 0.2226 -0.0491 0.0815  -0.0355 146 LEU   B C     
8279  O  O     . LEU   B 121 ? 0.6426 0.2051 0.2290 -0.0201 0.0773  -0.0221 146 LEU   B O     
8280  C  CB    . LEU   B 121 ? 0.6206 0.1967 0.2401 -0.0565 0.0615  -0.0109 146 LEU   B CB    
8281  C  CG    . LEU   B 121 ? 0.6295 0.2340 0.2577 -0.0458 0.0810  -0.0415 146 LEU   B CG    
8282  C  CD1   . LEU   B 121 ? 0.6678 0.2277 0.2850 -0.0399 0.0700  -0.0181 146 LEU   B CD1   
8283  C  CD2   . LEU   B 121 ? 0.6106 0.2691 0.2587 -0.0567 0.0905  -0.0450 146 LEU   B CD2   
8295  N  N     . THR   B 122 ? 0.5597 0.2207 0.2184 -0.0846 0.1017  -0.0473 147 THR   B N     
8296  C  CA    . THR   B 122 ? 0.5366 0.1938 0.2271 -0.0619 0.1226  -0.0319 147 THR   B CA    
8297  C  C     . THR   B 122 ? 0.5459 0.2165 0.2322 -0.0359 0.1093  -0.0447 147 THR   B C     
8298  O  O     . THR   B 122 ? 0.5274 0.2212 0.2567 -0.0487 0.0922  -0.0223 147 THR   B O     
8299  C  CB    . THR   B 122 ? 0.5396 0.2266 0.2281 -0.0706 0.1189  -0.0292 147 THR   B CB    
8300  O  OG1   . THR   B 122 ? 0.5689 0.2232 0.2366 -0.0606 0.1030  -0.0200 147 THR   B OG1   
8301  C  CG2   . THR   B 122 ? 0.5701 0.2537 0.2387 -0.0489 0.0876  -0.0074 147 THR   B CG2   
8309  N  N     . SER   B 123 ? 0.5092 0.1847 0.2154 -0.0162 0.1066  -0.0282 148 SER   B N     
8310  C  CA    . SER   B 123 ? 0.4457 0.2138 0.2248 0.0002  0.0850  -0.0394 148 SER   B CA    
8311  C  C     . SER   B 123 ? 0.4731 0.2172 0.2270 0.0147  0.0883  -0.0448 148 SER   B C     
8312  O  O     . SER   B 123 ? 0.4946 0.2371 0.2058 -0.0056 0.0774  -0.0431 148 SER   B O     
8313  C  CB    . SER   B 123 ? 0.3921 0.2178 0.2209 -0.0100 0.0691  -0.0351 148 SER   B CB    
8314  O  OG    . SER   B 123 ? 0.3997 0.2085 0.2363 0.0143  0.0598  -0.0304 148 SER   B OG    
8320  N  N     . SER   B 124 ? 0.4653 0.2215 0.2555 0.0335  0.0996  -0.0578 149 SER   B N     
8321  C  CA    . SER   B 124 ? 0.4568 0.2327 0.2883 0.0163  0.1086  -0.0512 149 SER   B CA    
8322  C  C     . SER   B 124 ? 0.4276 0.2003 0.2832 0.0011  0.0885  -0.0442 149 SER   B C     
8323  O  O     . SER   B 124 ? 0.4284 0.2038 0.2959 -0.0149 0.0812  -0.0398 149 SER   B O     
8324  C  CB    . SER   B 124 ? 0.4387 0.2310 0.3138 0.0148  0.1303  -0.0665 149 SER   B CB    
8325  O  OG    . SER   B 124 ? 0.4336 0.2277 0.3342 0.0201  0.1241  -0.0661 149 SER   B OG    
8331  N  N     . ASN   B 125 ? 0.4017 0.2017 0.2757 -0.0242 0.0838  -0.0415 150 ASN   B N     
8332  C  CA    . ASN   B 125 ? 0.3693 0.1970 0.2517 -0.0051 0.0732  -0.0487 150 ASN   B CA    
8333  C  C     . ASN   B 125 ? 0.3936 0.2413 0.2486 -0.0133 0.0801  -0.0435 150 ASN   B C     
8334  O  O     . ASN   B 125 ? 0.3685 0.2796 0.2608 -0.0357 0.0624  -0.0500 150 ASN   B O     
8335  C  CB    . ASN   B 125 ? 0.3646 0.2186 0.2577 0.0071  0.0949  -0.0162 150 ASN   B CB    
8336  C  CG    . ASN   B 125 ? 0.3490 0.2194 0.2774 0.0142  0.1054  0.0030  150 ASN   B CG    
8337  O  OD1   . ASN   B 125 ? 0.3626 0.2198 0.3135 -0.0073 0.0882  0.0290  150 ASN   B OD1   
8338  N  ND2   . ASN   B 125 ? 0.3755 0.2403 0.2682 0.0020  0.0998  -0.0184 150 ASN   B ND2   
8345  N  N     . TYR   B 126 ? 0.4009 0.2217 0.2326 -0.0305 0.0782  -0.0294 151 TYR   B N     
8346  C  CA    . TYR   B 126 ? 0.3968 0.2037 0.2483 -0.0320 0.0405  -0.0164 151 TYR   B CA    
8347  C  C     . TYR   B 126 ? 0.4009 0.2024 0.2989 -0.0179 0.0275  -0.0181 151 TYR   B C     
8348  O  O     . TYR   B 126 ? 0.4127 0.2381 0.3315 -0.0181 0.0244  0.0040  151 TYR   B O     
8349  C  CB    . TYR   B 126 ? 0.3915 0.1932 0.2296 -0.0166 0.0155  -0.0169 151 TYR   B CB    
8350  C  CG    . TYR   B 126 ? 0.4431 0.2007 0.2228 -0.0185 0.0186  -0.0191 151 TYR   B CG    
8351  C  CD1   . TYR   B 126 ? 0.4243 0.1639 0.2155 -0.0246 0.0257  -0.0302 151 TYR   B CD1   
8352  C  CD2   . TYR   B 126 ? 0.4822 0.2238 0.2228 -0.0147 0.0260  -0.0218 151 TYR   B CD2   
8353  C  CE1   . TYR   B 126 ? 0.4186 0.1882 0.2071 -0.0364 0.0145  -0.0237 151 TYR   B CE1   
8354  C  CE2   . TYR   B 126 ? 0.4826 0.2098 0.2262 -0.0336 0.0421  -0.0331 151 TYR   B CE2   
8355  C  CZ    . TYR   B 126 ? 0.4616 0.2055 0.2101 -0.0367 0.0417  -0.0255 151 TYR   B CZ    
8356  O  OH    . TYR   B 126 ? 0.5300 0.2231 0.2224 -0.0225 0.0267  -0.0131 151 TYR   B OH    
8366  N  N     . ASP   B 127 ? 0.4321 0.1945 0.3025 -0.0378 0.0172  -0.0278 152 ASP   B N     
8367  C  CA    . ASP   B 127 ? 0.4791 0.1987 0.3238 -0.0269 -0.0045 -0.0455 152 ASP   B CA    
8368  C  C     . ASP   B 127 ? 0.4697 0.2106 0.3376 -0.0183 -0.0047 -0.0252 152 ASP   B C     
8369  O  O     . ASP   B 127 ? 0.4960 0.2335 0.3440 0.0033  0.0179  -0.0424 152 ASP   B O     
8370  C  CB    . ASP   B 127 ? 0.5566 0.2154 0.3494 -0.0123 -0.0181 -0.0644 152 ASP   B CB    
8371  C  CG    . ASP   B 127 ? 0.6387 0.2451 0.3844 -0.0196 -0.0085 -0.0660 152 ASP   B CG    
8372  O  OD1   . ASP   B 127 ? 0.6315 0.2562 0.3982 -0.0495 -0.0036 -0.0558 152 ASP   B OD1   
8373  O  OD2   . ASP   B 127 ? 0.7004 0.2682 0.4029 -0.0223 -0.0113 -0.0681 152 ASP   B OD2   
8378  N  N     . ASP   B 128 ? 0.4616 0.2151 0.3526 -0.0116 -0.0283 0.0025  153 ASP   B N     
8379  C  CA    . ASP   B 128 ? 0.4444 0.2193 0.3762 -0.0362 0.0111  0.0092  153 ASP   B CA    
8380  C  C     . ASP   B 128 ? 0.4950 0.2212 0.3817 -0.0330 -0.0079 0.0089  153 ASP   B C     
8381  O  O     . ASP   B 128 ? 0.5089 0.2525 0.3789 -0.0520 -0.0107 0.0119  153 ASP   B O     
8382  C  CB    . ASP   B 128 ? 0.4520 0.2409 0.4156 -0.0623 0.0205  -0.0096 153 ASP   B CB    
8383  C  CG    . ASP   B 128 ? 0.4886 0.2755 0.4558 -0.0514 0.0240  -0.0360 153 ASP   B CG    
8384  O  OD1   . ASP   B 128 ? 0.5443 0.2731 0.4529 -0.0451 -0.0029 -0.0745 153 ASP   B OD1   
8385  O  OD2   . ASP   B 128 ? 0.4931 0.3212 0.4879 -0.0229 0.0356  -0.0182 153 ASP   B OD2   
8390  N  N     . ASP   B 129 ? 0.4843 0.2150 0.3934 -0.0357 -0.0294 -0.0036 154 ASP   B N     
8391  C  CA    . ASP   B 129 ? 0.5225 0.2296 0.4093 -0.0616 -0.0274 -0.0158 154 ASP   B CA    
8392  C  C     . ASP   B 129 ? 0.5248 0.2107 0.3917 -0.0401 0.0025  0.0056  154 ASP   B C     
8393  O  O     . ASP   B 129 ? 0.5488 0.2410 0.3994 -0.0056 -0.0133 0.0209  154 ASP   B O     
8394  C  CB    . ASP   B 129 ? 0.5661 0.2776 0.4637 -0.0840 -0.0333 -0.0629 154 ASP   B CB    
8395  C  CG    . ASP   B 129 ? 0.6542 0.3762 0.5164 -0.0829 -0.0390 -0.0836 154 ASP   B CG    
8396  O  OD1   . ASP   B 129 ? 0.6521 0.4151 0.5466 -0.0970 -0.0302 -0.0727 154 ASP   B OD1   
8397  O  OD2   . ASP   B 129 ? 0.7064 0.4322 0.5328 -0.0710 -0.0596 -0.0875 154 ASP   B OD2   
8402  N  N     . GLU   B 130 ? 0.5119 0.2078 0.3821 -0.0503 0.0017  -0.0414 155 GLU   B N     
8403  C  CA    . GLU   B 130 ? 0.5182 0.2183 0.3752 -0.0476 0.0185  -0.0560 155 GLU   B CA    
8404  C  C     . GLU   B 130 ? 0.4806 0.2414 0.3628 -0.0349 -0.0078 -0.0440 155 GLU   B C     
8405  O  O     . GLU   B 130 ? 0.4515 0.2359 0.3552 -0.0148 0.0006  -0.0469 155 GLU   B O     
8406  C  CB    . GLU   B 130 ? 0.5576 0.2531 0.4029 -0.0017 0.0403  -0.0596 155 GLU   B CB    
8407  C  CG    . GLU   B 130 ? 0.6345 0.2901 0.4367 0.0134  0.0607  -0.0680 155 GLU   B CG    
8408  C  CD    . GLU   B 130 ? 0.7017 0.3176 0.4675 0.0370  0.0839  -0.0665 155 GLU   B CD    
8409  O  OE1   . GLU   B 130 ? 0.7545 0.3595 0.4925 0.0736  0.1047  -0.0583 155 GLU   B OE1   
8410  O  OE2   . GLU   B 130 ? 0.6903 0.3256 0.4779 0.0169  0.0749  -0.0568 155 GLU   B OE2   
8417  N  N     . LYS   B 131 ? 0.4270 0.2618 0.3628 -0.0585 -0.0358 -0.0294 156 LYS   B N     
8418  C  CA    . LYS   B 131 ? 0.3477 0.2367 0.3646 -0.0614 -0.0521 -0.0178 156 LYS   B CA    
8419  C  C     . LYS   B 131 ? 0.3324 0.2539 0.3858 -0.0185 -0.0315 0.0140  156 LYS   B C     
8420  O  O     . LYS   B 131 ? 0.3854 0.3160 0.4271 -0.0501 -0.0543 0.0450  156 LYS   B O     
8421  C  CB    . LYS   B 131 ? 0.3639 0.2637 0.3761 -0.0653 -0.0595 -0.0135 156 LYS   B CB    
8422  C  CG    . LYS   B 131 ? 0.4030 0.3577 0.3942 -0.0694 -0.0496 0.0070  156 LYS   B CG    
8423  C  CD    . LYS   B 131 ? 0.3897 0.4095 0.4188 -0.1002 -0.0469 0.0368  156 LYS   B CD    
8424  C  CE    . LYS   B 131 ? 0.4059 0.4495 0.4465 -0.1045 -0.0197 0.0588  156 LYS   B CE    
8425  N  NZ    . LYS   B 131 ? 0.4084 0.4695 0.4573 -0.0878 0.0188  0.0926  156 LYS   B NZ    
8439  N  N     . LYS   B 132 ? 0.3140 0.1960 0.3626 -0.0017 -0.0236 -0.0266 157 LYS   B N     
8440  C  CA    . LYS   B 132 ? 0.2689 0.1885 0.3453 0.0168  -0.0138 -0.0312 157 LYS   B CA    
8441  C  C     . LYS   B 132 ? 0.2323 0.1853 0.3260 0.0352  0.0228  -0.0256 157 LYS   B C     
8442  O  O     . LYS   B 132 ? 0.2303 0.2300 0.3420 0.0337  0.0323  -0.0349 157 LYS   B O     
8443  C  CB    . LYS   B 132 ? 0.3583 0.2245 0.3619 0.0114  -0.0057 -0.0540 157 LYS   B CB    
8444  C  CG    . LYS   B 132 ? 0.4571 0.2394 0.3837 0.0208  0.0154  -0.0750 157 LYS   B CG    
8445  C  CD    . LYS   B 132 ? 0.5270 0.2543 0.3992 0.0171  0.0275  -0.0864 157 LYS   B CD    
8446  C  CE    . LYS   B 132 ? 0.5481 0.2563 0.4351 0.0394  0.0313  -0.0886 157 LYS   B CE    
8447  N  NZ    . LYS   B 132 ? 0.6108 0.3260 0.4465 0.0608  0.0446  -0.0762 157 LYS   B NZ    
8461  N  N     . VAL   B 133 ? 0.2559 0.2007 0.3129 0.0264  0.0374  -0.0129 158 VAL   B N     
8462  C  CA    . VAL   B 133 ? 0.2406 0.2263 0.3188 0.0125  0.0330  -0.0102 158 VAL   B CA    
8463  C  C     . VAL   B 133 ? 0.2690 0.2290 0.3204 0.0023  0.0557  -0.0063 158 VAL   B C     
8464  O  O     . VAL   B 133 ? 0.2555 0.2404 0.3297 0.0226  0.0434  0.0018  158 VAL   B O     
8465  C  CB    . VAL   B 133 ? 0.2436 0.2292 0.3247 0.0305  -0.0021 -0.0012 158 VAL   B CB    
8466  C  CG1   . VAL   B 133 ? 0.2565 0.2181 0.3161 0.0427  -0.0159 -0.0166 158 VAL   B CG1   
8467  C  CG2   . VAL   B 133 ? 0.2602 0.2249 0.3265 0.0536  -0.0089 -0.0083 158 VAL   B CG2   
8477  N  N     . THR   B 134 ? 0.2998 0.2204 0.3150 -0.0218 0.0542  -0.0166 159 THR   B N     
8478  C  CA    . THR   B 134 ? 0.2943 0.2246 0.3133 0.0022  0.0613  -0.0300 159 THR   B CA    
8479  C  C     . THR   B 134 ? 0.2509 0.2133 0.3008 -0.0105 0.0541  -0.0199 159 THR   B C     
8480  O  O     . THR   B 134 ? 0.2536 0.2397 0.3020 -0.0042 0.0482  -0.0228 159 THR   B O     
8481  C  CB    . THR   B 134 ? 0.3136 0.2638 0.3322 0.0182  0.0463  -0.0341 159 THR   B CB    
8482  O  OG1   . THR   B 134 ? 0.3678 0.2842 0.3280 -0.0213 0.0599  -0.0336 159 THR   B OG1   
8483  C  CG2   . THR   B 134 ? 0.3724 0.2780 0.3540 0.0319  0.0453  -0.0334 159 THR   B CG2   
8491  N  N     . GLY   B 135 ? 0.2688 0.2034 0.2938 -0.0013 0.0497  -0.0055 160 GLY   B N     
8492  C  CA    . GLY   B 135 ? 0.2825 0.1987 0.2945 0.0031  0.0483  -0.0142 160 GLY   B CA    
8493  C  C     . GLY   B 135 ? 0.3028 0.1985 0.2829 0.0052  0.0442  -0.0184 160 GLY   B C     
8494  O  O     . GLY   B 135 ? 0.2918 0.2090 0.2992 0.0359  0.0426  -0.0068 160 GLY   B O     
8498  N  N     . GLY   B 136 ? 0.3075 0.2156 0.2745 -0.0033 0.0718  0.0087  161 GLY   B N     
8499  C  CA    . GLY   B 136 ? 0.3279 0.2284 0.2662 -0.0079 0.0878  0.0126  161 GLY   B CA    
8500  C  C     . GLY   B 136 ? 0.3285 0.2103 0.2466 -0.0226 0.0797  0.0012  161 GLY   B C     
8501  O  O     . GLY   B 136 ? 0.3482 0.2008 0.2540 0.0179  0.0695  -0.0124 161 GLY   B O     
8505  N  N     . ARG   B 137 ? 0.3198 0.1975 0.2388 -0.0159 0.0478  -0.0047 162 ARG   B N     
8506  C  CA    . ARG   B 137 ? 0.3055 0.1898 0.2397 -0.0198 0.0370  -0.0067 162 ARG   B CA    
8507  C  C     . ARG   B 137 ? 0.3557 0.2078 0.2422 -0.0277 0.0431  -0.0114 162 ARG   B C     
8508  O  O     . ARG   B 137 ? 0.4077 0.2262 0.2527 -0.0346 0.0320  -0.0265 162 ARG   B O     
8509  C  CB    . ARG   B 137 ? 0.2939 0.1861 0.2395 0.0014  0.0314  0.0005  162 ARG   B CB    
8510  C  CG    . ARG   B 137 ? 0.2935 0.2188 0.2466 0.0305  0.0318  0.0219  162 ARG   B CG    
8511  C  CD    . ARG   B 137 ? 0.2883 0.2103 0.2676 0.0211  0.0564  0.0292  162 ARG   B CD    
8512  N  NE    . ARG   B 137 ? 0.2967 0.2397 0.2887 0.0162  0.0707  0.0255  162 ARG   B NE    
8513  C  CZ    . ARG   B 137 ? 0.3063 0.2536 0.2970 0.0175  0.0598  0.0418  162 ARG   B CZ    
8514  N  NH1   . ARG   B 137 ? 0.3392 0.2919 0.2816 0.0253  0.0407  0.0292  162 ARG   B NH1   
8515  N  NH2   . ARG   B 137 ? 0.3203 0.2803 0.3160 0.0023  0.0217  0.0609  162 ARG   B NH2   
8529  N  N     . ASN   B 138 ? 0.3302 0.2112 0.2416 -0.0395 0.0369  -0.0085 163 ASN   B N     
8530  C  CA    . ASN   B 138 ? 0.3267 0.2119 0.2314 -0.0393 0.0279  -0.0081 163 ASN   B CA    
8531  C  C     . ASN   B 138 ? 0.3702 0.2006 0.2264 -0.0205 0.0494  -0.0114 163 ASN   B C     
8532  O  O     . ASN   B 138 ? 0.4263 0.2160 0.2263 -0.0302 0.0437  -0.0003 163 ASN   B O     
8533  C  CB    . ASN   B 138 ? 0.3236 0.2450 0.2311 -0.0111 0.0472  0.0115  163 ASN   B CB    
8534  C  CG    . ASN   B 138 ? 0.3658 0.2953 0.2654 -0.0285 0.0428  0.0010  163 ASN   B CG    
8535  O  OD1   . ASN   B 138 ? 0.3293 0.2869 0.2815 -0.0431 0.0203  0.0132  163 ASN   B OD1   
8536  N  ND2   . ASN   B 138 ? 0.4343 0.3012 0.2769 -0.0521 0.0463  -0.0215 163 ASN   B ND2   
8543  N  N     . GLY   B 139 ? 0.3975 0.1933 0.2145 -0.0154 0.0591  -0.0076 164 GLY   B N     
8544  C  CA    . GLY   B 139 ? 0.4352 0.1995 0.2100 -0.0580 0.0809  0.0053  164 GLY   B CA    
8545  C  C     . GLY   B 139 ? 0.4464 0.1872 0.2094 -0.0329 0.0958  -0.0072 164 GLY   B C     
8546  O  O     . GLY   B 139 ? 0.5007 0.1941 0.2095 -0.0139 0.1026  -0.0139 164 GLY   B O     
8550  N  N     . TYR   B 140 ? 0.4550 0.1858 0.2323 -0.0501 0.0869  -0.0206 165 TYR   B N     
8551  C  CA    . TYR   B 140 ? 0.4351 0.1933 0.2396 -0.0369 0.0986  -0.0357 165 TYR   B CA    
8552  C  C     . TYR   B 140 ? 0.4083 0.2062 0.2378 -0.0125 0.1071  -0.0270 165 TYR   B C     
8553  O  O     . TYR   B 140 ? 0.4250 0.2308 0.2273 -0.0337 0.1315  -0.0289 165 TYR   B O     
8554  C  CB    . TYR   B 140 ? 0.4268 0.2134 0.2512 -0.0138 0.0889  -0.0430 165 TYR   B CB    
8555  C  CG    . TYR   B 140 ? 0.4082 0.2321 0.2871 -0.0222 0.0748  -0.0296 165 TYR   B CG    
8556  C  CD1   . TYR   B 140 ? 0.4208 0.2563 0.3138 -0.0277 0.0728  -0.0088 165 TYR   B CD1   
8557  C  CD2   . TYR   B 140 ? 0.4288 0.2691 0.3138 -0.0276 0.0340  -0.0356 165 TYR   B CD2   
8558  C  CE1   . TYR   B 140 ? 0.4266 0.2913 0.3340 -0.0168 0.0563  -0.0107 165 TYR   B CE1   
8559  C  CE2   . TYR   B 140 ? 0.4341 0.2935 0.3270 0.0004  0.0300  -0.0436 165 TYR   B CE2   
8560  C  CZ    . TYR   B 140 ? 0.4556 0.3047 0.3414 0.0099  0.0338  -0.0383 165 TYR   B CZ    
8561  O  OH    . TYR   B 140 ? 0.5094 0.3505 0.3473 0.0190  -0.0031 -0.0606 165 TYR   B OH    
8571  N  N     . GLY   B 141 ? 0.3848 0.1679 0.2398 -0.0095 0.1031  -0.0385 166 GLY   B N     
8572  C  CA    . GLY   B 141 ? 0.3638 0.1880 0.2521 -0.0360 0.1317  -0.0407 166 GLY   B CA    
8573  C  C     . GLY   B 141 ? 0.3861 0.1953 0.2632 -0.0478 0.1460  -0.0500 166 GLY   B C     
8574  O  O     . GLY   B 141 ? 0.4082 0.1960 0.2686 -0.0420 0.1415  -0.0614 166 GLY   B O     
8578  N  N     . ALA   B 142 ? 0.4252 0.2238 0.2703 -0.0201 0.1609  -0.0315 167 ALA   B N     
8579  C  CA    . ALA   B 142 ? 0.4510 0.2103 0.2713 -0.0128 0.1861  -0.0124 167 ALA   B CA    
8580  C  C     . ALA   B 142 ? 0.4810 0.2251 0.2734 -0.0166 0.1939  -0.0003 167 ALA   B C     
8581  O  O     . ALA   B 142 ? 0.5110 0.2301 0.3007 -0.0264 0.2084  -0.0139 167 ALA   B O     
8582  C  CB    . ALA   B 142 ? 0.4425 0.2309 0.2873 -0.0001 0.1970  -0.0169 167 ALA   B CB    
8588  N  N     . LYS   B 143 ? 0.4973 0.2228 0.2596 -0.0226 0.1783  -0.0233 168 LYS   B N     
8589  C  CA    . LYS   B 143 ? 0.5225 0.2018 0.2461 -0.0304 0.1757  -0.0289 168 LYS   B CA    
8590  C  C     . LYS   B 143 ? 0.5274 0.2068 0.2458 -0.0472 0.1809  -0.0293 168 LYS   B C     
8591  O  O     . LYS   B 143 ? 0.5812 0.2158 0.2466 -0.0528 0.1674  -0.0127 168 LYS   B O     
8592  C  CB    . LYS   B 143 ? 0.5592 0.2047 0.2317 -0.0080 0.1609  -0.0249 168 LYS   B CB    
8593  C  CG    . LYS   B 143 ? 0.5811 0.1981 0.2366 0.0069  0.1498  -0.0218 168 LYS   B CG    
8594  C  CD    . LYS   B 143 ? 0.5702 0.1865 0.2351 0.0103  0.1466  -0.0083 168 LYS   B CD    
8595  C  CE    . LYS   B 143 ? 0.5511 0.1836 0.2408 -0.0083 0.1394  0.0064  168 LYS   B CE    
8596  N  NZ    . LYS   B 143 ? 0.5331 0.2075 0.2449 -0.0270 0.1371  -0.0259 168 LYS   B NZ    
8610  N  N     . LEU   B 144 ? 0.5040 0.2103 0.2539 -0.0177 0.1761  -0.0270 169 LEU   B N     
8611  C  CA    . LEU   B 144 ? 0.4489 0.2061 0.2605 -0.0414 0.1867  -0.0228 169 LEU   B CA    
8612  C  C     . LEU   B 144 ? 0.4642 0.2089 0.2882 -0.0427 0.1736  -0.0296 169 LEU   B C     
8613  O  O     . LEU   B 144 ? 0.5107 0.1942 0.2960 -0.0564 0.1532  -0.0259 169 LEU   B O     
8614  C  CB    . LEU   B 144 ? 0.4275 0.1964 0.2595 -0.0223 0.1850  -0.0002 169 LEU   B CB    
8615  C  CG    . LEU   B 144 ? 0.4798 0.2076 0.2581 0.0063  0.1906  -0.0004 169 LEU   B CG    
8616  C  CD1   . LEU   B 144 ? 0.4796 0.2043 0.2657 0.0399  0.1759  -0.0111 169 LEU   B CD1   
8617  C  CD2   . LEU   B 144 ? 0.4894 0.2384 0.2564 0.0246  0.1806  -0.0210 169 LEU   B CD2   
8629  N  N     . CYS   B 145 ? 0.4139 0.2208 0.3029 -0.0635 0.2006  -0.0266 170 CYS   B N     
8630  C  CA    . CYS   B 145 ? 0.4432 0.2038 0.3136 -0.0532 0.2124  -0.0289 170 CYS   B CA    
8631  C  C     . CYS   B 145 ? 0.5265 0.2128 0.2959 -0.0513 0.2012  -0.0371 170 CYS   B C     
8632  O  O     . CYS   B 145 ? 0.5189 0.2418 0.2930 -0.0512 0.1867  -0.0324 170 CYS   B O     
8633  C  CB    . CYS   B 145 ? 0.4497 0.1960 0.3530 -0.0627 0.2065  -0.0234 170 CYS   B CB    
8634  S  SG    . CYS   B 145 ? 0.4307 0.2558 0.3963 -0.0338 0.1913  -0.0294 170 CYS   B SG    
8640  N  N     . ASN   B 146 ? 0.5845 0.2115 0.2951 -0.0509 0.2098  -0.0434 171 ASN   B N     
8641  C  CA    . ASN   B 146 ? 0.6098 0.2106 0.2938 -0.0470 0.2135  -0.0348 171 ASN   B CA    
8642  C  C     . ASN   B 146 ? 0.6266 0.2205 0.2944 -0.0515 0.2168  -0.0174 171 ASN   B C     
8643  O  O     . ASN   B 146 ? 0.6729 0.2168 0.3090 -0.0735 0.2086  -0.0214 171 ASN   B O     
8644  C  CB    . ASN   B 146 ? 0.6023 0.2139 0.2947 -0.0465 0.2140  -0.0362 171 ASN   B CB    
8645  C  CG    . ASN   B 146 ? 0.6641 0.2244 0.2996 -0.0578 0.2176  -0.0368 171 ASN   B CG    
8646  O  OD1   . ASN   B 146 ? 0.6986 0.2378 0.3062 -0.0907 0.2228  -0.0372 171 ASN   B OD1   
8647  N  ND2   . ASN   B 146 ? 0.6636 0.2522 0.2979 -0.0561 0.2200  -0.0298 171 ASN   B ND2   
8654  N  N     . ILE   B 147 ? 0.5871 0.2174 0.2888 -0.0300 0.2148  -0.0131 172 ILE   B N     
8655  C  CA    . ILE   B 147 ? 0.6010 0.2182 0.2725 -0.0337 0.1988  -0.0018 172 ILE   B CA    
8656  C  C     . ILE   B 147 ? 0.6015 0.2006 0.2792 -0.0417 0.1849  0.0071  172 ILE   B C     
8657  O  O     . ILE   B 147 ? 0.6460 0.1948 0.2874 -0.0415 0.1660  0.0095  172 ILE   B O     
8658  C  CB    . ILE   B 147 ? 0.6097 0.2273 0.2588 0.0132  0.1761  -0.0196 172 ILE   B CB    
8659  C  CG1   . ILE   B 147 ? 0.6171 0.2254 0.2463 0.0094  0.1504  -0.0052 172 ILE   B CG1   
8660  C  CG2   . ILE   B 147 ? 0.6039 0.2491 0.2583 0.0233  0.1628  -0.0012 172 ILE   B CG2   
8661  C  CD1   . ILE   B 147 ? 0.6195 0.2510 0.2317 -0.0159 0.1451  0.0326  172 ILE   B CD1   
8673  N  N     . PHE   B 148 ? 0.5607 0.2009 0.2717 -0.0514 0.1876  -0.0020 173 PHE   B N     
8674  C  CA    . PHE   B 148 ? 0.5501 0.2131 0.2758 -0.0627 0.1878  -0.0024 173 PHE   B CA    
8675  C  C     . PHE   B 148 ? 0.5786 0.2017 0.3043 -0.0576 0.2145  -0.0277 173 PHE   B C     
8676  O  O     . PHE   B 148 ? 0.5899 0.2219 0.3248 -0.0729 0.2271  -0.0222 173 PHE   B O     
8677  C  CB    . PHE   B 148 ? 0.5570 0.2244 0.2635 -0.0517 0.1689  -0.0082 173 PHE   B CB    
8678  C  CG    . PHE   B 148 ? 0.5389 0.2043 0.2545 -0.0149 0.1307  -0.0081 173 PHE   B CG    
8679  C  CD1   . PHE   B 148 ? 0.5446 0.2281 0.2640 0.0148  0.1176  0.0040  173 PHE   B CD1   
8680  C  CD2   . PHE   B 148 ? 0.5515 0.2310 0.2485 -0.0120 0.1101  -0.0031 173 PHE   B CD2   
8681  C  CE1   . PHE   B 148 ? 0.5484 0.2325 0.2603 0.0308  0.1270  0.0065  173 PHE   B CE1   
8682  C  CE2   . PHE   B 148 ? 0.5475 0.2425 0.2555 -0.0168 0.0922  -0.0013 173 PHE   B CE2   
8683  C  CZ    . PHE   B 148 ? 0.5411 0.2432 0.2558 0.0175  0.1134  0.0005  173 PHE   B CZ    
8693  N  N     . SER   B 149 ? 0.5993 0.2152 0.3288 -0.0780 0.2228  -0.0260 174 SER   B N     
8694  C  CA    . SER   B 149 ? 0.6016 0.2473 0.3404 -0.0782 0.2347  -0.0160 174 SER   B CA    
8695  C  C     . SER   B 149 ? 0.6649 0.2727 0.3612 -0.0909 0.2317  -0.0203 174 SER   B C     
8696  O  O     . SER   B 149 ? 0.6704 0.2902 0.3585 -0.1173 0.2271  -0.0070 174 SER   B O     
8697  C  CB    . SER   B 149 ? 0.6122 0.2693 0.3421 -0.0657 0.2238  -0.0144 174 SER   B CB    
8698  O  OG    . SER   B 149 ? 0.5839 0.2677 0.3456 -0.0742 0.2021  -0.0111 174 SER   B OG    
8704  N  N     . THR   B 150 ? 0.6905 0.2686 0.3637 -0.0901 0.2405  -0.0058 175 THR   B N     
8705  C  CA    . THR   B 150 ? 0.7212 0.2783 0.3811 -0.0980 0.2626  -0.0219 175 THR   B CA    
8706  C  C     . THR   B 150 ? 0.7694 0.2861 0.3857 -0.1021 0.2753  -0.0336 175 THR   B C     
8707  O  O     . THR   B 150 ? 0.8252 0.2949 0.3827 -0.1065 0.2645  -0.0224 175 THR   B O     
8708  C  CB    . THR   B 150 ? 0.7551 0.2946 0.4143 -0.1209 0.2539  -0.0248 175 THR   B CB    
8709  O  OG1   . THR   B 150 ? 0.7403 0.3095 0.4300 -0.1348 0.2556  -0.0215 175 THR   B OG1   
8710  C  CG2   . THR   B 150 ? 0.7571 0.2717 0.4218 -0.1287 0.2605  -0.0425 175 THR   B CG2   
8718  N  N     . LYS   B 151 ? 0.7362 0.2913 0.3957 -0.0917 0.2866  -0.0383 176 LYS   B N     
8719  C  CA    . LYS   B 151 ? 0.7321 0.3121 0.4154 -0.1032 0.2982  -0.0486 176 LYS   B CA    
8720  C  C     . LYS   B 151 ? 0.7039 0.2765 0.4070 -0.0852 0.2938  -0.0478 176 LYS   B C     
8721  O  O     . LYS   B 151 ? 0.7102 0.2764 0.3982 -0.0680 0.2882  -0.0515 176 LYS   B O     
8722  C  CB    . LYS   B 151 ? 0.7297 0.3811 0.4490 -0.1194 0.3142  -0.0616 176 LYS   B CB    
8723  C  CG    . LYS   B 151 ? 0.7441 0.4394 0.4860 -0.1502 0.3091  -0.0590 176 LYS   B CG    
8724  C  CD    . LYS   B 151 ? 0.7914 0.4971 0.5292 -0.1563 0.2715  -0.0518 176 LYS   B CD    
8725  C  CE    . LYS   B 151 ? 0.8509 0.5357 0.5675 -0.1533 0.2508  -0.0476 176 LYS   B CE    
8726  N  NZ    . LYS   B 151 ? 0.8908 0.5674 0.5941 -0.1624 0.2351  -0.0392 176 LYS   B NZ    
8740  N  N     . PHE   B 152 ? 0.6720 0.2819 0.4102 -0.0684 0.2939  -0.0448 177 PHE   B N     
8741  C  CA    . PHE   B 152 ? 0.6373 0.2583 0.4193 -0.0613 0.2937  -0.0502 177 PHE   B CA    
8742  C  C     . PHE   B 152 ? 0.6709 0.2971 0.4314 -0.0935 0.3026  -0.0672 177 PHE   B C     
8743  O  O     . PHE   B 152 ? 0.6772 0.3134 0.4257 -0.1254 0.2963  -0.0719 177 PHE   B O     
8744  C  CB    . PHE   B 152 ? 0.6439 0.2557 0.4148 -0.0464 0.2940  -0.0318 177 PHE   B CB    
8745  C  CG    . PHE   B 152 ? 0.5897 0.2524 0.4100 -0.0557 0.2836  -0.0377 177 PHE   B CG    
8746  C  CD1   . PHE   B 152 ? 0.5509 0.2755 0.4130 -0.0672 0.2772  -0.0472 177 PHE   B CD1   
8747  C  CD2   . PHE   B 152 ? 0.5738 0.2630 0.4140 -0.0581 0.2799  -0.0250 177 PHE   B CD2   
8748  C  CE1   . PHE   B 152 ? 0.5647 0.2753 0.4194 -0.0651 0.2817  -0.0595 177 PHE   B CE1   
8749  C  CE2   . PHE   B 152 ? 0.5403 0.2549 0.4191 -0.0378 0.2780  -0.0432 177 PHE   B CE2   
8750  C  CZ    . PHE   B 152 ? 0.5405 0.2770 0.4211 -0.0607 0.2787  -0.0532 177 PHE   B CZ    
8760  N  N     . THR   B 153 ? 0.6358 0.3151 0.4564 -0.0713 0.3062  -0.0783 178 THR   B N     
8761  C  CA    . THR   B 153 ? 0.6339 0.3388 0.4825 -0.0438 0.3165  -0.0719 178 THR   B CA    
8762  C  C     . THR   B 153 ? 0.6452 0.3405 0.4856 -0.0512 0.3211  -0.0724 178 THR   B C     
8763  O  O     . THR   B 153 ? 0.6584 0.3096 0.4827 -0.0516 0.3169  -0.0766 178 THR   B O     
8764  C  CB    . THR   B 153 ? 0.6543 0.3697 0.5042 -0.0367 0.3293  -0.0727 178 THR   B CB    
8765  O  OG1   . THR   B 153 ? 0.6915 0.3981 0.5170 -0.0669 0.3485  -0.0535 178 THR   B OG1   
8766  C  CG2   . THR   B 153 ? 0.6599 0.3764 0.5062 -0.0230 0.3289  -0.0712 178 THR   B CG2   
8774  N  N     . VAL   B 154 ? 0.6430 0.3443 0.4771 -0.0511 0.3143  -0.0791 179 VAL   B N     
8775  C  CA    . VAL   B 154 ? 0.6327 0.3423 0.4842 -0.0554 0.3156  -0.0821 179 VAL   B CA    
8776  C  C     . VAL   B 154 ? 0.6355 0.3584 0.4999 -0.0688 0.3194  -0.0995 179 VAL   B C     
8777  O  O     . VAL   B 154 ? 0.6756 0.3711 0.4859 -0.0708 0.3230  -0.0922 179 VAL   B O     
8778  C  CB    . VAL   B 154 ? 0.6469 0.3178 0.4827 -0.0528 0.3156  -0.0790 179 VAL   B CB    
8779  C  CG1   . VAL   B 154 ? 0.6623 0.3084 0.4904 -0.0403 0.3139  -0.0799 179 VAL   B CG1   
8780  C  CG2   . VAL   B 154 ? 0.6364 0.3273 0.4697 -0.0338 0.3022  -0.0807 179 VAL   B CG2   
8790  N  N     . GLU   B 155 ? 0.5994 0.3619 0.5167 -0.0560 0.3169  -0.1008 180 GLU   B N     
8791  C  CA    . GLU   B 155 ? 0.6219 0.3958 0.5473 -0.0332 0.3214  -0.1159 180 GLU   B CA    
8792  C  C     . GLU   B 155 ? 0.6545 0.3763 0.5457 -0.0443 0.3245  -0.1193 180 GLU   B C     
8793  O  O     . GLU   B 155 ? 0.6493 0.3414 0.5334 -0.0610 0.3170  -0.1195 180 GLU   B O     
8794  C  CB    . GLU   B 155 ? 0.6042 0.4536 0.5784 -0.0036 0.3230  -0.1212 180 GLU   B CB    
8795  C  CG    . GLU   B 155 ? 0.6247 0.5122 0.6206 -0.0302 0.3578  -0.1120 180 GLU   B CG    
8796  C  CD    . GLU   B 155 ? 0.6639 0.5584 0.6542 -0.0235 0.3787  -0.1149 180 GLU   B CD    
8797  O  OE1   . GLU   B 155 ? 0.6983 0.5492 0.6590 -0.0526 0.3892  -0.1307 180 GLU   B OE1   
8798  O  OE2   . GLU   B 155 ? 0.6696 0.5924 0.6704 0.0078  0.3828  -0.1065 180 GLU   B OE2   
8805  N  N     . THR   B 156 ? 0.6607 0.3712 0.5459 -0.0297 0.3231  -0.1125 181 THR   B N     
8806  C  CA    . THR   B 156 ? 0.6676 0.3614 0.5607 -0.0229 0.3247  -0.1116 181 THR   B CA    
8807  C  C     . THR   B 156 ? 0.6908 0.3756 0.5849 -0.0247 0.3259  -0.1298 181 THR   B C     
8808  O  O     . THR   B 156 ? 0.6624 0.3856 0.5819 -0.0310 0.3087  -0.1506 181 THR   B O     
8809  C  CB    . THR   B 156 ? 0.7106 0.3498 0.5567 -0.0245 0.3354  -0.0991 181 THR   B CB    
8810  O  OG1   . THR   B 156 ? 0.7046 0.3219 0.5516 -0.0385 0.3419  -0.0866 181 THR   B OG1   
8811  C  CG2   . THR   B 156 ? 0.6910 0.3692 0.5470 -0.0252 0.3261  -0.1103 181 THR   B CG2   
8819  N  N     . ALA   B 157 ? 0.6879 0.3861 0.5972 0.0087  0.3239  -0.1204 182 ALA   B N     
8820  C  CA    . ALA   B 157 ? 0.7169 0.3966 0.6121 0.0210  0.3270  -0.1225 182 ALA   B CA    
8821  C  C     . ALA   B 157 ? 0.7588 0.3913 0.6226 0.0043  0.3431  -0.1220 182 ALA   B C     
8822  O  O     . ALA   B 157 ? 0.7666 0.3821 0.6144 0.0031  0.3372  -0.1215 182 ALA   B O     
8823  C  CB    . ALA   B 157 ? 0.6860 0.4157 0.6137 0.0382  0.3254  -0.1168 182 ALA   B CB    
8829  N  N     . SER   B 158 ? 0.7607 0.3992 0.6329 -0.0064 0.3490  -0.1303 183 SER   B N     
8830  C  CA    . SER   B 158 ? 0.7304 0.3947 0.6405 -0.0027 0.3310  -0.1435 183 SER   B CA    
8831  C  C     . SER   B 158 ? 0.7663 0.4155 0.6640 0.0235  0.3291  -0.1493 183 SER   B C     
8832  O  O     . SER   B 158 ? 0.7937 0.4075 0.6582 0.0101  0.3303  -0.1512 183 SER   B O     
8833  C  CB    . SER   B 158 ? 0.7367 0.3957 0.6531 -0.0139 0.3253  -0.1593 183 SER   B CB    
8834  O  OG    . SER   B 158 ? 0.7541 0.4234 0.6679 -0.0294 0.3454  -0.1694 183 SER   B OG    
8840  N  N     . ARG   B 159 ? 0.7395 0.4446 0.6808 0.0788  0.3046  -0.1529 184 ARG   B N     
8841  C  CA    . ARG   B 159 ? 0.7407 0.4859 0.7071 0.0931  0.3160  -0.1594 184 ARG   B CA    
8842  C  C     . ARG   B 159 ? 0.7709 0.4927 0.7092 0.0572  0.3464  -0.1617 184 ARG   B C     
8843  O  O     . ARG   B 159 ? 0.7879 0.4930 0.6989 0.0435  0.3587  -0.1565 184 ARG   B O     
8844  C  CB    . ARG   B 159 ? 0.7344 0.5253 0.7313 0.1363  0.2958  -0.1720 184 ARG   B CB    
8845  C  CG    . ARG   B 159 ? 0.7801 0.5710 0.7713 0.1687  0.2929  -0.1915 184 ARG   B CG    
8846  C  CD    . ARG   B 159 ? 0.8472 0.6132 0.8011 0.2129  0.2807  -0.2092 184 ARG   B CD    
8847  N  NE    . ARG   B 159 ? 0.9383 0.6832 0.8265 0.1945  0.2430  -0.2023 184 ARG   B NE    
8848  C  CZ    . ARG   B 159 ? 0.9928 0.7288 0.8463 0.2026  0.2180  -0.1995 184 ARG   B CZ    
8849  N  NH1   . ARG   B 159 ? 1.0266 0.7526 0.8512 0.1906  0.2009  -0.1925 184 ARG   B NH1   
8850  N  NH2   . ARG   B 159 ? 1.0101 0.7512 0.8573 0.1960  0.2138  -0.1900 184 ARG   B NH2   
8864  N  N     . GLU   B 160 ? 0.8000 0.4922 0.7070 0.0331  0.3473  -0.1796 185 GLU   B N     
8865  C  CA    . GLU   B 160 ? 0.8324 0.4981 0.7005 0.0143  0.3524  -0.1860 185 GLU   B CA    
8866  C  C     . GLU   B 160 ? 0.8524 0.4941 0.6856 0.0329  0.3244  -0.1875 185 GLU   B C     
8867  O  O     . GLU   B 160 ? 0.8523 0.4923 0.6659 0.0527  0.3000  -0.1998 185 GLU   B O     
8868  C  CB    . GLU   B 160 ? 0.8480 0.5141 0.7144 -0.0190 0.3620  -0.1855 185 GLU   B CB    
8869  C  CG    . GLU   B 160 ? 0.8442 0.5243 0.7255 -0.0396 0.3725  -0.1907 185 GLU   B CG    
8870  C  CD    . GLU   B 160 ? 0.8497 0.5361 0.7424 -0.0733 0.3512  -0.1955 185 GLU   B CD    
8871  O  OE1   . GLU   B 160 ? 0.8403 0.5183 0.7405 -0.0830 0.3497  -0.2164 185 GLU   B OE1   
8872  O  OE2   . GLU   B 160 ? 0.8546 0.5650 0.7554 -0.0822 0.3410  -0.1797 185 GLU   B OE2   
8879  N  N     . TYR   B 161 ? 0.8396 0.4845 0.6720 0.0479  0.3193  -0.1840 186 TYR   B N     
8880  C  CA    . TYR   B 161 ? 0.8634 0.4700 0.6694 0.0289  0.3233  -0.1832 186 TYR   B CA    
8881  C  C     . TYR   B 161 ? 0.8896 0.4546 0.6627 0.0040  0.3255  -0.1830 186 TYR   B C     
8882  O  O     . TYR   B 161 ? 0.9295 0.4198 0.6464 -0.0422 0.3216  -0.1766 186 TYR   B O     
8883  C  CB    . TYR   B 161 ? 0.8674 0.4792 0.6715 0.0331  0.3272  -0.1777 186 TYR   B CB    
8884  C  CG    . TYR   B 161 ? 0.8801 0.4727 0.6771 0.0299  0.3176  -0.1756 186 TYR   B CG    
8885  C  CD1   . TYR   B 161 ? 0.8533 0.4646 0.6755 0.0324  0.3169  -0.1858 186 TYR   B CD1   
8886  C  CD2   . TYR   B 161 ? 0.8854 0.4834 0.6832 0.0178  0.3039  -0.1694 186 TYR   B CD2   
8887  C  CE1   . TYR   B 161 ? 0.8874 0.4753 0.6843 0.0150  0.3188  -0.1897 186 TYR   B CE1   
8888  C  CE2   . TYR   B 161 ? 0.9037 0.4923 0.6884 0.0127  0.2959  -0.1667 186 TYR   B CE2   
8889  C  CZ    . TYR   B 161 ? 0.9007 0.5006 0.6911 -0.0038 0.3032  -0.1750 186 TYR   B CZ    
8890  O  OH    . TYR   B 161 ? 0.9430 0.5128 0.6998 -0.0371 0.2805  -0.1704 186 TYR   B OH    
8900  N  N     . LYS   B 162 ? 0.8776 0.4862 0.6757 0.0398  0.3401  -0.1732 187 LYS   B N     
8901  C  CA    . LYS   B 162 ? 0.8603 0.5343 0.6744 0.0663  0.3528  -0.1640 187 LYS   B CA    
8902  C  C     . LYS   B 162 ? 0.8528 0.5293 0.6602 0.0510  0.3595  -0.1567 187 LYS   B C     
8903  O  O     . LYS   B 162 ? 0.8570 0.5458 0.6548 0.0571  0.3576  -0.1589 187 LYS   B O     
8904  C  CB    . LYS   B 162 ? 0.9312 0.5781 0.7008 0.0969  0.3679  -0.1632 187 LYS   B CB    
8905  C  CG    . LYS   B 162 ? 0.9996 0.6078 0.7250 0.1093  0.3758  -0.1666 187 LYS   B CG    
8906  C  CD    . LYS   B 162 ? 1.0784 0.6514 0.7534 0.0872  0.3556  -0.1531 187 LYS   B CD    
8907  C  CE    . LYS   B 162 ? 1.1268 0.6734 0.7691 0.0877  0.3400  -0.1587 187 LYS   B CE    
8908  N  NZ    . LYS   B 162 ? 1.1579 0.6924 0.7789 0.0719  0.3198  -0.1575 187 LYS   B NZ    
8922  N  N     . LYS   B 163 ? 0.8347 0.4988 0.6497 0.0500  0.3472  -0.1527 188 LYS   B N     
8923  C  CA    . LYS   B 163 ? 0.8203 0.4859 0.6419 0.0298  0.3514  -0.1506 188 LYS   B CA    
8924  C  C     . LYS   B 163 ? 0.8139 0.4609 0.6336 -0.0070 0.3641  -0.1440 188 LYS   B C     
8925  O  O     . LYS   B 163 ? 0.8126 0.4532 0.6365 -0.0349 0.3663  -0.1551 188 LYS   B O     
8926  C  CB    . LYS   B 163 ? 0.8240 0.5145 0.6562 0.0313  0.3633  -0.1537 188 LYS   B CB    
8927  C  CG    . LYS   B 163 ? 0.8546 0.5567 0.6855 0.0035  0.3736  -0.1417 188 LYS   B CG    
8928  C  CD    . LYS   B 163 ? 0.8952 0.5922 0.7100 -0.0227 0.3479  -0.1233 188 LYS   B CD    
8929  C  CE    . LYS   B 163 ? 0.9419 0.6276 0.7345 -0.0501 0.3175  -0.0950 188 LYS   B CE    
8930  N  NZ    . LYS   B 163 ? 0.9749 0.6482 0.7509 -0.0701 0.2978  -0.0738 188 LYS   B NZ    
8944  N  N     . MET   B 164 ? 0.7887 0.4367 0.6235 0.0015  0.3596  -0.1280 189 MET   B N     
8945  C  CA    . MET   B 164 ? 0.8172 0.4475 0.6218 0.0066  0.3700  -0.1186 189 MET   B CA    
8946  C  C     . MET   B 164 ? 0.8334 0.4440 0.5859 -0.0031 0.3736  -0.0990 189 MET   B C     
8947  O  O     . MET   B 164 ? 0.8380 0.4504 0.5761 -0.0015 0.3668  -0.1033 189 MET   B O     
8948  C  CB    . MET   B 164 ? 0.8547 0.4695 0.6598 0.0049  0.3955  -0.1203 189 MET   B CB    
8949  C  CG    . MET   B 164 ? 0.9138 0.4937 0.7016 -0.0081 0.4142  -0.1054 189 MET   B CG    
8950  S  SD    . MET   B 164 ? 0.9568 0.5199 0.7295 -0.0094 0.4178  -0.0949 189 MET   B SD    
8951  C  CE    . MET   B 164 ? 0.9591 0.5507 0.7428 -0.0404 0.4080  -0.0732 189 MET   B CE    
8961  N  N     . PHE   B 165 ? 0.7893 0.4131 0.5558 -0.0170 0.3667  -0.0801 190 PHE   B N     
8962  C  CA    . PHE   B 165 ? 0.8032 0.3946 0.5325 -0.0362 0.3644  -0.0722 190 PHE   B CA    
8963  C  C     . PHE   B 165 ? 0.8585 0.3702 0.5234 -0.0359 0.3657  -0.0637 190 PHE   B C     
8964  O  O     . PHE   B 165 ? 0.8811 0.3548 0.5192 -0.0306 0.3720  -0.0444 190 PHE   B O     
8965  C  CB    . PHE   B 165 ? 0.7841 0.4031 0.5134 -0.0451 0.3530  -0.0768 190 PHE   B CB    
8966  C  CG    . PHE   B 165 ? 0.7982 0.3911 0.4921 -0.0619 0.3423  -0.0827 190 PHE   B CG    
8967  C  CD1   . PHE   B 165 ? 0.7978 0.3859 0.4848 -0.0765 0.3353  -0.0860 190 PHE   B CD1   
8968  C  CD2   . PHE   B 165 ? 0.7982 0.3730 0.4805 -0.0880 0.3427  -0.0714 190 PHE   B CD2   
8969  C  CE1   . PHE   B 165 ? 0.7766 0.3650 0.4777 -0.1037 0.3394  -0.0701 190 PHE   B CE1   
8970  C  CE2   . PHE   B 165 ? 0.7899 0.3682 0.4773 -0.0872 0.3412  -0.0657 190 PHE   B CE2   
8971  C  CZ    . PHE   B 165 ? 0.7824 0.3626 0.4806 -0.1028 0.3419  -0.0606 190 PHE   B CZ    
8981  N  N     . LYS   B 166 ? 0.8307 0.3631 0.5223 -0.0433 0.3641  -0.0647 191 LYS   B N     
8982  C  CA    . LYS   B 166 ? 0.8699 0.3751 0.5196 -0.0770 0.3701  -0.0719 191 LYS   B CA    
8983  C  C     . LYS   B 166 ? 0.8558 0.3827 0.5017 -0.0620 0.3555  -0.0732 191 LYS   B C     
8984  O  O     . LYS   B 166 ? 0.8714 0.3918 0.5043 -0.0497 0.3536  -0.0768 191 LYS   B O     
8985  C  CB    . LYS   B 166 ? 0.9004 0.3939 0.5445 -0.0746 0.3717  -0.0935 191 LYS   B CB    
8986  C  CG    . LYS   B 166 ? 0.9309 0.4225 0.5790 -0.0704 0.3447  -0.1139 191 LYS   B CG    
8987  C  CD    . LYS   B 166 ? 0.9388 0.4339 0.6149 -0.0764 0.3170  -0.1249 191 LYS   B CD    
8988  C  CE    . LYS   B 166 ? 0.9566 0.4541 0.6479 -0.0752 0.2878  -0.1227 191 LYS   B CE    
8989  N  NZ    . LYS   B 166 ? 0.9606 0.4696 0.6652 -0.0773 0.2771  -0.1168 191 LYS   B NZ    
9003  N  N     . GLN   B 167 ? 0.8522 0.3991 0.4786 -0.0718 0.3443  -0.0709 192 GLN   B N     
9004  C  CA    . GLN   B 167 ? 0.8368 0.3750 0.4570 -0.0629 0.3248  -0.0748 192 GLN   B CA    
9005  C  C     . GLN   B 167 ? 0.8448 0.3562 0.4498 -0.0731 0.3260  -0.0643 192 GLN   B C     
9006  O  O     . GLN   B 167 ? 0.8365 0.3363 0.4399 -0.0889 0.3231  -0.0523 192 GLN   B O     
9007  C  CB    . GLN   B 167 ? 0.8961 0.3942 0.4442 -0.0651 0.3137  -0.0801 192 GLN   B CB    
9008  C  CG    . GLN   B 167 ? 0.9718 0.4122 0.4398 -0.0941 0.2942  -0.0758 192 GLN   B CG    
9009  C  CD    . GLN   B 167 ? 1.0137 0.4485 0.4440 -0.1277 0.2800  -0.0529 192 GLN   B CD    
9010  O  OE1   . GLN   B 167 ? 1.0012 0.4493 0.4310 -0.1549 0.3062  -0.0414 192 GLN   B OE1   
9011  N  NE2   . GLN   B 167 ? 1.0454 0.4722 0.4552 -0.1111 0.2514  -0.0498 192 GLN   B NE2   
9020  N  N     . THR   B 168 ? 0.8434 0.3519 0.4543 -0.0750 0.3303  -0.0613 193 THR   B N     
9021  C  CA    . THR   B 168 ? 0.8112 0.3661 0.4539 -0.0889 0.3292  -0.0635 193 THR   B CA    
9022  C  C     . THR   B 168 ? 0.8134 0.3781 0.4392 -0.0989 0.3204  -0.0547 193 THR   B C     
9023  O  O     . THR   B 168 ? 0.8607 0.4175 0.4512 -0.1008 0.3302  -0.0609 193 THR   B O     
9024  C  CB    . THR   B 168 ? 0.7921 0.3567 0.4578 -0.0985 0.3282  -0.0744 193 THR   B CB    
9025  O  OG1   . THR   B 168 ? 0.7863 0.3875 0.4674 -0.1004 0.3326  -0.0800 193 THR   B OG1   
9026  C  CG2   . THR   B 168 ? 0.7615 0.3418 0.4522 -0.0949 0.3241  -0.0653 193 THR   B CG2   
9034  N  N     . TRP   B 169 ? 0.7558 0.3300 0.4065 -0.0985 0.2958  -0.0470 194 TRP   B N     
9035  C  CA    . TRP   B 169 ? 0.7592 0.3271 0.3864 -0.1090 0.2706  -0.0206 194 TRP   B CA    
9036  C  C     . TRP   B 169 ? 0.7801 0.3169 0.3760 -0.0991 0.2746  -0.0372 194 TRP   B C     
9037  O  O     . TRP   B 169 ? 0.7872 0.3132 0.3828 -0.0801 0.2826  -0.0455 194 TRP   B O     
9038  C  CB    . TRP   B 169 ? 0.7552 0.3293 0.3774 -0.1100 0.2639  -0.0189 194 TRP   B CB    
9039  C  CG    . TRP   B 169 ? 0.7357 0.3281 0.3561 -0.0933 0.2573  -0.0231 194 TRP   B CG    
9040  C  CD1   . TRP   B 169 ? 0.7164 0.3165 0.3496 -0.0982 0.2504  -0.0235 194 TRP   B CD1   
9041  C  CD2   . TRP   B 169 ? 0.7471 0.3156 0.3505 -0.0914 0.2565  -0.0332 194 TRP   B CD2   
9042  N  NE1   . TRP   B 169 ? 0.7594 0.3104 0.3519 -0.0715 0.2596  -0.0251 194 TRP   B NE1   
9043  C  CE2   . TRP   B 169 ? 0.7642 0.3136 0.3551 -0.0716 0.2615  -0.0226 194 TRP   B CE2   
9044  C  CE3   . TRP   B 169 ? 0.7455 0.3085 0.3524 -0.0590 0.2593  -0.0430 194 TRP   B CE3   
9045  C  CZ2   . TRP   B 169 ? 0.7724 0.3252 0.3622 -0.0540 0.2683  -0.0151 194 TRP   B CZ2   
9046  C  CZ3   . TRP   B 169 ? 0.7753 0.3232 0.3609 -0.0411 0.2623  -0.0425 194 TRP   B CZ3   
9047  C  CH2   . TRP   B 169 ? 0.7785 0.3269 0.3660 -0.0287 0.2679  -0.0301 194 TRP   B CH2   
9058  N  N     . MET   B 170 ? 0.8170 0.2967 0.3667 -0.1125 0.2578  -0.0293 195 MET   B N     
9059  C  CA    . MET   B 170 ? 0.8385 0.3220 0.3670 -0.1187 0.2383  -0.0042 195 MET   B CA    
9060  C  C     . MET   B 170 ? 0.8560 0.3172 0.3462 -0.1125 0.2043  0.0129  195 MET   B C     
9061  O  O     . MET   B 170 ? 0.8772 0.3040 0.3355 -0.1043 0.1898  0.0132  195 MET   B O     
9062  C  CB    . MET   B 170 ? 0.8621 0.3641 0.3972 -0.1200 0.2613  0.0053  195 MET   B CB    
9063  C  CG    . MET   B 170 ? 0.9008 0.4146 0.4232 -0.1209 0.2892  0.0036  195 MET   B CG    
9064  S  SD    . MET   B 170 ? 0.9572 0.4743 0.4505 -0.1289 0.3129  0.0018  195 MET   B SD    
9065  C  CE    . MET   B 170 ? 0.9388 0.4871 0.4580 -0.1355 0.3138  0.0071  195 MET   B CE    
9075  N  N     . ASP   B 171 ? 0.8516 0.3294 0.3413 -0.1098 0.1997  0.0204  196 ASP   B N     
9076  C  CA    . ASP   B 171 ? 0.8533 0.3317 0.3475 -0.1121 0.1946  0.0276  196 ASP   B CA    
9077  C  C     . ASP   B 171 ? 0.8411 0.3053 0.3372 -0.1161 0.1669  0.0276  196 ASP   B C     
9078  O  O     . ASP   B 171 ? 0.8561 0.3074 0.3427 -0.1169 0.1525  0.0366  196 ASP   B O     
9079  C  CB    . ASP   B 171 ? 0.8812 0.3585 0.3682 -0.1131 0.2205  0.0263  196 ASP   B CB    
9080  C  CG    . ASP   B 171 ? 0.9272 0.4047 0.4015 -0.1316 0.2321  0.0279  196 ASP   B CG    
9081  O  OD1   . ASP   B 171 ? 0.9360 0.4095 0.4192 -0.1325 0.2389  0.0297  196 ASP   B OD1   
9082  O  OD2   . ASP   B 171 ? 0.9483 0.4384 0.4153 -0.1442 0.2440  0.0404  196 ASP   B OD2   
9087  N  N     . ASN   B 172 ? 0.8101 0.2906 0.3212 -0.1066 0.1558  0.0289  197 ASN   B N     
9088  C  CA    . ASN   B 172 ? 0.7840 0.2770 0.3106 -0.1050 0.1486  0.0257  197 ASN   B CA    
9089  C  C     . ASN   B 172 ? 0.8132 0.2770 0.3039 -0.0964 0.1408  0.0266  197 ASN   B C     
9090  O  O     . ASN   B 172 ? 0.8250 0.2791 0.2980 -0.0848 0.1333  0.0319  197 ASN   B O     
9091  C  CB    . ASN   B 172 ? 0.7759 0.2716 0.3122 -0.1213 0.1315  0.0234  197 ASN   B CB    
9092  C  CG    . ASN   B 172 ? 0.8061 0.2761 0.3270 -0.1147 0.1182  0.0368  197 ASN   B CG    
9093  O  OD1   . ASN   B 172 ? 0.8650 0.2837 0.3403 -0.1003 0.1006  0.0495  197 ASN   B OD1   
9094  N  ND2   . ASN   B 172 ? 0.8118 0.2697 0.3362 -0.1084 0.1341  0.0301  197 ASN   B ND2   
9101  N  N     . MET   B 173 ? 0.8529 0.2881 0.3111 -0.1098 0.1476  0.0187  198 MET   B N     
9102  C  CA    . MET   B 173 ? 0.8310 0.3026 0.3147 -0.1387 0.1630  0.0056  198 MET   B CA    
9103  C  C     . MET   B 173 ? 0.8850 0.3400 0.3271 -0.1493 0.1617  0.0167  198 MET   B C     
9104  O  O     . MET   B 173 ? 0.9184 0.3593 0.3307 -0.1660 0.1472  0.0220  198 MET   B O     
9105  C  CB    . MET   B 173 ? 0.8213 0.2759 0.3122 -0.1113 0.1917  -0.0102 198 MET   B CB    
9106  C  CG    . MET   B 173 ? 0.8004 0.2563 0.3082 -0.0931 0.2113  -0.0235 198 MET   B CG    
9107  S  SD    . MET   B 173 ? 0.8359 0.2816 0.3108 -0.0699 0.2177  -0.0191 198 MET   B SD    
9108  C  CE    . MET   B 173 ? 0.8549 0.3097 0.3196 -0.0279 0.1810  -0.0216 198 MET   B CE    
9118  N  N     . GLY   B 174 ? 0.8600 0.3660 0.3229 -0.1200 0.1791  0.0292  199 GLY   B N     
9119  C  CA    . GLY   B 174 ? 0.8999 0.3900 0.3253 -0.1151 0.1753  0.0366  199 GLY   B CA    
9120  C  C     . GLY   B 174 ? 0.9325 0.4143 0.3311 -0.1140 0.1793  0.0371  199 GLY   B C     
9121  O  O     . GLY   B 174 ? 0.9491 0.4316 0.3330 -0.1210 0.1690  0.0479  199 GLY   B O     
9125  N  N     . ARG   B 175 ? 0.9644 0.4468 0.3407 -0.1139 0.1917  0.0276  200 ARG   B N     
9126  C  CA    . ARG   B 175 ? 0.9738 0.4591 0.3482 -0.1126 0.2089  0.0281  200 ARG   B CA    
9127  C  C     . ARG   B 175 ? 0.9906 0.4304 0.3443 -0.0872 0.2183  0.0051  200 ARG   B C     
9128  O  O     . ARG   B 175 ? 0.9842 0.4028 0.3316 -0.0716 0.2055  0.0153  200 ARG   B O     
9129  C  CB    . ARG   B 175 ? 0.9597 0.4929 0.3649 -0.1314 0.2119  0.0471  200 ARG   B CB    
9130  C  CG    . ARG   B 175 ? 0.9647 0.5162 0.3870 -0.1571 0.2068  0.0661  200 ARG   B CG    
9131  C  CD    . ARG   B 175 ? 0.9942 0.5415 0.3997 -0.1791 0.2028  0.0712  200 ARG   B CD    
9132  N  NE    . ARG   B 175 ? 1.0043 0.5539 0.4126 -0.2011 0.1985  0.0749  200 ARG   B NE    
9133  C  CZ    . ARG   B 175 ? 1.0484 0.5644 0.4270 -0.2144 0.1860  0.0649  200 ARG   B CZ    
9134  N  NH1   . ARG   B 175 ? 1.0592 0.5765 0.4264 -0.2081 0.1859  0.0509  200 ARG   B NH1   
9135  N  NH2   . ARG   B 175 ? 1.0667 0.5616 0.4402 -0.2366 0.1750  0.0669  200 ARG   B NH2   
9149  N  N     . ALA   B 176 ? 1.0106 0.4452 0.3532 -0.0991 0.2311  -0.0024 201 ALA   B N     
9150  C  CA    . ALA   B 176 ? 1.0136 0.4620 0.3691 -0.1093 0.2514  -0.0174 201 ALA   B CA    
9151  C  C     . ALA   B 176 ? 1.0458 0.4844 0.3762 -0.1074 0.2559  -0.0203 201 ALA   B C     
9152  O  O     . ALA   B 176 ? 1.0721 0.5219 0.3769 -0.1071 0.2498  -0.0063 201 ALA   B O     
9153  C  CB    . ALA   B 176 ? 1.0113 0.4681 0.3727 -0.1270 0.2520  -0.0178 201 ALA   B CB    
9159  N  N     . GLY   B 177 ? 1.0386 0.4694 0.3931 -0.1042 0.2768  -0.0339 202 GLY   B N     
9160  C  CA    . GLY   B 177 ? 1.0586 0.4804 0.4198 -0.1058 0.2962  -0.0584 202 GLY   B CA    
9161  C  C     . GLY   B 177 ? 1.0680 0.4878 0.4432 -0.1160 0.3185  -0.0689 202 GLY   B C     
9162  O  O     . GLY   B 177 ? 1.0962 0.4974 0.4416 -0.1120 0.3103  -0.0790 202 GLY   B O     
9166  N  N     . GLU   B 178 ? 1.0396 0.4935 0.4673 -0.0982 0.3303  -0.0738 203 GLU   B N     
9167  C  CA    . GLU   B 178 ? 0.9986 0.5230 0.5068 -0.0754 0.3136  -0.0639 203 GLU   B CA    
9168  C  C     . GLU   B 178 ? 1.0302 0.4963 0.5040 -0.0816 0.3619  -0.0732 203 GLU   B C     
9169  O  O     . GLU   B 178 ? 1.0336 0.4821 0.5091 -0.0670 0.3697  -0.0756 203 GLU   B O     
9170  C  CB    . GLU   B 178 ? 0.9401 0.5702 0.5519 -0.0617 0.2425  -0.0381 203 GLU   B CB    
9171  C  CG    . GLU   B 178 ? 0.9158 0.6195 0.6004 -0.0435 0.1828  -0.0207 203 GLU   B CG    
9172  C  CD    . GLU   B 178 ? 0.8699 0.6746 0.6427 -0.0353 0.1565  -0.0070 203 GLU   B CD    
9173  O  OE1   . GLU   B 178 ? 0.8509 0.6978 0.6573 -0.0528 0.1523  0.0005  203 GLU   B OE1   
9174  O  OE2   . GLU   B 178 ? 0.8446 0.7035 0.6585 -0.0128 0.1490  -0.0002 203 GLU   B OE2   
9181  N  N     . MET   B 179 ? 1.0537 0.4981 0.5094 -0.0943 0.3734  -0.0740 204 MET   B N     
9182  C  CA    . MET   B 179 ? 1.0662 0.4888 0.5231 -0.1158 0.3786  -0.0649 204 MET   B CA    
9183  C  C     . MET   B 179 ? 1.0243 0.4721 0.5108 -0.1145 0.3750  -0.0546 204 MET   B C     
9184  O  O     . MET   B 179 ? 1.0265 0.4911 0.4981 -0.1039 0.3673  -0.0619 204 MET   B O     
9185  C  CB    . MET   B 179 ? 1.0996 0.5092 0.5509 -0.1176 0.4012  -0.0591 204 MET   B CB    
9186  C  CG    . MET   B 179 ? 1.1258 0.5237 0.5802 -0.1251 0.4141  -0.0657 204 MET   B CG    
9187  S  SD    . MET   B 179 ? 1.1741 0.5394 0.6088 -0.1054 0.4121  -0.0810 204 MET   B SD    
9188  C  CE    . MET   B 179 ? 1.1798 0.5511 0.6252 -0.0931 0.4032  -0.0792 204 MET   B CE    
9198  N  N     . GLU   B 180 ? 0.9932 0.4431 0.5228 -0.1078 0.3824  -0.0413 205 GLU   B N     
9199  C  CA    . GLU   B 180 ? 0.9913 0.4455 0.5412 -0.0703 0.3942  -0.0344 205 GLU   B CA    
9200  C  C     . GLU   B 180 ? 0.9688 0.4468 0.5399 -0.0388 0.3840  -0.0518 205 GLU   B C     
9201  O  O     . GLU   B 180 ? 0.9652 0.4375 0.5280 -0.0229 0.3722  -0.0713 205 GLU   B O     
9202  C  CB    . GLU   B 180 ? 1.0152 0.4734 0.5607 -0.0791 0.4071  -0.0127 205 GLU   B CB    
9203  C  CG    . GLU   B 180 ? 1.0535 0.5301 0.5904 -0.0865 0.4027  0.0041  205 GLU   B CG    
9204  C  CD    . GLU   B 180 ? 1.0827 0.5695 0.6201 -0.0971 0.3916  0.0269  205 GLU   B CD    
9205  O  OE1   . GLU   B 180 ? 1.0897 0.6051 0.6206 -0.0911 0.4008  0.0402  205 GLU   B OE1   
9206  O  OE2   . GLU   B 180 ? 1.0916 0.5691 0.6395 -0.1077 0.3816  0.0288  205 GLU   B OE2   
9213  N  N     . LEU   B 181 ? 0.9149 0.4540 0.5360 -0.0148 0.3808  -0.0585 206 LEU   B N     
9214  C  CA    . LEU   B 181 ? 0.9152 0.4908 0.5408 -0.0210 0.3865  -0.0553 206 LEU   B CA    
9215  C  C     . LEU   B 181 ? 0.8864 0.5338 0.5632 -0.0194 0.3906  -0.0734 206 LEU   B C     
9216  O  O     . LEU   B 181 ? 0.8537 0.5661 0.5633 -0.0262 0.3934  -0.0632 206 LEU   B O     
9217  C  CB    . LEU   B 181 ? 0.9173 0.4899 0.5306 -0.0096 0.3840  -0.0405 206 LEU   B CB    
9218  C  CG    . LEU   B 181 ? 0.9194 0.4890 0.5299 0.0171  0.3811  -0.0353 206 LEU   B CG    
9219  C  CD1   . LEU   B 181 ? 0.9351 0.4985 0.5276 0.0355  0.3830  -0.0170 206 LEU   B CD1   
9220  C  CD2   . LEU   B 181 ? 0.9101 0.4968 0.5333 0.0278  0.3777  -0.0439 206 LEU   B CD2   
9232  N  N     . LYS   B 182 ? 0.8844 0.5493 0.5861 -0.0123 0.3978  -0.0897 207 LYS   B N     
9233  C  CA    . LYS   B 182 ? 0.8832 0.5768 0.6087 -0.0266 0.4042  -0.0888 207 LYS   B CA    
9234  C  C     . LYS   B 182 ? 0.8406 0.5570 0.6140 0.0034  0.3900  -0.1179 207 LYS   B C     
9235  O  O     . LYS   B 182 ? 0.8186 0.5496 0.6109 0.0207  0.3705  -0.1328 207 LYS   B O     
9236  C  CB    . LYS   B 182 ? 0.9441 0.6193 0.6306 -0.0598 0.3992  -0.0629 207 LYS   B CB    
9237  C  CG    . LYS   B 182 ? 0.9886 0.6570 0.6534 -0.0790 0.3877  -0.0467 207 LYS   B CG    
9238  C  CD    . LYS   B 182 ? 1.0167 0.6892 0.6738 -0.0899 0.3783  -0.0315 207 LYS   B CD    
9239  C  CE    . LYS   B 182 ? 1.0331 0.7060 0.6880 -0.0973 0.3725  -0.0161 207 LYS   B CE    
9240  N  NZ    . LYS   B 182 ? 1.0449 0.7164 0.7016 -0.0921 0.3626  -0.0122 207 LYS   B NZ    
9254  N  N     . PRO   B 183 ? 0.8222 0.5724 0.6129 0.0239  0.3817  -0.1189 208 PRO   B N     
9255  C  CA    . PRO   B 183 ? 0.8369 0.5930 0.6235 0.0407  0.3776  -0.1326 208 PRO   B CA    
9256  C  C     . PRO   B 183 ? 0.8329 0.5978 0.6509 0.0473  0.3767  -0.1496 208 PRO   B C     
9257  O  O     . PRO   B 183 ? 0.8346 0.5969 0.6668 0.0170  0.3699  -0.1548 208 PRO   B O     
9258  C  CB    . PRO   B 183 ? 0.8476 0.5998 0.6203 0.0555  0.3740  -0.1307 208 PRO   B CB    
9259  C  CG    . PRO   B 183 ? 0.8543 0.6001 0.6175 0.0566  0.3776  -0.1233 208 PRO   B CG    
9260  C  CD    . PRO   B 183 ? 0.8563 0.5888 0.6144 0.0319  0.3800  -0.1173 208 PRO   B CD    
9268  N  N     . PHE   B 184 ? 0.7894 0.6010 0.6519 0.0621  0.3695  -0.1422 209 PHE   B N     
9269  C  CA    . PHE   B 184 ? 0.7730 0.6017 0.6765 0.0630  0.3704  -0.1438 209 PHE   B CA    
9270  C  C     . PHE   B 184 ? 0.8102 0.6239 0.7007 0.0973  0.3615  -0.1692 209 PHE   B C     
9271  O  O     . PHE   B 184 ? 0.8449 0.6308 0.6960 0.0971  0.3528  -0.1885 209 PHE   B O     
9272  C  CB    . PHE   B 184 ? 0.7079 0.5777 0.6629 0.0394  0.3678  -0.1335 209 PHE   B CB    
9273  C  CG    . PHE   B 184 ? 0.6691 0.5624 0.6604 0.0388  0.3592  -0.1274 209 PHE   B CG    
9274  C  CD1   . PHE   B 184 ? 0.6536 0.5590 0.6569 0.0387  0.3546  -0.1257 209 PHE   B CD1   
9275  C  CD2   . PHE   B 184 ? 0.6658 0.5514 0.6548 0.0435  0.3558  -0.1226 209 PHE   B CD2   
9276  C  CE1   . PHE   B 184 ? 0.6694 0.5545 0.6644 0.0315  0.3556  -0.1222 209 PHE   B CE1   
9277  C  CE2   . PHE   B 184 ? 0.6694 0.5419 0.6596 0.0501  0.3500  -0.1304 209 PHE   B CE2   
9278  C  CZ    . PHE   B 184 ? 0.6721 0.5469 0.6625 0.0439  0.3528  -0.1270 209 PHE   B CZ    
9288  N  N     . ASN   B 185 ? 0.8138 0.6526 0.7295 0.1399  0.3582  -0.1653 210 ASN   B N     
9289  C  CA    . ASN   B 185 ? 0.8389 0.6914 0.7640 0.1734  0.3637  -0.1650 210 ASN   B CA    
9290  C  C     . ASN   B 185 ? 0.8381 0.6862 0.7823 0.1535  0.3567  -0.1706 210 ASN   B C     
9291  O  O     . ASN   B 185 ? 0.8686 0.7104 0.7928 0.1331  0.3427  -0.1643 210 ASN   B O     
9292  C  CB    . ASN   B 185 ? 0.9078 0.7416 0.7929 0.2010  0.3657  -0.1430 210 ASN   B CB    
9293  C  CG    . ASN   B 185 ? 1.0153 0.8041 0.8234 0.1790  0.3254  -0.1043 210 ASN   B CG    
9294  O  OD1   . ASN   B 185 ? 1.0648 0.8340 0.8315 0.1613  0.3072  -0.0886 210 ASN   B OD1   
9295  N  ND2   . ASN   B 185 ? 1.0494 0.8250 0.8392 0.1796  0.3045  -0.0897 210 ASN   B ND2   
9302  N  N     . GLY   B 186 ? 0.7829 0.6693 0.7786 0.1335  0.3638  -0.1800 211 GLY   B N     
9303  C  CA    . GLY   B 186 ? 0.7476 0.6509 0.7896 0.1127  0.3659  -0.1767 211 GLY   B CA    
9304  C  C     . GLY   B 186 ? 0.7076 0.6300 0.7949 0.1070  0.3551  -0.1773 211 GLY   B C     
9305  O  O     . GLY   B 186 ? 0.7141 0.6366 0.8020 0.1078  0.3593  -0.1779 211 GLY   B O     
9309  N  N     . GLU   B 187 ? 0.6947 0.6015 0.8025 0.0930  0.3527  -0.1762 212 GLU   B N     
9310  C  CA    . GLU   B 187 ? 0.6805 0.5927 0.8123 0.0755  0.3386  -0.1568 212 GLU   B CA    
9311  C  C     . GLU   B 187 ? 0.6023 0.5613 0.7905 0.0746  0.3402  -0.1486 212 GLU   B C     
9312  O  O     . GLU   B 187 ? 0.5711 0.5935 0.7973 0.0862  0.3308  -0.1438 212 GLU   B O     
9313  C  CB    . GLU   B 187 ? 0.7483 0.6194 0.8380 0.0787  0.3232  -0.1521 212 GLU   B CB    
9314  C  CG    . GLU   B 187 ? 0.8231 0.6555 0.8624 0.0622  0.2899  -0.1378 212 GLU   B CG    
9315  C  CD    . GLU   B 187 ? 0.8853 0.6813 0.8832 0.0557  0.2590  -0.1378 212 GLU   B CD    
9316  O  OE1   . GLU   B 187 ? 0.9026 0.6894 0.8878 0.0438  0.2483  -0.1434 212 GLU   B OE1   
9317  O  OE2   . GLU   B 187 ? 0.9111 0.6882 0.8927 0.0664  0.2474  -0.1389 212 GLU   B OE2   
9324  N  N     . ASP   B 188 ? 0.5779 0.5136 0.7546 0.0521  0.3334  -0.1399 213 ASP   B N     
9325  C  CA    . ASP   B 188 ? 0.5524 0.4720 0.7202 0.0467  0.3122  -0.1402 213 ASP   B CA    
9326  C  C     . ASP   B 188 ? 0.5406 0.4465 0.6993 0.0379  0.3068  -0.1353 213 ASP   B C     
9327  O  O     . ASP   B 188 ? 0.5392 0.4400 0.6943 0.0546  0.2893  -0.1406 213 ASP   B O     
9328  C  CB    . ASP   B 188 ? 0.5598 0.4634 0.7077 0.0469  0.3099  -0.1408 213 ASP   B CB    
9329  C  CG    . ASP   B 188 ? 0.5755 0.4593 0.7154 0.0451  0.3081  -0.1494 213 ASP   B CG    
9330  O  OD1   . ASP   B 188 ? 0.5834 0.4535 0.7012 0.0877  0.2828  -0.1438 213 ASP   B OD1   
9331  O  OD2   . ASP   B 188 ? 0.5928 0.4605 0.7000 0.0358  0.3063  -0.1656 213 ASP   B OD2   
9336  N  N     . TYR   B 189 ? 0.5353 0.4242 0.6688 0.0322  0.3022  -0.1279 214 TYR   B N     
9337  C  CA    . TYR   B 189 ? 0.5544 0.4189 0.6540 0.0411  0.3063  -0.1161 214 TYR   B CA    
9338  C  C     . TYR   B 189 ? 0.5405 0.3902 0.6422 0.0303  0.2991  -0.1154 214 TYR   B C     
9339  O  O     . TYR   B 189 ? 0.5512 0.3804 0.6294 0.0349  0.2900  -0.1198 214 TYR   B O     
9340  C  CB    . TYR   B 189 ? 0.5646 0.4409 0.6550 0.0484  0.3141  -0.1104 214 TYR   B CB    
9341  C  CG    . TYR   B 189 ? 0.5990 0.4687 0.6577 0.0413  0.3403  -0.0985 214 TYR   B CG    
9342  C  CD1   . TYR   B 189 ? 0.6226 0.4874 0.6663 0.0436  0.3536  -0.0929 214 TYR   B CD1   
9343  C  CD2   . TYR   B 189 ? 0.6163 0.4796 0.6633 0.0207  0.3574  -0.0887 214 TYR   B CD2   
9344  C  CE1   . TYR   B 189 ? 0.6552 0.4872 0.6740 0.0495  0.3651  -0.0871 214 TYR   B CE1   
9345  C  CE2   . TYR   B 189 ? 0.6295 0.4839 0.6655 0.0217  0.3666  -0.0858 214 TYR   B CE2   
9346  C  CZ    . TYR   B 189 ? 0.6539 0.5000 0.6756 0.0366  0.3759  -0.0775 214 TYR   B CZ    
9347  O  OH    . TYR   B 189 ? 0.6837 0.5155 0.6787 0.0316  0.3923  -0.0659 214 TYR   B OH    
9357  N  N     . THR   B 190 ? 0.4843 0.3811 0.6205 0.0241  0.2874  -0.1015 215 THR   B N     
9358  C  CA    . THR   B 190 ? 0.4910 0.3452 0.6308 -0.0107 0.3015  -0.1049 215 THR   B CA    
9359  C  C     . THR   B 190 ? 0.4492 0.3186 0.6405 -0.0168 0.2910  -0.0974 215 THR   B C     
9360  O  O     . THR   B 190 ? 0.4063 0.2939 0.6543 0.0026  0.2600  -0.0914 215 THR   B O     
9361  C  CB    . THR   B 190 ? 0.5100 0.3347 0.6155 -0.0283 0.2943  -0.1290 215 THR   B CB    
9362  O  OG1   . THR   B 190 ? 0.5090 0.3176 0.5961 -0.0367 0.2864  -0.1312 215 THR   B OG1   
9363  C  CG2   . THR   B 190 ? 0.5290 0.3417 0.6126 -0.0469 0.2854  -0.1348 215 THR   B CG2   
9371  N  N     . CYS   B 191 ? 0.4908 0.3306 0.6399 -0.0189 0.3077  -0.1002 216 CYS   B N     
9372  C  CA    . CYS   B 191 ? 0.5341 0.3294 0.6528 -0.0449 0.3381  -0.0977 216 CYS   B CA    
9373  C  C     . CYS   B 191 ? 0.5274 0.3096 0.6077 -0.0409 0.3283  -0.0820 216 CYS   B C     
9374  O  O     . CYS   B 191 ? 0.5719 0.3030 0.5920 -0.0487 0.3368  -0.0854 216 CYS   B O     
9375  C  CB    . CYS   B 191 ? 0.5537 0.3627 0.7064 -0.0703 0.3495  -0.1143 216 CYS   B CB    
9376  S  SG    . CYS   B 191 ? 0.5931 0.4116 0.7480 -0.0917 0.3519  -0.1176 216 CYS   B SG    
9382  N  N     . ILE   B 192 ? 0.4767 0.2907 0.5672 -0.0443 0.3018  -0.0806 217 ILE   B N     
9383  C  CA    . ILE   B 192 ? 0.4712 0.3064 0.5358 -0.0679 0.2948  -0.0838 217 ILE   B CA    
9384  C  C     . ILE   B 192 ? 0.4802 0.3051 0.5215 -0.0786 0.2939  -0.0845 217 ILE   B C     
9385  O  O     . ILE   B 192 ? 0.4860 0.3080 0.5146 -0.0685 0.2923  -0.0916 217 ILE   B O     
9386  C  CB    . ILE   B 192 ? 0.4804 0.3249 0.5263 -0.0802 0.2949  -0.0856 217 ILE   B CB    
9387  C  CG1   . ILE   B 192 ? 0.5192 0.3206 0.5199 -0.0813 0.3007  -0.1078 217 ILE   B CG1   
9388  C  CG2   . ILE   B 192 ? 0.4985 0.3603 0.5264 -0.1003 0.2974  -0.0754 217 ILE   B CG2   
9389  C  CD1   . ILE   B 192 ? 0.5485 0.3109 0.5216 -0.0536 0.2892  -0.1180 217 ILE   B CD1   
9401  N  N     . THR   B 193 ? 0.5352 0.2932 0.5099 -0.0894 0.3072  -0.0809 218 THR   B N     
9402  C  CA    . THR   B 193 ? 0.5489 0.3166 0.5079 -0.0963 0.3091  -0.0757 218 THR   B CA    
9403  C  C     . THR   B 193 ? 0.5824 0.3116 0.4904 -0.0835 0.3098  -0.0785 218 THR   B C     
9404  O  O     . THR   B 193 ? 0.6017 0.3231 0.4943 -0.0817 0.2983  -0.0780 218 THR   B O     
9405  C  CB    . THR   B 193 ? 0.5339 0.3598 0.5323 -0.1072 0.3087  -0.0724 218 THR   B CB    
9406  O  OG1   . THR   B 193 ? 0.5041 0.3965 0.5347 -0.0780 0.3043  -0.0891 218 THR   B OG1   
9407  C  CG2   . THR   B 193 ? 0.5490 0.3807 0.5382 -0.1239 0.3092  -0.0690 218 THR   B CG2   
9415  N  N     . PHE   B 194 ? 0.5996 0.2998 0.4765 -0.0797 0.3096  -0.0812 219 PHE   B N     
9416  C  CA    . PHE   B 194 ? 0.5942 0.3032 0.4839 -0.1120 0.2940  -0.0684 219 PHE   B CA    
9417  C  C     . PHE   B 194 ? 0.5939 0.3027 0.4921 -0.1071 0.3080  -0.0689 219 PHE   B C     
9418  O  O     . PHE   B 194 ? 0.5806 0.2855 0.4972 -0.0934 0.3113  -0.0600 219 PHE   B O     
9419  C  CB    . PHE   B 194 ? 0.5715 0.3185 0.4772 -0.1183 0.2921  -0.0731 219 PHE   B CB    
9420  C  CG    . PHE   B 194 ? 0.5561 0.3343 0.4839 -0.1262 0.2815  -0.0724 219 PHE   B CG    
9421  C  CD1   . PHE   B 194 ? 0.5617 0.3725 0.4905 -0.1197 0.2667  -0.0779 219 PHE   B CD1   
9422  C  CD2   . PHE   B 194 ? 0.5419 0.3468 0.4849 -0.1381 0.2810  -0.0640 219 PHE   B CD2   
9423  C  CE1   . PHE   B 194 ? 0.5279 0.3751 0.5018 -0.1463 0.2574  -0.0755 219 PHE   B CE1   
9424  C  CE2   . PHE   B 194 ? 0.5259 0.3648 0.5055 -0.1509 0.2630  -0.0576 219 PHE   B CE2   
9425  C  CZ    . PHE   B 194 ? 0.4994 0.3719 0.5040 -0.1534 0.2612  -0.0585 219 PHE   B CZ    
9435  N  N     . GLN   B 195 ? 0.5852 0.2999 0.4899 -0.1316 0.2896  -0.0640 220 GLN   B N     
9436  C  CA    . GLN   B 195 ? 0.6002 0.3126 0.4924 -0.1321 0.3010  -0.0703 220 GLN   B CA    
9437  C  C     . GLN   B 195 ? 0.5990 0.2752 0.4755 -0.0918 0.3018  -0.0662 220 GLN   B C     
9438  O  O     . GLN   B 195 ? 0.6147 0.2634 0.4695 -0.1101 0.2995  -0.0669 220 GLN   B O     
9439  C  CB    . GLN   B 195 ? 0.6143 0.3804 0.5192 -0.1507 0.3146  -0.0793 220 GLN   B CB    
9440  C  CG    . GLN   B 195 ? 0.6696 0.4331 0.5520 -0.1877 0.3213  -0.0830 220 GLN   B CG    
9441  C  CD    . GLN   B 195 ? 0.7067 0.4936 0.5895 -0.2349 0.3180  -0.0728 220 GLN   B CD    
9442  O  OE1   . GLN   B 195 ? 0.7595 0.5737 0.6006 -0.2589 0.3277  -0.0591 220 GLN   B OE1   
9443  N  NE2   . GLN   B 195 ? 0.7002 0.4576 0.6164 -0.2439 0.3036  -0.0859 220 GLN   B NE2   
9452  N  N     . PRO   B 196 ? 0.5615 0.2814 0.4506 -0.0636 0.2952  -0.0521 221 PRO   B N     
9453  C  CA    . PRO   B 196 ? 0.5956 0.2664 0.4368 -0.0323 0.2908  -0.0423 221 PRO   B CA    
9454  C  C     . PRO   B 196 ? 0.6107 0.2675 0.4301 -0.0565 0.2690  -0.0435 221 PRO   B C     
9455  O  O     . PRO   B 196 ? 0.5943 0.2846 0.4313 -0.0923 0.2731  -0.0678 221 PRO   B O     
9456  C  CB    . PRO   B 196 ? 0.6253 0.3146 0.4404 0.0082  0.2770  -0.0670 221 PRO   B CB    
9457  C  CG    . PRO   B 196 ? 0.6072 0.3571 0.4500 0.0164  0.2747  -0.0818 221 PRO   B CG    
9458  C  CD    . PRO   B 196 ? 0.5426 0.3262 0.4522 -0.0215 0.2865  -0.0595 221 PRO   B CD    
9466  N  N     . ASP   B 197 ? 0.6022 0.2486 0.4293 -0.0848 0.2627  -0.0156 222 ASP   B N     
9467  C  CA    . ASP   B 197 ? 0.6321 0.2398 0.4352 -0.0747 0.2422  0.0083  222 ASP   B CA    
9468  C  C     . ASP   B 197 ? 0.5892 0.2578 0.4430 -0.0718 0.2626  0.0065  222 ASP   B C     
9469  O  O     . ASP   B 197 ? 0.5555 0.2789 0.4453 -0.0456 0.2765  0.0045  222 ASP   B O     
9470  C  CB    . ASP   B 197 ? 0.6882 0.2325 0.4335 -0.0656 0.2027  0.0234  222 ASP   B CB    
9471  C  CG    . ASP   B 197 ? 0.7411 0.2318 0.4279 -0.0546 0.1790  0.0088  222 ASP   B CG    
9472  O  OD1   . ASP   B 197 ? 0.7714 0.2284 0.4125 -0.0648 0.1903  0.0042  222 ASP   B OD1   
9473  O  OD2   . ASP   B 197 ? 0.7574 0.2340 0.4446 -0.0522 0.1478  -0.0003 222 ASP   B OD2   
9478  N  N     . LEU   B 198 ? 0.5725 0.2606 0.4485 -0.0930 0.2599  -0.0329 223 LEU   B N     
9479  C  CA    . LEU   B 198 ? 0.5964 0.2929 0.4573 -0.0893 0.2508  -0.0505 223 LEU   B CA    
9480  C  C     . LEU   B 198 ? 0.6353 0.3125 0.4457 -0.0401 0.2362  -0.0659 223 LEU   B C     
9481  O  O     . LEU   B 198 ? 0.6504 0.3434 0.4497 0.0018  0.2112  -0.0897 223 LEU   B O     
9482  C  CB    . LEU   B 198 ? 0.6160 0.3156 0.4825 -0.1006 0.2440  -0.0466 223 LEU   B CB    
9483  C  CG    . LEU   B 198 ? 0.6420 0.3481 0.5003 -0.1077 0.2574  -0.0480 223 LEU   B CG    
9484  C  CD1   . LEU   B 198 ? 0.6665 0.3839 0.5106 -0.0880 0.2546  -0.0577 223 LEU   B CD1   
9485  C  CD2   . LEU   B 198 ? 0.6723 0.3515 0.5140 -0.1013 0.2495  -0.0382 223 LEU   B CD2   
9497  N  N     . SER   B 199 ? 0.6906 0.3336 0.4403 -0.0310 0.2502  -0.0649 224 SER   B N     
9498  C  CA    . SER   B 199 ? 0.7404 0.3956 0.4433 0.0034  0.2339  -0.0546 224 SER   B CA    
9499  C  C     . SER   B 199 ? 0.7196 0.4071 0.4468 0.0239  0.2056  -0.0493 224 SER   B C     
9500  O  O     . SER   B 199 ? 0.7054 0.4032 0.4589 0.0581  0.2123  -0.0363 224 SER   B O     
9501  C  CB    . SER   B 199 ? 0.8207 0.4407 0.4515 0.0069  0.2240  -0.0587 224 SER   B CB    
9502  O  OG    . SER   B 199 ? 0.8828 0.4706 0.4655 0.0046  0.2180  -0.0396 224 SER   B OG    
9508  N  N     . LYS   B 200 ? 0.6975 0.3996 0.4324 0.0063  0.1700  -0.0586 225 LYS   B N     
9509  C  CA    . LYS   B 200 ? 0.6896 0.4020 0.4178 -0.0174 0.1592  -0.0600 225 LYS   B CA    
9510  C  C     . LYS   B 200 ? 0.6122 0.3582 0.4172 -0.0396 0.1441  -0.0558 225 LYS   B C     
9511  O  O     . LYS   B 200 ? 0.6310 0.3609 0.4244 -0.0266 0.1371  -0.0614 225 LYS   B O     
9512  C  CB    . LYS   B 200 ? 0.7574 0.4660 0.4235 -0.0390 0.1406  -0.0678 225 LYS   B CB    
9513  C  CG    . LYS   B 200 ? 0.7885 0.5201 0.4420 -0.0525 0.1312  -0.0531 225 LYS   B CG    
9514  C  CD    . LYS   B 200 ? 0.8054 0.5414 0.4545 -0.0689 0.1212  -0.0526 225 LYS   B CD    
9515  C  CE    . LYS   B 200 ? 0.8254 0.5390 0.4555 -0.0775 0.1227  -0.0727 225 LYS   B CE    
9516  N  NZ    . LYS   B 200 ? 0.8493 0.5394 0.4646 -0.0640 0.1107  -0.0812 225 LYS   B NZ    
9530  N  N     . PHE   B 201 ? 0.5072 0.2842 0.4149 -0.0486 0.1407  -0.0523 226 PHE   B N     
9531  C  CA    . PHE   B 201 ? 0.4588 0.2318 0.4058 -0.0580 0.1396  -0.0505 226 PHE   B CA    
9532  C  C     . PHE   B 201 ? 0.4768 0.2449 0.4259 -0.0590 0.1261  -0.0491 226 PHE   B C     
9533  O  O     . PHE   B 201 ? 0.4587 0.2505 0.4198 -0.0576 0.1187  -0.0459 226 PHE   B O     
9534  C  CB    . PHE   B 201 ? 0.4607 0.2305 0.3882 -0.0382 0.1298  -0.0505 226 PHE   B CB    
9535  C  CG    . PHE   B 201 ? 0.4433 0.2368 0.3608 -0.0374 0.1639  -0.0455 226 PHE   B CG    
9536  C  CD1   . PHE   B 201 ? 0.4520 0.2516 0.3581 -0.0391 0.1766  -0.0389 226 PHE   B CD1   
9537  C  CD2   . PHE   B 201 ? 0.4580 0.2442 0.3503 -0.0260 0.1516  -0.0343 226 PHE   B CD2   
9538  C  CE1   . PHE   B 201 ? 0.4529 0.2662 0.3436 -0.0403 0.1877  -0.0235 226 PHE   B CE1   
9539  C  CE2   . PHE   B 201 ? 0.4283 0.2399 0.3348 -0.0464 0.1862  -0.0009 226 PHE   B CE2   
9540  C  CZ    . PHE   B 201 ? 0.4468 0.2514 0.3397 -0.0485 0.2040  -0.0041 226 PHE   B CZ    
9550  N  N     . LYS   B 202 ? 0.5295 0.2633 0.4530 -0.0531 0.1220  -0.0436 227 LYS   B N     
9551  C  CA    . LYS   B 202 ? 0.5276 0.2703 0.4848 -0.0299 0.1463  -0.0522 227 LYS   B CA    
9552  C  C     . LYS   B 202 ? 0.4965 0.2945 0.4892 -0.0262 0.1636  -0.0509 227 LYS   B C     
9553  O  O     . LYS   B 202 ? 0.4666 0.2987 0.4847 -0.0181 0.1688  -0.0539 227 LYS   B O     
9554  C  CB    . LYS   B 202 ? 0.5838 0.2671 0.5241 -0.0109 0.1650  -0.0646 227 LYS   B CB    
9555  C  CG    . LYS   B 202 ? 0.6181 0.2959 0.5656 -0.0268 0.1936  -0.0679 227 LYS   B CG    
9556  C  CD    . LYS   B 202 ? 0.6782 0.3661 0.6093 -0.0337 0.1973  -0.0645 227 LYS   B CD    
9557  C  CE    . LYS   B 202 ? 0.7251 0.4194 0.6358 -0.0301 0.2145  -0.0593 227 LYS   B CE    
9558  N  NZ    . LYS   B 202 ? 0.7617 0.4410 0.6473 -0.0195 0.2218  -0.0562 227 LYS   B NZ    
9572  N  N     . MET   B 203 ? 0.4834 0.3224 0.4974 -0.0526 0.1634  -0.0490 228 MET   B N     
9573  C  CA    A MET   B 203 ? 0.4852 0.3418 0.5036 -0.0536 0.1560  -0.0317 228 MET   B CA    
9574  C  CA    B MET   B 203 ? 0.4914 0.3566 0.5063 -0.0610 0.1635  -0.0328 228 MET   B CA    
9575  C  C     . MET   B 203 ? 0.4946 0.3435 0.5317 -0.0699 0.1610  -0.0247 228 MET   B C     
9576  O  O     . MET   B 203 ? 0.5321 0.3294 0.5410 -0.0736 0.1682  0.0046  228 MET   B O     
9577  C  CB    A MET   B 203 ? 0.4509 0.3436 0.4785 -0.0575 0.1519  -0.0146 228 MET   B CB    
9578  C  CB    B MET   B 203 ? 0.4766 0.3950 0.4883 -0.0720 0.1720  -0.0179 228 MET   B CB    
9579  C  CG    A MET   B 203 ? 0.4164 0.3348 0.4486 -0.0416 0.1539  -0.0232 228 MET   B CG    
9580  C  CG    B MET   B 203 ? 0.4609 0.4292 0.4683 -0.0681 0.1834  -0.0175 228 MET   B CG    
9581  S  SD    A MET   B 203 ? 0.3435 0.2903 0.4235 -0.0592 0.1504  -0.0344 228 MET   B SD    
9582  S  SD    B MET   B 203 ? 0.4138 0.4453 0.4527 -0.0726 0.1967  -0.0163 228 MET   B SD    
9583  C  CE    A MET   B 203 ? 0.3092 0.2926 0.4172 -0.0426 0.1603  -0.0315 228 MET   B CE    
9584  C  CE    B MET   B 203 ? 0.3908 0.4513 0.4469 -0.0939 0.2079  -0.0084 228 MET   B CE    
9603  N  N     . GLN   B 204 ? 0.5005 0.3620 0.5810 -0.0650 0.1543  -0.0392 229 GLN   B N     
9604  C  CA    . GLN   B 204 ? 0.5414 0.4183 0.6308 -0.0737 0.1267  -0.0407 229 GLN   B CA    
9605  C  C     . GLN   B 204 ? 0.5373 0.4195 0.6311 -0.0676 0.1734  -0.0406 229 GLN   B C     
9606  O  O     . GLN   B 204 ? 0.5418 0.4386 0.6340 -0.0664 0.2002  -0.0180 229 GLN   B O     
9607  C  CB    . GLN   B 204 ? 0.5861 0.4829 0.6738 -0.1188 0.0722  -0.0363 229 GLN   B CB    
9608  C  CG    . GLN   B 204 ? 0.6440 0.5530 0.7053 -0.1201 0.0303  -0.0379 229 GLN   B CG    
9609  C  CD    . GLN   B 204 ? 0.6483 0.5924 0.7261 -0.1252 -0.0027 -0.0385 229 GLN   B CD    
9610  O  OE1   . GLN   B 204 ? 0.6732 0.6155 0.7270 -0.1296 -0.0268 -0.0627 229 GLN   B OE1   
9611  N  NE2   . GLN   B 204 ? 0.6021 0.5870 0.7402 -0.1525 -0.0071 -0.0167 229 GLN   B NE2   
9620  N  N     . SER   B 205 ? 0.4927 0.4046 0.6239 -0.0738 0.1847  -0.0483 230 SER   B N     
9621  C  CA    . SER   B 205 ? 0.4530 0.3953 0.6219 -0.0729 0.1861  -0.0626 230 SER   B CA    
9622  C  C     . SER   B 205 ? 0.4301 0.3658 0.6124 -0.0382 0.1967  -0.0486 230 SER   B C     
9623  O  O     . SER   B 205 ? 0.4311 0.3436 0.5949 -0.0409 0.1955  -0.0532 230 SER   B O     
9624  C  CB    . SER   B 205 ? 0.4907 0.4569 0.6325 -0.0691 0.1511  -0.0815 230 SER   B CB    
9625  O  OG    . SER   B 205 ? 0.5085 0.4824 0.6398 -0.0906 0.1093  -0.0931 230 SER   B OG    
9631  N  N     . LEU   B 206 ? 0.3937 0.3542 0.6156 -0.0110 0.2206  -0.0466 231 LEU   B N     
9632  C  CA    . LEU   B 206 ? 0.3232 0.3353 0.6140 -0.0152 0.2258  -0.0543 231 LEU   B CA    
9633  C  C     . LEU   B 206 ? 0.3003 0.3601 0.6205 -0.0422 0.2024  -0.0542 231 LEU   B C     
9634  O  O     . LEU   B 206 ? 0.3222 0.4328 0.6299 -0.0356 0.2014  -0.0648 231 LEU   B O     
9635  C  CB    . LEU   B 206 ? 0.3197 0.3354 0.6143 -0.0155 0.2228  -0.0583 231 LEU   B CB    
9636  C  CG    . LEU   B 206 ? 0.3420 0.3498 0.6063 -0.0346 0.2296  -0.0707 231 LEU   B CG    
9637  C  CD1   . LEU   B 206 ? 0.3329 0.3647 0.6024 -0.0682 0.2355  -0.0685 231 LEU   B CD1   
9638  C  CD2   . LEU   B 206 ? 0.3765 0.3842 0.6109 -0.0330 0.2143  -0.0835 231 LEU   B CD2   
9650  N  N     . ASP   B 207 ? 0.2790 0.2981 0.6066 -0.0679 0.1899  -0.0543 232 ASP   B N     
9651  C  CA    . ASP   B 207 ? 0.2697 0.2723 0.6091 -0.0569 0.1622  -0.0566 232 ASP   B CA    
9652  C  C     . ASP   B 207 ? 0.2681 0.2857 0.6079 -0.0612 0.1431  -0.0752 232 ASP   B C     
9653  O  O     . ASP   B 207 ? 0.2472 0.2951 0.6065 -0.0435 0.1316  -0.0891 232 ASP   B O     
9654  C  CB    . ASP   B 207 ? 0.2695 0.2781 0.6136 -0.0492 0.1581  -0.0674 232 ASP   B CB    
9655  C  CG    . ASP   B 207 ? 0.3090 0.3006 0.6272 -0.0379 0.1419  -0.0867 232 ASP   B CG    
9656  O  OD1   . ASP   B 207 ? 0.3252 0.2921 0.6212 -0.0422 0.1384  -0.0841 232 ASP   B OD1   
9657  O  OD2   . ASP   B 207 ? 0.3464 0.3439 0.6466 -0.0115 0.1341  -0.0870 232 ASP   B OD2   
9662  N  N     . LYS   B 208 ? 0.2498 0.2755 0.6058 -0.0627 0.1282  -0.0928 233 LYS   B N     
9663  C  CA    . LYS   B 208 ? 0.2337 0.2998 0.6167 -0.0913 0.0910  -0.0899 233 LYS   B CA    
9664  C  C     . LYS   B 208 ? 0.1961 0.2941 0.6014 -0.0666 0.0749  -0.0621 233 LYS   B C     
9665  O  O     . LYS   B 208 ? 0.1986 0.2709 0.6042 -0.0650 0.0629  -0.0816 233 LYS   B O     
9666  C  CB    . LYS   B 208 ? 0.2744 0.3300 0.6532 -0.0867 0.0639  -0.1165 233 LYS   B CB    
9667  C  CG    . LYS   B 208 ? 0.3188 0.3493 0.6835 -0.0689 0.0291  -0.1410 233 LYS   B CG    
9668  C  CD    . LYS   B 208 ? 0.4025 0.3751 0.7138 -0.0774 -0.0035 -0.1516 233 LYS   B CD    
9669  C  CE    . LYS   B 208 ? 0.4635 0.3976 0.7342 -0.0918 -0.0216 -0.1675 233 LYS   B CE    
9670  N  NZ    . LYS   B 208 ? 0.5128 0.4458 0.7548 -0.0674 -0.0240 -0.1552 233 LYS   B NZ    
9684  N  N     . ASP   B 209 ? 0.1736 0.2933 0.5813 -0.0347 0.0822  -0.0618 234 ASP   B N     
9685  C  CA    . ASP   B 209 ? 0.1761 0.2801 0.5393 -0.0316 0.0759  -0.0662 234 ASP   B CA    
9686  C  C     . ASP   B 209 ? 0.1844 0.2660 0.5112 -0.0357 0.0691  -0.0708 234 ASP   B C     
9687  O  O     . ASP   B 209 ? 0.1759 0.2796 0.5068 -0.0608 0.0748  -0.0574 234 ASP   B O     
9688  C  CB    . ASP   B 209 ? 0.1887 0.3041 0.5295 -0.0213 0.0541  -0.0776 234 ASP   B CB    
9689  C  CG    . ASP   B 209 ? 0.1850 0.3420 0.5350 -0.0468 0.0300  -0.0692 234 ASP   B CG    
9690  O  OD1   . ASP   B 209 ? 0.2013 0.3705 0.5426 0.0061  0.0244  -0.0740 234 ASP   B OD1   
9691  O  OD2   . ASP   B 209 ? 0.1645 0.3583 0.5355 -0.0292 0.0358  -0.0646 234 ASP   B OD2   
9696  N  N     . ILE   B 210 ? 0.2370 0.2417 0.4953 -0.0419 0.0649  -0.0792 235 ILE   B N     
9697  C  CA    . ILE   B 210 ? 0.2291 0.2485 0.4865 -0.0615 0.0937  -0.0745 235 ILE   B CA    
9698  C  C     . ILE   B 210 ? 0.1949 0.2560 0.4876 -0.0683 0.1119  -0.0781 235 ILE   B C     
9699  O  O     . ILE   B 210 ? 0.2004 0.2588 0.4860 -0.0521 0.1109  -0.0713 235 ILE   B O     
9700  C  CB    . ILE   B 210 ? 0.2635 0.2643 0.4800 -0.0991 0.1155  -0.0601 235 ILE   B CB    
9701  C  CG1   . ILE   B 210 ? 0.2388 0.2706 0.4752 -0.0910 0.1396  -0.0622 235 ILE   B CG1   
9702  C  CG2   . ILE   B 210 ? 0.3094 0.2789 0.4759 -0.0795 0.1178  -0.0296 235 ILE   B CG2   
9703  C  CD1   . ILE   B 210 ? 0.2378 0.2911 0.4815 -0.0990 0.1335  -0.0701 235 ILE   B CD1   
9715  N  N     . VAL   B 211 ? 0.1796 0.2715 0.5031 -0.0559 0.1016  -0.0618 236 VAL   B N     
9716  C  CA    . VAL   B 211 ? 0.1799 0.2769 0.5161 -0.0506 0.1040  -0.0648 236 VAL   B CA    
9717  C  C     . VAL   B 211 ? 0.1674 0.2875 0.5135 -0.0398 0.0938  -0.0572 236 VAL   B C     
9718  O  O     . VAL   B 211 ? 0.1650 0.3035 0.5249 -0.0319 0.0897  -0.0648 236 VAL   B O     
9719  C  CB    . VAL   B 211 ? 0.1844 0.2899 0.5201 -0.0471 0.1130  -0.0696 236 VAL   B CB    
9720  C  CG1   . VAL   B 211 ? 0.2048 0.3063 0.5384 -0.0572 0.1299  -0.0909 236 VAL   B CG1   
9721  C  CG2   . VAL   B 211 ? 0.2026 0.3039 0.5520 -0.0520 0.1221  -0.0626 236 VAL   B CG2   
9731  N  N     . ALA   B 212 ? 0.1757 0.2705 0.5064 -0.0407 0.0810  -0.0540 237 ALA   B N     
9732  C  CA    . ALA   B 212 ? 0.1654 0.2860 0.4935 -0.0549 0.0537  -0.0618 237 ALA   B CA    
9733  C  C     . ALA   B 212 ? 0.1553 0.2776 0.4810 -0.0265 0.0554  -0.0636 237 ALA   B C     
9734  O  O     . ALA   B 212 ? 0.1504 0.2731 0.4852 -0.0043 0.0670  -0.0624 237 ALA   B O     
9735  C  CB    . ALA   B 212 ? 0.1817 0.3141 0.4973 -0.0473 0.0216  -0.0666 237 ALA   B CB    
9741  N  N     . LEU   B 213 ? 0.1621 0.2661 0.4499 -0.0496 0.0602  -0.0557 238 LEU   B N     
9742  C  CA    . LEU   B 213 ? 0.1462 0.2463 0.4220 -0.0209 0.0610  -0.0527 238 LEU   B CA    
9743  C  C     . LEU   B 213 ? 0.1405 0.2675 0.4316 -0.0230 0.0607  -0.0383 238 LEU   B C     
9744  O  O     . LEU   B 213 ? 0.1469 0.2682 0.4298 -0.0190 0.0634  -0.0341 238 LEU   B O     
9745  C  CB    . LEU   B 213 ? 0.2097 0.2790 0.4061 -0.0101 0.0665  -0.0519 238 LEU   B CB    
9746  C  CG    . LEU   B 213 ? 0.2078 0.2678 0.4031 0.0103  0.0671  -0.0383 238 LEU   B CG    
9747  C  CD1   . LEU   B 213 ? 0.1914 0.2969 0.4190 0.0380  0.0615  -0.0257 238 LEU   B CD1   
9748  C  CD2   . LEU   B 213 ? 0.1961 0.2832 0.3866 -0.0207 0.0662  -0.0300 238 LEU   B CD2   
9760  N  N     . MET   B 214 ? 0.1868 0.2467 0.4458 -0.0364 0.0803  -0.0375 239 MET   B N     
9761  C  CA    . MET   B 214 ? 0.1948 0.2580 0.4696 -0.0184 0.0940  -0.0569 239 MET   B CA    
9762  C  C     . MET   B 214 ? 0.1546 0.2743 0.4945 -0.0075 0.0771  -0.0688 239 MET   B C     
9763  O  O     . MET   B 214 ? 0.1690 0.2791 0.5032 -0.0187 0.0930  -0.0650 239 MET   B O     
9764  C  CB    . MET   B 214 ? 0.2005 0.2591 0.4698 -0.0231 0.1265  -0.0557 239 MET   B CB    
9765  C  CG    . MET   B 214 ? 0.2390 0.2572 0.4840 -0.0389 0.1443  -0.0284 239 MET   B CG    
9766  S  SD    . MET   B 214 ? 0.3421 0.3297 0.5079 0.0253  0.1714  -0.0061 239 MET   B SD    
9767  C  CE    . MET   B 214 ? 0.3987 0.3206 0.5078 0.0083  0.1575  -0.0252 239 MET   B CE    
9777  N  N     . VAL   B 215 ? 0.1455 0.2927 0.5134 -0.0169 0.0638  -0.0444 240 VAL   B N     
9778  C  CA    . VAL   B 215 ? 0.1474 0.2948 0.5233 -0.0210 0.0599  -0.0522 240 VAL   B CA    
9779  C  C     . VAL   B 215 ? 0.1434 0.2656 0.5241 -0.0005 0.0530  -0.0496 240 VAL   B C     
9780  O  O     . VAL   B 215 ? 0.1426 0.2684 0.5269 -0.0142 0.0507  -0.0324 240 VAL   B O     
9781  C  CB    . VAL   B 215 ? 0.1592 0.3188 0.5598 -0.0363 0.0457  -0.0555 240 VAL   B CB    
9782  C  CG1   . VAL   B 215 ? 0.1548 0.3280 0.5805 0.0059  0.0308  -0.0550 240 VAL   B CG1   
9783  C  CG2   . VAL   B 215 ? 0.1656 0.3382 0.5533 -0.0433 0.0743  -0.0450 240 VAL   B CG2   
9793  N  N     . ARG   B 216 ? 0.1334 0.2796 0.4980 0.0032  0.0347  -0.0574 241 ARG   B N     
9794  C  CA    . ARG   B 216 ? 0.1354 0.2936 0.4883 0.0104  0.0420  -0.0626 241 ARG   B CA    
9795  C  C     . ARG   B 216 ? 0.1440 0.2692 0.4849 -0.0136 0.0467  -0.0566 241 ARG   B C     
9796  O  O     . ARG   B 216 ? 0.1547 0.2527 0.4901 -0.0143 0.0557  -0.0457 241 ARG   B O     
9797  C  CB    . ARG   B 216 ? 0.1373 0.3040 0.4711 -0.0155 0.0624  -0.0569 241 ARG   B CB    
9798  C  CG    . ARG   B 216 ? 0.1259 0.2855 0.4605 -0.0148 0.0331  -0.0644 241 ARG   B CG    
9799  C  CD    . ARG   B 216 ? 0.1204 0.2737 0.4471 -0.0124 0.0178  -0.0682 241 ARG   B CD    
9800  N  NE    . ARG   B 216 ? 0.1179 0.2595 0.4354 -0.0239 0.0138  -0.0437 241 ARG   B NE    
9801  C  CZ    . ARG   B 216 ? 0.1267 0.2533 0.4224 -0.0159 0.0227  -0.0407 241 ARG   B CZ    
9802  N  NH1   . ARG   B 216 ? 0.1760 0.2739 0.4162 0.0037  0.0200  -0.0565 241 ARG   B NH1   
9803  N  NH2   . ARG   B 216 ? 0.1771 0.2641 0.4212 0.0117  -0.0029 -0.0418 241 ARG   B NH2   
9817  N  N     . ARG   B 217 ? 0.1299 0.2527 0.4638 -0.0010 0.0368  -0.0548 242 ARG   B N     
9818  C  CA    . ARG   B 217 ? 0.1332 0.2667 0.4466 0.0178  0.0370  -0.0465 242 ARG   B CA    
9819  C  C     . ARG   B 217 ? 0.1310 0.2861 0.4588 0.0048  0.0522  -0.0581 242 ARG   B C     
9820  O  O     . ARG   B 217 ? 0.1378 0.2675 0.4557 0.0019  0.0414  -0.0574 242 ARG   B O     
9821  C  CB    . ARG   B 217 ? 0.1381 0.2676 0.4173 -0.0145 0.0514  -0.0391 242 ARG   B CB    
9822  C  CG    . ARG   B 217 ? 0.1661 0.2457 0.3856 -0.0009 0.0377  -0.0384 242 ARG   B CG    
9823  C  CD    . ARG   B 217 ? 0.1527 0.2392 0.3641 -0.0051 0.0449  -0.0523 242 ARG   B CD    
9824  N  NE    . ARG   B 217 ? 0.1739 0.2255 0.3541 -0.0083 0.0367  -0.0357 242 ARG   B NE    
9825  C  CZ    . ARG   B 217 ? 0.1749 0.2473 0.3662 -0.0186 0.0294  -0.0215 242 ARG   B CZ    
9826  N  NH1   . ARG   B 217 ? 0.1751 0.2638 0.3863 -0.0261 0.0310  -0.0388 242 ARG   B NH1   
9827  N  NH2   . ARG   B 217 ? 0.1775 0.2407 0.3496 0.0103  0.0245  -0.0018 242 ARG   B NH2   
9841  N  N     . ALA   B 218 ? 0.1420 0.3000 0.4760 0.0089  0.0658  -0.0603 243 ALA   B N     
9842  C  CA    . ALA   B 218 ? 0.1640 0.3152 0.5304 -0.0170 0.0836  -0.0590 243 ALA   B CA    
9843  C  C     . ALA   B 218 ? 0.1491 0.2975 0.5325 -0.0149 0.0601  -0.0574 243 ALA   B C     
9844  O  O     . ALA   B 218 ? 0.1506 0.2938 0.5522 -0.0153 0.0542  -0.0468 243 ALA   B O     
9845  C  CB    . ALA   B 218 ? 0.1761 0.3167 0.5312 -0.0259 0.1070  -0.0685 243 ALA   B CB    
9851  N  N     . TYR   B 219 ? 0.1379 0.2958 0.5151 -0.0064 0.0356  -0.0623 244 TYR   B N     
9852  C  CA    . TYR   B 219 ? 0.1363 0.3120 0.5231 0.0059  0.0074  -0.0622 244 TYR   B CA    
9853  C  C     . TYR   B 219 ? 0.1399 0.3178 0.5240 0.0017  0.0005  -0.0433 244 TYR   B C     
9854  O  O     . TYR   B 219 ? 0.1432 0.3150 0.5364 -0.0005 -0.0031 -0.0411 244 TYR   B O     
9855  C  CB    . TYR   B 219 ? 0.1424 0.3342 0.5487 0.0011  0.0002  -0.0635 244 TYR   B CB    
9856  C  CG    . TYR   B 219 ? 0.1574 0.3743 0.5951 0.0081  0.0012  -0.0487 244 TYR   B CG    
9857  C  CD1   . TYR   B 219 ? 0.1596 0.3637 0.6126 -0.0228 0.0227  -0.0455 244 TYR   B CD1   
9858  C  CD2   . TYR   B 219 ? 0.1533 0.4214 0.6000 -0.0097 -0.0127 -0.0338 244 TYR   B CD2   
9859  C  CE1   . TYR   B 219 ? 0.1598 0.3773 0.6125 -0.0185 0.0331  -0.0391 244 TYR   B CE1   
9860  C  CE2   . TYR   B 219 ? 0.1479 0.4216 0.5850 -0.0042 0.0013  -0.0221 244 TYR   B CE2   
9861  C  CZ    . TYR   B 219 ? 0.1553 0.4192 0.6105 0.0092  0.0073  -0.0328 244 TYR   B CZ    
9862  O  OH    . TYR   B 219 ? 0.1638 0.4633 0.6430 0.0016  0.0051  -0.0397 244 TYR   B OH    
9872  N  N     . ASP   B 220 ? 0.1265 0.3019 0.4897 0.0172  0.0049  -0.0324 245 ASP   B N     
9873  C  CA    . ASP   B 220 ? 0.1288 0.2745 0.4746 0.0008  0.0303  -0.0396 245 ASP   B CA    
9874  C  C     . ASP   B 220 ? 0.1369 0.2563 0.4763 0.0072  0.0310  -0.0320 245 ASP   B C     
9875  O  O     . ASP   B 220 ? 0.1616 0.2446 0.4669 0.0078  0.0377  -0.0059 245 ASP   B O     
9876  C  CB    . ASP   B 220 ? 0.1117 0.2583 0.4334 -0.0004 0.0241  -0.0124 245 ASP   B CB    
9877  C  CG    . ASP   B 220 ? 0.1134 0.2709 0.4319 -0.0134 0.0266  -0.0243 245 ASP   B CG    
9878  O  OD1   . ASP   B 220 ? 0.1093 0.2703 0.4258 -0.0104 -0.0093 -0.0236 245 ASP   B OD1   
9879  O  OD2   . ASP   B 220 ? 0.1431 0.2667 0.4330 -0.0006 0.0509  -0.0383 245 ASP   B OD2   
9884  N  N     . ILE   B 221 ? 0.1589 0.2649 0.4902 0.0008  0.0350  -0.0320 246 ILE   B N     
9885  C  CA    . ILE   B 221 ? 0.1536 0.2714 0.5049 0.0119  0.0533  -0.0288 246 ILE   B CA    
9886  C  C     . ILE   B 221 ? 0.1540 0.2803 0.5357 0.0254  0.0642  -0.0220 246 ILE   B C     
9887  O  O     . ILE   B 221 ? 0.1760 0.2940 0.5637 0.0347  0.0653  -0.0081 246 ILE   B O     
9888  C  CB    . ILE   B 221 ? 0.1771 0.3034 0.4981 0.0141  0.0676  -0.0229 246 ILE   B CB    
9889  C  CG1   . ILE   B 221 ? 0.1744 0.3170 0.4901 0.0119  0.0455  -0.0052 246 ILE   B CG1   
9890  C  CG2   . ILE   B 221 ? 0.1981 0.3319 0.5033 0.0401  0.0982  -0.0362 246 ILE   B CG2   
9891  C  CD1   . ILE   B 221 ? 0.1805 0.3303 0.4887 0.0093  0.0345  -0.0039 246 ILE   B CD1   
9903  N  N     . ALA   B 222 ? 0.1531 0.2992 0.5358 0.0433  0.0404  -0.0221 247 ALA   B N     
9904  C  CA    . ALA   B 222 ? 0.1570 0.3156 0.5777 0.0309  0.0263  -0.0137 247 ALA   B CA    
9905  C  C     . ALA   B 222 ? 0.1933 0.3176 0.5943 0.0255  0.0112  -0.0162 247 ALA   B C     
9906  O  O     . ALA   B 222 ? 0.2474 0.3166 0.6180 0.0541  0.0235  -0.0253 247 ALA   B O     
9907  C  CB    . ALA   B 222 ? 0.1578 0.3387 0.5731 0.0496  0.0148  -0.0137 247 ALA   B CB    
9913  N  N     . GLY   B 223 ? 0.1703 0.3100 0.5760 0.0156  -0.0062 -0.0156 248 GLY   B N     
9914  C  CA    . GLY   B 223 ? 0.1895 0.3383 0.5564 0.0238  -0.0060 -0.0258 248 GLY   B CA    
9915  C  C     . GLY   B 223 ? 0.1701 0.3263 0.5295 0.0321  0.0123  -0.0157 248 GLY   B C     
9916  O  O     . GLY   B 223 ? 0.2408 0.3496 0.5205 0.0503  -0.0287 0.0024  248 GLY   B O     
9920  N  N     . SER   B 224 ? 0.1427 0.3002 0.5067 0.0012  0.0230  -0.0168 249 SER   B N     
9921  C  CA    . SER   B 224 ? 0.1404 0.3043 0.5087 0.0381  0.0313  -0.0156 249 SER   B CA    
9922  C  C     . SER   B 224 ? 0.1942 0.3128 0.5289 0.0438  0.0188  -0.0227 249 SER   B C     
9923  O  O     . SER   B 224 ? 0.2047 0.3079 0.5117 0.0537  0.0040  -0.0107 249 SER   B O     
9924  C  CB    . SER   B 224 ? 0.1355 0.3211 0.5002 0.0291  0.0363  -0.0168 249 SER   B CB    
9925  O  OG    . SER   B 224 ? 0.1594 0.3010 0.4994 0.0200  0.0384  -0.0137 249 SER   B OG    
9931  N  N     . THR   B 225 ? 0.2414 0.3125 0.5656 0.0346  0.0385  -0.0356 250 THR   B N     
9932  C  CA    . THR   B 225 ? 0.2609 0.2999 0.6109 0.0292  0.0548  -0.0410 250 THR   B CA    
9933  C  C     . THR   B 225 ? 0.2640 0.3124 0.6527 0.0434  -0.0004 -0.0480 250 THR   B C     
9934  O  O     . THR   B 225 ? 0.2875 0.3361 0.6701 0.0608  -0.0595 -0.0424 250 THR   B O     
9935  C  CB    . THR   B 225 ? 0.2683 0.3178 0.6270 -0.0193 0.0802  -0.0298 250 THR   B CB    
9936  O  OG1   . THR   B 225 ? 0.2180 0.3586 0.6416 0.0415  0.1048  -0.0323 250 THR   B OG1   
9937  C  CG2   . THR   B 225 ? 0.2686 0.2971 0.6228 -0.0297 0.0842  -0.0073 250 THR   B CG2   
9945  N  N     . LYS   B 226 ? 0.2934 0.3259 0.6820 0.0593  0.0163  -0.0488 251 LYS   B N     
9946  C  CA    A LYS   B 226 ? 0.3474 0.3530 0.7035 0.0651  0.0218  -0.0361 251 LYS   B CA    
9947  C  CA    B LYS   B 226 ? 0.3517 0.3499 0.6970 0.0554  0.0472  -0.0453 251 LYS   B CA    
9948  C  C     . LYS   B 226 ? 0.3718 0.3597 0.7120 0.0658  0.0372  -0.0398 251 LYS   B C     
9949  O  O     . LYS   B 226 ? 0.4245 0.3510 0.7138 0.0474  0.0292  -0.0340 251 LYS   B O     
9950  C  CB    A LYS   B 226 ? 0.3605 0.3566 0.7137 0.0930  0.0171  -0.0146 251 LYS   B CB    
9951  C  CB    B LYS   B 226 ? 0.3749 0.3462 0.6942 0.0636  0.0942  -0.0422 251 LYS   B CB    
9952  C  CG    A LYS   B 226 ? 0.3702 0.3732 0.7219 0.1201  -0.0024 -0.0006 251 LYS   B CG    
9953  C  CG    B LYS   B 226 ? 0.4045 0.3529 0.6909 0.0703  0.1231  -0.0462 251 LYS   B CG    
9954  C  CD    A LYS   B 226 ? 0.3848 0.4079 0.7275 0.1307  -0.0104 0.0084  251 LYS   B CD    
9955  C  CD    B LYS   B 226 ? 0.4274 0.3553 0.6881 0.0693  0.1413  -0.0458 251 LYS   B CD    
9956  C  CE    A LYS   B 226 ? 0.4059 0.4350 0.7294 0.1329  -0.0272 0.0144  251 LYS   B CE    
9957  C  CE    B LYS   B 226 ? 0.4448 0.3390 0.6811 0.0715  0.1488  -0.0441 251 LYS   B CE    
9958  N  NZ    A LYS   B 226 ? 0.4308 0.4601 0.7307 0.1322  -0.0231 0.0096  251 LYS   B NZ    
9959  N  NZ    B LYS   B 226 ? 0.4162 0.2846 0.6737 0.0809  0.1453  -0.0369 251 LYS   B NZ    
9984  N  N     . ASP   B 227 ? 0.3951 0.3951 0.7357 0.0918  0.0523  -0.0367 252 ASP   B N     
9985  C  CA    . ASP   B 227 ? 0.4439 0.4127 0.7502 0.0989  0.0734  -0.0318 252 ASP   B CA    
9986  C  C     . ASP   B 227 ? 0.4311 0.3791 0.7417 0.0927  0.1064  -0.0410 252 ASP   B C     
9987  O  O     . ASP   B 227 ? 0.4741 0.3748 0.7432 0.0899  0.1145  -0.0390 252 ASP   B O     
9988  C  CB    . ASP   B 227 ? 0.5179 0.4466 0.7754 0.0897  0.0398  -0.0114 252 ASP   B CB    
9989  C  CG    . ASP   B 227 ? 0.5928 0.4843 0.8005 0.0970  0.0045  0.0094  252 ASP   B CG    
9990  O  OD1   . ASP   B 227 ? 0.6064 0.4844 0.8039 0.1147  -0.0108 0.0220  252 ASP   B OD1   
9991  O  OD2   . ASP   B 227 ? 0.6416 0.5130 0.8169 0.1042  -0.0075 0.0113  252 ASP   B OD2   
9996  N  N     . VAL   B 228 ? 0.3713 0.3617 0.7346 0.0775  0.1348  -0.0516 253 VAL   B N     
9997  C  CA    . VAL   B 228 ? 0.3152 0.3724 0.7316 0.0752  0.1467  -0.0586 253 VAL   B CA    
9998  C  C     . VAL   B 228 ? 0.2909 0.3761 0.7378 0.0520  0.1434  -0.0673 253 VAL   B C     
9999  O  O     . VAL   B 228 ? 0.3814 0.3527 0.7423 0.0419  0.1029  -0.0677 253 VAL   B O     
10000 C  CB    . VAL   B 228 ? 0.3247 0.3688 0.7277 0.0545  0.1409  -0.0550 253 VAL   B CB    
10001 C  CG1   . VAL   B 228 ? 0.3642 0.3783 0.7297 0.0876  0.1515  -0.0707 253 VAL   B CG1   
10002 C  CG2   . VAL   B 228 ? 0.3358 0.3739 0.7243 0.0659  0.1384  -0.0567 253 VAL   B CG2   
10012 N  N     . LYS   B 229 ? 0.2719 0.4189 0.7527 0.0531  0.1231  -0.0742 254 LYS   B N     
10013 C  CA    . LYS   B 229 ? 0.2501 0.4413 0.7712 0.0554  0.1035  -0.0909 254 LYS   B CA    
10014 C  C     . LYS   B 229 ? 0.2816 0.4223 0.7621 0.0466  0.0924  -0.1130 254 LYS   B C     
10015 O  O     . LYS   B 229 ? 0.3336 0.4247 0.7580 0.0794  0.0776  -0.1172 254 LYS   B O     
10016 C  CB    . LYS   B 229 ? 0.2994 0.5082 0.8006 0.0558  0.1084  -0.0822 254 LYS   B CB    
10017 C  CG    . LYS   B 229 ? 0.3438 0.5703 0.8288 0.0479  0.1175  -0.0711 254 LYS   B CG    
10018 C  CD    . LYS   B 229 ? 0.4100 0.6406 0.8551 0.0433  0.1124  -0.0578 254 LYS   B CD    
10019 C  CE    . LYS   B 229 ? 0.4354 0.6836 0.8734 0.0331  0.1078  -0.0513 254 LYS   B CE    
10020 N  NZ    . LYS   B 229 ? 0.4842 0.7030 0.8885 0.0242  0.0790  -0.0476 254 LYS   B NZ    
10034 N  N     . VAL   B 230 ? 0.2367 0.3993 0.7558 -0.0008 0.1040  -0.1170 255 VAL   B N     
10035 C  CA    . VAL   B 230 ? 0.2289 0.3774 0.7233 0.0012  0.1201  -0.1164 255 VAL   B CA    
10036 C  C     . VAL   B 230 ? 0.2411 0.3877 0.7406 0.0254  0.1224  -0.1057 255 VAL   B C     
10037 O  O     . VAL   B 230 ? 0.2588 0.3898 0.7481 0.0532  0.1227  -0.0959 255 VAL   B O     
10038 C  CB    . VAL   B 230 ? 0.2335 0.3907 0.7048 0.0049  0.1246  -0.1293 255 VAL   B CB    
10039 C  CG1   . VAL   B 230 ? 0.2443 0.4136 0.6928 0.0109  0.1339  -0.1391 255 VAL   B CG1   
10040 C  CG2   . VAL   B 230 ? 0.2396 0.4030 0.7175 0.0115  0.1285  -0.1251 255 VAL   B CG2   
10050 N  N     . PHE   B 231 ? 0.2445 0.3869 0.7426 0.0037  0.1413  -0.1041 256 PHE   B N     
10051 C  CA    . PHE   B 231 ? 0.2508 0.4062 0.7530 0.0070  0.1497  -0.0939 256 PHE   B CA    
10052 C  C     . PHE   B 231 ? 0.2582 0.3874 0.7530 -0.0029 0.1578  -0.1108 256 PHE   B C     
10053 O  O     . PHE   B 231 ? 0.2670 0.3767 0.7532 -0.0388 0.1712  -0.1317 256 PHE   B O     
10054 C  CB    . PHE   B 231 ? 0.2662 0.4340 0.7442 0.0464  0.1531  -0.0820 256 PHE   B CB    
10055 C  CG    . PHE   B 231 ? 0.2742 0.4650 0.7735 0.0516  0.1564  -0.0817 256 PHE   B CG    
10056 C  CD1   . PHE   B 231 ? 0.2675 0.4690 0.7729 0.0367  0.1627  -0.0676 256 PHE   B CD1   
10057 C  CD2   . PHE   B 231 ? 0.2715 0.4842 0.8021 0.0439  0.1532  -0.0828 256 PHE   B CD2   
10058 C  CE1   . PHE   B 231 ? 0.2679 0.4614 0.7829 0.0429  0.1554  -0.0722 256 PHE   B CE1   
10059 C  CE2   . PHE   B 231 ? 0.2731 0.4770 0.8121 0.0381  0.1561  -0.0834 256 PHE   B CE2   
10060 C  CZ    . PHE   B 231 ? 0.2729 0.4717 0.8076 0.0367  0.1580  -0.0818 256 PHE   B CZ    
10070 N  N     . LEU   B 232 ? 0.2385 0.3667 0.7504 -0.0173 0.1414  -0.0854 257 LEU   B N     
10071 C  CA    . LEU   B 232 ? 0.2410 0.3730 0.7562 -0.0343 0.1405  -0.0944 257 LEU   B CA    
10072 C  C     . LEU   B 232 ? 0.2567 0.3944 0.7523 -0.0423 0.1572  -0.1314 257 LEU   B C     
10073 O  O     . LEU   B 232 ? 0.2908 0.4059 0.7671 -0.0541 0.1878  -0.1668 257 LEU   B O     
10074 C  CB    . LEU   B 232 ? 0.2230 0.3567 0.7682 -0.0090 0.1101  -0.0744 257 LEU   B CB    
10075 C  CG    . LEU   B 232 ? 0.2149 0.3389 0.7653 -0.0139 0.0958  -0.0644 257 LEU   B CG    
10076 C  CD1   . LEU   B 232 ? 0.2361 0.3409 0.7690 0.0006  0.0824  -0.0702 257 LEU   B CD1   
10077 C  CD2   . LEU   B 232 ? 0.2613 0.3264 0.7739 -0.0061 0.0890  -0.0607 257 LEU   B CD2   
10089 N  N     . ASN   B 233 ? 0.2584 0.3926 0.7313 -0.0417 0.1632  -0.1326 258 ASN   B N     
10090 C  CA    . ASN   B 233 ? 0.2631 0.4018 0.7567 -0.0535 0.1605  -0.1429 258 ASN   B CA    
10091 C  C     . ASN   B 233 ? 0.2668 0.4197 0.7836 -0.0503 0.1521  -0.1483 258 ASN   B C     
10092 O  O     . ASN   B 233 ? 0.2594 0.4063 0.7724 -0.0640 0.1454  -0.1434 258 ASN   B O     
10093 C  CB    . ASN   B 233 ? 0.2693 0.4017 0.7694 -0.0620 0.1646  -0.1333 258 ASN   B CB    
10094 C  CG    . ASN   B 233 ? 0.2800 0.4067 0.7984 -0.0674 0.1476  -0.1429 258 ASN   B CG    
10095 O  OD1   . ASN   B 233 ? 0.3275 0.4055 0.8052 -0.0651 0.1532  -0.1459 258 ASN   B OD1   
10096 N  ND2   . ASN   B 233 ? 0.2889 0.4229 0.8135 -0.0272 0.1209  -0.1521 258 ASN   B ND2   
10103 N  N     . GLY   B 234 ? 0.2638 0.4335 0.8039 -0.0341 0.1454  -0.1526 259 GLY   B N     
10104 C  CA    . GLY   B 234 ? 0.2596 0.4297 0.8219 -0.0463 0.1142  -0.1380 259 GLY   B CA    
10105 C  C     . GLY   B 234 ? 0.2438 0.4449 0.8359 -0.0485 0.0936  -0.1270 259 GLY   B C     
10106 O  O     . GLY   B 234 ? 0.2442 0.4668 0.8394 -0.0512 0.0921  -0.1363 259 GLY   B O     
10110 N  N     . ASN   B 235 ? 0.2337 0.4563 0.8238 -0.0305 0.0961  -0.1034 260 ASN   B N     
10111 C  CA    . ASN   B 235 ? 0.2238 0.4823 0.8262 -0.0164 0.0747  -0.0757 260 ASN   B CA    
10112 C  C     . ASN   B 235 ? 0.2277 0.4972 0.8424 0.0037  0.0847  -0.0482 260 ASN   B C     
10113 O  O     . ASN   B 235 ? 0.2283 0.4781 0.8254 0.0232  0.0886  -0.0509 260 ASN   B O     
10114 C  CB    . ASN   B 235 ? 0.2159 0.5013 0.8158 -0.0386 0.0318  -0.0776 260 ASN   B CB    
10115 C  CG    . ASN   B 235 ? 0.2110 0.5193 0.8129 -0.0266 0.0098  -0.0754 260 ASN   B CG    
10116 O  OD1   . ASN   B 235 ? 0.1999 0.5428 0.7708 -0.0125 -0.0067 -0.0756 260 ASN   B OD1   
10117 N  ND2   . ASN   B 235 ? 0.2138 0.5231 0.8265 -0.0305 -0.0002 -0.0645 260 ASN   B ND2   
10124 N  N     . LYS   B 236 ? 0.2331 0.5520 0.8528 -0.0062 0.0850  -0.0171 261 LYS   B N     
10125 C  CA    . LYS   B 236 ? 0.2844 0.6043 0.8631 0.0290  0.0709  -0.0071 261 LYS   B CA    
10126 C  C     . LYS   B 236 ? 0.2250 0.6365 0.8342 -0.0200 0.0566  -0.0124 261 LYS   B C     
10127 O  O     . LYS   B 236 ? 0.2166 0.7058 0.8461 -0.0364 0.0273  -0.0061 261 LYS   B O     
10128 C  CB    . LYS   B 236 ? 0.3628 0.6293 0.8845 0.0733  0.0620  0.0047  261 LYS   B CB    
10129 C  CG    . LYS   B 236 ? 0.4052 0.6483 0.8957 0.1149  0.0439  0.0048  261 LYS   B CG    
10130 C  CD    . LYS   B 236 ? 0.3955 0.6600 0.9016 0.1532  0.0093  -0.0104 261 LYS   B CD    
10131 C  CE    . LYS   B 236 ? 0.4139 0.6895 0.9063 0.1578  -0.0125 -0.0271 261 LYS   B CE    
10132 N  NZ    . LYS   B 236 ? 0.4326 0.7021 0.9109 0.1696  -0.0165 -0.0399 261 LYS   B NZ    
10146 N  N     . LEU   B 237 ? 0.2091 0.5714 0.7881 -0.0043 0.0706  -0.0222 262 LEU   B N     
10147 C  CA    . LEU   B 237 ? 0.1966 0.5285 0.7571 -0.0251 0.0402  -0.0340 262 LEU   B CA    
10148 C  C     . LEU   B 237 ? 0.2003 0.5190 0.7841 -0.0189 -0.0046 -0.0486 262 LEU   B C     
10149 O  O     . LEU   B 237 ? 0.2073 0.5437 0.8135 -0.0018 -0.0080 -0.0504 262 LEU   B O     
10150 C  CB    . LEU   B 237 ? 0.1841 0.4918 0.6996 0.0035  0.0485  -0.0474 262 LEU   B CB    
10151 C  CG    . LEU   B 237 ? 0.1844 0.4541 0.6837 -0.0101 0.0588  -0.0632 262 LEU   B CG    
10152 C  CD1   . LEU   B 237 ? 0.1877 0.4248 0.6724 0.0053  0.0725  -0.0719 262 LEU   B CD1   
10153 C  CD2   . LEU   B 237 ? 0.1958 0.4815 0.7215 -0.0189 0.0651  -0.0650 262 LEU   B CD2   
10165 N  N     . PRO   B 238 ? 0.2118 0.4977 0.7926 -0.0361 -0.0230 -0.0414 263 PRO   B N     
10166 C  CA    . PRO   B 238 ? 0.2356 0.4877 0.7943 -0.0368 -0.0310 -0.0332 263 PRO   B CA    
10167 C  C     . PRO   B 238 ? 0.2656 0.4852 0.7912 -0.0370 -0.0282 -0.0101 263 PRO   B C     
10168 O  O     . PRO   B 238 ? 0.3086 0.5162 0.7978 -0.0437 -0.0360 -0.0001 263 PRO   B O     
10169 C  CB    . PRO   B 238 ? 0.2523 0.4959 0.7983 -0.0390 -0.0381 -0.0432 263 PRO   B CB    
10170 C  CG    . PRO   B 238 ? 0.2544 0.4836 0.7933 -0.0458 -0.0428 -0.0499 263 PRO   B CG    
10171 C  CD    . PRO   B 238 ? 0.2205 0.4790 0.7852 -0.0662 -0.0447 -0.0469 263 PRO   B CD    
10179 N  N     . VAL   B 239 ? 0.2215 0.4648 0.7851 -0.0265 -0.0260 0.0048  264 VAL   B N     
10180 C  CA    . VAL   B 239 ? 0.2060 0.4681 0.7854 0.0053  -0.0121 0.0137  264 VAL   B CA    
10181 C  C     . VAL   B 239 ? 0.2495 0.5192 0.8019 0.0116  0.0017  0.0119  264 VAL   B C     
10182 O  O     . VAL   B 239 ? 0.3466 0.5203 0.8122 0.0208  -0.0072 0.0230  264 VAL   B O     
10183 C  CB    . VAL   B 239 ? 0.1964 0.4317 0.7676 -0.0243 -0.0122 0.0354  264 VAL   B CB    
10184 C  CG1   . VAL   B 239 ? 0.2048 0.4256 0.7505 -0.0554 0.0051  0.0583  264 VAL   B CG1   
10185 C  CG2   . VAL   B 239 ? 0.2189 0.4227 0.7716 -0.0137 -0.0271 0.0300  264 VAL   B CG2   
10195 N  N     . LYS   B 240 ? 0.2372 0.5762 0.8109 0.0186  0.0203  0.0007  265 LYS   B N     
10196 C  CA    . LYS   B 240 ? 0.4044 0.6540 0.8248 0.0269  0.0007  0.0004  265 LYS   B CA    
10197 C  C     . LYS   B 240 ? 0.4662 0.6535 0.8107 -0.0239 0.0082  -0.0221 265 LYS   B C     
10198 O  O     . LYS   B 240 ? 0.5545 0.6904 0.8209 -0.0678 0.0004  -0.0304 265 LYS   B O     
10199 C  CB    . LYS   B 240 ? 0.5071 0.7277 0.8482 0.0483  -0.0210 0.0143  265 LYS   B CB    
10200 C  CG    . LYS   B 240 ? 0.5906 0.7817 0.8689 0.0697  -0.0466 0.0256  265 LYS   B CG    
10201 C  CD    . LYS   B 240 ? 0.6609 0.8194 0.8838 0.0879  -0.0663 0.0428  265 LYS   B CD    
10202 C  CE    . LYS   B 240 ? 0.7071 0.8419 0.8947 0.1027  -0.0740 0.0541  265 LYS   B CE    
10203 N  NZ    . LYS   B 240 ? 0.7292 0.8507 0.9023 0.1138  -0.0761 0.0589  265 LYS   B NZ    
10217 N  N     . GLY   B 241 ? 0.4009 0.6030 0.7818 0.0016  0.0131  -0.0264 266 GLY   B N     
10218 C  CA    . GLY   B 241 ? 0.2922 0.5305 0.7501 0.0595  -0.0117 -0.0187 266 GLY   B CA    
10219 C  C     . GLY   B 241 ? 0.2262 0.4799 0.7144 0.0939  -0.0214 -0.0131 266 GLY   B C     
10220 O  O     . GLY   B 241 ? 0.2175 0.4779 0.7261 0.0857  -0.0227 -0.0161 266 GLY   B O     
10224 N  N     . PHE   B 242 ? 0.2031 0.4348 0.6584 0.0937  -0.0438 -0.0033 267 PHE   B N     
10225 C  CA    . PHE   B 242 ? 0.1895 0.3874 0.6201 0.0500  -0.0664 -0.0086 267 PHE   B CA    
10226 C  C     . PHE   B 242 ? 0.2040 0.3894 0.6256 0.0443  -0.1086 0.0068  267 PHE   B C     
10227 O  O     . PHE   B 242 ? 0.2157 0.3882 0.6291 0.0640  -0.1105 0.0156  267 PHE   B O     
10228 C  CB    . PHE   B 242 ? 0.1859 0.3266 0.5708 0.0145  -0.0655 -0.0217 267 PHE   B CB    
10229 C  CG    . PHE   B 242 ? 0.1746 0.3106 0.5145 0.0019  -0.0554 -0.0205 267 PHE   B CG    
10230 C  CD1   . PHE   B 242 ? 0.2013 0.3224 0.4848 0.0085  -0.0553 -0.0151 267 PHE   B CD1   
10231 C  CD2   . PHE   B 242 ? 0.1933 0.3143 0.4933 0.0036  -0.0576 -0.0086 267 PHE   B CD2   
10232 C  CE1   . PHE   B 242 ? 0.1878 0.3165 0.4637 0.0000  -0.0758 -0.0160 267 PHE   B CE1   
10233 C  CE2   . PHE   B 242 ? 0.2094 0.3087 0.4746 -0.0177 -0.0554 -0.0095 267 PHE   B CE2   
10234 C  CZ    . PHE   B 242 ? 0.2067 0.2983 0.4618 -0.0054 -0.0689 -0.0190 267 PHE   B CZ    
10244 N  N     . ARG   B 243 ? 0.2158 0.3863 0.6243 0.0413  -0.1308 0.0312  268 ARG   B N     
10245 C  CA    . ARG   B 243 ? 0.2719 0.4075 0.6434 0.0448  -0.1690 0.0443  268 ARG   B CA    
10246 C  C     . ARG   B 243 ? 0.2615 0.4131 0.6385 0.0440  -0.1785 0.0329  268 ARG   B C     
10247 O  O     . ARG   B 243 ? 0.2834 0.4125 0.6432 0.0508  -0.1962 0.0242  268 ARG   B O     
10248 C  CB    . ARG   B 243 ? 0.3315 0.4461 0.6680 0.0725  -0.1711 0.0565  268 ARG   B CB    
10249 C  CG    . ARG   B 243 ? 0.3959 0.5232 0.6990 0.0643  -0.1585 0.0411  268 ARG   B CG    
10250 C  CD    . ARG   B 243 ? 0.4513 0.5973 0.7283 0.0481  -0.1456 0.0267  268 ARG   B CD    
10251 N  NE    . ARG   B 243 ? 0.5222 0.6685 0.7566 0.0305  -0.1335 0.0130  268 ARG   B NE    
10252 C  CZ    . ARG   B 243 ? 0.5479 0.7159 0.7842 -0.0043 -0.1336 -0.0014 268 ARG   B CZ    
10253 N  NH1   . ARG   B 243 ? 0.5628 0.7472 0.7969 -0.0349 -0.1254 -0.0079 268 ARG   B NH1   
10254 N  NH2   . ARG   B 243 ? 0.5278 0.7203 0.7934 -0.0320 -0.1382 -0.0102 268 ARG   B NH2   
10268 N  N     . SER   B 244 ? 0.2473 0.4183 0.6338 0.0515  -0.1638 0.0222  269 SER   B N     
10269 C  CA    . SER   B 244 ? 0.2243 0.4539 0.6545 0.0307  -0.1429 0.0075  269 SER   B CA    
10270 C  C     . SER   B 244 ? 0.2108 0.4135 0.6488 0.0059  -0.1293 0.0011  269 SER   B C     
10271 O  O     . SER   B 244 ? 0.2078 0.4157 0.6615 -0.0015 -0.1265 0.0120  269 SER   B O     
10272 C  CB    . SER   B 244 ? 0.2866 0.5273 0.6766 0.0252  -0.1120 -0.0054 269 SER   B CB    
10273 O  OG    . SER   B 244 ? 0.3258 0.5547 0.6939 -0.0057 -0.0846 -0.0081 269 SER   B OG    
10279 N  N     . TYR   B 245 ? 0.2246 0.3798 0.6308 0.0290  -0.1091 -0.0050 270 TYR   B N     
10280 C  CA    . TYR   B 245 ? 0.2261 0.3626 0.6052 0.0289  -0.0793 -0.0017 270 TYR   B CA    
10281 C  C     . TYR   B 245 ? 0.2103 0.3757 0.5917 0.0170  -0.0908 0.0020  270 TYR   B C     
10282 O  O     . TYR   B 245 ? 0.1837 0.4056 0.5948 0.0172  -0.0995 0.0073  270 TYR   B O     
10283 C  CB    . TYR   B 245 ? 0.2541 0.3368 0.5871 0.0438  -0.0651 -0.0115 270 TYR   B CB    
10284 C  CG    . TYR   B 245 ? 0.2768 0.3251 0.5731 0.0376  -0.0559 -0.0312 270 TYR   B CG    
10285 C  CD1   . TYR   B 245 ? 0.3131 0.3089 0.5611 0.0581  -0.0420 -0.0289 270 TYR   B CD1   
10286 C  CD2   . TYR   B 245 ? 0.2384 0.3366 0.5697 0.0386  -0.1034 -0.0190 270 TYR   B CD2   
10287 C  CE1   . TYR   B 245 ? 0.1941 0.3175 0.5488 0.0803  -0.0519 -0.0194 270 TYR   B CE1   
10288 C  CE2   . TYR   B 245 ? 0.2514 0.3441 0.5599 0.0080  -0.1004 0.0060  270 TYR   B CE2   
10289 C  CZ    . TYR   B 245 ? 0.2461 0.3369 0.5529 0.0185  -0.0810 -0.0049 270 TYR   B CZ    
10290 O  OH    . TYR   B 245 ? 0.2182 0.3607 0.5546 -0.0058 -0.0832 -0.0120 270 TYR   B OH    
10300 N  N     . VAL   B 246 ? 0.1879 0.3820 0.5791 0.0135  -0.1109 0.0186  271 VAL   B N     
10301 C  CA    . VAL   B 246 ? 0.2109 0.3894 0.5762 -0.0181 -0.1412 0.0325  271 VAL   B CA    
10302 C  C     . VAL   B 246 ? 0.2422 0.4210 0.5886 -0.0004 -0.1635 0.0367  271 VAL   B C     
10303 O  O     . VAL   B 246 ? 0.2800 0.4192 0.5809 -0.0353 -0.1489 -0.0004 271 VAL   B O     
10304 C  CB    . VAL   B 246 ? 0.2150 0.3763 0.5531 -0.0322 -0.1513 0.0397  271 VAL   B CB    
10305 C  CG1   . VAL   B 246 ? 0.2505 0.3897 0.5568 -0.0143 -0.1688 0.0657  271 VAL   B CG1   
10306 C  CG2   . VAL   B 246 ? 0.1866 0.3689 0.5301 -0.0114 -0.1263 0.0323  271 VAL   B CG2   
10316 N  N     . ASP   B 247 ? 0.2612 0.4409 0.6043 -0.0018 -0.1877 0.0652  272 ASP   B N     
10317 C  CA    . ASP   B 247 ? 0.2875 0.4678 0.6464 -0.0037 -0.2082 0.0680  272 ASP   B CA    
10318 C  C     . ASP   B 247 ? 0.2979 0.4527 0.6586 -0.0230 -0.2155 0.0557  272 ASP   B C     
10319 O  O     . ASP   B 247 ? 0.3271 0.4333 0.6631 -0.0664 -0.2348 0.0537  272 ASP   B O     
10320 C  CB    . ASP   B 247 ? 0.3253 0.5393 0.6823 -0.0083 -0.2239 0.0862  272 ASP   B CB    
10321 C  CG    . ASP   B 247 ? 0.4489 0.6104 0.7311 0.0069  -0.1701 0.0936  272 ASP   B CG    
10322 O  OD1   . ASP   B 247 ? 0.4995 0.6419 0.7518 0.0114  -0.1570 0.1135  272 ASP   B OD1   
10323 O  OD2   . ASP   B 247 ? 0.5185 0.6415 0.7503 0.0099  -0.1455 0.0780  272 ASP   B OD2   
10328 N  N     . MET   B 248 ? 0.2649 0.4248 0.6474 -0.0341 -0.1909 0.0492  273 MET   B N     
10329 C  CA    . MET   B 248 ? 0.2555 0.4164 0.6667 -0.0291 -0.1589 0.0243  273 MET   B CA    
10330 C  C     . MET   B 248 ? 0.2795 0.4175 0.6335 -0.0502 -0.1611 -0.0009 273 MET   B C     
10331 O  O     . MET   B 248 ? 0.2898 0.4061 0.6358 -0.0667 -0.1575 -0.0070 273 MET   B O     
10332 C  CB    . MET   B 248 ? 0.2435 0.4237 0.7106 -0.0146 -0.1101 0.0088  273 MET   B CB    
10333 C  CG    . MET   B 248 ? 0.2793 0.4411 0.7518 -0.0325 -0.0580 0.0036  273 MET   B CG    
10334 S  SD    . MET   B 248 ? 0.3471 0.4648 0.7863 -0.0726 -0.0183 -0.0038 273 MET   B SD    
10335 C  CE    . MET   B 248 ? 0.4135 0.5101 0.7992 -0.0492 -0.0039 -0.0011 273 MET   B CE    
10345 N  N     . TYR   B 249 ? 0.2477 0.4161 0.5921 -0.0344 -0.1766 -0.0158 274 TYR   B N     
10346 C  CA    . TYR   B 249 ? 0.2569 0.4269 0.5951 -0.0529 -0.1648 -0.0374 274 TYR   B CA    
10347 C  C     . TYR   B 249 ? 0.3384 0.5288 0.6288 -0.0465 -0.1533 -0.0324 274 TYR   B C     
10348 O  O     . TYR   B 249 ? 0.4054 0.5251 0.6166 -0.0674 -0.1436 -0.0430 274 TYR   B O     
10349 C  CB    . TYR   B 249 ? 0.2515 0.3738 0.5767 -0.0397 -0.1405 -0.0533 274 TYR   B CB    
10350 C  CG    . TYR   B 249 ? 0.2206 0.3563 0.5492 0.0029  -0.1441 -0.0732 274 TYR   B CG    
10351 C  CD1   . TYR   B 249 ? 0.2315 0.3455 0.5377 0.0147  -0.1495 -0.0820 274 TYR   B CD1   
10352 C  CD2   . TYR   B 249 ? 0.2327 0.3627 0.5406 0.0349  -0.1291 -0.0900 274 TYR   B CD2   
10353 C  CE1   . TYR   B 249 ? 0.2288 0.3427 0.5142 0.0117  -0.1588 -0.0896 274 TYR   B CE1   
10354 C  CE2   . TYR   B 249 ? 0.2414 0.3549 0.5237 0.0057  -0.1509 -0.0977 274 TYR   B CE2   
10355 C  CZ    . TYR   B 249 ? 0.2683 0.3463 0.5151 0.0208  -0.1450 -0.0883 274 TYR   B CZ    
10356 O  OH    . TYR   B 249 ? 0.3572 0.3464 0.5069 0.0332  -0.1333 -0.0822 274 TYR   B OH    
10366 N  N     . LEU   B 250 ? 0.3322 0.6392 0.6694 -0.0306 -0.1808 -0.0268 275 LEU   B N     
10367 C  CA    . LEU   B 250 ? 0.3836 0.7354 0.7165 -0.0487 -0.2168 -0.0396 275 LEU   B CA    
10368 C  C     . LEU   B 250 ? 0.4778 0.8604 0.8000 -0.0531 -0.2451 -0.0602 275 LEU   B C     
10369 O  O     . LEU   B 250 ? 0.4944 0.8727 0.8055 -0.0723 -0.2458 -0.0642 275 LEU   B O     
10370 C  CB    . LEU   B 250 ? 0.3786 0.7055 0.6886 -0.0635 -0.2006 -0.0309 275 LEU   B CB    
10371 C  CG    . LEU   B 250 ? 0.4079 0.6766 0.6722 -0.0853 -0.1506 -0.0265 275 LEU   B CG    
10372 C  CD1   . LEU   B 250 ? 0.4599 0.6756 0.6707 -0.0647 -0.1208 -0.0237 275 LEU   B CD1   
10373 C  CD2   . LEU   B 250 ? 0.3883 0.6593 0.6628 -0.1131 -0.1334 -0.0272 275 LEU   B CD2   
10385 N  N     . LYS   B 251 ? 0.5612 0.9648 0.8833 -0.0499 -0.2488 -0.0759 276 LYS   B N     
10386 C  CA    . LYS   B 251 ? 0.7015 1.0578 0.9695 -0.0399 -0.2286 -0.0861 276 LYS   B CA    
10387 C  C     . LYS   B 251 ? 0.8165 1.1099 1.0294 -0.0282 -0.2105 -0.0998 276 LYS   B C     
10388 O  O     . LYS   B 251 ? 0.8356 1.1191 1.0326 -0.0127 -0.2029 -0.0994 276 LYS   B O     
10389 C  CB    . LYS   B 251 ? 0.7322 1.0858 0.9948 -0.0447 -0.2158 -0.0841 276 LYS   B CB    
10390 C  CG    . LYS   B 251 ? 0.7709 1.1053 1.0179 -0.0525 -0.1969 -0.0818 276 LYS   B CG    
10391 C  CD    . LYS   B 251 ? 0.8035 1.1186 1.0360 -0.0521 -0.1784 -0.0799 276 LYS   B CD    
10392 C  CE    . LYS   B 251 ? 0.8259 1.1277 1.0481 -0.0461 -0.1663 -0.0790 276 LYS   B CE    
10393 N  NZ    . LYS   B 251 ? 0.8333 1.1313 1.0553 -0.0455 -0.1562 -0.0790 276 LYS   B NZ    
10407 N  N     . ASP   B 252 ? 0.8987 1.1425 1.0824 -0.0344 -0.2019 -0.1132 277 ASP   B N     
10408 C  CA    . ASP   B 252 ? 0.9704 1.1720 1.1317 -0.0399 -0.1928 -0.1269 277 ASP   B CA    
10409 C  C     . ASP   B 252 ? 0.9630 1.1724 1.1595 -0.0414 -0.1868 -0.1407 277 ASP   B C     
10410 O  O     . ASP   B 252 ? 0.9902 1.1785 1.1642 -0.0272 -0.1748 -0.1391 277 ASP   B O     
10411 C  CB    . ASP   B 252 ? 1.0340 1.2023 1.1507 -0.0369 -0.1923 -0.1258 277 ASP   B CB    
10412 C  CG    . ASP   B 252 ? 1.0822 1.2258 1.1661 -0.0358 -0.1935 -0.1267 277 ASP   B CG    
10413 O  OD1   . ASP   B 252 ? 1.1022 1.2333 1.1712 -0.0357 -0.1876 -0.1281 277 ASP   B OD1   
10414 O  OD2   . ASP   B 252 ? 1.0910 1.2340 1.1718 -0.0391 -0.1995 -0.1274 277 ASP   B OD2   
10419 N  N     . LYS   B 253 ? 0.9188 1.1645 1.1792 -0.0559 -0.1974 -0.1563 278 LYS   B N     
10420 C  CA    . LYS   B 253 ? 0.8765 1.1595 1.1985 -0.0746 -0.2039 -0.1678 278 LYS   B CA    
10421 C  C     . LYS   B 253 ? 0.8293 1.1525 1.2067 -0.0831 -0.2000 -0.1714 278 LYS   B C     
10422 O  O     . LYS   B 253 ? 0.7928 1.1480 1.2058 -0.0975 -0.2128 -0.1786 278 LYS   B O     
10423 C  CB    . LYS   B 253 ? 0.8848 1.1588 1.2071 -0.0945 -0.2107 -0.1776 278 LYS   B CB    
10424 C  CG    . LYS   B 253 ? 0.8824 1.1537 1.2142 -0.1159 -0.2218 -0.1875 278 LYS   B CG    
10425 C  CD    . LYS   B 253 ? 0.8741 1.1497 1.2207 -0.1367 -0.2378 -0.1944 278 LYS   B CD    
10426 C  CE    . LYS   B 253 ? 0.8573 1.1494 1.2248 -0.1599 -0.2551 -0.1999 278 LYS   B CE    
10427 N  NZ    . LYS   B 253 ? 0.8412 1.1508 1.2252 -0.1784 -0.2682 -0.2020 278 LYS   B NZ    
10441 N  N     . LEU   B 254 ? 0.8386 1.1519 1.2158 -0.0680 -0.1758 -0.1665 279 LEU   B N     
10442 C  CA    . LEU   B 254 ? 0.8620 1.1475 1.2232 -0.0470 -0.1503 -0.1650 279 LEU   B CA    
10443 C  C     . LEU   B 254 ? 0.9308 1.1629 1.2372 -0.0167 -0.1264 -0.1649 279 LEU   B C     
10444 O  O     . LEU   B 254 ? 0.9366 1.1633 1.2387 -0.0040 -0.1221 -0.1638 279 LEU   B O     
10445 C  CB    . LEU   B 254 ? 0.8302 1.1282 1.2143 -0.0532 -0.1529 -0.1677 279 LEU   B CB    
10446 C  CG    . LEU   B 254 ? 0.7920 1.1108 1.2061 -0.0581 -0.1545 -0.1700 279 LEU   B CG    
10447 C  CD1   . LEU   B 254 ? 0.7703 1.1091 1.2036 -0.0589 -0.1549 -0.1693 279 LEU   B CD1   
10448 C  CD2   . LEU   B 254 ? 0.7863 1.1016 1.2029 -0.0586 -0.1540 -0.1718 279 LEU   B CD2   
10460 N  N     . ASP   B 255 ? 0.9941 1.1809 1.2481 -0.0038 -0.1124 -0.1671 280 ASP   B N     
10461 C  CA    . ASP   B 255 ? 1.0547 1.2029 1.2586 0.0031  -0.1062 -0.1677 280 ASP   B CA    
10462 C  C     . ASP   B 255 ? 1.0887 1.2292 1.2641 0.0233  -0.1078 -0.1610 280 ASP   B C     
10463 O  O     . ASP   B 255 ? 1.0790 1.2305 1.2629 0.0147  -0.1116 -0.1644 280 ASP   B O     
10464 C  CB    . ASP   B 255 ? 1.0724 1.2007 1.2628 -0.0078 -0.0994 -0.1729 280 ASP   B CB    
10465 C  CG    . ASP   B 255 ? 1.0863 1.2006 1.2664 -0.0117 -0.0905 -0.1761 280 ASP   B CG    
10466 O  OD1   . ASP   B 255 ? 1.0922 1.2024 1.2657 -0.0153 -0.0909 -0.1810 280 ASP   B OD1   
10467 O  OD2   . ASP   B 255 ? 1.0898 1.1999 1.2691 -0.0116 -0.0852 -0.1733 280 ASP   B OD2   
10472 N  N     . GLU   B 256 ? 1.1185 1.2501 1.2695 0.0493  -0.1103 -0.1506 281 GLU   B N     
10473 C  CA    . GLU   B 256 ? 1.1410 1.2661 1.2719 0.0632  -0.1179 -0.1419 281 GLU   B CA    
10474 C  C     . GLU   B 256 ? 1.1581 1.2734 1.2604 0.0459  -0.1205 -0.1380 281 GLU   B C     
10475 O  O     . GLU   B 256 ? 1.1604 1.2726 1.2633 0.0423  -0.1182 -0.1393 281 GLU   B O     
10476 C  CB    . GLU   B 256 ? 1.1459 1.2730 1.2831 0.0901  -0.1231 -0.1381 281 GLU   B CB    
10477 C  CG    . GLU   B 256 ? 1.1473 1.2791 1.2921 0.1127  -0.1297 -0.1347 281 GLU   B CG    
10478 C  CD    . GLU   B 256 ? 1.1468 1.2817 1.2984 0.1289  -0.1360 -0.1350 281 GLU   B CD    
10479 O  OE1   . GLU   B 256 ? 1.1504 1.2840 1.2999 0.1325  -0.1375 -0.1343 281 GLU   B OE1   
10480 O  OE2   . GLU   B 256 ? 1.1422 1.2800 1.3011 0.1386  -0.1395 -0.1363 281 GLU   B OE2   
10487 N  N     . THR   B 257 ? 1.1691 1.2792 1.2436 0.0314  -0.1271 -0.1313 282 THR   B N     
10488 C  CA    . THR   B 257 ? 1.1727 1.2804 1.2242 0.0201  -0.1374 -0.1235 282 THR   B CA    
10489 C  C     . THR   B 257 ? 1.1576 1.2644 1.1939 0.0138  -0.1493 -0.1208 282 THR   B C     
10490 O  O     . THR   B 257 ? 1.1589 1.2732 1.1936 0.0033  -0.1529 -0.1212 282 THR   B O     
10491 C  CB    . THR   B 257 ? 1.1880 1.2937 1.2323 0.0168  -0.1363 -0.1179 282 THR   B CB    
10492 O  OG1   . THR   B 257 ? 1.1958 1.2993 1.2362 0.0159  -0.1344 -0.1148 282 THR   B OG1   
10493 C  CG2   . THR   B 257 ? 1.1876 1.2971 1.2341 0.0157  -0.1377 -0.1166 282 THR   B CG2   
10501 N  N     . GLY   B 258 ? 1.1323 1.2345 1.1610 0.0205  -0.1589 -0.1163 283 GLY   B N     
10502 C  CA    . GLY   B 258 ? 1.0922 1.2008 1.1218 0.0263  -0.1704 -0.1117 283 GLY   B CA    
10503 C  C     . GLY   B 258 ? 1.0599 1.1632 1.0790 0.0331  -0.1794 -0.1056 283 GLY   B C     
10504 O  O     . GLY   B 258 ? 1.0690 1.1562 1.0795 0.0304  -0.1840 -0.1096 283 GLY   B O     
10508 N  N     . ASN   B 259 ? 1.0098 1.1274 1.0346 0.0414  -0.1808 -0.0946 284 ASN   B N     
10509 C  CA    . ASN   B 259 ? 0.9412 1.0861 0.9948 0.0375  -0.1761 -0.0829 284 ASN   B CA    
10510 C  C     . ASN   B 259 ? 0.9363 1.0423 0.9638 0.0506  -0.2101 -0.0899 284 ASN   B C     
10511 O  O     . ASN   B 259 ? 0.9455 1.0456 0.9634 0.0484  -0.2052 -0.0934 284 ASN   B O     
10512 C  CB    . ASN   B 259 ? 0.8816 1.0825 0.9914 0.0201  -0.1331 -0.0627 284 ASN   B CB    
10513 C  CG    . ASN   B 259 ? 0.8655 1.0770 0.9958 0.0151  -0.0958 -0.0459 284 ASN   B CG    
10514 O  OD1   . ASN   B 259 ? 0.8716 1.0756 0.9993 0.0167  -0.0860 -0.0429 284 ASN   B OD1   
10515 N  ND2   . ASN   B 259 ? 0.8613 1.0730 0.9975 0.0136  -0.0791 -0.0392 284 ASN   B ND2   
10522 N  N     . SER   B 260 ? 0.9032 0.9936 0.9346 0.0661  -0.2435 -0.0929 285 SER   B N     
10523 C  CA    . SER   B 260 ? 0.8680 0.9464 0.9096 0.0928  -0.2625 -0.0873 285 SER   B CA    
10524 C  C     . SER   B 260 ? 0.8078 0.8986 0.8664 0.0615  -0.3103 -0.0953 285 SER   B C     
10525 O  O     . SER   B 260 ? 0.8217 0.8954 0.8672 0.0535  -0.3174 -0.0984 285 SER   B O     
10526 C  CB    . SER   B 260 ? 0.8801 0.9395 0.9194 0.1393  -0.2477 -0.0795 285 SER   B CB    
10527 O  OG    . SER   B 260 ? 0.8907 0.9320 0.9200 0.1629  -0.2473 -0.0762 285 SER   B OG    
10533 N  N     . LEU   B 261 ? 0.7383 0.8552 0.8188 0.0501  -0.3459 -0.0964 286 LEU   B N     
10534 C  CA    . LEU   B 261 ? 0.6916 0.8158 0.7708 0.0427  -0.3714 -0.0967 286 LEU   B CA    
10535 C  C     . LEU   B 261 ? 0.6665 0.7651 0.7244 0.0364  -0.3806 -0.0877 286 LEU   B C     
10536 O  O     . LEU   B 261 ? 0.6609 0.7440 0.7140 0.0414  -0.3962 -0.0991 286 LEU   B O     
10537 C  CB    . LEU   B 261 ? 0.7056 0.8242 0.7736 0.0561  -0.3659 -0.0998 286 LEU   B CB    
10538 C  CG    . LEU   B 261 ? 0.7284 0.8394 0.7799 0.0578  -0.3584 -0.1014 286 LEU   B CG    
10539 C  CD1   . LEU   B 261 ? 0.7218 0.8382 0.7784 0.0518  -0.3705 -0.1105 286 LEU   B CD1   
10540 C  CD2   . LEU   B 261 ? 0.7445 0.8492 0.7887 0.0655  -0.3398 -0.0949 286 LEU   B CD2   
10552 N  N     . LYS   B 262 ? 0.6870 0.7377 0.6898 0.0292  -0.3570 -0.0688 287 LYS   B N     
10553 C  CA    . LYS   B 262 ? 0.6810 0.7114 0.6495 0.0233  -0.3372 -0.0545 287 LYS   B CA    
10554 C  C     . LYS   B 262 ? 0.5725 0.6358 0.6109 0.0197  -0.3448 -0.0432 287 LYS   B C     
10555 O  O     . LYS   B 262 ? 0.5701 0.6173 0.6182 0.0264  -0.3251 -0.0625 287 LYS   B O     
10556 C  CB    . LYS   B 262 ? 0.7575 0.7569 0.6457 0.0171  -0.3200 -0.0514 287 LYS   B CB    
10557 C  CG    . LYS   B 262 ? 0.8136 0.8028 0.6428 0.0000  -0.3041 -0.0517 287 LYS   B CG    
10558 C  CD    . LYS   B 262 ? 0.8389 0.8337 0.6355 -0.0174 -0.3040 -0.0485 287 LYS   B CD    
10559 C  CE    . LYS   B 262 ? 0.8433 0.8435 0.6244 -0.0328 -0.3175 -0.0480 287 LYS   B CE    
10560 N  NZ    . LYS   B 262 ? 0.8460 0.8505 0.6227 -0.0455 -0.3297 -0.0431 287 LYS   B NZ    
10574 N  N     . VAL   B 263 ? 0.4958 0.5883 0.5756 0.0127  -0.3180 -0.0080 288 VAL   B N     
10575 C  CA    . VAL   B 263 ? 0.4382 0.5514 0.5605 0.0171  -0.2871 0.0313  288 VAL   B CA    
10576 C  C     . VAL   B 263 ? 0.4198 0.4901 0.5287 0.0179  -0.2723 0.0346  288 VAL   B C     
10577 O  O     . VAL   B 263 ? 0.4069 0.4936 0.5475 0.0664  -0.2574 0.0531  288 VAL   B O     
10578 C  CB    . VAL   B 263 ? 0.3957 0.5706 0.5813 0.0085  -0.2467 0.0569  288 VAL   B CB    
10579 C  CG1   . VAL   B 263 ? 0.3840 0.5925 0.5849 0.0284  -0.2316 0.0682  288 VAL   B CG1   
10580 C  CG2   . VAL   B 263 ? 0.4029 0.5740 0.5968 0.0039  -0.2163 0.0770  288 VAL   B CG2   
10590 N  N     . ILE   B 264 ? 0.4518 0.4351 0.4780 -0.0382 -0.2685 0.0197  289 ILE   B N     
10591 C  CA    . ILE   B 264 ? 0.4789 0.4143 0.4567 -0.0557 -0.2452 0.0284  289 ILE   B CA    
10592 C  C     . ILE   B 264 ? 0.4318 0.3773 0.4449 -0.0094 -0.2329 0.0388  289 ILE   B C     
10593 O  O     . ILE   B 264 ? 0.4742 0.3763 0.4482 0.0622  -0.2323 0.0348  289 ILE   B O     
10594 C  CB    . ILE   B 264 ? 0.5447 0.4276 0.4622 -0.1016 -0.2377 0.0248  289 ILE   B CB    
10595 C  CG1   . ILE   B 264 ? 0.5921 0.4478 0.4786 -0.0720 -0.2389 0.0398  289 ILE   B CG1   
10596 C  CG2   . ILE   B 264 ? 0.5680 0.4276 0.4646 -0.1096 -0.2189 0.0303  289 ILE   B CG2   
10597 C  CD1   . ILE   B 264 ? 0.5975 0.4760 0.4891 -0.0331 -0.2508 0.0543  289 ILE   B CD1   
10609 N  N     . HIS   B 265 ? 0.3512 0.3685 0.4506 0.0069  -0.1980 0.0678  290 HIS   B N     
10610 C  CA    . HIS   B 265 ? 0.3500 0.3606 0.4705 0.0307  -0.1582 0.0619  290 HIS   B CA    
10611 C  C     . HIS   B 265 ? 0.3450 0.3602 0.4488 0.0344  -0.1785 0.0490  290 HIS   B C     
10612 O  O     . HIS   B 265 ? 0.3733 0.3830 0.4364 0.0178  -0.1918 0.0377  290 HIS   B O     
10613 C  CB    . HIS   B 265 ? 0.3670 0.3881 0.5059 0.0158  -0.1292 0.0717  290 HIS   B CB    
10614 C  CG    . HIS   B 265 ? 0.3910 0.4090 0.5305 0.0610  -0.1263 0.0834  290 HIS   B CG    
10615 N  ND1   . HIS   B 265 ? 0.4553 0.4627 0.5366 0.1073  -0.1321 0.0970  290 HIS   B ND1   
10616 C  CD2   . HIS   B 265 ? 0.3961 0.4073 0.5363 0.0503  -0.1270 0.0816  290 HIS   B CD2   
10617 C  CE1   . HIS   B 265 ? 0.4677 0.4769 0.5438 0.1004  -0.1390 0.0889  290 HIS   B CE1   
10618 N  NE2   . HIS   B 265 ? 0.4215 0.4326 0.5467 0.0857  -0.1371 0.0896  290 HIS   B NE2   
10626 N  N     . GLU   B 266 ? 0.3160 0.3425 0.4449 0.0636  -0.1773 0.0409  291 GLU   B N     
10627 C  CA    . GLU   B 266 ? 0.3153 0.3547 0.4438 0.0356  -0.1548 0.0443  291 GLU   B CA    
10628 C  C     . GLU   B 266 ? 0.2965 0.3451 0.4368 0.0412  -0.1484 0.0451  291 GLU   B C     
10629 O  O     . GLU   B 266 ? 0.2488 0.3332 0.4210 0.0289  -0.1365 0.0527  291 GLU   B O     
10630 C  CB    . GLU   B 266 ? 0.3208 0.3732 0.4498 0.0287  -0.1542 0.0427  291 GLU   B CB    
10631 C  CG    . GLU   B 266 ? 0.3428 0.3914 0.4518 -0.0123 -0.1683 0.0408  291 GLU   B CG    
10632 C  CD    . GLU   B 266 ? 0.4651 0.4338 0.4513 -0.0258 -0.1466 0.0468  291 GLU   B CD    
10633 O  OE1   . GLU   B 266 ? 0.5048 0.4525 0.4287 -0.0432 -0.1472 0.0532  291 GLU   B OE1   
10634 O  OE2   . GLU   B 266 ? 0.5177 0.4787 0.4670 -0.0359 -0.1477 0.0546  291 GLU   B OE2   
10641 N  N     . GLN   B 267 ? 0.2777 0.3617 0.4582 0.0224  -0.1493 0.0454  292 GLN   B N     
10642 C  CA    . GLN   B 267 ? 0.3219 0.3586 0.4730 0.0156  -0.1287 0.0444  292 GLN   B CA    
10643 C  C     . GLN   B 267 ? 0.3010 0.3228 0.4724 0.0170  -0.1524 0.0543  292 GLN   B C     
10644 O  O     . GLN   B 267 ? 0.3228 0.3018 0.4869 0.0242  -0.1419 0.0544  292 GLN   B O     
10645 C  CB    . GLN   B 267 ? 0.3740 0.4045 0.4958 0.0062  -0.0745 0.0333  292 GLN   B CB    
10646 C  CG    . GLN   B 267 ? 0.4095 0.4585 0.5123 0.0562  -0.0220 0.0374  292 GLN   B CG    
10647 C  CD    . GLN   B 267 ? 0.4851 0.5323 0.5382 0.0685  -0.0045 0.0584  292 GLN   B CD    
10648 O  OE1   . GLN   B 267 ? 0.5321 0.5745 0.5570 0.0781  0.0080  0.0635  292 GLN   B OE1   
10649 N  NE2   . GLN   B 267 ? 0.5006 0.5473 0.5435 0.0802  0.0065  0.0575  292 GLN   B NE2   
10658 N  N     . VAL   B 268 ? 0.2860 0.3294 0.4651 0.0392  -0.1586 0.0583  293 VAL   B N     
10659 C  CA    . VAL   B 268 ? 0.3110 0.3350 0.4600 0.0437  -0.1539 0.0373  293 VAL   B CA    
10660 C  C     . VAL   B 268 ? 0.3185 0.3236 0.4690 0.0518  -0.1384 0.0412  293 VAL   B C     
10661 O  O     . VAL   B 268 ? 0.3560 0.3088 0.4759 0.0496  -0.1429 0.0480  293 VAL   B O     
10662 C  CB    . VAL   B 268 ? 0.3175 0.3516 0.4410 0.0347  -0.1452 0.0151  293 VAL   B CB    
10663 C  CG1   . VAL   B 268 ? 0.3438 0.3572 0.4299 0.0299  -0.1339 0.0101  293 VAL   B CG1   
10664 C  CG2   . VAL   B 268 ? 0.3317 0.3565 0.4443 0.0352  -0.1517 0.0149  293 VAL   B CG2   
10674 N  N     . ASN   B 269 ? 0.3275 0.2869 0.4531 0.0798  -0.1250 0.0450  294 ASN   B N     
10675 C  CA    . ASN   B 269 ? 0.3278 0.3003 0.4555 0.0500  -0.1169 0.0424  294 ASN   B CA    
10676 C  C     . ASN   B 269 ? 0.2812 0.3136 0.4578 0.0556  -0.1201 0.0359  294 ASN   B C     
10677 O  O     . ASN   B 269 ? 0.2767 0.3105 0.4527 0.0533  -0.1025 0.0507  294 ASN   B O     
10678 C  CB    . ASN   B 269 ? 0.3109 0.2839 0.4499 0.0556  -0.1060 0.0435  294 ASN   B CB    
10679 C  CG    . ASN   B 269 ? 0.2710 0.2704 0.4474 0.0518  -0.0968 0.0351  294 ASN   B CG    
10680 O  OD1   . ASN   B 269 ? 0.2476 0.2686 0.4391 0.0652  -0.0963 0.0168  294 ASN   B OD1   
10681 N  ND2   . ASN   B 269 ? 0.3008 0.2870 0.4545 0.0235  -0.0841 0.0637  294 ASN   B ND2   
10688 N  N     . HIS   B 270 ? 0.2976 0.3071 0.4768 0.0844  -0.1017 0.0187  295 HIS   B N     
10689 C  CA    . HIS   B 270 ? 0.2822 0.3441 0.4870 0.0952  -0.0855 0.0156  295 HIS   B CA    
10690 C  C     . HIS   B 270 ? 0.2798 0.3184 0.4554 0.0712  -0.0536 0.0319  295 HIS   B C     
10691 O  O     . HIS   B 270 ? 0.2777 0.3607 0.4764 0.0760  -0.0316 0.0252  295 HIS   B O     
10692 C  CB    . HIS   B 270 ? 0.3394 0.4003 0.5270 0.0995  -0.0775 -0.0111 295 HIS   B CB    
10693 C  CG    . HIS   B 270 ? 0.4230 0.4430 0.5650 0.1106  -0.0685 -0.0238 295 HIS   B CG    
10694 N  ND1   . HIS   B 270 ? 0.4577 0.4677 0.5830 0.0820  -0.0701 -0.0293 295 HIS   B ND1   
10695 C  CD2   . HIS   B 270 ? 0.4614 0.4627 0.5798 0.1009  -0.0750 -0.0281 295 HIS   B CD2   
10696 C  CE1   . HIS   B 270 ? 0.4830 0.4709 0.5874 0.0763  -0.0763 -0.0271 295 HIS   B CE1   
10697 N  NE2   . HIS   B 270 ? 0.4835 0.4744 0.5890 0.0794  -0.0898 -0.0272 295 HIS   B NE2   
10705 N  N     . ARG   B 271 ? 0.2754 0.2629 0.4095 0.0592  -0.0564 0.0335  296 ARG   B N     
10706 C  CA    . ARG   B 271 ? 0.2313 0.2503 0.3735 0.0504  -0.0619 0.0167  296 ARG   B CA    
10707 C  C     . ARG   B 271 ? 0.2522 0.2556 0.3558 0.0296  -0.0867 0.0358  296 ARG   B C     
10708 O  O     . ARG   B 271 ? 0.2453 0.2438 0.3606 0.0218  -0.0822 0.0281  296 ARG   B O     
10709 C  CB    . ARG   B 271 ? 0.2520 0.2179 0.3698 0.0478  -0.0449 0.0070  296 ARG   B CB    
10710 C  CG    . ARG   B 271 ? 0.2915 0.2258 0.3871 0.0497  -0.0420 -0.0083 296 ARG   B CG    
10711 C  CD    . ARG   B 271 ? 0.3234 0.2549 0.3822 0.0471  -0.0537 -0.0236 296 ARG   B CD    
10712 N  NE    . ARG   B 271 ? 0.3365 0.2506 0.3972 0.0603  -0.0761 -0.0355 296 ARG   B NE    
10713 C  CZ    . ARG   B 271 ? 0.3548 0.2598 0.4213 0.0460  -0.0742 -0.0239 296 ARG   B CZ    
10714 N  NH1   . ARG   B 271 ? 0.2925 0.2400 0.4224 0.0448  -0.0828 -0.0064 296 ARG   B NH1   
10715 N  NH2   . ARG   B 271 ? 0.4398 0.3214 0.4478 0.0469  -0.0823 -0.0346 296 ARG   B NH2   
10729 N  N     . TRP   B 272 ? 0.2604 0.2806 0.3535 0.0352  -0.1000 0.0420  297 TRP   B N     
10730 C  CA    . TRP   B 272 ? 0.2462 0.2477 0.3416 0.0156  -0.0978 0.0464  297 TRP   B CA    
10731 C  C     . TRP   B 272 ? 0.2111 0.2754 0.3591 0.0073  -0.0863 0.0514  297 TRP   B C     
10732 O  O     . TRP   B 272 ? 0.2169 0.2967 0.3519 0.0238  -0.0817 0.0613  297 TRP   B O     
10733 C  CB    . TRP   B 272 ? 0.2439 0.2538 0.3284 0.0012  -0.0719 0.0380  297 TRP   B CB    
10734 C  CG    . TRP   B 272 ? 0.2316 0.2519 0.3103 0.0239  -0.0728 0.0453  297 TRP   B CG    
10735 C  CD1   . TRP   B 272 ? 0.2683 0.2476 0.3101 0.0437  -0.0541 0.0478  297 TRP   B CD1   
10736 C  CD2   . TRP   B 272 ? 0.2208 0.2374 0.3076 0.0253  -0.0590 0.0352  297 TRP   B CD2   
10737 N  NE1   . TRP   B 272 ? 0.2599 0.2381 0.3114 0.0269  -0.0801 0.0392  297 TRP   B NE1   
10738 C  CE2   . TRP   B 272 ? 0.2273 0.2415 0.3081 0.0427  -0.0645 0.0263  297 TRP   B CE2   
10739 C  CE3   . TRP   B 272 ? 0.1979 0.2517 0.3125 -0.0007 -0.0429 0.0171  297 TRP   B CE3   
10740 C  CZ2   . TRP   B 272 ? 0.2228 0.2470 0.3140 0.0183  -0.0446 0.0365  297 TRP   B CZ2   
10741 C  CZ3   . TRP   B 272 ? 0.2019 0.2526 0.3208 -0.0092 -0.0601 0.0390  297 TRP   B CZ3   
10742 C  CH2   . TRP   B 272 ? 0.1913 0.2354 0.3189 -0.0126 -0.0561 0.0269  297 TRP   B CH2   
10753 N  N     . GLU   B 273 ? 0.1935 0.2721 0.3710 -0.0081 -0.0916 0.0467  298 GLU   B N     
10754 C  CA    . GLU   B 273 ? 0.1898 0.2996 0.3794 0.0107  -0.0910 0.0310  298 GLU   B CA    
10755 C  C     . GLU   B 273 ? 0.1945 0.2998 0.3646 0.0504  -0.1007 0.0324  298 GLU   B C     
10756 O  O     . GLU   B 273 ? 0.2088 0.3063 0.3626 0.0491  -0.0753 0.0265  298 GLU   B O     
10757 C  CB    . GLU   B 273 ? 0.1665 0.3490 0.4130 0.0082  -0.0860 0.0290  298 GLU   B CB    
10758 C  CG    . GLU   B 273 ? 0.1748 0.4039 0.4428 0.0302  -0.0753 0.0333  298 GLU   B CG    
10759 C  CD    . GLU   B 273 ? 0.2298 0.4358 0.4680 0.0366  -0.0616 0.0470  298 GLU   B CD    
10760 O  OE1   . GLU   B 273 ? 0.2054 0.4356 0.4894 0.0515  -0.0487 0.0682  298 GLU   B OE1   
10761 O  OE2   . GLU   B 273 ? 0.2963 0.4595 0.4654 0.0395  -0.0751 0.0426  298 GLU   B OE2   
10768 N  N     . VAL   B 274 ? 0.1955 0.3252 0.3691 0.0387  -0.1163 0.0338  299 VAL   B N     
10769 C  CA    . VAL   B 274 ? 0.2153 0.3185 0.3680 0.0077  -0.1178 0.0427  299 VAL   B CA    
10770 C  C     . VAL   B 274 ? 0.2497 0.3111 0.3816 -0.0197 -0.1395 0.0418  299 VAL   B C     
10771 O  O     . VAL   B 274 ? 0.2512 0.3174 0.3920 -0.0200 -0.1430 0.0506  299 VAL   B O     
10772 C  CB    . VAL   B 274 ? 0.2277 0.3533 0.3744 0.0034  -0.1111 0.0383  299 VAL   B CB    
10773 C  CG1   . VAL   B 274 ? 0.2434 0.3652 0.3753 -0.0102 -0.1055 0.0528  299 VAL   B CG1   
10774 C  CG2   . VAL   B 274 ? 0.2522 0.3554 0.3732 -0.0040 -0.1026 0.0292  299 VAL   B CG2   
10784 N  N     . CYS   B 275 ? 0.2987 0.3103 0.3891 0.0268  -0.1531 0.0281  300 CYS   B N     
10785 C  CA    . CYS   B 275 ? 0.3004 0.3313 0.4043 0.0200  -0.1629 0.0208  300 CYS   B CA    
10786 C  C     . CYS   B 275 ? 0.3127 0.3328 0.3742 0.0588  -0.1564 0.0237  300 CYS   B C     
10787 O  O     . CYS   B 275 ? 0.2991 0.3537 0.3742 0.0547  -0.1427 0.0184  300 CYS   B O     
10788 C  CB    . CYS   B 275 ? 0.2942 0.3687 0.4661 0.0176  -0.1452 0.0201  300 CYS   B CB    
10789 S  SG    . CYS   B 275 ? 0.3110 0.4067 0.5275 0.0189  -0.1318 0.0160  300 CYS   B SG    
10795 N  N     . LEU   B 276 ? 0.3325 0.3535 0.3649 0.0430  -0.1569 0.0028  301 LEU   B N     
10796 C  CA    . LEU   B 276 ? 0.3207 0.3809 0.3720 0.0331  -0.1754 0.0289  301 LEU   B CA    
10797 C  C     . LEU   B 276 ? 0.3083 0.3810 0.3694 0.0125  -0.1893 0.0228  301 LEU   B C     
10798 O  O     . LEU   B 276 ? 0.3181 0.3825 0.3724 -0.0001 -0.1980 0.0270  301 LEU   B O     
10799 C  CB    . LEU   B 276 ? 0.3177 0.4033 0.3965 0.0163  -0.1449 0.0405  301 LEU   B CB    
10800 C  CG    . LEU   B 276 ? 0.3470 0.4287 0.4230 0.0040  -0.1170 0.0446  301 LEU   B CG    
10801 C  CD1   . LEU   B 276 ? 0.2891 0.4414 0.4339 0.0331  -0.1211 0.0483  301 LEU   B CD1   
10802 C  CD2   . LEU   B 276 ? 0.4081 0.4427 0.4357 -0.0190 -0.0856 0.0323  301 LEU   B CD2   
10814 N  N     . THR   B 277 ? 0.3411 0.3820 0.3644 0.0283  -0.1837 0.0151  302 THR   B N     
10815 C  CA    . THR   B 277 ? 0.3880 0.4008 0.3577 -0.0008 -0.2052 0.0022  302 THR   B CA    
10816 C  C     . THR   B 277 ? 0.4414 0.4168 0.3395 0.0071  -0.2103 -0.0109 302 THR   B C     
10817 O  O     . THR   B 277 ? 0.4543 0.3999 0.3250 0.0302  -0.2061 -0.0145 302 THR   B O     
10818 C  CB    . THR   B 277 ? 0.3943 0.4347 0.3935 0.0209  -0.1917 0.0138  302 THR   B CB    
10819 O  OG1   . THR   B 277 ? 0.3890 0.4559 0.4182 0.0591  -0.1948 0.0158  302 THR   B OG1   
10820 C  CG2   . THR   B 277 ? 0.3915 0.4308 0.4125 0.0204  -0.1637 0.0201  302 THR   B CG2   
10828 N  N     . MET   B 278 ? 0.5226 0.4718 0.3559 -0.0021 -0.1947 -0.0256 303 MET   B N     
10829 C  CA    . MET   B 278 ? 0.5749 0.5276 0.3656 0.0184  -0.1836 -0.0260 303 MET   B CA    
10830 C  C     . MET   B 278 ? 0.4961 0.4943 0.3609 0.0217  -0.1657 -0.0452 303 MET   B C     
10831 O  O     . MET   B 278 ? 0.4997 0.4968 0.3861 0.0435  -0.1735 -0.0559 303 MET   B O     
10832 C  CB    . MET   B 278 ? 0.7051 0.6136 0.3815 0.0230  -0.1939 -0.0001 303 MET   B CB    
10833 C  CG    . MET   B 278 ? 0.8503 0.7072 0.4066 0.0266  -0.1754 0.0188  303 MET   B CG    
10834 S  SD    . MET   B 278 ? 0.9975 0.7864 0.4577 0.0252  -0.1380 0.0438  303 MET   B SD    
10835 C  CE    . MET   B 278 ? 1.0301 0.8010 0.4814 0.0245  -0.1147 0.0483  303 MET   B CE    
10845 N  N     . SER   B 279 ? 0.4251 0.4608 0.3471 0.0317  -0.1481 -0.0500 304 SER   B N     
10846 C  CA    . SER   B 279 ? 0.4281 0.4476 0.3583 0.0250  -0.1412 -0.0500 304 SER   B CA    
10847 C  C     . SER   B 279 ? 0.4588 0.4658 0.3875 0.0310  -0.1405 -0.0550 304 SER   B C     
10848 O  O     . SER   B 279 ? 0.4811 0.4741 0.3631 0.0147  -0.1296 -0.0551 304 SER   B O     
10849 C  CB    . SER   B 279 ? 0.4069 0.4088 0.3538 0.0108  -0.1187 -0.0431 304 SER   B CB    
10850 O  OG    . SER   B 279 ? 0.4347 0.3792 0.3475 0.0092  -0.0866 -0.0292 304 SER   B OG    
10856 N  N     . GLU   B 280 ? 0.4631 0.4636 0.4346 0.0241  -0.1453 -0.0663 305 GLU   B N     
10857 C  CA    . GLU   B 280 ? 0.5016 0.4831 0.4757 0.0233  -0.1435 -0.0836 305 GLU   B CA    
10858 C  C     . GLU   B 280 ? 0.4873 0.4716 0.4702 0.0292  -0.1058 -0.0776 305 GLU   B C     
10859 O  O     . GLU   B 280 ? 0.5307 0.4566 0.4848 0.0529  -0.1077 -0.0992 305 GLU   B O     
10860 C  CB    . GLU   B 280 ? 0.5914 0.5273 0.5284 0.0245  -0.1441 -0.0954 305 GLU   B CB    
10861 C  CG    . GLU   B 280 ? 0.7193 0.5842 0.5806 0.0225  -0.1140 -0.0992 305 GLU   B CG    
10862 C  CD    . GLU   B 280 ? 0.8386 0.6423 0.6296 0.0283  -0.0856 -0.1045 305 GLU   B CD    
10863 O  OE1   . GLU   B 280 ? 0.8894 0.6680 0.6492 0.0216  -0.0816 -0.1113 305 GLU   B OE1   
10864 O  OE2   . GLU   B 280 ? 0.8911 0.6669 0.6490 0.0241  -0.0715 -0.0998 305 GLU   B OE2   
10871 N  N     . LYS   B 281 ? 0.4423 0.4725 0.4440 0.0127  -0.0792 -0.0430 306 LYS   B N     
10872 C  CA    . LYS   B 281 ? 0.4298 0.4850 0.4177 0.0279  -0.0385 -0.0221 306 LYS   B CA    
10873 C  C     . LYS   B 281 ? 0.3938 0.4329 0.3599 0.0576  -0.0305 -0.0230 306 LYS   B C     
10874 O  O     . LYS   B 281 ? 0.4242 0.4199 0.3468 0.0470  -0.0347 -0.0069 306 LYS   B O     
10875 C  CB    . LYS   B 281 ? 0.4530 0.5480 0.4532 -0.0084 -0.0013 -0.0002 306 LYS   B CB    
10876 C  CG    . LYS   B 281 ? 0.5169 0.6013 0.4883 -0.0343 0.0163  0.0017  306 LYS   B CG    
10877 C  CD    . LYS   B 281 ? 0.5566 0.6425 0.5228 -0.0697 0.0297  -0.0041 306 LYS   B CD    
10878 C  CE    . LYS   B 281 ? 0.5951 0.6719 0.5490 -0.1027 0.0458  -0.0179 306 LYS   B CE    
10879 N  NZ    . LYS   B 281 ? 0.6363 0.6946 0.5605 -0.1341 0.0436  -0.0279 306 LYS   B NZ    
10893 N  N     . GLY   B 282 ? 0.3731 0.4069 0.3237 0.0426  -0.0557 -0.0299 307 GLY   B N     
10894 C  CA    . GLY   B 282 ? 0.3311 0.3952 0.2992 0.0589  -0.0463 -0.0248 307 GLY   B CA    
10895 C  C     . GLY   B 282 ? 0.2863 0.4056 0.2663 0.0389  -0.0411 -0.0328 307 GLY   B C     
10896 O  O     . GLY   B 282 ? 0.2902 0.4104 0.2745 0.0479  -0.0143 -0.0206 307 GLY   B O     
10900 N  N     . PHE   B 283 ? 0.2974 0.3762 0.2411 0.0255  -0.0321 -0.0231 308 PHE   B N     
10901 C  CA    . PHE   B 283 ? 0.2928 0.3830 0.2364 0.0432  -0.0195 -0.0230 308 PHE   B CA    
10902 C  C     . PHE   B 283 ? 0.3117 0.3524 0.2440 0.0671  -0.0164 -0.0047 308 PHE   B C     
10903 O  O     . PHE   B 283 ? 0.3566 0.3564 0.2605 0.0470  -0.0324 -0.0014 308 PHE   B O     
10904 C  CB    . PHE   B 283 ? 0.2762 0.4165 0.2337 0.0446  -0.0289 -0.0166 308 PHE   B CB    
10905 C  CG    . PHE   B 283 ? 0.2577 0.4058 0.2242 0.0550  -0.0392 -0.0278 308 PHE   B CG    
10906 C  CD1   . PHE   B 283 ? 0.2904 0.3857 0.2329 0.0680  -0.0265 -0.0474 308 PHE   B CD1   
10907 C  CD2   . PHE   B 283 ? 0.2633 0.4134 0.2371 0.0401  -0.0463 -0.0290 308 PHE   B CD2   
10908 C  CE1   . PHE   B 283 ? 0.2970 0.3637 0.2492 0.0496  -0.0407 -0.0326 308 PHE   B CE1   
10909 C  CE2   . PHE   B 283 ? 0.2440 0.3938 0.2450 0.0487  -0.0552 -0.0167 308 PHE   B CE2   
10910 C  CZ    . PHE   B 283 ? 0.2381 0.3572 0.2520 0.0440  -0.0535 -0.0281 308 PHE   B CZ    
10920 N  N     . GLN   B 284 ? 0.3007 0.3451 0.2551 0.0533  -0.0208 -0.0044 309 GLN   B N     
10921 C  CA    . GLN   B 284 ? 0.2608 0.3293 0.2819 0.0186  -0.0526 -0.0218 309 GLN   B CA    
10922 C  C     . GLN   B 284 ? 0.2484 0.3120 0.2621 0.0043  -0.0554 -0.0031 309 GLN   B C     
10923 O  O     . GLN   B 284 ? 0.2796 0.3221 0.2545 0.0084  -0.0538 -0.0023 309 GLN   B O     
10924 C  CB    . GLN   B 284 ? 0.2865 0.3556 0.3208 0.0099  -0.0841 -0.0342 309 GLN   B CB    
10925 C  CG    . GLN   B 284 ? 0.3132 0.3802 0.3395 -0.0120 -0.0552 -0.0324 309 GLN   B CG    
10926 C  CD    . GLN   B 284 ? 0.3184 0.3964 0.3470 -0.0178 -0.0731 -0.0314 309 GLN   B CD    
10927 O  OE1   . GLN   B 284 ? 0.3277 0.4068 0.3635 -0.0100 -0.0749 -0.0369 309 GLN   B OE1   
10928 N  NE2   . GLN   B 284 ? 0.3244 0.4108 0.3394 0.0059  -0.0686 -0.0109 309 GLN   B NE2   
10937 N  N     . GLN   B 285 ? 0.2391 0.2747 0.2419 0.0319  -0.0552 -0.0088 310 GLN   B N     
10938 C  CA    . GLN   B 285 ? 0.2260 0.2588 0.2403 0.0152  -0.0543 -0.0036 310 GLN   B CA    
10939 C  C     . GLN   B 285 ? 0.1997 0.2677 0.2622 0.0390  -0.0620 0.0015  310 GLN   B C     
10940 O  O     . GLN   B 285 ? 0.1670 0.3082 0.2845 0.0249  -0.0652 -0.0011 310 GLN   B O     
10941 C  CB    . GLN   B 285 ? 0.2228 0.2827 0.2218 0.0140  -0.0414 -0.0080 310 GLN   B CB    
10942 C  CG    . GLN   B 285 ? 0.2041 0.3072 0.2258 0.0091  -0.0160 -0.0015 310 GLN   B CG    
10943 C  CD    . GLN   B 285 ? 0.1798 0.2961 0.2398 -0.0083 -0.0266 -0.0037 310 GLN   B CD    
10944 O  OE1   . GLN   B 285 ? 0.2066 0.3072 0.2615 0.0073  -0.0261 -0.0123 310 GLN   B OE1   
10945 N  NE2   . GLN   B 285 ? 0.1597 0.3029 0.2426 -0.0285 -0.0424 0.0195  310 GLN   B NE2   
10954 N  N     . ILE   B 286 ? 0.1917 0.2758 0.2640 0.0023  -0.0711 -0.0016 311 ILE   B N     
10955 C  CA    . ILE   B 286 ? 0.1795 0.2743 0.2782 0.0147  -0.0581 -0.0067 311 ILE   B CA    
10956 C  C     . ILE   B 286 ? 0.1788 0.2845 0.2647 -0.0028 -0.0423 0.0196  311 ILE   B C     
10957 O  O     . ILE   B 286 ? 0.2151 0.3007 0.2660 -0.0214 -0.0441 0.0376  311 ILE   B O     
10958 C  CB    . ILE   B 286 ? 0.1749 0.3017 0.3040 0.0052  -0.0354 -0.0444 311 ILE   B CB    
10959 C  CG1   . ILE   B 286 ? 0.2102 0.3412 0.3198 -0.0083 -0.0223 -0.0833 311 ILE   B CG1   
10960 C  CG2   . ILE   B 286 ? 0.1711 0.2914 0.3133 -0.0251 -0.0353 -0.0328 311 ILE   B CG2   
10961 C  CD1   . ILE   B 286 ? 0.2760 0.3767 0.3317 0.0029  -0.0485 -0.0789 311 ILE   B CD1   
10973 N  N     . SER   B 287 ? 0.1921 0.2295 0.2438 -0.0104 -0.0320 0.0043  312 SER   B N     
10974 C  CA    . SER   B 287 ? 0.1657 0.2420 0.2420 -0.0154 -0.0261 0.0043  312 SER   B CA    
10975 C  C     . SER   B 287 ? 0.1181 0.2433 0.2607 0.0018  -0.0146 -0.0006 312 SER   B C     
10976 O  O     . SER   B 287 ? 0.1435 0.2574 0.2648 0.0154  -0.0206 0.0093  312 SER   B O     
10977 C  CB    . SER   B 287 ? 0.1724 0.2468 0.2310 0.0112  -0.0283 -0.0010 312 SER   B CB    
10978 O  OG    . SER   B 287 ? 0.1872 0.2802 0.2380 0.0087  -0.0347 0.0152  312 SER   B OG    
10984 N  N     . PHE   B 288 ? 0.1685 0.2374 0.2680 0.0047  0.0032  -0.0008 313 PHE   B N     
10985 C  CA    . PHE   B 288 ? 0.1465 0.2444 0.2685 0.0055  0.0091  0.0121  313 PHE   B CA    
10986 C  C     . PHE   B 288 ? 0.1451 0.2341 0.2645 -0.0012 0.0112  0.0133  313 PHE   B C     
10987 O  O     . PHE   B 288 ? 0.2164 0.2425 0.2722 -0.0012 -0.0168 0.0051  313 PHE   B O     
10988 C  CB    . PHE   B 288 ? 0.1637 0.2521 0.3197 0.0138  0.0040  0.0152  313 PHE   B CB    
10989 C  CG    . PHE   B 288 ? 0.1559 0.2743 0.3469 0.0190  -0.0239 0.0032  313 PHE   B CG    
10990 C  CD1   . PHE   B 288 ? 0.1429 0.2844 0.3620 0.0258  -0.0023 0.0116  313 PHE   B CD1   
10991 C  CD2   . PHE   B 288 ? 0.1678 0.2975 0.3741 0.0252  -0.0272 -0.0022 313 PHE   B CD2   
10992 C  CE1   . PHE   B 288 ? 0.1066 0.2764 0.3729 0.0103  -0.0071 0.0199  313 PHE   B CE1   
10993 C  CE2   . PHE   B 288 ? 0.1843 0.3046 0.3805 -0.0008 -0.0135 -0.0084 313 PHE   B CE2   
10994 C  CZ    . PHE   B 288 ? 0.1470 0.2830 0.3830 -0.0045 -0.0253 0.0024  313 PHE   B CZ    
11004 N  N     . VAL   B 289 ? 0.1707 0.1949 0.2411 0.0284  0.0005  -0.0002 314 VAL   B N     
11005 C  CA    . VAL   B 289 ? 0.1385 0.2091 0.2668 0.0289  -0.0019 -0.0043 314 VAL   B CA    
11006 C  C     . VAL   B 289 ? 0.1429 0.1851 0.2982 0.0296  -0.0101 -0.0165 314 VAL   B C     
11007 O  O     . VAL   B 289 ? 0.1743 0.1920 0.2966 0.0195  -0.0063 0.0013  314 VAL   B O     
11008 C  CB    . VAL   B 289 ? 0.1504 0.2355 0.2631 0.0089  0.0062  -0.0028 314 VAL   B CB    
11009 C  CG1   . VAL   B 289 ? 0.1509 0.2267 0.2853 0.0117  0.0146  0.0043  314 VAL   B CG1   
11010 C  CG2   . VAL   B 289 ? 0.1944 0.2545 0.2621 0.0090  0.0195  0.0086  314 VAL   B CG2   
11020 N  N     . ASN   B 290 ? 0.1605 0.1833 0.3142 0.0483  0.0206  -0.0138 315 ASN   B N     
11021 C  CA    . ASN   B 290 ? 0.1957 0.1894 0.3053 0.0157  0.0366  -0.0181 315 ASN   B CA    
11022 C  C     . ASN   B 290 ? 0.2167 0.1972 0.3078 0.0188  0.0629  -0.0024 315 ASN   B C     
11023 O  O     . ASN   B 290 ? 0.2094 0.2083 0.3054 -0.0068 0.0670  0.0103  315 ASN   B O     
11024 C  CB    . ASN   B 290 ? 0.2108 0.1984 0.2849 0.0073  0.0275  -0.0083 315 ASN   B CB    
11025 C  CG    . ASN   B 290 ? 0.2145 0.1987 0.2633 0.0189  0.0013  -0.0076 315 ASN   B CG    
11026 O  OD1   . ASN   B 290 ? 0.1913 0.2298 0.2703 0.0141  0.0028  0.0125  315 ASN   B OD1   
11027 N  ND2   . ASN   B 290 ? 0.2047 0.2039 0.2646 0.0162  0.0164  -0.0055 315 ASN   B ND2   
11034 N  N     . SER   B 291 ? 0.2163 0.2074 0.3230 0.0378  0.0572  -0.0095 316 SER   B N     
11035 C  CA    . SER   B 291 ? 0.2042 0.2151 0.3521 0.0367  0.0527  -0.0072 316 SER   B CA    
11036 C  C     . SER   B 291 ? 0.1576 0.2294 0.3326 0.0097  0.0443  0.0065  316 SER   B C     
11037 O  O     . SER   B 291 ? 0.1713 0.2263 0.3667 -0.0032 0.0352  0.0196  316 SER   B O     
11038 C  CB    . SER   B 291 ? 0.2016 0.2549 0.4025 0.0380  0.0435  -0.0065 316 SER   B CB    
11039 O  OG    . SER   B 291 ? 0.1738 0.2873 0.4324 0.0360  0.0449  -0.0190 316 SER   B OG    
11045 N  N     . ILE   B 292 ? 0.1596 0.2327 0.3097 0.0292  0.0191  -0.0084 317 ILE   B N     
11046 C  CA    . ILE   B 292 ? 0.1440 0.2315 0.2737 0.0125  -0.0063 0.0129  317 ILE   B CA    
11047 C  C     . ILE   B 292 ? 0.1582 0.2256 0.2711 0.0090  0.0135  0.0028  317 ILE   B C     
11048 O  O     . ILE   B 292 ? 0.1870 0.2295 0.2682 -0.0037 0.0178  0.0139  317 ILE   B O     
11049 C  CB    . ILE   B 292 ? 0.1432 0.2149 0.2451 0.0126  -0.0173 -0.0027 317 ILE   B CB    
11050 C  CG1   . ILE   B 292 ? 0.2101 0.2262 0.2374 -0.0078 -0.0136 -0.0211 317 ILE   B CG1   
11051 C  CG2   . ILE   B 292 ? 0.1453 0.2089 0.2555 0.0438  -0.0043 0.0229  317 ILE   B CG2   
11052 C  CD1   . ILE   B 292 ? 0.2499 0.2181 0.2524 0.0176  -0.0101 -0.0258 317 ILE   B CD1   
11064 N  N     . ALA   B 293 ? 0.1443 0.2246 0.2677 -0.0193 0.0291  -0.0099 318 ALA   B N     
11065 C  CA    . ALA   B 293 ? 0.1327 0.2198 0.2745 -0.0112 0.0212  -0.0056 318 ALA   B CA    
11066 C  C     . ALA   B 293 ? 0.1533 0.2220 0.2643 -0.0057 0.0094  -0.0167 318 ALA   B C     
11067 O  O     . ALA   B 293 ? 0.1654 0.2367 0.2750 0.0108  0.0036  -0.0014 318 ALA   B O     
11068 C  CB    . ALA   B 293 ? 0.1295 0.2333 0.2836 0.0072  0.0124  -0.0171 318 ALA   B CB    
11074 N  N     . THR   B 294 ? 0.0835 0.2304 0.2423 0.0192  0.0085  -0.0151 319 THR   B N     
11075 C  CA    . THR   B 294 ? 0.1008 0.2165 0.2295 0.0124  -0.0044 -0.0186 319 THR   B CA    
11076 C  C     . THR   B 294 ? 0.1296 0.2178 0.2136 -0.0016 0.0215  -0.0110 319 THR   B C     
11077 O  O     . THR   B 294 ? 0.1295 0.2412 0.2332 0.0083  0.0122  -0.0054 319 THR   B O     
11078 C  CB    . THR   B 294 ? 0.1266 0.2160 0.2395 -0.0151 -0.0240 0.0007  319 THR   B CB    
11079 O  OG1   . THR   B 294 ? 0.1500 0.2364 0.2529 0.0097  -0.0188 0.0121  319 THR   B OG1   
11080 C  CG2   . THR   B 294 ? 0.1651 0.2105 0.2483 -0.0242 -0.0287 -0.0053 319 THR   B CG2   
11088 N  N     . SER   B 295 ? 0.1298 0.2373 0.2149 -0.0131 0.0051  -0.0105 320 SER   B N     
11089 C  CA    . SER   B 295 ? 0.1494 0.2252 0.2424 -0.0188 0.0079  -0.0076 320 SER   B CA    
11090 C  C     . SER   B 295 ? 0.1643 0.2395 0.2405 -0.0057 0.0058  -0.0203 320 SER   B C     
11091 O  O     . SER   B 295 ? 0.1921 0.2739 0.2404 -0.0314 -0.0133 -0.0441 320 SER   B O     
11092 C  CB    . SER   B 295 ? 0.2089 0.2518 0.2682 -0.0464 0.0024  0.0147  320 SER   B CB    
11093 O  OG    . SER   B 295 ? 0.2961 0.2748 0.2890 -0.0635 -0.0188 0.0295  320 SER   B OG    
11099 N  N     . LYS   B 296 ? 0.1303 0.2489 0.2397 0.0045  0.0215  -0.0019 321 LYS   B N     
11100 C  CA    . LYS   B 296 ? 0.1307 0.2508 0.2611 -0.0067 0.0327  -0.0079 321 LYS   B CA    
11101 C  C     . LYS   B 296 ? 0.1750 0.2807 0.2690 0.0172  0.0588  0.0023  321 LYS   B C     
11102 O  O     . LYS   B 296 ? 0.2525 0.3316 0.3347 0.0294  0.0876  0.0476  321 LYS   B O     
11103 C  CB    . LYS   B 296 ? 0.1682 0.2486 0.2641 0.0133  0.0247  0.0046  321 LYS   B CB    
11104 C  CG    . LYS   B 296 ? 0.2222 0.2836 0.2912 0.0050  0.0354  0.0234  321 LYS   B CG    
11105 C  CD    . LYS   B 296 ? 0.3091 0.3388 0.3421 0.0224  0.0210  0.0413  321 LYS   B CD    
11106 C  CE    . LYS   B 296 ? 0.4207 0.4017 0.3885 -0.0023 0.0261  0.0232  321 LYS   B CE    
11107 N  NZ    . LYS   B 296 ? 0.5010 0.4152 0.4180 -0.0079 0.0224  0.0051  321 LYS   B NZ    
11121 N  N     . GLY   B 297 ? 0.1746 0.2724 0.2364 -0.0148 0.0260  -0.0079 322 GLY   B N     
11122 C  CA    . GLY   B 297 ? 0.1406 0.2754 0.2181 -0.0113 -0.0037 -0.0143 322 GLY   B CA    
11123 C  C     . GLY   B 297 ? 0.1364 0.2575 0.2211 -0.0142 -0.0198 -0.0119 322 GLY   B C     
11124 O  O     . GLY   B 297 ? 0.1538 0.2366 0.2211 0.0089  -0.0031 0.0067  322 GLY   B O     
11128 N  N     . GLY   B 298 ? 0.1645 0.2592 0.2181 -0.0338 -0.0086 0.0073  323 GLY   B N     
11129 C  CA    . GLY   B 298 ? 0.1858 0.2472 0.2229 -0.0440 -0.0455 0.0329  323 GLY   B CA    
11130 C  C     . GLY   B 298 ? 0.1922 0.2640 0.2184 -0.0199 -0.0292 0.0353  323 GLY   B C     
11131 O  O     . GLY   B 298 ? 0.2084 0.2668 0.2360 -0.0251 -0.0455 0.0318  323 GLY   B O     
11135 N  N     . ARG   B 299 ? 0.1804 0.2658 0.2048 -0.0386 -0.0174 0.0243  324 ARG   B N     
11136 C  CA    . ARG   B 299 ? 0.1881 0.2582 0.2186 -0.0637 -0.0360 0.0385  324 ARG   B CA    
11137 C  C     . ARG   B 299 ? 0.1925 0.2560 0.2262 -0.0504 -0.0366 0.0589  324 ARG   B C     
11138 O  O     . ARG   B 299 ? 0.2381 0.2824 0.2363 -0.0592 -0.0389 0.0715  324 ARG   B O     
11139 C  CB    . ARG   B 299 ? 0.2018 0.2821 0.2463 -0.0625 -0.0368 0.0570  324 ARG   B CB    
11140 C  CG    . ARG   B 299 ? 0.2043 0.3007 0.2770 -0.0383 -0.0163 0.0553  324 ARG   B CG    
11141 C  CD    . ARG   B 299 ? 0.1788 0.3523 0.3076 -0.0139 -0.0473 0.0737  324 ARG   B CD    
11142 N  NE    . ARG   B 299 ? 0.1624 0.3770 0.3471 -0.0083 -0.0373 0.0611  324 ARG   B NE    
11143 C  CZ    . ARG   B 299 ? 0.1755 0.4125 0.3701 0.0112  -0.0270 0.0515  324 ARG   B CZ    
11144 N  NH1   . ARG   B 299 ? 0.2180 0.4188 0.3741 0.0332  -0.0035 0.0551  324 ARG   B NH1   
11145 N  NH2   . ARG   B 299 ? 0.1918 0.4459 0.3904 0.0019  -0.0362 0.0504  324 ARG   B NH2   
11159 N  N     . HIS   B 300 ? 0.1977 0.2446 0.2330 -0.0380 -0.0548 0.0619  325 HIS   B N     
11160 C  CA    . HIS   B 300 ? 0.2322 0.2540 0.2446 -0.0457 -0.0539 0.0490  325 HIS   B CA    
11161 C  C     . HIS   B 300 ? 0.2416 0.2709 0.2583 -0.0356 -0.0566 0.0386  325 HIS   B C     
11162 O  O     . HIS   B 300 ? 0.2517 0.2791 0.2741 -0.0207 -0.0511 0.0380  325 HIS   B O     
11163 C  CB    . HIS   B 300 ? 0.1925 0.2478 0.2484 -0.0340 -0.0352 0.0531  325 HIS   B CB    
11164 C  CG    . HIS   B 300 ? 0.1685 0.2450 0.2268 -0.0020 -0.0311 0.0360  325 HIS   B CG    
11165 N  ND1   . HIS   B 300 ? 0.1681 0.2482 0.2274 0.0007  -0.0381 0.0391  325 HIS   B ND1   
11166 C  CD2   . HIS   B 300 ? 0.1847 0.2360 0.2252 0.0296  -0.0075 0.0279  325 HIS   B CD2   
11167 C  CE1   . HIS   B 300 ? 0.1945 0.2393 0.2432 0.0401  -0.0119 0.0188  325 HIS   B CE1   
11168 N  NE2   . HIS   B 300 ? 0.1816 0.2236 0.2364 0.0305  -0.0049 0.0206  325 HIS   B NE2   
11176 N  N     . VAL   B 301 ? 0.2175 0.2767 0.2402 -0.0135 -0.0417 0.0250  326 VAL   B N     
11177 C  CA    . VAL   B 301 ? 0.2054 0.2883 0.2404 0.0009  -0.0434 0.0232  326 VAL   B CA    
11178 C  C     . VAL   B 301 ? 0.1924 0.3264 0.2174 -0.0073 -0.0467 0.0275  326 VAL   B C     
11179 O  O     . VAL   B 301 ? 0.2166 0.3446 0.2107 -0.0120 -0.0402 0.0394  326 VAL   B O     
11180 C  CB    . VAL   B 301 ? 0.2122 0.3304 0.2536 -0.0015 -0.0230 0.0273  326 VAL   B CB    
11181 C  CG1   . VAL   B 301 ? 0.1904 0.3524 0.2558 -0.0165 -0.0348 0.0249  326 VAL   B CG1   
11182 C  CG2   . VAL   B 301 ? 0.2382 0.3486 0.2664 -0.0009 -0.0229 0.0205  326 VAL   B CG2   
11192 N  N     . ASP   B 302 ? 0.1745 0.3436 0.2212 -0.0208 -0.0189 0.0344  327 ASP   B N     
11193 C  CA    . ASP   B 302 ? 0.1962 0.3532 0.2329 -0.0281 -0.0132 0.0599  327 ASP   B CA    
11194 C  C     . ASP   B 302 ? 0.2244 0.3686 0.2319 -0.0423 -0.0346 0.0670  327 ASP   B C     
11195 O  O     . ASP   B 302 ? 0.2343 0.3919 0.2350 -0.0534 -0.0440 0.0781  327 ASP   B O     
11196 C  CB    . ASP   B 302 ? 0.2052 0.3791 0.2595 -0.0084 -0.0280 0.0529  327 ASP   B CB    
11197 C  CG    . ASP   B 302 ? 0.2273 0.3864 0.2937 -0.0133 -0.0407 0.0475  327 ASP   B CG    
11198 O  OD1   . ASP   B 302 ? 0.3105 0.3744 0.3086 0.0133  -0.0235 0.0237  327 ASP   B OD1   
11199 O  OD2   . ASP   B 302 ? 0.2403 0.4060 0.3233 -0.0172 -0.0629 0.0695  327 ASP   B OD2   
11204 N  N     . TYR   B 303 ? 0.2647 0.3380 0.2491 -0.0482 -0.0447 0.0694  328 TYR   B N     
11205 C  CA    . TYR   B 303 ? 0.2648 0.3121 0.2571 -0.0197 -0.0621 0.0894  328 TYR   B CA    
11206 C  C     . TYR   B 303 ? 0.2292 0.3285 0.2783 -0.0564 -0.0484 0.0990  328 TYR   B C     
11207 O  O     . TYR   B 303 ? 0.2878 0.3547 0.2957 -0.0367 -0.0570 0.1306  328 TYR   B O     
11208 C  CB    . TYR   B 303 ? 0.3010 0.3069 0.2884 -0.0008 -0.0685 0.0714  328 TYR   B CB    
11209 C  CG    . TYR   B 303 ? 0.2734 0.3196 0.3451 -0.0079 -0.0723 0.0880  328 TYR   B CG    
11210 C  CD1   . TYR   B 303 ? 0.3139 0.3189 0.3804 -0.0351 -0.0506 0.0866  328 TYR   B CD1   
11211 C  CD2   . TYR   B 303 ? 0.2805 0.3174 0.3831 0.0012  -0.0894 0.0903  328 TYR   B CD2   
11212 C  CE1   . TYR   B 303 ? 0.3472 0.3326 0.4117 -0.0135 -0.0249 0.0938  328 TYR   B CE1   
11213 C  CE2   . TYR   B 303 ? 0.3163 0.3082 0.4149 0.0123  -0.0607 0.1173  328 TYR   B CE2   
11214 C  CZ    . TYR   B 303 ? 0.3706 0.3144 0.4323 0.0117  -0.0155 0.1089  328 TYR   B CZ    
11215 O  OH    . TYR   B 303 ? 0.4522 0.3353 0.4540 0.0278  -0.0033 0.1208  328 TYR   B OH    
11225 N  N     . VAL   B 304 ? 0.2060 0.3638 0.2738 -0.0558 -0.0482 0.0715  329 VAL   B N     
11226 C  CA    . VAL   B 304 ? 0.2439 0.3854 0.2582 -0.0359 -0.0567 0.0645  329 VAL   B CA    
11227 C  C     . VAL   B 304 ? 0.2678 0.4072 0.2490 -0.0250 -0.0635 0.0702  329 VAL   B C     
11228 O  O     . VAL   B 304 ? 0.2572 0.4136 0.2446 -0.0284 -0.0581 0.0840  329 VAL   B O     
11229 C  CB    . VAL   B 304 ? 0.2937 0.3986 0.2571 -0.0092 -0.0683 0.0433  329 VAL   B CB    
11230 C  CG1   . VAL   B 304 ? 0.3244 0.4330 0.2751 -0.0055 -0.0646 0.0518  329 VAL   B CG1   
11231 C  CG2   . VAL   B 304 ? 0.3269 0.4022 0.2623 0.0088  -0.0460 0.0366  329 VAL   B CG2   
11241 N  N     . ALA   B 305 ? 0.2613 0.3972 0.2383 -0.0171 -0.0541 0.0754  330 ALA   B N     
11242 C  CA    . ALA   B 305 ? 0.2941 0.4425 0.2300 0.0016  -0.0511 0.0498  330 ALA   B CA    
11243 C  C     . ALA   B 305 ? 0.3021 0.4720 0.2456 -0.0256 -0.0522 0.0568  330 ALA   B C     
11244 O  O     . ALA   B 305 ? 0.3242 0.4759 0.2412 -0.0045 -0.0360 0.0589  330 ALA   B O     
11245 C  CB    . ALA   B 305 ? 0.2879 0.4595 0.2484 0.0335  -0.0267 0.0286  330 ALA   B CB    
11251 N  N     . ASP   B 306 ? 0.3136 0.5230 0.2659 -0.0485 -0.0409 0.0676  331 ASP   B N     
11252 C  CA    . ASP   B 306 ? 0.3052 0.5778 0.2934 -0.0178 -0.0496 0.0824  331 ASP   B CA    
11253 C  C     . ASP   B 306 ? 0.2970 0.5481 0.2932 -0.0397 -0.0294 0.0775  331 ASP   B C     
11254 O  O     . ASP   B 306 ? 0.2897 0.5539 0.2850 -0.0365 -0.0180 0.0559  331 ASP   B O     
11255 C  CB    . ASP   B 306 ? 0.3241 0.6435 0.3280 0.0313  -0.0519 0.0774  331 ASP   B CB    
11256 C  CG    . ASP   B 306 ? 0.4066 0.7071 0.3539 0.0919  -0.0233 0.0541  331 ASP   B CG    
11257 O  OD1   . ASP   B 306 ? 0.4612 0.7232 0.3504 0.1348  0.0062  0.0315  331 ASP   B OD1   
11258 O  OD2   . ASP   B 306 ? 0.4078 0.7450 0.3793 0.1173  -0.0354 0.0431  331 ASP   B OD2   
11263 N  N     . GLN   B 307 ? 0.3225 0.5310 0.2943 -0.0347 -0.0104 0.0863  332 GLN   B N     
11264 C  CA    . GLN   B 307 ? 0.3390 0.5042 0.3132 -0.0369 0.0064  0.0846  332 GLN   B CA    
11265 C  C     . GLN   B 307 ? 0.3788 0.4963 0.3220 -0.0313 0.0125  0.0770  332 GLN   B C     
11266 O  O     . GLN   B 307 ? 0.4181 0.5015 0.3332 -0.0417 0.0100  0.0617  332 GLN   B O     
11267 C  CB    . GLN   B 307 ? 0.3685 0.4845 0.3316 -0.0318 -0.0177 0.0935  332 GLN   B CB    
11268 C  CG    . GLN   B 307 ? 0.3833 0.4631 0.3310 -0.0091 -0.0372 0.0919  332 GLN   B CG    
11269 C  CD    . GLN   B 307 ? 0.3536 0.4445 0.3408 -0.0186 -0.0522 0.0860  332 GLN   B CD    
11270 O  OE1   . GLN   B 307 ? 0.3562 0.4261 0.3380 -0.0263 -0.0970 0.0569  332 GLN   B OE1   
11271 N  NE2   . GLN   B 307 ? 0.3491 0.4275 0.3366 0.0045  -0.0439 0.1109  332 GLN   B NE2   
11280 N  N     . ILE   B 308 ? 0.3606 0.4679 0.3169 -0.0076 0.0023  0.0894  333 ILE   B N     
11281 C  CA    . ILE   B 308 ? 0.3279 0.4805 0.3010 -0.0005 -0.0153 0.0819  333 ILE   B CA    
11282 C  C     . ILE   B 308 ? 0.3613 0.5207 0.2785 -0.0281 -0.0145 0.0788  333 ILE   B C     
11283 O  O     . ILE   B 308 ? 0.3844 0.5531 0.2628 -0.0242 0.0050  0.0985  333 ILE   B O     
11284 C  CB    . ILE   B 308 ? 0.3027 0.5002 0.3084 0.0378  -0.0243 0.0729  333 ILE   B CB    
11285 C  CG1   . ILE   B 308 ? 0.3151 0.4936 0.3103 0.0459  -0.0428 0.0712  333 ILE   B CG1   
11286 C  CG2   . ILE   B 308 ? 0.3117 0.5306 0.3155 0.0366  -0.0342 0.0571  333 ILE   B CG2   
11287 C  CD1   . ILE   B 308 ? 0.3347 0.4943 0.3063 0.0461  -0.0466 0.0698  333 ILE   B CD1   
11299 N  N     . VAL   B 309 ? 0.3255 0.5266 0.2740 -0.0411 -0.0192 0.0697  334 VAL   B N     
11300 C  CA    . VAL   B 309 ? 0.3548 0.5673 0.2807 -0.0392 -0.0034 0.0678  334 VAL   B CA    
11301 C  C     . VAL   B 309 ? 0.3723 0.6032 0.2942 -0.0231 0.0086  0.0821  334 VAL   B C     
11302 O  O     . VAL   B 309 ? 0.3832 0.6112 0.2984 0.0228  0.0226  0.0881  334 VAL   B O     
11303 C  CB    . VAL   B 309 ? 0.3810 0.5856 0.2740 -0.0182 0.0400  0.0720  334 VAL   B CB    
11304 C  CG1   . VAL   B 309 ? 0.4424 0.6147 0.2847 -0.0001 0.0380  0.0603  334 VAL   B CG1   
11305 C  CG2   . VAL   B 309 ? 0.4061 0.5945 0.2696 0.0013  0.0417  0.0745  334 VAL   B CG2   
11315 N  N     . THR   B 310 ? 0.3901 0.6312 0.3120 -0.0543 0.0215  0.0961  335 THR   B N     
11316 C  CA    . THR   B 310 ? 0.4368 0.6724 0.3395 -0.0866 0.0318  0.0978  335 THR   B CA    
11317 C  C     . THR   B 310 ? 0.4891 0.6910 0.3381 -0.0640 0.0425  0.1049  335 THR   B C     
11318 O  O     . THR   B 310 ? 0.5085 0.7160 0.3237 -0.0541 0.0370  0.1041  335 THR   B O     
11319 C  CB    . THR   B 310 ? 0.4527 0.6981 0.3713 -0.1249 0.0128  0.1045  335 THR   B CB    
11320 O  OG1   . THR   B 310 ? 0.4821 0.7172 0.3846 -0.1165 -0.0029 0.0933  335 THR   B OG1   
11321 C  CG2   . THR   B 310 ? 0.4488 0.7088 0.3886 -0.1364 0.0216  0.0969  335 THR   B CG2   
11329 N  N     . LYS   B 311 ? 0.5298 0.6846 0.3530 -0.0344 0.0353  0.1107  336 LYS   B N     
11330 C  CA    . LYS   B 311 ? 0.5698 0.6858 0.3769 0.0003  0.0202  0.1310  336 LYS   B CA    
11331 C  C     . LYS   B 311 ? 0.5482 0.6668 0.3590 0.0217  0.0020  0.1393  336 LYS   B C     
11332 O  O     . LYS   B 311 ? 0.5807 0.6501 0.3536 0.0085  -0.0038 0.1554  336 LYS   B O     
11333 C  CB    . LYS   B 311 ? 0.5974 0.7103 0.4184 0.0044  0.0275  0.1419  336 LYS   B CB    
11334 C  CG    . LYS   B 311 ? 0.6701 0.7466 0.4607 0.0048  0.0305  0.1468  336 LYS   B CG    
11335 C  CD    . LYS   B 311 ? 0.7382 0.7794 0.4939 0.0225  0.0331  0.1476  336 LYS   B CD    
11336 C  CE    . LYS   B 311 ? 0.7898 0.8156 0.5243 0.0381  0.0241  0.1354  336 LYS   B CE    
11337 N  NZ    . LYS   B 311 ? 0.8223 0.8333 0.5449 0.0402  0.0164  0.1247  336 LYS   B NZ    
11351 N  N     . LEU   B 312 ? 0.5081 0.6656 0.3488 0.0424  -0.0042 0.1456  337 LEU   B N     
11352 C  CA    . LEU   B 312 ? 0.5032 0.6868 0.3506 0.0476  -0.0110 0.1491  337 LEU   B CA    
11353 C  C     . LEU   B 312 ? 0.5221 0.7289 0.3364 0.0669  0.0029  0.1338  337 LEU   B C     
11354 O  O     . LEU   B 312 ? 0.5333 0.7401 0.3169 0.0757  0.0177  0.1322  337 LEU   B O     
11355 C  CB    . LEU   B 312 ? 0.5231 0.6800 0.3786 0.0291  -0.0169 0.1643  337 LEU   B CB    
11356 C  CG    . LEU   B 312 ? 0.5616 0.6989 0.4276 0.0239  -0.0274 0.1545  337 LEU   B CG    
11357 C  CD1   . LEU   B 312 ? 0.5366 0.7123 0.4507 0.0118  -0.0166 0.1322  337 LEU   B CD1   
11358 C  CD2   . LEU   B 312 ? 0.5811 0.7065 0.4356 0.0265  -0.0378 0.1730  337 LEU   B CD2   
11370 N  N     . VAL   B 313 ? 0.5265 0.7712 0.3487 0.0656  0.0052  0.1246  338 VAL   B N     
11371 C  CA    . VAL   B 313 ? 0.5733 0.8184 0.3805 0.0517  -0.0088 0.1325  338 VAL   B CA    
11372 C  C     . VAL   B 313 ? 0.6418 0.8422 0.4274 0.0304  0.0161  0.1593  338 VAL   B C     
11373 O  O     . VAL   B 313 ? 0.6609 0.8524 0.4314 0.0443  0.0064  0.1505  338 VAL   B O     
11374 C  CB    . VAL   B 313 ? 0.5563 0.8375 0.3738 0.0576  -0.0283 0.1197  338 VAL   B CB    
11375 C  CG1   . VAL   B 313 ? 0.5465 0.8466 0.3740 0.0574  -0.0276 0.1128  338 VAL   B CG1   
11376 C  CG2   . VAL   B 313 ? 0.5446 0.8400 0.3676 0.0654  -0.0409 0.1256  338 VAL   B CG2   
11386 N  N     . ASP   B 314 ? 0.6926 0.8668 0.4755 0.0057  0.0347  0.1822  339 ASP   B N     
11387 C  CA    . ASP   B 314 ? 0.7412 0.8903 0.5286 -0.0131 0.0405  0.2009  339 ASP   B CA    
11388 C  C     . ASP   B 314 ? 0.7379 0.8933 0.5251 -0.0121 0.0448  0.2189  339 ASP   B C     
11389 O  O     . ASP   B 314 ? 0.7141 0.8856 0.5225 -0.0404 0.0832  0.2291  339 ASP   B O     
11390 C  CB    . ASP   B 314 ? 0.7994 0.9131 0.5866 -0.0201 0.0249  0.1935  339 ASP   B CB    
11391 C  CG    . ASP   B 314 ? 0.8541 0.9359 0.6411 -0.0136 0.0186  0.1834  339 ASP   B CG    
11392 O  OD1   . ASP   B 314 ? 0.8486 0.9479 0.6619 -0.0028 0.0180  0.1821  339 ASP   B OD1   
11393 O  OD2   . ASP   B 314 ? 0.8995 0.9413 0.6626 -0.0243 0.0125  0.1764  339 ASP   B OD2   
11398 N  N     . VAL   B 315 ? 0.7517 0.9084 0.5260 0.0203  0.0085  0.2234  340 VAL   B N     
11399 C  CA    . VAL   B 315 ? 0.7765 0.9267 0.5343 0.0478  -0.0259 0.2275  340 VAL   B CA    
11400 C  C     . VAL   B 315 ? 0.7999 0.9500 0.5448 0.0393  -0.0320 0.2269  340 VAL   B C     
11401 O  O     . VAL   B 315 ? 0.8084 0.9481 0.5265 0.0426  -0.0345 0.2496  340 VAL   B O     
11402 C  CB    . VAL   B 315 ? 0.7855 0.9179 0.5434 0.0892  -0.0501 0.2243  340 VAL   B CB    
11403 C  CG1   . VAL   B 315 ? 0.8022 0.9105 0.5498 0.1045  -0.0453 0.2185  340 VAL   B CG1   
11404 C  CG2   . VAL   B 315 ? 0.7772 0.9156 0.5440 0.0991  -0.0640 0.2313  340 VAL   B CG2   
11414 N  N     . VAL   B 316 ? 0.8181 0.9773 0.5827 0.0253  -0.0355 0.2054  341 VAL   B N     
11415 C  CA    . VAL   B 316 ? 0.8530 1.0043 0.6399 0.0068  -0.0352 0.1861  341 VAL   B CA    
11416 C  C     . VAL   B 316 ? 0.8888 1.0385 0.7050 -0.0044 -0.0003 0.1575  341 VAL   B C     
11417 O  O     . VAL   B 316 ? 0.8896 1.0350 0.7042 -0.0091 0.0080  0.1469  341 VAL   B O     
11418 C  CB    . VAL   B 316 ? 0.8494 0.9976 0.6328 0.0068  -0.0657 0.1927  341 VAL   B CB    
11419 C  CG1   . VAL   B 316 ? 0.8229 0.9889 0.6187 0.0138  -0.0760 0.1938  341 VAL   B CG1   
11420 C  CG2   . VAL   B 316 ? 0.8728 1.0036 0.6466 0.0053  -0.0574 0.1939  341 VAL   B CG2   
11430 N  N     . LYS   B 317 ? 0.9235 1.0766 0.7659 -0.0075 0.0188  0.1425  342 LYS   B N     
11431 C  CA    . LYS   B 317 ? 0.9680 1.1128 0.8301 -0.0033 0.0390  0.1243  342 LYS   B CA    
11432 C  C     . LYS   B 317 ? 1.0028 1.1410 0.8649 -0.0019 0.0568  0.1203  342 LYS   B C     
11433 O  O     . LYS   B 317 ? 0.9864 1.1432 0.8625 -0.0085 0.0746  0.1183  342 LYS   B O     
11434 C  CB    . LYS   B 317 ? 0.9767 1.1149 0.8562 -0.0042 0.0432  0.1127  342 LYS   B CB    
11435 C  CG    . LYS   B 317 ? 0.9877 1.1158 0.8815 -0.0012 0.0446  0.1007  342 LYS   B CG    
11436 C  CD    . LYS   B 317 ? 0.9986 1.1162 0.9011 -0.0010 0.0499  0.0926  342 LYS   B CD    
11437 C  CE    . LYS   B 317 ? 1.0114 1.1142 0.9147 -0.0017 0.0521  0.0893  342 LYS   B CE    
11438 N  NZ    . LYS   B 317 ? 1.0195 1.1116 0.9199 -0.0052 0.0512  0.0882  342 LYS   B NZ    
11452 N  N     . LYS   B 318 ? 1.0568 1.1673 0.8997 0.0027  0.0548  0.1169  343 LYS   B N     
11453 C  CA    . LYS   B 318 ? 1.0997 1.1920 0.9299 0.0117  0.0523  0.1097  343 LYS   B CA    
11454 C  C     . LYS   B 318 ? 1.1081 1.2085 0.9436 0.0203  0.0356  0.0967  343 LYS   B C     
11455 O  O     . LYS   B 318 ? 1.1075 1.2120 0.9449 0.0274  0.0420  0.0970  343 LYS   B O     
11456 C  CB    . LYS   B 318 ? 1.1308 1.1959 0.9428 0.0096  0.0675  0.1142  343 LYS   B CB    
11457 C  CG    . LYS   B 318 ? 1.1511 1.1947 0.9527 0.0036  0.0815  0.1207  343 LYS   B CG    
11458 C  CD    . LYS   B 318 ? 1.1702 1.1944 0.9602 0.0012  0.0903  0.1270  343 LYS   B CD    
11459 C  CE    . LYS   B 318 ? 1.1799 1.1933 0.9632 0.0009  0.0968  0.1301  343 LYS   B CE    
11460 N  NZ    . LYS   B 318 ? 1.1849 1.1901 0.9632 -0.0010 0.0999  0.1302  343 LYS   B NZ    
11474 N  N     . LYS   B 319 ? 1.1138 1.2208 0.9548 0.0157  0.0120  0.0852  344 LYS   B N     
11475 C  CA    . LYS   B 319 ? 1.1238 1.2412 0.9685 0.0128  -0.0144 0.0711  344 LYS   B CA    
11476 C  C     . LYS   B 319 ? 1.1528 1.2677 0.9866 0.0056  -0.0256 0.0559  344 LYS   B C     
11477 O  O     . LYS   B 319 ? 1.1592 1.2720 0.9877 0.0035  -0.0230 0.0515  344 LYS   B O     
11478 C  CB    . LYS   B 319 ? 1.1062 1.2379 0.9650 0.0103  -0.0236 0.0709  344 LYS   B CB    
11479 C  CG    . LYS   B 319 ? 1.0957 1.2382 0.9655 0.0019  -0.0306 0.0658  344 LYS   B CG    
11480 C  CD    . LYS   B 319 ? 1.0867 1.2385 0.9685 -0.0011 -0.0381 0.0582  344 LYS   B CD    
11481 C  CE    . LYS   B 319 ? 1.0848 1.2405 0.9732 -0.0018 -0.0391 0.0502  344 LYS   B CE    
11482 N  NZ    . LYS   B 319 ? 1.0880 1.2425 0.9768 0.0001  -0.0383 0.0454  344 LYS   B NZ    
11496 N  N     . ASN   B 320 ? 1.1734 1.2853 1.0031 0.0024  -0.0403 0.0466  345 ASN   B N     
11497 C  CA    . ASN   B 320 ? 1.1973 1.2988 1.0191 0.0026  -0.0518 0.0388  345 ASN   B CA    
11498 C  C     . ASN   B 320 ? 1.1945 1.3017 1.0245 0.0095  -0.0524 0.0349  345 ASN   B C     
11499 O  O     . ASN   B 320 ? 1.1920 1.3025 1.0286 0.0123  -0.0545 0.0335  345 ASN   B O     
11500 C  CB    . ASN   B 320 ? 1.2157 1.3070 1.0284 -0.0024 -0.0574 0.0353  345 ASN   B CB    
11501 C  CG    . ASN   B 320 ? 1.2246 1.3129 1.0354 -0.0063 -0.0615 0.0329  345 ASN   B CG    
11502 O  OD1   . ASN   B 320 ? 1.2310 1.3151 1.0397 -0.0095 -0.0583 0.0335  345 ASN   B OD1   
11503 N  ND2   . ASN   B 320 ? 1.2241 1.3146 1.0358 -0.0085 -0.0675 0.0319  345 ASN   B ND2   
11510 N  N     . ALA   B 325 ? 0.7282 0.9139 0.7156 -0.0816 0.0915  0.2458  350 ALA   B N     
11511 C  CA    . ALA   B 325 ? 0.7518 0.9155 0.7178 -0.0687 0.0767  0.2446  350 ALA   B CA    
11512 C  C     . ALA   B 325 ? 0.7648 0.9017 0.7200 -0.0675 0.0597  0.2407  350 ALA   B C     
11513 O  O     . ALA   B 325 ? 0.7570 0.9051 0.7234 -0.0677 0.0611  0.2426  350 ALA   B O     
11514 C  CB    . ALA   B 325 ? 0.7590 0.9203 0.7155 -0.0684 0.0737  0.2483  350 ALA   B CB    
11519 N  N     . VAL   B 326 ? 0.7890 0.8893 0.7174 -0.0679 0.0399  0.2265  351 VAL   B N     
11520 C  CA    . VAL   B 326 ? 0.7966 0.8771 0.7150 -0.0485 -0.0001 0.2020  351 VAL   B CA    
11521 C  C     . VAL   B 326 ? 0.7527 0.8226 0.6984 -0.0462 -0.0296 0.2004  351 VAL   B C     
11522 O  O     . VAL   B 326 ? 0.7593 0.8310 0.7044 -0.0667 -0.0598 0.2076  351 VAL   B O     
11523 C  CB    . VAL   B 326 ? 0.8392 0.9143 0.7258 -0.0363 -0.0084 0.1829  351 VAL   B CB    
11524 C  CG1   . VAL   B 326 ? 0.8473 0.9270 0.7293 -0.0320 -0.0085 0.1759  351 VAL   B CG1   
11525 C  CG2   . VAL   B 326 ? 0.8617 0.9299 0.7312 -0.0265 -0.0171 0.1801  351 VAL   B CG2   
11535 N  N     . LYS   B 327 ? 0.6934 0.7601 0.6779 -0.0217 -0.0128 0.1922  352 LYS   B N     
11536 C  CA    . LYS   B 327 ? 0.6572 0.7106 0.6622 0.0128  -0.0022 0.1745  352 LYS   B CA    
11537 C  C     . LYS   B 327 ? 0.6148 0.6659 0.6335 0.0401  -0.0067 0.1679  352 LYS   B C     
11538 O  O     . LYS   B 327 ? 0.5855 0.6355 0.6251 0.0636  -0.0003 0.1892  352 LYS   B O     
11539 C  CB    . LYS   B 327 ? 0.6696 0.7053 0.6745 0.0148  0.0060  0.1658  352 LYS   B CB    
11540 C  CG    . LYS   B 327 ? 0.7064 0.7213 0.6879 -0.0002 0.0046  0.1450  352 LYS   B CG    
11541 C  CD    . LYS   B 327 ? 0.7376 0.7423 0.7001 -0.0250 0.0014  0.1117  352 LYS   B CD    
11542 C  CE    . LYS   B 327 ? 0.7563 0.7632 0.7052 -0.0462 -0.0002 0.0878  352 LYS   B CE    
11543 N  NZ    . LYS   B 327 ? 0.7750 0.7848 0.7080 -0.0570 -0.0059 0.0787  352 LYS   B NZ    
11557 N  N     . ALA   B 328 ? 0.5870 0.6571 0.6160 0.0368  -0.0184 0.1342  353 ALA   B N     
11558 C  CA    . ALA   B 328 ? 0.5322 0.6449 0.5940 0.0498  -0.0275 0.1034  353 ALA   B CA    
11559 C  C     . ALA   B 328 ? 0.4633 0.6129 0.5533 0.0688  -0.0499 0.0978  353 ALA   B C     
11560 O  O     . ALA   B 328 ? 0.4081 0.5870 0.5556 0.0612  -0.0767 0.0832  353 ALA   B O     
11561 C  CB    . ALA   B 328 ? 0.5423 0.6610 0.6085 0.0543  -0.0302 0.0925  353 ALA   B CB    
11567 N  N     . HIS   B 329 ? 0.4398 0.6094 0.5082 0.1085  -0.0535 0.1063  354 HIS   B N     
11568 C  CA    . HIS   B 329 ? 0.4349 0.6065 0.4570 0.1516  -0.0509 0.1091  354 HIS   B CA    
11569 C  C     . HIS   B 329 ? 0.4299 0.5861 0.4190 0.1354  -0.0552 0.0915  354 HIS   B C     
11570 O  O     . HIS   B 329 ? 0.4467 0.5901 0.3993 0.1304  -0.0622 0.0891  354 HIS   B O     
11571 C  CB    . HIS   B 329 ? 0.4272 0.6275 0.4402 0.1915  -0.0355 0.1198  354 HIS   B CB    
11572 C  CG    . HIS   B 329 ? 0.4883 0.6488 0.4289 0.2050  -0.0283 0.1275  354 HIS   B CG    
11573 N  ND1   . HIS   B 329 ? 0.5378 0.6739 0.4354 0.2034  -0.0215 0.1124  354 HIS   B ND1   
11574 C  CD2   . HIS   B 329 ? 0.5160 0.6600 0.4239 0.2059  -0.0175 0.1286  354 HIS   B CD2   
11575 C  CE1   . HIS   B 329 ? 0.5494 0.6797 0.4330 0.1939  0.0008  0.1094  354 HIS   B CE1   
11576 N  NE2   . HIS   B 329 ? 0.5492 0.6772 0.4314 0.1927  -0.0002 0.1153  354 HIS   B NE2   
11584 N  N     . GLN   B 330 ? 0.4414 0.5660 0.4018 0.1203  -0.0448 0.1018  355 GLN   B N     
11585 C  CA    . GLN   B 330 ? 0.4733 0.5978 0.3949 0.0906  -0.0248 0.0588  355 GLN   B CA    
11586 C  C     . GLN   B 330 ? 0.4374 0.5458 0.3734 0.0597  -0.0223 0.0414  355 GLN   B C     
11587 O  O     . GLN   B 330 ? 0.4212 0.5318 0.3592 0.0020  -0.0251 0.0195  355 GLN   B O     
11588 C  CB    . GLN   B 330 ? 0.5525 0.6549 0.4015 0.0894  -0.0065 0.0513  355 GLN   B CB    
11589 C  CG    . GLN   B 330 ? 0.6195 0.6908 0.4193 0.0711  0.0007  0.0267  355 GLN   B CG    
11590 C  CD    . GLN   B 330 ? 0.6908 0.7307 0.4428 0.0200  0.0174  -0.0062 355 GLN   B CD    
11591 O  OE1   . GLN   B 330 ? 0.7233 0.7393 0.4578 -0.0055 0.0221  -0.0116 355 GLN   B OE1   
11592 N  NE2   . GLN   B 330 ? 0.7185 0.7510 0.4480 0.0167  0.0294  -0.0313 355 GLN   B NE2   
11601 N  N     . VAL   B 331 ? 0.4389 0.5308 0.3796 0.0483  -0.0288 0.0392  356 VAL   B N     
11602 C  CA    . VAL   B 331 ? 0.4389 0.5010 0.3894 0.0460  -0.0525 0.0491  356 VAL   B CA    
11603 C  C     . VAL   B 331 ? 0.4117 0.5041 0.3720 0.0316  -0.0787 0.0329  356 VAL   B C     
11604 O  O     . VAL   B 331 ? 0.4067 0.4851 0.3747 0.0108  -0.0866 0.0333  356 VAL   B O     
11605 C  CB    . VAL   B 331 ? 0.4836 0.4919 0.4178 0.0668  -0.0631 0.0695  356 VAL   B CB    
11606 C  CG1   . VAL   B 331 ? 0.4812 0.4650 0.4199 0.0666  -0.0701 0.0861  356 VAL   B CG1   
11607 C  CG2   . VAL   B 331 ? 0.5352 0.5129 0.4441 0.0681  -0.0572 0.0726  356 VAL   B CG2   
11617 N  N     . LYS   B 332 ? 0.3951 0.5387 0.3484 0.0208  -0.0797 0.0223  357 LYS   B N     
11618 C  CA    . LYS   B 332 ? 0.3970 0.5885 0.3168 0.0237  -0.1104 0.0186  357 LYS   B CA    
11619 C  C     . LYS   B 332 ? 0.4133 0.5567 0.2887 0.0346  -0.0845 0.0331  357 LYS   B C     
11620 O  O     . LYS   B 332 ? 0.4027 0.5552 0.2714 0.0191  -0.0952 0.0174  357 LYS   B O     
11621 C  CB    . LYS   B 332 ? 0.4086 0.6606 0.3121 0.0607  -0.1191 0.0198  357 LYS   B CB    
11622 C  CG    . LYS   B 332 ? 0.4233 0.7025 0.3056 0.0515  -0.0939 0.0013  357 LYS   B CG    
11623 C  CD    . LYS   B 332 ? 0.4208 0.7247 0.3046 0.0371  -0.0877 0.0055  357 LYS   B CD    
11624 C  CE    . LYS   B 332 ? 0.4258 0.7374 0.2989 0.0257  -0.0763 0.0209  357 LYS   B CE    
11625 N  NZ    . LYS   B 332 ? 0.4342 0.7577 0.3059 0.0092  -0.0929 -0.0013 357 LYS   B NZ    
11639 N  N     . ASN   B 333 ? 0.4075 0.5373 0.2763 0.0365  -0.0582 0.0548  358 ASN   B N     
11640 C  CA    . ASN   B 333 ? 0.4317 0.5495 0.3312 0.0467  -0.0488 0.0473  358 ASN   B CA    
11641 C  C     . ASN   B 333 ? 0.4326 0.5095 0.2866 0.0434  -0.0634 0.0215  358 ASN   B C     
11642 O  O     . ASN   B 333 ? 0.4474 0.4921 0.2854 0.0395  -0.0683 0.0296  358 ASN   B O     
11643 C  CB    . ASN   B 333 ? 0.4847 0.6086 0.4253 0.0030  -0.0296 0.0788  358 ASN   B CB    
11644 C  CG    . ASN   B 333 ? 0.5121 0.6376 0.4970 -0.0144 -0.0185 0.1296  358 ASN   B CG    
11645 O  OD1   . ASN   B 333 ? 0.5123 0.6506 0.5112 0.0158  -0.0011 0.1213  358 ASN   B OD1   
11646 N  ND2   . ASN   B 333 ? 0.5492 0.6387 0.5341 -0.0420 -0.0050 0.1697  358 ASN   B ND2   
11653 N  N     . HIS   B 334 ? 0.3956 0.4896 0.2589 0.0491  -0.0550 0.0017  359 HIS   B N     
11654 C  CA    . HIS   B 334 ? 0.4130 0.5077 0.2602 0.0638  -0.0754 -0.0048 359 HIS   B CA    
11655 C  C     . HIS   B 334 ? 0.3926 0.4714 0.2714 0.0510  -0.0813 -0.0077 359 HIS   B C     
11656 O  O     . HIS   B 334 ? 0.4318 0.4890 0.2947 0.0429  -0.0535 -0.0248 359 HIS   B O     
11657 C  CB    . HIS   B 334 ? 0.4754 0.5844 0.2775 0.0647  -0.0743 -0.0248 359 HIS   B CB    
11658 C  CG    . HIS   B 334 ? 0.5256 0.6771 0.2990 0.0751  -0.0764 -0.0637 359 HIS   B CG    
11659 N  ND1   . HIS   B 334 ? 0.5506 0.7158 0.3237 0.0641  -0.0600 -0.0877 359 HIS   B ND1   
11660 C  CD2   . HIS   B 334 ? 0.5342 0.7162 0.3068 0.0914  -0.0800 -0.0844 359 HIS   B CD2   
11661 C  CE1   . HIS   B 334 ? 0.5620 0.7413 0.3245 0.0679  -0.0616 -0.1040 359 HIS   B CE1   
11662 N  NE2   . HIS   B 334 ? 0.5588 0.7459 0.3219 0.0953  -0.0559 -0.0997 359 HIS   B NE2   
11670 N  N     . MET   B 335 ? 0.3565 0.4263 0.2635 0.0305  -0.0914 0.0002  360 MET   B N     
11671 C  CA    . MET   B 335 ? 0.3351 0.3845 0.2698 0.0162  -0.0673 0.0092  360 MET   B CA    
11672 C  C     . MET   B 335 ? 0.3163 0.3510 0.2687 0.0364  -0.0664 0.0017  360 MET   B C     
11673 O  O     . MET   B 335 ? 0.3059 0.3599 0.2624 0.0515  -0.0722 -0.0076 360 MET   B O     
11674 C  CB    . MET   B 335 ? 0.3513 0.4131 0.2865 -0.0091 -0.0594 0.0313  360 MET   B CB    
11675 C  CG    . MET   B 335 ? 0.3924 0.4358 0.3193 -0.0143 -0.0336 0.0521  360 MET   B CG    
11676 S  SD    . MET   B 335 ? 0.4229 0.4580 0.3503 -0.0304 -0.0125 0.0430  360 MET   B SD    
11677 C  CE    . MET   B 335 ? 0.3981 0.4656 0.3460 -0.0173 -0.0286 0.0250  360 MET   B CE    
11687 N  N     . TRP   B 336 ? 0.3280 0.3482 0.2867 0.0218  -0.0652 0.0086  361 TRP   B N     
11688 C  CA    . TRP   B 336 ? 0.3098 0.3320 0.2919 0.0089  -0.0715 -0.0170 361 TRP   B CA    
11689 C  C     . TRP   B 336 ? 0.3091 0.3244 0.2940 0.0368  -0.0881 -0.0168 361 TRP   B C     
11690 O  O     . TRP   B 336 ? 0.3128 0.3566 0.2995 0.0497  -0.1033 -0.0164 361 TRP   B O     
11691 C  CB    . TRP   B 336 ? 0.3135 0.3450 0.3065 -0.0140 -0.0708 -0.0177 361 TRP   B CB    
11692 C  CG    . TRP   B 336 ? 0.2780 0.3670 0.3334 -0.0086 -0.0814 -0.0056 361 TRP   B CG    
11693 C  CD1   . TRP   B 336 ? 0.2707 0.3629 0.3388 -0.0307 -0.0726 0.0050  361 TRP   B CD1   
11694 C  CD2   . TRP   B 336 ? 0.2951 0.3724 0.3623 -0.0279 -0.0801 -0.0036 361 TRP   B CD2   
11695 N  NE1   . TRP   B 336 ? 0.2906 0.3595 0.3545 -0.0033 -0.0711 0.0174  361 TRP   B NE1   
11696 C  CE2   . TRP   B 336 ? 0.2909 0.3661 0.3704 -0.0117 -0.0792 0.0090  361 TRP   B CE2   
11697 C  CE3   . TRP   B 336 ? 0.3032 0.3775 0.3764 -0.0625 -0.0985 -0.0129 361 TRP   B CE3   
11698 C  CZ2   . TRP   B 336 ? 0.2835 0.3732 0.3863 -0.0457 -0.0917 -0.0003 361 TRP   B CZ2   
11699 C  CZ3   . TRP   B 336 ? 0.3150 0.3700 0.3916 -0.0912 -0.1072 -0.0068 361 TRP   B CZ3   
11700 C  CH2   . TRP   B 336 ? 0.3197 0.3753 0.3944 -0.0619 -0.0814 -0.0054 361 TRP   B CH2   
11711 N  N     . ILE   B 337 ? 0.2673 0.3031 0.2869 0.0281  -0.0916 -0.0053 362 ILE   B N     
11712 C  CA    . ILE   B 337 ? 0.2606 0.3152 0.2928 -0.0011 -0.0744 0.0100  362 ILE   B CA    
11713 C  C     . ILE   B 337 ? 0.2283 0.3018 0.2827 0.0315  -0.0830 0.0103  362 ILE   B C     
11714 O  O     . ILE   B 337 ? 0.2582 0.2991 0.2975 0.0429  -0.0762 0.0274  362 ILE   B O     
11715 C  CB    . ILE   B 337 ? 0.2677 0.3313 0.2973 -0.0157 -0.0917 0.0134  362 ILE   B CB    
11716 C  CG1   . ILE   B 337 ? 0.3401 0.3749 0.3367 -0.0434 -0.0958 0.0192  362 ILE   B CG1   
11717 C  CG2   . ILE   B 337 ? 0.2418 0.3505 0.2731 -0.0069 -0.0828 0.0069  362 ILE   B CG2   
11718 C  CD1   . ILE   B 337 ? 0.3970 0.4049 0.3569 -0.0251 -0.0801 0.0371  362 ILE   B CD1   
11730 N  N     . PHE   B 338 ? 0.2038 0.3145 0.2966 0.0284  -0.0786 -0.0046 363 PHE   B N     
11731 C  CA    . PHE   B 338 ? 0.1865 0.3036 0.3026 0.0062  -0.0739 -0.0108 363 PHE   B CA    
11732 C  C     . PHE   B 338 ? 0.2177 0.2800 0.2935 0.0169  -0.0566 0.0110  363 PHE   B C     
11733 O  O     . PHE   B 338 ? 0.2549 0.2766 0.3023 0.0085  -0.0850 0.0153  363 PHE   B O     
11734 C  CB    . PHE   B 338 ? 0.2006 0.3282 0.3490 0.0314  -0.0766 -0.0382 363 PHE   B CB    
11735 C  CG    . PHE   B 338 ? 0.2215 0.3320 0.3969 0.0415  -0.1177 -0.0493 363 PHE   B CG    
11736 C  CD1   . PHE   B 338 ? 0.2436 0.3479 0.4246 0.0370  -0.1415 -0.0550 363 PHE   B CD1   
11737 C  CD2   . PHE   B 338 ? 0.2117 0.3434 0.4309 0.0105  -0.1295 -0.0558 363 PHE   B CD2   
11738 C  CE1   . PHE   B 338 ? 0.2725 0.3722 0.4494 0.0429  -0.1435 -0.0550 363 PHE   B CE1   
11739 C  CE2   . PHE   B 338 ? 0.2052 0.3445 0.4548 0.0157  -0.1425 -0.0508 363 PHE   B CE2   
11740 C  CZ    . PHE   B 338 ? 0.2449 0.3529 0.4595 0.0239  -0.1496 -0.0564 363 PHE   B CZ    
11750 N  N     . VAL   B 339 ? 0.2121 0.2602 0.2767 -0.0059 -0.0434 0.0175  364 VAL   B N     
11751 C  CA    . VAL   B 339 ? 0.1691 0.2749 0.2818 -0.0199 -0.0390 0.0268  364 VAL   B CA    
11752 C  C     . VAL   B 339 ? 0.1846 0.2417 0.2935 0.0133  -0.0541 0.0221  364 VAL   B C     
11753 O  O     . VAL   B 339 ? 0.2443 0.2361 0.3082 0.0198  -0.0586 0.0312  364 VAL   B O     
11754 C  CB    . VAL   B 339 ? 0.1527 0.2824 0.2729 -0.0281 -0.0432 0.0290  364 VAL   B CB    
11755 C  CG1   . VAL   B 339 ? 0.1952 0.3020 0.2602 -0.0243 -0.0399 -0.0016 364 VAL   B CG1   
11756 C  CG2   . VAL   B 339 ? 0.2072 0.2945 0.2788 -0.0256 -0.0390 0.0484  364 VAL   B CG2   
11766 N  N     . ASN   B 340 ? 0.1954 0.2440 0.3140 0.0110  -0.0485 0.0155  365 ASN   B N     
11767 C  CA    . ASN   B 340 ? 0.1502 0.2342 0.3288 0.0174  -0.0386 0.0136  365 ASN   B CA    
11768 C  C     . ASN   B 340 ? 0.1875 0.2569 0.3323 0.0224  -0.0540 0.0215  365 ASN   B C     
11769 O  O     . ASN   B 340 ? 0.2277 0.2704 0.3295 0.0427  -0.0679 0.0068  365 ASN   B O     
11770 C  CB    . ASN   B 340 ? 0.1426 0.2605 0.3320 0.0302  -0.0124 -0.0015 365 ASN   B CB    
11771 C  CG    . ASN   B 340 ? 0.1463 0.2750 0.3444 0.0335  -0.0055 0.0090  365 ASN   B CG    
11772 O  OD1   . ASN   B 340 ? 0.1916 0.2626 0.3537 0.0389  -0.0171 0.0202  365 ASN   B OD1   
11773 N  ND2   . ASN   B 340 ? 0.2010 0.3081 0.3585 0.0175  -0.0331 0.0131  365 ASN   B ND2   
11780 N  N     . ALA   B 341 ? 0.1862 0.2403 0.3237 0.0140  -0.0499 0.0343  366 ALA   B N     
11781 C  CA    . ALA   B 341 ? 0.1722 0.2426 0.3191 -0.0128 -0.0314 0.0296  366 ALA   B CA    
11782 C  C     . ALA   B 341 ? 0.1593 0.2252 0.3123 0.0121  -0.0152 0.0322  366 ALA   B C     
11783 O  O     . ALA   B 341 ? 0.1764 0.2400 0.3123 0.0220  -0.0181 0.0266  366 ALA   B O     
11784 C  CB    . ALA   B 341 ? 0.1583 0.2325 0.3065 -0.0231 -0.0297 0.0506  366 ALA   B CB    
11790 N  N     . LEU   B 342 ? 0.2137 0.2216 0.3244 0.0183  -0.0113 0.0346  367 LEU   B N     
11791 C  CA    . LEU   B 342 ? 0.1771 0.2327 0.3257 0.0320  -0.0020 0.0317  367 LEU   B CA    
11792 C  C     . LEU   B 342 ? 0.2030 0.2273 0.3131 0.0248  -0.0154 0.0232  367 LEU   B C     
11793 O  O     . LEU   B 342 ? 0.2116 0.2389 0.3175 0.0278  -0.0109 0.0414  367 LEU   B O     
11794 C  CB    . LEU   B 342 ? 0.1724 0.2751 0.3562 0.0590  0.0048  0.0228  367 LEU   B CB    
11795 C  CG    . LEU   B 342 ? 0.1493 0.2832 0.3795 0.0610  0.0064  0.0149  367 LEU   B CG    
11796 C  CD1   . LEU   B 342 ? 0.1978 0.3149 0.3949 0.0886  0.0320  0.0031  367 LEU   B CD1   
11797 C  CD2   . LEU   B 342 ? 0.1812 0.3005 0.3958 0.0323  -0.0059 0.0200  367 LEU   B CD2   
11809 N  N     . ILE   B 343 ? 0.1856 0.2245 0.2870 0.0094  -0.0079 0.0054  368 ILE   B N     
11810 C  CA    . ILE   B 343 ? 0.1711 0.1939 0.2760 0.0171  -0.0134 0.0140  368 ILE   B CA    
11811 C  C     . ILE   B 343 ? 0.1881 0.1723 0.2911 0.0122  -0.0048 0.0033  368 ILE   B C     
11812 O  O     . ILE   B 343 ? 0.2131 0.1969 0.2846 0.0167  -0.0051 0.0025  368 ILE   B O     
11813 C  CB    . ILE   B 343 ? 0.1463 0.2326 0.2604 0.0040  -0.0164 0.0010  368 ILE   B CB    
11814 C  CG1   . ILE   B 343 ? 0.1768 0.2874 0.2554 -0.0057 -0.0244 0.0083  368 ILE   B CG1   
11815 C  CG2   . ILE   B 343 ? 0.1501 0.2406 0.2540 -0.0188 -0.0117 -0.0093 368 ILE   B CG2   
11816 C  CD1   . ILE   B 343 ? 0.1997 0.2946 0.2488 -0.0366 -0.0165 0.0099  368 ILE   B CD1   
11828 N  N     . GLU   B 344 ? 0.2091 0.1742 0.2937 -0.0107 0.0012  -0.0001 369 GLU   B N     
11829 C  CA    . GLU   B 344 ? 0.2480 0.1716 0.2793 0.0117  0.0055  0.0055  369 GLU   B CA    
11830 C  C     . GLU   B 344 ? 0.2333 0.1798 0.2610 0.0083  0.0129  0.0087  369 GLU   B C     
11831 O  O     . GLU   B 344 ? 0.2282 0.2153 0.2599 0.0130  -0.0076 0.0180  369 GLU   B O     
11832 C  CB    . GLU   B 344 ? 0.3100 0.1730 0.3056 0.0042  -0.0018 0.0283  369 GLU   B CB    
11833 C  CG    . GLU   B 344 ? 0.3267 0.1561 0.3395 -0.0015 -0.0372 0.0229  369 GLU   B CG    
11834 C  CD    . GLU   B 344 ? 0.3380 0.2032 0.3777 0.0113  -0.0578 0.0177  369 GLU   B CD    
11835 O  OE1   . GLU   B 344 ? 0.3752 0.2172 0.3839 -0.0346 -0.0241 0.0119  369 GLU   B OE1   
11836 O  OE2   . GLU   B 344 ? 0.3420 0.2509 0.3979 0.0267  -0.0956 0.0204  369 GLU   B OE2   
11843 N  N     . ASN   B 345 ? 0.2317 0.1839 0.2683 -0.0023 0.0098  0.0127  370 ASN   B N     
11844 C  CA    . ASN   B 345 ? 0.2605 0.1942 0.2639 0.0193  -0.0281 -0.0020 370 ASN   B CA    
11845 C  C     . ASN   B 345 ? 0.2207 0.2035 0.2532 0.0016  -0.0218 -0.0015 370 ASN   B C     
11846 O  O     . ASN   B 345 ? 0.2384 0.2116 0.2527 -0.0116 -0.0136 0.0215  370 ASN   B O     
11847 C  CB    . ASN   B 345 ? 0.2919 0.1958 0.2727 0.0010  -0.0353 0.0069  370 ASN   B CB    
11848 C  CG    . ASN   B 345 ? 0.3163 0.2218 0.2911 -0.0143 -0.0324 -0.0197 370 ASN   B CG    
11849 O  OD1   . ASN   B 345 ? 0.3226 0.2270 0.2909 -0.0103 -0.0060 -0.0264 370 ASN   B OD1   
11850 N  ND2   . ASN   B 345 ? 0.3502 0.2331 0.3192 -0.0152 -0.0122 -0.0481 370 ASN   B ND2   
11857 N  N     . PRO   B 346 ? 0.2082 0.1856 0.2467 0.0086  -0.0144 0.0103  371 PRO   B N     
11858 C  CA    . PRO   B 346 ? 0.1951 0.1998 0.2238 -0.0022 0.0062  0.0232  371 PRO   B CA    
11859 C  C     . PRO   B 346 ? 0.2500 0.1904 0.2151 0.0147  0.0018  0.0276  371 PRO   B C     
11860 O  O     . PRO   B 346 ? 0.2746 0.2144 0.2300 0.0499  0.0184  0.0264  371 PRO   B O     
11861 C  CB    . PRO   B 346 ? 0.1712 0.2098 0.2280 -0.0031 0.0296  0.0180  371 PRO   B CB    
11862 C  CG    . PRO   B 346 ? 0.2100 0.1879 0.2504 -0.0001 0.0333  0.0158  371 PRO   B CG    
11863 C  CD    . PRO   B 346 ? 0.2119 0.1758 0.2601 -0.0140 0.0205  0.0159  371 PRO   B CD    
11871 N  N     . THR   B 347 ? 0.2495 0.1904 0.2019 0.0076  -0.0036 0.0160  372 THR   B N     
11872 C  CA    . THR   B 347 ? 0.2088 0.2003 0.2036 0.0044  -0.0211 0.0022  372 THR   B CA    
11873 C  C     . THR   B 347 ? 0.1645 0.2050 0.2008 0.0002  -0.0311 0.0060  372 THR   B C     
11874 O  O     . THR   B 347 ? 0.1733 0.2016 0.2130 -0.0022 -0.0107 0.0087  372 THR   B O     
11875 C  CB    . THR   B 347 ? 0.2098 0.2146 0.2043 0.0032  -0.0381 0.0166  372 THR   B CB    
11876 O  OG1   . THR   B 347 ? 0.2309 0.2171 0.2213 -0.0194 -0.0307 0.0100  372 THR   B OG1   
11877 C  CG2   . THR   B 347 ? 0.2227 0.2302 0.2116 0.0184  -0.0313 0.0120  372 THR   B CG2   
11885 N  N     . PHE   B 348 ? 0.1827 0.2073 0.2031 -0.0068 -0.0072 0.0107  373 PHE   B N     
11886 C  CA    . PHE   B 348 ? 0.1506 0.2089 0.2092 -0.0102 -0.0093 -0.0053 373 PHE   B CA    
11887 C  C     . PHE   B 348 ? 0.1944 0.2107 0.2302 -0.0141 -0.0049 0.0064  373 PHE   B C     
11888 O  O     . PHE   B 348 ? 0.1843 0.2226 0.2723 0.0079  -0.0309 0.0044  373 PHE   B O     
11889 C  CB    . PHE   B 348 ? 0.1451 0.1915 0.2164 0.0037  0.0123  -0.0064 373 PHE   B CB    
11890 C  CG    . PHE   B 348 ? 0.1559 0.1899 0.2174 -0.0007 0.0252  -0.0128 373 PHE   B CG    
11891 C  CD1   . PHE   B 348 ? 0.1762 0.2169 0.2281 0.0014  0.0319  -0.0056 373 PHE   B CD1   
11892 C  CD2   . PHE   B 348 ? 0.1805 0.2023 0.2376 -0.0230 0.0333  -0.0068 373 PHE   B CD2   
11893 C  CE1   . PHE   B 348 ? 0.1959 0.2123 0.2354 -0.0057 0.0052  -0.0066 373 PHE   B CE1   
11894 C  CE2   . PHE   B 348 ? 0.1593 0.2123 0.2358 -0.0024 0.0291  0.0037  373 PHE   B CE2   
11895 C  CZ    . PHE   B 348 ? 0.1670 0.2118 0.2347 0.0057  0.0264  0.0090  373 PHE   B CZ    
11905 N  N     . ASP   B 349 ? 0.1558 0.2202 0.2291 -0.0070 0.0082  0.0029  374 ASP   B N     
11906 C  CA    . ASP   B 349 ? 0.1748 0.2375 0.2587 0.0436  0.0042  0.0101  374 ASP   B CA    
11907 C  C     . ASP   B 349 ? 0.1929 0.2255 0.2830 0.0054  0.0084  0.0116  374 ASP   B C     
11908 O  O     . ASP   B 349 ? 0.2363 0.2385 0.3181 0.0058  0.0125  0.0104  374 ASP   B O     
11909 C  CB    . ASP   B 349 ? 0.2352 0.2590 0.2898 0.0506  0.0407  -0.0114 374 ASP   B CB    
11910 C  CG    . ASP   B 349 ? 0.2852 0.2654 0.3328 0.0172  -0.0032 0.0008  374 ASP   B CG    
11911 O  OD1   . ASP   B 349 ? 0.2936 0.2430 0.3717 -0.0154 -0.0205 0.0046  374 ASP   B OD1   
11912 O  OD2   . ASP   B 349 ? 0.2980 0.2962 0.3176 0.0026  -0.0092 -0.0163 374 ASP   B OD2   
11917 N  N     . SER   B 350 ? 0.1781 0.2129 0.2571 0.0097  -0.0021 0.0064  375 SER   B N     
11918 C  CA    . SER   B 350 ? 0.2125 0.2024 0.2400 0.0138  -0.0083 0.0053  375 SER   B CA    
11919 C  C     . SER   B 350 ? 0.2097 0.1912 0.2078 0.0272  -0.0099 0.0269  375 SER   B C     
11920 O  O     . SER   B 350 ? 0.1931 0.1945 0.2045 0.0000  0.0033  0.0106  375 SER   B O     
11921 C  CB    . SER   B 350 ? 0.2961 0.2651 0.2860 0.0335  -0.0207 -0.0302 375 SER   B CB    
11922 O  OG    . SER   B 350 ? 0.3333 0.2940 0.3346 -0.0304 0.0084  -0.0456 375 SER   B OG    
11928 N  N     . GLN   B 351 ? 0.2411 0.1953 0.1989 0.0207  0.0113  0.0118  376 GLN   B N     
11929 C  CA    . GLN   B 351 ? 0.2569 0.1856 0.2038 0.0219  0.0226  0.0048  376 GLN   B CA    
11930 C  C     . GLN   B 351 ? 0.2324 0.1707 0.2161 0.0313  0.0529  0.0072  376 GLN   B C     
11931 O  O     . GLN   B 351 ? 0.2493 0.1999 0.2411 0.0143  0.0758  0.0049  376 GLN   B O     
11932 C  CB    . GLN   B 351 ? 0.2785 0.1947 0.2030 0.0010  0.0499  0.0023  376 GLN   B CB    
11933 C  CG    . GLN   B 351 ? 0.3073 0.2166 0.2234 0.0070  0.0725  -0.0030 376 GLN   B CG    
11934 C  CD    . GLN   B 351 ? 0.3283 0.2372 0.2349 -0.0241 0.0896  -0.0072 376 GLN   B CD    
11935 O  OE1   . GLN   B 351 ? 0.3713 0.2601 0.2357 -0.0456 0.0752  -0.0161 376 GLN   B OE1   
11936 N  NE2   . GLN   B 351 ? 0.3247 0.2229 0.2395 0.0015  0.1288  -0.0047 376 GLN   B NE2   
11945 N  N     . THR   B 352 ? 0.2228 0.1849 0.2148 -0.0131 0.0474  0.0181  377 THR   B N     
11946 C  CA    . THR   B 352 ? 0.1836 0.2069 0.2403 -0.0171 0.0354  -0.0007 377 THR   B CA    
11947 C  C     . THR   B 352 ? 0.1930 0.2046 0.2240 -0.0425 0.0228  0.0166  377 THR   B C     
11948 O  O     . THR   B 352 ? 0.1966 0.2540 0.2336 -0.0405 0.0183  0.0239  377 THR   B O     
11949 C  CB    . THR   B 352 ? 0.1965 0.2087 0.2915 0.0002  0.0545  -0.0058 377 THR   B CB    
11950 O  OG1   . THR   B 352 ? 0.1857 0.2456 0.3269 -0.0268 0.0314  -0.0350 377 THR   B OG1   
11951 C  CG2   . THR   B 352 ? 0.2405 0.2254 0.3094 -0.0178 0.0544  0.0036  377 THR   B CG2   
11959 N  N     . LYS   B 353 ? 0.1845 0.1956 0.2208 -0.0031 0.0289  0.0146  378 LYS   B N     
11960 C  CA    A LYS   B 353 ? 0.1556 0.1981 0.2317 -0.0215 0.0299  0.0236  378 LYS   B CA    
11961 C  CA    B LYS   B 353 ? 0.1578 0.1911 0.2184 -0.0064 0.0289  0.0040  378 LYS   B CA    
11962 C  C     . LYS   B 353 ? 0.1467 0.2092 0.2396 -0.0133 0.0236  0.0102  378 LYS   B C     
11963 O  O     . LYS   B 353 ? 0.1724 0.2383 0.2521 0.0239  -0.0005 0.0002  378 LYS   B O     
11964 C  CB    A LYS   B 353 ? 0.1408 0.1988 0.2367 -0.0411 0.0416  0.0421  378 LYS   B CB    
11965 C  CB    B LYS   B 353 ? 0.1822 0.2078 0.2063 0.0055  0.0453  -0.0170 378 LYS   B CB    
11966 C  CG    A LYS   B 353 ? 0.1491 0.1858 0.2445 -0.0436 0.0457  0.0559  378 LYS   B CG    
11967 C  CG    B LYS   B 353 ? 0.2425 0.1810 0.2117 0.0302  0.0511  -0.0192 378 LYS   B CG    
11968 C  CD    A LYS   B 353 ? 0.1757 0.1944 0.2597 -0.0262 0.0557  0.0628  378 LYS   B CD    
11969 C  CD    B LYS   B 353 ? 0.3669 0.2015 0.2497 0.0557  0.0579  -0.0265 378 LYS   B CD    
11970 C  CE    A LYS   B 353 ? 0.2623 0.1736 0.2619 -0.0061 0.0437  0.0733  378 LYS   B CE    
11971 C  CE    B LYS   B 353 ? 0.4644 0.1778 0.2495 0.0597  0.0603  -0.0618 378 LYS   B CE    
11972 N  NZ    A LYS   B 353 ? 0.2952 0.1520 0.2583 0.0387  0.0340  0.0994  378 LYS   B NZ    
11973 N  NZ    B LYS   B 353 ? 0.5175 0.1749 0.2520 0.0340  0.0646  -0.0577 378 LYS   B NZ    
12000 N  N     . GLU   B 354 ? 0.1564 0.2071 0.2377 0.0120  0.0217  0.0053  379 GLU   B N     
12001 C  CA    . GLU   B 354 ? 0.1450 0.2259 0.2279 0.0067  0.0195  -0.0069 379 GLU   B CA    
12002 C  C     . GLU   B 354 ? 0.1679 0.2191 0.2080 -0.0167 0.0184  0.0042  379 GLU   B C     
12003 O  O     . GLU   B 354 ? 0.1538 0.2491 0.2041 -0.0110 -0.0079 -0.0075 379 GLU   B O     
12004 C  CB    . GLU   B 354 ? 0.1623 0.2456 0.2679 0.0014  0.0003  0.0019  379 GLU   B CB    
12005 C  CG    . GLU   B 354 ? 0.2013 0.2555 0.3316 -0.0329 0.0438  -0.0154 379 GLU   B CG    
12006 C  CD    . GLU   B 354 ? 0.3191 0.3245 0.4179 -0.0023 0.1120  -0.0225 379 GLU   B CD    
12007 O  OE1   . GLU   B 354 ? 0.4003 0.3402 0.4508 0.0190  0.1985  -0.0304 379 GLU   B OE1   
12008 O  OE2   . GLU   B 354 ? 0.4011 0.3315 0.4533 -0.0311 0.0934  -0.0103 379 GLU   B OE2   
12015 N  N     . ASN   B 355 ? 0.1797 0.1983 0.2063 0.0050  0.0258  -0.0038 380 ASN   B N     
12016 C  CA    . ASN   B 355 ? 0.1227 0.2014 0.2089 0.0197  0.0216  -0.0059 380 ASN   B CA    
12017 C  C     . ASN   B 355 ? 0.1574 0.2044 0.2094 -0.0287 0.0047  -0.0065 380 ASN   B C     
12018 O  O     . ASN   B 355 ? 0.1727 0.2104 0.2120 -0.0041 -0.0246 0.0038  380 ASN   B O     
12019 C  CB    . ASN   B 355 ? 0.1270 0.2242 0.2341 -0.0032 0.0326  0.0089  380 ASN   B CB    
12020 C  CG    . ASN   B 355 ? 0.1734 0.3178 0.2716 0.0470  0.0430  0.0362  380 ASN   B CG    
12021 O  OD1   . ASN   B 355 ? 0.2193 0.3798 0.3108 0.0547  0.0566  0.0684  380 ASN   B OD1   
12022 N  ND2   . ASN   B 355 ? 0.2169 0.3525 0.2911 0.0028  0.0500  0.0329  380 ASN   B ND2   
12029 N  N     . MET   B 356 ? 0.1661 0.1995 0.2027 -0.0017 -0.0064 -0.0049 381 MET   B N     
12030 C  CA    . MET   B 356 ? 0.1625 0.1835 0.2115 0.0027  -0.0102 0.0114  381 MET   B CA    
12031 C  C     . MET   B 356 ? 0.1662 0.1982 0.2024 -0.0307 -0.0163 0.0160  381 MET   B C     
12032 O  O     . MET   B 356 ? 0.1631 0.2512 0.2055 -0.0467 -0.0104 0.0455  381 MET   B O     
12033 C  CB    . MET   B 356 ? 0.1759 0.1889 0.2310 0.0293  0.0191  0.0106  381 MET   B CB    
12034 C  CG    . MET   B 356 ? 0.1645 0.2020 0.2505 0.0115  0.0304  0.0199  381 MET   B CG    
12035 S  SD    . MET   B 356 ? 0.1870 0.2258 0.2505 -0.0035 -0.0098 0.0237  381 MET   B SD    
12036 C  CE    . MET   B 356 ? 0.2372 0.2208 0.2448 0.0037  -0.0236 0.0449  381 MET   B CE    
12046 N  N     . THR   B 357 ? 0.1423 0.2120 0.1993 0.0074  -0.0159 0.0143  382 THR   B N     
12047 C  CA    . THR   B 357 ? 0.1300 0.2421 0.2090 -0.0166 -0.0212 0.0128  382 THR   B CA    
12048 C  C     . THR   B 357 ? 0.1213 0.2488 0.2278 -0.0103 -0.0067 0.0420  382 THR   B C     
12049 O  O     . THR   B 357 ? 0.1549 0.2565 0.2401 -0.0199 -0.0121 0.0499  382 THR   B O     
12050 C  CB    . THR   B 357 ? 0.1738 0.2438 0.2005 -0.0215 -0.0243 0.0004  382 THR   B CB    
12051 O  OG1   . THR   B 357 ? 0.2021 0.2574 0.1922 -0.0015 -0.0273 0.0080  382 THR   B OG1   
12052 C  CG2   . THR   B 357 ? 0.1709 0.2527 0.2114 0.0058  -0.0298 0.0067  382 THR   B CG2   
12060 N  N     . LEU   B 358 ? 0.1300 0.2394 0.2355 -0.0226 -0.0143 0.0347  383 LEU   B N     
12061 C  CA    . LEU   B 358 ? 0.1453 0.2415 0.2449 -0.0209 -0.0373 0.0452  383 LEU   B CA    
12062 C  C     . LEU   B 358 ? 0.2018 0.2340 0.2585 -0.0337 -0.0145 0.0528  383 LEU   B C     
12063 O  O     . LEU   B 358 ? 0.1857 0.2420 0.2768 -0.0386 -0.0291 0.0337  383 LEU   B O     
12064 C  CB    . LEU   B 358 ? 0.1766 0.2056 0.2677 -0.0195 -0.0414 0.0204  383 LEU   B CB    
12065 C  CG    . LEU   B 358 ? 0.1846 0.1933 0.2821 -0.0121 -0.0300 0.0088  383 LEU   B CG    
12066 C  CD1   . LEU   B 358 ? 0.2591 0.2197 0.2986 -0.0038 -0.0594 -0.0047 383 LEU   B CD1   
12067 C  CD2   . LEU   B 358 ? 0.2178 0.2177 0.2843 -0.0067 -0.0226 0.0142  383 LEU   B CD2   
12079 N  N     . GLN   B 359 ? 0.1843 0.2520 0.2620 -0.0257 -0.0043 0.0622  384 GLN   B N     
12080 C  CA    . GLN   B 359 ? 0.1836 0.2646 0.2713 -0.0368 0.0156  0.0579  384 GLN   B CA    
12081 C  C     . GLN   B 359 ? 0.1946 0.2848 0.2710 -0.0306 0.0177  0.0767  384 GLN   B C     
12082 O  O     . GLN   B 359 ? 0.2037 0.2572 0.2749 -0.0280 -0.0033 0.0661  384 GLN   B O     
12083 C  CB    . GLN   B 359 ? 0.1880 0.2893 0.3075 -0.0048 0.0036  0.0605  384 GLN   B CB    
12084 C  CG    . GLN   B 359 ? 0.2476 0.3289 0.3497 0.0108  0.0123  0.0702  384 GLN   B CG    
12085 C  CD    . GLN   B 359 ? 0.2674 0.4001 0.4006 0.0433  -0.0076 0.0754  384 GLN   B CD    
12086 O  OE1   . GLN   B 359 ? 0.2579 0.4380 0.4151 0.0511  0.0023  0.0644  384 GLN   B OE1   
12087 N  NE2   . GLN   B 359 ? 0.2870 0.4266 0.4302 0.0148  -0.0141 0.0827  384 GLN   B NE2   
12096 N  N     . PRO   B 360 ? 0.1904 0.3188 0.2970 -0.0192 -0.0191 0.0987  385 PRO   B N     
12097 C  CA    . PRO   B 360 ? 0.2433 0.3439 0.3198 0.0105  -0.0094 0.1094  385 PRO   B CA    
12098 C  C     . PRO   B 360 ? 0.2334 0.3049 0.3574 -0.0013 -0.0104 0.1167  385 PRO   B C     
12099 O  O     . PRO   B 360 ? 0.2722 0.3141 0.3631 -0.0230 -0.0056 0.0973  385 PRO   B O     
12100 C  CB    . PRO   B 360 ? 0.2873 0.3852 0.3287 0.0313  -0.0204 0.1047  385 PRO   B CB    
12101 C  CG    . PRO   B 360 ? 0.2574 0.3845 0.3283 0.0366  -0.0197 0.0954  385 PRO   B CG    
12102 C  CD    . PRO   B 360 ? 0.2202 0.3481 0.3173 0.0135  -0.0062 0.1025  385 PRO   B CD    
12110 N  N     . LYS   B 361 ? 0.2404 0.3044 0.4019 -0.0233 0.0079  0.1135  386 LYS   B N     
12111 C  CA    . LYS   B 361 ? 0.2822 0.3028 0.4553 -0.0527 0.0145  0.1111  386 LYS   B CA    
12112 C  C     . LYS   B 361 ? 0.2967 0.2772 0.4667 -0.0577 -0.0391 0.0880  386 LYS   B C     
12113 O  O     . LYS   B 361 ? 0.3415 0.2692 0.4982 -0.0847 -0.0208 0.0972  386 LYS   B O     
12114 C  CB    . LYS   B 361 ? 0.2974 0.3574 0.4959 -0.0527 0.0165  0.0940  386 LYS   B CB    
12115 C  CG    . LYS   B 361 ? 0.2531 0.4306 0.5298 -0.0736 0.0054  0.0679  386 LYS   B CG    
12116 C  CD    . LYS   B 361 ? 0.3337 0.5061 0.5635 -0.0839 0.0345  0.0714  386 LYS   B CD    
12117 C  CE    . LYS   B 361 ? 0.4651 0.5998 0.5969 -0.0487 0.0587  0.0483  386 LYS   B CE    
12118 N  NZ    . LYS   B 361 ? 0.5391 0.6538 0.6210 -0.0250 0.0805  0.0418  386 LYS   B NZ    
12132 N  N     . SER   B 362 ? 0.2457 0.2415 0.4341 -0.0308 -0.0663 0.0798  387 SER   B N     
12133 C  CA    . SER   B 362 ? 0.2561 0.2537 0.4069 -0.0579 -0.0887 0.0502  387 SER   B CA    
12134 C  C     . SER   B 362 ? 0.2580 0.2328 0.3630 -0.0419 -0.0865 0.0335  387 SER   B C     
12135 O  O     . SER   B 362 ? 0.3011 0.2309 0.3455 -0.0393 -0.0835 0.0282  387 SER   B O     
12136 C  CB    . SER   B 362 ? 0.1779 0.3062 0.4167 -0.0685 -0.1010 0.0655  387 SER   B CB    
12137 O  OG    . SER   B 362 ? 0.2455 0.3638 0.4269 -0.0894 -0.1061 0.0825  387 SER   B OG    
12143 N  N     . PHE   B 363 ? 0.2251 0.2563 0.3378 -0.0475 -0.0731 0.0459  388 PHE   B N     
12144 C  CA    . PHE   B 363 ? 0.2111 0.2425 0.3138 -0.0444 -0.0541 0.0516  388 PHE   B CA    
12145 C  C     . PHE   B 363 ? 0.2246 0.2488 0.3025 -0.0255 -0.0315 0.0505  388 PHE   B C     
12146 O  O     . PHE   B 363 ? 0.2229 0.2606 0.2859 0.0031  -0.0191 0.0504  388 PHE   B O     
12147 C  CB    . PHE   B 363 ? 0.2110 0.2576 0.3019 -0.0103 -0.0394 0.0370  388 PHE   B CB    
12148 C  CG    . PHE   B 363 ? 0.1989 0.2517 0.3030 0.0034  -0.0279 0.0420  388 PHE   B CG    
12149 C  CD1   . PHE   B 363 ? 0.1841 0.2467 0.3077 -0.0049 -0.0247 0.0485  388 PHE   B CD1   
12150 C  CD2   . PHE   B 363 ? 0.2205 0.2814 0.3071 0.0185  -0.0425 0.0458  388 PHE   B CD2   
12151 C  CE1   . PHE   B 363 ? 0.2021 0.2885 0.3172 -0.0305 -0.0326 0.0450  388 PHE   B CE1   
12152 C  CE2   . PHE   B 363 ? 0.2305 0.2691 0.3063 0.0212  -0.0638 0.0258  388 PHE   B CE2   
12153 C  CZ    . PHE   B 363 ? 0.1904 0.2932 0.3118 -0.0268 -0.0263 0.0431  388 PHE   B CZ    
12163 N  N     . GLY   B 364 ? 0.2675 0.2369 0.3206 -0.0042 -0.0339 0.0410  389 GLY   B N     
12164 C  CA    . GLY   B 364 ? 0.2753 0.2544 0.3334 0.0084  -0.0531 0.0207  389 GLY   B CA    
12165 C  C     . GLY   B 364 ? 0.3040 0.2491 0.3380 0.0165  -0.0508 0.0185  389 GLY   B C     
12166 O  O     . GLY   B 364 ? 0.3370 0.2834 0.3454 0.0427  -0.0394 -0.0023 389 GLY   B O     
12170 N  N     . SER   B 365 ? 0.2968 0.2226 0.3282 -0.0040 -0.0716 0.0527  390 SER   B N     
12171 C  CA    . SER   B 365 ? 0.3344 0.2506 0.3452 0.0316  -0.0690 0.0682  390 SER   B CA    
12172 C  C     . SER   B 365 ? 0.3241 0.2863 0.3464 0.0283  -0.0672 0.0949  390 SER   B C     
12173 O  O     . SER   B 365 ? 0.2516 0.3193 0.3480 0.0031  -0.0643 0.0886  390 SER   B O     
12174 C  CB    . SER   B 365 ? 0.3325 0.2237 0.3577 0.0153  -0.0572 0.0434  390 SER   B CB    
12175 O  OG    . SER   B 365 ? 0.3252 0.2267 0.3715 -0.0317 -0.0711 0.0223  390 SER   B OG    
12181 N  N     . THR   B 366 ? 0.3806 0.2984 0.3465 0.0033  -0.0780 0.1035  391 THR   B N     
12182 C  CA    . THR   B 366 ? 0.3848 0.3295 0.3576 -0.0048 -0.0956 0.1024  391 THR   B CA    
12183 C  C     . THR   B 366 ? 0.3500 0.3397 0.3431 0.0078  -0.0837 0.1036  391 THR   B C     
12184 O  O     . THR   B 366 ? 0.3561 0.3728 0.3549 0.0135  -0.0783 0.0695  391 THR   B O     
12185 C  CB    . THR   B 366 ? 0.4162 0.3697 0.3882 -0.0204 -0.1303 0.1025  391 THR   B CB    
12186 O  OG1   . THR   B 366 ? 0.4520 0.3675 0.4116 -0.0262 -0.1313 0.1206  391 THR   B OG1   
12187 C  CG2   . THR   B 366 ? 0.4233 0.4180 0.3933 -0.0330 -0.1187 0.1058  391 THR   B CG2   
12195 N  N     . CYS   B 367 ? 0.3276 0.3292 0.3251 -0.0082 -0.0714 0.0950  392 CYS   B N     
12196 C  CA    . CYS   B 367 ? 0.3680 0.3491 0.3348 -0.0226 -0.0778 0.0937  392 CYS   B CA    
12197 C  C     . CYS   B 367 ? 0.4300 0.3908 0.3457 -0.0313 -0.0875 0.0885  392 CYS   B C     
12198 O  O     . CYS   B 367 ? 0.4636 0.4188 0.3406 -0.0002 -0.0425 0.0967  392 CYS   B O     
12199 C  CB    . CYS   B 367 ? 0.3358 0.3516 0.3499 -0.0225 -0.0925 0.0767  392 CYS   B CB    
12200 S  SG    . CYS   B 367 ? 0.3180 0.3601 0.3734 0.0161  -0.0964 0.0682  392 CYS   B SG    
12206 N  N     . GLN   B 368 ? 0.4266 0.4036 0.3633 -0.0590 -0.1419 0.1021  393 GLN   B N     
12207 C  CA    . GLN   B 368 ? 0.4300 0.3970 0.4049 -0.1119 -0.1709 0.0903  393 GLN   B CA    
12208 C  C     . GLN   B 368 ? 0.4002 0.3707 0.3937 -0.0721 -0.1498 0.0844  393 GLN   B C     
12209 O  O     . GLN   B 368 ? 0.4467 0.3667 0.3993 -0.0287 -0.1622 0.0391  393 GLN   B O     
12210 C  CB    . GLN   B 368 ? 0.5003 0.4450 0.4724 -0.1641 -0.1985 0.0748  393 GLN   B CB    
12211 C  CG    . GLN   B 368 ? 0.6146 0.5414 0.5522 -0.1538 -0.1854 0.0475  393 GLN   B CG    
12212 C  CD    . GLN   B 368 ? 0.7100 0.6283 0.6250 -0.1062 -0.1906 0.0183  393 GLN   B CD    
12213 O  OE1   . GLN   B 368 ? 0.7249 0.6846 0.6488 -0.1043 -0.1965 -0.0027 393 GLN   B OE1   
12214 N  NE2   . GLN   B 368 ? 0.7591 0.6296 0.6509 -0.0672 -0.1928 0.0121  393 GLN   B NE2   
12223 N  N     . LEU   B 369 ? 0.3605 0.3555 0.3825 -0.0609 -0.1415 0.1019  394 LEU   B N     
12224 C  CA    . LEU   B 369 ? 0.3824 0.3495 0.3923 -0.0672 -0.1550 0.1117  394 LEU   B CA    
12225 C  C     . LEU   B 369 ? 0.4059 0.3503 0.3939 -0.0588 -0.1727 0.1164  394 LEU   B C     
12226 O  O     . LEU   B 369 ? 0.4373 0.3661 0.3994 -0.0504 -0.1640 0.1136  394 LEU   B O     
12227 C  CB    . LEU   B 369 ? 0.3807 0.3477 0.3901 -0.0634 -0.1672 0.1186  394 LEU   B CB    
12228 C  CG    . LEU   B 369 ? 0.3918 0.3682 0.3957 -0.0781 -0.1479 0.1043  394 LEU   B CG    
12229 C  CD1   . LEU   B 369 ? 0.3920 0.3788 0.3852 -0.0671 -0.1784 0.0712  394 LEU   B CD1   
12230 C  CD2   . LEU   B 369 ? 0.4135 0.3857 0.4123 -0.0840 -0.0928 0.1124  394 LEU   B CD2   
12242 N  N     . SER   B 370 ? 0.4155 0.3532 0.3993 -0.0170 -0.1898 0.1282  395 SER   B N     
12243 C  CA    . SER   B 370 ? 0.4411 0.3928 0.4152 0.0005  -0.1924 0.1153  395 SER   B CA    
12244 C  C     . SER   B 370 ? 0.4666 0.4069 0.4166 -0.0095 -0.1946 0.1357  395 SER   B C     
12245 O  O     . SER   B 370 ? 0.4490 0.4003 0.4040 -0.0190 -0.1952 0.1255  395 SER   B O     
12246 C  CB    . SER   B 370 ? 0.4220 0.4034 0.4272 0.0025  -0.1797 0.0836  395 SER   B CB    
12247 O  OG    . SER   B 370 ? 0.4291 0.3943 0.4310 0.0022  -0.1756 0.0807  395 SER   B OG    
12253 N  N     . GLU   B 371 ? 0.4876 0.4141 0.4292 -0.0425 -0.1932 0.1561  396 GLU   B N     
12254 C  CA    . GLU   B 371 ? 0.5317 0.4565 0.4504 -0.0732 -0.1908 0.1767  396 GLU   B CA    
12255 C  C     . GLU   B 371 ? 0.5405 0.4563 0.4413 -0.0776 -0.2135 0.1700  396 GLU   B C     
12256 O  O     . GLU   B 371 ? 0.5459 0.4761 0.4332 -0.0984 -0.2205 0.1449  396 GLU   B O     
12257 C  CB    . GLU   B 371 ? 0.6167 0.5344 0.4892 -0.0782 -0.1516 0.1798  396 GLU   B CB    
12258 C  CG    . GLU   B 371 ? 0.6878 0.6182 0.5223 -0.1034 -0.1157 0.1781  396 GLU   B CG    
12259 C  CD    . GLU   B 371 ? 0.7849 0.7025 0.5555 -0.1087 -0.0610 0.1800  396 GLU   B CD    
12260 O  OE1   . GLU   B 371 ? 0.8208 0.7268 0.5778 -0.1253 -0.0222 0.1831  396 GLU   B OE1   
12261 O  OE2   . GLU   B 371 ? 0.8226 0.7428 0.5648 -0.1026 -0.0564 0.1704  396 GLU   B OE2   
12268 N  N     . LYS   B 372 ? 0.5256 0.4499 0.4463 -0.0484 -0.2254 0.1755  397 LYS   B N     
12269 C  CA    . LYS   B 372 ? 0.5328 0.4646 0.4648 -0.0288 -0.2058 0.1493  397 LYS   B CA    
12270 C  C     . LYS   B 372 ? 0.4751 0.4398 0.4321 -0.0289 -0.2275 0.1331  397 LYS   B C     
12271 O  O     . LYS   B 372 ? 0.5091 0.4570 0.4273 -0.0641 -0.2387 0.1226  397 LYS   B O     
12272 C  CB    . LYS   B 372 ? 0.5856 0.4995 0.5085 0.0148  -0.1730 0.1479  397 LYS   B CB    
12273 C  CG    . LYS   B 372 ? 0.6914 0.5575 0.5466 0.0114  -0.1095 0.1314  397 LYS   B CG    
12274 C  CD    . LYS   B 372 ? 0.7670 0.6211 0.5712 0.0243  -0.0645 0.1213  397 LYS   B CD    
12275 C  CE    . LYS   B 372 ? 0.8108 0.6744 0.5916 0.0252  -0.0402 0.1102  397 LYS   B CE    
12276 N  NZ    . LYS   B 372 ? 0.8428 0.7088 0.6045 0.0172  -0.0273 0.1037  397 LYS   B NZ    
12290 N  N     . PHE   B 373 ? 0.4211 0.3994 0.4101 -0.0191 -0.2157 0.1299  398 PHE   B N     
12291 C  CA    . PHE   B 373 ? 0.4131 0.3878 0.3950 -0.0256 -0.2071 0.1094  398 PHE   B CA    
12292 C  C     . PHE   B 373 ? 0.4030 0.4075 0.3821 -0.0338 -0.2020 0.0860  398 PHE   B C     
12293 O  O     . PHE   B 373 ? 0.4211 0.3815 0.3894 -0.0095 -0.2113 0.0735  398 PHE   B O     
12294 C  CB    . PHE   B 373 ? 0.3925 0.3760 0.3925 0.0051  -0.2004 0.1168  398 PHE   B CB    
12295 C  CG    . PHE   B 373 ? 0.3841 0.3646 0.4060 -0.0119 -0.1790 0.1086  398 PHE   B CG    
12296 C  CD1   . PHE   B 373 ? 0.3663 0.3840 0.4058 -0.0378 -0.1794 0.0988  398 PHE   B CD1   
12297 C  CD2   . PHE   B 373 ? 0.3923 0.3558 0.4170 -0.0120 -0.1552 0.1129  398 PHE   B CD2   
12298 C  CE1   . PHE   B 373 ? 0.3405 0.4007 0.4045 -0.0360 -0.1885 0.1009  398 PHE   B CE1   
12299 C  CE2   . PHE   B 373 ? 0.3967 0.3815 0.4187 -0.0280 -0.1604 0.1056  398 PHE   B CE2   
12300 C  CZ    . PHE   B 373 ? 0.3894 0.3896 0.4139 -0.0488 -0.1662 0.0993  398 PHE   B CZ    
12310 N  N     . ILE   B 374 ? 0.4136 0.4542 0.3697 -0.0451 -0.1701 0.0782  399 ILE   B N     
12311 C  CA    . ILE   B 374 ? 0.4431 0.4948 0.3594 -0.0309 -0.1508 0.0929  399 ILE   B CA    
12312 C  C     . ILE   B 374 ? 0.4819 0.4989 0.3637 -0.0172 -0.1505 0.0737  399 ILE   B C     
12313 O  O     . ILE   B 374 ? 0.4804 0.4698 0.3514 0.0119  -0.1439 0.0471  399 ILE   B O     
12314 C  CB    . ILE   B 374 ? 0.4647 0.5177 0.3538 -0.0465 -0.1092 0.1186  399 ILE   B CB    
12315 C  CG1   . ILE   B 374 ? 0.4374 0.5136 0.3533 -0.0603 -0.1052 0.1386  399 ILE   B CG1   
12316 C  CG2   . ILE   B 374 ? 0.4969 0.5339 0.3553 -0.0369 -0.0793 0.1264  399 ILE   B CG2   
12317 C  CD1   . ILE   B 374 ? 0.4307 0.5280 0.3488 -0.0794 -0.0882 0.1399  399 ILE   B CD1   
12329 N  N     . LYS   B 375 ? 0.4827 0.5145 0.3692 0.0072  -0.1842 0.0839  400 LYS   B N     
12330 C  CA    . LYS   B 375 ? 0.5035 0.5388 0.3883 0.0080  -0.1737 0.0907  400 LYS   B CA    
12331 C  C     . LYS   B 375 ? 0.4806 0.5493 0.3892 0.0175  -0.1646 0.0816  400 LYS   B C     
12332 O  O     . LYS   B 375 ? 0.5077 0.5562 0.4003 0.0213  -0.1506 0.0618  400 LYS   B O     
12333 C  CB    . LYS   B 375 ? 0.5927 0.5633 0.4213 0.0126  -0.1407 0.1046  400 LYS   B CB    
12334 C  CG    . LYS   B 375 ? 0.6531 0.5996 0.4589 0.0531  -0.1215 0.1119  400 LYS   B CG    
12335 C  CD    . LYS   B 375 ? 0.6934 0.6211 0.4945 0.0857  -0.1192 0.1156  400 LYS   B CD    
12336 C  CE    . LYS   B 375 ? 0.7386 0.6328 0.5188 0.0864  -0.1212 0.1183  400 LYS   B CE    
12337 N  NZ    . LYS   B 375 ? 0.7529 0.6352 0.5318 0.0703  -0.1314 0.1185  400 LYS   B NZ    
12351 N  N     . ALA   B 376 ? 0.4057 0.5335 0.3826 0.0204  -0.1687 0.1009  401 ALA   B N     
12352 C  CA    . ALA   B 376 ? 0.4052 0.5165 0.3822 -0.0068 -0.1733 0.0947  401 ALA   B CA    
12353 C  C     . ALA   B 376 ? 0.4503 0.5294 0.3822 -0.0253 -0.1863 0.0803  401 ALA   B C     
12354 O  O     . ALA   B 376 ? 0.4645 0.5411 0.4093 -0.0423 -0.1936 0.0734  401 ALA   B O     
12355 C  CB    . ALA   B 376 ? 0.3454 0.4989 0.3753 0.0054  -0.1643 0.1018  401 ALA   B CB    
12361 N  N     . ALA   B 377 ? 0.4527 0.5270 0.3625 -0.0215 -0.1822 0.0695  402 ALA   B N     
12362 C  CA    . ALA   B 377 ? 0.5089 0.5199 0.3481 -0.0035 -0.1882 0.0482  402 ALA   B CA    
12363 C  C     . ALA   B 377 ? 0.6074 0.5394 0.3562 0.0153  -0.1800 0.0389  402 ALA   B C     
12364 O  O     . ALA   B 377 ? 0.6302 0.5264 0.3729 0.0235  -0.1941 0.0351  402 ALA   B O     
12365 C  CB    . ALA   B 377 ? 0.4933 0.5008 0.3427 0.0003  -0.2063 0.0387  402 ALA   B CB    
12371 N  N     . ILE   B 378 ? 0.6627 0.5716 0.3403 0.0347  -0.1738 0.0463  403 ILE   B N     
12372 C  CA    . ILE   B 378 ? 0.7211 0.6264 0.3476 0.0320  -0.1787 0.0398  403 ILE   B CA    
12373 C  C     . ILE   B 378 ? 0.7456 0.6443 0.3694 0.0578  -0.2222 0.0155  403 ILE   B C     
12374 O  O     . ILE   B 378 ? 0.7834 0.6616 0.3684 0.0567  -0.2085 0.0092  403 ILE   B O     
12375 C  CB    . ILE   B 378 ? 0.7455 0.6697 0.3354 0.0045  -0.1355 0.0659  403 ILE   B CB    
12376 C  CG1   . ILE   B 378 ? 0.7665 0.6815 0.3566 -0.0259 -0.0951 0.0896  403 ILE   B CG1   
12377 C  CG2   . ILE   B 378 ? 0.7431 0.6864 0.3153 0.0024  -0.1477 0.0749  403 ILE   B CG2   
12378 C  CD1   . ILE   B 378 ? 0.7830 0.6874 0.3668 -0.0461 -0.0675 0.0975  403 ILE   B CD1   
12390 N  N     . GLY   B 379 ? 0.7256 0.6457 0.4112 0.0802  -0.2627 -0.0102 404 GLY   B N     
12391 C  CA    . GLY   B 379 ? 0.7133 0.6628 0.4707 0.0807  -0.2893 -0.0442 404 GLY   B CA    
12392 C  C     . GLY   B 379 ? 0.6990 0.6936 0.5371 0.0793  -0.3083 -0.0680 404 GLY   B C     
12393 O  O     . GLY   B 379 ? 0.6904 0.7136 0.5536 0.0741  -0.3095 -0.0948 404 GLY   B O     
12397 N  N     . CYS   B 380 ? 0.7026 0.7061 0.5928 0.0694  -0.3098 -0.0667 405 CYS   B N     
12398 C  CA    . CYS   B 380 ? 0.7107 0.7201 0.6567 0.0550  -0.2948 -0.0595 405 CYS   B CA    
12399 C  C     . CYS   B 380 ? 0.7162 0.7408 0.6792 0.0421  -0.2666 -0.0753 405 CYS   B C     
12400 O  O     . CYS   B 380 ? 0.7350 0.7570 0.6964 0.0277  -0.2529 -0.0593 405 CYS   B O     
12401 C  CB    . CYS   B 380 ? 0.7459 0.7115 0.7037 0.0414  -0.2826 -0.0317 405 CYS   B CB    
12402 S  SG    . CYS   B 380 ? 0.7512 0.6928 0.7399 0.0177  -0.2822 -0.0178 405 CYS   B SG    
12408 N  N     . GLY   B 381 ? 0.7020 0.7409 0.6769 0.0529  -0.2541 -0.1083 406 GLY   B N     
12409 C  CA    . GLY   B 381 ? 0.6850 0.7300 0.6640 0.0702  -0.2472 -0.1267 406 GLY   B CA    
12410 C  C     . GLY   B 381 ? 0.6824 0.7098 0.6447 0.0813  -0.2350 -0.1326 406 GLY   B C     
12411 O  O     . GLY   B 381 ? 0.6857 0.6974 0.6625 0.0910  -0.2096 -0.1646 406 GLY   B O     
12415 N  N     . ILE   B 382 ? 0.6493 0.6862 0.5985 0.0703  -0.2613 -0.1016 407 ILE   B N     
12416 C  CA    . ILE   B 382 ? 0.6708 0.6730 0.5541 0.0833  -0.2576 -0.0656 407 ILE   B CA    
12417 C  C     . ILE   B 382 ? 0.7047 0.6736 0.5484 0.1146  -0.2517 -0.0585 407 ILE   B C     
12418 O  O     . ILE   B 382 ? 0.7236 0.6588 0.5469 0.1327  -0.2437 -0.0382 407 ILE   B O     
12419 C  CB    . ILE   B 382 ? 0.6590 0.6664 0.5221 0.0677  -0.2494 -0.0361 407 ILE   B CB    
12420 C  CG1   . ILE   B 382 ? 0.6390 0.6648 0.5124 0.0649  -0.2471 -0.0198 407 ILE   B CG1   
12421 C  CG2   . ILE   B 382 ? 0.6573 0.6577 0.5073 0.0611  -0.2448 -0.0231 407 ILE   B CG2   
12422 C  CD1   . ILE   B 382 ? 0.6378 0.6572 0.5095 0.0943  -0.2380 -0.0017 407 ILE   B CD1   
12434 N  N     . VAL   B 383 ? 0.7248 0.6847 0.5433 0.1192  -0.2572 -0.0744 408 VAL   B N     
12435 C  CA    . VAL   B 383 ? 0.7625 0.7200 0.5443 0.1371  -0.2621 -0.0788 408 VAL   B CA    
12436 C  C     . VAL   B 383 ? 0.7844 0.7681 0.5692 0.1606  -0.2728 -0.0684 408 VAL   B C     
12437 O  O     . VAL   B 383 ? 0.7612 0.7778 0.5605 0.1869  -0.2746 -0.0554 408 VAL   B O     
12438 C  CB    . VAL   B 383 ? 0.7739 0.7225 0.5326 0.1510  -0.2413 -0.0799 408 VAL   B CB    
12439 C  CG1   . VAL   B 383 ? 0.7855 0.7258 0.5339 0.1609  -0.2260 -0.0778 408 VAL   B CG1   
12440 C  CG2   . VAL   B 383 ? 0.7631 0.7189 0.5280 0.1397  -0.2380 -0.0816 408 VAL   B CG2   
12450 N  N     . GLU   B 384 ? 0.8081 0.8018 0.6055 0.1627  -0.2880 -0.0655 409 GLU   B N     
12451 C  CA    . GLU   B 384 ? 0.8600 0.8394 0.6565 0.1384  -0.2691 -0.0602 409 GLU   B CA    
12452 C  C     . GLU   B 384 ? 0.8998 0.8648 0.6691 0.1023  -0.2414 -0.0675 409 GLU   B C     
12453 O  O     . GLU   B 384 ? 0.9187 0.8817 0.6666 0.0956  -0.2375 -0.0682 409 GLU   B O     
12454 C  CB    . GLU   B 384 ? 0.8720 0.8593 0.6958 0.1303  -0.2723 -0.0495 409 GLU   B CB    
12455 C  CG    . GLU   B 384 ? 0.8843 0.8803 0.7378 0.1356  -0.2650 -0.0320 409 GLU   B CG    
12456 C  CD    . GLU   B 384 ? 0.9001 0.9050 0.7779 0.1504  -0.2492 -0.0125 409 GLU   B CD    
12457 O  OE1   . GLU   B 384 ? 0.9171 0.9177 0.7927 0.1458  -0.2356 -0.0093 409 GLU   B OE1   
12458 O  OE2   . GLU   B 384 ? 0.9046 0.9170 0.7933 0.1693  -0.2449 0.0000  409 GLU   B OE2   
12465 N  N     . SER   B 385 ? 0.9057 0.8670 0.6808 0.0760  -0.2230 -0.0713 410 SER   B N     
12466 C  CA    . SER   B 385 ? 0.9166 0.8627 0.6917 0.0540  -0.2016 -0.0661 410 SER   B CA    
12467 C  C     . SER   B 385 ? 0.9438 0.8503 0.6885 0.0451  -0.1656 -0.0607 410 SER   B C     
12468 O  O     . SER   B 385 ? 0.9574 0.8357 0.6944 0.0427  -0.1472 -0.0882 410 SER   B O     
12469 C  CB    . SER   B 385 ? 0.9268 0.8764 0.7052 0.0448  -0.1995 -0.0666 410 SER   B CB    
12470 O  OG    . SER   B 385 ? 0.9519 0.8982 0.7167 0.0404  -0.1911 -0.0672 410 SER   B OG    
12476 N  N     . ILE   B 386 ? 0.9383 0.8516 0.6731 0.0475  -0.1526 -0.0232 411 ILE   B N     
12477 C  CA    . ILE   B 386 ? 0.9427 0.8527 0.6647 0.0443  -0.1334 0.0134  411 ILE   B CA    
12478 C  C     . ILE   B 386 ? 0.9512 0.8634 0.6709 0.0552  -0.1319 0.0358  411 ILE   B C     
12479 O  O     . ILE   B 386 ? 0.9654 0.8591 0.6651 0.0561  -0.1260 0.0441  411 ILE   B O     
12480 C  CB    . ILE   B 386 ? 0.9345 0.8443 0.6536 0.0226  -0.1179 0.0227  411 ILE   B CB    
12481 C  CG1   . ILE   B 386 ? 0.9231 0.8351 0.6439 0.0076  -0.1104 0.0303  411 ILE   B CG1   
12482 C  CG2   . ILE   B 386 ? 0.9473 0.8474 0.6544 0.0219  -0.1059 0.0239  411 ILE   B CG2   
12483 C  CD1   . ILE   B 386 ? 0.9217 0.8302 0.6389 0.0030  -0.1063 0.0339  411 ILE   B CD1   
12495 N  N     . LEU   B 387 ? 0.9352 0.8750 0.6829 0.0663  -0.1477 0.0473  412 LEU   B N     
12496 C  CA    . LEU   B 387 ? 0.9391 0.8936 0.6996 0.0738  -0.1672 0.0458  412 LEU   B CA    
12497 C  C     . LEU   B 387 ? 0.9544 0.9209 0.7188 0.0541  -0.1663 0.0354  412 LEU   B C     
12498 O  O     . LEU   B 387 ? 0.9615 0.9248 0.7191 0.0510  -0.1661 0.0290  412 LEU   B O     
12499 C  CB    . LEU   B 387 ? 0.9298 0.8889 0.6977 0.1011  -0.1877 0.0567  412 LEU   B CB    
12500 C  CG    . LEU   B 387 ? 0.9313 0.8869 0.7021 0.1201  -0.1972 0.0653  412 LEU   B CG    
12501 C  CD1   . LEU   B 387 ? 0.9321 0.8866 0.7071 0.1201  -0.1975 0.0584  412 LEU   B CD1   
12502 C  CD2   . LEU   B 387 ? 0.9337 0.8874 0.7049 0.1327  -0.2005 0.0708  412 LEU   B CD2   
12514 N  N     . ASN   B 388 ? 0.9546 0.9425 0.7378 0.0443  -0.1643 0.0324  413 ASN   B N     
12515 C  CA    . ASN   B 388 ? 0.9628 0.9576 0.7569 0.0391  -0.1565 0.0254  413 ASN   B CA    
12516 C  C     . ASN   B 388 ? 0.9970 0.9663 0.7637 0.0540  -0.1469 0.0239  413 ASN   B C     
12517 O  O     . ASN   B 388 ? 1.0006 0.9698 0.7636 0.0550  -0.1517 0.0254  413 ASN   B O     
12518 C  CB    . ASN   B 388 ? 0.9423 0.9621 0.7686 0.0144  -0.1518 0.0222  413 ASN   B CB    
12519 C  CG    . ASN   B 388 ? 0.9320 0.9640 0.7755 -0.0032 -0.1540 0.0225  413 ASN   B CG    
12520 O  OD1   . ASN   B 388 ? 0.9307 0.9601 0.7750 -0.0070 -0.1593 0.0273  413 ASN   B OD1   
12521 N  ND2   . ASN   B 388 ? 0.9265 0.9662 0.7788 -0.0076 -0.1563 0.0182  413 ASN   B ND2   
12528 N  N     . TRP   B 389 ? 1.0163 0.9695 0.7696 0.0615  -0.1271 0.0234  414 TRP   B N     
12529 C  CA    . TRP   B 389 ? 1.0213 0.9730 0.7817 0.0615  -0.1003 0.0282  414 TRP   B CA    
12530 C  C     . TRP   B 389 ? 1.0172 0.9833 0.7886 0.0507  -0.0740 0.0201  414 TRP   B C     
12531 O  O     . TRP   B 389 ? 1.0252 0.9876 0.7865 0.0482  -0.0819 0.0162  414 TRP   B O     
12532 C  CB    . TRP   B 389 ? 1.0346 0.9673 0.7889 0.0694  -0.0976 0.0430  414 TRP   B CB    
12533 C  CG    . TRP   B 389 ? 1.0492 0.9623 0.7954 0.0733  -0.0981 0.0564  414 TRP   B CG    
12534 C  CD1   . TRP   B 389 ? 1.0506 0.9612 0.7938 0.0706  -0.0982 0.0593  414 TRP   B CD1   
12535 C  CD2   . TRP   B 389 ? 1.0599 0.9573 0.8034 0.0753  -0.1033 0.0669  414 TRP   B CD2   
12536 N  NE1   . TRP   B 389 ? 1.0538 0.9584 0.7947 0.0709  -0.1026 0.0662  414 TRP   B NE1   
12537 C  CE2   . TRP   B 389 ? 1.0588 0.9563 0.8012 0.0762  -0.1053 0.0711  414 TRP   B CE2   
12538 C  CE3   . TRP   B 389 ? 1.0655 0.9568 0.8115 0.0787  -0.1080 0.0716  414 TRP   B CE3   
12539 C  CZ2   . TRP   B 389 ? 1.0605 0.9593 0.8064 0.0842  -0.1118 0.0764  414 TRP   B CZ2   
12540 C  CZ3   . TRP   B 389 ? 1.0703 0.9635 0.8149 0.0796  -0.1101 0.0721  414 TRP   B CZ3   
12541 C  CH2   . TRP   B 389 ? 1.0662 0.9631 0.8118 0.0854  -0.1132 0.0758  414 TRP   B CH2   
12552 N  N     . VAL   B 390 ? 1.0051 0.9901 0.7984 0.0399  -0.0432 0.0178  415 VAL   B N     
12553 C  CA    . VAL   B 390 ? 0.9990 0.9963 0.8062 0.0335  -0.0294 0.0132  415 VAL   B CA    
12554 C  C     . VAL   B 390 ? 1.0005 1.0048 0.8081 0.0344  -0.0179 0.0247  415 VAL   B C     
12555 O  O     . VAL   B 390 ? 0.9902 1.0186 0.8047 0.0328  -0.0103 0.0260  415 VAL   B O     
12556 C  CB    . VAL   B 390 ? 0.9831 0.9913 0.8105 0.0296  -0.0317 -0.0010 415 VAL   B CB    
12557 C  CG1   . VAL   B 390 ? 0.9802 0.9932 0.8125 0.0292  -0.0312 -0.0042 415 VAL   B CG1   
12558 C  CG2   . VAL   B 390 ? 0.9718 0.9839 0.8121 0.0298  -0.0351 -0.0069 415 VAL   B CG2   
12568 N  N     . LYS   B 391 ? 1.0045 0.9935 0.8132 0.0370  -0.0127 0.0325  416 LYS   B N     
12569 C  CA    . LYS   B 391 ? 1.0084 0.9818 0.8221 0.0339  -0.0072 0.0305  416 LYS   B CA    
12570 C  C     . LYS   B 391 ? 1.0468 0.9766 0.8264 0.0364  0.0006  0.0252  416 LYS   B C     
12571 O  O     . LYS   B 391 ? 1.0416 0.9743 0.8277 0.0311  0.0026  0.0215  416 LYS   B O     
12572 C  CB    . LYS   B 391 ? 0.9736 0.9757 0.8265 0.0279  -0.0076 0.0340  416 LYS   B CB    
12575 N  N     . PHE   B 392 ? 1.0879 0.9721 0.8290 0.0524  0.0085  0.0232  417 PHE   B N     
12576 C  CA    . PHE   B 392 ? 1.1170 0.9643 0.8309 0.0768  0.0142  0.0161  417 PHE   B CA    
12577 C  C     . PHE   B 392 ? 1.1382 0.9695 0.8408 0.0916  0.0249  0.0096  417 PHE   B C     
12578 O  O     . PHE   B 392 ? 1.1536 0.9706 0.8474 0.1012  0.0295  0.0055  417 PHE   B O     
12579 C  CB    . PHE   B 392 ? 1.1134 0.9521 0.8238 0.0829  0.0072  0.0169  417 PHE   B CB    
12582 P  PG    . ANP   C .   ? 0.3616 0.1760 0.1977 0.0238  -0.0386 0.0178  501 ANP   A PG    
12583 O  O1G   . ANP   C .   ? 0.3634 0.1746 0.2263 0.0284  -0.0574 0.0311  501 ANP   A O1G   
12584 O  O2G   . ANP   C .   ? 0.3750 0.1721 0.2055 0.0076  -0.0443 0.0021  501 ANP   A O2G   
12585 O  O3G   . ANP   C .   ? 0.3896 0.2035 0.2126 0.0243  -0.0515 0.0370  501 ANP   A O3G   
12586 P  PB    . ANP   C .   ? 0.4321 0.1964 0.2049 0.0180  -0.0746 0.0171  501 ANP   A PB    
12587 O  O1B   . ANP   C .   ? 0.4084 0.1706 0.1890 0.0151  -0.0821 0.0409  501 ANP   A O1B   
12588 O  O2B   . ANP   C .   ? 0.4490 0.2023 0.2187 0.0094  -0.0717 0.0134  501 ANP   A O2B   
12589 N  N3B   . ANP   C .   ? 0.3707 0.1791 0.1881 0.0351  -0.0589 0.0473  501 ANP   A N3B   
12590 P  PA    . ANP   C .   ? 0.4243 0.1916 0.2127 0.0517  -0.1160 0.0069  501 ANP   A PA    
12591 O  O1A   . ANP   C .   ? 0.3769 0.1850 0.2228 0.0550  -0.1064 0.0101  501 ANP   A O1A   
12592 O  O2A   . ANP   C .   ? 0.4186 0.2195 0.2110 0.0551  -0.1065 0.0296  501 ANP   A O2A   
12593 O  O3A   . ANP   C .   ? 0.4498 0.1745 0.2130 0.0055  -0.1114 0.0127  501 ANP   A O3A   
12594 O  "O5'" . ANP   C .   ? 0.4521 0.2136 0.2159 0.0738  -0.1303 0.0154  501 ANP   A "O5'" 
12595 C  "C5'" . ANP   C .   ? 0.5054 0.2273 0.2318 0.0845  -0.1379 0.0133  501 ANP   A "C5'" 
12596 C  "C4'" . ANP   C .   ? 0.5304 0.2320 0.2458 0.1025  -0.1417 0.0007  501 ANP   A "C4'" 
12597 O  "O4'" . ANP   C .   ? 0.5152 0.2096 0.2498 0.0921  -0.1532 -0.0160 501 ANP   A "O4'" 
12598 C  "C3'" . ANP   C .   ? 0.5245 0.2211 0.2425 0.1008  -0.1344 0.0068  501 ANP   A "C3'" 
12599 O  "O3'" . ANP   C .   ? 0.5700 0.2263 0.2543 0.1129  -0.1150 0.0159  501 ANP   A "O3'" 
12600 C  "C2'" . ANP   C .   ? 0.5389 0.2165 0.2557 0.0870  -0.1318 0.0217  501 ANP   A "C2'" 
12601 O  "O2'" . ANP   C .   ? 0.5792 0.2264 0.2768 0.0761  -0.1363 0.0360  501 ANP   A "O2'" 
12602 C  "C1'" . ANP   C .   ? 0.5297 0.2154 0.2602 0.0858  -0.1508 -0.0088 501 ANP   A "C1'" 
12603 N  N9    . ANP   C .   ? 0.5048 0.2294 0.2736 0.0970  -0.1675 -0.0025 501 ANP   A N9    
12604 C  C8    . ANP   C .   ? 0.5142 0.2235 0.2745 0.0756  -0.1777 -0.0047 501 ANP   A C8    
12605 N  N7    . ANP   C .   ? 0.4417 0.2336 0.2860 0.0955  -0.1697 -0.0020 501 ANP   A N7    
12606 C  C5    . ANP   C .   ? 0.4697 0.2359 0.2901 0.1022  -0.1871 -0.0262 501 ANP   A C5    
12607 C  C6    . ANP   C .   ? 0.4894 0.2594 0.3085 0.0985  -0.2045 -0.0270 501 ANP   A C6    
12608 N  N6    . ANP   C .   ? 0.4649 0.2469 0.3220 0.1145  -0.1899 -0.0241 501 ANP   A N6    
12609 N  N1    . ANP   C .   ? 0.5011 0.2887 0.3238 0.1020  -0.1872 -0.0266 501 ANP   A N1    
12610 C  C2    . ANP   C .   ? 0.5064 0.2735 0.3077 0.1136  -0.1880 -0.0078 501 ANP   A C2    
12611 N  N3    . ANP   C .   ? 0.5219 0.2573 0.3007 0.1139  -0.1803 -0.0052 501 ANP   A N3    
12612 C  C4    . ANP   C .   ? 0.4855 0.2339 0.2911 0.1113  -0.1728 -0.0140 501 ANP   A C4    
12625 MG MG    . MG    D .   ? 0.3640 0.2000 0.2081 0.0361  -0.0825 0.0116  502 MG    A MG    
12626 C  C1    . A1ASC E .   ? 0.3652 0.4330 0.3433 0.1208  -0.0289 0.0361  503 A1ASC A C1    
12627 C  C2    . A1ASC E .   ? 0.2677 0.3544 0.2771 0.0660  -0.0223 0.0504  503 A1ASC A C2    
12628 C  C3    . A1ASC E .   ? 0.2683 0.3386 0.2484 0.0309  0.0194  0.0746  503 A1ASC A C3    
12629 C  C5    . A1ASC E .   ? 0.1480 0.2031 0.2341 -0.0028 0.0163  0.0247  503 A1ASC A C5    
12630 C  C8    . A1ASC E .   ? 0.1146 0.2067 0.2223 -0.0202 0.0205  0.0160  503 A1ASC A C8    
12631 C  C11   . A1ASC E .   ? 0.1446 0.2155 0.2232 -0.0069 0.0424  0.0037  503 A1ASC A C11   
12632 C  C12   . A1ASC E .   ? 0.1525 0.2243 0.2394 -0.0264 0.0057  0.0043  503 A1ASC A C12   
12633 C  C13   . A1ASC E .   ? 0.1799 0.1986 0.2180 -0.0162 0.0151  0.0332  503 A1ASC A C13   
12634 C  C14   . A1ASC E .   ? 0.1502 0.2401 0.2359 0.0032  0.0172  0.0220  503 A1ASC A C14   
12635 C  C15   . A1ASC E .   ? 0.1437 0.1988 0.2248 -0.0094 0.0011  0.0059  503 A1ASC A C15   
12636 C  C16   . A1ASC E .   ? 0.1456 0.2619 0.2442 0.0179  -0.0026 -0.0019 503 A1ASC A C16   
12637 C  C17   . A1ASC E .   ? 0.1233 0.2019 0.2159 -0.0327 0.0220  0.0021  503 A1ASC A C17   
12638 C  C20   . A1ASC E .   ? 0.2535 0.3285 0.2231 0.0362  0.0190  0.0843  503 A1ASC A C20   
12639 N  N     . A1ASC E .   ? 0.2705 0.3246 0.2607 0.0162  0.0005  0.0673  503 A1ASC A N     
12640 C  C     . A1ASC E .   ? 0.1573 0.2164 0.2558 -0.0032 0.0428  0.0429  503 A1ASC A C     
12641 O  O     . A1ASC E .   ? 0.2125 0.2709 0.2250 -0.0005 0.0167  0.0542  503 A1ASC A O     
12642 C  C10   . A1ASC E .   ? 0.1797 0.3308 0.2633 0.0482  -0.0155 -0.0014 503 A1ASC A C10   
12643 C  C18   . A1ASC E .   ? 0.1384 0.2220 0.2248 -0.0124 0.0201  -0.0097 503 A1ASC A C18   
12644 C  C19   . A1ASC E .   ? 0.2023 0.2903 0.2857 -0.0279 -0.0320 0.0085  503 A1ASC A C19   
12645 C  C1A   . A1ASC E .   ? 0.2738 0.3537 0.2932 0.0400  -0.0123 0.0311  503 A1ASC A C1A   
12646 C  C1B   . A1ASC E .   ? 0.1266 0.2319 0.2466 0.0067  0.0407  0.0226  503 A1ASC A C1B   
12647 C  C1C   . A1ASC E .   ? 0.2822 0.3282 0.2752 0.0181  0.0098  0.0323  503 A1ASC A C1C   
12648 C  C1E   . A1ASC E .   ? 0.1973 0.3117 0.3192 -0.0098 -0.0032 -0.0225 503 A1ASC A C1E   
12649 C  C1F   . A1ASC E .   ? 0.1653 0.2069 0.2219 0.0095  0.0470  -0.0089 503 A1ASC A C1F   
12650 C  C1G   . A1ASC E .   ? 0.1425 0.2061 0.2369 -0.0147 0.0200  0.0106  503 A1ASC A C1G   
12651 C  C1H   . A1ASC E .   ? 0.2009 0.3377 0.3488 -0.0078 0.0277  0.0037  503 A1ASC A C1H   
12652 C  C1I   . A1ASC E .   ? 0.1277 0.2263 0.2495 0.0246  0.0205  0.0104  503 A1ASC A C1I   
12653 C  C1J   . A1ASC E .   ? 0.2948 0.3675 0.2991 0.0362  -0.0361 0.0358  503 A1ASC A C1J   
12654 C  C1K   . A1ASC E .   ? 0.1221 0.2232 0.2122 0.0063  0.0377  -0.0047 503 A1ASC A C1K   
12655 C  C7    . A1ASC E .   ? 0.1903 0.1847 0.2238 0.0021  0.0146  0.0204  503 A1ASC A C7    
12656 C  C9    . A1ASC E .   ? 0.1506 0.2579 0.2484 0.0383  0.0041  0.0229  503 A1ASC A C9    
12657 N  N4    . A1ASC E .   ? 0.1272 0.2172 0.2573 -0.0168 0.0238  0.0473  503 A1ASC A N4    
12658 N  N6    . A1ASC E .   ? 0.3298 0.3962 0.3190 0.0627  -0.0116 0.0354  503 A1ASC A N6    
12659 O  O1    . A1ASC E .   ? 0.1382 0.2455 0.2467 -0.0037 0.0027  0.0169  503 A1ASC A O1    
12660 O  O2    . A1ASC E .   ? 0.1910 0.2276 0.2508 -0.0229 0.0383  0.0561  503 A1ASC A O2    
12661 O  O3    . A1ASC E .   ? 0.1679 0.2438 0.2757 -0.0004 0.0027  0.0089  503 A1ASC A O3    
12699 CL CL    . CL    F .   ? 0.2337 0.2964 0.2703 0.0047  0.0325  -0.0184 504 CL    A CL    
12700 P  PG    . ANP   G .   ? 0.3315 0.1933 0.2296 -0.0197 0.0880  -0.0203 501 ANP   B PG    
12701 O  O1G   . ANP   G .   ? 0.2884 0.1945 0.2469 -0.0055 0.0872  -0.0225 501 ANP   B O1G   
12702 O  O2G   . ANP   G .   ? 0.3227 0.2037 0.2107 0.0086  0.0618  -0.0104 501 ANP   B O2G   
12703 O  O3G   . ANP   G .   ? 0.3485 0.1954 0.2265 -0.0075 0.0830  0.0066  501 ANP   B O3G   
12704 P  PB    . ANP   G .   ? 0.3662 0.2120 0.2441 -0.0220 0.0968  -0.0230 501 ANP   B PB    
12705 O  O1B   . ANP   G .   ? 0.3495 0.2004 0.2510 -0.0234 0.0970  -0.0468 501 ANP   B O1B   
12706 O  O2B   . ANP   G .   ? 0.4000 0.1903 0.2612 -0.0210 0.0851  -0.0405 501 ANP   B O2B   
12707 N  N3B   . ANP   G .   ? 0.3674 0.2097 0.2207 -0.0117 0.1088  -0.0496 501 ANP   B N3B   
12708 P  PA    . ANP   G .   ? 0.4031 0.1946 0.2546 0.0053  0.1335  -0.0326 501 ANP   B PA    
12709 O  O1A   . ANP   G .   ? 0.3952 0.1811 0.2658 -0.0051 0.1202  -0.0299 501 ANP   B O1A   
12710 O  O2A   . ANP   G .   ? 0.4137 0.1787 0.2568 -0.0067 0.1379  -0.0278 501 ANP   B O2A   
12711 O  O3A   . ANP   G .   ? 0.4104 0.1870 0.2478 -0.0421 0.1278  -0.0137 501 ANP   B O3A   
12712 O  "O5'" . ANP   G .   ? 0.3888 0.2162 0.2704 0.0087  0.1467  -0.0429 501 ANP   B "O5'" 
12713 C  "C5'" . ANP   G .   ? 0.4192 0.2160 0.2794 0.0097  0.1654  -0.0585 501 ANP   B "C5'" 
12714 C  "C4'" . ANP   G .   ? 0.4526 0.2203 0.2909 0.0087  0.1731  -0.0592 501 ANP   B "C4'" 
12715 O  "O4'" . ANP   G .   ? 0.4816 0.2324 0.3089 -0.0155 0.1831  -0.0630 501 ANP   B "O4'" 
12716 C  "C3'" . ANP   G .   ? 0.4575 0.2237 0.2950 -0.0172 0.1762  -0.0719 501 ANP   B "C3'" 
12717 O  "O3'" . ANP   G .   ? 0.4705 0.2535 0.3028 -0.0154 0.1356  -0.0604 501 ANP   B "O3'" 
12718 C  "C2'" . ANP   G .   ? 0.4864 0.2402 0.3188 -0.0195 0.1894  -0.0758 501 ANP   B "C2'" 
12719 O  "O2'" . ANP   G .   ? 0.5271 0.2419 0.3291 -0.0407 0.1735  -0.0820 501 ANP   B "O2'" 
12720 C  "C1'" . ANP   G .   ? 0.4666 0.2424 0.3323 -0.0319 0.2140  -0.0657 501 ANP   B "C1'" 
12721 N  N9    . ANP   G .   ? 0.4485 0.2501 0.3731 -0.0474 0.2247  -0.0663 501 ANP   B N9    
12722 C  C8    . ANP   G .   ? 0.4611 0.2559 0.3798 -0.0301 0.2387  -0.0612 501 ANP   B C8    
12723 N  N7    . ANP   G .   ? 0.4637 0.2345 0.3904 -0.0492 0.2452  -0.0651 501 ANP   B N7    
12724 C  C5    . ANP   G .   ? 0.4148 0.2588 0.4126 -0.0124 0.2356  -0.0606 501 ANP   B C5    
12725 C  C6    . ANP   G .   ? 0.4370 0.2428 0.4499 -0.0152 0.2454  -0.0689 501 ANP   B C6    
12726 N  N6    . ANP   G .   ? 0.4131 0.2391 0.4769 -0.0075 0.2370  -0.0713 501 ANP   B N6    
12727 N  N1    . ANP   G .   ? 0.4634 0.2396 0.4449 0.0034  0.2540  -0.0465 501 ANP   B N1    
12728 C  C2    . ANP   G .   ? 0.4711 0.2567 0.4362 0.0191  0.2401  -0.0579 501 ANP   B C2    
12729 N  N3    . ANP   G .   ? 0.4669 0.2472 0.4216 -0.0019 0.2377  -0.0664 501 ANP   B N3    
12730 C  C4    . ANP   G .   ? 0.4130 0.2553 0.4008 -0.0097 0.2294  -0.0617 501 ANP   B C4    
12743 MG MG    . MG    H .   ? 0.3333 0.2125 0.2650 -0.0142 0.1128  -0.0391 502 MG    B MG    
12744 C  C1    . GOL   I .   ? 0.2495 0.5612 0.8218 0.0559  0.0455  -0.0445 503 GOL   B C1    
12745 O  O1    . GOL   I .   ? 0.2325 0.5049 0.8252 0.0619  0.0372  -0.0402 503 GOL   B O1    
12746 C  C2    . GOL   I .   ? 0.2330 0.5789 0.8193 0.0414  0.0439  -0.0634 503 GOL   B C2    
12747 O  O2    . GOL   I .   ? 0.2173 0.5660 0.8268 0.0008  0.0440  -0.0808 503 GOL   B O2    
12748 C  C3    . GOL   I .   ? 0.2602 0.6472 0.7932 0.0306  -0.0010 -0.0444 503 GOL   B C3    
12749 O  O3    . GOL   I .   ? 0.2211 0.6960 0.7483 0.1152  -0.0431 -0.0139 503 GOL   B O3    
12757 C  C1    . A1ASC J .   ? 0.3666 0.4875 0.3773 -0.0380 0.0641  -0.0667 504 A1ASC B C1    
12758 C  C2    . A1ASC J .   ? 0.2741 0.3848 0.3080 0.0538  -0.0113 -0.0250 504 A1ASC B C2    
12759 C  C3    . A1ASC J .   ? 0.1992 0.3554 0.2839 0.0108  -0.0322 -0.0507 504 A1ASC B C3    
12760 C  C5    . A1ASC J .   ? 0.1496 0.2626 0.2902 -0.0055 0.0222  -0.0274 504 A1ASC B C5    
12761 C  C8    . A1ASC J .   ? 0.1284 0.2537 0.3044 -0.0065 -0.0222 -0.0348 504 A1ASC B C8    
12762 C  C11   . A1ASC J .   ? 0.1686 0.2489 0.2796 -0.0223 0.0222  0.0014  504 A1ASC B C11   
12763 C  C12   . A1ASC J .   ? 0.1439 0.2312 0.3047 -0.0061 0.0305  -0.0007 504 A1ASC B C12   
12764 C  C13   . A1ASC J .   ? 0.1259 0.2574 0.2849 0.0112  0.0121  -0.0204 504 A1ASC B C13   
12765 C  C14   . A1ASC J .   ? 0.1488 0.2708 0.3013 -0.0165 0.0266  -0.0146 504 A1ASC B C14   
12766 C  C15   . A1ASC J .   ? 0.1245 0.2428 0.2991 -0.0249 -0.0146 -0.0379 504 A1ASC B C15   
12767 C  C16   . A1ASC J .   ? 0.1446 0.3036 0.3248 -0.0125 0.0132  -0.0551 504 A1ASC B C16   
12768 C  C17   . A1ASC J .   ? 0.1498 0.2766 0.2778 -0.0037 -0.0504 -0.0023 504 A1ASC B C17   
12769 C  C20   . A1ASC J .   ? 0.1990 0.3457 0.2930 0.0304  -0.0185 -0.0469 504 A1ASC B C20   
12770 N  N     . A1ASC J .   ? 0.2474 0.3367 0.3053 0.0207  0.0012  -0.0656 504 A1ASC B N     
12771 C  C     . A1ASC J .   ? 0.1422 0.2718 0.3065 0.0173  0.0092  -0.0443 504 A1ASC B C     
12772 O  O     . A1ASC J .   ? 0.1827 0.3130 0.2993 0.0053  -0.0001 -0.0526 504 A1ASC B O     
12773 C  C10   . A1ASC J .   ? 0.1637 0.3465 0.3223 -0.0177 0.0185  -0.0541 504 A1ASC B C10   
12774 C  C18   . A1ASC J .   ? 0.1384 0.2512 0.2963 -0.0407 -0.0153 -0.0008 504 A1ASC B C18   
12775 C  C19   . A1ASC J .   ? 0.2351 0.3309 0.3633 -0.0242 0.0286  -0.0395 504 A1ASC B C19   
12776 C  C1A   . A1ASC J .   ? 0.2730 0.4097 0.3336 -0.0053 0.0065  -0.0618 504 A1ASC B C1A   
12777 C  C1B   . A1ASC J .   ? 0.1113 0.3095 0.3152 0.0152  -0.0041 -0.0518 504 A1ASC B C1B   
12778 C  C1C   . A1ASC J .   ? 0.2559 0.3779 0.3287 0.0162  -0.0079 -0.0620 504 A1ASC B C1C   
12779 C  C1E   . A1ASC J .   ? 0.1907 0.3310 0.3679 0.0162  0.0418  -0.0212 504 A1ASC B C1E   
12780 C  C1F   . A1ASC J .   ? 0.1428 0.2500 0.2742 -0.0074 -0.0192 0.0078  504 A1ASC B C1F   
12781 C  C1G   . A1ASC J .   ? 0.1375 0.2492 0.3118 -0.0121 0.0077  -0.0296 504 A1ASC B C1G   
12782 C  C1H   . A1ASC J .   ? 0.2378 0.3601 0.3886 0.0237  0.0097  -0.0040 504 A1ASC B C1H   
12783 C  C1I   . A1ASC J .   ? 0.1396 0.2792 0.3295 0.0114  0.0076  -0.0192 504 A1ASC B C1I   
12784 C  C1J   . A1ASC J .   ? 0.2886 0.4417 0.3237 0.0150  0.0294  -0.0345 504 A1ASC B C1J   
12785 C  C1K   . A1ASC J .   ? 0.1506 0.2642 0.2828 -0.0066 -0.0358 -0.0110 504 A1ASC B C1K   
12786 C  C7    . A1ASC J .   ? 0.1219 0.2515 0.2806 -0.0003 0.0176  -0.0264 504 A1ASC B C7    
12787 C  C9    . A1ASC J .   ? 0.1438 0.2979 0.3282 0.0099  0.0186  -0.0406 504 A1ASC B C9    
12788 N  N4    . A1ASC J .   ? 0.0943 0.2880 0.3108 -0.0017 -0.0112 -0.0337 504 A1ASC B N4    
12789 N  N6    . A1ASC J .   ? 0.3070 0.4607 0.3419 -0.0012 0.0310  -0.0452 504 A1ASC B N6    
12790 O  O1    . A1ASC J .   ? 0.1492 0.2691 0.3302 -0.0054 0.0171  -0.0527 504 A1ASC B O1    
12791 O  O2    . A1ASC J .   ? 0.1525 0.2782 0.3369 -0.0143 -0.0152 -0.0453 504 A1ASC B O2    
12792 O  O3    . A1ASC J .   ? 0.1705 0.2954 0.3325 0.0012  0.0194  -0.0291 504 A1ASC B O3    
12830 CL CL    . CL    K .   ? 0.2181 0.3427 0.3098 0.0100  -0.0052 0.0203  505 CL    B CL    
12831 O  O     . HOH   L .   ? 0.8052 0.3349 0.4798 -0.0691 0.0198  -0.0529 601 HOH   A O     
12832 O  O     . HOH   L .   ? 0.8837 0.4337 0.5968 0.2353  0.1545  0.0386  602 HOH   A O     
12833 O  O     . HOH   L .   ? 0.8342 0.4089 0.3758 0.0893  0.1282  0.0585  603 HOH   A O     
12834 O  O     . HOH   L .   ? 0.4797 0.5947 0.5360 0.1138  0.2660  0.1965  604 HOH   A O     
12835 O  O     . HOH   L .   ? 0.6437 0.9081 0.8613 0.0221  0.1142  -0.0053 605 HOH   A O     
12836 O  O     . HOH   L .   ? 0.6667 0.6832 0.7935 0.0417  0.0658  0.1396  606 HOH   A O     
12837 O  O     . HOH   L .   ? 0.6508 0.6246 0.6754 -0.0080 -0.2081 -0.1492 607 HOH   A O     
12838 O  O     . HOH   L .   ? 0.6046 0.3044 0.6355 -0.0224 -0.3370 0.0899  608 HOH   A O     
12839 O  O     . HOH   L .   ? 0.3229 0.5832 0.7273 -0.0658 -0.0279 -0.0181 609 HOH   A O     
12840 O  O     . HOH   L .   ? 0.4274 0.5203 0.9829 -0.0490 -0.1877 0.0790  610 HOH   A O     
12841 O  O     . HOH   L .   ? 1.0500 0.4530 0.7100 -0.0959 0.2795  -0.0416 611 HOH   A O     
12842 O  O     . HOH   L .   ? 0.9576 0.4613 0.4692 0.0136  -0.0691 0.0863  612 HOH   A O     
12843 O  O     . HOH   L .   ? 0.6564 0.6129 0.6323 0.1974  -0.2036 0.0227  613 HOH   A O     
12844 O  O     . HOH   L .   ? 1.0839 0.4542 0.4859 0.2173  0.0123  -0.0331 614 HOH   A O     
12845 O  O     . HOH   L .   ? 0.4502 0.4976 0.4901 0.1265  -0.0150 0.0197  615 HOH   A O     
12846 O  O     . HOH   L .   ? 0.3668 0.5384 1.2905 0.0835  -0.0783 0.0098  616 HOH   A O     
12847 O  O     . HOH   L .   ? 0.7280 0.6391 0.8118 -0.0274 0.3082  0.3006  617 HOH   A O     
12848 O  O     . HOH   L .   ? 0.8073 0.8436 0.3346 -0.1924 0.1263  -0.0493 618 HOH   A O     
12849 O  O     . HOH   L .   ? 0.4326 0.5170 0.5972 0.0290  0.1200  0.2780  619 HOH   A O     
12850 O  O     . HOH   L .   ? 0.3115 0.3964 0.3278 -0.0020 -0.0247 -0.0590 620 HOH   A O     
12851 O  O     . HOH   L .   ? 0.5009 0.3381 0.5405 0.0191  0.0488  0.0072  621 HOH   A O     
12852 O  O     . HOH   L .   ? 0.2363 0.2500 0.4029 0.0315  0.0152  0.0384  622 HOH   A O     
12853 O  O     . HOH   L .   ? 0.7561 0.7776 0.4944 0.2172  0.1223  0.0210  623 HOH   A O     
12854 O  O     . HOH   L .   ? 0.3627 0.2943 0.2860 -0.0102 -0.0901 0.0140  624 HOH   A O     
12855 O  O     . HOH   L .   ? 0.2616 0.1810 0.2367 0.0399  -0.0431 0.0228  625 HOH   A O     
12856 O  O     . HOH   L .   ? 0.5472 0.3557 1.0330 -0.1483 -0.1126 -0.0350 626 HOH   A O     
12857 O  O     . HOH   L .   ? 0.5659 0.3983 0.6499 0.0216  -0.1111 -0.2317 627 HOH   A O     
12858 O  O     . HOH   L .   ? 0.7221 0.4969 0.6253 0.2636  -0.2760 -0.1298 628 HOH   A O     
12859 O  O     . HOH   L .   ? 0.5545 0.3723 0.5694 0.1911  -0.2874 -0.1331 629 HOH   A O     
12860 O  O     . HOH   L .   ? 0.2401 0.6970 0.5645 0.0603  0.0044  -0.2560 630 HOH   A O     
12861 O  O     . HOH   L .   ? 0.4346 0.2735 0.4194 -0.0469 0.0420  0.0116  631 HOH   A O     
12862 O  O     A HOH   L .   ? 0.5497 0.3599 0.5525 0.0920  0.3239  0.0782  632 HOH   A O     
12863 O  O     B HOH   L .   ? 0.4951 0.3879 0.6957 0.1714  0.1983  0.2305  632 HOH   A O     
12864 O  O     . HOH   L .   ? 0.9074 0.6539 0.4267 0.1501  0.0853  0.1948  633 HOH   A O     
12865 O  O     . HOH   L .   ? 0.9738 0.4837 0.5843 -0.1047 0.2796  -0.0494 634 HOH   A O     
12866 O  O     . HOH   L .   ? 1.1737 0.3671 0.4184 0.1312  0.1925  -0.0071 635 HOH   A O     
12867 O  O     . HOH   L .   ? 0.5005 0.5967 0.5827 -0.0226 0.1215  0.2683  636 HOH   A O     
12868 O  O     . HOH   L .   ? 0.4970 0.3140 0.3961 0.0893  -0.0225 -0.0348 637 HOH   A O     
12869 O  O     . HOH   L .   ? 0.7885 0.4221 0.5504 0.1361  -0.3731 -0.0773 638 HOH   A O     
12870 O  O     . HOH   L .   ? 0.3283 0.2098 0.3896 0.0148  0.0735  -0.0465 639 HOH   A O     
12871 O  O     . HOH   L .   ? 0.8492 0.4232 0.3777 -0.0683 0.1019  -0.0382 640 HOH   A O     
12872 O  O     . HOH   L .   ? 0.3908 0.2672 0.4064 -0.0546 -0.1449 0.0909  641 HOH   A O     
12873 O  O     . HOH   L .   ? 0.8549 0.5418 0.6884 0.3239  -0.3702 -0.2094 642 HOH   A O     
12874 O  O     . HOH   L .   ? 0.4662 0.5833 0.9654 -0.0392 -0.2386 0.0470  643 HOH   A O     
12875 O  O     . HOH   L .   ? 0.5847 0.4896 0.2814 -0.0198 -0.0477 -0.0363 644 HOH   A O     
12876 O  O     . HOH   L .   ? 0.4295 0.6228 0.5950 0.0593  0.1113  0.0580  645 HOH   A O     
12877 O  O     . HOH   L .   ? 0.2989 0.2627 0.3367 -0.0111 -0.0376 0.0116  646 HOH   A O     
12878 O  O     . HOH   L .   ? 0.3852 0.2160 0.2834 0.0769  -0.0635 0.0206  647 HOH   A O     
12879 O  O     . HOH   L .   ? 0.5498 0.4011 0.3492 0.0911  0.1167  0.0240  648 HOH   A O     
12880 O  O     . HOH   L .   ? 0.2329 0.3673 0.3308 -0.0061 0.0700  0.0192  649 HOH   A O     
12881 O  O     . HOH   L .   ? 0.8694 0.3296 0.7963 0.0632  0.0310  -0.1787 650 HOH   A O     
12882 O  O     . HOH   L .   ? 0.7093 0.3209 0.6007 0.1312  -0.1610 -0.0837 651 HOH   A O     
12883 O  O     . HOH   L .   ? 0.8560 0.6817 0.5956 0.1474  -0.3832 0.0299  652 HOH   A O     
12884 O  O     . HOH   L .   ? 0.7443 0.4723 0.8048 -0.0754 -0.1152 0.0085  653 HOH   A O     
12885 O  O     . HOH   L .   ? 0.2927 0.3899 0.7146 -0.0437 0.0621  0.0848  654 HOH   A O     
12886 O  O     . HOH   L .   ? 0.8589 0.8424 0.5797 -0.2432 0.1715  -0.0994 655 HOH   A O     
12887 O  O     . HOH   L .   ? 0.9930 0.3607 0.5397 0.0193  -0.3241 -0.0042 656 HOH   A O     
12888 O  O     . HOH   L .   ? 0.2277 0.2193 0.4643 0.0085  -0.0003 0.0104  657 HOH   A O     
12889 O  O     . HOH   L .   ? 0.3589 0.5749 0.7782 0.0892  -0.0360 -0.3660 658 HOH   A O     
12890 O  O     . HOH   L .   ? 0.5337 0.2625 0.4384 0.0693  -0.1210 -0.0163 659 HOH   A O     
12891 O  O     . HOH   L .   ? 0.7480 0.3450 0.4470 0.1116  -0.3134 -0.0914 660 HOH   A O     
12892 O  O     . HOH   L .   ? 0.5924 0.3147 0.4198 0.1655  -0.2639 -0.0891 661 HOH   A O     
12893 O  O     . HOH   L .   ? 0.6410 0.2475 0.3854 0.0277  -0.0161 0.0602  662 HOH   A O     
12894 O  O     . HOH   L .   ? 0.6609 0.5158 0.9002 -0.0779 -0.3956 0.0488  663 HOH   A O     
12895 O  O     . HOH   L .   ? 0.3892 0.3688 0.3432 0.0180  -0.0232 0.0168  664 HOH   A O     
12896 O  O     . HOH   L .   ? 0.6976 0.5265 0.4863 -0.0775 0.2012  0.0207  665 HOH   A O     
12897 O  O     . HOH   L .   ? 0.3293 0.2779 0.4261 0.0875  0.1132  0.0138  666 HOH   A O     
12898 O  O     . HOH   L .   ? 0.3077 0.5160 1.0067 -0.0348 0.0378  -0.0872 667 HOH   A O     
12899 O  O     . HOH   L .   ? 0.3107 0.3427 0.5898 -0.0507 -0.1212 -0.0156 668 HOH   A O     
12900 O  O     . HOH   L .   ? 0.7893 0.7443 0.4628 0.1725  -0.2534 0.1316  669 HOH   A O     
12901 O  O     . HOH   L .   ? 0.5616 0.5690 0.9913 0.0643  -0.2787 -0.3397 670 HOH   A O     
12902 O  O     . HOH   L .   ? 0.5975 0.3424 0.4987 0.0653  -0.1999 -0.0600 671 HOH   A O     
12903 O  O     . HOH   L .   ? 0.1959 0.2072 0.2822 0.0070  0.0207  -0.0078 672 HOH   A O     
12904 O  O     . HOH   L .   ? 0.2170 0.1830 0.3012 0.0284  0.0323  0.0401  673 HOH   A O     
12905 O  O     . HOH   L .   ? 0.2726 0.4298 0.9936 0.0014  0.0395  0.2238  674 HOH   A O     
12906 O  O     . HOH   L .   ? 0.3587 0.4402 0.9755 -0.0486 0.0894  -0.1531 675 HOH   A O     
12907 O  O     . HOH   L .   ? 0.3560 0.3968 0.9562 0.0688  -0.2378 -0.1466 676 HOH   A O     
12908 O  O     . HOH   L .   ? 0.2476 0.3606 0.6681 -0.0363 0.0573  0.0148  677 HOH   A O     
12909 O  O     . HOH   L .   ? 0.2466 0.4984 0.5441 0.0726  0.0119  0.0991  678 HOH   A O     
12910 O  O     . HOH   L .   ? 1.0014 0.6757 0.4458 0.3764  -0.1768 -0.1551 679 HOH   A O     
12911 O  O     . HOH   L .   ? 0.4181 0.2582 0.3864 -0.0154 0.0390  0.0665  680 HOH   A O     
12912 O  O     . HOH   L .   ? 0.4171 0.4268 0.4103 0.0304  -0.0439 -0.0575 681 HOH   A O     
12913 O  O     . HOH   L .   ? 0.7594 0.2979 0.5289 0.1457  0.1720  -0.0549 682 HOH   A O     
12914 O  O     . HOH   L .   ? 0.3187 0.3010 0.4458 -0.0039 -0.0803 0.0580  683 HOH   A O     
12915 O  O     . HOH   L .   ? 0.7064 0.7359 0.2777 0.0375  -0.1921 -0.0351 684 HOH   A O     
12916 O  O     . HOH   L .   ? 0.5467 0.3264 0.8290 -0.0150 -0.0432 0.0721  685 HOH   A O     
12917 O  O     . HOH   L .   ? 0.6062 0.5896 0.8358 -0.0208 -0.1380 -0.2305 686 HOH   A O     
12918 O  O     . HOH   L .   ? 0.4100 0.3373 0.4022 0.0440  0.1100  -0.0452 687 HOH   A O     
12919 O  O     . HOH   L .   ? 0.2852 0.3392 0.5269 0.0401  -0.0501 -0.0481 688 HOH   A O     
12920 O  O     . HOH   L .   ? 0.6552 0.3155 0.3387 0.0035  -0.1208 0.0166  689 HOH   A O     
12921 O  O     . HOH   L .   ? 0.4204 0.6253 0.3849 0.0621  -0.0338 0.0901  690 HOH   A O     
12922 O  O     . HOH   L .   ? 0.3644 0.6364 0.5065 0.1300  -0.1125 -0.1755 691 HOH   A O     
12923 O  O     . HOH   L .   ? 0.4688 0.3075 0.5180 -0.0011 -0.0479 -0.0495 692 HOH   A O     
12924 O  O     . HOH   L .   ? 0.2903 0.4604 0.5007 -0.0298 0.1493  -0.0320 693 HOH   A O     
12925 O  O     . HOH   L .   ? 0.1985 0.1945 0.2318 -0.0052 -0.0054 -0.0076 694 HOH   A O     
12926 O  O     . HOH   L .   ? 0.6751 0.3361 0.5101 -0.0706 0.2042  -0.1173 695 HOH   A O     
12927 O  O     . HOH   L .   ? 0.3595 0.3734 0.4801 0.0027  0.0765  0.0403  696 HOH   A O     
12928 O  O     . HOH   L .   ? 0.9813 0.4798 0.2906 0.2531  0.0978  0.0224  697 HOH   A O     
12929 O  O     . HOH   L .   ? 0.6856 0.3844 0.4036 0.0164  -0.0237 0.0920  698 HOH   A O     
12930 O  O     . HOH   L .   ? 0.6517 0.6350 0.6328 -0.2051 0.2268  -0.1394 699 HOH   A O     
12931 O  O     . HOH   L .   ? 0.3459 0.3203 0.3524 0.0228  -0.0970 0.0652  700 HOH   A O     
12932 O  O     . HOH   L .   ? 0.2381 0.6683 0.8666 -0.0663 0.0413  -0.0852 701 HOH   A O     
12933 O  O     . HOH   L .   ? 0.4579 0.4494 0.6699 0.0090  0.2401  0.1349  702 HOH   A O     
12934 O  O     . HOH   L .   ? 0.5881 0.4079 0.2862 -0.0045 -0.0014 0.0018  703 HOH   A O     
12935 O  O     . HOH   L .   ? 0.2670 0.2792 0.3831 -0.0127 -0.0209 0.0464  704 HOH   A O     
12936 O  O     . HOH   L .   ? 0.8762 0.3255 0.6378 0.1196  -0.0114 -0.0846 705 HOH   A O     
12937 O  O     . HOH   L .   ? 0.8377 0.8400 0.3688 0.0617  0.2277  0.0121  706 HOH   A O     
12938 O  O     . HOH   L .   ? 0.3520 0.5853 0.5939 0.0378  0.1853  0.1287  707 HOH   A O     
12939 O  O     . HOH   L .   ? 0.6776 0.4837 0.4323 0.2142  -0.1040 -0.0857 708 HOH   A O     
12940 O  O     . HOH   L .   ? 0.6841 0.6217 0.5229 -0.0492 -0.0054 0.0575  709 HOH   A O     
12941 O  O     . HOH   L .   ? 0.3330 0.7522 0.7607 0.1520  -0.0738 -0.1130 710 HOH   A O     
12942 O  O     . HOH   L .   ? 0.5307 0.5153 0.5414 0.1282  -0.2893 -0.0709 711 HOH   A O     
12943 O  O     . HOH   L .   ? 0.6998 0.3543 0.6405 -0.0451 0.0547  -0.1045 712 HOH   A O     
12944 O  O     . HOH   L .   ? 0.4299 0.3888 0.3033 0.0461  -0.0387 0.0447  713 HOH   A O     
12945 O  O     . HOH   L .   ? 0.5683 0.3339 0.6072 0.0966  -0.3451 -0.0905 714 HOH   A O     
12946 O  O     . HOH   L .   ? 0.4862 0.6102 0.7911 -0.0534 0.2748  0.0184  715 HOH   A O     
12947 O  O     . HOH   L .   ? 0.3711 0.3205 0.5450 -0.0307 0.0470  0.0125  716 HOH   A O     
12948 O  O     . HOH   L .   ? 0.3133 0.3795 0.3306 -0.0397 0.0127  0.0765  717 HOH   A O     
12949 O  O     . HOH   L .   ? 0.3132 0.5708 0.6267 0.0003  0.0854  0.1657  718 HOH   A O     
12950 O  O     . HOH   L .   ? 0.2043 0.1952 0.2638 -0.0146 -0.0347 -0.0213 719 HOH   A O     
12951 O  O     . HOH   L .   ? 0.6744 0.4197 0.2872 0.0677  0.0318  0.0738  720 HOH   A O     
12952 O  O     . HOH   L .   ? 0.4225 0.4140 1.0392 0.0478  -0.0001 0.0493  721 HOH   A O     
12953 O  O     . HOH   L .   ? 0.4830 0.6603 0.4246 0.1505  0.1197  0.1664  722 HOH   A O     
12954 O  O     . HOH   L .   ? 0.4837 0.2172 0.2619 0.0662  -0.1438 0.0000  723 HOH   A O     
12955 O  O     . HOH   L .   ? 0.4911 0.4188 0.3931 -0.0244 0.0002  0.0016  724 HOH   A O     
12956 O  O     . HOH   L .   ? 0.3301 0.3413 0.3782 0.0293  -0.0691 -0.0158 725 HOH   A O     
12957 O  O     . HOH   L .   ? 0.3221 0.3954 0.4281 0.0266  -0.0446 0.0899  726 HOH   A O     
12958 O  O     . HOH   L .   ? 0.4579 0.3431 0.6104 0.0561  0.1886  0.1089  727 HOH   A O     
12959 O  O     . HOH   L .   ? 0.2754 0.2256 0.2307 0.0034  0.0342  0.0253  728 HOH   A O     
12960 O  O     . HOH   L .   ? 0.3259 0.2703 0.5172 0.0792  -0.2026 -0.0182 729 HOH   A O     
12961 O  O     . HOH   L .   ? 0.1699 0.2245 0.3209 0.0144  -0.0258 0.0156  730 HOH   A O     
12962 O  O     . HOH   L .   ? 0.2750 0.3801 0.8219 -0.0021 0.0951  0.0517  731 HOH   A O     
12963 O  O     . HOH   L .   ? 0.8827 0.4157 0.4918 0.0690  -0.3535 -0.0016 732 HOH   A O     
12964 O  O     . HOH   L .   ? 0.8961 0.3374 0.5126 0.0640  0.0294  0.0074  733 HOH   A O     
12965 O  O     . HOH   L .   ? 0.2867 0.2249 0.3443 0.0109  -0.0663 0.0082  734 HOH   A O     
12966 O  O     . HOH   L .   ? 0.8191 0.4543 0.4640 0.1556  0.0559  -0.0736 735 HOH   A O     
12967 O  O     A HOH   L .   ? 0.3645 0.3341 0.6586 0.1341  -0.1347 -0.1042 736 HOH   A O     
12968 O  O     . HOH   L .   ? 0.3076 0.4534 0.3859 0.0389  0.1010  0.1408  737 HOH   A O     
12969 O  O     . HOH   L .   ? 0.3876 0.7483 0.8068 -0.0430 -0.1012 0.1066  738 HOH   A O     
12970 O  O     . HOH   L .   ? 0.5060 0.8255 0.4974 -0.0533 0.1054  0.0379  739 HOH   A O     
12971 O  O     . HOH   L .   ? 0.2515 0.4769 0.4523 0.0305  0.0424  -0.1135 740 HOH   A O     
12972 O  O     . HOH   L .   ? 0.2244 0.3557 0.6169 -0.0959 0.0208  0.0138  741 HOH   A O     
12973 O  O     . HOH   L .   ? 0.2871 0.6429 0.4657 0.0653  0.0340  -0.1610 742 HOH   A O     
12974 O  O     . HOH   L .   ? 0.9350 0.4362 0.3807 -0.1222 -0.1482 -0.0723 743 HOH   A O     
12975 O  O     . HOH   L .   ? 0.3669 0.2074 0.3199 0.0433  -0.0388 0.0233  744 HOH   A O     
12976 O  O     . HOH   L .   ? 0.2797 0.5497 1.0062 0.0646  0.0905  0.0215  745 HOH   A O     
12977 O  O     . HOH   L .   ? 0.3081 0.2644 0.7775 -0.0691 0.0435  0.0102  746 HOH   A O     
12978 O  O     . HOH   L .   ? 0.9931 0.3376 0.4705 -0.0846 -0.1348 -0.0983 747 HOH   A O     
12979 O  O     . HOH   L .   ? 0.4195 0.3192 0.6033 0.1050  -0.0299 0.0112  748 HOH   A O     
12980 O  O     . HOH   L .   ? 1.0089 0.6139 0.4460 0.1441  -0.3116 0.0019  749 HOH   A O     
12981 O  O     . HOH   L .   ? 0.2936 0.2058 0.2360 0.0271  -0.0615 0.0029  750 HOH   A O     
12982 O  O     . HOH   L .   ? 0.8386 0.4918 0.5344 0.0097  0.2957  -0.1657 751 HOH   A O     
12983 O  O     . HOH   L .   ? 0.7204 0.2728 0.4589 0.0978  -0.1810 -0.1028 752 HOH   A O     
12984 O  O     . HOH   L .   ? 0.7723 0.7458 0.5480 -0.1060 -0.3461 -0.0921 753 HOH   A O     
12985 O  O     . HOH   L .   ? 0.3509 0.5241 0.3751 -0.0988 0.0619  -0.1039 754 HOH   A O     
12986 O  O     . HOH   L .   ? 0.3975 0.2886 0.4315 0.0077  0.0649  0.0599  755 HOH   A O     
12987 O  O     . HOH   L .   ? 0.2928 0.4031 1.0091 -0.0262 0.1437  -0.1091 756 HOH   A O     
12988 O  O     . HOH   L .   ? 0.4302 0.2705 0.3113 0.0722  -0.1874 -0.0705 757 HOH   A O     
12989 O  O     . HOH   L .   ? 0.7190 0.4786 0.6476 0.1858  -0.1530 -0.1284 758 HOH   A O     
12990 O  O     . HOH   L .   ? 0.2433 0.4419 0.4580 0.0191  0.0330  0.0751  759 HOH   A O     
12991 O  O     . HOH   L .   ? 0.4629 0.3660 0.7372 -0.0265 0.0606  0.1128  760 HOH   A O     
12992 O  O     . HOH   L .   ? 0.3968 0.2445 0.3947 -0.0351 -0.0506 0.0106  761 HOH   A O     
12993 O  O     . HOH   L .   ? 0.2449 0.5199 0.4404 0.0490  0.0208  0.1573  762 HOH   A O     
12994 O  O     . HOH   L .   ? 0.2804 0.3283 0.3340 -0.0424 -0.0357 -0.0078 763 HOH   A O     
12995 O  O     . HOH   L .   ? 0.4958 0.7622 0.9113 -0.1521 0.1368  0.3274  764 HOH   A O     
12996 O  O     . HOH   L .   ? 0.3463 0.3309 0.3708 -0.0735 0.0093  0.0595  765 HOH   A O     
12997 O  O     . HOH   L .   ? 0.2109 0.3117 0.8050 0.0252  -0.0126 -0.0737 766 HOH   A O     
12998 O  O     . HOH   L .   ? 0.5263 0.3377 0.5239 0.0866  0.0124  0.0191  767 HOH   A O     
12999 O  O     . HOH   L .   ? 0.7886 0.6698 0.7363 0.1833  0.2515  0.0221  768 HOH   A O     
13000 O  O     . HOH   L .   ? 0.2731 0.2813 0.2576 -0.0004 -0.0312 -0.0033 769 HOH   A O     
13001 O  O     . HOH   L .   ? 0.3361 0.7342 0.8267 0.1342  -0.1474 -0.0703 770 HOH   A O     
13002 O  O     . HOH   L .   ? 0.4378 0.3443 0.6587 0.0673  0.2707  0.0557  771 HOH   A O     
13003 O  O     . HOH   L .   ? 0.4891 0.4136 0.7308 0.1393  -0.1468 -0.1241 772 HOH   A O     
13004 O  O     . HOH   L .   ? 0.7493 0.9515 0.7923 -0.3630 -0.0662 -0.3110 773 HOH   A O     
13005 O  O     . HOH   L .   ? 0.5296 0.2440 0.3342 0.0071  -0.0447 -0.0344 774 HOH   A O     
13006 O  O     . HOH   L .   ? 0.8145 0.3326 0.4126 0.0234  0.1074  -0.1152 775 HOH   A O     
13007 O  O     . HOH   L .   ? 0.3533 0.2522 0.4131 0.0338  -0.0765 0.0289  776 HOH   A O     
13008 O  O     . HOH   L .   ? 0.3442 0.2746 0.6017 -0.0560 -0.0440 0.0608  777 HOH   A O     
13009 O  O     . HOH   L .   ? 0.3888 0.2631 0.3610 -0.0780 -0.0063 -0.0433 778 HOH   A O     
13010 O  O     . HOH   L .   ? 0.9591 0.3337 0.5739 0.1317  0.3292  0.1020  779 HOH   A O     
13011 O  O     . HOH   L .   ? 0.3297 0.4042 0.8773 -0.0893 -0.1482 -0.0216 780 HOH   A O     
13012 O  O     . HOH   L .   ? 0.3255 0.3702 0.3133 -0.0114 0.0432  0.0590  781 HOH   A O     
13013 O  O     . HOH   L .   ? 0.1862 0.2742 0.3765 -0.0281 -0.0422 0.0164  782 HOH   A O     
13014 O  O     . HOH   L .   ? 0.9071 0.4418 0.7147 0.1308  0.0974  -0.0402 783 HOH   A O     
13015 O  O     . HOH   L .   ? 0.6492 0.8049 0.5623 0.0067  0.1023  -0.2561 784 HOH   A O     
13016 O  O     . HOH   L .   ? 0.3981 0.7460 0.4205 0.1230  0.0718  0.0437  785 HOH   A O     
13017 O  O     . HOH   L .   ? 0.7873 0.5242 0.4406 0.2145  0.1849  -0.1003 786 HOH   A O     
13018 O  O     . HOH   L .   ? 0.3351 0.3054 0.2367 -0.0332 0.0247  -0.0447 787 HOH   A O     
13019 O  O     . HOH   L .   ? 0.7576 0.2369 0.4643 0.0645  0.0368  0.0714  788 HOH   A O     
13020 O  O     . HOH   L .   ? 1.0123 0.6499 0.6815 0.3648  -0.1265 0.1624  789 HOH   A O     
13021 O  O     . HOH   L .   ? 0.9749 0.3344 0.4698 -0.0729 0.0079  0.1057  790 HOH   A O     
13022 O  O     . HOH   L .   ? 0.3485 0.9131 0.6557 0.0869  0.0303  -0.2648 791 HOH   A O     
13023 O  O     . HOH   L .   ? 0.4817 0.4449 0.5873 0.0869  0.2068  0.0050  792 HOH   A O     
13024 O  O     . HOH   L .   ? 0.2406 0.5926 0.9121 0.0488  0.0155  -0.0504 793 HOH   A O     
13025 O  O     . HOH   L .   ? 0.3786 0.2810 0.2679 -0.0296 -0.0605 -0.0172 794 HOH   A O     
13026 O  O     . HOH   L .   ? 0.2555 0.3636 0.7456 0.0374  0.0438  0.1338  795 HOH   A O     
13027 O  O     . HOH   L .   ? 0.8197 0.3416 0.3978 0.1721  -0.2445 -0.1123 796 HOH   A O     
13028 O  O     . HOH   L .   ? 0.2330 0.3326 0.5618 -0.0125 0.0482  -0.0907 797 HOH   A O     
13029 O  O     . HOH   L .   ? 0.6232 0.6311 0.5178 0.1447  0.3179  0.0519  798 HOH   A O     
13030 O  O     . HOH   L .   ? 0.4267 0.6496 0.9285 -0.2518 -0.1299 0.0675  799 HOH   A O     
13031 O  O     . HOH   L .   ? 0.3164 0.8585 0.8083 -0.1830 -0.0114 0.1611  800 HOH   A O     
13032 O  O     . HOH   L .   ? 0.2620 0.2316 0.4426 0.0814  -0.0030 0.0060  801 HOH   A O     
13033 O  O     . HOH   L .   ? 0.3164 0.2896 0.3053 0.0139  -0.0046 0.0327  802 HOH   A O     
13034 O  O     . HOH   L .   ? 0.3739 0.2856 0.3467 0.0397  -0.0622 -0.0002 803 HOH   A O     
13035 O  O     . HOH   L .   ? 0.8292 0.5014 0.6250 -0.2460 0.0777  -0.1684 804 HOH   A O     
13036 O  O     . HOH   L .   ? 0.4518 0.6165 0.6689 -0.0155 -0.2998 0.1276  805 HOH   A O     
13037 O  O     . HOH   L .   ? 0.4567 1.0151 0.3859 -0.0778 -0.0567 0.1930  806 HOH   A O     
13038 O  O     . HOH   L .   ? 0.4420 0.2439 0.3150 0.0546  -0.0086 -0.0361 807 HOH   A O     
13039 O  O     . HOH   L .   ? 0.2266 0.2066 0.3182 0.0128  0.0075  0.0183  808 HOH   A O     
13040 O  O     . HOH   L .   ? 0.5616 0.5141 0.2687 0.0606  -0.0292 0.0293  809 HOH   A O     
13041 O  O     . HOH   L .   ? 0.8950 0.7703 0.3561 0.2091  -0.2140 -0.0238 810 HOH   A O     
13042 O  O     . HOH   L .   ? 0.3398 0.3986 0.3366 -0.0520 0.0349  -0.0702 811 HOH   A O     
13043 O  O     . HOH   L .   ? 0.8269 0.4648 0.3992 0.2025  0.1333  0.1700  812 HOH   A O     
13044 O  O     . HOH   L .   ? 0.3030 0.5158 0.6772 0.0356  -0.0209 0.2694  813 HOH   A O     
13045 O  O     . HOH   L .   ? 0.3277 0.4127 0.4245 0.0657  -0.0433 -0.0237 814 HOH   A O     
13046 O  O     . HOH   L .   ? 0.4615 0.3205 0.6777 -0.0604 0.0243  -0.0475 815 HOH   A O     
13047 O  O     . HOH   L .   ? 0.6427 0.2971 0.2657 0.0627  -0.0714 0.0512  816 HOH   A O     
13048 O  O     . HOH   L .   ? 0.3331 0.2485 0.2805 0.0972  -0.1509 -0.0433 817 HOH   A O     
13049 O  O     . HOH   L .   ? 0.4676 0.3789 1.0981 -0.0954 0.0643  -0.0928 818 HOH   A O     
13050 O  O     . HOH   L .   ? 0.7230 0.7918 0.9254 0.3615  0.0754  -0.2459 819 HOH   A O     
13051 O  O     . HOH   L .   ? 0.4370 0.5203 0.4481 0.0510  -0.1771 -0.0251 820 HOH   A O     
13052 O  O     . HOH   L .   ? 1.1838 0.4306 0.3214 0.1016  0.0126  0.0513  821 HOH   A O     
13053 O  O     . HOH   L .   ? 0.4837 0.2549 0.3848 0.0041  -0.0413 -0.0016 822 HOH   A O     
13054 O  O     . HOH   L .   ? 1.0868 0.3423 0.3441 -0.0768 0.0700  -0.0667 823 HOH   A O     
13055 O  O     . HOH   L .   ? 0.3029 0.3386 0.3427 0.0357  -0.0260 -0.0080 824 HOH   A O     
13056 O  O     . HOH   L .   ? 1.0538 0.4448 0.6974 0.1712  0.0526  -0.1378 825 HOH   A O     
13057 O  O     . HOH   L .   ? 0.6295 0.4120 0.4582 0.1839  0.1936  -0.0679 826 HOH   A O     
13058 O  O     . HOH   L .   ? 0.7043 0.5195 0.3611 0.3212  -0.1900 -0.1060 827 HOH   A O     
13059 O  O     . HOH   L .   ? 0.3765 0.2932 0.3520 0.0865  -0.0652 0.0301  828 HOH   A O     
13060 O  O     . HOH   L .   ? 1.2181 0.4682 0.5891 0.1468  -0.1579 -0.1836 829 HOH   A O     
13061 O  O     . HOH   L .   ? 0.3759 0.2420 0.3254 0.1004  -0.1351 -0.0175 830 HOH   A O     
13062 O  O     . HOH   L .   ? 0.7759 0.5171 0.5446 0.0407  0.2293  0.0793  831 HOH   A O     
13063 O  O     . HOH   L .   ? 0.9128 0.6225 0.4813 -0.0380 0.2165  0.1458  832 HOH   A O     
13064 O  O     . HOH   L .   ? 0.6596 0.6064 0.7303 0.0288  0.2953  0.2188  833 HOH   A O     
13065 O  O     . HOH   L .   ? 0.5860 0.2756 0.3459 0.0409  0.0172  0.0281  834 HOH   A O     
13066 O  O     . HOH   L .   ? 0.6296 0.3384 0.5817 -0.1225 0.1676  -0.1517 835 HOH   A O     
13067 O  O     . HOH   L .   ? 0.3409 0.2590 0.5890 -0.0432 0.0897  0.0886  836 HOH   A O     
13068 O  O     . HOH   L .   ? 0.5171 0.3565 0.6263 0.0309  0.0676  -0.1548 837 HOH   A O     
13069 O  O     . HOH   L .   ? 0.6296 0.4110 0.9405 -0.0315 -0.3674 0.0829  838 HOH   A O     
13070 O  O     . HOH   L .   ? 0.5915 0.2545 0.2763 0.1084  -0.1493 -0.0231 839 HOH   A O     
13071 O  O     . HOH   L .   ? 0.5535 0.3235 0.7980 -0.1665 0.1578  0.0176  840 HOH   A O     
13072 O  O     . HOH   L .   ? 0.4638 0.5347 0.4572 0.0009  -0.0182 -0.0196 841 HOH   A O     
13073 O  O     . HOH   L .   ? 0.6150 0.5322 0.5726 -0.0229 0.0319  0.0421  842 HOH   A O     
13074 O  O     . HOH   L .   ? 0.4005 0.2638 0.3756 -0.0388 -0.0931 0.0125  843 HOH   A O     
13075 O  O     . HOH   L .   ? 0.4915 0.4763 0.9646 0.1538  0.1923  0.3113  844 HOH   A O     
13076 O  O     . HOH   L .   ? 0.5019 0.6134 0.8034 0.1806  -0.3238 -0.2037 845 HOH   A O     
13077 O  O     . HOH   L .   ? 0.6141 0.9260 0.6734 0.2752  -0.2611 0.0460  846 HOH   A O     
13078 O  O     . HOH   L .   ? 0.9164 0.4304 0.5890 -0.0147 0.2459  -0.1773 847 HOH   A O     
13079 O  O     . HOH   L .   ? 0.2666 0.3056 0.3181 -0.0375 0.0912  -0.0147 848 HOH   A O     
13080 O  O     . HOH   L .   ? 0.4500 0.6618 0.3491 -0.0157 0.1190  0.0666  849 HOH   A O     
13081 O  O     . HOH   L .   ? 0.3672 0.4780 0.7200 0.0774  0.0360  0.1150  850 HOH   A O     
13082 O  O     . HOH   L .   ? 0.4537 0.5739 0.5874 -0.0821 -0.0706 0.1875  851 HOH   A O     
13083 O  O     . HOH   L .   ? 0.9284 0.4913 0.2907 0.1333  -0.0667 0.0828  852 HOH   A O     
13084 O  O     . HOH   L .   ? 0.2516 0.3371 0.6337 0.0361  -0.0338 0.0323  853 HOH   A O     
13085 O  O     . HOH   L .   ? 1.0063 0.4878 0.3748 0.1417  0.0058  -0.0392 854 HOH   A O     
13086 O  O     . HOH   L .   ? 0.9546 0.6135 0.6320 0.2422  -0.1606 0.1111  855 HOH   A O     
13087 O  O     . HOH   L .   ? 0.7618 0.7855 0.4410 0.1842  -0.1039 0.1069  856 HOH   A O     
13088 O  O     . HOH   L .   ? 0.4703 0.5833 0.4941 -0.0682 0.0890  0.1111  857 HOH   A O     
13089 O  O     . HOH   L .   ? 0.9441 0.3986 0.5901 -0.1154 0.1024  -0.1908 858 HOH   A O     
13090 O  O     . HOH   L .   ? 0.4257 0.2502 0.3158 0.0605  -0.0274 -0.0041 859 HOH   A O     
13091 O  O     . HOH   L .   ? 0.5245 0.9646 0.5550 -0.0827 0.0611  -0.2098 860 HOH   A O     
13092 O  O     . HOH   L .   ? 0.6121 0.7317 0.9146 0.1771  -0.0025 -0.2485 861 HOH   A O     
13093 O  O     . HOH   L .   ? 0.4531 0.6130 0.9029 0.0825  -0.3047 -0.2423 862 HOH   A O     
13094 O  O     . HOH   L .   ? 0.2047 0.2612 0.5562 -0.0351 -0.0364 0.0077  863 HOH   A O     
13095 O  O     . HOH   L .   ? 0.8053 0.5379 0.6355 -0.0103 0.1727  -0.0479 864 HOH   A O     
13096 O  O     . HOH   L .   ? 0.5231 0.3543 0.4964 -0.0287 0.1632  0.0419  865 HOH   A O     
13097 O  O     . HOH   L .   ? 1.1514 0.4632 0.3979 0.3104  0.1024  -0.0026 866 HOH   A O     
13098 O  O     . HOH   L .   ? 0.5201 0.9021 0.3510 -0.1466 0.0486  -0.1934 867 HOH   A O     
13099 O  O     . HOH   L .   ? 0.2462 0.2525 0.4526 0.0205  0.0274  0.0934  868 HOH   A O     
13100 O  O     . HOH   L .   ? 0.7327 0.5498 0.9116 -0.0114 -0.2486 -0.0267 869 HOH   A O     
13101 O  O     . HOH   L .   ? 0.6885 0.4742 0.5675 0.0825  -0.2089 -0.1443 870 HOH   A O     
13102 O  O     . HOH   L .   ? 0.1895 0.4006 0.3753 0.0211  0.0001  0.1243  871 HOH   A O     
13103 O  O     . HOH   L .   ? 0.3465 0.3179 0.7480 -0.0425 -0.1900 -0.0261 872 HOH   A O     
13104 O  O     . HOH   L .   ? 0.3758 0.4475 0.8773 0.0094  -0.2567 0.1153  873 HOH   A O     
13105 O  O     . HOH   L .   ? 1.0130 0.5075 0.6124 -0.1032 0.1595  0.2114  874 HOH   A O     
13106 O  O     . HOH   L .   ? 1.1678 0.5799 0.4274 -0.0864 0.2804  -0.0876 875 HOH   A O     
13107 O  O     . HOH   L .   ? 0.6650 0.3411 0.4549 -0.0326 -0.0984 0.0099  876 HOH   A O     
13108 O  O     . HOH   L .   ? 0.3932 0.3134 0.5268 0.0175  -0.0025 -0.0124 877 HOH   A O     
13109 O  O     . HOH   L .   ? 0.8674 0.6491 0.5623 0.1880  -0.2887 0.0432  878 HOH   A O     
13110 O  O     . HOH   L .   ? 0.7141 0.6592 0.4601 0.4054  -0.0942 -0.0717 879 HOH   A O     
13111 O  O     . HOH   L .   ? 0.6268 0.5526 0.6767 -0.0574 -0.2100 0.1428  880 HOH   A O     
13112 O  O     . HOH   L .   ? 0.6931 0.7116 0.7043 0.2870  0.3297  0.0662  881 HOH   A O     
13113 O  O     . HOH   L .   ? 0.3984 1.0437 0.5541 -0.0439 -0.0124 -0.3988 882 HOH   A O     
13114 O  O     . HOH   L .   ? 0.5561 0.3374 0.4249 0.0898  -0.0914 0.0116  883 HOH   A O     
13115 O  O     . HOH   L .   ? 0.4113 0.8177 0.5864 -0.0342 0.1073  0.2311  884 HOH   A O     
13116 O  O     . HOH   L .   ? 0.3100 0.4899 0.7916 -0.0010 -0.0072 -0.0498 885 HOH   A O     
13117 O  O     . HOH   L .   ? 0.8859 0.4742 0.7383 0.0112  -0.3165 0.0574  886 HOH   A O     
13118 O  O     . HOH   L .   ? 0.5857 0.8203 0.5360 0.2281  0.0209  0.2777  887 HOH   A O     
13119 O  O     . HOH   L .   ? 0.5402 0.6566 0.5797 0.1838  -0.1819 -0.0095 888 HOH   A O     
13120 O  O     . HOH   L .   ? 0.7186 0.6270 0.6858 0.0573  -0.0378 -0.0445 889 HOH   A O     
13121 O  O     . HOH   L .   ? 0.4424 0.7365 0.6245 -0.1460 -0.0123 -0.1716 890 HOH   A O     
13122 O  O     . HOH   L .   ? 0.6910 0.6018 0.7527 -0.1555 -0.1297 0.2448  891 HOH   A O     
13123 O  O     . HOH   L .   ? 0.3791 0.5376 0.9594 -0.0930 -0.2551 0.1062  892 HOH   A O     
13124 O  O     . HOH   L .   ? 0.6597 0.6832 0.8240 0.1671  -0.0337 0.0037  893 HOH   A O     
13125 O  O     . HOH   L .   ? 0.8056 0.6488 0.8717 -0.0759 -0.1284 -0.0871 894 HOH   A O     
13126 O  O     . HOH   L .   ? 0.6229 0.5979 0.5558 0.0311  -0.1192 0.0947  895 HOH   A O     
13127 O  O     . HOH   L .   ? 0.7201 0.5574 0.9890 -0.1370 0.2847  -0.2869 896 HOH   A O     
13128 O  O     . HOH   L .   ? 0.4656 0.2076 0.3275 0.0156  -0.0279 0.0174  897 HOH   A O     
13129 O  O     . HOH   L .   ? 0.4802 0.4431 0.4648 -0.1152 0.0679  -0.0558 898 HOH   A O     
13130 O  O     . HOH   L .   ? 0.2986 0.4530 0.8762 0.0600  0.1768  0.0935  899 HOH   A O     
13131 O  O     . HOH   L .   ? 0.3757 0.3824 0.3958 0.0508  -0.0708 -0.0421 900 HOH   A O     
13132 O  O     . HOH   L .   ? 0.5644 0.5036 0.4812 -0.0302 -0.1061 0.0312  901 HOH   A O     
13133 O  O     . HOH   L .   ? 0.4286 0.8248 0.7395 0.0612  -0.0063 0.2628  902 HOH   A O     
13134 O  O     . HOH   L .   ? 0.5125 0.8203 0.4126 0.1083  -0.0050 0.0647  903 HOH   A O     
13135 O  O     . HOH   L .   ? 0.7410 0.6040 0.4937 -0.1597 0.1649  0.0191  904 HOH   A O     
13136 O  O     . HOH   L .   ? 0.5611 0.4063 0.3989 0.0337  0.0508  -0.0102 905 HOH   A O     
13137 O  O     . HOH   L .   ? 0.3941 0.8412 0.8022 -0.1858 0.0930  -0.3152 906 HOH   A O     
13138 O  O     . HOH   L .   ? 0.4114 0.5438 0.9223 0.0676  0.0700  0.1767  907 HOH   A O     
13139 O  O     . HOH   L .   ? 0.7022 0.5525 0.5021 0.0322  0.0610  0.1545  908 HOH   A O     
13140 O  O     . HOH   L .   ? 0.8732 0.3254 0.4641 -0.0348 0.0142  0.0121  909 HOH   A O     
13141 O  O     . HOH   L .   ? 0.8903 0.4034 0.8447 0.0218  -0.0118 -0.1192 910 HOH   A O     
13142 O  O     . HOH   L .   ? 0.3194 0.5807 0.9555 -0.0952 -0.1745 0.1146  911 HOH   A O     
13143 O  O     . HOH   L .   ? 0.5282 0.4972 0.7809 -0.1206 0.1135  0.0827  912 HOH   A O     
13144 O  O     . HOH   L .   ? 0.3070 0.4732 0.6827 0.0165  -0.0266 0.1596  913 HOH   A O     
13145 O  O     . HOH   L .   ? 0.9576 0.4919 0.5840 -0.1698 0.1304  -0.1116 914 HOH   A O     
13146 O  O     . HOH   L .   ? 0.6199 0.5354 0.7927 -0.0536 -0.0479 -0.1308 915 HOH   A O     
13147 O  O     . HOH   L .   ? 0.5074 0.6145 0.7979 -0.2023 0.2008  -0.0648 916 HOH   A O     
13148 O  O     . HOH   L .   ? 0.6519 0.5214 0.8385 -0.2700 -0.1203 0.0203  917 HOH   A O     
13149 O  O     . HOH   L .   ? 0.4318 0.3254 0.5173 -0.0366 -0.0777 -0.0383 918 HOH   A O     
13150 O  O     . HOH   L .   ? 0.6164 0.5424 0.5570 -0.1244 -0.0218 -0.1167 919 HOH   A O     
13151 O  O     . HOH   L .   ? 0.4396 0.5401 0.9716 0.0179  -0.1000 0.1123  920 HOH   A O     
13152 O  O     . HOH   L .   ? 0.8830 0.7930 0.3976 0.1666  -0.1094 0.0581  921 HOH   A O     
13153 O  O     . HOH   L .   ? 0.9171 0.5978 0.4955 -0.2734 0.1534  -0.0714 922 HOH   A O     
13154 O  O     . HOH   L .   ? 0.3309 0.6284 0.8579 -0.0249 0.1304  -0.2614 923 HOH   A O     
13155 O  O     . HOH   L .   ? 0.7644 0.5816 0.8661 0.2568  -0.1346 0.1325  924 HOH   A O     
13156 O  O     . HOH   L .   ? 0.7348 0.8542 0.6864 0.0150  0.0429  -0.1577 925 HOH   A O     
13157 O  O     . HOH   L .   ? 0.6184 0.4974 0.4597 0.0848  -0.0469 -0.0804 926 HOH   A O     
13158 O  O     . HOH   L .   ? 0.4359 0.5349 0.9701 -0.1057 -0.0992 0.0289  927 HOH   A O     
13159 O  O     . HOH   L .   ? 0.5569 0.2890 0.8538 0.0198  -0.2577 0.0975  928 HOH   A O     
13160 O  O     . HOH   L .   ? 0.6072 0.9315 0.9299 0.2440  0.3339  -0.0262 929 HOH   A O     
13161 O  O     . HOH   L .   ? 0.7897 0.4347 0.7116 -0.2176 0.0994  -0.0384 930 HOH   A O     
13162 O  O     . HOH   L .   ? 0.4566 0.5097 0.5808 0.0897  -0.0420 0.0695  931 HOH   A O     
13163 O  O     . HOH   L .   ? 0.4020 0.5999 0.3666 -0.0321 0.0955  -0.0853 932 HOH   A O     
13164 O  O     . HOH   L .   ? 0.5849 0.6785 0.5031 0.1748  0.0006  -0.1960 933 HOH   A O     
13165 O  O     . HOH   L .   ? 0.7121 0.4641 0.8669 0.0335  0.2872  0.0010  934 HOH   A O     
13166 O  O     . HOH   L .   ? 0.4964 0.9476 0.7496 0.2831  -0.2182 -0.4375 935 HOH   A O     
13167 O  O     . HOH   L .   ? 1.1708 0.3747 0.7838 -0.0745 -0.0656 0.1867  936 HOH   A O     
13168 O  O     . HOH   L .   ? 0.6048 0.5863 0.5028 0.1784  -0.0123 0.0496  937 HOH   A O     
13169 O  O     . HOH   L .   ? 0.8132 0.6878 0.4793 0.0298  0.3282  0.0282  938 HOH   A O     
13170 O  O     . HOH   L .   ? 0.7844 0.4921 0.5246 -0.0861 -0.1467 -0.0842 939 HOH   A O     
13171 O  O     . HOH   L .   ? 0.4055 0.4216 0.4204 0.0105  -0.0731 0.0110  940 HOH   A O     
13172 O  O     . HOH   L .   ? 0.5444 0.5308 0.8346 -0.0199 0.3050  0.0858  941 HOH   A O     
13173 O  O     . HOH   L .   ? 0.3558 0.3635 0.3637 -0.0242 0.0669  0.0421  942 HOH   A O     
13174 O  O     . HOH   L .   ? 0.7679 0.5351 0.4819 -0.0289 -0.0733 0.0179  943 HOH   A O     
13175 O  O     . HOH   L .   ? 0.6364 0.6881 0.9515 -0.0875 -0.0412 0.1358  944 HOH   A O     
13176 O  O     . HOH   L .   ? 0.8507 0.4837 0.9274 -0.2030 0.1276  -0.1086 945 HOH   A O     
13177 O  O     . HOH   L .   ? 0.8250 0.4754 0.7669 0.2170  0.1558  0.0418  946 HOH   A O     
13178 O  O     . HOH   L .   ? 0.6891 0.6570 0.8336 -0.1165 0.0495  -0.2821 947 HOH   A O     
13179 O  O     . HOH   L .   ? 0.5836 0.6797 0.7973 -0.1682 -0.0417 -0.1993 948 HOH   A O     
13180 O  O     . HOH   M .   ? 0.8258 0.4451 0.5791 -0.0662 0.3868  -0.0296 601 HOH   B O     
13181 O  O     . HOH   M .   ? 0.4067 0.4671 0.7286 0.0097  -0.0913 0.0261  602 HOH   B O     
13182 O  O     . HOH   M .   ? 1.0273 0.9301 0.4362 0.0737  0.1768  -0.2367 603 HOH   B O     
13183 O  O     . HOH   M .   ? 0.7996 0.4308 0.4864 0.0284  -0.1526 -0.0997 604 HOH   B O     
13184 O  O     . HOH   M .   ? 0.8418 0.3288 0.4781 0.1325  -0.0154 -0.0240 605 HOH   B O     
13185 O  O     . HOH   M .   ? 0.6190 0.9012 0.6356 0.1457  -0.0541 0.1404  606 HOH   B O     
13186 O  O     . HOH   M .   ? 0.3454 0.8875 0.7774 0.0259  0.0372  0.0009  607 HOH   B O     
13187 O  O     . HOH   M .   ? 0.4711 0.9353 0.4993 -0.0744 0.0975  -0.0473 608 HOH   B O     
13188 O  O     . HOH   M .   ? 0.3708 0.6330 0.7755 0.0531  0.1967  -0.0843 609 HOH   B O     
13189 O  O     . HOH   M .   ? 0.6062 0.9117 0.6469 0.0384  0.1733  -0.0803 610 HOH   B O     
13190 O  O     . HOH   M .   ? 0.6456 0.5698 0.5714 -0.1315 0.3477  -0.1276 611 HOH   B O     
13191 O  O     . HOH   M .   ? 0.4571 0.4512 0.3625 0.0267  -0.0192 0.0642  612 HOH   B O     
13192 O  O     . HOH   M .   ? 0.3956 0.7478 0.9239 0.1064  0.1326  0.3812  613 HOH   B O     
13193 O  O     . HOH   M .   ? 1.0447 0.5417 0.5844 -0.0384 -0.0498 -0.1254 614 HOH   B O     
13194 O  O     . HOH   M .   ? 0.3656 0.4498 0.5959 -0.0196 0.0294  -0.1189 615 HOH   B O     
13195 O  O     . HOH   M .   ? 0.3582 0.4998 0.4482 0.0109  -0.0739 0.0066  616 HOH   B O     
13196 O  O     . HOH   M .   ? 0.2682 0.2800 0.3715 -0.0308 -0.0352 0.0960  617 HOH   B O     
13197 O  O     . HOH   M .   ? 0.9495 0.4191 0.5720 0.0017  0.3731  -0.0868 618 HOH   B O     
13198 O  O     . HOH   M .   ? 0.3365 0.2248 0.2793 0.0005  0.1021  -0.0584 619 HOH   B O     
13199 O  O     . HOH   M .   ? 0.6288 0.6800 0.7026 -0.1449 0.3772  -0.1569 620 HOH   B O     
13200 O  O     . HOH   M .   ? 0.8505 0.6774 0.5094 0.4103  0.1223  0.1875  621 HOH   B O     
13201 O  O     . HOH   M .   ? 0.9890 0.2958 0.6642 -0.1446 -0.0654 0.0653  622 HOH   B O     
13202 O  O     . HOH   M .   ? 1.0598 0.3136 0.5211 0.0044  -0.2324 0.0100  623 HOH   B O     
13203 O  O     . HOH   M .   ? 0.2709 0.4404 0.2879 0.1525  -0.0930 -0.0386 624 HOH   B O     
13204 O  O     . HOH   M .   ? 0.2660 0.5318 0.7979 -0.0513 0.1054  -0.2645 625 HOH   B O     
13205 O  O     . HOH   M .   ? 0.4619 0.1982 0.3561 -0.0007 0.1072  -0.0447 626 HOH   B O     
13206 O  O     . HOH   M .   ? 0.5809 0.7655 0.5204 0.0653  -0.0796 -0.1251 627 HOH   B O     
13207 O  O     . HOH   M .   ? 0.7758 0.4451 0.6604 0.0357  0.4251  0.0422  628 HOH   B O     
13208 O  O     . HOH   M .   ? 0.4792 0.5564 0.8675 -0.0625 -0.2058 -0.0163 629 HOH   B O     
13209 O  O     . HOH   M .   ? 0.8845 0.3719 0.9984 0.0834  0.4207  0.1250  630 HOH   B O     
13210 O  O     . HOH   M .   ? 0.3665 0.3041 0.3967 0.0169  0.1347  -0.0355 631 HOH   B O     
13211 O  O     . HOH   M .   ? 0.7914 0.6189 0.4184 0.2205  -0.1215 -0.0558 632 HOH   B O     
13212 O  O     . HOH   M .   ? 0.5692 0.5442 0.9748 -0.0713 0.4108  -0.0963 633 HOH   B O     
13213 O  O     . HOH   M .   ? 0.2175 0.3398 0.3675 0.0160  -0.0274 -0.0276 634 HOH   B O     
13214 O  O     . HOH   M .   ? 0.2282 0.5116 0.8494 -0.0001 -0.0635 -0.0989 635 HOH   B O     
13215 O  O     . HOH   M .   ? 0.3986 0.4610 0.6659 0.0424  -0.0853 -0.0642 636 HOH   B O     
13216 O  O     . HOH   M .   ? 0.3025 0.5638 0.6461 0.1293  0.1107  0.0041  637 HOH   B O     
13217 O  O     . HOH   M .   ? 0.3698 0.2770 0.5645 0.0427  0.0190  -0.0879 638 HOH   B O     
13218 O  O     . HOH   M .   ? 0.4889 0.4099 0.5667 -0.0475 0.0150  -0.1064 639 HOH   B O     
13219 O  O     . HOH   M .   ? 0.5739 0.6174 0.9847 0.2310  0.2770  -0.0249 640 HOH   B O     
13220 O  O     . HOH   M .   ? 0.9639 0.4532 0.6870 -0.1261 -0.2009 0.0338  641 HOH   B O     
13221 O  O     . HOH   M .   ? 0.3837 0.2982 0.4559 -0.0564 0.0828  -0.0477 642 HOH   B O     
13222 O  O     . HOH   M .   ? 0.2325 0.3935 0.5747 -0.0011 0.0184  -0.0581 643 HOH   B O     
13223 O  O     . HOH   M .   ? 1.0685 0.5258 0.5572 0.1283  0.3470  -0.0666 644 HOH   B O     
13224 O  O     . HOH   M .   ? 0.3505 0.6060 0.9645 0.1279  -0.1941 -0.0989 645 HOH   B O     
13225 O  O     . HOH   M .   ? 0.4864 0.4365 0.5140 0.0635  -0.1279 0.0464  646 HOH   B O     
13226 O  O     . HOH   M .   ? 0.2439 0.2290 0.3649 0.0091  -0.0231 0.0191  647 HOH   B O     
13227 O  O     . HOH   M .   ? 0.3105 0.2253 0.5765 0.0275  0.0046  0.0448  648 HOH   B O     
13228 O  O     . HOH   M .   ? 0.5566 0.4601 0.7086 -0.0828 0.3595  -0.1389 649 HOH   B O     
13229 O  O     . HOH   M .   ? 0.8085 0.3767 0.4451 -0.0374 0.1481  -0.0743 650 HOH   B O     
13230 O  O     . HOH   M .   ? 0.2030 0.3295 0.6731 -0.0643 0.0101  -0.0877 651 HOH   B O     
13231 O  O     . HOH   M .   ? 0.1862 0.2775 0.3497 -0.0041 0.0065  0.0058  652 HOH   B O     
13232 O  O     . HOH   M .   ? 0.3809 0.5143 0.2938 0.1737  0.0879  -0.0613 653 HOH   B O     
13233 O  O     . HOH   M .   ? 0.2739 0.3748 0.4502 0.0888  -0.0619 0.0097  654 HOH   B O     
13234 O  O     . HOH   M .   ? 0.5575 0.7245 0.5849 0.2665  -0.1917 -0.3088 655 HOH   B O     
13235 O  O     . HOH   M .   ? 0.4074 0.3584 0.9031 -0.1015 -0.0502 -0.0977 656 HOH   B O     
13236 O  O     . HOH   M .   ? 0.2806 0.4323 0.9554 0.0400  0.1112  0.0640  657 HOH   B O     
13237 O  O     . HOH   M .   ? 0.2529 0.3574 0.4364 -0.0540 0.0621  -0.0677 658 HOH   B O     
13238 O  O     . HOH   M .   ? 0.3417 0.5502 0.8622 -0.1007 -0.0080 -0.2991 659 HOH   B O     
13239 O  O     . HOH   M .   ? 0.4703 0.8145 0.7349 -0.1414 -0.1898 0.4309  660 HOH   B O     
13240 O  O     . HOH   M .   ? 1.0911 0.5082 0.4924 0.1698  -0.1456 0.1490  661 HOH   B O     
13241 O  O     . HOH   M .   ? 0.6460 0.4306 0.4548 0.2164  -0.1166 -0.1296 662 HOH   B O     
13242 O  O     . HOH   M .   ? 0.5515 0.3998 0.7651 0.0886  0.3210  -0.0520 663 HOH   B O     
13243 O  O     . HOH   M .   ? 0.5683 0.3514 0.7062 0.0522  0.0914  0.0900  664 HOH   B O     
13244 O  O     . HOH   M .   ? 0.7112 0.8222 0.2659 0.2640  -0.0054 -0.0495 665 HOH   B O     
13245 O  O     . HOH   M .   ? 0.3917 0.3171 0.6790 0.0036  -0.1543 -0.0484 666 HOH   B O     
13246 O  O     . HOH   M .   ? 0.6189 1.0501 0.4532 0.1616  -0.0466 0.2887  667 HOH   B O     
13247 O  O     . HOH   M .   ? 0.5337 0.8165 0.5837 -0.0282 -0.0964 0.3862  668 HOH   B O     
13248 O  O     . HOH   M .   ? 0.2149 0.4616 0.8084 -0.0123 0.0652  -0.0645 669 HOH   B O     
13249 O  O     . HOH   M .   ? 0.9639 0.3227 0.6000 0.1659  -0.0861 -0.0275 670 HOH   B O     
13250 O  O     . HOH   M .   ? 0.5545 0.5438 0.5849 0.0950  -0.1307 -0.1903 671 HOH   B O     
13251 O  O     . HOH   M .   ? 0.9400 0.5530 0.4515 0.3168  -0.1043 -0.1747 672 HOH   B O     
13252 O  O     . HOH   M .   ? 0.8861 0.3200 0.3258 0.0697  -0.0365 0.0894  673 HOH   B O     
13253 O  O     . HOH   M .   ? 0.4387 0.3328 0.5981 0.0139  0.2758  -0.0785 674 HOH   B O     
13254 O  O     A HOH   M .   ? 0.3151 0.2740 0.2735 0.0169  -0.0172 -0.0613 675 HOH   B O     
13255 O  O     B HOH   M .   ? 0.3327 0.3167 0.3117 0.0768  0.0437  -0.0226 675 HOH   B O     
13256 O  O     . HOH   M .   ? 0.4620 0.2899 0.4253 -0.0528 0.1636  -0.0852 676 HOH   B O     
13257 O  O     . HOH   M .   ? 0.3295 0.8087 0.3448 -0.1757 -0.0676 0.1675  677 HOH   B O     
13258 O  O     . HOH   M .   ? 0.6879 0.3444 0.6521 -0.0505 0.0005  0.0676  678 HOH   B O     
13259 O  O     . HOH   M .   ? 0.4464 0.2831 0.5892 -0.0075 0.0149  -0.0404 679 HOH   B O     
13260 O  O     . HOH   M .   ? 0.7467 0.4688 0.5280 0.2644  -0.0528 0.0092  680 HOH   B O     
13261 O  O     . HOH   M .   ? 0.3143 0.5661 0.6333 0.0177  -0.0070 -0.2105 681 HOH   B O     
13262 O  O     . HOH   M .   ? 0.8417 0.4629 0.3604 0.0046  -0.0692 -0.1859 682 HOH   B O     
13263 O  O     . HOH   M .   ? 0.2976 0.6027 0.4844 0.0699  0.0206  0.2260  683 HOH   B O     
13264 O  O     . HOH   M .   ? 0.2805 0.3311 0.4847 -0.0007 0.0369  -0.0835 684 HOH   B O     
13265 O  O     . HOH   M .   ? 0.1763 0.2481 0.2830 0.0192  0.0450  0.0176  685 HOH   B O     
13266 O  O     . HOH   M .   ? 0.5743 0.2927 0.3241 0.1067  -0.1221 -0.0107 686 HOH   B O     
13267 O  O     . HOH   M .   ? 0.3741 0.3779 0.4426 0.0079  0.0823  -0.0988 687 HOH   B O     
13268 O  O     . HOH   M .   ? 0.4241 0.3192 0.3926 0.0036  0.0857  -0.0379 688 HOH   B O     
13269 O  O     . HOH   M .   ? 0.4048 0.2319 0.4007 -0.0139 0.0668  0.0096  689 HOH   B O     
13270 O  O     . HOH   M .   ? 0.2223 0.4385 0.6616 0.0188  0.0197  -0.0290 690 HOH   B O     
13271 O  O     . HOH   M .   ? 0.4076 0.3378 0.3601 0.0553  0.0857  0.0119  691 HOH   B O     
13272 O  O     . HOH   M .   ? 0.5477 0.7968 0.3446 0.3377  -0.0164 -0.0301 692 HOH   B O     
13273 O  O     . HOH   M .   ? 0.1512 0.2773 0.4418 0.0157  0.0289  -0.0435 693 HOH   B O     
13274 O  O     . HOH   M .   ? 0.2761 0.6417 0.3443 0.0207  -0.0237 0.0960  694 HOH   B O     
13275 O  O     . HOH   M .   ? 0.5545 0.3968 0.5615 -0.0493 0.2128  -0.0129 695 HOH   B O     
13276 O  O     . HOH   M .   ? 0.2505 0.4067 0.4497 -0.0319 -0.0331 -0.1071 696 HOH   B O     
13277 O  O     . HOH   M .   ? 0.5928 0.3249 0.6836 0.0884  0.1985  0.0203  697 HOH   B O     
13278 O  O     . HOH   M .   ? 0.1812 0.5813 0.4012 0.0112  0.0026  0.1838  698 HOH   B O     
13279 O  O     . HOH   M .   ? 0.2696 0.3700 0.4467 -0.0543 0.0144  -0.0529 699 HOH   B O     
13280 O  O     . HOH   M .   ? 0.1903 0.2595 0.3218 -0.0034 0.0344  0.0076  700 HOH   B O     
13281 O  O     . HOH   M .   ? 0.8034 0.2667 0.3272 -0.0376 0.0725  0.0754  701 HOH   B O     
13282 O  O     . HOH   M .   ? 0.4208 0.4849 0.9845 -0.1158 0.0665  -0.1528 702 HOH   B O     
13283 O  O     . HOH   M .   ? 0.4388 0.2849 0.7928 -0.0370 0.1266  0.1545  703 HOH   B O     
13284 O  O     . HOH   M .   ? 0.7609 0.3976 0.7323 -0.0525 0.0005  0.1293  704 HOH   B O     
13285 O  O     . HOH   M .   ? 0.5507 0.8205 0.5945 -0.0400 -0.2591 -0.0206 705 HOH   B O     
13286 O  O     . HOH   M .   ? 0.3597 0.3849 0.7586 -0.0004 -0.1125 -0.0650 706 HOH   B O     
13287 O  O     . HOH   M .   ? 0.5289 0.4653 0.4581 0.0238  0.0535  0.1074  707 HOH   B O     
13288 O  O     . HOH   M .   ? 0.7080 0.5131 0.2543 0.0230  0.0307  0.0096  708 HOH   B O     
13289 O  O     . HOH   M .   ? 0.8663 0.5384 0.5187 -0.0743 0.1525  0.0461  709 HOH   B O     
13290 O  O     . HOH   M .   ? 0.3040 0.4704 0.3291 0.0128  -0.0140 0.0094  710 HOH   B O     
13291 O  O     . HOH   M .   ? 0.4671 0.4285 0.3147 -0.0037 -0.0343 -0.1055 711 HOH   B O     
13292 O  O     . HOH   M .   ? 0.4462 0.5805 0.4190 -0.0591 0.0953  0.0403  712 HOH   B O     
13293 O  O     . HOH   M .   ? 0.3666 0.3526 0.6223 -0.0761 0.0746  -0.0636 713 HOH   B O     
13294 O  O     . HOH   M .   ? 0.7669 0.3361 0.3542 -0.1552 0.2386  -0.0362 714 HOH   B O     
13295 O  O     . HOH   M .   ? 0.4113 0.2511 0.3677 -0.0102 0.1550  -0.0665 715 HOH   B O     
13296 O  O     . HOH   M .   ? 0.2819 0.2910 0.5798 0.0281  0.0368  -0.0341 716 HOH   B O     
13297 O  O     . HOH   M .   ? 0.2643 0.2496 0.2413 -0.0269 0.0766  -0.0322 717 HOH   B O     
13298 O  O     . HOH   M .   ? 0.9573 0.4505 0.4632 -0.1139 0.3403  -0.0452 718 HOH   B O     
13299 O  O     . HOH   M .   ? 0.7376 0.4015 0.3406 0.0519  -0.0865 0.0771  719 HOH   B O     
13300 O  O     . HOH   M .   ? 0.2329 0.4023 0.3666 -0.0199 0.1028  0.0419  720 HOH   B O     
13301 O  O     . HOH   M .   ? 0.2859 0.2511 0.2915 0.0041  0.0377  -0.0146 721 HOH   B O     
13302 O  O     . HOH   M .   ? 0.4435 0.4614 0.9689 0.0621  0.1818  -0.0446 722 HOH   B O     
13303 O  O     . HOH   M .   ? 0.3700 0.6201 0.8158 -0.1546 -0.1820 0.0889  723 HOH   B O     
13304 O  O     . HOH   M .   ? 0.2540 0.4072 0.3388 0.0087  0.0559  -0.0433 724 HOH   B O     
13305 O  O     . HOH   M .   ? 0.2870 0.3741 0.5961 0.0266  -0.1449 -0.0720 725 HOH   B O     
13306 O  O     . HOH   M .   ? 0.9800 0.4262 0.6613 0.1037  0.0795  -0.0009 726 HOH   B O     
13307 O  O     . HOH   M .   ? 0.2732 0.5587 0.3531 0.0628  0.0214  0.1032  727 HOH   B O     
13308 O  O     . HOH   M .   ? 0.3528 0.2885 0.6724 -0.0262 0.2284  -0.1327 728 HOH   B O     
13309 O  O     . HOH   M .   ? 0.2753 0.5296 0.7172 -0.0422 0.0507  -0.1521 729 HOH   B O     
13310 O  O     . HOH   M .   ? 0.9146 0.3135 0.4141 -0.0285 0.1929  0.0017  730 HOH   B O     
13311 O  O     . HOH   M .   ? 0.2273 0.3834 0.5702 -0.0126 0.0939  0.0191  731 HOH   B O     
13312 O  O     . HOH   M .   ? 0.8570 0.4452 0.6079 -0.0017 0.3524  0.0284  732 HOH   B O     
13313 O  O     . HOH   M .   ? 0.8841 0.4357 0.6840 -0.0831 0.1520  0.1042  733 HOH   B O     
13314 O  O     . HOH   M .   ? 0.5323 0.5933 0.6511 -0.0846 0.1605  -0.1619 734 HOH   B O     
13315 O  O     . HOH   M .   ? 0.2718 0.2709 0.4680 0.0473  0.0317  -0.0491 735 HOH   B O     
13316 O  O     . HOH   M .   ? 0.3089 0.2213 0.2694 -0.0067 -0.0051 0.0099  736 HOH   B O     
13317 O  O     . HOH   M .   ? 0.3013 0.2968 0.2770 -0.0191 0.0279  -0.0132 737 HOH   B O     
13318 O  O     . HOH   M .   ? 0.2883 0.3992 0.8245 -0.0016 0.1817  -0.1096 738 HOH   B O     
13319 O  O     . HOH   M .   ? 0.3136 0.3893 0.2644 -0.0122 0.0556  0.0050  739 HOH   B O     
13320 O  O     . HOH   M .   ? 0.8354 0.3530 0.6071 0.0427  0.2908  0.1478  740 HOH   B O     
13321 O  O     . HOH   M .   ? 0.5856 0.5969 0.5449 -0.2709 0.1085  -0.2001 741 HOH   B O     
13322 O  O     . HOH   M .   ? 0.8135 0.4971 0.8162 0.0961  0.0857  0.3218  742 HOH   B O     
13323 O  O     . HOH   M .   ? 0.2071 0.3032 0.6846 -0.0266 0.0907  -0.0659 743 HOH   B O     
13324 O  O     . HOH   M .   ? 0.7606 0.6495 0.7323 -0.0935 0.1771  -0.0931 744 HOH   B O     
13325 O  O     . HOH   M .   ? 0.3211 0.4067 0.4374 -0.0405 -0.1010 -0.1051 745 HOH   B O     
13326 O  O     . HOH   M .   ? 0.4718 0.3709 0.8119 0.1195  0.1974  -0.0616 746 HOH   B O     
13327 O  O     . HOH   M .   ? 0.6354 0.7039 0.4553 -0.1438 -0.2376 0.1190  747 HOH   B O     
13328 O  O     . HOH   M .   ? 0.5130 0.4776 0.5628 0.0170  0.1453  0.0182  748 HOH   B O     
13329 O  O     . HOH   M .   ? 0.3621 0.2784 0.3343 0.0318  0.1022  -0.0380 749 HOH   B O     
13330 O  O     . HOH   M .   ? 0.3632 0.3788 0.5189 0.0580  -0.0263 0.0525  750 HOH   B O     
13331 O  O     . HOH   M .   ? 0.3271 0.6179 1.0423 0.0347  -0.1910 0.0396  751 HOH   B O     
13332 O  O     . HOH   M .   ? 0.8016 0.4747 0.4115 0.1885  0.0264  0.0027  752 HOH   B O     
13333 O  O     . HOH   M .   ? 0.5187 0.7110 0.6324 0.3141  0.1788  0.2602  753 HOH   B O     
13334 O  O     . HOH   M .   ? 0.6832 0.7142 0.5562 -0.0968 -0.0811 0.0322  754 HOH   B O     
13335 O  O     . HOH   M .   ? 0.3322 0.5614 0.9290 0.1677  0.0424  -0.0709 755 HOH   B O     
13336 O  O     . HOH   M .   ? 0.8229 0.3843 0.2496 0.0896  0.0055  0.0792  756 HOH   B O     
13337 O  O     . HOH   M .   ? 0.2588 0.3324 0.2378 -0.0288 -0.0025 0.0164  757 HOH   B O     
13338 O  O     . HOH   M .   ? 0.2508 0.4134 0.4012 -0.0746 0.0308  -0.0797 758 HOH   B O     
13339 O  O     . HOH   M .   ? 0.4698 0.4510 0.5755 -0.1386 0.0552  -0.1167 759 HOH   B O     
13340 O  O     . HOH   M .   ? 0.3021 0.5108 0.4267 -0.1319 -0.1130 0.1557  760 HOH   B O     
13341 O  O     . HOH   M .   ? 0.7278 0.3378 1.0065 -0.0148 -0.1784 -0.0604 761 HOH   B O     
13342 O  O     . HOH   M .   ? 0.8231 0.6287 0.7363 0.0377  -0.0756 0.0892  762 HOH   B O     
13343 O  O     . HOH   M .   ? 0.3153 0.6050 0.8474 0.0196  0.0027  -0.1515 763 HOH   B O     
13344 O  O     . HOH   M .   ? 0.6690 0.7496 0.4621 0.1041  0.0254  0.2406  764 HOH   B O     
13345 O  O     . HOH   M .   ? 0.3081 0.2552 0.3039 0.0077  0.0310  0.0124  765 HOH   B O     
13346 O  O     . HOH   M .   ? 0.6321 0.3665 0.5710 -0.0962 0.3515  -0.1033 766 HOH   B O     
13347 O  O     . HOH   M .   ? 0.2028 0.2922 0.4365 -0.0192 0.0839  -0.0454 767 HOH   B O     
13348 O  O     . HOH   M .   ? 0.7899 0.3642 0.6406 -0.0902 0.2831  -0.0746 768 HOH   B O     
13349 O  O     . HOH   M .   ? 0.9465 0.3590 0.3145 0.1172  0.1427  0.0686  769 HOH   B O     
13350 O  O     . HOH   M .   ? 0.4942 0.8429 0.5033 0.2357  0.1816  0.1409  770 HOH   B O     
13351 O  O     . HOH   M .   ? 0.4220 0.5494 0.4917 0.2165  -0.1339 0.0774  771 HOH   B O     
13352 O  O     . HOH   M .   ? 0.3983 0.2751 0.3282 -0.0334 0.0367  0.0067  772 HOH   B O     
13353 O  O     . HOH   M .   ? 1.1257 0.4141 0.6361 0.0506  0.2681  0.0893  773 HOH   B O     
13354 O  O     . HOH   M .   ? 0.2490 0.3741 0.7888 0.0064  -0.0798 -0.0077 774 HOH   B O     
13355 O  O     . HOH   M .   ? 1.1184 0.5214 0.4338 0.0562  0.3086  0.0497  775 HOH   B O     
13356 O  O     . HOH   M .   ? 0.2964 0.6358 1.0081 0.0585  0.1400  -0.0246 776 HOH   B O     
13357 O  O     . HOH   M .   ? 0.3936 0.3238 0.5795 0.0612  0.1640  0.0155  777 HOH   B O     
13358 O  O     . HOH   M .   ? 0.5053 0.3238 0.2475 0.0009  0.0121  -0.0913 778 HOH   B O     
13359 O  O     . HOH   M .   ? 0.8045 0.7262 0.5332 -0.1149 0.0815  0.1036  779 HOH   B O     
13360 O  O     . HOH   M .   ? 0.5548 0.3730 0.3887 0.0091  0.0441  -0.0262 780 HOH   B O     
13361 O  O     . HOH   M .   ? 0.2345 0.5050 0.6886 -0.0350 -0.0028 0.2635  781 HOH   B O     
13362 O  O     . HOH   M .   ? 0.3451 0.2235 0.5330 0.0035  0.0773  -0.0323 782 HOH   B O     
13363 O  O     . HOH   M .   ? 0.6102 0.3459 0.9295 -0.0959 -0.4249 0.1388  783 HOH   B O     
13364 O  O     . HOH   M .   ? 0.7715 0.6439 0.4256 0.0999  0.0073  -0.1792 784 HOH   B O     
13365 O  O     . HOH   M .   ? 1.1914 0.3654 0.3455 -0.0088 -0.1109 -0.0419 785 HOH   B O     
13366 O  O     . HOH   M .   ? 0.2246 0.2944 0.3730 0.0076  0.0513  -0.0048 786 HOH   B O     
13367 O  O     . HOH   M .   ? 0.6483 0.5571 0.9372 0.1476  -0.0574 -0.1907 787 HOH   B O     
13368 O  O     . HOH   M .   ? 0.4857 0.7403 0.4468 0.0417  -0.0402 0.1218  788 HOH   B O     
13369 O  O     . HOH   M .   ? 0.4350 0.2724 0.3546 -0.0148 0.2246  -0.0524 789 HOH   B O     
13370 O  O     . HOH   M .   ? 0.8022 0.5531 0.2732 0.1376  0.1272  0.0044  790 HOH   B O     
13371 O  O     . HOH   M .   ? 0.5526 0.7336 0.2901 0.2976  0.0665  0.0642  791 HOH   B O     
13372 O  O     . HOH   M .   ? 0.6399 0.3230 0.6412 0.0623  -0.1339 -0.0560 792 HOH   B O     
13373 O  O     . HOH   M .   ? 0.2871 0.3457 0.4713 0.0720  -0.0189 0.0280  793 HOH   B O     
13374 O  O     . HOH   M .   ? 0.5474 0.3951 0.5504 0.1437  0.0018  0.1104  794 HOH   B O     
13375 O  O     . HOH   M .   ? 0.6199 0.4796 0.5104 0.1052  -0.3011 0.0411  795 HOH   B O     
13376 O  O     . HOH   M .   ? 0.8566 0.5539 0.5091 0.0045  -0.2539 0.1202  796 HOH   B O     
13377 O  O     . HOH   M .   ? 0.3711 0.2411 0.4670 -0.0008 0.2155  -0.0560 797 HOH   B O     
13378 O  O     . HOH   M .   ? 0.5895 0.3696 0.4409 -0.0732 -0.1555 0.1047  798 HOH   B O     
13379 O  O     . HOH   M .   ? 0.9210 0.3794 0.3468 0.0873  -0.2351 -0.0597 799 HOH   B O     
13380 O  O     . HOH   M .   ? 0.3617 0.6183 1.2662 0.0802  -0.0438 -0.2374 800 HOH   B O     
13381 O  O     . HOH   M .   ? 0.2921 0.5528 0.5507 0.0135  0.1090  0.0266  801 HOH   B O     
13382 O  O     . HOH   M .   ? 0.3213 0.5692 0.5313 0.0646  -0.0470 -0.0047 802 HOH   B O     
13383 O  O     . HOH   M .   ? 0.7286 0.4843 0.3265 0.2893  -0.1000 0.0133  803 HOH   B O     
13384 O  O     . HOH   M .   ? 0.8027 0.5052 0.7442 -0.0110 0.2162  -0.1295 804 HOH   B O     
13385 O  O     . HOH   M .   ? 0.3024 0.2832 0.6832 -0.0462 0.0991  -0.0859 805 HOH   B O     
13386 O  O     . HOH   M .   ? 0.4008 0.6089 0.6180 0.0551  0.2680  0.1217  806 HOH   B O     
13387 O  O     . HOH   M .   ? 0.2873 0.3176 0.4249 0.0856  0.0362  -0.0907 807 HOH   B O     
13388 O  O     . HOH   M .   ? 0.5275 1.0978 0.7781 0.0846  -0.2832 0.1304  808 HOH   B O     
13389 O  O     . HOH   M .   ? 0.4808 0.2899 0.3941 -0.0445 0.0344  -0.0675 809 HOH   B O     
13390 O  O     . HOH   M .   ? 0.8199 0.5002 0.8177 -0.1238 0.0748  -0.0150 810 HOH   B O     
13391 O  O     . HOH   M .   ? 0.5088 0.5816 0.8013 0.1591  -0.2734 -0.3569 811 HOH   B O     
13392 O  O     . HOH   M .   ? 0.4231 0.3797 0.7042 -0.1502 -0.0124 -0.0640 812 HOH   B O     
13393 O  O     . HOH   M .   ? 0.3767 0.5339 0.5801 0.0674  0.0371  -0.1302 813 HOH   B O     
13394 O  O     . HOH   M .   ? 0.3300 0.7405 0.4895 0.0047  -0.1570 -0.0505 814 HOH   B O     
13395 O  O     . HOH   M .   ? 0.2158 0.3774 0.3232 -0.0491 -0.0532 0.0494  815 HOH   B O     
13396 O  O     . HOH   M .   ? 0.5057 0.5807 0.3292 -0.0170 -0.0647 0.0275  816 HOH   B O     
13397 O  O     . HOH   M .   ? 0.8368 0.4208 0.5432 -0.1619 0.3711  -0.0796 817 HOH   B O     
13398 O  O     . HOH   M .   ? 0.5493 0.2580 0.4871 -0.0067 0.2331  -0.0361 818 HOH   B O     
13399 O  O     . HOH   M .   ? 0.3945 0.3926 0.3602 -0.1080 0.0493  0.0084  819 HOH   B O     
13400 O  O     . HOH   M .   ? 0.5098 0.3816 0.6368 -0.0034 -0.0274 0.0211  820 HOH   B O     
13401 O  O     . HOH   M .   ? 0.7418 0.3953 0.9979 -0.0120 0.2814  0.1411  821 HOH   B O     
13402 O  O     . HOH   M .   ? 0.3599 0.3513 0.5267 0.0686  0.0630  -0.0379 822 HOH   B O     
13403 O  O     . HOH   M .   ? 0.9376 0.3785 0.3434 0.0959  0.1490  -0.0668 823 HOH   B O     
13404 O  O     . HOH   M .   ? 0.6165 0.4111 0.6708 0.0100  -0.0989 0.1696  824 HOH   B O     
13405 O  O     . HOH   M .   ? 0.3975 0.3995 0.7422 0.0408  -0.0937 0.0976  825 HOH   B O     
13406 O  O     . HOH   M .   ? 0.3954 0.3097 0.3079 0.0307  -0.0538 0.0133  826 HOH   B O     
13407 O  O     . HOH   M .   ? 0.2457 0.4149 0.3941 0.0096  0.0635  0.1668  827 HOH   B O     
13408 O  O     . HOH   M .   ? 0.3004 0.5768 0.7606 0.0224  0.0266  -0.2364 828 HOH   B O     
13409 O  O     . HOH   M .   ? 0.8252 0.6165 0.6345 -0.0810 -0.2152 0.0219  829 HOH   B O     
13410 O  O     . HOH   M .   ? 0.5749 0.7805 0.6210 -0.1556 -0.2161 -0.0935 830 HOH   B O     
13411 O  O     . HOH   M .   ? 0.4030 0.4675 0.5065 -0.0260 -0.0844 -0.0544 831 HOH   B O     
13412 O  O     . HOH   M .   ? 0.7946 0.4272 0.3370 0.0931  0.0551  0.0682  832 HOH   B O     
13413 O  O     . HOH   M .   ? 0.3945 0.3924 0.7346 0.0293  -0.0073 -0.0735 833 HOH   B O     
13414 O  O     . HOH   M .   ? 0.4490 1.1987 0.4694 0.0503  0.0660  0.0886  834 HOH   B O     
13415 O  O     . HOH   M .   ? 0.4686 0.5452 1.0364 -0.0199 0.3494  -0.0150 835 HOH   B O     
13416 O  O     . HOH   M .   ? 0.2427 0.3415 0.5229 -0.0042 0.0463  -0.1116 836 HOH   B O     
13417 O  O     . HOH   M .   ? 0.3105 0.8316 0.5814 -0.1171 0.0491  -0.3564 837 HOH   B O     
13418 O  O     . HOH   M .   ? 0.8881 0.5985 0.6811 -0.1234 0.4212  -0.1969 838 HOH   B O     
13419 O  O     . HOH   M .   ? 0.3530 0.5056 1.0388 0.0070  -0.1680 0.0419  839 HOH   B O     
13420 O  O     . HOH   M .   ? 0.2334 0.4972 0.3749 -0.0641 0.0477  -0.1625 840 HOH   B O     
13421 O  O     . HOH   M .   ? 0.7356 0.3882 0.7017 0.0099  -0.3513 0.1063  841 HOH   B O     
13422 O  O     . HOH   M .   ? 0.9725 0.5898 0.8179 -0.1866 0.0794  0.1131  842 HOH   B O     
13423 O  O     . HOH   M .   ? 0.1490 0.3041 0.5154 0.0335  -0.0364 -0.1024 843 HOH   B O     
13424 O  O     . HOH   M .   ? 0.5013 0.6416 0.7455 0.0817  -0.0280 -0.2677 844 HOH   B O     
13425 O  O     . HOH   M .   ? 0.5347 0.4441 0.8001 -0.2065 0.1297  -0.0132 845 HOH   B O     
13426 O  O     . HOH   M .   ? 0.4849 0.4006 0.5051 0.0775  0.1140  0.0929  846 HOH   B O     
13427 O  O     . HOH   M .   ? 0.3437 0.8077 0.8569 -0.0738 0.1163  -0.1036 847 HOH   B O     
13428 O  O     . HOH   M .   ? 0.3864 0.3215 0.5496 0.0039  0.2352  -0.0262 848 HOH   B O     
13429 O  O     . HOH   M .   ? 0.4733 0.7972 0.4892 -0.1480 -0.0866 0.1973  849 HOH   B O     
13430 O  O     . HOH   M .   ? 0.4924 0.3230 0.3236 0.0490  -0.0475 -0.0153 850 HOH   B O     
13431 O  O     . HOH   M .   ? 0.3739 0.7146 0.7006 0.0408  0.1020  0.0391  851 HOH   B O     
13432 O  O     . HOH   M .   ? 0.6755 0.7381 0.5959 -0.0148 0.0093  0.0423  852 HOH   B O     
13433 O  O     . HOH   M .   ? 0.9009 0.5953 0.4679 -0.0270 0.0390  -0.1331 853 HOH   B O     
13434 O  O     . HOH   M .   ? 0.5287 0.6595 0.7399 -0.0325 -0.2326 -0.0295 854 HOH   B O     
13435 O  O     . HOH   M .   ? 0.7670 0.7447 0.6703 -0.0108 -0.2989 -0.1746 855 HOH   B O     
13436 O  O     . HOH   M .   ? 0.4694 0.5082 1.0126 0.0607  0.1200  -0.0665 856 HOH   B O     
13437 O  O     . HOH   M .   ? 0.4677 0.4794 0.4954 0.0424  -0.0869 -0.0367 857 HOH   B O     
13438 O  O     . HOH   M .   ? 0.3286 0.7218 0.8891 0.0854  0.1314  0.0201  858 HOH   B O     
13439 O  O     . HOH   M .   ? 0.8959 0.9035 0.5300 -0.0244 0.1016  0.3712  859 HOH   B O     
13440 O  O     . HOH   M .   ? 0.6334 0.4602 0.5117 0.0922  -0.2140 -0.0650 860 HOH   B O     
13441 O  O     . HOH   M .   ? 0.7691 0.3459 0.4801 -0.0554 -0.0130 -0.0151 861 HOH   B O     
13442 O  O     . HOH   M .   ? 0.4687 0.3939 0.6833 0.0774  0.0243  -0.0732 862 HOH   B O     
13443 O  O     . HOH   M .   ? 0.9118 0.4288 0.6734 -0.0248 0.1675  -0.0351 863 HOH   B O     
13444 O  O     . HOH   M .   ? 0.8514 0.6337 0.6756 0.0527  -0.1644 0.1019  864 HOH   B O     
13445 O  O     . HOH   M .   ? 0.6691 0.7248 0.3128 0.0402  0.0485  0.0350  865 HOH   B O     
13446 O  O     . HOH   M .   ? 0.3848 0.7123 0.7343 -0.0587 -0.0530 -0.0701 866 HOH   B O     
13447 O  O     . HOH   M .   ? 0.6512 0.6565 0.6884 0.0379  0.0540  0.2138  867 HOH   B O     
13448 O  O     . HOH   M .   ? 0.4039 0.7029 0.9665 -0.0944 -0.1279 0.4768  868 HOH   B O     
13449 O  O     . HOH   M .   ? 0.5681 0.9696 0.5934 0.0618  0.0834  0.0890  869 HOH   B O     
13450 O  O     . HOH   M .   ? 0.5553 0.2870 0.7774 0.0516  0.2823  -0.0522 870 HOH   B O     
13451 O  O     . HOH   M .   ? 0.3197 0.5921 0.8916 -0.0052 0.1220  -0.0282 871 HOH   B O     
13452 O  O     . HOH   M .   ? 0.4613 0.9342 0.7013 0.0630  -0.0107 0.0917  872 HOH   B O     
13453 O  O     . HOH   M .   ? 0.4148 0.7491 0.5961 -0.0118 0.1277  -0.0817 873 HOH   B O     
13454 O  O     . HOH   M .   ? 0.8169 0.5991 0.7101 -0.0053 0.2817  -0.0677 874 HOH   B O     
13455 O  O     . HOH   M .   ? 0.2772 0.5994 0.5312 0.0298  -0.0859 -0.0024 875 HOH   B O     
13456 O  O     . HOH   M .   ? 0.3933 0.8671 0.7455 0.1266  -0.0084 0.1521  876 HOH   B O     
13457 O  O     . HOH   M .   ? 0.2802 0.9465 0.9780 0.1543  0.0100  -0.0034 877 HOH   B O     
13458 O  O     . HOH   M .   ? 0.3382 0.7369 0.3647 -0.0228 -0.0403 0.0211  878 HOH   B O     
13459 O  O     . HOH   M .   ? 0.7004 0.6139 0.9280 0.1388  0.0343  -0.1403 879 HOH   B O     
13460 O  O     . HOH   M .   ? 0.2903 0.4850 0.7104 -0.1144 0.0902  0.0214  880 HOH   B O     
13461 O  O     . HOH   M .   ? 0.3918 0.8056 0.7716 0.0507  0.1454  0.1920  881 HOH   B O     
13462 O  O     . HOH   M .   ? 0.4328 0.5633 1.0149 -0.0129 -0.1912 -0.0004 882 HOH   B O     
13463 O  O     . HOH   M .   ? 0.7344 0.7973 0.6707 -0.2951 0.1092  0.2303  883 HOH   B O     
13464 O  O     . HOH   M .   ? 0.5621 0.3641 0.8454 -0.0248 0.1463  -0.0036 884 HOH   B O     
13465 O  O     . HOH   M .   ? 0.9005 0.8615 0.5526 0.1415  0.1252  0.0598  885 HOH   B O     
13466 O  O     . HOH   M .   ? 0.7835 0.4275 0.6011 -0.0398 -0.1080 0.0390  886 HOH   B O     
13467 O  O     . HOH   M .   ? 0.7279 0.6709 0.6571 -0.0573 -0.1714 -0.0028 887 HOH   B O     
13468 O  O     . HOH   M .   ? 0.6740 0.9466 0.6078 0.1215  -0.2917 -0.0455 888 HOH   B O     
13469 O  O     . HOH   M .   ? 0.7651 0.8671 0.8283 0.0944  0.2625  -0.1190 889 HOH   B O     
13470 O  O     . HOH   M .   ? 0.5788 0.7069 0.9276 -0.0748 0.1379  0.0459  890 HOH   B O     
13471 O  O     . HOH   M .   ? 0.9200 0.5383 0.4804 -0.0639 0.2545  0.1438  891 HOH   B O     
# 
